UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
|---|---|---|
Q7RVH5
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MALKKMPPKKPYHQKASKTKACYNCHRKRLRCDKSLPACLKCSINGEECLGYGIVLRWAACNSPTSTITTRTTNKTNFNGTNTTTPRTVKSSTPTQAPTPSDSPRQLDTDVTSSSAPSHTCSRSTTTSTTTTRISSPTLEETIDSFTVETPIDNNVDPLPRAPDDNPDPSSQIIKRPVNLIKIPLTDPLLNGLSTKARWYMHHFATIVCRDLVSIDQKERNPFRAIIPLVRKFDYLQSVVLATAAMHLSTIHKYQGRSLPSESALVDALMLKSRALHLLRAAINDNTLTDKAMILSAIVFLVNLDLIDSGRGGWKAHVGAARRLISSLYLTKAHLDGAIAPLVNAIAADCLTYRIYGSTISGNTSSWSDNTIDDGVVLPYILQNAEAYSYHCAPPAILQIILSASQLCSGSSTTLETDGGAGRIVTAAALLHKARNFDVQTWVYNIKGLPPDDDLEARVSVASAHRAAACLFVLLSVPETGLLEIPLLEPKDLVQEILGHLSCIPDNHVHLKGTVWPTFVVGAETDDLSERAWCLERLVAVWTKNPWTYPWGYVHTAMEMLQEIWRLKDLAAQQGDDGINWLQRLKATENSCLIV
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Probable transcriptional regulator. Extended N-terminus.
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Q6TM72
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MIAQQHKDTVAACEAAEAIAIAKDQVWDGEGYTKYTFDDNSVLIQSGTTQYAMDADDADSIKGYADWLDDEARSAEASEIERLLESVEEE
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Allows the phage to evade the CRISPR/Cas system type I-F.
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Q6TM71
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MSTQYTYEQIAEDFRLWGEYMDPNAEMTEEEFQALSTEEKVAMQVEAFGAEA
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Allows the phage to evade the CRISPR/Cas system type I-E (PubMed:24736222, PubMed:26416740). Prevents the DNA-binding activity of the CRISPR-Cas complex.
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A6TP80
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MGNENVVHEGKGIGFFERYLTVWVAACIIVGVAIGQLLPAVPETLSRWEYAQVSIPVAILIWLMIYPMMLKIDFTSIVEATKKPKGIIVTCVTNWLIKPFTMYLIAAFFFKIVFQNLIPESLANDYLAGAVLLGAAPCTAMVFVWSHLTKGDPAYTLVQVAVNNIILLFAFTPIVAILLGITDVIVPYDTLFLSVVLFIVIPLVGGYLSRKYIVQSKGIEYFENVFLKKFDNVTIVGLLLTLIIIFTFQAEVILSNPLHVLLIAVPLTIQTFFIFFLAYGWSKAWKLPHNVASPAGMIGASNFFELAVAVAITLFGLNSGATLATVVGVLVEVPVMLTLVKISNRTRHWFPEVAREN
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Catalyzes arsenite efflux from the cell. Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59) family.
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Q8LA88
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MAKVYWPYFDPEYENLSSRINPPSVSIDNTSCKECTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKVTDSKTIDYIEKVLGPKGHASASQNTWPGKRVGVHSLGDHTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIACVLYVNDNATSRAVDDPERLSSMEEQLNNVLRGCEEQDEKFARTSLSIGSTHVDRRLHQMFFADRDYEAVTKLDDSASCGFEPKITVEHCEEKGYSVINVSCEDRPKLMFDIVCTLTDMQYIVFHATISSSGSHASQEYFIRHKDGCTLDTEGEKERVVKCLEAAIHRRVSEGWSLELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPVDVKTIEALRGEIGHSMMIDFKNKVPSRKWKEEGQAGTGGGWAKTSFFFGNLLEKLLP
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May bind amino acids. Expressed in roots, cotyledons, rosette and cauline leaves, sepals, style, and pedicels and tips of young developing siliques. Down-regulated by abscisic acid (ABA).
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Q93149
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MQKIWLFSIITIFLITELQCYPNSAEERLLSYIFDGYNSLIRPVLNASSPPIEVFFSLAFVLLINVDEKNQIMQTNVWPTMKWNDYQMQWDPREFDGIKTIRVPPDKVWLPDIVLFNNADGNYLVSFYSNVVVEHTGDMLWVPPAVYKSSCLIDVEFFPFDEQVCSLTFGSWTFRKDELQLSYLSGKRHVELNDYLPSGVWDLIDAPGLLIDERSKISYQIKIRRKALFYTVILIMPTVLMAFLSMMVFYLPAESSEKITLAISILLALVVFLLVVSKILPPTSSTIPLMAKYLLMTFIMNMITIMVSVIIINVYFRGPATHIMPNWVKTVFLKFLPVLFVMRRPESTEKELAKMKREKRERRSMKSALKTFFKRNDAKISEQPKQTSRKDGSSSEEKLSSDAKKAIEAIEYITTHLTHDNAFKRQREEWKFVSVVIDRLLLYLFFAVTTGGTVGILLSAPNVFEQVNQTSVIERLKQQAAEEMLNS
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Non-alpha subunit of nicotinic acetylcholine receptor (nAChR) (PubMed:9606719, PubMed:20027209). Probably acts in cholinergic motoneurons to regulate presynaptic neurotransmitter release, thereby ensuring normal level of excitation of cholinergic motoneurons during locomotion (PubMed:20027209). Component of nicotinic acetylcholine receptor. In cholinergic motoneurons, composed of 2 non-alpha subunits acr-2 and acr-3, and 3 alpha subunits unc-38, unc-63 and acr-12. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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Q6M576
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MTNSTQTRAKPARISFLDKYIPLWIILAMAFGLFLGRSVSGLSGFLGAMEVGGISLPIALGLLVMMYPPLAKVRYDKTKQIATDKHLMGVSLILNWVVGPALMFALAWLFLPDQPELRTGLIIVGLARCIAMVLVWSDMSCGDREATAVLVAINSVFQVAMFGALGWFYLQVLPSWLGLPTTTAQFSFWSIVTSVLVFLGIPLLAGVFSRIIGEKIKGREWYEQKFLPAISPFALIGLLYTIVLLFSLQGDQIVSQPWAVVRLAIPLVIYFVGMFFISLIASKLSGMNYAKSASVSFTAAGNNFELAIAVSIGTFGATSAQAMAGTIGPLIEIPVLVGLVYAMLWLGPKLFPNDPTLPSSARSTSQIINS
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Catalyzes the proton motive force-dependent arsenite efflux from the cell. Probably functions as an arsenite/H(+) antiporter. Does not transport antimonite. Inhibited by carbonyl cyanide m-chlorophenylhydrazone (CCCP). Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59) family. Extended N-terminus.
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Q9LX29
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MRMFETRAREWILLVKLVLFTSIWQLASALGSMSSIAISYGEGGSVFCGLKSDGSHLVVCYGSNSAILYGTPGHLQFIGLTGGDGFMCGLLMLSHQPYCWGNSAFIQMGVPQPMTKGAEYLEVSAGDYHLCGLRKPIVGRRKNSNIISSSLVDCWGYNMTRNFVFDKQLHSLSAGSEFNCALSSKDKSVFCWGDENSSQVISLIPKEKKFQKIAAGGYHVCGILDGLESRVLCWGKSLEFEEEVTGTSTEEKILDLPPKEPLLAVVGGKFYACGIKRYDHSAVCWGFFVNRSTPAPTGIGFYDLAAGNYFTCGVLTGTSMSPVCWGLGFPASIPLAVSPGLCIDTPCPPGTHELSNQENSPCKFTGSHICLPCSTSCPPGMYQKSVCTERSDQVCVYNCSSCSSHDCSSNCSSSATSGGKEKGKFWSLQLPIATAEIGFALFLVAVVSITAALYIRYRLRNCRCSENDTRSSKDSAFTKDNGKIRPDLDELQKRRRARVFTYEELEKAADGFKEESIVGKGSFSCVYKGVLRDGTTVAVKRAIMSSDKQKNSNEFRTELDLLSRLNHAHLLSLLGYCEECGERLLVYEFMAHGSLHNHLHGKNKALKEQLDWVKRVTIAVQAARGIEYLHGYACPPVIHRDIKSSNILIDEEHNARVADFGLSLLGPVDSGSPLAELPAGTLGYLDPEYYRLHYLTTKSDVYSFGVLLLEILSGRKAIDMHYEEGNIVEWAVPLIKAGDINALLDPVLKHPSEIEALKRIVSVACKCVRMRGKDRPSMDKVTTALERALAQLMGNPSSEQPILPTEVVLGSSRMHKKSWRIGSKRSGSENTEFRGGSWITFPSVTSSQRRKSSASEGDVAEEEDEGRKQQEALRSLEEEIGPASPGQSLFLHHNF
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Controls formative cell division in meristems, including root tips and lateral root initiation zones of the pericycle, in response to CLE40 signal. Acts with CLE40p peptide as a ligand-receptor pair in a signal transduction pathway, coordinating movement of the root tip and organization of cell divisions in the root meristem. Required during embryogenesis and development, probably for the differentiation of protoderm and epidermal cells. Involved in the regulation of cellular organization during the development of sepal margins and ovule integument outgrowth. Can phosphorylate ALE2. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Homodimer (Probable). Interacts with PP2A3 (PubMed:26792519). Also localized into protein export bodies. Internalization may be involved in degradation of ACR4 for its rapid turn-over. In the epidermis, mostly expressed in the lateral and basal planes of cells. Expressed in seedlings, floral buds, siliques, leaves, shoot apical meristems (SAM), and, to a lower extent, in roots. First observed in all young embryo cells. At the globular stage, restricted to apical region. Later confined to the protoderm area leading to cotyledon primordia and the root apex. In mature embryos, mostly localized in the L1 layer of the SAM, apical regions of cotyledons and the root apex, and, to a lower extent, in protoderm of other regions. In seedlings, expressed in developing tissues of the shoot, including the SAM and epidermis of organs primordia, especially in L1 layer cells. In roots, localized in quiescent center (QC) central cells, columella initials and cells below the QC, the lateral root cap (LRC) and the initial cells destined to give rise to the root epidermal cell file and the LRC. Expressed in epidermal emerged from under the LRC, with levels vanishing in elongation zone. Specifically detected in the small daughter cells after the first asymmetric pericycle cell division during lateral roots emergence. Subsequently, the expression expands to the adjacent small daughter cells from the second asymmetric cell division, resulting in a central core-specific expression pattern. By CLE40 in root quiescent center (QC). Autophosphorylated and phosphorylated by ALE2. Reduced fertility due to abnormal embryogenesis and integument formation. Abnormal seed coat and leaves epidermis, with transient fusion between adjacent developing leaves and reduced hydrophobicity of leaf surfaces. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
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Q9LQB5
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MSFSQDMDNEYEKLIRRMNPPRVVIDNDSCKKATVIRVDSANEYGILLEVVQILTDLNLTITKAYISSDGGWFMDVFNVTDQDGNKVTDEVVLDYIQKSLGPEACFSTSMRSVGVIPSTDSTVIELTGCDRPGLLSELSAVLTHLKCSVLNAEIWTHNTRAAAVMQVTDDLTGCGISDPERLSRIKNLLRNVLKGSNTPREAKTVVSHGEVHTDRRLHQMMFEDRDYEHRLVDDDSSIQDERQRPDVCVDNWLDKDYSVVTVRCKDRPKLLFDTVCTLTDMQYVVFHGSVDTEGTEAFQEYYVRHIDGSPVKSEAEKQRVIQCLEAAIKRRVSEGLKLELCTTDRVGLLSNVTRIFRENSLTVTRAEVKTKGGKALNTFYVSDASGYSIDAKTIDSIRQTIGQTILKVKNNPQEQQQRQKSPSHESPTRFLFGGLFKSKSFVNFGLVRSYS
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May bind amino acids. A number of isoforms are produced. According to EST sequences. Highly expressed in flowers and at lower levels in leaves and siliques. By the cytokinin benzyladenine (BA) and cold stress. Truncated N-terminus.
