UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
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B0Y473
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MKGYLSLSILPLLVAASPVVVDSIHNGAAPILSSMNAKEVPDSYIVVFKKHVNAESAAAHHSWVQDIHSAQNERVELRKRSLFGFGEEAYLGLKNTFDIAGSLVGYSGHFHEDVIEQVRKHPDVEYIEKDSEVHTMEDPTVEKSAPWGLARISHRDSLSFGTFNKYLYASEGGEGVDAYTIDTGINVDHVDFEGRAQWGKTIPTDDEDADGNGHGTHCSGTIAGRKYGVAKKANLYAVKVLRSSGSGTMSDVVAGVEWAVKSHLKKVKDAKDGKIKGFKGSVANMSLGGGKSRTLEAAVNAGVEAGLHFAVAAGNDNADACNYSPAAAENPITVGASTLQDERAYFSNYGKCTDIFAPGLNILSTWIGSKHAVNTISGTSMASPHIAGLLAYFVSLQPSKDSAFAVDELTPKKLKKDIIAIATQGALTDIPSDTPNLLAWNGGGSSNYTDIIASGGYKVNASVKDRFEGLVHKAEKLLTEELGAIYSEIHDAAVA
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Alkaline protease that allows assimilation of proteinaceous substrates. Acts as a significant virulence factor in invasive aspergillosis. Required for regular sporulation (By similarity). Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides. Acts as a major allergen in patients suffering from extrinsic bronchial asthma. Binds to IgE. Belongs to the peptidase S8 family.
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Q4WUP6
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MKGYLSLSILPLLVAASPVVVDSIHNGAAPILSSMNAKEVPDSYIVVFKKHVNAESAAAHHSWVQDIHSAQNERVELRKRSLFGFGEEAYLGLKNTFDIAGSLVGYSGHFHEDVIEQVRKHPDVEYIEKDSEVHTMEDPTVEKSAPWGLARISHRDSLSFGTFNKYLYASEGGEGVDAYTIDTGINVDHVDFEGRAQWGKTIPTDDEDADGNGHGTHCSGTIAGRKYGVAKKANLYAVKVLRSSGSGTMSDVVAGVEWAVKSHLKKVKDAKDGKIKGFKGSVANMSLGGGKSRTLEAAVNAGVEAGLHFAVAAGNDNADACNYSPAAAENPITVGASTLQDERAYFSNYGKCTDIFAPGLNILSTWIGSKHAVNTISGTSMASPHIAGLLAYFVSLQPSKDSAFAVDELTPKKLKKDIIAIATQGALTDIPSDTPNLLAWNGGGSSNYTDIIASGGYKVNASVKDRFEGLVHKAEKLLTEELGAIYSEIHDAAVA
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Alkaline protease that allows assimilation of proteinaceous substrates. Acts as a significant virulence factor in invasive aspergillosis. Required for regular sporulation. Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides. Acts as a major allergen in patients suffering from extrinsic bronchial asthma. Binds to IgE. Belongs to the peptidase S8 family.
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Q9Y705
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MVRSISSVLAKEESENGSPIPALEEGSVYHVSLKSEGVSPFSDRIQLNYLYDGKTFSDPSNLNIHQQEACLINELLNAFMGMEGVFVHLQDMKASSEFETIIMPPSFYILPGFDLGIKDIASEMLEMGSHYLSITAFIESRSHFEYGFVNHALCAALRKFVMDYVVLIMQCENQSRIDPNFSLQTLRLYTLPTSRSLRQVYLILRDLLLSMEKNASSSDDLGLSNIDDLLEQLNEGNDISHVVNATRSKKKVCKGGQVISFLTESLTKYAGDPVARKILTYLLREASRPYTKMLNEWIHLGLVNDPYDEFMIKIHKGITSMQLDEDYTDEYWEKRYVIREDQVPPQLLDLQNKVLFAGKYLNVVLECRKGVNNLASLNAKDDTQNQLLWPSTFDDDNFTLNIMNAYVYANESLLQLLQSSQSLYAHLYSLKHYFFLDQSDFFTTFLDNAQHELRKPAKYISITKLQSQLDLALRQPGTITATDPHKEYVTVEVNQTSLIDWLMHIVSISGLEEGTSSQGNEVWNESITKQADVGNETRNFESEHNRSTQGTSKVGSDKDINGFETMQLCYKVPFPLSLILSRKAIIRYQLLFRYFLLLRHVEMQLENSWVQHSKNSAWRLNSSNAKIEQWKRNSWLLRTRMLSFVQKIIYYTTSEVIETHWGKFMGELENARTVDNLMQEHIDFLDTCLKECMLTNSRLLKVQSKLLNTCAMFASYTSTFTRSLYLLENSEESFDEGRMDKMEEILRRYEDSFSRHLKSLVNACNYFASTETAALLSLVMKLTG
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Component of the gamma tubule complex that is required for the regulation of both interphase microtubules and mitotic bipolar spindles. Required for correct septation. Part of the gamma-tubulin complex. Interacts with mcp6. Localizes to the SPB and also to the equatorial MTOC. Belongs to the TUBGCP family.
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Q9P954
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MSEIHVKTALSRLADKYLQNSKNPSVPYTIETIVSFFQEIIHSISPDTFQLDIDDILYKIYSKIPPEENNDALFSKLSNLVSRLKSQTVIHNKSQILYFLYLLSPISQSSRDVSSHLLDESISNPINIPSTEVESSNFGQTRYDQVPENPQITDWDEGLENESSISIAHDSSRLNRSTETSSVQHTLITEADLLSSISYVLQGISTEYVQFKNELALLSKRIPVQYLLQMRALSETGLLYQELKVFSNYDPSVSQSIDGDNVSKAFINDQSLALQSLKSVISKELTNFLALIASLDSQIRADASLEKPMVTIRRCIAWTQVAKLKLRILSSVVNDNMNQENKKRLIQVVSKYNVHGDPLIQELSDKILTEITGPLYEMIENWIYKGELVDPYQEFFVKEKNGSESHDHQGQGDVVWKGKYFLDKELIPSFLSEELVDKIFLIGKSLNFARYGCGDFDWAQEHYQKLVKKLSYRDPHSLETVVDKAYTESINHLVYLMEEVFHLTDHLKAIKKYLLLGQGDFVDLLMESLGNSLDQPANTLFRHNLTASLESAIRSSNASYEPEYVLKRLDARLLELSHGETGWDVFTLEYKVDSPINVIITPYCSRQYLKIFNFLWRLKRIEFALAHSWRRVNLGERNVFRNLDYTKFEWHFVSCHLAEMIHFVCQLQYYILFEVIEISWQELQLAMEKPNATLDTYIEAHEKYVTSITHKGLLGGGKSRNEDSFLHQLHDILKVILNFHDAIELLYNFSCSLSNRIRINVPISTDALAAQYTPIKNELSNFTEEFQVRLQKLLHGLASHKDPEMRFLSVRLNYNEFYVSHRRRHDKDVTSQ
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Component of the gamma tubule complex that is required for the regulation of both interphase microtubules and mitotic bipolar spindles. Part of the gamma-tubulin complex. Interacts directly with mzt1. Localizes to the SPB and also to the equatorial MTOC. Belongs to the TUBGCP family.
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Q9UU56
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MSDIVSSSTDYSRRSPSSSSIGTNETDHTGFHEKRQGASSESLIPPAQRSSEESMPAPKLFPKLTSKPNPQLNLKDTLNKRVSDRLQALELNKSFDFSGTPRPMHPISHPLSQHKTPEFKHRKRNVESILTPKNPSLFSSSNAASQRGSLNTAPSNFAYSHSSSLQTSASSRPPVLSNGSFPRQTNTAPLNPPVHLKDNIRNSATPSTSQADIPTQYPINSTQKQQAKYEAEIEGYKAKLAGTYHEISVLQNTIVNVSGQLIAVNDQLQQLRSGKASTSPSTKDTNMRLVEGHNEETLALQRGKYTQEEVDKLIQERMEKVAEDLHAQYSAKHTQKINAFKANYARKYEATIQELQNQIGTAPNAPKISNSNWEEERRALKADNQTLQKQLEKAIQERQDMSDFLNNFKADMAKSDKLLMQQQSQQTGDLETLRLQLQALQEELRVEREERQQLIQMSEDLVIAMDQLNLEQKS
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Required for bipolar spindle formation and proper chromosome segregation. Has an indirect role in connecting the kinetochores and the plus end of pole to chromosome microtubules by targeting alp14 to the spindle pole body. Involved in the emergence of large microtubule organizing centers (MTOC) in interphase cells. Attaches to the minus ends of microtubules and associates with the sites of microtubule attachment on the nuclear envelope. This leads to the stabilzation of the microtubule bundles. Interacts with alp14. Associated with the equatorial MTOC, spindle midzones, spindle pole body and mitotic kinetochore periphery. Spindle and kinetochore localization is alp14-dependent.
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Q2MAE7
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MNNRSAVRILRLPAVIQKTGMARATIYDWLNPKSPRYDATFPKKRMLGVKSVGWIEAEIDEWLSQRCKLI
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Positive regulator of the expression of the slpA gene (PubMed:7511582). When overexpressed, leads to suppression of the capsule overproduction and UV sensitivity phenotypes of cells mutant for the Lon ATP-dependent protease (PubMed:7511582). Part of the cryptic P4-like prophage CP4-57 (PubMed:7511583). Overexpression of AlpA leads to excision of the CP4-57 prophage by IntA. This inactivates ssrA (the gene upstream of the prophage) that encodes tmRNA which is required to rescue stalled ribosomes in a process known as trans-translation (PubMed:7511583).
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P17595
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MASDEIVRNLISREEVMGNLISTASSSVRSPLHDVLCSHVRTIVDSVDKKAVSRKHEDVRRNISSEELQMLINAYPEYAVSSSACESGTHSMAACFRFLETEYLLDMVPMKETFVYDIGGNWFSHMKFRADREIHCCCPILSMRDSERLETRMMAMQKYMRGSKDKPLRLLSRYQNILREQAARTTAFMAGEVNAGVLDGDVFCENTFQDCVRRVPEGFLKTAIAVHSIYDIKVEEFASALKRKGITQAYGCFLFPPAVLIGQKEGILPSVDGHYLVENGRIKFFFANDPNAGYSHDLKDYLKYVEKTYVDIEDGVFAIELMQMRGDTMFFKITDVTAAMYHMKYRGMKRDETFKCIPLLKNSSVVVPLFSWDNRSLKITSGLLPRTLVEQGAAFIMKNKEKDLNVAVLKNYLSAVNNSYIFNGSQVRDGVKIAPDLISKLAVTLYLREKVYRQRENSIISYFEQEMLHDPNLKAMFGDFLWFVPNTLSSVWKNMRKSLMEWFGYAEFDLTTFDICDPVLYVEIVDRYKIIQKGRIPLGEFFDCHEECENYELREKEKNDLAVKMAQKVTGTVTECEKDLGPLVQPIKEILVQLVMPNLVRALCRPRSPTSPLDLKSIPGSTPSHSSSDSEHSMTEEASCTIAGSVPTWEIATRKDLTFQRIDEDMSRRTGMPPRPKVTSSYNMNARAEFLYYQLCSVICERAQILSVIEDFRQNLIFSDKVAVPLNARFYSFQSLRPGWVFKTPSHSEVGHSYAVHFDFKTIGTDLEESLAFCRMVPISWDKSGKYIATTPHFPERHGYYVICDNTKLCNNWLIYNKLVDVYALVADRPLRFELIDGVPGCGKSTMILNSCDIRREVVVGEGRNATDDLRERFKRKKNLNSKTANHRVRTLDSLLLAEGPCVPQADRFHFDEALKVHYGAIMFCADKLGASEILAQGDRAQLPMICRVEGIELQFQSPDYTKTIINPKLRSYRIPGDVAFYLSAKEFYKVKGIPQKVITSNSVKRSLYARGETTPERFVSLLDVPVRKDTHYLTFLQAEKESLMSHLIPKGVKKESISTIHEAQGGTYENVILVRLQRTPNEIYPGGPRSAPYIVVGTSRHTKTFTYCSVTDDKLLLDIADVGGIAHTPIRTFESHIV
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Probably contains methyltransferase and helicase activities (PubMed:2209552). Methyltransferase displays a cytoplasmic capping enzyme activity (Probable). This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus (Probable). Helicase region probably exhibits NTPase and RNA unwinding activities (Probable). ATP + H2O = ADP + H(+) + phosphate Interacts with the suppressor of RNA silencing Gamma-B (via C-terminus). The viral replication sites are located at the host chloroplast membrane. The genome of this virus consists of three linear, positive, single-stranded RNAs encapsidated in separate virions designated RNA-alpha, RNA-beta and RNA-gamma. Three proteins (alpha-A, beta-A and gamma-A) are translated directly from these genomic RNAs and the remaining proteins encoded on RNA-beta (beta-B, beta-C and beta-D) and RNA-gamma (gamma-B) are expressed via three subgenomic messenger RNAs.
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P86348
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DINGGGATLPQALYQTSGVL
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Has hemorrhagic activity. a phosphate monoester + H2O = an alcohol + phosphate Expressed by the venom gland.
