UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
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Q6G945
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MPKKSVRHIKIREIISNEQIETQDELVKRLNDYDLNVTQATVSRDIKELQLIKVPIPSGQYVYSLPNDRKFHPLEKLGRYLMDSFVNIDGTDNLLVLKTLPGNAQSIGAILDQINWEEVLGTICGDDTCLIICRSKEASDEIKSRIFNLL
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Regulates arginine biosynthesis genes. Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Belongs to the ArgR family.
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B9DNS1
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MAKKSVRHIKIREIISTEQVETQDELVRRLNQFDLNVTQATVSRDIKELQLIKVPAPTGQYIYSLPNDRKYHPLEKLGRYLMDSFVNIEGTGNLLVLKTLPGNAQSIGAILDQIDWEEVLGTICGDDTCLLICHDEESANAIKTRIFNLL
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Regulates arginine biosynthesis genes. Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Belongs to the ArgR family.
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Q5HP32
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MPKKSVRHIKIREIISNEQIETQDELVKRLNEYDLNVTQATVSRDIKELQLIKVPAPTGQYVYSLPNDRRYHPLEKLGRYLMDSFVNIEGTGNLLVLKTLPGNAQSIGAILDQIDWDEVLGTICGDDTCLLICRDEEASEEIKTRIFNLL
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Regulates arginine biosynthesis genes. Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Belongs to the ArgR family.
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Q8CP40
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MPKKSVRHIKIREIISNEQIETQDELVKRLNEYDLNVTQATVSRDIKELQLIKVPAPTGQYVYSLPNDRRYHPLEKLGRYLMDSFVNIEGTGNLLVLKTLPGNAQSIGAILDQIDWDEVLGTICGDDTCLLICRDEEASEEIKTRIFNLL
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Regulates arginine biosynthesis genes. Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Belongs to the ArgR family.
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Q4L6M1
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MAKKSVRHIKIREIISSEQIETQDELVKRLNEYDLNVTQATVSRDIKELQLIKVPAPSGQYVYSLPNDRKYHPLEKLGRYLMDSFVNIEGTGNLLVLKTLPGNAQSIGAILDQIDWDEVLGTICGDDTCLLICKDEDASNTIKTRIFNLL
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Regulates arginine biosynthesis genes. Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Belongs to the ArgR family.
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Q49XW5
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MAKKSVRHIKIREIISNEKIETQDELVKRLNEYELNVTQATVSRDIKELQLIKVPTPAGQYVYSLPNDRKYHPLEKLGRYLIDSFVNIDGTGNLLVLKTLPGNAQSIGAILDQIDWEDVLGTICGDDTCLIICRDDAASEKIKTRIFNLL
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Regulates arginine biosynthesis genes. Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Belongs to the ArgR family.
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Q828A2
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MSQAQENEHAGPAVPQTRTARHRRIVDILNRQPVRSQSQLAKLLADDGLSVTQATLSRDLDELNAVKIRNNDGDLIYAVPSEGGFRTPRVPLGESAKEERMRRLSAELLISAEASANLVVLRTPPGAAQFLASAIDQAELHDILGTIAGDDTLLLISREPTGGQALADHLLRLAQNHH
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Regulates arginine biosynthesis genes. Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Belongs to the ArgR family.
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Q9LCS4
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MTEAHATDAGGPAVPQTRMARHRRIVDILNRQPVRSQSQLAKLLADNGLSVTQATLSRDLDELGAVKIRNTMARLIYAVPARGVPHSAGALGESAKEERMRRLAGELLISAEASANLVVLRTPPGAAQFLASAIDQAELHDILGTIAGDDTLMLISRSPTGGQALADHLLRLAQNDRA
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Regulates arginine biosynthesis genes. Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Belongs to the ArgR family.
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Q9L1A5
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MSHAQEHEQPAGPALPQTRTARHRRIVDILNRQAVRSQSQLAKLLADDGLTVTQATLSRDLDELNAVKIRNTDGDLIYAVPSEGGFRTPRAPLGESAKEERMRRLSAELLISAEASANLVVLRTPPGAAQFLASAIDQAELHDILGTIAGDDTLMLISREPTGGQALADHLLRLAQNGG
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Regulates arginine biosynthesis genes. Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Belongs to the ArgR family.
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A8AYK6
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MNKIESRHRLIRSLIMEKKVHTQQELQELLEANGVIVTQSTLSRDMKALNLVKVTENNISYYVINSIAPSRWEKRLRFYMEDALIMLRPVQNQVVMKTLPGLAQSFGAILDALELPQIVATVCGDDVCLIICEDNPSAIECFDKLKEFAPPFFFSK
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In the presence of arginine, coactivates the transcription of the arcABDC operon, with other regulatory proteins such as ArcR and CcpA. Amino-acid degradation; L-arginine degradation via ADI pathway. Belongs to the ArgR family.
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Q9JIX4
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MEPNSLQWVGSPCGLHGPYIFYKAFQFHLEGKPRILSLGDFFFVRCTPKDPICIAELQLLWEERTSRQLLSSSKLYFLPEDTPQGRNSDHGEDEVIAVSEKVIVKLEDLVKWAHSDFSKWRCGLRATPVKTEAFGRNGQKEALLRYRQSTLNSGLNFKDVLKEKADLGEDEEETNVIVLSYPQYCRYRSMLKRIQDKPSSILTDQFALALGGIAVVSRNPQILYCRDTFDHPTLIENESVCDEFAPNLKGRPRKKKTCPQRRDSFSGSKDPNNNCDGKVISKVKGEARSALTKPKNNHNNCKKTSNEEKPKLSIGEECRADEQAFLVALYKYMKERKTPIERIPYLGFKQINLWTMFQAAQKLGGYETITARRQWKHIYDELGGNPGSTSAATCTRRHYERLILPYERFIKGEEDKPLPPIKPRKQENNTQENENKTKVSGNKRIKQEMAKNKKEKENTPKPQDTSEVSSEQRKEEETLNHKSAPEPLPAPEVKGKPEGHKDLGARAPVSRADPEKANETDQGSNSEKEAEEMGDKGLAPLLPSPPLPPEKDSAPTPGAGKQPLASPSTQMDSKQEAKPCCFTESPEKDLQGAPFSSFSATKPPLTSQNEAEEEQLPATANYIANCTVKVDQLGSDDIHTALKQTPKVLVVQSFDMFKDKDLTGPMNENHGLNYTPLLYSRGNPGIMSPLAKKKLLSQVSGASLSSSYPYGSPPPLISKKKLIAREDLCSGLSQGHHSQSSDHTAVSRPSVIQHVQSFKNKASEDRKSINDIFKHDKLSRSDAHRCGFSKHQLGSLADSYILKQETQEGKDKLLEKRAVSHAHVPSFLADFYSSPHLHSLYRHTEHHLHNEQSSKYAARDAYQESENGAFLSHKHPEKIHVNYLASLHLQDKKVAAAEASTDDQPTDLSLPKNPHKLTSKVLGLAHSTSGSQEIKGASQFQVVSNQSRDCHPKACRVSPMTMSGPKKYPESLARSGKPHQVRLENFRKMEGMVHPILHRKMSPQNIGAARPIKRSLEDLDLVIAGKKARAVSPLDPAKEASGKEKASEQESEGNKGAYGGHSGAASEGHKLPLSTPIFPGLYSGSLCNSGLNSRLPAGYSHSLQYLKNQTVLSPLMQPLAFHSLVMQRGIFTSPTNSQQLYRHLAAATPVGSSYGDLLHNSIYPLAGINPQAAFPSSQLSSVHPSTKL
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Transcription coactivator that binds to the 5'-AATA[CT]-3' core sequence and plays a key role in adipogenesis and liver development. Acts by forming a complex with phosphorylated PHF2, which mediates demethylation at Lys-337, leading to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver (By similarity). Required for adipogenesis: regulates triglyceride metabolism in adipocytes by regulating expression of adipogenic genes. Overexpression leads to induction of smooth muscle marker genes, suggesting that it may also act as a regulator of smooth muscle cell differentiation and proliferation. Widely expressed. Expressed in lung, heart, small intestine, kidney, muscle and brain. Also expressed in spleen, thymus, endocrine organs and in uterus and testis. First detected in the intermediate plate mesoderm, and subsequently in the nephrogenic cords of the urogenital ridges. Expressed in the developing limb. Also expressed in the myotome of the somites from 9.5 dpc, the oro-nasopharyngeal ectoderm and underlying mesenchyme, otic vesicles, the gut and its derivatives, and transiently in the liver at 11.5 dpc. During smooth muscle cell differentiation in vitro. Upon adipogenesis. The ARID domain mediates the interaction with DNA. Methylation at Lys-337 prevents DNA-binding. Demethylation by PHF2 promotes recruitment of the PHF2-ARID5B complex to promoters (By similarity). High rate of neonatal mortality. Embryonic growth or birth weight are not effected, while lipid accumulation is severely reduced in brown adipose neonates at 24 hours of age. Mice weigh significantly less than controls from postnatal day 5 onward. Adult mice are lean, with significant reductions in brown and white adipose tissues, and in the percentage of body fat. Mice are also resistant to weight gains and obesity when maintained on high-fat diets. Belongs to the ARID5B family. Truncated C-terminus. Truncated N-terminus.
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Q9MA37
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MDSDDDMHDMDSVDYDYYSGGTYDDNDSDETDFGFGEADTDDAAIIASYRSKSNYVVLKEEDIRRHQNDDVGRVSAVLSITDVEASTLLLHYHWSVSKVNDEWFADEERVRRTVGILEGPVVTTPDGREFTCGICFDSYTLEEIVSVSCGHPFCATCWTGYISTTINDGPGCLMLKCPDPSCPAAIGRDMIDKLASKEDKEKYYRYFLRSYVEVNREMKWCPAPGCEHAIDFAGGTESYDVSCLCSHSFCWNCTEEAHRPVDCDTVGKWILKNSAESENMNWILANSKPCPKCKRPIEKNHGCMHMTCTPPCKFEFCWLCLNAWTEHGERTGGFYACNRYEAAKQEGLYDEAERRREMAKNSLERYTHYYERWASNQVSRQKAMGDLQKMQSEKLGKLSDIQCTPESQLKFIAEAWLQIIECRRVLKWTYAYGYYLQDHAKKPFFEYLQGEAESGLERLHKCVEKDIEVFELAEGPSEEFNHFRTKLTGLTSITKTFFENLVKALENGLADVDSQAASSKPANSKPSSKTKGGGKGKGSSKNGGSSRNPDGN
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Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine. Binds 4 Zn(2+) ions per subunit. Protein modification; protein ubiquitination. A number of isoforms are produced. According to EST sequences. Ubiquitous. Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate. Belongs to the RBR family. Ariadne subfamily.
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P0C8K8
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MMDSDDDMLDAHDMDSVDYDFDSGGTDDDNDIDETDYVFGEADTDDAAIIAYHRSQINYVVLKEEDIRRHQKDDVGRVSVVLSITDVQASLLLLHYHWSVSKVNDEWFADEDRVRRTVGILEGPAPDGREFTCGICFESYPLEETISVSCGHPFCATCWTGYISTSINDGPGCLMLKCPYPCCPAAIGRDMIDNLCSKEDKERYYRYFLRSYVEVNREMKCCPAPGCEHAISFAAGTESNYDVSCLCSHSFCWNCSEEAHRPVDCDTVGKWILKNSTESENMNWILANSKPCPKCKRPIEKNHGCMHMTCTPPCKFEFCWLCLNAWTEHGESSGGYYACNRYEAAKKQGLYDEAERRREMAKNSLEKYTHYYKRWASNQVSRQKAMGDLQKMQSEKLRKLSDIQCTSESQLKFIAEAWLQIIECRRVLKWTYAYGYYVPDDHTKKQFFEYLQGEAESGLERLHECIENDIEVFEFGEGPSEEFNHFRTKLTDLTSITKTFFQNLVKALENGLADVDSHAASSKPANCKPSSNTKDGGKGKKEALTMAGSAET
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Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine. Binds 4 Zn(2+) ions per subunit. Protein modification; protein ubiquitination. Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate. Belongs to the RBR family. Ariadne subfamily. Could be the product of a pseudogene. Truncated C-terminus. Truncated C-terminus.
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Q9SIQ6
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MDSEEDMLDAHDMESGEDDFYSGGTDDCNDSDDGEPDYGFVEEDADDSAMIASHRSQKNFCVLREEDIRRHQMDNIERVSVVLSITEVEASILLRHFHWSVGRVHDEWFADEERVRKTVGILESHVVPPSDDSELTCGICFDSYPPEKIASVSCGHPFCTTCWTGYISTTINDGPGCLMLRCPDPSCLAAVGHDMVDKLASEDEKEKYNRYFLRSYIEDNRKMKWCPAPGCDFAIDFVAGSGNYDVSCLCSFSFCWNCTEEAHRPVDCSTVSKWILKNSAESENMNWILANSKPCPRCKRPIEKNQGCMHMTCTPPCKYEFCWLCLGAWMDHGERTGGFYACNRYEVAKQEGQYDETERRREMAKNSLERYTHYYERWASNQTSRQKAMADLQQAQMQNLEKLSDKQCTPESQLKFILEAWLQIIECRRVLKWTYAYGYYLPEHEHAKRQFFEYLQGEAESGLERLHQCVEKDLVQFLIAEGPSKDFNDFRTKLAGLTSVTKNYFENLVKALENGLADVDSHAACSSKSTSSKSTGCSSKTRGKGKGSSRTGGSSRNPDDNL
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Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine. Binds 4 Zn(2+) ions per subunit. Protein modification; protein ubiquitination. Ubiquitous. Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate. Belongs to the RBR family. Ariadne subfamily.
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Q84VL9
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MEADDDFYSGTENYSDYADSDEDDADGEYEFVDDAADDSDDLIFRRRQQNYSVLSEADICKLQEDDISRISTVLSISRNSSAILLRHYNWCVSRVHDEWFADEEKVRDAVGLLEKPVVDFPTDGELDCGICFETFLSDKLHAAACGHPFCDSCWEGYITTAINDGPGCLTLRCPDPSCRAAVGQDMINLLAPDKDKQKYTSYFVRSYVEDNRKTKWCPAPGCDYAVNFVVGSGNYDVNCRCCYSFCWNCAEEAHRPVDCDTVSKWVLKNSAESENMNWILANSKPCPKCKRPIEKNQGCMHITCTPPCKFEFCWLCLGAWTEHGEKTGGFYACNRYEAAKQDGIYDETEKRREMAKNSLERYTHYYERWATNQSSRQKALLDLKKMQTDDIEKLSDIQCQPESQLKFIIEAWLQIVECRRVLKWTYAYGFYIPDQEHGKRVFFEYLQGEAESGLERLHQCAEKELLPYLDAKGPSEDFNEFRTKLAGLTSVTKNYFENLVRALENGLSDVNSHDAYDRTSSSKSLGGKTKGSSSKASSSDSSHWPCEYCTYVNPRSTTICQMCEHGR
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Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine. Binds 4 Zn(2+) ions per subunit. Protein modification; protein ubiquitination. Ubiquitous. Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate. Belongs to the RBR family. Ariadne subfamily.
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A0MER2
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MDFSDDDMIDNKSGEENYSYGGGNESDDYNDVVDTIIPSEKSYVILKEEDILKLQRDDIERVSSILSLSQVEVIVLLLHYNWCVSKVEDEWFTDEERIRKAVGLLKEPVVDFNGGEKDKKCRKVNIQCGICFESYTREEIARVSCGHPYCKTCWAGYITTKIEDGPGCLRVKCPEPSCSAAVGKDMIEDVTETKVNEKYSRYILRSYVEDGKKIKWCPSPGCGYAVEFGGSESSSYDVSCLCSYRFCWNCSEDAHSPVDCDTVSKWIFKNQDESENKNWMLANSKPCPECKRPIEKNDGCNHMTCSAPCGHEFCWICLKAYRRHSGACNRFVVEQAESKRALLQSEIKRYTHYYVRWAENQSSRLKAMRDLEKLQSVQLKELSDNQCTSETQLQFTVDAWLQIIECRRVLKWTYAYGYYLQDLPKRKFFEYLQGEAESGLERLHHCAENELKQFFIKSEDPSDTFNAFRMKLTGLTTVTKTYFENLVKALENGLVDVTHNEFPPDNETKSTQEKYEEYQDYEDDFLETQRLYDEALLSGCYYD
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Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine. Binds 4 Zn(2+) ions per subunit. Protein modification; protein ubiquitination. Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate. Belongs to the RBR family. Ariadne subfamily. Extended C-terminus.