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Q8LJW2
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MDVCLSYSYNMDDEIAKFIRRVNPPRVVIDNEVCKDVTVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDGGWFMDVFNVTDQDGNKVTDEIVLEYIRKSLGPDESSCFSPSMRSTIGVKQSVDYTVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTDEETCSAITDPERLSKIRKLLGYVLTGGSSGRRFREPKTTVSSALNETHTDRKLHQLMFADRDYDEWENNVDDEDKCGRVIPDVDVSNLHDLDYSIVMIKCKDRPKLLFDTVFTLTDMNYVVSHASIDAEGPQAYQEYYIRHTDGSPVKSEAERQRVIKCLKAAIQRRVSEGLKLELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNTFYVRDASGYQVDTKTIESIRQVIGQTILQVKGGNTDAKPSPQDSPTGFLFGVFKSRSFVNFGLIRS
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May bind amino acids. Expressed in stems and siliques. By dark.
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Q3Y417
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MLPNIILILLIRYCSCGAGSRVYEKYGKQVQLSPATTSSYREWYDSNREHSTRNNTNVDDFQTQLKKSLENTTAAYNATFMQELIEERQRYLEKLNEGQFINDQRRLVEELLDPNYYEKTVHPKRDYTRPTRVNLSMSLYQILDVDEHMQSIEVNVWMVQHWYDEFLDWNPVDYGMINRTIVPYHQIWIPDTYLYNSEELEQKKTESLMNAQLETGHWNQKKDGAKVQLMFPAIYKLSCRMDVRWFPYDRQNCTFIISSWTHDKQTIDYWPLSSTVNLGNMARNDEWEVISFEFVRVEETFKCCTAPWVMLYAHLVIRRKPLYYMINLVVPTSIITIVAVTGFFTPTSSSSERDEKLYLGINTLLTMSVMMLMVCNQMPSTSTYVPLMSWYYIGIIMVIVVGTFLATGVLAIHGQKHYNKPISDRIRKLIYNPVVEFFILSPPTSLIDLWTEFGVISEQRHSTHLDPLLLQHMDPISHTTRADPQHFFGSISSQMCDLQSTYSYTARLATITRQYTQHAKMKALRKNQYRMSMDTSQARGVKKQKMQRRCSLEWEFLANVLDRILLTIFCGFTFAVFIILIGFDSFFTFHTDSPPKTM
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Subunit of nicotinic acetylcholine receptor (nAChR) (PubMed:23351035). Involved in nAChR sensitivity to nicotine (PubMed:23351035). Modulates locomotion towards the drug nicotine (PubMed:23351035). Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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Q9SGI1
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MDDDEYAKLIRRMNPPRVVIDNNASDDATVIQVDSVNKHGTLLEVVQVLTDMNLVIKKAYISSDGGWFMDVFKVIDQDGNKIRDTQVLDYIQKRIESNAGWFIPPLRSSVGVMPTDEYTSIELAGTDRPGLLSEVSAVLTDLHCNVVNAEIWTHNTRAAAVIHVTDNSTHSAITDPIRLSTIKELLCNVVRTNSGSRAAKTVFSCSDTHRERRLHQIMFDDRDYEGVKRARTSASRPSVTLMNIEKDYTVVTMRSKDRPKLVFDVVCTLTDMQYVVFHGMVSTEPVEAYQEFYIRHVDGLPINSEAEQERVIQCLEAAIERRASEGLELELSAEDRVGLLSDITRTFRENSLTIVRAEISTREGKAKDTFYVTDVTGNPVESKIVESIRQQIGVSKLKVKKKEKEHCSVLGTSRPSHETTTMGYLLSNIFKPK
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May bind amino acids.
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Q8LPH4
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MELSDCSNEYEKLVVRMNMPRVVIDNGVCPNSTVVKIDSARSPGILLESVQLLTDMNLWIKKAYISSDGKWNMDVFHVSDLNGDKLTDENLIRYIEKSIETSHYCKTEGYTGLTALELTGTDRVGLLSEVFAVLADLECDVVEAKAWTHNGRIASMIYVKDGNSGTPIDGDSDRVQRVEGQLRNLLKADDGYQNDTRTCVSYGGNTHMERRLHQRMFMDRDYEKKFDIEKSPIVSVQNLPKRGYSVVNLQCKDRMKLLFDVVCTLTDMAYIVFHAAIRTVGETAFLEFYVRHSDGHPVSSEPERQRLIQCLQAAIERRTVKGVRLELCTADRPGLLAEVTRILRENGLNIARAEISTKDSIARNVFYVTDANGNLIDPEIIKSIREKIGIDDLSVKEPFPISCREAVEKEQHIEPQDHQGRYGGGTVLVSLGSLVMRNLYHLGLIKSYF
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May bind amino acids. Expressed in roots, leaves and stems. By cold stress.
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Q9GQV0
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MMVQSIQIVLPVALFFLIVFNGFTVEGSKKEAQLYRDLLTNYSYLVRPVRNPKKALTVTMKVFIQQVLLVDAKHQMIEVNAWLKYIWTDFRLRWNPLDYENITSVRFQGEDQIWQPDILLYNRYIEDEQESFDITYKTNAVAYSDGVINWIPPGIFKLSCKMDITLFPFDEQICFMKFGSWTYHGFALDLRLDVVKGQEPSADLSTYITNGEWHLLSAPARREEKFYKCCKEPYPTVKFYLHLRRRTFYYVFNVVLPTLLVSFMSLLAFCLPATDLSEKIGLQTTILLSVCFFLTILSEMTPTTSEAVPLLGVFFSALTFIVAMSTTFTILVLNIRYRQITNHYLSPMFRSIFLECLPWLMMMKRPDHKFRRGSSYRDSSADQCVQCAKNAELKSILRGTDNQQQIETNTFYPFPTETLSLNRKVGDGLFIQRRCQIHEEARSEKFTHGMLACEKSLRENGSELANILVTILKMYEVMVSQVERIRKRIALKRKRKDIQDEWKFAAQAVDRFCLIIFTIVFIICCFIFVAIPPIKILD
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After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. Forms a homooligomeric channel blocked by alpha-bungarotoxin. The structure is probably pentameric (By similarity). Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
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Q9LNA5
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MAMKGYLDEYEKLVIRMNTPRVVIDNGVCSSATIVKVDSSRRNGILLEAVQILTDLNLSIKKAYISSDGTWNMDVFHVTDLNGNKLNDQSVLRYIEQSIETVYYGENIEVNGLTALELTGTDRIGLLSEMFAVLSDLNCDVVDAKLWTHNGRVASVIYLKDCISGAPILDSHRISKIEGRLKNVLNGDNDVNSAAKTCVTVDSMMHIERRLHQLMFEDRDYERRSKKHERSPMVVVTVQNWAERGYSVVNVHCRDRTKLLFDVVCTLTDMEYAVFHATINTAEDQAHLEFYIRHKDGSPISSEAERQRVIQCLEAAVERRALEGVRLELRHPDKQGLLAEVTRTFRENGLNVTRTEISTSSDMATNIFYVTDANGDEPDFKLIESVREKIGLECLRVKEMPTMYHKKGDGEEQQQTKAVLVSLGSLVWRNLFNFGLIKSCS
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May bind amino acids. Expressed in roots, leaves, flowers and siliques. By abscisic acid (ABA), and cold and salt stresses.
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Q94AW0
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MGILNDDAVLIEPGKISGDPTVVTVNCPDESGLGSTLCRIILEFGLSITRADFSTDGRWCYIVFWVTPDISSPKIDWDSLKNRLLSACPSCLGSFYFCLQSNVSKPPSLYLLKFFCRDRKGLLHDVTKVLTELEFTIQRVKVMTTPDGRVLDMFFITDAMDLLHTKQRQTKTCDHLTAVLGEHGVSCELELAGPELESVQRFSSLPPLAADELFGPDGFDISGSSSNKAVLTVDNQLSPAHTLLQIRCVDQKGLFYDILRTSKDCDVHIAYGRFSSKVKGYRNLELFVRGTDGNKIMDPKHQANFCARLKEEMVCPLRVIIVNRGPDTELLVANPVELSGKGRPRVFYDVTLALKSLGICIFSAEIGRHSTLDRQWEVYRFLLDESREFPLASLRARNQVVDRVTKTLMGW
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May bind amino acids.