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Q9KJX5
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MLTPKKWLLGVLVVSGMLGAQKTNAVPRPKLVVGLVVDQMRWDYLYRYYSKYGEGGFKRMLNTGYSLNNVHIDYVPTVTAIGHTSIFTGSVPSIHGIAGNDWYDKELGKSVYCTSDETVQPVGTTSNSVGQHSPRNLWSTTVTDQLGLATNFTSKVVGVSLKDRASILPAGHNPTGAFWFDDTTGKFITSTYYTKELPKWVNDFNNKNVPAQLVANGWNTLLPINQYTESSEDNVEWEGLLGSKKTPTFPYTDLAKDYEAKKGLIRTTPFGNTLTLQMADAAIDGNQMGVDDITDFLTVNLASTDYVGHNFGPNSIEVEDTYLRLDRDLADFFNNLDKKVGKGNYLVFLSADHGAAHSVGFMQAHKMPTGFFVEDMKKEMNAKLKQKFGADNIIAAAMNYQVYFDRKVLADSKLELDDVRDYVMTELKKEPSVLYVLSTDEIWESSIPEPIKSRVINGYNWKRSGDIQIISKDGYLSAYSKKGTTHSVWNSYDSHIPLLFMGWGIKQGESNQPYHMTDIAPTVSSLLKIQFPSGAVGKPITEVIGR
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Alkaline phosphatase with broad substrate specificity. Has phosphatase activity towards nucleotide phosphates with a preference for ATP. Active towards a great variety of phosphomonoesters with the exception of 2',3'-cyclic AMP and myo-inositol hexakisphosphate. a phosphate monoester + H2O = an alcohol + phosphate Binds 2 Zn(2+) ions. Strongly inhibited by orthovanadate and EDTA. Also inhibited by inorganic phosphate. Optimum pH is 8.5 with 4-nitrophenyl phosphate as substrate. Has 50% residual activity at pH 7.5 and 30% at pH 9.0, being virtually inactive at pH 10 and at pH 5 or lower. Heat-labile. Incubation for 10 minutes at 50 or 60 degrees Celsius causes 40% and 60% inactivation, respectively. Heating at 100 degrees Celsius for 2 minutes causes total loss of activity. Heat-inactivated enzyme cannot be renaturated. Expression is not repressed by inorganic phosphate.
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A1YYW7
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MLKHVAAALLLATAMPVVAQSPAPAAAPAPAARSIAATPPKLIVAISVDQFSADLFSEYRQYYTGGLKRLTSEGAVFPRGYQSHAATETCPGHSTILTGSRPSRTGIIANNWFDLDAKREDKNLYCAEDESQPGSSSDKYEASPLHLKVPTLGGRMKAANPATRVVSVAGKDRAAIMMGGATADQVWWLGGPQGYVSYKGVAPTPLVTQVNQAFAQRLAQPNPGFELPAQCVSKDFPVQAGNRTVGTGRFARDAGDYKGFRISPEQDAMTLAFAAAAIENMQLGKQAQTDIISIGLSATDYVGHTFGTEGTESCIQVDRLDTELGAFFDKLDKDGIDYVVVLTADHGGHDLPERHRMNAMPMEQRVDMALTPKALNATIAEKAGLPGKKVIWSDGPSGDIYYDKGLTAAQRARVETEALKYLRAHPQVQTVFTKAEIAATPSPSGPPESWSLIQEARASFYPSRSGDLLLLLKPRVMSIPEQAVMGSVATHGSPWDTDRRVPILFWRKGMQHFEQPLGVETVDILPSLAALIKLPVPKDQIDGRCLDLVAGKDDSCAGQ
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Alkaline phosphatase with broad substrate specificity. Precipitates uranium from alkaline solutions. a phosphate monoester + H2O = an alcohol + phosphate Binds 2 Zn(2+) ions. Optimum pH is 9.0. Monomer. Constitutively expressed.
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Q55320
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MKIKLLCISLAVLFCSSANAQKKQAKVQPSVFPQTVARPKLVVGMVIDQMRWDYLYRFYARYGNGGFKRLINEGFSAENTLIPYTPTLTACGHSSIYTGSVPAINGIIGNNWFDPQLGRDVYCVEDKSVKTVGSSSNEGLMSPKNLLVTTVTDELRMATNFRSKVISVSIKDRGAILPGGHTANGAYWYDDMTGSFISSTHYMQQLPTWVNDFNAQRLPNKYFEQDWNTLYPIETYTESTADAKPYERTFKGAKTSSFPHLFKQYANKNYSMMASMPQGNSFTLEFAKAAIPAEKLGQTGNTDFLAVSLSSTDYVGHQFGPNSIELEDTYLRLDKDLEDFFNYLDKTIGKGNYLLFLTADHGATHVPGFLRNKMPGGRLLLKVQTDLDSLIFNEFKVRCNFTIINNQVIFDTDAIKEAKADYAKIKQSTIDYLVKQDGVLNAVDIKNMGAVTIPQEIKNKIINGYNARRSGDVYIILDAGWYPTLTPGTGHAAWNPYDSHIPALFMGWGVKPGKTNKEYYMSDIAPTVSALLHIQQPSGSIGKVITDLLK
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Alkaline phosphatase with broad substrate specificity. a phosphate monoester + H2O = an alcohol + phosphate Binds 2 Zn(2+) ions. Subject to competitive inhibition by phosphate. Inhibited by manganese. Magnesium mildly increases enzyme activity when the zinc concentration is suboptimal. Optimal activity is dependent on the presence of 0.01-2% Triton X-100. Triton X-100 at a concentration of 0.05% increases the activity about fivefold relative to that in its absence. The enzyme is even active in Triton X-100 concentrations up to 80%. 50% inhibition by 4 mM EDTA and 50% inhibition by 48 mM sodium citrate. Optimum pH is 7-10. Activity on 4-nitrophenyl phosphate is observed between pH 6 and pH 11. Heat-labile. Activity increases with temperature between 15 and 35 degrees Celsius and decreases with further heating. No activity at 65 degrees Celsius. Preincubation for 10 minutes at 50 or 60 degrees Celsius causes 50% or 100% inactivation, respectively. Heat-inactivated enzyme cannot be renaturated. Associated with the periplasmic side of the inner membrane.
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Q60113
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MNSLLHHSFLKTVFSSLAIAIVTSSLSSVTIAATHPLDNHPKGEIAASSETAHNPWSGTRLIVAISVDQFSSDLFSEYRGRFRSGMKQLQNGVVYPMAYHSHAATETCPGHSVLLTGDHPARTGIIANNWYDFSVKRADKKVYCSEDPSLSADPQNYQPSVHYLKVPTLGDRMKKANPHSRVISVAGKDRAAIMMGGHMTDQIWFWSDNAYKTLADHKGEMPVTVKTVNEQVTRFMQQDEAPVMPSVCADHASALKIGNNRIIGLAPASRKAGDFKTFRVTPDYDRTTTDIAIGLIDELKLGHGNAPDLLTVSLSATDAVGHAYGTEGAEMCSQMAGLDDNIARIIAALDSNGVPYVLVLTADHGGQDVPERAKLRGVETAQRVDPALSPDQLSLRLAERFQLSHNQPLFFANEPQGDWYINRNLPEQTKAQLIQAAKSELSNHPQVAAVFTASELTHIPYPTRSPELWNLAERAKASFDPLRSGDLIVLLKPRVTPIAKPVSYVATHGSAWDYDRRVPIIFYTPHASGFEQPMPVETVDIMPSLAALLQIPLRKGEVDGRCLDLDPTEATTCPVK
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Alkaline phosphatase with broad substrate specificity. Has phosphatase activity towards nucleotide and sugar phosphates with a preference to nucleotide phosphates. Has no phosphodiesterase activity. a phosphate monoester + H2O = an alcohol + phosphate Binds 2 Zn(2+) ions. Monomer.
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Q1RGU4
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MSLCTLEINLSAIKANYRLLKNICENSVDFLHNVANKEEFAGNTSPRTAAYTLVREDASLGSTPKLPLGASYAKNLLVGAAVKANSYGLGAIEISKTLLEENCRYFFVASSNEGISLRKAIGDEVNILILNGVFEHDALELIEYNLIPVLNNLNQIKIWQKFSNLKNQLLPCYLHFNTGINRLGLNHNEIEQLINNRDLLKGLNVEYIISHLSASEDSDNPYNLEQLNKFKAYLEYFPNAKASLANSGGIFLGKDYHFNLVRPGAALYGLNPLGSNKPNPMQNPVTLKAPIIHLQNLTYGSRIGYNMTFTTKRDSLIATLPFGYADGFSRNFSNQGTVFINSRNVPIIGRISMDLVNIDVTDLPPSDIFLGQEVEIIGNNCTPDKIADIIGTIGYEILTSLGNRYKRIYT
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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A8EXF8
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MSLCTLAINLSAIKNNYFLLQDICKTSLVGAVVKADGYGLGAVQISKALIEENCRHFFVASSEEGVNVRKALGIDVNILVLNGVFEHDALELIEYNLIPILNNLKQIEIWQQFGNLKNLLLPCYLHFNTGINRLGLSSNEIEQLINNRDLLKGLNLQYIISHLAISEEIDNPYNLEQLNKFKAYLRYFPSIKASLANSGGIFLGQDYHFDLVRPGAALYGLNPLMQNPVTLKAPIIHLQNLTLDSHIGYNMTFTTKRDSVIATLPLGYADGYSRNFSNQGKVFINGRSVPIVGRVSMDLINIDVTDLPPSDIFLGQEVEIIGNHCTPDKIASIIGTIGYEVLTSLGNRYRRKYTR
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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Q92JD9
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MSLCTVEINLSTIKNNYLLLQDICKTSLVGAAVKANGYGLGAVQISKALIEENCRHFFVASSEEGVNLRNALGLDVNILVLNGVFEHDALELIEYNLTPVLNNLKQIEIWQKFSNLKNRLLPCYLHFNTGINRLGLSSDEIEQLINDRDLLKGLDLQYIISHLAISEEIDNPYNLEQLNRFKAYLQYFPNVKASLANSGGIFLGQDYHFDLARPGAALYGLNPLTKNPVTLKAPIIHLQNLTLDSHIGYNMTFTTKRDSVIATLPLGYADGFSRNFSNQGEVFINSRSVPIVGRVSMDLINIDVTDLPPSEIFLGQEAEIIGNYCTPDKIASIIGTIGYEVLTNLGSRYKRKYIG
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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Q4UNC8
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MSLCTLEINLSAIKNNYLLLQDICKTSLVGAAVKANGYGLGAVQISKALIEENCRHFFVASSEEGVNLRKALASWHESVFRHCEKNYTVIRRSNPVKNSVSQNFFNYFSGLQQCFAPRNDGSSIHATTPKALDNDVNILVLNGVFEHDALELIEYNLTPVLNNLKQIEIWQKFSNLKNRLLPCYLHFNTGINRLGLTHNEIEQLINNRDLLKGLDLQYIISHLAVSEEIDNPYNLEQLNRFKTYLQYFPNVKASLANSGGIFLGQDYHFDLARPGAALYGLNPVIDLSNNLSYKEEFEGDTERRTAAYINVREDSSTGSTYKLPLEGGYSRGLQNPVTLKAPIIHLQNLTLDSHIGYNMTFTTERDSVIATLPLGYADGFSRNFSNQGEVFINGRSVPIVGRISMDLINIDVTDLPPLDIFLGQEAEIIGNYCTPDKIASIIGTIGYEVLTSLGSRYKRIYK
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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Q9ZE52
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MSLCTLEINLSAIKNNYRLLQDICKTALVGAVVKANGYGLGAMQIAKALIKENCQYFFVATSEEGINLRKVLNNDITILVLNGVFTHDALELIQYNLTPVLNNLSQIEIWQKFSNLKGKILPCYLHFNTGLNRFGLNSDEIEQLINDRDLLKGLDLQYIISHLAASEETGNPYNLIQLNRFKVYLEYFPNVKASFANSGGIFLGQDYHFDLARPGAALYGLNSLIEVSSNLSYTEEFESNTAALTTTACINKCPDVSVRLTPKLPLKGSYTVRLQNPVTLKAPIIDLQNLTLDSHIGYNMTFTTKRDSVIATLPLGYADGFSRNFSSQGEVFINSCSVPIVGRVSMDLINIDVTDLPPSEVFLGQEAEIIGNYCTPDKIASIIGTIGYEVLTSLGSRYKRKYIS
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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C4K1B0
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MSLCTVEINLSTIKNNYLLLQDVCKTSLVGAAVKANGYGLGAVQISKALIEENCRHFFVASSEEGVNLRNALGLDVNILVLNGVFEHDALELIEYNLTPVLNNLKQIEIWQKFSNLKNRLLPCYLHFNTGINRLGLSSDEIEQLINDRDLLKGLDLQYIISHLAISEEIDNPYNLEQLNRFKAYLQYFPNVKASLANSGGIFLGQDYHFDLARPGAALYGLNPLTKNPVTLKAPIIHLQNLTLDSHIGYNMTFTTKRDSVIATLPLGYADGFSRNFSNQGEVFINSRSVPIVGRVSMDLINIDVTDLPPSEIFLGQEAEIIGNYCTPDKIASIIGTIGYEVLTNLGSRYKRKYIG
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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B0BW55