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Q56ZQ9
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MDQQPERREGRSFPERKGQKRKLEEGAAAVEDREISAVSTDGGQALLSEVAAQVSVLNSAFSWQESDRAAAKRATQVLAELAKNEDLVNVIVDGGAVPALMTHLQAPPYNDGDLAEKPYEHEVEKGSAFALGLLAIKPEYQKLIVDKGALPHLVNLLKRNKDGSSSRAVNSVIRRAADAITNLAHENSSIKTRVRVEGGIPPLVELLEFSDSKVQRAAAGALRTLAFKNDDNKNQIVECNALPTLILMLGSEDAAIHYEAVGVIGNLVHSSPHIKKEVLTAGALQPVIGLLSSCCPESQREAALLLGQFASTDSDCKVHIVQRGAVRPLIEMLQSPDVQLKEMSAFALGRLAQDAHNQAGIAHSGGLGPLLKLLDSRNGSLQHNAAFALYGLADNEDNVSDFIRVGGIQKLQDGEFIVQATKDCVSKTLKRLEEKIHGRVLRHLLYLMRISEKSIQRRVALALAHLCSPEDQRTIFIDDNGLELLLGLLGSLNTKQQLDGAAALYKLANKSMALSPVDAAPPSPTQRVYLGEQYVNNATLSDVTFLVEGRTFYAHRICLLASSDAFRAMFDGGYREKDARDIEIPNIKWEVFELMMRFIYTGSVDITNEISKDLLRAADQYLLEGLKRLCEYTIAQDITLESIGDMYELSEAFHAMSLRQACIMFILEHFDKLSSMPWQNELVQRTIPEIREYFCRALTKSTTNLQSLRL
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May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2, a transcription factor which controls ABA-dependent gene expression via the G-box-type ABA-responsive elements. Negative regulator of seed germination and young seedling growth. Protein modification; protein ubiquitination. Interacts with ABF2 (PubMed:15516505). Interacts with DUF7/AIP1 (PubMed:26538092). A number of isoforms are produced. According to EST sequences. Detected in embryos and most of the vegetative and reproductive organs. Up-regulated by abscisic acid (ABA) and high salt. The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes. Abscisic acid (ABA) and glucose insensitivities. More efficient germination and postgermination growth.
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O82364
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MAGWSMVADEDAVDYSKTPKSLDANRSPESVNPESTGFEKKIKELISLFRPLLDSFLAEFCSADGFLPLPAMTGEGRTVDLFNLFLNVTHKGGFDAVSENGSWDEVVQESGLESYDSASAKLIYVKYLDAFGRWLNRVVAGDTDVSSVELSGISDALVARLNGFLSEVKKKYELRKGRPAKELGAELKWFISKTKRRYDKHHVGKESASNDAVKEFQGSKLAERRLEQIMILESVTQECSSPGKRKRECPLETLKWLSDVAKDPCDPSLGIVPDRSEWVSYGSEEPWKQLLLFRASRTNNDSACEKTWQKVQKMHPCLYDDSAGASYNLRERLSYEDYKRGKTGNGSDIGSSDEEDRPCALVGSKFQAKVPEWTGITPESDSKWLGTRIWPLTKEQTKANLLIERDRIGKGRQDPCGCHNPGSIECVKFHITAKRDKLKLELGPAFYMWCFDVMGECTLQYWTDLELKKIKSLMSSPPSLSPAFIHQAKMILPSKSRGKIVSYFYNVTLLQYRASQSRITPHDIDSDTDQIFLRATENENPAPEANTFQKPALLSPNKKRCR
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Extended N-terminus.
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Q95Y31
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MSDDPAFLALGTEVSAKFKGAYCEAKIQKVDRSLKVKVSLKESPFGQMIVQDNDLPNAKFEINELTDVVFQRKFIRCQIQSIKDQSKYHVVFNDGDEKELRRTQLVLKGGKHFAADGNLDSMPLTNPESFSTPVIRGAAKRGAQKIRNAISEASGSRGGAVLLHNDDDENDEEDQEDGENEEDADDDDDDTEEQQQPRERRRAAAISAIGVLKKAIEDTQSEESSADSSEERERARSRRKRKDEASSAVTSDEEDQEDLATTDSENPVINGASSAAALSKTLQRKLEKQAMKREKQRLKEEEREEKLRLKEENREKKRREKARIMELKRLEKVYRTSNARIQENHEKSMTQIISHRSVRYFARFSDLKHRRKKKKLYLHEHRQKVNSRIRNVKLYFAWRFVAHKARLSYFARYALQWWRTSEDQAYSLIRTEKLLRSQRRRDWVGSWLEGLEREKIRFVVIHESYTQARRILKYIERGTEKRTFAERCDIEYEDIESSTVSSHFRDQEWFPAVLFPQVFSDENGSEGRQRIVRHMGNGQLVQVWEDDLVPFDWLPEYSFADVTAMTEKKPVEMRRKFKLAWRFATDYAQNRLDARSIRSILEWKFIRPSSRRLKITPIPVQAPSPNRCGEDHDDLVSTPNESDYDSDATIKNVDAETKDLFVAMLVQFHDAHNSVIDTNPTIQGHEVDLYYLYELAKKTGGPKKVYAANLWSDYAKKLVPAATDAEEELKTIFKNFLESYLAINTKLSWPMESLQPRTERKVVLPGQYSESRKKRTQAIMSQVQTPPTAPGSSKKGRVGSGGTRGRKRKVSSESVQLKKRNRKSSSRATTASPGPSEDRFSFQRPQDSDDVTDVPDDMTDHEDLLPEAATRKKYERKSQTPGRRSLSSRRDDTTPVSSMAAAPPKKGRPRKNTTVTTPVLSVPKSEGRGPRKEDTTTKFVRANVLSHILSGQKLRAFYGDEWFRANAIEDATDCTDEIMDIMLAHQDFFTPDTPRLSPSAIQDLDKVLKKIRAKTHYTGWNQRYDEFMKLEKLMVTVEDQMIARGRFRHLPRGRELKAETLALVEKHFRADDEDDGVPKTLAFYLKIAQEALSLSEKRAVADDDESSDSDTDFEQKPDTSAAAAVNGGKSESEEEEEEKTVVMGGDEEAEEEVKSEDVLVESVDQESPPTTSQGTTTPETAATGGLESESDEPEYPPVPEELVPPPPVLLENFPSTDRFSSGGSSNYPTLSRQGSINSMASPMFSPNSDLSLSGPLTLPRSGPLTMANIRQSPTPDEVVGSLRKRLSQTSESSESSELPPPPSAASKSKRIRRASERSIDSASEHHRMMRSPRILTTQHSSGALIFDISTTQPTDTSGPIEALSVRKPGRRKTVFAASPTLLTSGPLTLSSSAPPPPPASPAPPQHAQKTLGRPRKTPSTSSRKPEEEDEAEQIPTTVVGVTEEASVADSSAKEDLTSEDGSATPQDEKDDSESTTTTDTITPKSIRGGKRRRGGGRFGGSYPVKPAKPGRKPKDPHAEEGADEKDPEDQTPTTMTTSTPTRADSFQTQKNRMAKLMEGKPHDYSFLDLPDFDKIIEEAPKEDINILMEERTYELREIFAQCKADLSALEKRYRQQNEAKRKAEFAAKTASSAAAAQASSSTCSTPRP
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DNA-binding protein which modulates activity of several transcription factors (By similarity). Plays a role in the modulation of endoplasmic reticulum (ER) homeostasis during chemical and pathogen stress, including exposure to the Gram-negative bacterium P.aeruginosa (PubMed:30287474).
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Q9HCL5
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MANSTGKAPPDERRKGLAFLDELRQFHHSRGSPFKKIPAVGGKELDLHGLYTRVTTLGGFAKVSEKNQWGEIVEEFNFPRSCSNAAFALKQYYLRYLEKYEKVHHFGEDDDEVPPGNPKPQLPIGAIPSSYNYQQHSVSDYLRQSYGLSMDFNSPNDYNKLVLSLLSGLPNEVDFAINVCTLLSNESKHVMQLEKDPKIITLLLANAGVFDDTLGSFSTVFGEEWKEKTDRDFVKFWKDIVDDNEVRDLISDRNKSHEGTSGEWIWESLFHPPRKLGINDIEGQRVLQIAVILRNLSFEEGNVKLLAANRTCLRFLLLSAHSHFISLRQLGLDTLGNIAAELLLDPVDFKTTHLMFHTVTKCLMSRDRFLKMRGMEILGNLCKAEDNGVLICEYVDQDSYREIICHLTLPDVLLVISTLEVLYMLTEMGDVACTKIAKVEKSIDMLVCLVSMDIQMFGPDALAAVKLIEHPSSSHQMLSEIRPQAIEQVQTQTHVASAPASRAVVAQHVAPPPGIVEIDSEKFACQWLNAHFEVNPDCSVSRAEMYSEYLSTCSKLARGGILTSTGFYKCLRTVFPNHTVKRVEDSSSNGQAHIHVVGVKRRAIPLPIQMYYQQQPVSTSVVRVDSVPDVSPAPSPAGIPHGSQTIGNHFQRTPVANQSSNLTATQMSFPVQGVHTVAQTVSRIPQNPSPHTHQQQNAPVTVIQSKAPIPCEVVKATVIQNSIPQTGVPVSIAVGGGPPQSSVVQNHSTGPQPVTVVNSQTLLHHPSVIPQQSPLHTVVPGQIPSGTPVTVIQQAVPQSHMFGRVQNIPACTSTVSQGQQLITTSPQPVQTSSQQTSAGSQSQDTVIIAPPQYVTTSASNIVSATSVQNFQVATGQMVTIAGVPSPQASRVGFQNIAPKPLPSQQVSSTVVQQPIQQPQQPTQQSVVIVSQPAQQGQTYAPAIHQIVLANPAALPAGQTVQLTGQPNITPSSSPSPVPATNNQVPTAMSSSSTPQSQGPPPTVSQMLSVKRQQQQQHSPAPPPQQVQVQVQQPQQVQMQVQPQQSNAGVGQPASGESSLIKQLLLPKRGPSTPGGKLILPAPQIPPPNNARAPSPQVVYQVASNQAAGFGVQGQTPAQQLLVGQQNVQLVPSAMPPSGGVQTVPISNLQILPGPLISNSPATIFQGTSGNQVTITVVPNTSFAPATVSQGNATQLIAPAGITMSGTQTGVGLPVQTLPATQASPAGQSSCTTATPPFKGDKIICQKEEEAKEATGLHVHERKIEVMENPSCRRGATNTSNGDTKENEMHVGSLLNGRKYSDSSLPPSNSGKIQSETNQCSLISNGPSLELGENGASGKQNSEQIDMQDIKSDLRKPLVNGICDFDKGDGSHLSKNIPNHKTSNHVGNGEISPMEPQGTLDITQQDTAKGDQLERISNGPVLTLGGSSVSSIQEASNAATQQFSGTDLLNGPLASSLNSDVPQQRPSVVVSPHSTTSVIQGHQIIAVPDSGSKVSHSPALSSDVRSTNGTAECKTVKRPAEDTDRETVAGIPNKVGVRIVTISDPNNAGCSATMVAVPAGADPSTVAKVAIESAVQQKQQHPPTYVQNVVPQNTPMPPSPAVQVQGQPNSSQPSPFSGSSQPGDPMRKPGQNFMCLWQSCKKWFQTPSQVFYHAATEHGGKDVYPGQCLWEGCEPFQRQRFSFITHLQDKHCSKDALLAGLKQDEPGQAGSQKSSTKQPTVGGTSSTPRAQKAIVNHPSAALMALRRGSRNLVFRDFTDEKEGPITKHIRLTAALILKNIGKYSECGRRLLKRHENNLSVLAISNMEASSTLAKCLYELNFTVQSKEQEKDSEMLQ
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Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes. Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin. Interacts with SRF. Forms complexes with SRF and SRF cofactors MYOCD, NKX2-5 and SRFBP1. Highly expressed in heart. Up-regulated in adult heart (at protein level). The disease is caused by variants affecting the gene represented in this entry. Differs from position 1094 onward for unknown reason. Truncated N-terminus. Unlikely isoform. Cloning artifact.
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E9Q7E2
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MANSTGKAPPDERRKGLAFLDELRQFHHSRGSPFKKIPAVGGKELDLHGLYTRVTTLGGFAKVSEKNQWGEIVEEFNFPRSCSNAAFALKQYYLRYLEKYEKVHHFGEDDDEVPPGNPKPQLPIGAIPSSYNYQQHSVSDYLRQSYGLSMDFNSPNDYNKLVLSLLSGLPNEVDFAINVCTLLSNESKHVMQLEKDPKIITLLLANAGVFDDTLGSFSSVFGEEWREKTDRDFVKFWKDIVDDNEVRDLISDRNKAHEDTPGEWIWESLFHPPRKLGINDIEGQRVLQIAVILRNLSFEESNVKLLAANRTCLRFLLLSAHSHFISLRQLGLDTLGNIAAELLLDPVDFRTTHLMFHTVTKCLMSRDRFLKMRGMEILGNLCKAEDNGVLICEYVDQDSYREIICHLTLPDVLLVTSTLEVLYMLTEMGDVACTKIAKVEKSIDVLVCLVSMDAQMFGPDALAAVKLIEHPSSSHQVLSEIRPQAIEQVQTQTHIASGPASRAVVAQHAAPPPGIVEIDSEKFACQWLNAHFEVNPDCSVSRAEMYSEYLSTCSKLARGGILTSTGFYKCLRTVFPNHTVKRVEDSTSSGQAHIHVIGVKRRALPLPIQMYYQQQPISTPVVRVDAVADLSPTPSPAGIPHGPQAAGNHFQRTPVTNQSSNLTATQMSFPVQGIHTVAQTVSRIPPNPSVHTHQQQNSPVTVIQNKAPIPCEVVKATVIQNSVPQTAVPVSISVGGAPAQNSVGQNHSAGPQPVTVVNSQTLLHHPSVMPQPSPLHTVVPGQVPSGTPVTVIQQTVPQSRMFGRVQSIPACTSTVSQGQQLITTSPQPMHTSSQQTAAGSQPQDTVIIAPPQYVTTSASNIVSATSVQNFQVATGQVVTIAGVPSPQPSRVGFQNIAPKPLPSQQVSPSVVQQPIQQPQQPAQQSVVIVSQPAQQGQAYAPAIHQIVLANPAALPAGQTVQLTGQPNITPSSSPSPVPPTNNQVPTAMSSSSTLQSQGPPPTVSQMLSVKRQQQQQHSPAAPAQQVQVQVQQPQQVQVQVQPQQPSAGVGQPAPNESSLIKQLLLPKRGPSTPGGKLILPAPQIPPPNNARAPSPQVVYQVANNQAAGFGVQGQTPAQQLLVGQQNVQLVQSAMPPAGGVQTVPISNLQILPGPLISNSPATIFQGTSGNQVTITVVPNTSFATATVSQGNAAQLIAPAGLSMSGAQASAGLQVQTLPAGQSACTTAPLPFKGDKIICQKEEEAKEATGLHVHERKIEVMENPSCRRGTTNTSNGDTSESELQVGSLLNGRKYSDSSLPPSNSGKLQSETSQCSLISNGPSLELGENGAPGKQNSEPVDMQDVKGDLKKALVNGICDFDKGDGSHLSKNIPNHKTSNHVGNGEISPVEPQGTSGATQQDTAKGDQLERVSNGPVLTLGGSPSTSSMQEAPSVATPPLSGTDLPNGPLASSLNSDVPQQRPSVVVSPHSTAPVIQGHQVIAVPHSGPRVTPSALSSDARSTNGTAECKTVKRPAEDNDRDTVPGIPNKVGVRIVTISDPNNAGCSATMVAVPAGADPSTVAKVAIESAAQQKQQHPPTYMQSVAPQNTPMPPSPAVQVQGQPSSSQPSPVSASSQHADPVRKPGQNFMCLWQSCKKWFQTPSQVFYHAATEHGGKDVYPGQCLWEGCEPFQRQRFSFITHLQDKHCSKDALLAGLKQDEPGQVANQKSSTKQPTVGGTGSAPRAQKAIASHPSAALMALRRGSRNLVFRDFTDEKEGPITKHIRLTAALILKNIGKYSECGRRLLKRHENNLSVLAISNMEASSTLAKCLYELNFTVQSKEQEKDSEML
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Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes. Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin. Interacts with SRF. Forms complexes with SRF and SRF cofactors MYOCD, NKX2-5 and SRFBP1. Highly expressed in testis, expressed in heart, liver and kidney. Belongs to the RFX family.