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A0A1L9WQM9
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TGTPEPIAIVGMGCRFPGGANTPSKLWDLLCAKRDVQRRIPTDRFHVDAFYDRDGERAGCLNVREAYTLDEDIRQFDAAFFKTNALEAEAMDPQQRLLLETVYEALESAGGVMEDLHGSDTAVYVGVMTGDYHELLLRDPEDMPKYMATGTARSILSNRISYFFDWTGPSMTIDTACSSSLVAVHEAVQALRQGRSTLACAAGANLILGPEMMISESKLHMLSPTGRSRMWDAGADGYARGEGFAAVMLKTLSQAVADGDYVYGVIRETGVNSDGRTNGITLPGADSQTALIRQTYARAGLDIDSQRCQYFEAHGTGTAAGDPIEARAIYNAFFASSSEQAETPLYVGSVKTAVGHLEGTAGLAGLVKAVEAVRRGVIPPNMLFESLNPEIQPFYHRLAVPTDTIPWPEVREGEPRRASVNSFGFGGTNAHAIIESYDNPHRRPSSATSSLYTPLVLSANSESSLRGQVEALHAFLSTTDTPVQHILHTLQTRRSQHPVRATFSAPDRDTLSTALSKAVASDSTLGTRVDKRPAKPRILAVFTGQGAQWPTMGREILRASPLAQRTLSTLQSALDTLPDGPDWLLSTEILADKDTSRLASASVAQPLCTAVQILVVDLLRLAGITPSVVVGHSSGEIAAAYAAGMISAAEAIRIAYYRGVHASLARGQNGQRGGMMAVGMSYDEATEFCEENFAERIEVAASNAPSSVTLSGDEDAIAEAKAILDERGVFARPLRVDTAYHSAHMIPCSEPYLDSLAACEIAPQEAREGCVWVSSVHGARMEGYRVDTLTGEYWNDNMVSPVMFSTAVEMALSEEAACDVAIEIGAHPALKGPFTQTAKQVAAAASSATPLPYSGTLSRGQHDIEALSETLGYLWLHLGAKAVAFPAYTSAFTDALPQWVPDLPRYSWDHRQSFWRESTKSANFRSRLPRHPLLGVRSTEDLDQEMRWAITLRTQELPWLEGHKVEGQVIYPAAAYLVMAMEAAHNLVGEGLSVQMLELFDVEIANAIPLPEDGKGVEVQFTLVPSPGNAKSETKTAQWACYARTAGTGKSSWRSNARGTVRVVLGPAADEDLPPRNPPTGVFHEVKTERFYEALTAIGLHYTGPFRGLDSVHRRSGTAMATATQIPAAELGVPIHPAVLDAAFQTLFAAYCWPEDGSLRAPFVPTGLQSLRIVNRDLVQASAQLTVDAAITHSSGTTIIADLDLYSPAAAGLIQLQGLRCSSLTPPGPRDYKELYTQTAWEVDLSSGLAALSSVSDSDSPSNLALVDLSERLAYYYLRHLNTTIPRSAVPQMEWHHQRIFEWIDHLFPLVTSGKHPTIRPEWSTDTKPHLLALASQYPDSVDLQLIRAVGEHLPAVVRGEAWMLEHMVANDTLDRFYKFGLGFARANGYMGRVAGQIAHRYPRSRILEIGAGTGGATKGILEALDGRFERYTFTDISTGFFEAAATQFERWAGKMSYRALDVEKELSSQGWDGEEAGFDVIVASNVLHATKSLRKTMENVRRLLKPGGFLLLLEVTSEIVRVKLMMAGLPGWWLGGEDGRRYGPTITVEQWDTLLKETGFAGVDHVVNDFVDESKYMTSVMVTQAVDADVRLLREPLSAGWTLPPVTVVGGQKGLAGRVVEALGSAGSVQLVENLEGLFVQPDISVTSLVILEDFDHPVLEDFTPCKLEALQRALPECRQLLWVSGQCREKNPYGNMAIGLCRAIAAEQPHIQFQHLDIEDAVDAGAAKAVTEALVRLVFASQTRLATKNVLWTCEPELVRENGQWLVPRIVPDKRLNDQLNARKMVVQGMATSEEKLELVKQAERYVLSPALPSVVEKDGAVEVKVTHALVNAVQLDQGSVCVVSGNLLSKPDVQVIACTNSVRSVVTVSEEMVFPAENASPPLLQTVAFGLVADEWLHGLSSSDVLVLHQADEQLGRVLRSKAAEAGVKVVDVRTHAYASERSIRAQIPPSTKLLVDFAQSSVQWERILPAQCKIRSYGDAIAPGTSIADTANLNTSQLQRAISWAQQQQPADTALETIPAAELATTPTPSYHAILSFSPSTTIPTITRPVNPALLFRPDRTYLLVGCTGGLGQSLCRWMVLNGARHLALTTRNRTRISTTWLADLAQLGANVQLFEADVADMASLTAIHQTITTGMPPIAGIANAAMVLSDRSFGELKHTDFTTVFGPKVLGTKNLDTLFHSQKLDFFIMFSSLASIVGNRGQSNYVAANLFMSTVAAQRRARGLAASVFHIGMVLGVGYVSTTGVYETTLRQYKYMPIAEPEFWDMFAQAIVIGHPTLAGGHAPEMITGLHRHSLREEVAKAFWAENPRFSLHTLVEESQTVVVDAASAKQVPLAEAVAEAETLEEVDGVIQEAFVVKMERMLQAAKGSIERGQPLINLGVDSLIAVEIRSWFLKELEVDMPVLKLVGGMSVGELCREAASEVL
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Highly reducing polyketide synthase; part of the cluster that mediates the biosynthesis of acurin A, a highly reduced polyketide coupled to a serine via a peptide bond (PubMed:32234543). The activities of the highly reducing polyketide synthase acrA and the nonribosomal peptide synthetase acrB are collectively responsible for the synthesis of the acurin A core structure with a heptaketide backbone produced by acrA covalently fused to a L-serine by acrB (PubMed:32234543). After the formation of the PK-NRP hybrid product, it is detached from acrB by reductive release to set up the formation of the lactam ring by aldol condensation (Probable). The hydrolyase acrC then catalyzes water loss to generate a double bond in the ring (Probable). This double bond is probably reduced, which is followed by three oxidations at C-22 to generate the carboxylic acid moiety, involving probably the FAD-binding monooxygenase acrE and the cytochrome P450 monooxygenases acrD and acrF (Probable). Finally, a last methylation step performed by the O-methyltransferase acrG leads to the production of acurin A (Probable). Secondary metabolite biosynthesis. Expression is positively regulated by the acurin A cluster-specific transcription regulator acrR. Multidomain protein; including a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain that reduces hydroxyl groups to enoyl groups; a methyltransferase (MT) domain responsible for the incorporation of methyl groups; a ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm. Abolishes the production of acurin A.
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P31223
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MNKNRGFTPLAVVLMLSGSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENGKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVTADNNQQAASGAQPEQSKS
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AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together (By similarity). Monomeric in solution. Homotrimeric; interacts independently with AcrB and TolC as well as AcrZ. Part of the AcrA-AcrB-TolC efflux pump (By similarity). Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.
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Q2MBW4
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MNKNRGFTPLAVVLMLSGSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENGKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVTADNNQQAASGAQPEQSKS
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AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm. Monomeric in solution. Homotrimeric; interacts independently with AcrB and TolC as well as AcrZ. Part of the AcrA-AcrB-TolC efflux pump. Complex assembly is independent of an efflux substrate and appears to be constitutive. An unlipidated version of this protein (directed to the periplasm by the OmpA signal sequence) functions normally. Cannot grow on efflux substrates novobiocin or fusidic acid. Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.
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Q7M9Y2
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MTQTHSTELFKPNRAFAKTARIKNLCEYEDLRLDAEEDFEGFWGKLAKEKIDWMEPFSKVLDESEAPFYKWFVGGKLNVCAQCLDRHLDTRKNKAAIIFEGELGDSRIITYRELFYEVKRTANLLKNKFNVKKGDRVVIYMPMIPEAAFMMLACARIGAIHSVVFGGFSAEALRDRIIDAEAKLVITADGAYRRGKPYMLKPVVDDALAEGACPSIEKVLIVIRNKEEINYVPGRDYIYNEMIGLESAHCPPEPMDAEDPLFLLYTSGSTGKPKGVQHNQAGYILWAQTTMEWVFDVKENDTYWCTADVGWITGHTYIVYGPLAMGATTVMYEGVPIYPDTGRWWKMIEHYRVNQFYTAPTAIRLLHKEGKEEPKKYNLSNLKVLGTVGEPINPDAWNWYYNEIGGGQCPIVDTWWQTETGGHMISPLPGATPIKPGCATLPLPGIFAEVIDEEGNPKPAGEQGYLCITKPWPSMIRNIWGDPKRYESSYFSTCKKNGKPVYFAGDGAIRDERGYITITGRMDDVINVSGHRLGTAEIESAIAKHPGVAETAVVSRLDEIKGESVYAFIVLKPGYEDNVAEELQLLKEINAVITREIGPLAKADTMLFVPGLPKTRSGKIMRRILRSIARGEEITQDTSTLEDPAIVQKIQQLA
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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Q8PF09
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MADVYPVDPAFAADARVTREQYAALYRESIQHPEQFWGKAAQRLEWFKQPTQIKDVSYALDDFHIRWFGDGELNASVNCLDRQLATRGDKTALLFEPDSPDAASYPVTYRELYERVCKLGNALRNLGVKKGDRVTIYLPMIVDAAVAMLACARIGAVHSVVFGGFAANSIADRVIDCQSKLIITADEGLRGGKKIPLKANVDAALKIPGTNTVETVLVVRHTGGAVEMQAPRDRWFHDVVDGQPAACEPERMNAEDPLFILYTSGSTGKPKGVLHTTAGYLLFASYTHEVVFDLREDDIYWCTADVGWVTGHSYIVYGPLANGATAVMFEGVPNYPNVSRFWEVIDKHQVTIFYTAPTAIRALMRDGADPVKKTSRKSLRLLGSVGEPINPEAWRWYYEVVGDSRCPIVDTWWQTETGGILISPLAGAVDLKPGSATLPFFGVQPALVDAEGKILEGATEGNLVLLDSWPGQMRSVYGDHQRFIDTYFRTYPGSYFTGDGCRRDADGYYWITGRVDDVINVSGHRIGTAEVESALVSHPKVAEAAVVGFPHDVKGQGIYAYVTLIAGQTPSEDLHKELVSWVRKEIGPIASPDHLQWAPGLPKTRSGKIMRRILRKIAENAPDQLGDTSTLADPSVVDSLVNERLAR
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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Q4UP35
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MADVYPVDPAFAADARITREQYATLYRESIEHPEQFWGKAAQRLDWFKQPTQIKDVSFALDDFHVRWFGDGELNASVNCLDRQLATRGDKTALLFEPDSPDSPSYPVTYRELYERVCKLGNALRNLGVKKGDRVTIYLPMIVDAAVAMLACARIGAVHSVVFGGFAANSIADRVIDCQSKLIITADEGLRGGKKIPLKANVDAALKIPGTNTVETVLVVRHTGGAVDMQAPRDRWFHDVVDGQPAECEPERMNAEDPLFILYTSGSTGKPKGVLHTTAGYLLFASYTHEVVFDLREDDIYWCTADVGWVTGHSYIVYGPLANGATAVMFEGVPNYPNVSRFWEVIDKHQVTIFYTAPTAIRALMREGEAPVKKTSRSSLRLLGSVGEPINPEAWRWYYEVVGDSRCPIVDTWWQTETGGILISPLAGAVDLKPGSATLPFFGVQPALVDAEGKILEGATEGNLVLLDSWPGQMRTVYGDHQRFIDTYFRTYPGSYFTGDGCRRDADGYYWITGRVDDVINVSGHRIGTAEVESALVSHPKVAEAAVVGFPHDVKGQGIYAYVTLIAGETPSEELHKELVSWVRKEIGPIASPDHLQWAPGLPKTRSGKIMRRILRKIAENAPDQLGDTSTLADPSVVDSLVNERLTR