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MSLCTVEINLSTIKNNYLLLQDVCKTSLVGAAVKANGYGLGAIQISKALIEENCRHFFVASSEEGVNLRNALGLDINILVLNGVFEHDALELIEYNLTPVLNNLKQIEIWQKFSNLKNRLLPCYLHFNTGINRLGLSSDEIEQLINDRDLLKGLDLQYIISHLAISEEIDNPYNLEQLNRFKAYLQYFPNVKASLANSGGIFLGQDYHFDLARPGAALYGLNPLTKNPVTLKAPIIHLQNLTLDSHIGYNMTFTTKRDSVIATLPLGYADGFSRNFSNQGEVFINSRSVPIVGRVSMDLINIDVTDLPPSEIFLGQEAEIIGNYCTPNKIASIIGTIGYEVLTNLGSRYKRKYIG
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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A8GQR1
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MSLCTVEINLSTIKNNYLLLQDVCKTSLVGAAVKANGYGLGAIQISKALIEENCRHFFVASSEEGVNLRNALGLDINILVLNGVFEHDALELIEYNLTPVLNNLKQIEIWQKFSNLKNRLLPCYLHFNTGINRLGLSSDEIEQLINDRDLLKGLDLQYIISHLAISEEIDNPYNLEQLNRFKAYLQYFPNVKASLANSGGIFLGQDYHFDLARPGAALYGLNPLTKNPVTLKAPIIHLQNLTLDSHIGYNMTFTTKRDSVIATLPLGYADGFSRNFSNQGEVFINSRSVPIVGRVSMDLINIDVTDLPPSEIFLGQEAEIIGNYCTPNKIASIIGTIGYEVLTNLGSRYKRKYIG
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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Q68XW3
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MSLCTLEINLSAIKNNYRLLQDICTTALVGAAVKANGYGIGAMQIAKALIEENCQYFFVATSEEGINLRKALNNDITILVLNGVFTHDALELIQYNLTPVLNNLKQIEIWQKFSNLKEKILPCYLHFNTGLNRFGLNYDEIEQLINDRDLLKGLDLQYIISHLAASEEMDNPYNLAQLNRFKDYLEYFPNVKASLANSGGIFLGQDYHFDLARPGAALYGLNSLIEVSYNLSYKEKFERNTPALATTVCINKCADVNTRLTYKVPLKGSYRLQNPVTLKAPIIHLQNLTLDSHIGYNMTFTTKRDSIIATLPLGYADGFSRNFSNQGEVFINSRSVPIVGRVSMDLINIDVTDLPPSEVFLGQEVEIIGNYCTPDKIASIIGTVGYEVLTSLGSRYKRKYIS
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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Q163V1
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MSTAVLTIDLSALAANWRSLNALSDVETAAVVKANAYGLGVGTAASALAEAGARHFFVAVAEEGVALRQALGAGPQISVFSGHMAGDTALIRDAGLTPMINSIDQMIRHVEALPEHDFGIQLDTGMNRLGMEDGEWRAVREVATQRPPSLVMSHLACADEPSHQMNRQQLDCFVEMTQDITAPRSLAATGGILMGPDYHFDLTRPGIGLYGGLPFVDALPVVQLDVPVIQVRDVHPGETVGYANTWTATAPARIATISAGYADGLIRAMGAKARLHAGDTALPVVGRVSMDLIGVDVTALGSDPDSLQLIGRHQSVDTVAGFADTIGYEILTSLGDRYKRVYTQ
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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Q1GFQ4
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MSTARLKINLDALAINWRNLDAKTNCETAAVVKANGYGLESGRVGKALAQAGARNFFVAIAEEGIALRRALGPGPGISVFAGHMEGDAKLLRDFQLTPMLNSLDQMLRHFESLPGHPFGVQLDSGMNRLGMEAAEWMAVRDIALDQNPVLLMSHLACSDEPGHGMNAYQLKNFIEMTEGLNIPRSLAATGGLLLGRDYHFDLCRPGIGLYGGAPYADALPVVELEVPVIQVRDLAPGESVGYGNTWIAQRDSKIATIAGGYADGLHRAFQRQGIMAYAGGTPCPVVGRISMDLITVDVTDLAEVPPYLSLMNETQTVDVLANAADTIGYEVLTSLGNRYARTYSA
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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A8M4B3
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MWQAEVRVDLDAIRENVSWLRSGSAAELMAVVKGDGYGHGMVPAALAALDGGADWLGVCTLDEALTLRREGITAPILAWLLAPGLPLHEGVAAGIDLGAASVAQLDEMVQAGRTAGRPARLHLKIDTGLSRGGATVSDWPGLLTAAAKAQADGTVEVVGVWSHFVYADAPGHPTTDRQLAVFHEGLDMVEKAGLRPRYRHLANSAATLTRPDAHFDLVRPGLAVYGLSPVAGESFGLRPAMTARARVMLTKQVPAGAGVSYGHTYTTERDSTLAVIPLGYADGVPRSASNSGPVHLGGVRRTISGRVCMDQFVLDCGDDPVAPGDVAVLFGSGRNGEPTADDWAEAVGTINYEIVTRFGSTRVPRSYDGERP
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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A4XBI0
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MWQAEVRVDLDAIRENVSWLRSGSAAELMAVVKGDGYGHGMVPAAHAALDGGADWLGVCTLDEALTLRRAGITVPVLAWLLAPGLPLHEGVTAGIDLGVASVAQLEEMVEAGRVAGRPARLHLKIDTGLSRGGATISEWPELLDAAAKAQADGAVEVVGVWSHFVYADAPGHPTTDRQLAVFHEGLGMVEKAGLRPRYRHLANSAATLTRPDAHFDLVRPGLAVYGLSPVAGERFGLRPAMTARARVMLTKQVPAGAGVSYGHTYTTDRASNLAVIPLGYADGVPRDASNSGPVQLGGVRRTISGRVCMDQFVLDCGDDPVAPGDVATLFGTGRDGEPTADDWAEAVGTINYEIVTRFGSTRVPRCYDGERP
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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A1SA53
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MKPFPRAEISSRALKANLKRLRQIAPGSKVMAVVKANGYGHGLLNVAEVLTDAHSNADADGFGLARLEEALEVRAGGVSARLLLLEGFFRSEDLPLLVEHDIDTVVHHVSQLDMLESVSLSKPVTVWLKIDSGMHRLGFHASEFKDVYQRLQQNPNVAKPVHLMTHFSCADEPQKDFTATQMAHFNALTQGLPGDRTLANSAGVLYWPQSQADWIRPGIALYGVSPVAGDLGSNHGLEPAMELVSQLIAVREHSAGESVGYGAYWTASRDTRLGVVAIGYGDGYPRNAPEGTPVLVNGRRVPIVGRVSMDMLTVDLGPDAADKVGDRALLWGKELPVEEVAERIGTIAYELVTKLTPRVAVCLD
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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B8E9P2
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MNPFPRAEISSSALQTNLAALRQQAPASRVMAVVKANGYGHGLLNVAHCLVSADGFGLARLDEALELRAGGVTARLLLLEGFFRATDLPLLVGHDIDTVVHHSSQLEMLEQTVLSKPVTVWLKVDSGMHRLGFTPEQFSTVYDRLMACPNVAKPIHLMTHFACADEPDNTYTSVQMAAFNSLTAGLPGFRTLANSAGALYWPQSQGDWIRPGIALYGVSPVTGDCGANHGLVPAMELVSQLIAVRDHKANQPVGYGCFWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWVNGRRVPIVGRVSMDMLTVDLGQDAQDKVGDSALLWGKALPVEEVAEHIGTIAYELVTKLTPRVAVCLA
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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A3D8P9
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MNPFPRAEISSSALQTNLAALRQQAPASRVMAVVKANGYGHGLLNVANCLVSADGFGLARLDEALELRAGGVTARLLLLEGFFRATDLPLLVGHDIDTVVHHSSQLEMLEQTVLSKPVTVWLKVDSGMHRLGFTPEQFSTVYDRLMACPNVAKPIHLMTHFACADEPDNTYTSVQMAAFNSLTAGLPGFRTLANSAGALYWPQSQGDWIRPGIALYGVSPVTGDCGANHGLVPAMELVSQLIAVRDHKANQPVGYGCFWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWVNGRRVPIVGRVSMDMLTVDLGQDAQDKVGDSALLWGKALPVEEVAEHIGTIAYELVTKLTPRVAVCLA
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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A6WJ85
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MNPFPRAEISSSALQTNLAALRQQAPASRVMAVVKANGYGHGLLNVANCLVSADGFGLARLDEALELRAGGVTARLLLLEGFFRATDLPLLVGHDIDTVVHHSSQLEMLEQTVLSKPVTVWLKVDSGMHRLGFTPEQFSTVYARLMACPNVAKPIHLMTHFACADEPDNSYTSVQMAAFNSLTAGLPGFRTLANSAGALYWPQSQGDWIRPGIALYGVSPVTGDCGANHGLVPAMELVSQLIAVRDHKANQPVGYGCFWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWVNGRRVPIVGRVSMDMLTVDLGQDAQDKVGDSALLWGKALPVEEVAEHIGTIAYELVTKLTPRVAVCLA
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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A9L126
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MNPFPRAEISSSALQTNLAALRQQAPASRVMAVVKANGYGHGLLNVANCLVSADGFGLARLDEALELRAGGVTARLLLLEGFFRATDLPLLVGHDIDTVVHHSSQLEMLEQTVLSKPVTVWLKVDSGMHRLGFTPEQFSTVYDRLMACSNVAKPIHLMTHFACADEPDNTYTSVQMAAFNTLTAGLPGFRTLANSAGALYWPQSQGDWIRPGIALYGVSPVTGDCGANHGLVPAMELVSQLIAVRDHKANQPVGYGCFWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWVNGRRVPIVGRVSMDMLTVDLGQDAQDKVGDSALLWGKALPVEEVAEHIGTIAYELVTKLTPRVAVCLA
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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Q12RW2
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MKPFPRAEISRKALQANLARIRELAPQSKIMAVVKANGYGHGLLNVANSVATYDQGADGFGLARLEEALELRSGGVNARLLLLEGFFRVTDLPLLVQHHIDTVVHHESQVEMLEQAELTTPVTVWMKIDTGMHRLGFSLAQFDAIYQRLLACHNIAKPIHLMTHFACSDEPDNSFTQAQIDAFESVTASLDGDRSLANSGGMLFWPQSQRDWIRAGIALYGVSPMVGDKGGNHGLVPAMELKSQLISVKDHQAGDSVGYGAFWRARKDTRIGVVAIGYGDGYPRHAPEGTPVWLNGRRVPIVGRVSMDMLTVDLGLDSQDKVGDEVLLWGSALAVEEVADHIGTIAYELVTKLTPRVAVALLP
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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Q07XT3
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MKPFPRAEISRYALQSNLAQLRLIAPNSKIMAVVKANGYGHGLLNVAECVGLLNYVESVCKYHGGADGFGLARLEEALQLREGGVKGKLLLLEGFFRQSDLPTLVSHNIDTVVHHESQLQMLETIALDKPVTVWIKIDTGMHRIGFSLEQFNSIYQRLLACPQVAKPIHLMTHFACADEPDNPLTQTQMNAFEQQVSGLEGDRTLANSAGTLFWPTSQADWVRPGIALYGVSPVVGDRGVNHRLIPAMELVSNLIAVREHKAGDSVGYGASWTAKKDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGADAQDNVGDSVQLWGKALAVEEVAEHIGTIAYELVTKLTPRVVVELLD
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Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. L-alanine = D-alanine Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. Belongs to the alanine racemase family.
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Q9DCW6
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MVLRGVRVVELAGLAPGPFCGMVLADFGAEVVRVNRLGSTGENFLARGKRSLALDLKRSQGVTVLRRMCARADVLLEPFRCGVMEKLQLGPETLLQDNPKLIYARLSGFGQSGIFSKVAGHDINYLALSGVLSKIGRSGENPYPPLNLLADFGGGGLMCTLGIVLALFERTRSGRGQVIDSSMVEGTAYLSSFLWKTQPMGLWKQPRGQNILDGGAPFYTTYKTADGEFMAVGAIEPQFYALLLKGLGLESEELPSQMSSADWPEMKKKFADVFAKKTKAEWCQIFDGTDACVTPVLTFEEALHHQHNRERASFITDGEQLPSPRPAPLLSRTPAVPSAKRDPSVGEHTVEVLREYGFSQEEILQLHSDRIVESDKLKANL
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Catalyzes the interconversion of (R)- and (S)-stereoisomers of alpha-methyl-branched-chain fatty acyl-CoA esters (By similarity). Acts only on coenzyme A thioesters, not on free fatty acids, and accepts as substrates a wide range of alpha-methylacyl-CoAs, including pristanoyl-CoA, trihydroxycoprostanoyl-CoA (an intermediate in bile acid synthesis), and arylpropionic acids like the anti-inflammatory drug ibuprofen (2-(4-isobutylphenyl)propionic acid) but neither 3-methyl-branched nor linear-chain acyl-CoAs (By similarity). a (2S)-2-methylacyl-CoA = a (2R)-2-methylacyl-CoA (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA = (25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA (2R,6)-dimethylheptanoyl-CoA = (2S,6)-dimethylheptanoyl-CoA Lipid metabolism; bile acid biosynthesis. Lipid metabolism; fatty acid metabolism. Monomer. Belongs to the CoA-transferase III family. Truncated N-terminus.