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Q67YT6
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MENLTEIESTMESLTEMESERVEQGTDKEIGSGEKRQDDVKETENENSGERVGEEAPVREHEDSPCLIVIEEGTSLASLEEVTNADDLPKIDDEKNSQFETSPHPSPSPSVALDTEEGLINPTAEDTVEENIVSSEVSSDILKDDGDAVEVDRDTAEVQEETANIPESKLSEDTGSPHHHADILMVQEKAAEEHDMIASGDHEEFPVNPDNKHSEENQSPHHHANNVMEQDQAAEEREIISPGEHKEIPANPDTKVVEENNDRIDEGEANNLNLAGDGSGAVDHDYLTKTELDKVLEVPGSETISKLEDRPSEHLSETSMNVEKELEMPAVEILPDNDKNSDVLAVGVSGDSDNVVSVLPASQTSSDRDEGMITVDAEPTEDMKLDVPDSKLVTDTTVDSTNNKDAHVEANTERQDNSSALVLNDANNESAPVKRVPGPYVASSNIKSEARGSGDLNNGVHKIVRTPPVFDGTMRAKRSFLLDDASDGNESGTEEDQSAFMKELDSFFRERNMDFKPPKFYGEGLNCLKLWRAVTRLGGYDKVTGSKLWRQVGESFRPPKTCTTVSWTFRGFYEKALLEYERHKVSEGELQIPLPLELEPMNIDNQASGSGRARRDAASRAMQGWHSQRLNGNGEVSDPAIKDKNLVLHQKREKQIGTTPGLLKRKRAAEHGAKNAIHVSKSMLDVTVVDVGPPADWVKINVQRTQDCFEVYALVPGLVREEVRVQSDPAGRLVISGEPENPMNPWGATPFKKVVSLPTRIDPHHTSAVVTLNGQLFVRVPLEQLE
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A number of isoforms are produced. According to EST sequences. Belongs to the small heat shock protein (HSP20) family.
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Q9C9K6
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MMADTEMQEQDVPSGTKGVVEEPSELEKDLNSIERPKSPVPEDTTHTLDSDVHLSDAPIANQIEANEEVGGQNSVDGRNGDVDQSEKKITSDGGQEETTLGESNPLKGDPSSPHVPEESVKKWKTWLLSDAEAREVDEAGAPQDQEAFIKEVEAFNKENFLEFKAPKFYGQPLNCLKLWRAVIKLGGYDVVTTSKLWRQVGESFHPPKTCTTVSWTFRIFYEKALLEYEKHLRQNGELNLPGSASLPSSGIEKEASSHQASGSGRTRRDAAARAMQGWHSQRLLGSGEVTEPIVKEKGLNSTPKQKNLKNIGVQKQKTTTGMDLVFSHESEKQSTAEVIDVGPPADWVKINVRETKDCFEIFALVPGLLREEVRVQSDPAGRLVIAGQPEQLDNPWGITPFKKVVNFPARIDPLHTSAVVSLHGRLFVRVPFEQ
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A number of isoforms are produced. According to EST sequences. Belongs to the small heat shock protein (HSP20) family.
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Q9SYP7
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MVDTEMQEQDVTFGALVETKYLEEEPLEPENDHNPSEIPQPLLLGDGQANNGHGMNGGAVGVVDHSERKTRRVQMLSPKTEGENAKKRKTWLLDSEAQGTDEAGTPVEQVAFLREVEAFYKESFLEFKPPKFYGQPLNILKLWRAVVNLGGYEVVTTNKLWRQVGESFNPPKTCTTVSYTFRNFYEKALLEYEKCLRNNGELNLPGSTLILSSSVEKEPSSHQGSGSGRARRDSAARAMQGWHAQRLVGSGEVTAPAVKDKGLISTPKHKKLKSIGLQKHKQQTSMDHVVTNEADKQLAAEVVDVGPVADWVKINVKESKDSFEIFALVPGLLRKEVRIQSDPAGKVVITGQPEQLDNPWGITPFKKIVDLSARIDPLHTSAVMSMHGRLFIRVPFEQ
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Belongs to the small heat shock protein (HSP20) family.
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P83988
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GVGYKVVVTTTAAADDDDVV
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Has antifungal activity against B.cinerea, F.oxysporum and M.arachidicola. Inhibits cell-free translation in rabbit reticulocyte lysate system. Does not have mitogenic and anti-HIV-1 reverse transcriptase activities.
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Q9BV54
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MSDESASGSDPDLDPDVELEDAEEEEEEEEVAVEECDRDDEEDLLDDPSLEGMCGTEHAQLGEDGQQPPRCTSTTSSQSEPSEQLRRHQGKNLASEDPKKKRAQKPSHMRRNIRKLLREDQLEPVTKAAQQEELERRKRLEQQRKDYAAPIPTVPLEFLPEEIALRASDGPQLPPRVLAQEVICLDSSSGSEDEKSSRDEVIELSSGEEDTLHIVDSSESVSEDDEEEEKGGTHVNDVLNQRDALGRVLVNLNHPPEEENVFLAPQLARAVKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWLPPPEALPADNKPEEVQPRFFKVHILNDEHKTMASRAKVMADWVSEGGVLLMGYEMYRLLTLKKSFATGRPKKTKKRSHPVIIDLDEEDRQQEFRREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSKIQRDLYTQFMDRFRDCGSSGWLGLNPLKAFCVCCKIWNHPDVLYEALQKESLANEQDLDVEELGSAGTSARCPPQGTKGKGEDSTLASSMGEATNSKFLQGVGFNPFQERGNNIVTYEWAKDLLTNYQTGVLENSPKMVLLFHLIEESVKLGDKILVFSQSLSTLALIEEFLGKREVPCPPGTEGQGAQKWVRNISYFRLDGSTPAFERERLINQFNDPSNLTTWLFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCYIYRLVADYTLEKKIYDRQISKQGMSDRVVDDLNPMLNFTRKEVENLLHFVEKEPAPQVSLNVKGIKESVLQLACLKYPHLITKEPFEHESLLLNRKDHKLTKAEKKAAKKSYEEDKRTSVPYTRPSYAQYYPASDQSLTSIPAFSQRNWQPTLKGDEKPVASVRPVQSTPIPMMPRHVPLGGSVSSASSTNPSMNFPINYLQRAGVLVQKVVTTTDIVIPGLNSSTDVQARINAGESIHIIRGTKGTYIRTSDGRIFAVRATGKPKVPEDGRMAASGSQGPSCESTSNGRHSASSPKAPDPEGLARPVSPDSPEIISELQQYADVAAARESRQSSPSTNAALPGPPAQLMDSSAVPGTALGTEPRLGGHCLNSSLLVTGQPCGDRHPVLDLRGHKRKLATPPAAQESSRRRSRKGHLPAPVQPYEHGYPVSGGFAMPPVSLNHNLTTPFTSQAGENSLFMGSTPSYYQLSNLLADARLVFPVTTDPLVPAGPVSSSSTATSVTASNPSFMLNPSVPGILPSYSLPFSQPLLSEPRMFAPFPSPVLPSNLSRGMSIYPGYMSPHAGYPAGGLLRSQVPPFDSHEVAEVGFSSNDDEDKDDDVIEVTGK
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DNA helicase that modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. Not able to remodel mononucleosomes in vitro (By similarity). ATP + H2O = ADP + H(+) + phosphate Enzyme activity is enhanced by dsDNA (double-stranded DNA) and ssDNA (single-stranded DNA). Interacts with AR via its N-terminus. Interacts with DYRK1A. Binds DNA and mononucleosomes, but does not seem to form large multiprotein complexes (By similarity). Localizes in speckle-like nuclear compartments. Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to be important for the association with nuclear receptors. Sumoylated. Belongs to the SNF2/RAD54 helicase family. Truncated N-terminus.
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Q3UPJ1
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MSDESASGSDPDLDPDVELEDEEEEEEEEEVAVEEHDRDDEEGLLDDTSLEGMCGTEHAQLGEDGQRPPRCTSTTSSQSEPSEQLRHQGKILASEDPKKKRAQKPSHMRRNIRKLLREDQLEPVTKAAQQEELERRKRLEQQRKEYAAPIPTVPLEFLPEEIVLRASDGPQLPPRVLAQEVICLDSSSGSEDEKSSRDEVIELSSGEEDTLHIVDSSESVSEEDEEEEKGGTHVNDALNQHDALGRVLVNLNHPPEEENVFLAPQLARAVKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWLPAPEALPADSKPEEVQPRFFKVHILNDEHKTVASRAKVTADWVSEGGVLLMGYEMYRLLTLKKSLATSRPKKTKKRSHPVIIDLDEEDRQQEFRREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSQIQRDLYTQFMDRFRDCGTSGWLGLNPLKAFCVCCKIWNHPDVLYEALQKENLANEQDLDVEELGSAGTSARCPPHGTKVKGEDSALPSSMGEATNSKFLQGVGFNPFQERGNNIVTYEWAKELLTNYQTGVLENSPKMVLLFHLIEESVKLGDKILVFSQSLSTLALIEEFLGKRDMPCLPGAEGQGTQKWVRNVSYFRLDGSTPAFERERLINQFNDPSNLTTWLFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCHIYRLVADYTLEKKIYDRQISKQGMSDRVVDDLNPMLNFTRKEVENLLHFVEKEPAPQTSLDIKGIKESVLQLACLKYPHLITKEPFEHESLLLNRKDHKLTKAEKKAAKKSYEEDKRTSVPYTRPSYAQYYPASDQSLTSIPAFSQRNWQPTLKGDEKPVASVRPVQSTPIPMMPRHVPLSGGVSSASSTNTSMNFPINYLQRAGVLVQKVVTTTDIVIPGLNSSTDVQARINAGESIHIIRGTKGTYIRTSDGRIFAVRATGKPKAPEDGRMAASGSQGPSLASTSNGRHSASSPKAPDPEGLARPVSPDSPEIISELQQYADVAAARESRQSSPSISAALPGPPGQLMDNSTIPGTALGTEPCLGGHCLNSSLLVTGQPSGGRHPVLDLRGHKRKLATPSVTQESIRRRSRKGHLPAPVQPYEHGYPVSGGFAMPPVSLNHNLTTPFTSQAGENSLFMGSNPSYYQLSNLLADARLVFPVTTDPLVPAGPVSSSSTATSVTASNPSFMLNPSVPGMLPSYSLPFSQPLLSEPRMFAPFPSPGLPSNLSRGVSVYPGYMSPHAGYPAGGLLRSQVPPFDSHEVAEVGFSSNDDEDKDDDVIEVTGK
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DNA helicase that modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. Not able to remodel mononucleosomes in vitro. Acts as an AR-coregulator in Sertoli cells. ATP + H2O = ADP + H(+) + phosphate Enzyme activity is enhanced by dsDNA (double-stranded DNA) and ssDNA (single-stranded DNA). Interacts with AR via its N-terminus. Interacts with DYRK1A. Binds DNA and mononucleosomes, but does not seem to form large multiprotein complexes. Localizes in speckle-like nuclear compartments. Expressed at relatively low level, with highest expression in testis, liver and kidney. In brain, it is expressed in hippocampal and cerebellar neurons. In testis, it is present at high level in Sertoli cell nuclei. Also present in Leydig cell (at protein level). Mainly expressed in the neural tube and limb buds during early embryonic development. Also present in testis: at the onset of spermatogenesis, it is expressed in spermatogonia, pachytene, and diplotene spermatocytes. In Sertoli cells it is expressed in a stage-dependent manner, with high expression levels at stages II-VI and VII-VIII. Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to be important for the association with nuclear receptors. Sumoylated. Death by 11.5 dpc. At 9.5 dpc and 10.5 dpc, almost all major tissues are proportionally smaller, and the neural tube is shrunk in some embryos. Dramatically reduced cell proliferation and increased apoptosis are observed in 9.5 dpc and 10.5 dpc embryos. Embryonic fibroblasts stop to grow after 2 or 3 passages and exhibit increased apoptosis and decreased DNA synthesis compared with wild-type. Belongs to the SNF2/RAD54 helicase family.
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A4IHD2
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MSDASISGSEPELDPEDMEEEEEDDEDDDEEEEEEEDEEDNDGDDEDDKQDINEKSQNAALGEDSPEQGEEGWKRSTTSGQSGQESDEAKKKRLQKPANLRRNIRKLLREDQLESVTKTAQQEELERRKRLEQQRKDYPLPLTLPPVSLDFLQEEIELRAADVSQLVKSQEIICLDSSSGESDDEGKVKSHSIKDEIIELSSGEEDNLQISDNADSTNEVDGDITTENSGSHVNDALNQADHLGRVLVNINHPPNEKDIFLAPQLARAVKSHQIGGIRFLYDNLVESLERFSGSSGFGCILAHSMGLGKTLQVISFLDVLFQHTSAKTVLAIVPVNTLQNWLAEFNMWLPPPESLPKDHNQELVQPRAFKVHTMNDEHKTTAARAKVVNDWATDGGVLLMGYEMYRLLSLKKSFTAGRKKKSKKAAGPVIIDLDEEDRQQEMLKGIEKALSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDKRLMRYRSHVLHSLLEGFVQRRGHTVLKAQLPFKEEHVILVRLSKIQRDLYTEFMNRFRDAGNSGWLGLNPLKAFCVCCKIWNHPDVLYEALQKENLANEQDLDVEDLGTNNRCNAQSGKIKVEPNSLGALMGETAHTKQLQGIVLNPSHEKANQVVTYEWAKEILSDYIPGQLQNSPKMVLLFHLIEESMRMGDKILVFSQSLSTLSIMEEFLAKRKMPIPAGSDGQEGHTWIRNVNYYRLDGSTSASERERLINQFNDPSNEKVWLFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQRKPCYIYRLVSDFTLEKKIYDRQITKQGMSDRVVDDLNPEVNFTRREVENLLHFVEEEPDASRQHLDSSSFHEAVLQKACLQYPHLITKEPFQHESLLLDRKEQKLTLAEKKAAKRGYEEEKRASVPYTRPSYTQYYPAPDHNLGNIPAFSQRHWRPLMKGDDRPVASVRPLQSTPIPMLPRHVSVNHPGSASASVHPYNFPVNYLQRAGVLVQKVVTTTDIVIPGMTTSTDVQARISAGESIHVIRGTKGTYIRTSDGRIFAIRASGKQKSGEVRRQATSGAQGSSAPYLSNGRHSTSSPSQQDSEDPPRPLSPDSPEILNELQKYADAAAARGSHTAPQLQNLGLHHQGINPAPKLQPRKRKDPQDQSSHWPSNKRNPYSQLSYPNTGGFGVTPSTMNHNLVRSSNPVFMGPGGGSSHFQLPSLLSDPQTGLPLVQDSLLTHSSGTSSAPSVPPHYLLPRGFPLPFSQSLLPQTRMFAPYPSQILNRGLPTNNPASTFPGYLSSHSNYQASPGTSSRPLPSGETELGSCEEDGRDDDVVEVTGE
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DNA helicase that modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ATP + H2O = ADP + H(+) + phosphate Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to be important for the association with nuclear receptors. Belongs to the SNF2/RAD54 helicase family.
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Q3TBK5
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MGQLIAKLMRIFGSQEHKVIIVGLDNAGKTTILYQFLTNEVVHTCSTIGSNVEEIVLRKTHFLMWDLGGQEALRSTWDTYYSNAEFVILVIDSTDRNRLLTTREELYKMLAHEALQNASVLIFANKQDVKDSMTTAEISQFLTLSAIKDHPWHIQGCCALTGEGLPAGLQWMQAQATAN
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Binds and exchanges GTP and GDP. Belongs to the small GTPase superfamily. Arf family.
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P34212
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MGLIMAKLFQSWWIGKKYKIIVVGLDNAGKTTILYNYVTKDQVETKPTIGSNVEEVSYRNLDFVIWDIGGQESLRKSWSTYYVQTDVVIVVIDSSDTTRIPIMKEQLHNMLQHEDLARAHILVLANKQDLPGAMNPAEVSTQLGLQTLRGARKWQINGCCAVKGEGLPEALEWIANNL
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GTP-binding protein that may be involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus (By similarity). Plays a role in the shedding of pathogen spores from intestinal cells (PubMed:24843160). RNAi-mediated knockdown results in disrupted clearance of intracellular pathogen N.parisii from intestinal cells. Belongs to the small GTPase superfamily. Arf family.
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Q55AD9
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MGSSLSIFASIWNRFFNNAEYKVIIVGLNAAGKTTTLYKLLLDEVVSTTPTVGSNLEEFVYRNIRLLMWDLGGQDLLRSTWNQYYINTQAVILVIDSTDRARVNLIKEELFKMLAHENLKKSIILIYANKQDLKDAMSPTELSTLLSLHSIKDHDYHIQACCALTGQGLESGLDWLVSHINKS
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May bind and exchange GTP and GDP. Belongs to the small GTPase superfamily. Arf family.
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Q0IIM2
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MGLLDRLSGLLGLKKKEVHVLCLGLDNSGKTTIINKLKPSNAQSQDIVPTIGFSIQKFKSSSLSFTVFDMSGQGRYRNLWEHYYKEGQAIIFVIDSSDKLRMVVAKEELRTLLNHPDIKHRRIPILFFANKMDLRDALTSVKVSQLLCLEDIKDKPWHICASDAIKGEGLQEGVDWLQDQIQSVKT
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Involved in membrane protein trafficking at the base of the ciliary organelle. Mediates recruitment onto plasma membrane of the BBSome complex which would constitute a coat complex required for sorting of specific membrane proteins to the primary cilia. Together with the BBSome complex and LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. May regulate cilia assembly and disassembly and subsequent ciliary signaling events such as the Wnt signaling cascade. Isoform 2 may be required for proper retinal function and organization (By similarity). Interacts with SEC61B, ARL6IP1, ARL6IP2, ARL6IP3, ARL6IP4 ARL6IP5 and ARL6IP6. Interacts (GTP-bound form) with the BBSome a complex that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (GTP-free form) with IFT27. Appears in a pattern of punctae flanking the microtubule axoneme that likely correspond to small membrane-associated patches. Localizes to the so-called ciliary gate where vesicles carrying ciliary cargo fuse with the membrane (By similarity). Belongs to the small GTPase superfamily. Arf family.