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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Q8P3L1
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MADVYPVDPAFAADARITREQYATLYRESIEHPEQFWGKAAQRLDWFKQPTQIKDVSFALDDFHVRWFGDGELNASVNCLDRQLATRGDKTALLFEPDSPDSPSYPVTYRELYERVCKLGNALRNLGVKKGDRVTIYLPMIVDAAVAMLACARIGAVHSVVFGGFAANSIADRVIDCQSKLIITADEGLRGGKKIPLKANVDAALKIPGTNTVETVLVVRHTGGAVDMQAPRDRWFHDVVDGQPAECEPERMNAEDPLFILYTSGSTGKPKGVLHTTAGYLLFASYTHEVVFDLREDDIYWCTADVGWVTGHSYIVYGPLANGATAVMFEGVPNYPNVSRFWEVIDKHQVTIFYTAPTAIRALMREGEAPVKKTSRSSLRLLGSVGEPINPEAWRWYYEVVGDSRCPIVDTWWQTETGGILISPLAGAVDLKPGSATLPFFGVQPALVDAEGKILEGATEGNLVLLDSWPGQMRTVYGDHQRFIDTYFRTYPGSYFTGDGCRRDADGYYWITGRVDDVINVSGHRIGTAEVESALVSHPKVAEAAVVGFPHDVKGQGIYAYVTLIAGETPSEELHKELVSWVRKEIGPIASPDHLQWAPGLPKTRSGKIMRRILRKIAENAPDQLGDTSTLADPSVVDSLVNERLTR
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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Q2NXE2
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MADVYPVDPAFAADARVTREQYAALYRESIEHPEQFWGKAAQRLEWFKQPTQVKDVSYALDDFHIRWFGDGELNASVNCLDRQLATRGDKTALLFEPDSPDAASYPVTYRQLYERVCKLGNALRNLGVKKGDRVTIYLPMIVDAAVAMLACARIGAVHSVVFGGFAANSIADRVIDCQSKLIITADEGLRGGKKIPLKANVDAALKIPGTNTIETVLVVRHTGGAVEMQAPRDRWFHDVVDGQPAECEPERMNAEDPLFILYTSGSTGKPKGVLHTTAGYLLFASYTHEVVFDLREDDIYWCTADVGWVTGHSYIVYGPLANGATAVMFEGVPNYPNVSRFWEVIDKHQVTIFYTAPTAIRALMRDGAEPVKKTSRKSLRLLGSVGEPINPEAWRWYYDVVGDSRCPIVDTWWQTETGGILISPLAGAVDLKPGSATLPFFGVQPALVDAEGKILEGATEGNLVLLDSWPGQMRSVYGDHQRFIDTYFRTYPGSYFTGDGCRRDADGYYWITGRVDDVINVSGHRIGTAEVESALVSHPKVAEAAVVGFPHDVKGQGIYAYVTLIAGETPSDELHKELVSWVRKEIGPIASPDHLQWAPGLPKTRSGKIMRRILRKIAENAPDQLGDTSTLADPSVVDSLVNERLTR
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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A7IFD4
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MSDKIYYVPSEWAQKAYVDDAHYQSMYAASVNDPHAFWGEHGKRIDWFTPYTKVKNTSFDPGHVSIKWFEDGITNVAYNCVDRHLETRGDQVAIIWEGDSPDESRNITYRELSSEVNKLANVLRNRGVEKGDRVTIYLPMIPEAAFAMLACARLGAIHSIVFGGFSPDSLAGRVADCGSKCIITADEGLRGGRKVPLKANVDAAIAQINGGVDHVIVVRRTGGKVDMLPGRDVYYDEATAMVTDECPAEHVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYASMTHQYIFDYHPGDIYWCTADVGWVTGHSYIVYGPLANGATTLMFEGIPNYPSVSRFWDVIDKHKVNIFYTAPTAIRSLMQAGEEPVKRTSRSSLRLLGSVGEPINPEAWEWYYRVVGEERCPIVDTWWQTETGGILITPLPGATKLKPGSATRPFFGVMPEVVDAEGKVLEGACEGNLVIADSWPGQMRTVYGDHERFEQTYFSTYPGKYFTGDGCRRDADGFYWITGRVDDVINVSGHRMGTAEVESALVAHPKVSEAAVVGFPHDIKGQGIYAYVTLMDGEEPTEELRKELVGWVRREIGPIASPDLIQFAPGLPKTRSGKIMRRILRKIAEDQFESLGDTSTLADPGVVEDLIHNRQNKRDAAA
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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Q9PB89
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MSDLYTIDPMLAKDAHVDRAHYKTLYHESLEQPEAFWSNIAQRLEWFKTPTKIKDVSYQLEDVHIRWFEDGELNASVNCLDRHLTLRGDKTALLFEPDAPDAPSSRITYRELYERVCQLGNALRHLNIEKGDRVTIYLPMIPDAVVAILACARIGAIHSVVFGGFAPNSIADRINDCGSKLIITADEGLRGGRKIPLKANVDAALKIHGTQSVETVLVVRHTGGTINMHTPRDRWFHHVVDIQATECAPERMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYTSYTHETVFDLRENDIYWCTADIGWITGHSYIVYGPLANGATVLLFEGVPHYPTVSRFWEVIDKHHVTLFYTAPTAIRALMREGDTPVKKTSRKSLRLLGSVGEPINPEAWHWYYTIVGNGRCPIVDTWWQTETGGILITPLIGATDLKPGSVTLPFFGIRPALVDTNGQILDGPAAGNLVLLDSWPGQMRTVYGDHQRFIDTYFRTYPNTYFTGDGCRRDADGYYWITGRVDDVINISGHRIGTAEIESTLVAHPKVAEAAVVGFPHPIKGQGIYAYVTLITGETPSEALHQELLTWVRKEIGAIATPDHVQWAPNLPKTRSGKIMRRILRKIAENAPDQLGDTSTLADPSIVDLLLNERLTH
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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Q87C00
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MSDLYTIDPMLAKDAHIDRAHYKTLYHESIEQPEAFWNKVSQRLEWFKAPTKIKNVSYQLEDVHIRWFEDGELNASVNCLDRHLTLRGDKTALLFEPDAPDAPSSRITYRELYERVCQLGNALRHLGIEKGDRVTIYLPMIPDAVVAILACARIGAIHSVVFGGFAANSIADRVNDCGSKLIITADEGLRGGRKIPLKANVDAALKIHGTQSVETVLVVRHTGSTINMHTPRDRWFHDLVDIQATECAPERMNAEDSLFILYTSGSTGKPKGVLHTTGGYLVYTSYTHETVFDLRENDIYWCTADIGWITGHSYIVYGPLANGTTVLLFEGTPHYPTVSRFWEVIDKHHVTLFYTAPTAIRALMREGDTPVKKTSRKSLRLLGSVGEPINPEAWHWYYTIVGNGRCPIVDTWWQTETGGILITPLIGATDLKPGSVTLPFFGIRPALVDTNGQTLDGPAAGNLVLLDSWPGQMRTLYGDHQRFIDTYFRTYPNTYFTGDGCRRDADGYYWITGRVDDVINISGHRIGTAEIESTLVAHPKVAEAAVVGFPHPIKGQGIYAYVTLITGETPSEALHQELLTWVRKEIGAIAIPDHVQWASNLPKTRSGKIMRRILRKIAENAPDQLGDTSTLADPSIVDLLLNERLKH
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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A1JIK3
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MSQIHKHPIPTAIAEHALINPEQYHQYYQQSVQNPDEFWGEHGKIIDWIKPYKTVKNTSFDPGHVSIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPNQSKTVTYKQLHHDVCQFANVLKKLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPDAVAGRIIDSNSKLVITADEGIRAGRAIPLKKNVDEALKNPAITSIKNVVVFQRTGNASYWKDGRDVWWHDLIKDASVDCPPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGAITLMFEGVPNYPGVNRLGQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTKRTSLRIMGSVGEPINPEAWEWYYNKIGNSKCPIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNLGNPQEGAAEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGVPHNIKGQAIYAYITLNHGEEPTPELYTEVRNWVRKEIGPIATPDILHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVDKLLEEKQSMQAPS
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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A7FNG1
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MSQIHKHPIPAAIAEHALITPEKYQHYYQQSVQNPDEFWGEQGKIIDWIKPYKTVKNTSFDPGHVSIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPNQSKTVTYKQLHHDVCQFANVLKSLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPDAVAGRIIDSHSKLVITADEGIRAGRAIPLKKNVDEALKNPAITSIKNVVVFQRTGNASYWEDGRDVWWHDLIKEASADCPPEEMNAEDPLFILYTSGSTGKPKGVVHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGAITLMFEGVPNYPGVNRLSQVVDKHKVNILYTAPTAIRALMAEGDKAIEGTKRDSLRIMGSVGEPINPEAWEWYYNKIGNSKCPIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNLGNPQEGVAEGNLVITDSWPGQARTLFGDHDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGVPHNIKGQAIYAYITLNHGEEPTPELYTEVRNWVRKEIGPLATPDILHWTDSLPKTRSGKIMRRILRKIATGDTSNLGDTSTLADPSVVEKLLEEKQSMQTPS
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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Q1C0N0
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MSQIHKHPIPAAIAEHALITPEKYQHYYQQSVQNPDEFWGEQGKIIDWIKPYKTVKNTSFDPGHVSIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPNQSKTVTYKQLHHDVCQFANVLKSLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPDAVAGRIIDSHSKLVITADEGIRAGRAIPLKKNVDEALKNPAITSIKNVVVFQRTGNASYWEDGRDVWWHDLIKEASADCPPEEMNAEDPLFILYTSGSTGKPKGVVHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGAITLMFEGVPNYPGVNRLSQVVDKHKVNILYTAPTAIRALMAEGDKAIEGTKRDSLRIMGSVGEPINPEAWEWYYNKIGNSKCPIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNLGNPQEGVAEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGVPHNIKGQAIYAYITLNHGEEPTPELYTEVRNWVRKEIGPLATPDILHWTDSLPKTRSGKIMRRILRKIATGDTSNLGDTSTLADPSVVEKLLEEKQSMQTPS
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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Q8ZJ71
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MSQIHKHPIPAAIAEHALITPEKYQHYYQQSVQNPDEFWGEQGKIIDWIKPYKTVKNTSFDPGHVSIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPNQSKTVTYKQLHHDVCQFANVLKSLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPDAVAGRIIDSHSKLVITADEGIRAGRAIPLKKNVDEALKNPAITSIKNVVVFQRTGNASYWEDGRDVWWHDLIKEASADCPPEEMNAEDPLFILYTSGSTGKPKGVVHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGAITLMFEGVPNYPGVNRLSQVVDKHKVNILYTAPTAIRALMAEGDKAIEGTKRDSLRIMGSVGEPINPEAWEWYYNKIGNSKCPIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNLGNPQEGVAEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGVPHNIKGQAIYAYITLNHGEEPTPELYTEVRNWVRKEIGPLATPDILHWTDSLPKTRSGKIMRRILRKIATGDTSNLGDTSTLADPSVVEKLLEEKQSMQTPS
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family. Extended N-terminus. Extended N-terminus.