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I6XAR5
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MAGPLSGLRVVELAGIGPGPHAAMILGDLGADVVRIDRPSSVDGISRDAMLRNRRIVTADLKSDQGLELALKLIAKADVLIEGYRPGVTERLGLGPEECAKVNDRLIYARMTGWGQTGPRSQQAGHDINYISLNGILHAIGRGDERPVPPLNLVGDFGGGSMFLLVGILAALWERQSSGKGQVVDAAMVDGSSVLIQMMWAMRATGMWTDTRGANMLDGGAPYYDTYECADGRYVAVGAIEPQFYAAMLAGLGLDAAELPPQNDRARWPELRALLTEAFASHDRDHWGAVFANSDACVTPVLAFGEVHNEPHIIERNTFYEANGGWQPMPAPRFSRTASSQPRPPAATIDIEAVLTDWDG
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Catalyzes the epimerization of (2R)- and (2S)-methylacyl-coenzyme A (CoA) thioesters (PubMed:15632186, PubMed:19854148, PubMed:26348625). Accepts as substrates a wide range of alpha-methylacyl-CoAs, including (2R)-2-methylmyristoyl-CoA and (2S)-2-methylmyristoyl-CoA, (2R)-pristanoyl-CoA and (2S)-pristanoyl-CoA, and the cholesterol esters (25R)-3-oxo-cholest-4-en-26-oyl-CoA and (25S)-3-oxo-cholest-4-en-26-oyl-CoA (PubMed:15632186, PubMed:26348625). Can also catalyze the interconversion of the non-physiologic substrates (2R)-ibuprofenoyl-CoA and (2S)-ibuprofenoyl-CoA, which are potential competitive inhibitors of the enzyme (PubMed:19854148). a (2S)-2-methylacyl-CoA = a (2R)-2-methylacyl-CoA (2S)-2-methyltetradecanoyl-CoA = (2R)-2-methyltetradecanoyl-CoA (2R)-pristanoyl-CoA = (2S)-pristanoyl-CoA (25S)-3-oxocholest-4-en-26-oyl-CoA = (25R)-3-oxocholest-4-en-26-oyl-CoA (2S)-ibuprofenoyl-CoA = (2R)-ibuprofenoyl-CoA Inactivated by N,N-dialkylcarbamoyl-CoA substrate-product analogs. kcat is 3.7 sec(-1) with (25R)-3-oxo-cholest-4-en-26-oyl-CoA as substrate (PubMed:26348625). kcat is 450 sec(-1) with (2S)-ibuprofenoyl-CoA as substrate (PubMed:19854148). kcat is 291 sec(-1) with (2R)-ibuprofenoyl-CoA as substrate (PubMed:19854148). Homodimer. Development of gem-disubstituted substrate-product analogs as inhibitors of racemases and epimerases is elaborated using alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis as a model enzyme. These non-physiologic substrates could be used as a therapeutic agent to inhibit human AMACR, which is overexpressed in prostate cancer. Interconversion is achieved via a planar enolate intermediate. Belongs to the CoA-transferase III family.
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O09176
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MALRGVRVLELAGLAPGPFCGMILADFGAEVVLVDRLGSVNHPSHLARGKRSLALDLKRSPGAAVLRRMCARADVLLEPFRCGVMEKLQLGPETLRQDNPKLIYARLSGFGQSGIFSKVAGHDINYVALSGVLSKIGRSGENPYPPLNLLADFGGGGLMCTLGILLALFERTRSGLGQVIDANMVEGTAYLSTFLWKTQAMGLWAQPRGQNLLDGGAPFYTTYKTADGEFMAVGAIEPQFYTLLLKGLGLESEELPSQMSIEDWPEMKKKFADVFARKTKAEWCQIFDGTDACVTPVLTLEEALHHQHNRERGSFITDEEQHACPRPAPQLSRTPAVPSAKRDPSVGEHTVEVLKDYGFSQEEIHQLHSDRIIESNKLKANL
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Catalyzes the interconversion of (R)- and (S)-stereoisomers of alpha-methyl-branched-chain fatty acyl-CoA esters (PubMed:8020470, PubMed:9106621). Acts only on coenzyme A thioesters, not on free fatty acids, and accepts as substrates a wide range of alpha-methylacyl-CoAs, including pristanoyl-CoA, trihydroxycoprostanoyl-CoA (an intermediate in bile acid synthesis), and arylpropionic acids like the anti-inflammatory drug ibuprofen (2-(4-isobutylphenyl)propionic acid) but neither 3-methyl-branched nor linear-chain acyl-CoAs (PubMed:8020470, PubMed:9106621). a (2S)-2-methylacyl-CoA = a (2R)-2-methylacyl-CoA (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA = (25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA (2R,6)-dimethylheptanoyl-CoA = (2S,6)-dimethylheptanoyl-CoA Optimum pH is 6-7. Lipid metabolism; bile acid biosynthesis. Lipid metabolism; fatty acid metabolism. Monomer. Belongs to the CoA-transferase III family.
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U5L3J5
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MSDINTARLPVFSLPVFFPFVSDDIQAVLTRGESLC
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Cyclic nonapeptide that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24050899). Expressed in basidiocarps (PubMed:24050899). Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic nonapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By similarity). The enzyme rebinds the remaining peptide in a different conformation and catalyzes macrocyclization of the N-terminal 9 residues (By similarity). Amanexitides have a structure closely related to antamanide, a cyclic decapeptide with antidote activity against amatoxins and phallotoxins, and might therefore exhibit the same activity (Ref.2). Belongs to the MSDIN fungal toxin family.
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U5L3K1
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MSDINATRLPVFSLPVFFPFVSDDIQAVLTRGESLC
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Cyclic nonapeptide that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24050899). Expressed in basidiocarps (PubMed:24050899). Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic nonapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By similarity). The enzyme rebinds the remaining peptide in a different conformation and catalyzes macrocyclization of the N-terminal 9 residues (By similarity). Amanexitides have a structure closely related to antamanide, a cyclic decapeptide with antidote activity against amatoxins and phallotoxins, and might therefore exhibit the same activity (Ref.2). Belongs to the MSDIN fungal toxin family.
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P86781
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QKIQEIDLQTYLQPQ
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Has antifungal activity against A.flavus and F.oxysporum.
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Q5V0X0
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MSVTRHYDREFVRTFFTSPTAVDGEEDSAKMLRSAGQLRGLQAPDVWVPDNEDATAPNMRAEGVENIIDVVANQGAEFPGEIHPRVVWHRESPATRYKGFQQMLEITDPENGAVEHIDGFVIPEVGDIDDWKKADEFFTIIEHEHGLEEGSLSMSVIVESGEAELAMGDLREEMGKPSNNLERMFLLVDGEVDYTKDMRAMTPTGELPPWPELRHNTSRGASAAGLIAVDGPYDDIRDVEGYRERMKDNRAKGMTGIWSLTPGQVVEANTAPLPPKTGSWLLEAGGQEVELEAQDGKQVYDGDDLSLEEVSDGGYVLQAGGDRLELDEDELTEELLDRTAYIPSMTDIVDSMEEFEAAKEAGKGAIAMTQAATLVINGVEVDISKDRMWDEATYQAAQTPITLFQDVYEHRPDQHEELAEMYGADIVERATAVGN
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Involved in the methylaspartate cycle. Catalyzes the biosynthesis of malate in two steps. In the first reaction acetyl-CoA is condensed reversibly with glyoxylate to form (S)-malyl-CoA. In the second reaction (S)-malyl-CoA is hydrolyzed to malate and CoA. It can also catalyzes the condensation of propionyl-CoA with glyoxylate and of acetyl-CoA with pyruvate, however the CoA-ester hydrolysis reaction is highly specific for (S)-malyl-CoA. (S)-malyl-CoA = acetyl-CoA + glyoxylate (S)-malyl-CoA + H2O = (S)-malate + CoA + H(+) Divalent cations. Mg(2+) and to a lesser extent, Mn(2+), Co(2+) and Ca(2+). Belongs to the HpcH/HpaI aldolase family.
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Q9I1H0
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MQERHGLPLRSFSSGKALTAGRAVRPEVAQERRYLQGAPLGLELPGRIALRDPHCAWQWFEPEAAAEAFPAAHWLAAFLVLLGRYGNEEITLGFPEPITVRGRQAPALLRSSYRAMESSAERSARLAEELDDARRQLSADGQERAALAGRCAVQVLAARPTASSPGWLALVLAADGSVGLALRDPQYDELRRIAGHLARLARGLVDAQACVGRLPWLDADEERRLQALRSEPQAAPSRGVLHHLFEAQARRTPQRIAVHAADRSLSYAELERESAALAVRLRAAGVAPEQRVGVCLRRDSGLLVGLLGVLRAGGCYVPLDPAYPEERVAYMLDDADCLLVLVDASTRERVAALGRPCLTLEEGGDQANDLALPASEVGADHLAYIIYTSGSTGRPKGVAIEHGSAHAFLRWAGQHYAAEEWSGVLAATSVCFDLSVYELFGTLAEGGTLHLVENLFSLPDYPRRDEISLLNTVPSVCAALLALGDLPGGVRTLNLAGEPLRGHLVRQIRGQPQVRRLVNLYGPTEDTTYSTVHELDLHAEALDEPPIGRPLPGTTVEVLDGFEAPLPLGVAGELYLGGIGLARGYFGKPEQTAERFRVDPGSGERRYRTGDRVRMREDGVLEHLGRLDDQVKFNGFRIELGEIASCLASFPGVSEACAMLTEDSAGLRRLVGYLAAPFAPPLQALNEHLGQSLPHYMLPSAFVVLAELPKTLNGKIDRKALPRPQATGAEPQALPSDPLEQALHQAWQAQLGAPPRAGQGFYAAGGDSLRAVHLLATLRQRLSRRVPLQAFAGGPATPEALLELLRQAAPEGDEPEPSAGAAGLSLAERRLWVAQQLAPEDTSYNLLAHLRIVGATADAIEQALRQLLERHVALRRRVETGVDGPQPHALAAHAVPLQRLLASDAVHAERLLEDGVRREGARVFDLAHEAPARLLLVVTRDSARADLLLSVHHYAFDDVSLAVFAAELKTLLDGGRLGVLASTPEQVAARERAALASGRLDRVAERWAERLLPLAKAPGAAPARPEESGGRAGQRLALPVSAAVHAACRALAERTSVSPFSAALQAFAEVLGAELGVDDLLVGVALAGRSRLEMQGLVGCFVNLLPLAVGLRPEQSVEWRLRQVGHDLLELLEHQDVPLECVTQALRQRGASGLPIRIACGAHNGRAAPAVDAGVRVEADFIPVPGARLDLTLWLEDQPQGWLAVWTGVSAIFDLHRIERLHQAWERRLLANAGEPISKRMSPEGCNAS
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Involved in the biosynthesis of the antimetabolite L-2-amino-4-methoxy-trans-3-butenoic acid (AMB), a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes (PubMed:20543073, PubMed:25814981). Adenylates L-alanine and loads it onto its peptidyl carrier domain via a thioester linkage to the phosphopanthetheine moiety. In addition, loads activated L-Ala in trans onto the second carrier domain of AmbE (PubMed:25814981). Can also activate L-Ser, Gly and D-Ala, albeit to a lower extent (PubMed:25814981). The condensation domain of AmbB probably condenses the activated L-Ala and the L-Glu loaded on AmbE to form a L-Glu-L-Ala dipeptide at the first carrier domain of AmbE (PubMed:25814981). ATP + holo-[peptidyl-carrier protein] + L-alanine = AMP + diphosphate + L-alanyl-[peptidyl-carrier protein] Expression is regulated by the PhoR-PhoB two-component system. Modular protein that contains an adenylation domain which activates the alanine residue into an aminoacyl-AMP ester, a peptidyl carrier protein domain which bears a phosphopantetheinyl arm to attach the activated alanine and a condensation domain involved in the condensation of this amino acid with a second amino acid bound at the carrier protein domain of another module. Mutation abolishes AMB production (PubMed:20543073, PubMed:23542643). Deletion of the gene almost abolishes the production of the quorum sensing signals 2-heptyl-3-hydroxy-4(1H)-quinolone (PQS) and N-butanoylhomoserine lactone (C4HSL), but it has no effect on the biosynthesis of the quorum sensing signal N-3-oxododecanoylhomoserine lactone (3OC12HSL) (PubMed:23542643). Deletion causes a substantial reduction in the production of the virulence factors pyocyanine and elastase, and it reduces bacterial virulence by about 32-40% (PubMed:23542643). Belongs to the NRP synthetase family. It was suggested by Lee et al that the amb cluster is involved in the biosynthesis of 2-(2-hydroxyphenyl)-thiazole-4-carbaldehyde (IQS), a cell-cell communication signal that modulates the production of AMB through the pqs and rhl quorum sensing systems (PubMed:23542643). The chemical structure of IQS indicates that this compound may be assembled from salicylate and cysteine. However, neither of the two peptide synthases encoded by the amb gene cluster present adenylation domains with a specificity for these substrates. It is thus highly implausible that IQS is specified by the amb gene cluster (PubMed:25814981).