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A8XSQ6
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MGFLSSLSNLFGMGKKDVNIVVVGLDNSGKTTILNQLKTPETRSQQIVPTVGHVVTNFSTQNLSFHAFDMAGQMKYRSTWESYFHSSQGVIFVLDSSDRVRMELLKDELWLVLDHKDVASRGIPVVILANKMDIPGAMTCADITAALGLNLHRSGTWSIHSTCALTGDGLDKAMQQLSSEIQKYLETRKS
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Belongs to the small GTPase superfamily. Arf family.
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Q18510
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MGFFSSLSSLFGLGKKDVNIVVVGLDNSGKTTILNQLKTPETRSQQIVPTVGHVVTNFSTQNLSFHAFDMAGQMKYRSTWESYFHSSQGVIFVLDSSDRLRMELLKDELMMVMEHKDVVSRGIPIVILANKMDIPGAMTASDITVALGLNLYRSGTWSIHSTCALTGDGLDKAMQQLSAEITKYMESRRT
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Specifically expressed in ciliated cells. Belongs to the small GTPase superfamily. Arf family.
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Q5M9P8
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MGLFDKLAGWLGLKKKEVNVLCLGLDNSGKTTIINQLKPSNAQAQDIVPTIGFSIEKFKTSSLSFTVFDMSGQGRYRNLWEHYYKEGQAIIFVIDSGDKLRMVVAKEELDTLLNHPDIKHRRIPLLFFANKMDLRDALSAVKVSQLLCLENIKDKPWHICASDAVKGEGLLEGVDWLQDQIRAMKT
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Probably involved in membrane protein trafficking at the base of the ciliary organelle. May function in cilia biogenesis. Isoform 2 is required for proper retinal function and organization. Expressed in brain, heart and eye. Isoform 2 is expressed only in the retina. Expressed throughout all the development stages. Isoform 2 is not expressed until 48 hours post fertilization. Results in the cardinal features of Bardet-Biedl syndrome in zebrafish, including defects to the ciliated Kupffer's vesicle and delayed retrograde melanosome transport. Isoform 2 defects does not result in Kupffer vesicle or melanosome transport defects, but rather leads to impaired visual function and mislocalization of the photopigment green cone opsin. Isoform 2, but not isoform 1, is sufficient to rescue both the vision defect as well as green opsin localization in the retina. Belongs to the small GTPase superfamily. Arf family.
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D3DN31
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MGLLDRLSVLLGLKKKEVHVLCLGLDNSGKTTIINKLKPSNAQSQNILPTIGFSIEKFKSSSLSFTVFDMSGQGRYRNLWEHYYKEGQAIIFVIDSSDRLRMVVAKEELDTLLNHPDIKHRRIPILFFANKMDLRDAVTSVKVSQLLCLENIKDKPWHICASDAIKGEGLQEGVDWLQDQIQTVKT
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Involved in membrane protein trafficking at the base of the ciliary organelle. Mediates recruitment onto plasma membrane of the BBSome complex which would constitute a coat complex required for sorting of specific membrane proteins to the primary cilia (PubMed:20603001). Together with BBS1, is necessary for correct trafficking of PKD1 to primary cilia (By similarity). Together with the BBSome complex and LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation (PubMed:22072986). May regulate cilia assembly and disassembly and subsequent ciliary signaling events such as the Wnt signaling cascade (PubMed:20207729). Isoform 2 may be required for proper retinal function and organization (By similarity). Interacts with SEC61B, ARL6IP1, ARL6IP2, ARL6IP3, ARL6IP4 ARL6IP5 and ARL6IP6. Interacts (GTP-bound form) with the BBSome a complex that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (GTP-free form) with IFT27. Appears in a pattern of punctae flanking the microtubule axoneme that likely correspond to small membrane-associated patches. Localizes to the so-called ciliary gate where vesicles carrying ciliary cargo fuse with the membrane. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Belongs to the small GTPase superfamily. Arf family.
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Q3TY77
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MGLLDRLSGLLGLKKKEVHVLCLGLDNSGKTTIINKLKPSNAQSQDIVPTIGFSIEKFKSSSLSFTVFDMSGQGRYRNLWEHYYKDGQAIIFVIDSSDKLRMVVAKEELDTLLNHPDIKHRRIPILFFANKMDLRDSVTSVKVSQLLCLESIKDKPWHICASDAIKGEGLQEGVDWLQDQIQAVKT
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Involved in membrane protein trafficking at the base of the ciliary organelle (By similarity). Mediates recruitment onto plasma membrane of the BBSome complex which would constitute a coat complex required for sorting of specific membrane proteins to the primary cilia (By similarity). Together with BBS1, is necessary for correct trafficking of PKD1 to primary cilia (PubMed:24939912). Together with the BBSome complex and LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation (By similarity). May regulate cilia assembly and disassembly and subsequent ciliary signaling events such as the Wnt signaling cascade (By similarity). Isoform 2 may be required for proper retinal function and organization (PubMed:20333246). Interacts with SEC61B, ARL6IP1, ARL6IP2, ARL6IP3, ARL6IP4 ARL6IP5 and ARL6IP6. Interacts (GTP-bound form) with the BBSome a complex that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (GTP-free form) with IFT27. Appears in a pattern of punctae flanking the microtubule axoneme that likely correspond to small membrane-associated patches. Localizes to the so-called ciliary gate where vesicles carrying ciliary cargo fuse with the membrane (By similarity). Most abundant in brain and kidney. Expressed in heart and eye. Isoform 2 is expressed only in the retina. Isoform 2 deficient mice present a disruption of the normal photoreceptor architecture. Belongs to the small GTPase superfamily. Arf family.
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Q5R400
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MGLLDRLSILLGLKKKEVHVLCLGLDNSGKTTIINKLKPSNAQSQNILPTIGFSIEKFKSSSLSFTVFDMSGQGRYRNLWEHYYKEGQAIIFVIDSSDRLRMVVAKEELDTLLNHPDIKHRRIPILFFANKMDLRDAVTSVKVSQLLCLENIKDKPWHICASDAIKGEGLQEGVDWLQDQIQTVKT
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Involved in membrane protein trafficking at the base of the ciliary organelle. Mediates recruitment onto plasma membrane of the BBSome complex which would constitute a coat complex required for sorting of specific membrane proteins to the primary cilia. Together with the BBSome complex and LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. May regulate cilia assembly and disassembly and subsequent ciliary signaling events such as the Wnt signaling cascade. Isoform 2 may be required for proper retinal function and organization (By similarity). Interacts with SEC61B, ARL6IP1, ARL6IP2, ARL6IP3, ARL6IP4 ARL6IP5 and ARL6IP6. Interacts (GTP-bound form) with the BBSome a complex that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (GTP-free form) with IFT27. Appears in a pattern of punctae flanking the microtubule axoneme that likely correspond to small membrane-associated patches. Localizes to the so-called ciliary gate where vesicles carrying ciliary cargo fuse with the membrane (By similarity). Belongs to the small GTPase superfamily. Arf family.
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Q9M2X1
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MGLLEAFLNWLRSLFFKQEMELSLIGLQNAGKTSLVNVVATGGYSEDMIPTVGFNMRKVTKGNVTIKLWDLGGQPRFRSMWERYCRAVSAIVYVVDAADPDNLSVSKSELHDLLSKTSLNGIPLLVLGNKIDKPGALSKEALTDEMGLTSLTDREVCCFMISCKNSTNIDQVIDWLVKHSKSKN
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May play a role in lysosome motility. May play a role in chromosome segregation. (Microbial infection) Component of tomato mosaic virus (ToMV) RNA replication complexes. Required for tobamovirus multiplication, especially for efficient negative-strand RNA synthesis and viral RNA capping. Interacts with tubulin. Localizes with microtubules at the spindle mid-zone during mitosis. In double and triple mutants arl8a-1 arl8b-1 and arl8a-1 arl8b-1 arl8c-1, impaired multiplication of tomato mosaic virus (ToMV) associated with reduced production of negative-strand RNA. Belongs to the small GTPase superfamily. Arf family.
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Q5ZKQ8
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MLALFNKLLDWFRALFWKEEMELTLVGLQYSGKTTFVNVIASGQFNEDMIPTVGFNMRKITKGNVTIKLWDIGGQPRFRSMWERYCRGVSAIVYMVDAADQEKIEASKNELHNLLDKPQLQGIPVLVLGNKRDLPGALDEKELIEKMNLSAIQDREICCYSISCKEKDNIDITLQWLIQHSKSRRS
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Plays a role in lysosome motility. In neurons, mediates the anterograde axonal long-range transport of presynaptic lysosome-related vesicles required for presynaptic biogenesis and synaptic function (By similarity). May play a role in chromosome segregation (By similarity). Localizes with microtubules at the spindle mid-zone during mitosis. Belongs to the small GTPase superfamily. Arf family.
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B3KXD0
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MIALFNKLLDWFKALFWKEEMELTLVGLQYSGKTTFVNVIASGQFNEDMIPTVGFNMRKITKGNVTIKLWDIGGQPRFRSMWERYCRGVSAIVYMVDAADQEKIEASKNELHNLLDKPQLQGIPVLVLGNKRDLPGALDEKELIEKMNLSAIQDREICCYSISCKEKDNIDITLQWLIQHSKSRRS
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Plays a role in lysosome motility (By similarity). In neurons, mediates the anterograde axonal long-range transport of presynaptic lysosome-related vesicles required for presynaptic biogenesis and synaptic function (By similarity). May play a role in chromosome segregation (By similarity). Interacts with PLEKHM1. Localizes with microtubules at the spindle mid-zone during mitosis. Ubiquitously expressed. Belongs to the small GTPase superfamily. Arf family.
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Q9CTB0
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MIALFNKLLDWFKALFWKEEMELTLVGLQYSGKTTFVNVIASGQFNEDMIPTVGFNMRKITKGNVTIKLWDIGGQPRFRSMWERYCRGVSAIVYMVDAADQEKIEASKNELHNLLDKPQLQGIPVLVLGNKRDLAGALDEKELIEKMNLSAIQDREICCYSISCKEKDNIDITLQWLIQHSKSRRS
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Plays a role in lysosomes motility (PubMed:30174114). In neurons, mediates the anterograde axonal long-range transport of presynaptic lysosome-related vesicles required for presynaptic biogenesis and synaptic function (PubMed:30174114). May play a role in chromosome segregation (By similarity). Interacts with PLEKHM1. Localizes with microtubules at the spindle mid-zone during mitosis. Belongs to the small GTPase superfamily. Arf family.
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Q6P8C8
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MLALFNKLLDWFKALFWKEEMELTLVGLQYSGKTTFVNVIASGQFNEDMIPTVGFNMRKITKGNVTIKLWDIGGQPRFRSMWERYCRGVSAIVYMVDAADQDKIEASKNELHNLLDKAQLQGIPVLVLGNKRDIPGALDEKELIERMNLSAIQDREICCYSISCKEKDNIDITLQWLIQHSKSRRS
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May play a role in lysosomes motility. Alternatively, may play a role in chromosome segregation (By similarity). Belongs to the small GTPase superfamily. Arf family.
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Q9FJW7
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MGLWDALLNWLRSLFFKQEMELSLIGLQNAGKTSLVNVVATGGYSEDMIPTVGFNMRKVTKGSVTIKLWDLGGQPRFRSMWERYCRSVSAIVYVVDAADPDNLSVSKSELHDLLSKTSLNGIPLLVLGNKIDKPGALSKEALTDEMGLKSLTDREVCCFMISCKNSTNIDQVIDWLVKHSKSSN
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May play a role in lysosome motility. May play a role in chromosome segregation. (Microbial infection) Component of tomato mosaic virus (ToMV) RNA replication complexes. Required for tobamovirus multiplication, especially for efficient negative-strand RNA synthesis and viral RNA capping. Interacts with tubulin. Localizes with microtubules at the spindle mid-zone during mitosis. In double and triple mutants arl8a-1 arl8b-1 and arl8a-1 arl8b-1 arl8c-1, impaired multiplication of tomato mosaic virus (ToMV). Belongs to the small GTPase superfamily. Arf family.
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Q2KI07
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MLALISRLLDWFRSLFWKEEMELTLVGLQYSGKTTFVNVIASGQFSEDMIPTVGFNMRKVTKGNVTIKIWDIGGQPRFQSMWERYCRGVNAIVYMIDAADREKIEASRNELHNLLDKPQLQGIPVLVLGNKRDLPNALDEKQLIEKMNLSAIQDREICCYSISCKEKDNIDITLQWLIQHSKSRRS
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Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins playing a key role in the regulation of lysosomal positioning which is important for nutrient sensing, natural killer cell-mediated cytotoxicity and antigen presentation. Along with its effectors, orchestrates lysosomal transport and fusion. Localizes specifically to lysosomal membranes and mediates anterograde lysosomal motility by recruiting PLEKHM2, which in turn recruits the motor protein kinesin-1 on lysosomes. Required for lysosomal and cytolytic granule exocytosis. Critical factor involved in NK cell-mediated cytotoxicity. Drives the polarization of cytolytic granules and microtubule-organizing centers (MTOCs) toward the immune synapse between effector NK lymphocytes and target cells (By similarity). In neurons, mediates the anterograde axonal long-range transport of presynaptic lysosome-related vesicles required for presynaptic biogenesis and synaptic function (By similarity). Also acts as a regulator of endosome to lysosome trafficking pathways of special significance for host defense. Regulates cargo trafficking to lysosomes by binding to PLEKHM1 and recruiting the HOPS subunit VPS41, resulting in functional assembly of the HOPS complex on lysosomal membranes. Plays an important role in cargo delivery to lysosomes for antigen presentation and microbial killing. Directs the intersection of CD1d with lipid antigens in lysosomes, and plays a role in intersecting phagosomes with lysosomes to generate phagolysosomes that kill microbes (By similarity). Involved in the process of MHC II presentation. Regulates the delivery of antigens to lysosomes and the formation of MHC II-peptide complexes through the recruitment of the HOPS complex to lysosomes allowing the fusion of late endosomes to lysosomes (By similarity). May play a role in chromosome segregation (By similarity). GTP + H2O = GDP + H(+) + phosphate Interacts with tubulin. Interacts with BORCS5; recruits ARL8B to lysosomes. Interacts with VPS41; the interaction mediates the recruitment of the HOPS complex to lysosomes. Interacts (GTP-bound form) with PLEKHM2 (via RUN domain); the interaction is required to recruit the motor protein kinesin-1 on lysosomes. Interacts (GTP-bound form) with PLEKHM1 (via RUN domain); the interaction is required for PLEKHM1 localization to lysosomes and for ARL8B function in delivery and degradation of endocytic and autophagic cargo in lysosomes. PLEKHM1 and PLEKHM2 compete for interaction with ARL8B. GTP-bound form resides on lysosomal membranes, whereas GDP-bound form is likely associated with microtubular structures. Localizes with microtubules at the spindle mid-zone during mitosis (By similarity). In dendritic cells, localizes to MHC II+ compartments (By similarity). Ubiquitinated at Lys-141 by RNF167, leading to its degradation. Belongs to the small GTPase superfamily. Arf family.