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C4GYD8
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MSQIHKHPIPAAIAEHALITPEKYQHYYQQSVQNPDEFWGEQGKIIDWIKPYKTVKNTSFDPGHVSIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPNQSKTVTYKQLHHDVCQFANVLKSLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPDAVAGRIIDSHSKLVITADEGIRAGRAIPLKKNVDEALKNPAITSIKNVVVFQRTGNASYWEDGRDVWWHDLIKEASADCPPEEMNAEDPLFILYTSGSTGKPKGVVHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGAITLMFEGVPNYPGVNRLSQVVDKHKVNILYTAPTAIRALMAEGDKAIEGTKRDSLRIMGSVGEPINPEAWEWYYNKIGNSKCPIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNLGNPQEGVAEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGVPHNIKGQAIYAYITLNHGEEPTPELYTEVRNWVRKEIGPLATPDILHWTDSLPKTRSGKIMRRILRKIATGDTSNLGDTSTLADPSVVEKLLEEKQSMQTPS
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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A4TS06
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MSQIHKHPIPAAIAEHALITPEKYQHYYQQSVQNPDEFWGEQGKIIDWIKPYKTVKNTSFDPGHVSIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPNQSKTVTYKQLHHDVCQFANVLKSLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPDAVAGRIIDSHSKLVITADEGIRAGRAIPLKKNVDEALKNPAITSIKNVVVFQRTGNASYWEDGRDVWWHDLIKEASADCPPEEMNAEDPLFILYTSGSTGKPKGVVHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGAITLMFEGVPNYPGVNRLSQVVDKHKVNILYTAPTAIRALMAEGDKAIEGTKRDSLRIMGSVGEPINPEAWEWYYNKIGNSKCPIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNLGNPQEGVAEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGVPHNIKGQAIYAYITLNHGEEPTPELYTEVRNWVRKEIGPLATPDILHWTDSLPKTRSGKIMRRILRKIATGDTSNLGDTSTLADPSVVEKLLEEKQSMQTPS
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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Q66FM8
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MSQIHKHPIPAAIAEHALITPEKYQHYYQQSVQNPDEFWGEQGKIIDWIKPYKTVKNTSFDPGHVSIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPNQSKTVTYKQLHHDVCQFANVLKSLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPDAVAGRIIDSHSKLVITADEGIRAGRAIPLKKNVDEALKNPAITSIKNVVVFQRTGNASYWEDGRDVWWHDLIKEASADCPPEEMNAEDPLFILYTSGSTGKPKGVVHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGAITLMFEGVPNYPGVNRLSQVVDKHKVNILYTAPTAIRALMAEGDKAIEGTKRDSLRIMGSVGEPINPEAWEWYYNKIGNSKCPIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNLGNPQEGVAEGNLVITDSWPGQARTLFGDHDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGVPHNIKGQAIYAYITLNHGEEPTPELYTEVRNWVRKEIGPLATPDILHWTDSLPKTRSGKIMRRILRKIATGDTSNLGDTSTLADPSVVEKLLEEKQSMQTPS
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Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. Belongs to the ATP-dependent AMP-binding enzyme family.
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Q869S4
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MFSNGLSKLIKSKIASTSIITTKNNYSISKLSFSSTSILLNKKYKLSEPFNYEQDCEYALKEPIQFWDEVASKYVHWNKRYEKVYSGDEYNPEWFKGGVLNACYNALDVHAKDPITKNRIAIIHETPSKNNTNKLTYGELWDEVCIFARGLHNLGVEKGDRVVIYMPMINQALIAMLACARLGATHSVVFGGFASPQLAQRIEHFKPKVVISANFGVEGHKINCYTPLLSKALELSSHKPNHTIVYNRLDVKLDAGEVLPPRVEGSLDWSELIKNIAPYRDYALVDSTHPLYILYTSGTTGMPKGVVRDTGGYSVALNYSIRNCYGMKSGDTFFAGSDVGWVVGHTLSVYGPLMVGLTSIIFEGKPTVPDASTYWKLIEKHRVNALFSAPTAIRAIHRDDADGKLASKCDLSSLRSIWLGGERLDSSTFNFLRNITNNKPILDNYWNTESGSPLITNPSCQVPIKANATGKPMPGYQFHVLSPTSERLGADKIGEVCIKLPVAPGFTNTLYLNPEGYKNAYLNEYPGYLRTADSGYYDENGYYHIISRVDDIINVSGHRLSTGSIEEILVKHPKIVECAVIGVHDELKGEIPFGLVVLKPQYKDCAEEVENELIKEVRENIGPVATFKKVLSVNRLPKTRSGKILRNILRKMYNKEEYTVPPTIEDMEVLKEIDIEFEKYKLSHPPKK
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Activates acetate so that it can be used for lipid synthesis or for energy generation. acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate Belongs to the ATP-dependent AMP-binding enzyme family.
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P37718
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MTHKRYASSLSAGLLATTCVAGLLLQANGARAQQAAEAQAPASSTTMMQAATVAPAQSGQAAVVQRLVQQARFWMQQHQYENARQSLQSAARLAPDSVDLLEAEGEYQSHIGNRDAALDTQRRLHQAAPGSTYESQLNDLLHEQAISQPDLAHARSLAASGHSDQAVEAYQHLFNGSTPTPSLAVEYYQTLAGVSGQAGTAQDGLIRLVKANPSDFRAQLALAQVLTYQPGTRMEGLQRLQALQKYQSSAPVEAATAEKSYRQTLSWLPVTPETLPLMQKWLDAHPSDSALRTHMAEPAGGPPDKGALARQDGFKALNAGRLSAAQAAFQSALNLNAKDGDALGGLGLVAMRAGHNEEAHRYLEDAIAADPKNAAHWRPALAGMAVGEEYGSVRRLIASGQTQEAEQRLMTLARQPGQSEGATLMLADLQRSTGQTGEAERNYRAILARNGDNPIALMGLARVLMGEGQESEANALLSRLGGRYSDQVQQIEVSGIMAEAARTSDSAQKVSLLRQAMTKAPDDPWLRINLANALQQQGDSAEAANVMRPLLTSPRTPADYQAAILYASGNGNDTLARRLLAGLSPDDYSPAIRTIADEMAIKADLASRLSMVSNPTPLVREALAAPDPTGARGVAVADLFRQRGDMLHAHMALRIASTRNIDLTTEQRLAYATEYMKISNPVAAARLLAPLGDGSGTATGSAMSPDQRQTLMQLRMGISVAQSDLLNQRGDQAAAYDHLAPALQADPEATSPKLALARLYNGRGKYGHALDIDLAVLRHNPQDLDARQAAVQAAANDGKDNLAMQLAQDGVQQSPMDARSWLGMAVADRAVGHGDRTLADLRRAYELRLQQLKISRGDAIGGDETQATAPPTANPFRRDAYGHALSLGAPPGENGYSTAGSVPEISDQMLSSINGQIHTLSEDMAPSVDAGLGFRVRSGTPGMGALTEASVPIVGRIPLQAGTSALTFTATPTFLTSGHLPQTGYDIPRFGTNLFALERNLQNQNNSAEHRINTDTIGREAGVAPDVRFANNWVSADVGASPLGFTLPNVIGGVEFAPRVGPVTFRVSGERRSITNSVLSYGGMTDALTGKKWGGVVTNHFHGQVEATLGNTIVYGGGGYAIQTGHHVQSNTEVEGGLGANTLVYRNRKHEVRVGVNLTYFGYKHNEDFYTYGQGGYFSPQSYFAATVPVRYSGHSGLFDWDVTGSIGYQLFHEHSSAFFPTNPVYQALANGLAGVSTAELSLESARYPGDDVGSLVGGFDGRVGYRVSHSLRLDLSGRFQKAGNWDEGGAMISAHYLIMDQ
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Required for maximal bacterial cellulose synthesis. It may be involved in the formation of a membrane complex for extrusion of the cellulose product. Glycan metabolism; bacterial cellulose biosynthesis. Belongs to the AcsC/BcsC family.
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Q07340
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MPLTGLEIYKQLPKKNCGECGTPTCLAFAMNLASGKASLDSCPYVSDAAREALDAAAAPPIAKVVLGAGPTAVEMGDETELFRHDKRFYHETAIAIQVSDNLSSEELKAKVEAINGLNFDRVGQHYTIQAIAIRHDADDPAAFKAAVASVAAATQLNLVLMADDPDVLKEALAGVADRKPLLYAATGANYEAMTALAKENNCPLAVYGNGLEELAELVDKIVALGHKQLVLDPGARETSRAIADFTQIRRLAIKKRFRSFGYPIIALTTAANPLDEVLQAVNYVTKYASLVVLRTDAKEHLLPLLSWRQNLYTDPQVPIRVEEKLNEIGAVNENSPVYVTTNFSLTYYSVEGEIESTKIPSYLLSVDTDGLSVLTAYADGKFEAEKIAAVMKKVDLDNKVKRHRIIIPGAVAVLKGKLEDLTGWEVIVGPREASGIVAFARANLAS
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Acts as a methyl group carrier in the anaerobic acetyl-CoA pathway (Wood-Ljungdahl pathway) of carbon monoxide and carbon dioxide fixation. Binds the corrinoid 5-methoxybenzimidazolylcobamide which is then methylated by the AcsE subunit (PubMed:2821001). Binds 1 [4Fe-4S] cluster. Heterohexamer composed of 2 subunits of AcsC, 2 subunits of AcsD and 2 subunits of AcsE.
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P37719
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MTIFEKKPDFTLFLQTLSWEIDDQVGIEVRNELLREVGRGMGTRIMPPPCQTVDKLQIELNALLALIGWGTVTLELLSEDQSLRIVHENLPQVGSAGEPSGTWLAPVLEGLYGRWVTSQAGAFGDYVVTRDVDAEDLNAVPRQTIIMYMRVRSSAT
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May have a major role in the perfection of crystallization, involved either in the pore structure itself or in the organization of the pores within the linear array of terminal synthesizing complexes (TCs). Glycan metabolism; bacterial cellulose biosynthesis.