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Q9I1H3
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MSASEDLQSAVQPAASEALEGFPLSPLQTRAWRRHAERPENTVVGVRLHAPADPVATLERLRRALDGEAQLRVAYRTMPGMSLPVQVLDGRAADLLVERLPGDGDWAGRFARESARLAASPLGGEGQPVLALGLLLDAAGETLQGLLLAAPAFVVDAASLVALLRRGLGPAGQASADEGDEALLFQHFSEWANEALAGEDGESASGYWREQAAVAAESPLALADDLGEGEWTARRLLPRALLERLAANGLPEAAALLAWTQVAGQFQGDEGLPLEMARLVSGRLFNEFAELAGPFAGVAPLCLENVRAGSVGERLDALQAAILAQEEAAALRDPFAPDWPLAELGFAWLAGELDGAGVAELDCRQPPLGGFLELQVLPHGEGRLASLRVRRDHDGTLAGRLLDAWVECLESIAADRQLPLAGLPLIGAAERERYQAWQGERVEPAPVESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGRAREAFAGACLDLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYANVVGEGLRVTVNAPFSFDSSIKQILQLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGRILVGGERFDEASWEVAAGWRRCQVFNLYGPTEATVNASLARVAEHARPTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEADAAEPGADRRIVAFVTAAEETADESWLEVDLPSGHRVAGLNLNETEYVYQEIFVDEVYSRDGIVLPPDAVVLDVGANIGLFSLYIASRAPRARVVAFEPLAPIRRRLEANLGRYAPQVEVFGIGLSDAEREETFTYYPGYSTFSGIAEYADASGERDVIRRYLSNQGEEGGANLLLDNIDEILDDRLRAEAHRCRLRRLDQVIGELGLERIDLLKIDVQRAEMDVLLGLDDAALAKVRQIVLEVHDKRDGATAGRADALSDLLRRHGFEVSIRQDALLEGTDRYNCYAVRPGYAESLAERIDWRALAPRPAAALGGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEAPANATEAALLEIWKSVLKRPAIGVSDNFFQVGGDSIRLIQMQVMAREAGLAFTLRDVFNHQSIRELARLLAAPASPADALGTSAPQSLEPFALLSAAERKRLPEGLDDAYPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPATAVAAEVPVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAGVVAREAEAPAVGFRDYVALEREAEANAASALFWLDYLAGARYRPLPGLAEEGPRRMAAVRVDVPADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEEPGADRLLGLFLNTLPCRLSASVDLLDSARRAFDYERASLEHRRHPLAAIRRRNRELRLDSLFNFVDFHQDDAAPAGVRHGGILDQVVVDVDVPLAVDFEVAGERLEVGFQYAAGRFPAERAEALAGAYREALLALLGDPVQPPAAAQAEDSVELRRVLKVLSRVLGRPLAADQGFASAGGHSLLGVQAIAELRRLTGRQLSLGLLQGDPDAREVVRRCHAADAPPLPPATERARALWLQRSGSAQPRLRLIALPPAGGNAGTFRGWDARLPADVELLAIQYPGRQERQDEPFVTDVEAMLCAIDDALLPLLDRPFALIGASLGGMLAYELAARLESLHGLRARQLFVISSRAPGPDLEYPRFHAMGDAELLRTLREYDVLPLEVLDDPELREISLATLRADSRLAADYRYRPREPLAIPITAILGEQDPGVSRVAIDGWRRHASRYELETLAGGHGLVVTAAEEVCAILRQRLAPDVPGGVPANLAT
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Involved in the biosynthesis of the antimetabolite L-2-amino-4-methoxy-trans-3-butenoic acid (AMB), a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes (PubMed:20543073, PubMed:25814981). Adenylates L-glutamate and loads it onto its first peptidyl carrier domain via a thioester linkage to the phosphopanthetheine moiety (PubMed:25814981). The second peptidyl carrier domain is loaded with a L-alanine activated by AmbB (PubMed:25814981). After formation by AmbB of the L-Glu-L-Ala dipeptide at the first carrier domain of AmbE, the condensation domain of AmbE probably condenses this dipeptide with the L-Ala residue attached at the second carrier domain of AmbE to give the L-Ala-L-Glu-L-Ala tripeptide. The central amino acid, L-Glu, would then undergo a series of modifications to be converted into AMB while the two flanking L-Ala residues remain in place (PubMed:25814981). Finally, the L-Ala-AMB-L-Ala tripeptide is probably released by thioester cleavage via the thioester domain of AmbE (PubMed:25814981). ATP + holo-[peptidyl-carrier protein] + L-glutamate = AMP + diphosphate + L-glutamyl-[peptidyl-carrier protein] Expression is regulated by the PhoR-PhoB two-component system. Modular protein that contains an adenylation domain which activates the glutamate residue into an aminoacyl-AMP ester, a methyltransferase domain, a first peptidyl carrier protein domain which bears a phosphopantetheinyl arm to attach the activated L-glutamate, a condensation domain involved in the condensation of this amino acid with a second amino acid bound at the carrier protein domain of another module, a second peptidyl carrier protein domain which bears a phosphopantetheinyl arm to attach a L-alanine activated by AmbB and a thioesterase domain that may release the newly synthesized peptide from the enzyme. Mutation abolishes AMB production (PubMed:20543073). Deletion of the gene causes a substantial reduction in the production of the quorum sensing signal 2-heptyl-3-hydroxy-4(1H)-quinolone (PQS) (PubMed:23542643). Belongs to the NRP synthetase family. It was suggested by Lee et al that the amb cluster is involved in the biosynthesis of 2-(2-hydroxyphenyl)-thiazole-4-carbaldehyde (IQS), a cell-cell communication signal that modulates the production of AMB through the pqs and rhl quorum sensing systems (PubMed:23542643). The chemical structure of IQS indicates that this compound may be assembled from salicylate and cysteine. However, neither of the two peptide synthases encoded by the amb gene cluster present adenylation domains with a specificity for these substrates. It is thus highly implausible that IQS is specified by the amb gene cluster (PubMed:25814981).
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V5TF65
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MISEKILRHIFQYRRLLSDTEPCAKEPCSICLAPHLPKIQSFIENNEPIHFILPAFPAKSPNPQKVLGPMPDMGERVALQFLQNLCNQISEIYASGAKITICSDGRVFTDLVAITDENVSLYRQGIQRLLNEINADAIDTFCLENVFTGMSFDQMRKTLVKQYAQPIESIQERVNSEDKHRQFFKGIYHLLFDDYLVLYPDKSREQIEVECNLRAYEVIQRSNAWTTLVGQHFPQSLRLSIHPQDYHSNKIGIHMIKTSDQWGTPWHNAPMFNGKEFLLMKRKHIEDIGASLVWHNDHPSHYILSEQVSQALVTLDNKS
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Involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids (PubMed:24180436). Responsible for the synthesis of the isonitrile group on tryptophan using ribulose 5-phosphate as the source of the carbon atom (PubMed:24180436, PubMed:28212039). D-ribulose 5-phosphate + L-tryptophan = (2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate + formaldehyde + H(+) + H2O + hydroxyacetone + phosphate Belongs to the isocyanide synthase family.
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V5TES5
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MTQIINITQSKVISEQILRHVFRHRRLISDTEPCVHQPCSLCLAPHLEKVQYFVEHNEPIHFILPAFPAKSPNTQKVLGTMPDMGEQVSLKFLQSLCDQISEIYAPGAKLTICSDGRVFSDLVGVTDENVTLYGQIIQALLKEMKADAIDVFNLEDMYTDLSFDEMRQKLVKLYGQTIEAIKDAVKNNDHQCQMFNGIHRFLVEDYQVLEAHKSRNKIRLECKTRAYEVIQRSNAWSVLISELYPHSVRLSIHPQHYHSEKIGIHMIKTLDQWGTPWHNATVFDGKEFMLMKRSHLESMGATLVCQNGHPSYFAWTEQPLETRITVQEVI
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Involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids (PubMed:24180436). Responsible for the synthesis of the isonitrile group on tryptophan using ribulose 5-phosphate as the source of the carbon atom (PubMed:24180436, PubMed:28212039). D-ribulose 5-phosphate + L-tryptophan = (2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate + formaldehyde + H(+) + H2O + hydroxyacetone + phosphate AmbI1 and AmbI3 alone are sufficient to generate Z-3-(2-isocyanoethen)-indole from L-tryptophan and ribulose 5-phosphate, but AmbI2 and AmbI3 are not, suggesting that AmbI2 is functionally redundant in vitro. Belongs to the isocyanide synthase family.
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V5TD18
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MIVSTSVEQSAQFSVKSLTPFGALLEATEDHSDIQQLSIEQLCQLTWEHRLIVLRGFSLLEREELSTYCQRWGELLVWNFGTVLDLIVHQNPENYLFTNGNVPFHWDGAFAEAVPRFLFFQCLKAPEAGSGGESLFCDTVRILQNVSPQQREIWQKTEISYKTQKVAHYGGEITKSLVIKHPITGLSTLRFAEPLNDASVHLNPLYVEVCNLPAEEQNPFINELIENLYLPQNCFAHEWQEGDFLIADNHALLHGRNPFLSNSQRHLQRVHIL
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Involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids (PubMed:24180436). Responsible for the synthesis of Z-3-(2-isocyanoethen)-indole, a biosynthetic precursor to all ambiguines (PubMed:24180436, PubMed:28212039). (2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate + 2-oxoglutarate + H(+) + O2 = 3-[(Z)-2-isocyanoethenyl]-1H-indole + 2 CO2 + H2O + succinate Binds 1 Fe(2+) per subunit. Belongs to the TfdA dioxygenase family.
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P81540
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MKKIVIVGGGIAGMGIANTLADKLKGKAEITVINKEDFYFAGPSRXIL
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Ambineela is a blue protein and has a pI of 8.7. Monomer. The blue color is due to an unidentified non-fluorescent cofactor, covalently bound to it.
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Q9XSX7
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MPALKIPLFKMKDMILILCLLKMSSAVPAFPQQPGIPGMASLSLETMRQLGSLQGLNLLSQYSRFGFGKSFNSLWMNGLLPPHSSFPWMRPREHETQQPSLQPQQPGQKPFLQPTVVTSMQNAVQKGVPQPPIYQGHPPLQQAEGPMVEQQVAPSEKPPTTELPGMDFADLQDPPMFPIAHLISRGPMPQNKPSQLYPGIFYVTYGANQLGGRGDPLAYGAIFPGFGGMRPRLGGMPHNPDMGGDFTLEFDSPVAATKGPEKGEGGAQDSPVPEAHLADPESPALLSELAPGALEGLLANPEGNIPNLARGPAGRSRGFLRGVTPAAADPLMTPGLAEVYETYGADETTTLGLQEETTVDSTATPDTQHTLMPRNKAQQPQIKHDAWHFQEP
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Involved in the mineralization and structural organization of enamel. Belongs to the ameloblastin family.
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Q9H4L1
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MSASKIPLFKMKDLILILCLLEMSFAVPFFPQQSGTPGMASLSLETMRQLGSLQRLNTLSQYSRYGFGKSFNSLWMHGLLPPHSSLPWMRPREHETQQYEYSLPVHPPPLPSQPSLKPQQPGLKPFLQSAAATTNQATALKEALQPPIHLGHLPLQEGELPLVQQQVAPSDKPPKPELPGVDFADPQGPSLPGMDFPDPQGPSLPGLDFADPQGSTIFQIARLISHGPMPQNKQSPLYPGMLYVPFGANQLNAPARLGIMSSEEVAGGREDPMAYGAMFPGFGGMRPGFEGMPHNPAMGGDFTLEFDSPVAATKGPENEEGGAQGSPMPEANPDNLENPAFLTELEPAPHAGLLALPKDDIPGLPRSPSGKMKGLPSVTPAAADPLMTPELADVYRTYDADMTTSVDFQEEATMDTTMAPNSLQTSMPGNKAQEPEMMHDAWHFQEP
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Involved in the mineralization and structural organization of enamel. Ameloblast-specific. Located at the Tomes processes of secretory ameloblasts and in the sheath space between rod-interrod enamel. The disease is caused by variants affecting the gene represented in this entry. Belongs to the ameloblastin family.
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O55189
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MSASKIPLFKMKGLILFLSLVKMSLAVPAFPQQPGAQGMAPPGMASLSLETMRQLGSLQGLNALSQYSRLGFGKALNSLWLHGLLPPHNSFPWIGPREHETQQPSLQPHQPGLKPFLQPTAATGVQVTPQKPGPQPPMHPGQLPLQEGELIAPDEPQVAPSENPPTPEVPIMDFADPQFPTVFQIARSISRGPMAHNKASAFYPGMFYMSYGANQLNAPARIGFMSSEEMPGERGSPMAYGTLFPRFGGFRQTLRRLNQNSPKGGDFTVEVDSPVSVTKGPEKGEGPEGSPLQEANPGKRENPALLSQMAPGAHAGLLAFPNDHIPSMARGPAGQRLLGVTPAAADPLITPELAEVYETYGADVTTPLGDGEATMDITMSPDTQQPLLPGNKVHQPQVHNAWRFQEP
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Involved in the mineralization and structural organization of enamel. Ameloblast-specific. Belongs to the ameloblastin family.
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Q28989
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MPALKIPLFKMKDMVLILCLLKMSSAVPAFPRQPGTPGVASLSLETMRQLGSLQGLNMLSQYSRFGFGKSFNSLWMHGLLPPHSSFQWMRPREHETQQYEYSLPVHPPPLPSQPSLQPQQPGQKPFLQPTVVTSIQNPVQKGVPQPPIYQGHPPLQQVEGPMVQQQVAPSEKPPEAELPGLDFADPQDPSMFPIARLISQGPVPQDKPSPLYPGMFYMSYGANQLNSPARLGILSSEEMAGGRGGPLAYGAMFPGFGGMRPNLGGMPPNSAKGGDFTLEFDSPAAGTKGPEKGEGGAEGSPVAEANTADPESPALFSEVASGVLGGLLANPKGKIPNLARGPAGRSRGPPGVTPADADPLMTPGLADAYETYGADETTTLGLQEEMTMDSTATPYSEHTSMPGNKAQQPQIKRDAWRFQEP
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Involved in the mineralization and structural organization of enamel. Ameloblast-specific. Located at the Tomes processes of secretory ameloblasts and in the sheath space between rod-interrod enamel. Belongs to the ameloblastin family.