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B4DI85
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MLALISRLLDWFRSLFWKEEMELTLVGLQYSGKTTFVNVIASGQFSEDMIPTVGFNMRKVTKGNVTIKIWDIGGQPRFRSMWERYCRGVNAIVYMIDAADREKIEASRNELHNLLDKPQLQGIPVLVLGNKRDLPNALDEKQLIEKMNLSAIQDREICCYSISCKEKDNIDITLQWLIQHSKSRRS
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Small GTPase which cycles between active GTP-bound and inactive GDP-bound states (PubMed:15331635, PubMed:16537643). In its active state, binds to a variety of effector proteins playing a key role in the regulation of lysosomal positioning which is important for nutrient sensing, natural killer cell-mediated cytotoxicity and antigen presentation. Along with its effectors, orchestrates lysosomal transport and fusion (PubMed:16650381, PubMed:16537643, PubMed:28325809, PubMed:25898167, PubMed:27808481). Localizes specifically to lysosomal membranes and mediates anterograde lysosomal motility by recruiting PLEKHM2, which in turn recruits the motor protein kinesin-1 on lysosomes. Required for lysosomal and cytolytic granule exocytosis (PubMed:22172677, PubMed:29592961, PubMed:24088571). Critical factor involved in NK cell-mediated cytotoxicity. Drives the polarization of cytolytic granules and microtubule-organizing centers (MTOCs) toward the immune synapse between effector NK lymphocytes and target cells (PubMed:24088571). In neurons, mediates the anterograde axonal long-range transport of presynaptic lysosome-related vesicles required for presynaptic biogenesis and synaptic function (By similarity). Also acts as a regulator of endosome to lysosome trafficking pathways of special significance for host defense (PubMed:21802320). Regulates cargo trafficking to lysosomes by binding to PLEKHM1 and recruiting the HOPS subunit VPS41, resulting in functional assembly of the HOPS complex on lysosomal membranes (PubMed:16537643, PubMed:25908847). Plays an important role in cargo delivery to lysosomes for antigen presentation and microbial killing. Directs the intersection of CD1d with lipid antigens in lysosomes, and plays a role in intersecting phagosomes with lysosomes to generate phagolysosomes that kill microbes (PubMed:25908847, PubMed:21802320). Involved in the process of MHC II presentation. Regulates the delivery of antigens to lysosomes and the formation of MHC II-peptide complexes through the recruitment of the HOPS complex to lysosomes allowing the fusion of late endosomes to lysosomes (By similarity). May play a role in chromosome segregation (PubMed:15331635). (Microbial infection) During Mycobacterium tuberculosis (Mtb) infection, is required for plasma membrane repair by controlling the exocytosis of lysosomes in macrophages. ARL8B secretion pathway is crucial to control the type of cell death of the M. tuberculosis-infected macrophages, distinguishing avirulent from virulent Mtb induced necrotic cell death. (Microbial infection) During infection, coronaviruses such as SARS-CoV-2 and the chaperone HSPA5/GRP78 are probably co-released through ARL8B-dependent lysosomal exocytic pathway for unconventional egress. GTP + H2O = GDP + H(+) + phosphate Interacts with tubulin (PubMed:15331635, Ref.25). Interacts with BORCS5; recruits ARL8B to lysosomes (PubMed:25898167). Interacts with VPS41; the interaction mediates the recruitment of the HOPS complex to lysosomes (PubMed:21802320, PubMed:25908847). Interacts (GTP-bound form) with PLEKHM2 (via RUN domain); the interaction is required to recruit the motor protein kinesin-1 on lysosomes (PubMed:22172677, PubMed:28325809). Interacts (GTP-bound form) with PLEKHM1 (via RUN domain); the interaction is required for PLEKHM1 localization to lysosomes and for ARL8B function in delivery and degradation of endocytic and autophagic cargo in lysosomes (PubMed:28325809). PLEKHM1 and PLEKHM2 compete for interaction with ARL8B (PubMed:28325809). GTP-bound form resides on lysosomal membranes, whereas GDP-bound form is likely associated with microtubular structures (PubMed:16650381). Localizes with microtubules at the spindle mid-zone during mitosis. In dendritic cells, localizes to MHC II+ compartments (By similarity). Ubiquitously expressed. Ubiquitinated at Lys-141 by RNF167, leading to its degradation. Belongs to the small GTPase superfamily. Arf family.
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Q4R4S4
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MLALISRLLDWFRSLFWKEEMELTLVGLQYSGKTTFVNVIASGQFSEDMIPTVGFNMRKVTKGNVTIKIWDIGGQPRYRSMWERYCRGVNAIVYMIDAADREKIEASRNELHNLLDKPQLQGIPVLVLGNKRDLPNALDEKQLIEKMNLSAIQDREICCYSISCKEKDNIDITLQWLIQYSKSRRS
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Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins playing a key role in the regulation of lysosomal positioning which is important for nutrient sensing, natural killer cell-mediated cytotoxicity and antigen presentation. Along with its effectors, orchestrates lysosomal transport and fusion. Localizes specifically to lysosomal membranes and mediates anterograde lysosomal motility by recruiting PLEKHM2, which in turn recruits the motor protein kinesin-1 on lysosomes. Required for lysosomal and cytolytic granule exocytosis. Critical factor involved in NK cell-mediated cytotoxicity. Drives the polarization of cytolytic granules and microtubule-organizing centers (MTOCs) toward the immune synapse between effector NK lymphocytes and target cells (By similarity). In neurons, mediates the anterograde axonal long-range transport of presynaptic lysosome-related vesicles required for presynaptic biogenesis and synaptic function (By similarity). Also acts as a regulator of endosome to lysosome trafficking pathways of special significance for host defense. Regulates cargo trafficking to lysosomes by binding to PLEKHM1 and recruiting the HOPS subunit VPS41, resulting in functional assembly of the HOPS complex on lysosomal membranes. Plays an important role in cargo delivery to lysosomes for antigen presentation and microbial killing. Directs the intersection of CD1d with lipid antigens in lysosomes, and plays a role in intersecting phagosomes with lysosomes to generate phagolysosomes that kill microbes (By similarity). Involved in the process of MHC II presentation. Regulates the delivery of antigens to lysosomes and the formation of MHC II-peptide complexes through the recruitment of the HOPS complex to lysosomes allowing the fusion of late endosomes to lysosomes (By similarity). May play a role in chromosome segregation (By similarity). GTP + H2O = GDP + H(+) + phosphate Interacts with tubulin. Interacts with BORCS5; recruits ARL8B to lysosomes. Interacts with VPS41; the interaction mediates the recruitment of the HOPS complex to lysosomes. Interacts (GTP-bound form) with PLEKHM2 (via RUN domain); the interaction is required to recruit the motor protein kinesin-1 on lysosomes. Interacts (GTP-bound form) with PLEKHM1 (via RUN domain); the interaction is required for PLEKHM1 localization to lysosomes and for ARL8B function in delivery and degradation of endocytic and autophagic cargo in lysosomes. PLEKHM1 and PLEKHM2 compete for interaction with ARL8B. GTP-bound form resides on lysosomal membranes, whereas GDP-bound form is likely associated with microtubular structures. Localizes with microtubules at the spindle mid-zone during mitosis (By similarity). In dendritic cells, localizes to MHC II+ compartments (By similarity). Ubiquitinated at Lys-141 by RNF167, leading to its degradation. Belongs to the small GTPase superfamily. Arf family.
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Q3UJU2
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MLALISRLLDWFRSLFWKEEMELTLVGLQYSGKTTFVNVIASGQFSEDMIPTVGFNMRKVTKGNVTIKIWDIGGQPRFRSMWERYCRGVNAIVYMIDAADREKIEASRNELHNLLDKPQLQGIPVLVLGNKRDLPNALDEKQLIEKMNLSAIQDREICCYSISCKEKDNIDITLQWLIQHSKSRRS
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Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins playing a key role in the regulation of lysosomal positioning which is important for nutrient sensing, natural killer cell-mediated cytotoxicity and antigen presentation (PubMed:33157038, PubMed:30174114). Along with its effectors, orchestrates lysosomal transport and fusion. Localizes specifically to lysosomal membranes and mediates anterograde lysosomal motility by recruiting PLEKHM2, which in turn recruits the motor protein kinesin-1 on lysosomes. Required for lysosomal and cytolytic granule exocytosis. Critical factor involved in NK cell-mediated cytotoxicity. Drives the polarization of cytolytic granules and microtubule-organizing centers (MTOCs) toward the immune synapse between effector NK lymphocytes and target cells (By similarity). In neurons, mediates the anterograde axonal long-range transport of presynaptic lysosome-related vesicles required for presynaptic biogenesis and synaptic function (PubMed:30174114). Also acts as a regulator of endosome to lysosome trafficking pathways of special significance for host defense. Regulates cargo trafficking to lysosomes by binding to PLEKHM1 and recruiting the HOPS subunit VPS41, resulting in functional assembly of the HOPS complex on lysosomal membranes. Plays an important role in cargo delivery to lysosomes for antigen presentation and microbial killing. Directs the intersection of CD1d with lipid antigens in lysosomes, and plays a role in intersecting phagosomes with lysosomes to generate phagolysosomes that kill microbes (PubMed:21802320). Involved in the process of MHC II presentation. Regulates the delivery of antigens to lysosomes and the formation of MHC II-peptide complexes through the recruitment of the HOPS complex to lysosomes allowing the fusion of late endosomes to lysosomes (PubMed:25637027). May play a role in chromosome segregation (By similarity). (Microbial infection) During infection, murine coronavirus (MHV) and the chaperone HSPA5/GRP78 are co-released through ARL8B-dependent lysosomal exocytic pathway for unconventional egress. GTP + H2O = GDP + H(+) + phosphate Interacts with tubulin. Interacts with BORCS5; recruits ARL8B to lysosomes. Interacts with VPS41; the interaction mediates the recruitment of the HOPS complex to lysosomes. Interacts (GTP-bound form) with PLEKHM2 (via RUN domain); the interaction is required to recruit the motor protein kinesin-1 on lysosomes. Interacts (GTP-bound form) with PLEKHM1 (via RUN domain); the interaction is required for PLEKHM1 localization to lysosomes and for ARL8B function in delivery and degradation of endocytic and autophagic cargo in lysosomes. PLEKHM1 and PLEKHM2 compete for interaction with ARL8B. GTP-bound form resides on lysosomal membranes, whereas GDP-bound form is likely associated with microtubular structures. Localizes with microtubules at the spindle mid-zone during mitosis (By similarity). In dendritic cells, localizes to MHC II+ compartments (PubMed:25637027). Ubiquitinated at Lys-141 by RNF167, leading to its degradation. Belongs to the small GTPase superfamily. Arf family.
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Q0BWK6
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MADDKGQMMWGGRFAATPSAIMEEINASLDIDRRMAEEDVAGSRAHADMLAEMGILSVADNEAIQGGLDAVIEEMRAGTFPFRRELEDIHMNVEARLKELIGEPAGRLHTARSRNDQVITDFRLWTRRALDETGQLVAGLQAMLVRRADENTSTVMPGFTHLQTAQPVTLGHHLLAYVEMLERDRSRLLDCAVRLNECPLGAAALAGTGFPIDRDMTAEALGFARPMANSLDAVSARDFALEALSSLSIAATHLSRLAEEIVLWTSPQFGFARLSDQWSTGSSIMPQKRNPDAAELIRAKASLITGHFSALQGAIKALPLAYAKDLQDDKRLTFDAFDTFNLCVRAMTGMIETISFKPDAMRAAAAKGFSTATDLADWLVRELGMPFRDAHHVTGRIVARAEAKGVDLADLPLKEMQAVHSAITQEVYGVLSVEASAASRTSYGATSPVRVAEQVAQWKQRLRVE