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Q07341
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MAVQILRDRSRAAVQKVVLGATKDQGGTRSHTIVVGGDAALPFHHFEGEIVNRPVIGMEVQDIVPDWPDVLKDPFTDVINEPGRWAQKCVAEYGADLIYLKLDGADPEGANHSVDQCVATVKEVLQAVGVPLVVVGCGDVEKDHEVLEAVAEAAAGENLLLGNAEQENYKSLTAACMVHKHNIIARSPLDINICKQLNILINEMNLPLDHIVIDPSIGGLGYGIEYSFSIMERIRLGALQGDKMLSMPVICTVGYEAWRAKEASAPVSEYPGWGKETERGILWEAVTATALLQAGAHILLMRHPEAVARVKENIDQLMVSNAY
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Acts as a methyl group carrier in the anaerobic acetyl-CoA pathway (Wood-Ljungdahl pathway) of carbon monoxide and carbon dioxide fixation. Heterohexamer composed of 2 subunits of AcsC, 2 subunits of AcsD and 2 subunits of AcsE.
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Q25379
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AEREIVRNIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETCYNSIMKCDVDIRKFLYANTVLSGGSTMFPGIADRMQKEITAFAPPTMKVKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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Q75LK6
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MADGEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVNNWDDMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNAPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDCLMKILTERGYSFTTTAEREIVRDIKEKLAYIALDYEQELETAKSSSSVEKSYELPDGQVITIGAERFRCPEVLFQPSLIGMEAPGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWISKGEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. There are at least eight actin genes in rice. Belongs to the actin family.
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P46258
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MAEAEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDGLMKILTERGYTFTTSAEREIVRDMKEKLAYIALDYEQELETAKTSSAVEKTYELPDGQVITIGAERFRCPEVTVQPSMIGMESPGIHETTFNSIMKCDVDIRKDLYGNIVLSGGSTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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P41113
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MADDDVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAIIRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEQEMQTAVTSSSLEKSYELPDGQVITIGNERFRCPETLFQPAFIGMESAGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMFPGIADRMQKEISSLAPPTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. There are at least six actin genes in Podocoryne carnea. Belongs to the actin family.
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Q96484
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AGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEADPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAIPRLDLAGRDLTDHLMKILTERGYSFTTTAEREIVRDVKEKLSYIALDYEQEIETAKTSSSVEKSYELPDGQVITIGSERFRCPEVLFQPSMIGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQ
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. There are at least 5 different actin genes in tomato. Belongs to the actin family.
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P30167
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MAEGEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPRIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDHLMKILTERGYSFTTTAEREIVRDVKEKLSYIALDFEQELETSKTSSSVEKSYELPDGQVITIGAERFRCPEVLFQPSLIGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKELTALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. There are at least 13 actin genes in potato. Belongs to the actin family.
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Q96427
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MADAEDIEPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDXYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVVSEEPXVLSXEAPLNPKVNRESAQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGDALPHAILRLDLAGRDLTDHLMKILTERGYMFTTSAEREIVRDMKEKLAYVALDYEQELETAKSSSSVEKSHELPDGQVITIGAERFRCPKILFQPSMIEMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGSTMFLGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWISKGEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. There are at least 16 actin genes in soybean. Belongs to the actin family.
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P16544
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MATQDSEVALVTGATSGIGLEIARRLGKEGLRVFVCARGEEGLRTTLKELREAGVEADGRTCDVRSVPEIEALVAAVVERYGPVDVLVNNAGRPGGGATAELADELWLDVVETNLTGVFRVTKQVLKAGGMLERGTGRIVNIASTGGKQGVVHAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVREHYSDIWEVSTEEAFDRITARVPIGRYVQPSEVAEMVAYLIGPGAAAVTAQALNVCGGLGNY
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Antibiotic biosynthesis; actinorhodin biosynthesis. Homotetramer. Belongs to the short-chain dehydrogenases/reductases (SDR) family.
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P93373
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AGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIASNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFSVPAMYVAIQAVLSLYASGRTTGTGIVLDSGDGVSHHVPIYEGYALPHAILRLDLAGRDLTDSLMKILTERGYMFTTTAEREIVRDMKEKLAYVALDYEQELETARSSSSIEKNYELPDGQVITIGAERFRCPEVLFQPSMIGMEAAGIHETTYNSIMKRDVDIRKDLYGNIVLSGGSTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTLQQV
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. There are at least 7 different actin genes in tobacco. Belongs to the actin family.
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Q5D0D1
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MCDDDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIQRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLAYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Shows overlapping but distinct expression patterns with other actins. In tailbud embryos, expressed in embryonic muscle (myotomes). In adults, expressed exclusively in skeletal muscle. First expressed after neurulation (stage 18), and expressed throughout development. Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin repolymerization. Monomethylation at Lys-86 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. Xenopus contains at least three sarcomeric alpha actin genes that are preferentially expressed in either heart or skeletal muscle. Due to the tetraploid nature of Xenopus laevis, each of these three alpha actin genes is present in at least two copies. PubMed:3172214 suggest that the sequences isolated in PubMed:3009830 (alpha3-II) and PubMed:3172214 (alpha3-I) may represent paralogous genes in tetraploid Xenopus laevis. The cardiac versus skeletal expression patterns of actins are probably sequence-dependent; Xenopus cardiac actins contain a Glu at position 3 of the mature peptide, whereas skeletal actins contain an Asp at this position. Belongs to the actin family.
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Q6P8G3
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MCDDDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIQRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLAYVALDFENEMATAATSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. In tailbud embryos, expressed in embryonic muscle (myotomes). Unlike Xenopus laevis act3, expression is restricted to embryonic and tadpole stages. Not expressed in adults. Oxidation of Met-46 and Met-49 by MICALs (mical1, mical2 or mical3) to form methionine sulfoxide promotes actin filament depolymerization. Mical1 and mical2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by msrb1 and msrb2, which promote actin repolymerization (By similarity). Xenopus contains at least three different sarcomeric alpha actin genes that are preferentially expressed in either heart or skeletal muscle. The cardiac versus skeletal expression patterns of actins are probably sequence-dependent; Xenopus cardiac actins contain a Glu at position 3 of the mature peptide, whereas skeletal actins contain an Asp at this position. Belongs to the actin family.
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P53494
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MADGEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVNNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDHLMKILTERGYSFTTTAEREIVRDMKEKLSYIALDFEQELETSKTSSSVEKSFELPDGQVITIGAERFRCPEVLFQPSMIGMENPGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFGGIGDRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. This is considered as one of the reproductive actins. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. The binding of profilin to monomeric G-actin cause the sequestration of actin into profilactin complexes, and prevents the polymerization. Little or no reproductive-gene expression is detected in vegetative organs, such as root, stems, leaves, sepals and petals. Expressed primarily in pollen. There are 8 actin genes in A.thaliana. Belongs to the actin family.
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P18603
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MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSTSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. Oxidation of Met-45 to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced (By similarity). There are at least 4 actin isoforms expressed during artemia development. Belongs to the actin family.
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Q27250
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MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. Brain of newly enclosed adults. Expressed during pupal development and in adults. Oxidation of Met-45 to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced (By similarity). Belongs to the actin family.
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Q7YSY2
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MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGVVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITVGNERFRCPEALFQPSFLGMESAGIHETSYNSIMKCDIDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. In this organism there are four genes coding for actin. The sequences coded by genes 1 and 3 are identical. There are a few variations in the actins coded by genes 2 and 4. Belongs to the actin family.
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Q9VNW5
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MCDEEASALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDCYVGDEAQSKRGILSLKYPIEHGIITNWDDMEKVWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRTPEALFQPSFLGMESCGIHETVYQSIMKCDVDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTIKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPGIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. Expressed during larval stages and at a lower level in pupae. Oxidation of Met-45 by Mical to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced. In Drosophila there are 6 closely related actin genes. Belongs to the actin family.
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Q25380
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EKLCYVALDFEQEMQTAASSSSLEKSYELPDGQVITTGNERFRAPESLYQPSFLGMESSGIHETTYNSIMMCDVDIRKDLYANTVLSGGSTIFPGIADRMQKEITSLAPPTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGP
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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Q96481
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AGFAGDDAPRAVFPSIVGRPRYTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIRHGIVDNWDDMEKIWHHTFYNELRVAPEDDSILLTEAPLNPKANREKMTQIMFETFNVPAMYIAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMMILTERGYSFTTAAEREIVRDVKEKLAYVALDYEQELETTKNGKDAEKSYELPDGQIVTIGAERFRCPEVLFQPSLIGMEAVGIHETTYSSIMKCDVDIRRDLYGNVVLSGGSTMFPGITDRMSKEFTALAPSSMKIKVVAPPESKYSVWIGGSILASLSTFQQ
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. There are at least 5 different actin genes in tomato. Belongs to the actin family.
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P93585
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AGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILSLKYPIEHGIVSNWDDMEKIWHHTFYNELRVVPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMGSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDHLMKILTERGYSFTTTAEREIVRDVKEKLSYIAPDYEQEIIDTTSSSKTVEKTYELPDGQVITIGAERFRCPEVLFQPSIIGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQL
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. There are at least 13 actin genes in potato. Belongs to the actin family.
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Q6AY16
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MDVNGPKRWEPHRSLDLNPRSTPVYKSPLQEPCGVFGNKGTTKMSGVVIDMGTGICKMGFAGQTRPTYIVRNIVGCQPKRRTTMEQPKMEMFIGEAAHARPELTLMHPVRNGIVVDWEAAEFIWRHILENDLRLDTQDHPLLFTDPPFNPASNREKLVEVAFESLHSPAIYVASQSVLSVYANGRVNGLVVDTGHGVSYTVPVFQGYNLPSGIQRMDLAGHYLTKFLAEKILRSSFAVKKEDMDTMENIKQQYCYVALDFQKEQGRPDEKFRRCLKLPDGQMITVGKELFQCPELLFHPPDTSGPSSLGLPSMVEHSLSTVPQELRADMEQNVLLCGGSSLFTGFEGRFKTELLRRLGPEAHVVVVAQANRNLSVWIGGSILASLCAFQTRWVLREQYEEHGPDIVLRKCS
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Testis-specic protein that plays an important role in fusion of proacrosomal vesicles and perinuclear theca formation. Interacts with ACTL7A. Localizes predominantly in the equatorial segment of the sperm head and neck regions, with some localization in the acrosomal segment of the head. Colocalizes in the acrosomal and equatorial segments of sperm with ACTL7A. Colocalizes with PLCZ1 in the equatorial segment of the head of capacitated sperm. Belongs to the actin family.
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P17304
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MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVPPEEHPVLLTEAPLNPKANREKMTQIMFETFNAPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLSKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPESLFQPILLGMESAGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMFPGIADRMQKEITSLAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Expressed in the muscular cells of the sheath surrounding abdominal ganglions. Belongs to the actin family.