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Q63043
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MSASKIPLFKMKGLLLFLSLVKMSLAVPAFPQQPGAQGMAPPGMASLSLETMRQLGSLQGLNALSQYSRLGFGKALNSLWLHGLLPPHNSFPWIGPREHETQQYEYSLPVHPPPLPSQPSLQPHQPGLKPFLQPTAATGVQVTPQKPGPHPPMHPGQLPLQEGELIAPDEPQVAPSENPPTPEVPIMDFADPQFPTVFQIAHSLSRGPMAHNKVPTFYPGMFYMSYGANQLNAPARIGFMSSEEMPGERGSPMAYGTLFPGYGGFRQTLRGLNQNSPKGGDFTVEVDSPVSVTKGPEKGEGPEGSPLQEASPDKGENPALLSQMAPGAHAGLLAFPNDHIPNMARGPAGQRLLGVTPAAADPLITPELAEVYETYGADVTTPLGDGEATMDITMSPDTQQPPMPGNKVHQPQVHNAWRFQEP
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Involved in the mineralization and structural organization of enamel. Ameloblast-specific. Belongs to the ameloblastin family.
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Q3SZZ4
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MRSLSGLLLLLTACLAVNASSVPTLPDDIQVQENFDLSRIYGKWFNVAVGSTCPWLKRFKEKMTMSTVVLIAGPTSKEISVTNTHRRKGVCESISGTYEKTSADGKFLYHKAKWNITMESYVVHTNYDEYAIFLTKKLSRRHGPTITVKLYGREPQLRESLLEEFREVALGVGIPEDAIFTMPDRGECVPGEQDPVPTPLSRARRAVLTQEEEGSGAGQPVTNFSKKADSCQLDYSQGPCLGLFKRYFYNGTSMACETFLYGGCMGNGNNFLSEKECLQTCRTVEACNLPIVQGPCRSYIQLWAFDAVKGKCVRFSYGGCKGNGNKFYSEKECKEYCGIPGEADEELLRFSN
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Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments. Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis. Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential. Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage. Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures. Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation. Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria. Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (By similarity). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity). Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion. Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule-stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases. As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (By similarity). Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity). Also inhibits calcium oxalate crystallization (By similarity). Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. Monomer. Homodimer. In plasma, it occurs as a monomer or dimer and in covalently-linked complexes with immunoglobulin A (IgA), ALB/albumin and F2/prothrombin. Chromophore-bound alpha-1-microglobulin interacts with the constant region of immunoglobulin A. Chromophore-bound alpha-1-microglobulin interacts with ALB with molar ratio 2:1 and 1:1; this interaction does not prevent fatty acid binding to ALB. Interacts with F2/prothrombin (via N-terminus) with molar ratio 2:1 and 1:1; this interaction does not prevent the activation of prothrombin to thrombin. Interacts with NDUFAB1, a subunit of mitochondrial complex I (By similarity). Interacts with FN1 (By similarity). I-alpha-I plasma protease inhibitors are assembled from one or two heavy chains (HC) and one light chain, bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of ITIH1/HC1, ITIH2/HC2 and bikunin, and pre-alpha-inhibitor (P-alpha-I) of ITIH3/HC3 and bikunin. Interacts with TNFAIP6 (via Link domain). Monomer. Also occurs as a complex with tryptase in mast cells. The cellular uptake occurs via a non-endocytotic pathway and allows for localization to various membrane structures. A specific binding to plasma membrane suggests the presence of a cell receptor, yet to be identified. Directly binds collagen fibers type I. Expressed by the liver and secreted in plasma. The Kunitz domains 1 and 2 serve as protease inhibitor domains. The precursor is proteolytically processed into separately functioning proteins. 3-hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with Cys-53, Lys-111, Lys-137, and Lys-149 to form heterogeneous polycyclic chromophores including hydroxanthommatin. The reaction by alpha-1-microglobulin is autocatalytic; the human protein forms chromophore even when expressed in insect and bacterial cells. The chromophore can react with accessible cysteines forming non-reducible thioether cross-links with other molecules of alpha-1-microglobulin or with other proteins such as Ig alpha-1 chain C region 'Cys-352'. Heavy chains are interlinked with bikunin via a chondroitin 4-sulfate bridge to the C-terminal aspartate. Proteolytically cleaved by PRSS3 at Kunitz domain 2. In the N-terminal section; belongs to the calycin superfamily. Lipocalin family.
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O81338
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MAKVSSSLLKFAIVLILVLSMSAIISAKCIKNGKGCREDQGPPFCCSGFCYRQVGWARGYCKNR
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Possesses antifungal and antibacterial activity. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. Belongs to the AMP family.
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P25403
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LPVAFLKFAIVLILFIAMSAMIEAQCIGNGGRCNENVGPPYCCSGFCLRQPGQGYGYCKNR
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Possesses antifungal activity and is also active on two tested Gram-positive bacteria but is non-toxic for Gram-negative bacteria and cultured human cells. Homodimer. Found only in seeds. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. Three disulfide bonds are present. Belongs to the AMP family.
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B3EWQ6
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YSKSLPLSVLNP
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Has bactericidal activity against E.coli ATCC 29522 and S.aureus. Inhibits growth of S.marcescens and B.cereus ATCC 14579. A synthetic peptide has antibacterial activity against E.coli ATCC 29522 (MIC=8 ug/ml), S.aureus (MIC=64 ug/ml), S.marcescens (MIC=32 ug/ml), B.cereus ATCC 14579 (MIC=64 ug/ml), B.subtilis (MIC=32 ug/ml), L.plantarum ATCC 8014 (MIC=32 ug/ml), B.flexus (MIC=32 ug/ml), S.enteritidis ATCC 13076 (MIC=4 ug/ml), Enterobacter spp (MIC=32 ug/ml), B.anthracis (MIC=128 ug/ml), B.licheniformis (MIC>128 ug/ml) and L.lactis ATCC 11454 (MIC>128 ug/ml). Active between pH 2 and 12. Active between 37 and 90 degrees Celsius. Activity is reduced at 100 degrees Celsius and absent at 110 degrees Celsius. Activity is unaffected by storage at -20 degrees Celsius. A synthetic peptide has no antibacterial activity against S.agalactiae ATCC 12386, S.epidermidis, P.aeruginosa and methicillin-resistant S.aureus (MRSA).
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A0A2I8B346
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MGPMKVLLVLLVVMVAAPHIADAWQQPSCSSICDYSCGKSACISYSGRCGCCASCRRGPIYG
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Has weak antibacterial activity, mainly against marine Gram-positive bacteria like C.maltaromaticum (MIC=200 uM), C.mobile (MIC=100 uM), C.divergens (MIC=200 uM) and C.funditum (MIC=200 uM) but also against C.glutamicum (MIC=50 uM). Has very little or no activity against Gram-negative bacteria. The amidated form is probably the active form. Amidated. Not amidated. Belongs to the paralithocin family.
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Q2M5E6
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METKRLAYVMFVLVCLFLAMAQPSQASYFSAWAGPGCNNHNARYSKCGCSNIGHNVHGGYEFVYQGQTAAAYNTDNCKGVAQTRFSSSVNQACSNFGWKSVFIQC
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Antimicrobial peptide. Detected at higher levels in needles and twigs from canker-resistant seedlings than in needles from canker-susceptible plants. During summer, detected on cankered, healthy and marginal bark. During winter, detected at lower levels in cankered bark and bark from the canker margin than in healthy bark (at protein level). In summer, present at higher levels in older needles and twigs than in tissues from the current year. In winter, detected at high levels in both older and current-year needles and twigs. By wounding and by methyl jasmonate.
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P84524
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LRPAVIVRTKAL
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Has antimicrobial activity against the Gram-positive bacterium M.luteus. Expressed by the skin glands.
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O96935
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MKLTKGCAYKYIIFTVLILANILYDNKKRCMIKKNLRISSCGIISRLLKSNSNYNSFNKNYNFTSAISELQFSNFWNLDILQKDIFSNIHNNKNKPQSYIIHKRLMSEKGDNNNNNHQNNNGNDNKKRLGSVVNNEENTCSDKRMKPFEEGHGITQVDKMNNNSDHLQQNGVMNLNSNNVENNNNNNSVVVKKNEPKIHYRKDYKPSGFIINNVTLNINIHDNETIVRSVLDMDISKHNVGEDLVFDGVGLKINEISINNKKLVEGEEYTYDNEFLTIFSKFVPKSKFAFSSEVIIHPETNYALTGLYKSKNIIVSQCEATGFRRITFFIDRPDMMAKYDVTVTADKEKYPVLLSNGDKVNEFEIPGGRHGARFNDPHLKPCYLFAVVAGDLKHLSATYITKYTKKKVELYVFSEEKYVSKLQWALECLKKSMAFDEDYFGLEYDLSRLNLVAVSDFNVGAMENKGLNIFNANSLLASKKNSIDFSYARILTVVGHEYFHNYTGNRVTLRDWFQLTLKEGLTVHRENLFSEEMTKTVTTRLSHVDLLRSVQFLEDSSPLSHPIRPESYVSMENFYTTTVYDKGSEVMRMYLTILGEEYYKKGFDIYIKKNDGNTATCEDFNYAMEQAYKMKKADNSANLNQYLLWFSQSGTPHVSFKYNYDAEKKQYSIHVNQYTKPDENQKEKKPLFIPISVGLINPENGKEMISQTTLELTKESDTFVFNNIAVKPIPSLFRGFSAPVYIEDNLTDEERILLLKYDSDAFVRYNSCTNIYMKQILMNYNEFLKAKNEKLESFNLTPVNAQFIDAIKYLLEDPHADAGFKSYIVSLPQDRYIINFVSNLDTDVLADTKEYIYKQIGDKLNDVYYKMFKSLEAKADDLTYFNDESHVDFDQMNMRTLRNTLLSLLSKAQYPNILNEIIEHSKSPYPSNWLTSLSVSAYFDKYFELYDKTYKLSKDDELLLQEWLKTVSRSDRKDIYEILKKLENEVLKDSKNPNDIRAVYLPFTNNLRRFHDISGKGYKLIAEVITKTDKFNPMVATQLCEPFKLWNKLDTKRQELMLNEMNTMLQEPNISNNLKEYLLRLTNKL
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Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC. Binds 1 zinc ion per subunit. Inhibited by 1,10-phenanthroline, EDTA and bestatin. Activity is not affected by phosphoramidin, PMSF, leupeptin, iodoacetamide or pepstatin. Optimum pH is 7.4. Active from pH 5.8 to 8.6, with less than 20% of normal activity at pH 6.0. Expressed in all erythrocytic stages. The 120 kDa precursor is cleaved in vitro into 96 kDa and 68 kDa forms. Belongs to the peptidase M1 family.
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P0CH48
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FLPKMSTKLRVPYRRGTKDYH
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Antimicrobial peptide against both Gram-positive, -negative and yeast. Also induces histamine release by mast cells and shows moderate hemolytic activities against both human and rabbit red cells. Expressed by the venom gland. Minimum inhibitory concentrations (MIC) are the following: E.coli standard strain (MIC=12.5 ug/ml), E.coli drug-resistant strain (MIC=15 ug/ml), S.aureus standard strain (MIC=1.2 ug/ml), S.aureus drug-resistant strain (MIC=5.0 ug/ml), B.dysenteriae standard and drug-resistant strains (MIC=7.5 ug/ml) and C.albicans (MIC=15 ug/ml).
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A1YV58
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MRSSLLLGLTVVLLLGVTVPPCMAGQALNKLMPKIVSAIIYMIGQPNAGVTFLGHQCLVESTRQPDGFYTAKMWCTSWTSDNPIVGEGRSRVELEALKGSIRNFVQTASDYKKFTIEEVEDWIASY
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Has antibacterial activity against the Gram-positive bacteria E.coli (MIC<50 ug/ml) and P.aeruginosa (MIC<25 ug/ml), and the Gram-negative bacteria S.aureus (MIC<100 ug/ml) and S.pyogenes (MIC<50 ug/ml). Strongly expressed in gills, hemocytes and reproductive tract, with weaker expression in muscle, heart and digestive tract. Not detected in eyes and hepatopancreas (at protein level).
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E1UYT9
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MLNMKSFALVMLFATLVGVTIASGPNGQCGPGWGGCRGGLCCSQYGYCGSGPKYCAHNTPLSEIEPTDAGRCSGRGTCSGGRCCSKYGYCGTGPAYCGLGMCQGSCLPDMPNHPAQIQARTEAAQAEAQAEAYNQANEAAQVEAYYQATQAQTQAQPQVEPAVTKAP
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Antimicrobial peptide active against the fungus A.alternata (IC(50)=8.6 uM) and the oomycetes P.infestans OSV 12 (IC(50)=11 uM) and P.infestans PRILL 2 (IC(50)=6.5 uM). Expressed in roots, flowers and, to a lesser extent, in stem and leaves. Strongly induced (up to 70-fold) by infection with phytopathogenic fungi like R.solanum, F.culmorum and B.cinerea. Antimicrobial peptide 1.1a. Antimicrobial peptide 1.2a.
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B3EWQ1
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VAKCTEESGGKYFVFCCYKPTRICYMNEQKCESTCIGK
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Antimicrobial peptide. Active against fungal species B.cinerea (IC(50)=5.8 uM) and A.niger (IC(50)=5.6 uM) but not against F.oxysporum, F.graminearum, B.sorokinina and P.debaryanum at concentrations below 10 uM. Active against bacterial species P.syringae, B.subtilis and X.campestris. Expressed in flowers but not in leaves, seeds or roots (at protein level). Disulfide bonds.