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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A6SX31
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MTAQLSKKSEAWSARFNEPVSDLVKRYTASVFFDKRLAQVDIQGSLAHAEMLAHQKIISQQDHAEIQRGMAQIQEEIASGKFEWLLDLEDVHLNIEKRLTELVGDAGKRLHTGRSRNDQVATDIRLYVRSEIDNIVGLLRDLRLALLDLAEKHADTILPGFTHMQVAQPITFGHHMLAYVEMFSRDAERMLDCRKRVNRLPLGAAALAGTTFPIDRERVARTLDFEDVCHNSLDAVSDRDFAIEFCAAAALIMTHVSRMSEELVIWMSPRVGFIDIADRFCTGSSIMPQKKNPDVPELARGKTGRVNGHLIALLTLMKGQPLAYNKDNQEDKEPLFDTVDTVVDTLRIFADMATGITVKPDAMRAAALQGYATATDLADYLVKKGLPFRDAHEAVAHAVRACVDRGCDLSDLTLEEMRVFSPLIEADIFEVLTLEGSVAARNHIGGTAPQQVRLAIARHRSKLN
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q28V48
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MTDTGSSDTNTDTTGTSKANTMWGGRFAAGPDAIMEAINASISFDQRMARQDIEGSRAHAAMLAATGIVESSDVDVIREGLLTVLSEIEGGTFQYSTALEDIHMNVEARLTEIIGTPAGRLHTARSRNDQVATDFKLWVRDQMDAAISGIEALQRALLGQAEAGADWVMPGFTHLQTAQPVTWGHHMMAYVEMLGRDASRFRDARTRMNESPLGAAALAGTSFPIDRDMTAEALGFDRPSANSLDAVADRDFALEFLSAASICAMHLSRFAEELVIWSSAQFRFVALSDRFSTGSSIMPQKKNPDAAELIRAKIGRIFGANVALMTVMKGLPLTYSKDMQEDKEQTFDAADNLMLALAAMEGMVRDMQANVPSLEAAASSGFSTATDLADWLVRELNMPFREAHHVTGSLVKLAEDKGCDLPDLALSDMHSVHGDITDGVFDVLGVHNSVASRTSYGGTSPVQVREQVARWRDILG
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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A6WCT0
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MTQSTDPQGEKGLWGARFASGPATAMAALSKSTHFDFRLARYDLAGSRAHARVLHAAGLLDDDVLTALLAGLDALEADVVSGAFVPAEEDEDVHSALERALVERVGADVGGRLRAGRSRNDQIATLLRMFLRDHARVVAGLVLDVVEALLTQAAAHPGAAMPGRTHLQHAQPVLLGHHLMAHAWPLLRDVERLRDWDARAAVSPYGSGALAGSSLGLDPVAVARELGFTRSVENSIDGTASRDVAAEFAFVAAMIGVDLSRISEEVIAWATKEFSFVTLDDAWSTGSSIMPQKKNPDVAELARGKAGRLIGDLTGLLATLKGLPLAYNRDLQEDKEPVFDAVDTLEVLLPAVAGMVATLHFHTDRMASLAPQGFALATDIAEWLVRRGVPFRDAHRISGACVRRCEERAIAEGRGVELWDLTVEDLAAISPHLAPAVRDVLSTEGSLSSRDGIGGTAPVRVAEQLEAAQDALAAHLAWARP
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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B5XZ16
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MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLSAAEQQQLEEALNVLLEEVRANPQQILASDAEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVVELLSANRQLQSALVETAQHNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSDASIGMVHLSRFAEDLIFFNSGEANFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHMATLVLDGIQVKRPRCAEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIAQGKPLEALPLVDLQKFSPVIADDVYPILSLQSCLDKRAAKGGVSPQQVAQAISDAKARLS
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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A6TGE4
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MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLSAAEQQQLEEALNVLLEEVRANPQQILASDAEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVVELLSANRQLQSALVETAQQNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSDAAIGMVHLSRFAEDLIFFNSGEANFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCAEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIAQGKPLEALTLADLQKFSPVIADDVYPILSLQSCLEKRAAKGGVSPQQVAQAINEAKARLS
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q1IIZ3
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MKMWSGRFSQSLDPEFESWQRSLPFDKKLLRHEVAASGAHATALAKAGVLSSEELALIKSGLAQIARDGAPDADDPSIEDVHHFVESRLIEIAGEVGRKLHTGRSRNEQIATDLRLYVREQIDETTLLIADVIAALIERAESVGEAAMPSYTHLQRAEPVLIAHWLLAYAEMFFRDITRLADCRKRANLCPLGSAAVAGTFVALDRGYIATLLGFDAPTANSIDATSDRDFAIEFVQSLSVIGLHLSRMAEEMILFATTEFGFLQLPEQFATGSSAMPQKKNPDSLELVRGKSAALLAHAMQLAVTLKALPLAYNKDMQETQQPVFASAEECIAMLRITAGFLRAVKFNTAVMHTAASTGYMNAMAAAGYLVQQGIPFRRAHELIGAAVKLAVEKHCELHDLSADDLRNLGIAADDSFYAALQLPAVLAQKNVAGGTAPNQVSTALKAAKKKLIAIGEVQHVSA
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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C4Z0V2
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MKLWGGRFTKETNELVNNFNASISFDQKFYKQDIEGSIAHATMLGKQGIIPESESEQIVEGLKGILADIESGKLEITDEYEDIHTFMEATLIERIGDAGKRLHTGRSRNDQVALDMRLFTRQEVLNTDAELKELMAVILRIMKENTHTFMPGFTHLQKAQPVTVAHHFGAYFEMFKRDRSRLHDIYERMNYCPLGAGALAGTTYPLDRELTASLLGFYGPTLNSMDSVSDRDYLIEFLSALSTIMMHLSRFSEEICIWNSNEYRFIELDDAFSTGSSIMPQKKNPDIAELVRGKTGRVYGALISLLTTMKGIPLAYNKDMQEDKELSFDAFDTAKGCISLFKGMIDTMKFNNKRMEASAKNGFTNATDAADYLVKKGVPFREAHGIVGQLVLMCIEKNIALDDLSLDEYKAVSPVFDEDIYEAISLQTCVDKRLTLGAPGPEVMNKVIAIYDKYMEEN
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q9CJ76
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MVEKLWGGRFEASLDKQTEEFGASIKFEQRLAPFDLKGSLAHVKMLGETGIITTEESKKIAEGLKKVEEKLLNGQIEFKMENEDIHMNMESYLHQEIGPLAGKLHTARSRNDQVVTDMHLYLKSILEAVLEALKVLRETIVKLAVNQIDTIMPGYTHLQHAQPISFGQHLMAYYQMLTRDFERFEFNVKHTDMNPLGAAALAGTTFPIDRMLTTKLLGFEKAYDNSMDAVSDRDFILEFLSNASLLMMHLSRFCEELLLWSSHEFKFVSLSDTYSTGSSIMPQKKNPDMAELIRGKTGRVYGNLTALLTVMKGLPLAYNKDFQEDKEGMFDSADTIITSLTVMNGMLSTLTVNRVNMEKSTEQDFSNATELADYLATKGLPFRKAHELVGLLVLDCIKKGIYLQDVNLQDYQMLSPLINEDVYEVLKSRTAVSRRNSLGGTGFESVKKQIEEAKKELQI
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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A2RHL0
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MVEKLWGGRFEASLDKQTEEFGASIKFEQRLAPFDLKGSLAHVKMLGETGIITAEEATTIADGLIKVEEKLMKGQIEFKIENEDIHMNMETYLHDEIGPLAGKLHTARSRNDQVATDMHLYLKSVLSDLLKALRTLRETIVNLSVNHVDTLMPGYTHLQHAQPISFAQHLMAYYQMFTRDFERFEFNVKHTDMNPLGAAALAGTTFPIDRELTTNLLQFEKVYANSMDAVSDRDFILEFLSNSSLLMMHLSRLCEELLLWSSHEFNFVSLSDNYSTGSSIMPQKKNPDMAELIRGKSGRVYGNLISLLTVMKGLPLTYNKDLQEDKEGMFDSADTILTSLSVMDGMLSTMTVNRVNMEKATEQDFSNATELADYLAAKGLPFREAHELVGQLVLKCIKKGIYLQEVSLKDYQALSQLIEEDVYEILKSRTAVSRRNSLGGTGFESIKKQIEQAKKELQK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q032X5
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MVEKLWGGRFEASLDKQTEEFGASIKFEQRLAPFDLKGSLAHVKMLGETGIITAEEATTIANGLIKVEEKLMKGQIEFKIENEDIHMNMETYLHDEIGPLAGKLHTARSRNDQVATDMHLYLKSVLSDLLKALRTLRETIVNLSVNHVDTLMPGYTHLQHAQPISFAQHLMAYYQMFTRDFDRFEFNVKHTDMNPLGAAALAGTTFPIDRELTTNLLQFEKAYANSMDAVSDRDFILEFLSNSSLLMMHLSRLCEELLLWSSHEFNFVSLSDNYSTGSSIMPQKKNPDMAELIRGKSGRVYGNLMSLLTVMKGLPLTYNKDLQEDKEGMFDSADTILTSLSVMDGMLSTMTVNRVNMEKATEQDFSNATELADYLAAKGLPFREAHELVGQLVLTCIKKGIYLQEVSLKDYQALSQLIEEDVYEILQSRTAVSRRNSLGGTGFESIKKQIEQAKKELQK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q033U6
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MTDKLWGGRFTEKAAHWVDAFGASIGFDQQMAQEDLEGSLAHVKMLGKTGIIPQADADTITAGLQHLQKELAAGKLHFTVENEDIHLNMEALLTAEIGPVAGKLHTARSRNDQVATDLHLWLKHRLPTIKEALTNLQTVLVGQAKVHAATIMPGYTHMQHAQPITYGHYLLAYFEMFQRDWERFDFTQKHTDILPLGAAALAGTTFPIDRTLVAQELGFDQIYHNSLDAVSDRDFALEFLSNSAILMQHLSRMAEELILWSTYEFNYIELGDDFSTGSSIMPQKKNPDFAELIRGKTGRVYGALMGLLTTMKAIPLAYNKDMQEDKEPIFDAYNTILGSLHIFTGMLSDLTVHEKRMAEATTHDFSNATELADYLATKGVPFRQAHAIVGELVLKGIKTNTALQEMPLSELQAAAPQIQQDVYAELTSKAAVDRRTSLGGTAVSNVLKEVARDEEMIASH
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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A9KQ51
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MKLWGGRFTKETNQLVHNFNASISFDQKFYVQDIRGSIAHVTMLAKQGILNDEEKNKIIDGLNGIRDDIESGSLVIDSTYEDIHSFVEAHLISRIEEIGKKLHTGRSRNDQVALDMKLYTRDEITVLDELLRDLLFELYSLMKEHTETYMPGFTHLQKAQPITLSHHMSAYFEMFRRDRDRLSDIFKRMNTCPLGAGALAGTTYPLDRAYTASLLSFTEPTRNSMDSVSDRDYLIELLSALSTIMMHLSRFSEEIIIWNTNEYRFVEIDDAYSTGSSIMPQKKNPDIAELVRGKTGRVYGALMSLLTTMKGLPLAYNKDMQEDKELTFDAIDTVKGCLSLFTGMIRTMKFNRDTMKASAVLGFTNATDAADYLVNHGVAFRDAHGIIGHLVLTCIEKNCSIEDLSLTELQAISPVFKEDIYDAISLKTCVEKRNTIGGPGVDAMNEVIKECAKYLENNPSIS
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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F9UM00
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MSTQKLWGGRFTETGAKYVDDFGASISFDQLLAAEDIAGSLAHVKMLKKTGILPAADVDQIVAGLETLAERQKQGELEFSTVNEDIHMNIESLLTEEIGPVAGKLHTARSRNDQVATDFHLYLKHQLPLILDRLHELETVLVDKASENVETVMPGYTHLQHAQPISYAHYLLAYYQMFKRDMERFEFNLKHTDISPLGAAALAGTTFPIDREYSAKLLGFSEVYHNSLDAVSDRDFVLEFLSNASILMMHLSRFCEEIVSWSSYEFKYISLSDQFSTGSSIMPQKKNPDMAELIRGKSGRVYGNLMGLLTVMKGIPLAYNKDLQEDKEGAFDTVTTVLTSLHVFTGMLATLTVNEDRMADATTNDFSNATELADYLANKGIPFREAHAIVGKLVLDGLKKQRPLQDIPLKEYQSISPLIQEDVYHDLNAKVAVERRHSLGGTGFDQIRQELQRAQTQLSAYQSETTD
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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C1D665
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MNDNKAWSGRFAEPVAELVKTYTASVDFDRRMAEFDIQGSLAHAQMLTRAGVLSETDLDAIRSGMHTILEDIRAGRFEWSVDLEDVHMNVEKRLTDRIGDAGKRLHTGRSRNDQVATGIRLYLRDAIDRIVGFVRGLQAALLDLAEPNAATVMPGFTHLQVAQPVTFGHHLLAYVEMLGRDAERMQDCRKRVNRLPLGAAALAGTTYPIDRHYTAELLGFDDVCHNSLDAVSDRDFAIEFTAAASLVMTHLSRLSEELILWMSPRVGFIDIADRFCTGSSIMPQKKNPDVPELVRGKAGRVTGHLMALLMLMKAQPLAYNKDNQEDKEPLFDTVDTLIDTLRIYADMMRGITVRPEAMRAAVLQGFATATDLADYLVKKGVPFRDSHEIVARTVKLAEVQGCDIADLPLDELREFSELIEADVYDVLTPEGSLAQRNHVGGTAPEQVREQIARWRQRLAHA
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q1MQL6
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MPKKKLWGGRFHEKTASPVEQYTQSISYDKKMYAQDIAGSKAHASMLGRQGILTSEEVLLLLNGLDSIQKEIETDTFPWKIELEDVHMNIESRLTDLIGTVGEKLHTGRSRNDQVALDFRLFVSDNISLWKRQLLELIGIFVAKAEEYKDTILPGFTHLQPAQPVSLAQHLLAYAWMFKRDVQRVYECNQRVRVSPLGAAALSGTTYNIDPFFIANELHMYGVFDNSMDAVSDRDFVIEALFCASVIMMHLSRFCEELIIWSNPAFGFVQLPDAYATGSSIMPQKKNPDVAEIMRGKVGRVYGALYNMLTILKALPLTYNRDLQEDKEPFFDTNTTIQSSLSIMADMLAAITFNKNKMASALSDGYLNATELADYLVTKGLSFREAHHTTGSIVALAEQQKIPLEELSLQDFQSICDKIESDVFHVLDYHVSIERRKSTGGTGYHSIEKQIEKLKSWLTQ
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q5X7P8
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MTNKTWGGRFKKSLDSSVNQFNASLSFDHVLFDQDINGSQVHVKQLAKQKILTEAECQGIYSALEEIRTEIKQGQYSFNERDEEDIHMFIEQLLIQKIGDLGKKLHTGRSRNDQVALDLRLYTRDKGCLINELLTRLIDCLDDLTSKHQQDLMPGYTHLQQAQPVALGAYFNAYQCMFGRDKSRLDDWFKRMNYSPLGAGALAGSTLPLDREWVAESLGFAGIIPNTLDAVSDRDFVIELCSVAAMIMMHLSRLCEDLILWSTQEFNFVILDDAFATGSSLMPNKKNPDVPELIRGKSGRVYGHLMAILTVMKGLPLAYNKDMQEDKEGLFDTINTIIACLQMITPFLQSLTFNTLLMKTKAQSGYLDATAILESLVMKGMPFRNAHHQVGAWIAEAIEKQCSLNELLKGG
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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A5IHA2
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MTNKTWGGRFKKSLDSGVNQFNASLSFDHVLFDQDINGSQVHVKQLAKQKILTEVESQAIYSALEEIRSEIKQGQYSFNVRDEEDIHMFIEQLLIQKIGDLGKKLHTGRSRNDQVALDLRLYTRDKGCLINELLTRLIDCLDDLTSKHQQDLMPGYTHLQQAQPVTLGAYFNAYQCMFGRDKSRLEDWFKRMNYSPLGAGALAGSTLPLDREWVAESLGFAGIIPNTLDAVSDRDFVIELCSVAAMIMMHLSRLCEDLILWSTQEFNFVILDDAFATGSSLMPNKKNPDVPELIRGKSGRVYGHLMAILTVMKGLPLAYNKDMQEDKEGLFDTINTIIACLQMITPFLQSLTFNTLLMKTKAQSGYLDATAILESLVMKGMPFRDAHHQVGAWIAEAIEKQCSLNELLKGG
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q5ZY77
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MTNKTWGGRFKKSLDSSVNQFNASLSFDHVLFDQDINGSQVHVKQLAKQKILTEAECQEIYSALEEIRTEIKQGQYSFNERDEEDIHMFIEQLLIQKIGDLGKKLHTGRSRNDQVALDLRLYTRDKGCLINELLTRLIDCLDDLTSKHQQDLMPGYTHLQQAQPVTLGAYFNAYQCMFSRDKSRLEDWFKRMNYSPLGAGALAGSTLPLDREWVAESLGFAGIIPNTLDAVSDRDFVIELCSVAAMIMMHLSRLCEDLILWSTQEFNFVTLDDAFATGSSLMPNKKNPDVPELIRGKSGRVYGHLMAILTVMKGLPLAYNKDMQEDKEGLFDTINTIIVCLQMITPFLQSLTFNTPLMRTKAQSGYLDATAILESLVMKGMPFRDAHHQVGAWIAEAIEKQCSLNELLKGG
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q5WZ49
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MTNKTWGGRFKKSLDSGVNQFNASLSFDHVLFDQDINGSQVHVKQLAKQKILTEAECQGIYSALEEIRTEIKQGQYSFNERDEEDIHMFIEQLLIQKIGDLGKKLHTGRSRNDQVALDLRLYTRDKGCLINELLTRLIVCLDDLTSKHQQDLMPGYTHLQQAQPVALGAYFNAYQCMFSRDKSRLEDWFKRMNYSPLGAGALAGSTLPLDREWVAESLGFAGIIPNTLDAVSDRDFVIELCSVAAMIMMHLSRLCEDLILWSTQEFNFVTLDDAFATGSSLMPNKKNPDVPELIRGKSGRVYGHLMAILTVMKGLPLAYNKDMQEDKEGLFDTINTIIVCLQMITPFLQSLTFNTPLMRTKAQSGYLDATAILESLVMKGMPFRDAHHQVGAWIAEAIEKQCSLNELLKGG
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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A8AUN7