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Q93130
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MCDDEEEEATPLVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDAYVGDEAQSKRGILTLKYPVEHGIVTNWDDMEKVWHHTFYNELRIAPEENPCLLTEAPLNPKANREKMTQIMFETFNSPAMYVCIQAVLCLYASGRTTGIVLDSGDGVSHTVPIYEGYAMPHAILRLDLAGRELTNYLMRVMCDRGYAFVTTAEREIVRDIKEKLGYVALDFEQEMLTAATSTSLEKSYELPDGQVITIGNERFRCAEALFQPSFLGMESAGVHETVYNSIMKCDIDVRKDLYANNVLSGGTTMFPGIGDRMQKEMVSLAPSTMKIKIIAPPERKYSCWIGGSILASLSTFAAMWIKKSEYDEAGPAIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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Q93132
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MSDEEEEATPLVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDAYVGDEAQSKRGILTLKYPVEHGIVTNWDDMEKVWHHTFYNELRIAPEENPCLLTEAPLNPKANREKMTQIMFETFNSPAMYVCIQAVLCLYASGRTTGIVLDSGDGVSHTVPIYEGYAMPHAILRLDLAGRELTNYLMRVMCDRGYAFVTTAEREIVRDIKEKLGYVALDFEQEMLTAATSTSLEKSYELPDGQVITIGNERFRCAEALFQPSFLGMESAGVHETVYNSIMKCDIDVRKDLYANNVLSGGTTMFPGIGDRMQKEMVALAPSTMKIKIIAPPERKYSCWIGGSILASLSTFASMWIKKSEYDEAGPAIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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O17502
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MCDDEEEEEATPLVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDAYVGDEAQSKRGILTLKYPVEHGIVTNWDDMEKIWHHTFYNELRIAPEENPCLLTEAPLNPKANREKMTQIMFETFNSPAMYVCIQAVLCLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRELTNYLMKIMTDRGYSFVTTAEREIVRDIKEKLGYVALDFEQEMLTAATSTSLEKSYELPDGQVITIGNERFRCAEALFQPSFLGMESAGVHETVYNSIMKCDIDVRKDLYANNVLSGGTTMFPGIGDRMQKEMVSLAPSTMKIKIIAPPERKYSCWIGGSILASLSTFAAMWIKKSEYDEAGPAIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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O15998
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MSDSEEDQTALVCDNGSGLVKSGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVMDAGDGVSHNVPIYEGYALPHAIARLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFEQEMATAASSTSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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P53463
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MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNAPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYSALDFEQEMATAAASSSLEKSYELPDGQVITIGNERFRCPETLFQPAFIGMESAGIHETTYNSIMKCDIDIRKDLYANTVLSGGTSMYPGIADRMQKEITALAPSSMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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P53464
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MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNAPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYTALDFEQEMATAAASSSLEKSYELPDGQVITIGNERFRCPETLFQPAFIGMESAGIHETTYNSIMKCDIDIRKDLYANTVLSGGTSMYPGIADRMQKEITALAPSSMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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Q25381
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AEREIVRNIKEKLCYVALDFEQEMATPAASSSLEKSYELPDGQVITIGNERFRCPETLFQPAFIGMESAGIHETTYNSIMKCDIDIRKDLYANTVLSGGTSMYPGIADRMQKEITALAPSSMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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P53467
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MSSEEEDQTAIVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRIAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGISHNVPIYEGYALPHAIARMDLAGRDLTEYLTKILTERGYSFVTTAEKEIVRDIKEKLCYVALDFEQEMATAASSTSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILSSLSTFNQMWITKAEYDEAGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. Belongs to the actin family.
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P12717
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MCDEDVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVFDTGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYTALDFEQEMQTASSSSSLEKSYELPDGQVITIGNERFRCPETLFQPAFIGMESAGIHETTYNSIMKCDIDIRKDLYANTVLSGGTSMYPGIADRMQKEIQALAPPTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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P12431
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MCDEDVAALVVDNGSGMCKTGFAGDDAPRAVFPSIVGRPRHHGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNAPAMYVAIKAVLSLYASGRTTGIXXXXGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYTALNFEREMATAAASSSLEKSYELPDGQVITIGNERFRCPETLFEPAFIGMESAGIHETTYNSIMKCDIDIRKDLYANTVLSGGTSMYPGIADRMQKEITALAPSSVKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYSGASIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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P26198
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MSDGEEDQTAIVCDNGSGLVKSGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTMYNELRVAPEEHPTLLTEAPHNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVMDAGDGVSHNVPIYEGYALPHAIARLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFEQEMATAASSTSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Belongs to the actin family.
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Q00214
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MEDDQDEEQTALVCDNGSGLVKAGFPGDAPPRAVFPLTVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDNMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESSGVHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKSKIIAPPERKYSVWIGASILASLSTFQQMWITKQEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Belongs to the actin family.
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Q3B7N2
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MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRAPENTMHAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHARQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLNHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDPQGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITVDELRRELPPDQAEYCIARMAPYTGPDAVPGALDYMSFSTALYGESDL
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F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity). Homodimer; antiparallel. Interacts with MYOZ2, TTID and LPP. Interacts with DDN (By similarity). Interacts with PSD. Interacts with MICALL2 (By similarity). Interacts with DNM2 and CTTN. Interacts with PDLIM1. Interacts with PDLIM2. Interacts with PDLIM4 (via PDZ domain) (By similarity). Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures. Belongs to the alpha-actinin family.
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Q99001
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MDHHYDPQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRAPENTMQAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNAWGGLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHESWTDGKEAMLQQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERQAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWEHVRQLVPRRDQALMEEHARQQQNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLNHLRQYEKSIVNYKPKIDQLEGDHQQIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDAQGEAEFARIMSIVDPNRMGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITVDELRRELPPDQAEYCIARMAPYNGRDAVPGALDYMSFSTALYGESDL
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F-actin cross-linking protein is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Homodimer; antiparallel (By similarity). Interacts with PDLIM4 (via PDZ domain) (PubMed:14729062). Isoforms only differ in the region of the first EF-hand calcium-binding motif. Belongs to the alpha-actinin family.
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Q9BTN1
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MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRVPENTMHAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQVEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHARQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLSHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDPQGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITMDELRRELPPDQAEYCIARMAPYTGPDSVPGALDYMSFSTALYGESDL
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F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Homodimer; antiparallel. Interacts with MYOZ2, TTID and LPP (PubMed:10369880, PubMed:11114196, PubMed:12615977). Interacts with DDN (PubMed:16464232). Interacts with PSD. Interacts with MICALL2 (By similarity). Interacts with DNM2 and CTTN. Interacts with PDLIM1. Interacts with PDLIM2. Interacts with PDLIM4 (via PDZ domain) (By similarity). Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures. The disease is caused by variants affecting the gene represented in this entry. Belongs to the alpha-actinin family.
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Q2PFV7
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MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRVPENTMHAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQVEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHARQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLSHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDPQGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITVDELRRELPPDQAEYCIARMAPYTGPDSVPGALDYMSFSTALYGESDL
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F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity). Homodimer; antiparallel. Interacts with MYOZ2, TTID and LPP. Interacts with DDN (By similarity). Interacts with PSD. Interacts with MICALL2 (By similarity). Interacts with DNM2 and CTTN. Interacts with PDLIM1. Interacts with PDLIM2. Interacts with PDLIM4 (via PDZ domain) (By similarity). Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures. Belongs to the alpha-actinin family.
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Q7TPR4
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MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAERFLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRVPENTMHAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHARQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLSHLRQYEKSIVNYKPKIDQLECDHQLIQEALIFDNKHTNYNMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDPQGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITEDELRRELPPDQAEYCIARMAPYAGPDSVPGALDYMSFSTALYGESDL
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F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity). Homodimer; antiparallel. Interacts with MYOZ2, TTID and LPP. Interacts with DDN (By similarity). Interacts with PSD (PubMed:17298598). Interacts with MICALL2 (PubMed:23100251). Interacts with DNM2 and CTTN. Interacts with PDLIM1. Interacts with PDLIM2. Interacts with PDLIM4 (via PDZ domain) (By similarity). Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle (PubMed:11114196). Colocalizes with PSD in membrane ruffles and central reticular structures (PubMed:17298598). Belongs to the alpha-actinin family.
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Q9Z1P2
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MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAERYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRVPENTMQAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHSRQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLSHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDPQGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITGDELRRELPPDQAEYCIARMAPYAGPDSVPGALDYMSFSTALYGESDL
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F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity). Homodimer; antiparallel. Interacts with MYOZ2, TTID and LPP (By similarity). Interacts with DDN (PubMed:16464232). Interacts with PSD. Interacts with MICALL2 (By similarity). Interacts with DNM2 and CTTN (PubMed:21210813). Interacts with PDLIM1 (PubMed:22659164). Interacts with PDLIM2 (PubMed:15505042). Interacts with PDLIM4 (via PDZ domain) (PubMed:14729062). Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures. Belongs to the alpha-actinin family.
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B6I5T5
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MKRVLTALAATLPFAANAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFSEAMAVHPKGVDIMKPGGLVKDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPEYKDAAGHLIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFKKGATEREELRVSKITVLILGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMMGGWLGLITAVVLMILGPTIWVQILGHEKAIFPYEYPALFSITVAFLGIWFFSATDNSAEGARERELFRAQFIRSQTGFGVEQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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B1LPN2
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MKRVLTALAATLPFAANAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRNDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFSEAMAVHPKGVDIMKPGGLVKDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPEYKDAAGHLIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFKKGATEREELRVSKITVLILGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMLGGWLGLITAVVLMILGPTIWVQILGHEKAIFPYEYPALFSISVAFLGIWFFSATDNSAEGARERELFRAQFIRSQTGFGVEQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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Q1R3J9
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MKRVLTALAATLPFAANAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRNDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFSEAMAVHPKGVDIMKPGGLVKDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPEYKDAAGHLIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFKKGATEREELRVSKITVLILGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMLGGWLGLITAVVLMILGPTIWVQILGHEKAIFPYEYPALFSISVAFLGIWLFSATDNSAEGARERELFRAQFIRSQTGFGVEQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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A4W5I3
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MKRVLTALAATLPFAANAADALTGAVERQPTNWQAIIMFLIFVLLTLYITYWASKRVRSRNDYYTAGGNITGFQNGLAIAGDFMSAASFLGISALVYTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRTLSACGSLVVVALYLIAQMVGAGKLIQLLFGLNYHIAVVLVGVLMVMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFTQAMAVHPKGEAIMSPGGLVKDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPAFKDAAGTLIGGNNMAAVHLADAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVWRKGATERQELKVSKITVLILGVVAILLGILFENQNIAFMVGLAFSIAASCNFPIILLSMYWSKLTTRGAMIGGWLGLLTAVILMVLGPTIWVQILGHEKAIFPYEYPALFSIAVAFIGIWFFSATDNSAEGKLEREKFRAQFIRSQTGLGIDQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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P0DMX3
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SLALAGTIIEGASLTFSVLTTILDALGSVSRKIDVGVYNE
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Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cytolysis and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers (By similarity). This toxin shows hemolytic activities (PubMed:10665806). Tetramer in the presence of a lipidic interface. Monomer, in soluble state. Forms an alpha-helical membrane channel in the prey. The N-terminal region, before the pore is formed, is bound to the lipid membrane. It partitions into the lipid-water interface and stabilizes the monomeric molecule on the membrane. Finally, it traverses the bilayer, thus forming the transmembrane pore. The Trp-rich region is important for the binding to lipid membrane. Belongs to the actinoporin family. Sea anemone subfamily.