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P0CF39
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KDGYIIEHRGCKYSCFFGTNSWCNTECTLKKGSSGYCAWPACWCYGLPDNVKIFDSNNLKC
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Shows antibacterial activity against both Gram-positive bacteria (B.subtilis, M.luteus, E.faecalis) and Gram-negative bacteria (P.aeruginosa, Y.enterocolitica, A.calcoaceticus) (PubMed:19540868). Modifies membrane sodium permeability on Y.enterocolitica (PubMed:19540868). Is toxic to cockroaches and crabs, but is not toxic to mice. Does not induce haemolysis in human erythrocytes (PubMed:19540868). Acts by inhibiting the sodium (Nav) currents (By similarity). Expressed by the venom gland. Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta). Monoisotopic. Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily.
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B3A0L3
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EGPVGLADPDGPASAPLGAP
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The synthetic peptide inhibits growth of fungus P.capsici and partially that of V.dahliae, F.graminearum and F.omysporum.
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Q9SPL5
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MAINTSNLCSLLFLLSLFLLSTTVSLAESEFDRQEYEECKRQCMQLETSGQMRRCVSQCDKRFEEDIDWSKYDNQEDPQTECQQCQRRCRQQESGPRQQQYCQRRCKEICEEEEEYNRQRDPQQQYEQCQKHCQRRETEPRHMQTCQQRCERRYEKEKRKQQKRYEEQQREDEEKYEERMKEEDNKRDPQQREYEDCRRRCEQQEPRQQHQCQLRCREQQRQHGRGGDMMNPQRGGSGRYEEGEEEQSDNPYYFDERSLSTRFRTEEGHISVLENFYGRSKLLRALKNYRLVLLEANPNAFVLPTHLDADAILLVIGGRGALKMIHHDNRESYNLECGDVIRIPAGTTFYLINRDNNERLHIAKFLQTISTPGQYKEFFPAGGQNPEPYLSTFSKEILEAALNTQTEKLRGVFGQQREGVIIRASQEQIRELTRDDSESRHWHIRRGGESSRGPYNLFNKRPLYSNKYGQAYEVKPEDYRQLQDMDLSVFIANVTQGSMMGPFFNTRSTKVVVVASGEADVEMACPHLSGRHGGRGGGKRHEEEEDVHYEQVRARLSKREAIVVLAGHPVVFVSSGNENLLLFAFGINAQNNHENFLAGRERNVLQQIEPQAMELAFAAPRKEVEESFNSQDQSIFFPGPRQHQQQSPRSTKQQQPLVSILDFVGF
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Antimicrobial peptides 2b, 2c and 2d have antibacterial and antifungal activity against a range of species. Belongs to the 7S seed storage protein family.
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Q9SPL4
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MAINTSNLCSLLFLLSLFLLSTTVSLAESEFDRQEYEECKRQCMQLETSGQMRRCVSQCDKRFEEDIDWSKYDNQDDPQTDCQQCQRRCRQQESGPRQQQYCQRRCKEICEEEEEYNRQRDPQQQYEQCQERCQRHETEPRHMQTCQQRCERRYEKEKRKQQKRYEEQQREDEEKYEERMKEEDNKRDPQQREYEDCRRRCEQQEPRQQYQCQRRCREQQRQHGRGGDLINPQRGGSGRYEEGEEKQSDNPYYFDERSLSTRFRTEEGHISVLENFYGRSKLLRALKNYRLVLLEANPNAFVLPTHLDADAILLVTGGRGALKMIHRDNRESYNLECGDVIRIPAGTTFYLINRDNNERLHIAKFLQTISTPGQYKEFFPAGGQNPEPYLSTFSKEILEAALNTQAERLRGVLGQQREGVIISASQEQIRELTRDDSESRRWHIRRGGESSRGPYNLFNKRPLYSNKYGQAYEVKPEDYRQLQDMDVSVFIANITQGSMMGPFFNTRSTKVVVVASGEADVEMACPHLSGRHGGRRGGKRHEEEEDVHYEQVKARLSKREAIVVPVGHPVVFVSSGNENLLLFAFGINAQNNHENFLAGRERNVLQQIEPQAMELAFAAPRKEVEELFNSQDESIFFPGPRQHQQQSSRSTKQQQPLVSILDFVGF
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Antimicrobial peptides 2b, 2c and 2d have antibacterial and antifungal activity against a range of species. Belongs to the 7S seed storage protein family.
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Q9SPL3
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QCMQLETSGQMRRCVSQCDKRFEEDIDWSKYDNQEDPQTECQQCQRRCRQQESDPRQQQYCQRRCKEICEEEEEYNRQRDPQQQYEQCQKRCQRRETEPRHMQICQQRCERRYEKEKRKQQKRYEEQQREDEEKYEERMKEGDNKRDPQQREYEDCRRHCEQQEPRLQYQCQRRCQEQQRQHGRGGDLMNPQRGGSGRYEEGEEKQSDNPYYFDERSLSTRFRTEEGHISVLENFYGRSKLLRALKNYRLVLLEANPNAFVLPTHLDADAILLVIGGRGALKMIHRDNRESYNLECGDVIRIPAGTTFYLINRDNNERLHIAKFLQTISTPGQYKEFFPAGGQNPEPYLSTFSKEILEAALNTQTERLRGVLGQQREGVIIRASQEQIRELTRDDSESRRWHIRRGGESSRGPYNLFNKRPLYSNKYGQAYEVKPEDYRQLQDMDVSVFIANITQGSMMGPFFNTRSTKVVVVASGEADVEMACPHLSGRHGGRGGGKRHEEEEEVHYEQVRARLSKREAIVVLAGHPVVFVSSGNENLLLFAFGINAQNNHENFLAGRERNVLQQIEPQAMELAFAASRKEVEELFNSQDESIFFPGPRQHQQQSPRSTKQQQPLVSILDFVGF
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Antimicrobial peptides 2b, 2c and 2d have antibacterial and antifungal activity against a range of species. Belongs to the 7S seed storage protein family.
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Q22531
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MRRKLLLLLCFIGLFSLISTAPAPNNVGLESEFTEGHAETINLEEVEFNHPSILPEHPDNFRQDKLAARKRQSLYVTKTRLPPNLYAIDYSLWFQPYFPSPGVQYAPEKNFTFDGRASIQVEALVASDRFILNAYNFKIQSYKVVDIDGTVVPINSISQDDTTQQLSLITNANGVVAGQIYNIEFVYTGIINPYTDGGVYYTSYNDPQGNTHYMIATHMEPFSARKVFPSLDEPSYKAKFTITVQYPASQVALSNMMETEPTKIDNIWSTITFPQTPKMSSYLIAFAVGPYVNSQYVNKHNTLTRAWGWPGTEQYLQFAAQNAGECLYQLGEYTGIKFPLSKADQLGMPEFLAGAMENWGLIIYKYQYIAYNPTTMTTRNMEAAAKVMCHELAHQWFGDLVTTAWWDDLFLNEGFADYFMTFIQKSVYPQQATYLDTLQVLDELQVGLTADVRYDAHPLVYPDGPAFDDITYNKGASMLRMLSDVLGADVFKQGIRAYLQKMQYSNANDFDLFSTLTDTAKSNNILDWCGLPLNVTDFMQPYIHQTNHPLIRYNNNQKIGGSTFSQEPFLDISDLTATPWNYTWSIPLTSANLRHADPYKQWLPRQQGCANMNENIQEERIKEPNKRAVQWELTSITSATYGRIIYDDIGFDRILKLIKQDDINDNLKLTLLADEYNYMLREKKANRPFGYNRFLDLAKVIFNTQSFTNYPSYGVFAQAQPVLEQIAQLYRDGIDAEFVPRLYKLFFQNSYNQLKWQDTSIWDTDTFSEVFLPFAVRYDIGDVQNRTLNMFANVKSACINSLNGTAWCNPYSTNLRKAIYCGAAKYAPATSDYFFQMLHSYNKEVITNPYFYQEYMALLEGMSCTQSPATLKVLIRLFTTSTLNPSTIFGFLKYNPAASDVLYNYFMANPQLVNSTMLDAYLDAMTYNWNSYFREGQLSTLMNTLTLTNDQFDIFDFYINRVSLMFEYKSTYALPTYNWLYDNLVVIGKTPWEKTPNIDAVFPYYKLDLQVNIPGSGPYQWYENMTFSATSTVTFQLVSPTSSITINAHRLMFDPVSIRLYNENDENAHTPIPIDFSKVMKDYDKGTVTIPTMNNTVLYPNQYSLFIEYTGFIFQNPDEGDASNTYLGGLNNRKGWIFTTDFEGGPGARSLLPCWDEPSYKGQFEVSVFHPTDMIALSNEVDIQRTIYDNGWTTTKFATTNQMSTYLLALCVGHFSNLATVTRTGVLTRVWTWSGMEQYGEFALNVTAGTIDFMENYFSYDFPLKKLDVMALPEYTMNAGAMENWGLIIGEYSLFMFDPDYATTRDITEVAETTAHEVVHQWFGDIVTLDWWNDIFLNEGFAQYWFANGIDNTFPEQHAYSIDYNRFYMNHIALKYDCIPGVAKPVISDTPPVFGIEPYYKGSALLNLLNNVLTPAVFQEGLSSYLTQYGYVNASPRNLWTSLTVAAQRHNITDWNGQPLDVSSFMDPYTLQTSYPIITLTLRGTSTVQANQQSCMSDETLWNVPLFTQTPGALDFNWFVNFTGGNDATWLRPLPTGYRVDNAGSTSFARINYDDKSWYSIQAQLLSNMNTMSSTTRAMLLDDANFFYQSGRWEMTKFLDLTLYLVNEDSLAPWEQAIEFFTEMLNRFQYQPEIDTVRNYVIQITKNAVSKFQWNTNGLWANDRIVQLLVNVNNLAVNRQSRQVALTLFNNFVLKCKYSLSGTGKCSGIHPNLRQPTYCYGLRQSNNIDDFTTVNNLYSWFVQNAGYLQTDGSNLLNALGCVQNLDLQKTMLRSILSGDYPPSLLNSIAVHDDSSDVLYNFLLDNTQDILNAPFDFSLYVKAMFQNWSTSNQLELAKDFQNSSNYNLLNAAQKNIYKQGILTVNSNANWMLIYKTPFLEWIQKNFGAPNL
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Putative aminopeptidase which plays a role in oocyte maturation. Binds 1 zinc ion per subunit. RNAi-mediated knockdown causes an expansion of the pachytene zone in the gonads of 31 percent of animals and a delay in oocyte nucleolus disassembly. Brood size is normal and embryos are viable. Belongs to the peptidase M1 family.
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B3EWI6
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DLPECCSATELELDSGKQTS
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May have antimicrobial activity.
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P86706
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TESYFVFSVGM
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Has antimicrobial activity against Gram-positive bacteria B.subtilis (MIC=150 ug/ml) and S.aureus (MIC=170 ug/ml), and against Gram-negative bacteria E.coli (MIC=170 ug/ml) and P.aeruginosa (MIC=169 ug/ml). Monomer. Found in the liquid endosperm contained in green fruit of coconut palms, also known as coconut water (at protein level).
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Q72F03
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MDIRFQAGGHAAWRAGAVMVFVFKDEPLAEVDSQLVEAAPWLTIAPAGNDFRAAKDEVAVLHGPPAFDIPRVVAVGLGKREDCTLERIRLAAAAGIRRCRDLRVENVGVVAAQLGRMAPTEHDALRVAEEVVCGALLGLYRYDRFRTVKDDERAEDPRWLALLCEGKNVPDDLHGAARKGEAVALGMGVARDLVNGPANIVTPAFLASEAEALGRKHGFRVEVLGRDELSSMGMGAFASVFRGAEEEARLIVIEHAPAGTEEQQPLVFVGKGVTFDTGGISLKPAAKMHEMKGDMAGAAAILGLFAALGERDLPRRVVGVLPCTENMPDGRATRPGDVVTTLSGKTVEILNTDAEGRLLLCDALTYAQRRWQPEALVDLATLTGACVVALGTEVAGLFCDDAALADAIASRGETVGDLFWPLPLWKSYAENLKSDVADLANVGPREGGAVNAALFLRQFIDDGVRWAHLDIAGPAFTAKKSALCPGGGTGFAVRTLFELVSEGIPAA
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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A8LI79
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MTELAAVSFVYPDLDALAAETAKIAVLVPAEGTLNPGARRLNRLTKGAVARAVESAAFEKLKSGESLSLGYPAGMASDEVILVKLARNAKPLEARKAGAGLGKTLGKEGLLIWAAGLGQVAELAFGAALRAYRFDARKSKSEDALGPITVCATKRDEAEAAFADRRAVAEGVFFTRDLVNEPANVLTTTEFADRLTAMADLGLEVSVLEEADMEKLGMGALLGVGQGSESPSKIVVMKWMGGGDGAPFALVGKGVVFDTGGISIKPSAGMEDMTMDMGGAGVVAGVMRTLALRKAKANVVGLVGLVENMPDGKAQRPGDVVTSMKGDTIEVINTDAEGRLVLADVMWYAQEEFKPCAMIDLATLTGAIIIGLGHENAGVFSNSDDLSGAFLKAATAEGEGAWRMPMGPAYDKLIKSRVADIKNVGGRAAGSITAAQFLGRFVKDETPWCHLDIAGTASVSSATDYAPAGATGWGVRALDRLIRDGYEG
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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A7ZVE0
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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B7UQR7
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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B7MLR5
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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B7LCX0
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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P11648
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Required for plasmid ColE1 site-specific recombination but not in its aminopeptidase activity. Could act as a structural component of the putative nucleoprotein complex in which the Xer recombination reaction takes place (By similarity). Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Inhibited by zinc and EDTA. Homohexamer. Belongs to the peptidase M17 family.