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MANHKLWGGRFEASLEGWVEEFGASIGFDYRLAPYDLEGSLAHVKMLGQTGIIAPEEAAAIQAGLEKLLARYESGELEFDVRNEDIHMNMEALLTEKIGPVAGKLHTARSRNDQVATDMHLYLKDQLGQIADKLLNLRQVLLDLAEEHVETIMPGYTHLQHAQPISFAHHLLAYYQMFSRDSQRFAFNLEHTDLSPLGAAALAGTTFPIDRELTADLLGFKGIYHNSLDAVSDRDFILEFLSNSSILIMHLSRLCEELINWCSYEYGFVSLSDTFSTGSSIMPQKKNPDMAELIRGKSGRVYGHLFSLLTVMKSLPLAYNKDLQEDKEGMFDTVDTIQKSLDIMAGILSSMTVNKEKMLVSTQQDFSNATELADYLAKKGLPFREAHEIVGKLVLECSKAGYYLQDIPLSRYQEVSSLIEEDVYQALESQTAVQKRNSLGGTGFEQIRQELERAKKDLNNK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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B1W3B4
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MSSNNGDVRLWGARFADGPAEALAKLSASVHFDWRLAPYDIAGSRAHARVLSKAGLLSEDELTRMLAGLDQLEADVADGSFTGTIADEDVHTALERGLLERLGADLGGKLRAGRSRNDQIATLFRMYLRDHARTIGGLIADLQSALVGLAEAHADVAMPGRTHLQHAQPVLFAHHVLAHVQSLSRDAERLRQWDERTAVSPYGSGALAGSSLGLDPQAVAADLGFERGSVANSIDGTASRDFVAEFAFITAMIGVNLSRIAEEVIIWNTKEFSFVTLHDAFSTGSSIMPQKKNPDIAELARGKSGRLIGNLTGLLATLKALPLAYNRDLQEDKEPVFDSCDQLEVLLPAFTGMMATLTVNRERMEELAPAGFSLATDIAEWLVKQGVPFRVAHEVAGACVKECERAGIELDQLTDEQFAEISEHLTPEVRTVLNVRGALASRDGRGGTAPSAVAVQLAEVKEDLAAQHAWATARP
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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B4SQ92
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MADLLWQKPGVAVDAKIQTFLAGDDVILDREFFLHDIAASAAHAQGLQHIGILSADELAGLLRELDVLAQDFRAGRFVLDTQYEDGHSAIEARLTERLGDAGRKIHTGRSRNDQILVATRLWLKEKLQRVAQLSAEVAKVALDRAQAEKDLPIPGYTHIQRAVVSSAGMWWAGWAEAFIDNAIRARDTHALVDANPLGTAAGYGVNLPLDREHTTAALGFARMQISPIYAQLSRGKFELAALEALGAATLDLRRIAWDLSLFTSAEFGFVALPAQYTTGSSIMPNKRNPDVIELMRATHASVAAARTEIEQLLSLPSGYHRDLQSSKGAIFHGFGRGLAALELLPSLLANLEWRDDKLRAAIDSGMYATDVAVEAAVAGVPFREAYKAAAAGADSAGQGRTPEGSLAARVSPGSAADLRLDELRARWQALS
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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B2FMD6
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MADLLWQKPGVAVDAQIQTFLAGDDVILDREFFLHDIAASAAHAQGLQHIGILSADELAGLLRELEILAQDFREGRFVLDTQYEDGHSAIEARLTERLGDAGRKIHTGRSRNDQILVATRLWLKEKLLSVAQLSADVAKVALDRAQAEKDLPIPGYTHIQRAVVSSAGMWWAGWAEAFIDNAIRARDTHALVDANPLGTAAGYGVNLPLDREHTTAALGFARMQISPIYAQLSRGKFELAALEALGGATLDLRRIAWDLSLFTSAEFGFVALPAQYTTGSSIMPNKRNPDVIELMRATHASVAAARTEIEQLLSLPSGYHRDLQSSKGAIFHGFGRGLAALELLPALLANLEWRDDKLRAAIDSGMYATDVAVEAAVAGVPFREAYKAAAAGADSAGQGRTPEGSLAARVSPGSAADLRLDELRARWQALS
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q8DVX5
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MTTKNHKLWGGRFEAGLAQWVEEFGASISFDQKLAEFDLKGSIAHVTMLGEKGIISQEDAATIKAGLEDLLEEYKAGQLKFDVSNEDIHMNMESLLTAKIGPVAGKLHTARSRNDQVATDMHLYLKAKLDEVIEKLANLRTVLVDLADKHVHTIMPGYTHLQHAQPISFGHHLMAYYNMFTRDSERFIFNVKHTDLSPLGAAALAGTTFPIDREMTAQLMGFAEPYSNSLDAVSDRDFILEFLSNASILMMHMSRMCEEVISWCSHEYQFVTLSDTFSTGSSIMPQKKNPDMAELIRGKSGRVYANLFGLLTVMKALPLAYNKDLQEDKEGMFDTAETITVALDILAGMLSSMIVNDKHMAESTQKDFSNATELADYLASKGMPFRQAHEIVGKLILECSKNGHYLQDVPLERYQTISDLIEEDVYETLKSHTAVERRHSLGGTGFEQVKWQIAEAKKAL
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q04MW6
|
MAKNTKLWGGRFEGTVEDWVERFGASISFDQKLAKFDVIGSLAHVQMLGQTGILSLEESEKIQVGLKELLEELEAGQLDFDIANEDIHMNMEVLLTEKIGPLAGKLHTARSRNDQVATDMHLYLKEQLGYVLDKLAHLKGVLLDLAENHVATIMPGYTHLQHAQPISFAYHLMAYYNMFQRDSERFEFNQKHTDLCPLGAAALAGTTFPIDRQLSSDLLEFKQPYTNSLDAVSDRDFILEFLSNASILMMHMSRFCEEMINWCSFEYQFITLSDTFTIGSSIMPQKKNPDMAELIRGKTGRVYGHLFGLLTVMKSLPLAYNKDLQEDKEGMFDTVETILNSLDVLAGMLSSLQVNKEKMQESTEKDFSNATELADYLAGKGLPFREAHEVVGRLVLDSIKSAKNLQDWTLEELQTYHSLITEDIYVYLQPKTAVQRRNSLGGTGFDQVEYQIAVAKKANEAKK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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C1CAC7
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MAKNTKLWGGRFEGTVEDWVERFGASISFDQKLAKFDVIGSLAHVQMLGQTGILSLEESEKIQVGLKELLEELEAGQLDFDIANEDIHMNMEVLLTEKIGPLAGKLHTARSRNDQVATDMHLYLKEQLGYVLDKLAHLKGVLLDLAENHVATIMPGYTHLQHAQPISFAHHLMAYYNMFQRDSERFEFNQKHTDLCPLGAAALAGTTFPIDRQLSSDLLEFKQPYTNSLDAVSDRDFILEFLSNASILMMHMSRFCEEMINWCSFEYQFITLSDTFTIGSSIMPQKKNPDMAELIRGKTGRVYGHLFGLLTVMKSLPLAYNKDLQEDKEGMFDTVETILNSLDVLAGMLSSLQVNKEKMQESTEKDFSNATELADYLAGKGLPFREAHEVVGRLVLDSIKSAKNLQDWTLEELQTYHSLITEDIYVYLQPKTAVQRRNSLGGTGFDQVEYQIAVAKKANEAKK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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B1I815
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MAKNTKLWGGRFEGTVEDWVERFGASISFDQKLAKFDVIGSLAHVQMLGQTGILSLEESEKIQVGLKELLEELEAGQLDFDIANEDIHMNMEVLLTEKIGPLAGKLHTARSRNDQVATDMHLYLKEQLGYVLDKLAHLKGVLLDLAENHVATIMPGYTHLQHAQPISFAYHLMAYYNMFQRDSERFEFNQKHTDLCPLGAAALAGTTFPIDRQLSSDLLEFKQPYTNSLDAVSDRDFILEFLSNASILMMHMSRFCEEMINWCSFEYQFITLSDTFTIGSSIMPQKKNPDMAELIRGKTGRVYGHLFGLLTVMKSLPLAYNKDLQEDKEGMFDTVETILNSLDVLAGMLSSLQVNKEKMQESTEKDFSNATELADYLAGKGLPFREAHEVVGRLVLDSIKSAKNLQDWTLEELQTYHSLITEDIYVYLQPKTAVQRRNSLGGTGFDQVEYQIAVAKKANEAKK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q8DRI4
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MAKNTKLWGGRFEGTVEDWVERFGASISFDQKLAKFDVIGSLAHVQMLGQTGILSLEESEKIQVGLKELLEELEAGQLDFDIANEDIHMNMEVLLTEKIGPLAGKLHTARSRNDQVATDMHLYLKEQLGYVLDKLAHLKGVLLDLAENHVATIMPGYTHLQHAQPISFAYHLMAYYNMFQRDSERFEFNQKHTDLCPLGAAALAGTTFPIDRQLSSDLLEFKQPYTNSLDAVSDRDFILEFLSNASILMMHMSRFCEEMINWCSFEYQFITLSDTFTIGSSIMPQKKNPDMAELIRGKTGRVYGHLFGLLTVMKSLPLAYNKDLQEDKEGMFDTVETILNSLDVLAGMLSSLQVNKEKMQESTEKDFSNATELADYLAGKGLPFREAHEVVGRLVLDSIKSAKNLQDWTLEELQTYHSLITEDIYVYLQPKTAVQRRNSLGGTGFDQVEYQIAVAKKANEAKK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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A4W487
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MEAKKLWGGRFEASLEEWVEEFGASIRFDQKLAKYDIQGSLAHVKMLGQTRIISQAEAQVIQAGLEELLEEYEAGKLVFDIRNEDIHMNIESLLTEKIGSVAGKLHTARSRNDQVATDMHLYLKDTLFQVVDKLTNLRQILVDLAQEHVETIMPGYTHLQHAQPISFAQHLLAYYNMFSRDSERFAFNMQHTNVSPLGAAALAGTTFPIDRQMTSDLMGFAKPYSNSLDAVSDRDFILEFLSNASILMMHMSRLCEEIINWCSYEYQFVTLSDTFSTGSSIMPQKKNPDMAELIRGKTGRVYGNLVGLLTVMKSLPLTYNKDLQEDKEGMFDTAETVLISIDILAGMLKTMTVHKERMAQSTEKDFSNATELADYLASKGLPFRQAHEIVGKLVLECSKAGHYLQDVSFETYQAISPLIQADIYDALSSKVAVSRRNSLGGTGFESIADQLKSAKEEIQNAKSL
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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A3CQQ3
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MVNHKLWGGRFEASLEDWVEEFGASIGFDYRLAPYDLQGSLAHVKMLGQTGIIAPEEAAAIQAGLEKLLVRYQAGELEFDVRNEDIHMNMEALLTEEIGPVAGKLHTARSRNDQVATDMHLYLKDQIGQIADKLLNLRQVLLNLAEEHVETIMPGYTHLQHAQPISFAHHLLAYYQMFSRDSQRFAFNLEHTNLSPLGAAALAGTTFSIDRELTADLLGFKGIYHNSLDAVSDRDFILEFLSNSSILIMHLSRLCEELINWCSYEYGFVSLSDTFSTGSSIMPQKKNPDMAELIRGKSGRVYGHLFSLLTVMKSLPLAYNKDLQEDKEGMFDTVDTIQKSLDIMAGMLSSMTVNKEKMLVSTQQDFSNATELADYLAKKGLPFREAHEIVGKLVLECSKAGYYLQDIPLSRYQEVSSLIEEDIYQALESQTAVQKRNSLGGTGFAQIRQELERAKRQLEK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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A4VXZ3
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MEAKKLWGGRFEASLEEWVEEFGASIRFDQKLAKYDIQGSLAHVKMLGQTRIISQAEAQVIQAGLEELLEEYEAGKLVFDIRNEDIHMNIESLLTEKIGSVAGKLHTARSRNDQVATDMHLYLKDTLFQVVDKLTNLRQILVDLAQEHVETIMPGYTHLQHAQPISFAQHLLAYYNMFSRDSERFAFNMQHTNVSPLGAAALAGTTFPIDRQMTSDLMGFAKPYSNSLDAVSDRDFILEFLSNASILMMHMSRLCEEIINWCSYEYQFVTLSDTFSTGSSIMPQKKNPDMAELIRGKTGRVYGNLVGLLTVMKSLPLTYNKDLQEDKEGMFDTAETVLISIDILAGMLKTMTVHKERMAQSTEKDFSNATELADYLASKGLPFRQAHEIVGKLVLECSKAGHYLQDVSFETYQAISPLIQADIYDALSSKVAVSRRNSLGGTGFESIADQLKSAKEEIQNAKSL
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q5LXZ9
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MAENHKLWGGRFEASLEKWVEEFGASISFDQKMAEFDLKGSIAHVTMLGETGIIAQEEALQIKQGLEELLEEYKAGKLEFDVSNEDIHMNIESLLTAKIGPVAGKLHTARSRNDQVATDMHLYLKAKLVEVIEKIDNLRNTLVSLADKHTYTIMPGYTHLQHAQPISFGHHLMAYYNMFTRDSERFEFNIKHTDISPLGAAALAGTTFPIDRNMTSDLMGFAKPYSNSLDAVSDRDFILEFLSNSSILMMHMTRICEEIINWCSNEFKFVTLSDTFSTGSSIMPQKKNPDMAELIRGKSGRVYGNLIGLLTVMKSLPLAYNKDLQEDKEGMFDTVETITVAIDILAGMLNTMTVNDKHMAESTEKDFSNATELADYLATKGLPFREAHEIVGKLVLECTKAGYYLQDVPLERYQEVSDLIEEDIYETLKSHTAVERRHSLGGTGFDQVKWQIKEAQQSLNK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q5M2K3
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MAENHKLWGGRFEASLEKWVEEFGASISFDQKMAEFDLKGSIAHVTMLGETGIIAQEEALQIKQGLEELLEEYKAGKLEFDVSNEDIHMNIESLLTAKIGPVAGKLHTARSRNDQVATDMHLYLKAKLVEVIEKIDNLRNTLVSLADKHTYTIMPGYTHLQHAQPISFGHHLMAYYNMFTRDSERFEFNIKHTDISPLGAAALAGTTFPIDRNMTSDLMGFAKPYSNSLDAVSDRDFILEFLSNSSILMMHMTRICEEIINWCSNEFKFVTLSDTFSTGSSIMPQKKNPDMAELIRGKSGRVYGNLIGLLTVMKSLPLAYNKDLQEDKEGMFDTVETITVAIDILAGMLNTMTVNDKHMAESTEKDFSNATELADYLATKGLPFREAHEIVGKLVLECTKAGYYLQDVPLERYQEVSDLIEEDIYETLKSHTAVERRHSLGGTGFDQVKWQIKEAQQSLNK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q03IP9
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MAENHKLWGGRFEASLEKWVEEFGASISFDQKMAEFDLKGSIAHVTMLGETGIIAQEEALQIKQGLEELLEEYKAGKLEFDVSNEDIHMNIESLLTAKIGPVAGKLHTARSRNDQVATDMHLYLKAKLVEVIEKIDNLRNTLVSLADKHTYTIMPGYTHLQHAQPISFGHHLMAYYNMFTRDSERFEFNIKHTDISPLGAAALAGTTFPIDRNMTSDLMGFAKPYSNSLDAVSDRDFILEFLSNSSILMMHMTRICEEIINWCSNEFKFVTLSDTFSTGSSIMPQKKNPDMAELIRGKSGRVYGNLIGLLTVMKSLPLAYNKDLQEDKEGMFDTVETITVAIDILAGMLNTMTVNDKHMAESTEKDFSNATELADYLATKGLPFREAHEIVGKLVLECTKAGYYLQDVPLERYQEVSDLIEEDIYETLKSHTAVERRHSLGGTGFDQVKWQIKEAQQSLNK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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B9DVV8
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MMGNQKLWGGRFEKGLEQWVEEFGASISFDYKLATFDIKASIAHVSMLGQQGIISKDEAELIKTGLEDIHRDILEEEIVFDSQDEDIHMTIERQLLAKIGPLAGKLHTARSRNDQVATDMHLYLKHILEALLEKLLQLRKVLVTLAEEHIETILPGYTHLQHAQPISFGHHLMAYYQMFTRDSERFKFNMKHTDMSPLGAAALAGTTFPIDRELTAQLLGFNELYHNSLDAVSDRDFIIEFLANASLLMMHMSRFCEEIILWTSYEYQFVSLSDSFSTGSSIMPQKKNPDMAELIRGKTGRVYGNLFSLLTVMKALPLAYNKDLQEDKEGLFDTAETILVAVDILAGMLSTMTVHKETMYRATQKDFSNATELADYLANKDMPFRQAHEIVGQLVLQASKEGIYLQDIPIKDFKAISPLIEEDIYDTLTSRAAVERRTSIGGTGFNQVSSQIALARKDLS
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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C1CBS9
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MAKNTKLWGGRFEGTVEDWVERFGASISFDQKLAKFDVIGSLAHVQMLGQTGILSLEESEKIQVGLKELLEELEAGQLDFDIANEDIHMNMEVLLTEKIGPLAGKLHTARSRNDQVATDMHLYLKEQLGYVLDKLAHLKGVLLDLAENHVATIMPGYTHLQHAQPISFAYHLMAYYNMFQRDSERFEFNQKHTDLCPLGAAALAGTTFPIDRQLSSDLLEFKQPYTNSLDAVSDRDFILEFLSNASILMMHMSRFCEEMINWCSFEYQFITLSDTFTTGSSIMPQKKNPDMAELIRGKTGRVYGHLFGLLTVMKSLPLAYNKDLQEDKEGMFDTVETILNSLDVLAGMLSSLQVNKEKMQESTEKDFSNATELADYLAGKGLPFREAHEVVGRLVLDSIKSAKNLQDWTLEELQTYHSLITEDIYVYLQPKTAVQRRNSLGGTGFDQVEYQIAVAKKANEAKK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q4J8F0
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MLYRRWGSDKDFVISYTSSNESDKEIVEEVKLTLKAHVIELYLSNYISKDTAKKIIRAINSFKDYPSSGYEDVHEALEDYIIKNIGEEGGWVGLGRSRNDHVATALRLRTREYIFDIMEELYLLRKSLIEQAKKNLNTIMPSYTHFQPAQPTTLAHYFMYLEEELNTPWEALFNSLKLINRSPLGSGAIVGSNVKIDRKREAELLGFDDVLYNTISSTSSRIDFINAISSLTLLMLVLSRFAEDMILLSSMFVNIIKLPDSHVSTSSLMPQKRNSVTMEILRTKVGECYGDLSSLMMIYKGLPSGYNLDLQEMNKHYWNCIKHVIPSIHITRDIIQNIQIKNFGEIQGLTATDLAEEMAISGIPYRKAYIDVANKIKAGTFVAGISYTKSIENKKVIGSPNPSLLTQEIEIKEKRLNNQHEKFKQYKESVIEKMGQLGVIEDGLLQQ
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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Q30S87
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MDKMWSGRFSATASSLLDQFNASIMFDRKLYREDIEGSIAHATMLAKQGILTTDELSQITKGLSQVKEEIESGVFEWKISDEDLHMGIEKRLTAIIGDAGKKLHTARSRNDQVAVDFRRYVLRKNLEIVDALKLLMNEILVIASKHTQTLLPGMTHLQHAQPINFAFHLSAYLSMFKRDIERFESSYKRNNISPLGCAALAGTPHKIDRDMTAELLGFESASINCLDTVSDRDFALEILFNISTMMMHISRLSEELVMWSSYEFRFVELSDEYSTGSSIMPQKKNPDVPELLRGKTGRVYGSLMGLLTVMKALPLAYNKDTQEDKEGVFDAVETAEISLEILKEALKTMQVKPHYMKNACKIGHLSATDLADYLVQKCDIPFREAHFITGKAVAKSEELKIDLSDIELKYLKEIDDRINEDVLAFLSIENSMNARTSAGGTSTKRTEEQLKYFENFLKAE
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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A6Q7P5