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B5Z3L7
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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B7NUH4
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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B7MSZ3
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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B7M9L9
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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C4ZRD1
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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B1XEN9
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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A8A816
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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A1AJG3
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q0T9D1
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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B1ISB1
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q2M649
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Probably involved in the processing and regular turnover of intracellular proteins (PubMed:20067529). Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Required for plasmid ColE1 site-specific recombination but not in its aminopeptidase activity. Could act as a structural component of the putative nucleoprotein complex in which the Xer recombination reaction takes place (PubMed:8057849). Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Inhibited by zinc and EDTA. Homohexamer. A quadruple peptidase disruption (pepA, pepB, pepD and pepN) does not grow in M9 minimal medium, grows better when supplemented with casamino acids (PubMed:20067529). Belongs to the peptidase M17 family. The ligation for manganese is based on the ligation for zinc, an inhibitor, in the crystallographic structure reported in PubMed:10449417. The ligation for manganese in the active form of the enzyme may differ.
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B7NGJ2
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MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q67NI4
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MKVEVTSQALTEVAVDVLILPLTEGTPAPADVNEALGGLCAQVVGADFKGEMGQTTLLYTGGRLPARKVLLLGLGKAEKVTNRSLRRAAGIGARAARKSGARSIAFALPGAVEMDEAAAARFITEGALHGLFRLPDWKSEKKPRPEVEAVHILGGERAREGAEHGRIVAEGVNLARALAWTPGNHLTAAKLAERAAEMCRENGIEVEVYDKKGCEELGLGLLLAVNQGSREEPRFIVMRYKGNGGQGPWLGLVGKGLTFDSGGISIKPTEGMWNMKMDMGGAAAVIGAMQAIARLKVKADVMAVIPSTDNMPDGGSYKPGDVVSGLSGKTVEIRSTDAEGRLILADGLAYAAKQGCRKIITASTLTGACNIALGPIRYALVANDDAWEEEVYRAGEAAGERGWKLPHDEEYYDLIKSSVADMINGTKNRAAGTVAGGLFLMKHVGDTPCVHLDIAAVAWKSGSDEYEDEGATGVGTRTFVEAARRFAEGLR
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q3A831
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MQIVVGCMPALTLKTDCLMLGVWQDRTDTPLLKELDTALHGALGQSVDSKAFVGKEGETLLFQTGAGLPAARVLLIGLGAYAQADCGAMRRGAAEGARVLQQQRVKRAGLALSEAPAGLPLTQAVQVLVEGLLLASYRFDRFLTQKREDLPPLLETLDILIADQGSLEGVAAAVERARHIGHGVALARDLVNQPGNVKSPEFLAERARQLAGECGLSCTVLEQEQLEREGFGALLAVAQGSARPPRLIVLEYRGGAPDEKPLALVGKGVVFDSGGISLKPGEKMDEMKMDMAGAAAVFGAMSAAAGLRLPVNLVAIVPAVENLPSASAYRPGDIITSLSGRTIEVLNTDAEGRLILADALTYAGRFEPRAVIDLATLTGACIIALGHEASAVFSNRDELARNLIRAGETSRERLWQLPLWDSYDKQIKSEIADMKNTGGRPAGTITAAAFLQRFVPDCPWAHIDIAGTAWEAKGTALCPRGGTGVGVRLLIDLLEQE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q8KPQ6
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MTFQAIATHPQDWTGDTLALGLTTAAIGETLSSELQKLDQQWNGVLQELISDSEFKAKLAETTTTRIGGSIRKLILVGLGESPTTEDYRRAAAAVAKQARSFKSQTLAIAFPPSDDPAAIASAIVEGISLALYKDQRFKSEPDTASGPSSIELLGLAGQEAAIARAEQVVAGVELARQLVAAPANVVTPVTMADTAQELAAELGLELEILEADECEKRGMGAFLGVAKASDLPPKFIHLTYRPESTPRRKLAIVGKGLTFDSGGYNIKGAGSGIEMMKTDMGGAAATLGAAKAIGLIKPDVEVHFISAVTENMISGRGMHPGDILTASNGKTIEVNNTDAEGRLTLADALVFADGLGVDAIVDLATLTGACIIALGDDIAGLWSPSDDLAEQLLQAGKAAGEKLWRLPLEEPYLDGLKSPVADYKNTGPRAGGSITAALFLKQFVKHPVWAHLDVAGPVWSDKEKHYNPAGATGYGVRTLVNWVLS
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity). Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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A0LK12
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MEIDWQIGPASEWRADALIFFGLEEATEPLPGFKRWLDQHGQWLSASPVLRDFQGKYQEVAVCYGPPEANIPRVVMAGLGTREKFDMERLQGSAAAALNRCRELRLARPAFCLRSFYGLPLMVDSALKEALIGGLTGLHRYEELKTRDIAPSAAPSRLVVLNEYETTPELRALPGAAAAAAAGIILARDLVSSPANRATPAFLADCARRLADRDGCRIEVIGLEKAESMGMGGFAAVARGSRQPACMIVLERFPEADRRESPIVFVGKGITFDTGGISLKPRDHLEEMKQDMAGAAAVLGAFETLGRLGSDRHVVGIMPCTENMPGGNAYKPGDVIRTMSGLTVEVISTDAEGRMVLCDALTYAMRYKPAAVFDIATLTAAVIIALGQRVAAVMANRDILAEAVVDIGAQVGERLWPLPLYDLYFDYLKSDVADFKNVGDRTAGSIVGGMFLKQFVPDTTPWAHLDIAGTAWTDKDLGTTPRGGTGFGVRTLTELALQWPDLGIR
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q2JRU4
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MQLRLGEPPLTQAECALVYCFAPSGENATFSLPAEIASLDEKVWSGLVAEAAQEQKFQGKPNSSLALRLPGPIRKLVLVGLGDPAALTLEALRRATANGLRQAHSLKAKQVVLSLPDTGLDQVRAVQAVAEASLLVAHQDNRFKSPPKPEEERGFSVEEVTLLVPGLAQARQDYENALQRATEMAAGTILARELVAAPANVVTPPALAETARQLAQDYGLEVEILGREECQALGMGAFLGVAQASDLPPQFIHLTYKPKEGDPVAKLALVGKGLTFDSGGLNIKTDSRSIAMMKTDMGGAAAVLGAARALAALKPQVEVHFIVAATENMISGRALHPGDILTASNGKTIEVNNTDAEGRLTLADALVFAEKLGVDAIVDLATLTGACVIALGEEIAGLFTPDEKLAQELQQAANLSGEKIWRLPLEESYFEGLSSTVADMKNTGPRSGGSITAALFLKQFVEKTPWAHLDIAGPVWAEKDSGYTNKGATGYGVRTLVEWVLAREMAAASS
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q2JKL5
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MQLHLSEPPLTQGECALVYCFAASGGNGRFPLPPEIASWDEKAWSGLVAETVQEQGFQGKPNSSVALRLTGEIRKLVLVGLGDPAALTLEALRRATANGLRQAHSLKAKQVMLSLPETGLDRVRGVQAVAEACLLVAHRDNRFKSSAKGEEENSFSVQEVTLLVPGLAQARPDYEVALQRAIEMAAGTILARELVAAPANIVTPLALADTARQLAQEYGLEVEILGQEECEALGMGAFLGVAKASDLPPQFIHLTYKPAQGDPVTKLALVGKGLTFDSGGLNIKTDSRSIAMMKTDMGGAAAVLGAARALAALKPQVELHFIVAATENMISGHAIHPGDILTASNQKTIEVNNTDAEGRLTLADALVFAEKLGVDAILDLATLTGACVIALGEEIAGLFTPDETLAQELQQAANLSGEKIWRLPLEEGYFEGLSSIVADMKNTGPRSGGSITAALFLKQFVEKTPWAHLDIAGPVWTEKDAGYNNKGATGYGVRTLVEWVLARQAAAACS
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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B1XK83
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MEIRGSSQTAAAWAGEAIALGFFESETVLTVPENLTALDERLSGVIAEVIAETEFKGKSGKLSVTRLGSGAPIKKLLLVGLGNAEKWNSAVLRSTAAAIARAVKGDKAITTLGLQLPVAETEAITAQMVTEGMYLGFYEDNRFKSEQKDPPALEAVEILGIGDQPAAIALGTSLCEGVIYARELVNAPANIINPVTLAASVESLASTYGLELNILEEADCEAAGMGSFLGVAAASDLPPKFIHLVYKPLGTPRKKVAIVGKGLTFDSGGYNIKPSGPSIAMMKMDMGGAAATFGAAKAIAELKPDVEVHFISAATENMISGRGMRPGDILTASNGKTIEVNNTDAEGRLTLADALVYAEKLGVEAIVDIATLTGACVIALGDDICGLWSDNDDLAQAIATASEKAGEKFWQMPLEEKYFEGLKSPIADMKNTGPREGGSITAALFLKEFVENTPWAHLDIAGPAWSEKDADIYSKGGTGFPVRTLVHWVLS
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q5N569
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MTFQAIATHPQDWTGDTLALGLTTAAIGETLSSELQKLDQQWNGVLQELISDSEFKAKLAETTTTRIGGSIRKLILVGLGESPTTEDYRRAAAAVAKQARSFKSQTLAIAFPPSDDPAAIASAIVEGISLALYKDQRFKSEPDTASGPSSIELLGLAGQEAAIARAEQVVAGVELARQLVAAPANVVTPVTMADTAQELAAELGLELEILEADECEKRGMGAVLGVAKASDLPPKFIHLTYRPESTPRRKLAIVGKGLTFDSGGYNIKGAGSGIEMMKTDMGGAAATLGAAKAIGLIKPDVEVHFISPVTENMISGRGMHPGDILTASNGKTIEVNNTDAEGRLTLADALVFADGLGVDAIVDLATLTGACIIALGDDIAGLWSPSDDLAEQLLQAGKAAGEKLWRLPLEEPYLDGLKSPVADYKNTGPRAGGSITAALFLKQFVKHPVWAHLDVAGPVWSDKEKHYNPAGATGYGVRTLVNWVLS
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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A5GN62
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MKISLSPATPEAWSGSVLALGIPENDPQGLVAAMEQRFSLQLSDWLKQKPFSGKPGDCVSLPLLRSDCTALVLVGLGEASSVDRDRLRLAAAAAARAAQGQGGTLGLLLPWSSDTPEEDAAAAAEAVRLALYSDERFRSKPEPSPKPDQLELLGSLPGGLSHGLEAVHPVCAGVELARELVAAPPNSVTPAELARTASHLAHEHGLELTILERSDCEERGMGSFLSVCQGSDMDPKFIHLTYRPNDAASKRLVLVGKGLTFDSGGYNLKVGAAQIDMMKFDMGGSAAVFGAMRAIAELRPAGVEVHMLVASCENMINGSAVHPGDIVTASNGTTIEINNTDAEGRLTLADALVYACKLKPDAIVDLATLTGACVIALGDEIAGLWSGDDSLSSQLEMAAQAAGEGLWRMPLHSPYRKGLKSLLADMKNTGPRPGGSITAALFLKEFVDAGIPWAHIDIAGTVWSDKGRGLDPSGATGYGVRTLVNWITNQANT
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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A5GV03
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MNFRCSSAPLAELGCDGVALGLFSSSWQQQLAALLPAMAAQLQPLLEQREFKAKGGEKHSFSFPGQQPSLVIISGLGEPDSFDGLALRKAAASLALASRGSNLKALALGLPIEAFAPDQALTALMQGCRLALYKDERFRSENKPSLDPGEIVLQGLASELDQQLAQQEAICQGVMLARELVAAPPNVVNALSLESTARSIADQFGCELTVLDEAACRERGMGAYLAVAQGASIPPRFLHLVIRPQGPVKRKLALVGKGLTFDSGGYNLKVGGSQIELMKFDMGGCGAVLGAARTLAELKLEGLEIHVISAATENMVSAEAIYPGAIVTASNGKTIEINNTDAEGRLTLADALVYACGLEPDAIVDLATLTGACVIALGDEIAGYWSPDDGLAQQLNDAAHRAGEGLWRMPLQSSYKDGLKSGLADMKNTGPRPGGSITAALFLKEFVKPEIPWAHIDIAGPVWSDKGRSTDPSGATGYGVRTLVEWCQAVAADAKEGLSQG
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q0I816
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MQISLSSAQPQAWSGTVLALGIAEGDPNGWIPAMEERFSISLGDWLEQRKFQGKNGESASLQLLNPNCESLVLIGLGPLEALDVNSFRQAGAAAARASKNQTGSIGLLLPWNAVDPAEAVTVAAQAVRLALYSDQRFRSKPEPSIHPERLELLGPLPNTLSSALEAVHPICAGVELARELVAAPPNSVTPSALAESAAQMAHEHGLDLKVLERSDCEARGMGSFLSVCQGSDMDPKFIHLTYRPSGPATKRVVLVGKGLTFDSGGYNLKVGAAQIDMMKFDMGGSAAVLGAMRSIAELRPQGVEVHMLVASCENMINGSAVHPGDIVTASNGTTIEINNTDAEGRLTLADALVYASELEPDAIVDLATLTGACVIALGDEIAGLWTGDDSLANSLEGAAKDAGEGLWRMPMHQAYRKGLKSLLADLKNTGPRPGGSITAALFLKEFVRSSIPWAHIDIAGTVWSDKGRGMDPAGATGYGVRTLVSWVCAQTQQAEN
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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