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MSKKIASARISEKSSKLLQDLNNSLPFDKVLYREDIEGSRAHAFMLSEQGIISREDQEKIDAGLQDILADIESGLFKLEGDDEDIHMAIEGELTRRIGDAGKRLHTARSRNDQVALDFRLYVQRNTKTIAELLLKNIETFVKVAEENAETMLPGMTHLQHAQPINFGYHMMAYASMFKRDYERFMSSYERNNYSPIGCAALAGTPHPINRQTTSDKLGFNAPTLNCLDTVSDRDFALEILFNISTVMMHMSRLSEELILWSAAEFKWVTLSDRHATGSSIMPQKKNPDIPELLRGKTGRVNGNLVALLTVMKSLPLAYNKDMQEDKEGVFDSVRTAILSLQVLEEMIADMTVNKEAMERACMVGHLSATDLADYLVKEQGLPFRDAYHITGNVVNLAEEKGLDISELSLEDLQSIDERIAEDVVALLDNRASMNARQSEGGTATVRTLEQIEDLKKWLEKQDEK
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2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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B2VBI9
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MKAVVFAYHDIGCTGIRALAEAGYEIAAIFTHADNAAENHFFASVARTAAELGVPVYAPEDANHPLWVDRIRGMKPDAIFSFHYRHMLNDDIINSASLGAFNLHASLLPKYRGRAPLNWVLVNGEQETGVTLHRMVKRADAGAIIAQNTVAIADRDDALTLHRKVCAAAGELLAEALPAIKIGEFSEHQQDESQASYVGRRTPEDGRIDWHLPAQRVYNLVRAVTDPWPGAFGYVGTGKFIVWQSKIHYDRAAAKPGTVLSVAPFVVACAEGALEIVTGQSESGVYMQGSQLAQTLGLVAGARLYNHPAAVAKRRTRVLILGVNGFIGNHLTERLLVDDNFEVFGLDIGSDAIGRFIGHERFHFVEGDISIHSEWIEYHIKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLKIIRDCVKYKKRIIFPSTSEVYGMCTDASFDEDSSNLVVGPINKQRWIYSVSKQLLDRVIWAYGDKEGLRFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIDGGRQKRCFTDIHDGIEALFLIIENKQKNCDGQIINIGNPENEASIKQLAEQLLESFERHPLRDRFPPFAGFREVESSTYYGKGYQDVEHRKPSIRNAKQLLNWQPTIAMDKTIDDTLDFFLQSVEPGDAEE
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Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
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B7LM76
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MKAVVFAYHDMGCLGVQALLDAGYEISAIFTHADNPAEKVFYGSVSRLAALAGIPVYAPDDINHPLWVERIAQLAPDVIFSFYYRNLLNNEILKLAPHGAFNLHGSLLPKYRGRAPLNWVLENGENETGVTLHRMVAKADAGAIIAQQRVAIDPEDAALTLHKKLCQSASQMLEYALPAIKQGQTQETAQNESEATYFGRRKPEDSFLDWNKPATVLHNMVRAVADPWPGAFSYVGTQKFTIWSSRVHPRVNAAQPGSVISVAPFLIACGDGALEVITGQSVDGITMQGSQLAQTLGLVEGSRLNSQPVCTVQRRTRVLILGVNGFIGNHLTERLLREDHYEVYGLDIGSDAISRFLTHPNFHFVEGDISIHSEWIEYHIKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLRIIRYCVQYHKRIIFPSTSEVYGMCTDKFFDEDHSNLIVGPINKPRWIYSVSKQLLDRVIWAYGEKEGLQFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIDGGKQKRCFTDIRDGIEALYRIIENTGNRCDGEIINIGNPDNEASIEELGKMLLASFDKHPLRQHFPPFAGFRVVESSSYYGKGYQDVEHRKPSIRNARRCLDWEPTIDMQETIDETLDFFLRTVDIVEKSS
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Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
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B5XTK9
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MKAVVFAYHDMGCTGIQSLLDAGYDIAAIFTHPDNPGENHFFGSVARLAAEQGIPVWAPEDVNHPLWIERIREMKPDVLFSFYYRNLLGDEILNLAPKGAFNLHGSLLPKYRGRAPLNWVLVNGESETGVTLHRMVNRADAGDIVAQQTVAIGPDDAALTLHRKLCAAATELLGQALPAILEGKTAERPQDHSQATYVGRRTPEDGRLDWEQPAQTLHNLVRAVSDPWPGAFGYAGANKFIVWKSRVRHDLPAAKPGTVISVAPLIVACQDGALEIVTGQTERGVYMQGAQLAQALGLVSGAVISSKPVVAIKRRTRVLILGVNGFIGNHLTERLLQDDNYEIYGLDIGSDAISRFLESPRFHFVEGDISIHSEWIEYHIKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLKIIRDCVKYNKRIIFPSTSEVYGMCTDKNFDEDTSNLVVGPINKQRWIYSVSKQLLDRVIWAYGDKYDLKFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIEGGKQKRCFTDISDGIEALFRIIENKDGRCDGQIINIGNPENEASIKELAEMLLACFERHPLRDRFPPFAGFREVESSDYYGKGYQDVEHRKPSIRNAKRCLNWEPKVEMEETVEHTLDFFLRTVELVDDKNP
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Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
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A6TF98
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MKAVVFAYHDMGCTGIQALLDAGYDIAAIFTHPDNPGENHFFGSVARLAAEQGIPVWAPEDVNHPLWIERIREMKPDVLFSFYYRNLLGDEILNLAPKGAFNLHGSLLPKYRGRAPLNWVLVNGESETGVTLHRMVNRADAGDIVAQQAVAIGADDAALTLHRKLCAAATELLSRALPAILAGTTDERPQDHSQATYVGRRTPEDGRLDWELPAQTLHNLVRAVSDPWPGAFGYAGANKFIVWKSRVRHDLPAAKPGTVLSIAPLIVACQDGALEIVTGQTERGVYMQGAQLAQALGLVSGAVISSKPVVAIKRRTRVLILGVNGFIGNHLTERLLQDDNYEIYGLDIGSDAISRFLDCPRFHFVEGDISIHSEWIEYHIKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLKIIRDCVKYNKRIIFPSTSEVYGMCTDKNFDEDSSNLVVGPINKQRWIYSVSKQLLDRVIWAYGDKNGLKFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIEGGKQKRCFTDISDGIEALFRIIENKDGRCDGQIINIGNPDNEASIKELAEMLLACFERHPLRDRFPPFAGFREVESSDYYGKGYQDVEHRKPSIRNAKRCLNWEPKVEMEETVEHTLDFFLRTVELVDDKNP
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Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
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Q6D2F1
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MKAIVFAYHDIGCVGLEALALAGYEIQAVFTHSDAPGENHFYASVAKTAAGMDVPVFAPEDINHPLWVNRIRELAPDVIFSFYYRTILSDDILQLPSFGAFNLHGSLLPRYRGRAPVNWVLVNGETQTGVTLHKMVSRADAGDIVAQSVVAIDDEDTALTLHGKCRTAAATLLAQQLPLIRSREIALTPQDDSQASYFGRRTAADGLIDWQKSAHEINNLIRAVTEPYPGAFTFLGERKVIIWRARVVKNNRVNVNHPHGGDAGSIISTSPLVVSCGEDALEIVSGQSEAGLYMSGSRLAAEMGMVPQARLGNLASRVQRRRTRVLILGVNGFIGNHLTERLLRDDRYEIYGLDISSDAIARFLGDPRFHFVEGDISIHNEWIEYHIKKCDVILPLVAIATPIEYTRNPLRVFELDFEENLKIVRDCVRYNKRIVFPSTSEVYGMCDDKEFDEDTSRLIVGPINKQRWIYSVSKQLLDRVIWAYGAKNGLRFTLFRPFNWMGPRLDTLDAARIGSSRAITQLILNLVEGSPIKLVDGGAQKRCFTDIHDGIEALFRVIENRNGQCDGQIINIGNPHNEASIRELGEMLLTSFNAHPLRDRFPPFAGFIDVESSSYYGKGYQDVAHRTPSIRNAKRLLEWEPTVKMEQTVAETLDYFLRTVDVPHTADATDTQG
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Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
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C6DAW5
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MKAIVFAYHDIGCVGLEALKLAGYEIQAVFTHSDAPGENHFYASVAKAAAEMDVPVFAPEDVNHPLWVNRIRELAPDVIFSFYYRTLLSDDILQLPSFGAFNLHGSLLPRYRGRAPVNWVLVNGETQTGVTLHKMVSRADAGDIVAQSVVEIDDEDTALTLHGKCRTTAAALLAQQLPLIRSREIMLTPQDESQASYFGRRTAADGLIDWQKSAREINNLIRAVTEPYPGAFTFLGERKVVIWRARVLKNDSVKANGVKQEPGSIISTSPLVVSCGEDALEIVSGQSESGLYMSGSRLAAEMGMVPQAKLGNLASRVQRRRTRVLILGVNGFIGNHLTERLLRDDRYEIYGLDISSDAIARFLGDPRFHFVEGDISIHNEWIEYHIKKCDVILPLVAIATPIEYTRNPLRVFELDFEENLKIVRDCVRYNKRIVFPSTSEVYGMCDDKEFDEDTSRLIVGPINKQRWIYSVSKQLLDRVIWAYGAKNGLRFTLFRPFNWMGPRLDTLDAARIGSSRAITQLILNLVEGSPIKLVDGGAQKRCFTDIHDGIEALFRIIENRNGQCDGQIINIGNPHNEASIRELGDMLLTSFNAHPLRDRFPPFAGFIEVESSSYYGKGYQDVAHRTPSIRNAKRLLEWEPTVKMEQTVAETLDYFLRTVDPQHADNVTDTQG
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Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
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Q7N3Q7
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MKAIVFAYHDIGCVGINALTKAGFDIQAVFTHTDDPNENHFFSSVARLSADLALPVFAPENVNHPLWIERIRELKPDVIFSFYYRDMLSEDILSLASTGAFNLHGSLLPKYRGRAPINWAILNGEVETGVTLHKMVLKPDAGDIIAQYKVAIAETDTALTLHGKIREAAEKLFDQVLPQIKAGIYPAIPQDESQATYFGRRTAVDGEIDWHKSATEINNLVRAVTEPYPGAFTFLGERKITIWRACPLNETHDKQPGTVLSVDPLIIACGKGTLEIINGQSESGLYVQGHRLAVDMSMVTDVRVGPKATTQINHRKRVLILGVNGFIGNHLTERLLRDGNYDIYGMDIGSSAIERFISNPRFHFIEGDINIHTEWIEYHIKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLKIVRYCVKYNKRIIFPSTSEVYGMCDDKEFDEDDSRLIVGPINKQRWIYSVSKQLLDRVIWAYGEKEGLKFTLFRPFNWMGPRLDNLNSARIGSSRAITQLILNLVEGSPIKLVDGGEQKRCFTDINDGIEALFRIIENREGLCDGQIINIGNPTNEASIRQLAEILLDSFEDHELRDHFPPFAGFKKVESGSYYGKGYQDVEHRKPSIKNAERLLDWKPTIDMKQTINETLDFFLRGAVEELGKN
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Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
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B4ETL7
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MKAIVFAYHDIGCVGLKALEKAGFDIQAVFTHTDDPNENHFFSSVARVSAEMGLTVFAPENVNHPLWIERIREMKPDVIFSFYYRHMLSDEILNLAPKGAFNLHGSLLPKYRGRAPINWAIVNGETETGVTLHKMTAKADAGDIVAQEKVTIEDTDTSLILHEKVREAAAKLMAHTLPHIASGNYSTTAQDESQATYYGRRCADDGLIDWNADAKTVHNLVRAVTEPYPGAFTFLGERKMIIWRARPVADNQGKRPGTVISTEPLVIACAKGAIEVITGQSENGLYVQGSRLATEMGIVTDVRVGPKATAQVKRRQRVLILGVNGFIGNHLTERLLKDGNYDIYGMDIGSSAIERFIGNPRFHFIEGDVSIHTEWIEYHIKKCDVILPLVAIATPIEYTRNPLRVFELDFEENLKIVRYCVKYNKRIIFPSTSEVYGMCDDKEFDEDNSRLIVGPINKQRWIYSVSKQLLDRVIWAYGAKEGLKFTLFRPFNWMGPRLDNLNSARIGSSRAITQLILNLVEGSPIKLVDGGEQKRCFTDINDGIEALFRIIENRDNKCDGQIINIGNPTNEASIRELAEMLLDCFEKHELRGHFPPFAGFKKIESSSYYGKGYQDVEHRKPSIKNAERLLDWKPTIETRQTVEETLDFFLRGAVEELGNK
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Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
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Q48HZ1
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MSPKAVVFAYHDIGCVGLQALLGAGYEIAAVFTHADDPKEKTFFGSVAQLCARHGIPVHAPEDPNHPLWVERIDKLAPDFIFSFYYRQLLGDPLLACAKKGALNLHGSLLPRYRGRAPANWVLVNGESETGVTLHQMVKRADAGPIVAQQRVSISSTDTALTLHGKLREAAADLLSETLPLLALGQLSGTPQDETRASCFGRRTPADGLIDWSLPATQLYNLIRAVTQPYPGAFCAVGENKLIVWAASAEAGNNGEAPGTVISHDPLRIACGEGSLVINAGQRGDNGLYLSGAQLAREFGLVEGSQLLDTEKRRPARRTRVLILGVNGFIGNHLSERLLQDDRYDIYGMDIGSDAIERLRTKPNFHFIEGDISIHTEWIEYHIKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLKIVRYCVKYNKRVIFPSTSEVYGMCQDASFNEDTSNLIVGPINKQRWIYSVSKQLLDRVIWAYGQKGLQFTLFRPFNWMGPRLDRLDSARIGSSRAITQLILHLVEGTPIRLVDGGAQKRCFTDVADGIEALARIIENRDGCCNGQIINIGNPDNEASIRQLGEELLRQFEAHPLRGNFPPFAGFREVESQSFYGKGYQDVSHRKPSIDNARQLIGWTPGIELSETIGKTLDFFLREAMAEKADMR
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Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
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A6V1P0
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MTSKAVVFAYHDIGCTGIEALLNAGYEIAAVFTHADDPRENTFYASVARLCAERGIALHAPEDVNHPLWLERIRQLRPDFLFSFYYRRLLGAELLACAARGAYNLHGSLLPRYRGRAPANWVLVNGETQTGVTLHRMVERADAGPILAQQAVAIDPEDTALSLHGKLRKAAGALLRDSLPLLALGVLPEVEQDESQASHFGRRTAADGLLDWHRPARQLYDLVRAVTQPYPGAFCQVGEQKLIVWSAEVVAGNHGREPGSVLSCDPLRIACGEDSLVLRFGQRGERGLYLAGTQLATELGLVEGARLRGPASGPQRRTRVLILGVNGFIGNHLSERLLRDGRYEVHGMDIGSDAIERLKADPHFHFVEGDIGIHSEWLEYHVKKCDVILPLVAIATPIEYTRNPLRVFELDFEENLRIVRYCVKYGKRVVFPSTSEVYGMCQDPDFDEDRSNLVVGPINKQRWIYSVSKQLLDRVIWAYGQQGLRFTLFRPFNWMGPRLDRLESARIGSSRAITQLILHLVEGTPIRLVDGGAQKRCFTDVDDGIEALARIIDNRDGRCDGQIVNIGNPDNEASIRQLGEELLRQFEAHPLRAQFPPFAGFREVESRSFYGDGYQDVAHRKPSIENARRLLDWQPAIELRETIGKTLDFFLHEALREREAQA
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Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
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B7VBN2
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MTSKAVVFAYHDIGCTGIEALLNAGYEIAAVFTHADDPRENTFYASVARLCAERGIPLHAPEDVNHPLWLERIRQLRPDFLFSFYYRRLLGAELLACAARGAYNLHGSLLPRYRGRAPANWVLVNGETQTGVTLHRMIERADAGPILAQQAVAIDPEDTALSLHGKLRKAAGALLRDSLPLLALGVLPEVEQDESQASHFGRRTPADGLLDWHRPARQLYDLVRAVTQPYPGAFCQVGEQKLIVWSAEVVAGNHGREPGSVLSCDPLRIACGEDSLVLRFGQRGERGLYLAGTQLATELGLVEGARLRGAASGPQRRTRVLILGVNGFIGNHLSERLLRDGRYEVHGMDIGSDAIERLKADPHFHFVEGDIGIHSEWLEYHVKKCDVILPLVAIATPIEYTRNPLRVFELDFEENLRIVRYCVKYGKRVVFPSTSEVYGMCQDPDFDEDRSNLVVGPINKQRWIYSVSKQLLDRVIWAYGQQGLRFTLFRPFNWMGPRLDRLDSARIGSSRAITQLILHLVEGTPIRLVDGGAQKRCFTDVDDGIEALARIIDNRDGRCDGQIVNIGNPDNEASIRQLGEELLRQFEAHPLRAQFPPFAGFREVESRSFYGDGYQDVAHRKPSIDNARRLLDWQPTIELRETIGKTLDFFLHEALREREAQA
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Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
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Q02R25
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MTSKAVVFAYHDIGCTGIEALLNAGYEIAAVFTHADDPRENTFYASVARLCAERGIPLHAPEDVNHPLWLERIRQLRPDFLFSFYYRRLLGAELLACAARGAYNLHGSLLPRYRGRAPANWVLVNGETQTGVTLHRMIERADAGPILAQQAVAIDPEDTALSLHGKLRKAAGALLRDSLPLLALGVLPEVEQDESQASHFGRRTPADGLLDWHRPARQLYDLVRAVTQPYPGAFCQVGEQKLIVWSAEVVAGNHGREPGSVLSCDPLRIACGEDSLVLRFGQRGERGLYLAGTQLATELGLVEGARLRGAASGPQRRTRVLILGVNGFIGNHLSERLLRDGRYEVHGMDIGSDAIERLKADPHFHFVEGDIGIHSEWLEYHVKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLRIVRYCVKYGKRVVFPSTSEVYGMCQDPDFDEDRSNLVVGPINKQRWIYSVSKQLLDRVIWAYGQQGLRFTLFRPFNWMGPRLDRLDSARIGSSRAITQLILHLVEGTPIRLVDGGAQKRCFTDVDDGIEALARIIDNRDGRCDGQIVNIGNPDNEASIRQLGEELLRQFEAHPLRAQFPPFAGFREVESRSFYGDGYQDVAHRKPSIDNARRLLDWQPTIELRETIGKTLDFFLHEALREREAQA
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Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
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