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B2VKE4
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MSKNYLLAVLALLLSGPVVAADAIAGTVERQPVNMEAIVMFLIFVAMTLGITYWASRRTRSRSDYYTAGGNITGFQNGLAMAGDFMSAASFLGISALVYTSGFDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQMPIRTLSACGSLVVVALYLIAQMVGAGKLIQLLFGLDYHVAVVLVGILMVMYVLFGGMLATTWVQIIKAVLLLFGASFMAIMVMKNVGFSFDTLFSEAMKIHPKGVAIMRPGGLVNDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGLMGYFYFLTFIIGFGAILLVGANPAFKDATGALLGGNNMAAVHLADAVGGSLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYASVVRKGQASEREELRVSKITVVALGVVAILLGILFEKQNIAFMVGLAFSIAASCNFPIILLSMYWSRLTTRGAMTGGWLGLLTAVILMILGPTIWVQVLGHARPIFPYEYPALFSMLVAFIGTWLFSVTDNSTQGAEERLRFRAQFVRSQTGVGIEGGKGH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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B7LMN9
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MKRVLTALAATLPFAANAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRNDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFSEAMAVHPKGVDIMKPGGLVKDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPEYKDAAGHLIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFKKGATEREELRVSKITVLILGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMMGGWLGLITAVVLMILGPTIWVQILGHEKAIFPYEYPALFSITVAFLGIWFFSATDNSAEGARERELFRAQFIRSQTGFGVEQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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B5XXT7
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MIKRVLTALAATLLPLGAHAADAITGAVQRQPTNWQAIVMFLIFVALTLYITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDFMSAASFLGISALVYTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRTLSACGSLVVVALYLIAQMVGAGKLIQLLFGLNYHVAVVLVGVLMVLYVLFGGMLATTWVQIIKAVLLLCGASFMAFMVMKHVGFSFNNLFTEAMAVHPKGAAIMSPGGLVKDPISALSLGLGLMFGTAGLPHILMRFFTVSDAKEARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPAFKDAAGQLIGGNNMAAVHLADAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFRKGATERQELKVSKITVLILGVVAILLGILFENQNIAFMVGLAFSIAASCNFPIILLSMYWSKLTTRGAMVGGWLGLLTAVILMILGPTIWVQILGHEKALFPYEYPALFSIAIAFIGIWVFSATDNSPEGMREREQFRAQFIRSQTGIGIERGQAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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A6TGZ7
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MIKRVLTALAATLLPLGAHAADAITGAVQRQPTNWQAIVMFLIFVALTLYITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDFMSAASFLGISALVYTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRTLSACGSLVVVALYLIAQMVGAGKLIQLLFGLNYHVAVVLVGVLMVLYVLFGGMLATTWVQIIKAVLLLCGASFMAFMVMKHVGFSFNNLFTEAMAVHPKGAAIMSPGGLVKDPISALSLGLGLMFGTAGLPHILMRFFTVSDAKEARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPAFKDAAGQLIGGNNMAAVHLADAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFRKGATERQELKVSKITVLILGVVAILLGILFENQNIAFMVGLAFSIAASCNFPIILLSMYWSKLTTRGAMVGGWLGLLTAVILMILGPTIWVQILGHEKALFPYEYPALFSIAIAFIGIWVFSATDNSPEGMREREQFRAQFIRSQTGIGIERGQAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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Q6D913
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MKIRFMMLFGLLTLPVLAWAADALTGDVQRQPLNIQAIVMFLLFVGGTLYITYWASKKTRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVYTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQNPIRSLSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHVAVVLVGILMVMYVMFGGMLATTWVQIIKAVLLLFGATFMAVMVMKSVGFSFDALFKQAMEVHPKGAAIMSPGGLVSDPISALSLGLGLMFGTAGLPHILMRFFTVSDAKEARKSVFYATGFMGYFYFLTFIIGFGAILLVSANPEFKDATGALIGGNNMAAIHLADAVGGNFFLGFISAVAFATILAVVAGLTLAGASAVSHDLYSNVIKKGKATERDELKVSKITVLVLGVVAISLGILFENQNIAFMVGLAFSIAASCNFPIIIISMYWSKLTTRGAMIGGWAGLLTAVILMVLGPTIWVKILGHAAPIYPYDYPALFSMLVAFIGIWFFSITDRSETGQQERARFHAQFVRSQTGVGASKGSSH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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C6D930
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MKIRFMMLFGLLTLPVLAWAADALTGDVQRQPLNIQAIVMFLLFVGGTLYITYWASKKTRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVYTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLQQRPIRSLSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHVAVILVGILMVMYVMFGGMLATTWVQIIKAVLLLFGATFMAVMVMKSVGFSFDALFKQAMAVHPKGASIMSPGGLVSDPISALSLGLGLMFGTAGLPHILMRFFTVSDAKEARKSVFYATGFMGYFYFLTFIIGFGAILLVSANPEFKDATGALIGGNNMAAVHLADAVGGDFFLGFISAVAFATILAVVAGLTLAGASAVSHDLYSNVIKKGKATERDELKVSKITVLVLGVVAISLGILFENQNIAFMVGLAFSIAASCNFPIIIISMYWSKLTTRGAMIGGWAGLLTAVILMILGPTIWVKILGHATPIYPYDYPALFSMLVAFIGIWFFSITDRSEAGQQERARFHAQFVRSQTGVGASKGSSH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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Q7NA72
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MKNFLLLAIMLFPHLTWANVISETGERQPVNIQAIIMFVLFVGFTLYITYWASKKTRSRTDYYTAGGRITGFQNGMAIAGDFMSAASFLGISALVYTSGYDGLIYSIGFLIGWPIILFLIAERLRNLGRYTFADVASYRLQQRPIRILSAIGSLFVVALYLIAQMVGAGKLIELLFGLNYHVAVVLVGILMVLYVLFGGMLATTWVQIIKAILLLAGATFMALMVMKIVNFNFNTLFKEAIAVHSRGEAIMSPGGLVSDPISALSLGLALMFGTAGLPHIIMRFFTVSDAKEARKSVFYATGFIGYFYILTFIIGFGAILLVSPNPSFKDTTGALIGGTNMAAVHLASAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANAIKSGKANERDELRVSKITVVILGFIAIGLGILFENQNIAFMVGLAFSIAASCNFPIILLSMYWHKLTTRGALVGGWLGLITAVVLMILGPTIWVSILGHEKPIYPYEYPALFSMIIAFIGSWLFSITDNSQQGMQEREQFRIQFIRSQTGLGIAQGKTH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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B5F2E9
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MKRVLTALAAALPFAAHAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFTEAMAVHPKGTAIMSPGGLVQDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPAYKDAAGALIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFRKGATEREELKVSKITVLVLGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMLGGWLGLLTAVVLMILGPTIWVQILGHEKAIFPYEYPALFSISVAFLGIWFFSATDNSAEGNREREQFRAQFIRSQTGFGVQQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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A9MGK8
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MKRVLTALAAALPFAAHAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFTEAMAVHPKGTAIMSPGGLVQDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPAYKDAAGALIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFRKGATEREELKVSKITVLVLGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMLGGWLGLLTAVVLMILGPTIWVQILGHEKAIFPYEYPALFSISVAFLGIWFFSATDNSAEGNREREQFRAQFIRSQTGFGVEQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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Q57GV4
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MKRVLTALAAALPFAAHAADAISGAVEHQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFTEAMAVHPKGTAIMSPGGLVQDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPAYKDAAGALIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFRKGATEREELKVSKITVLVLGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMLGGWLGLLTAVVLMILGPTIWVQILGHEKAIFPYEYPALFSISVAFLGIWFFSATDNSAEGNREREQFRAQFIRSQTGFGVQQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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B5FRF0
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MKRVLTALAAALPFAAHAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFTEAMAVHPKGTAIMSPGGLVQDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPAYKDAAGALIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFRKGATEREELKVSKITVLVLGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMLGGWLGLLTAVVLMILGPTIWVQILGHEKAIFPYEYPALFSISVAFLGIWFFSATDNSAEGNREREQFRAQFIRSQTGFGVEQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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B5QZ97
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MKRVLTALAAALPFAAHAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFTEAMAVHPKGTAIMSPGGLVQDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPAYKDAAGALIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFRKGATEREELKVSKITVLVLGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMLGGWLGLLTAVVLMILGPTIWVQILGHEKAIFPYEYPALFSISVAFLGIWFFSATDNSAEGNREREQFRAQFIRSQTGFGVEQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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B5R937
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MKRVLTALAAALPFAAHAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFTEAMAVHPKGTAIMSPGGLVQDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGTNPAYKDAAGALIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFRKGATEREELKVSKITVLVLGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMLGGWLGLLTAVVLMILGPTIWVQILGHEKAIFPYEYPALFSISVAFLGIWFFSATDNSAEGNREREQFRAQFIRSQTGFGVEQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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B4TEB2
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MKRVLTALAAALPFAAHAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFTEAMAVHPKGTAIMSPGGLVQDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPAYKDAAGALIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFRKGATEREELKVSKITVLVLGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMLGGWLGLLTAVVLMILGPTIWVQILGHEKAIFPYEYPALFSISVAFLGIWFFSATDNSAEGNREREQFRAQFIRSQTGFGVQQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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B4T1W9
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MKRVLTALAAALPFAAHAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFTEAMAVHPKGTAIMSPGGLVQDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPAYKDAAGALIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFRKGATEREELKVSKITVLVLGVIAIILGILFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMLGGWLGLLTAVVLMILGPTIWVQILGHEKAIFPYEYPALFSISVAFLGIWFFSATDNSAEGNREREQFRAQFIRSQTGFGVQQGRAH
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Transports acetate. Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
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A0A1L9WN49
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MSKTFEYVICGGGTVGCVLASRLSLAGHSVLLIEAGPEDYNDRIMSPVAAPHLHGTEWEHNLMTTKQPGLGNRSVPNYAGKLLSGSSGINYGLWTRGHSVDYDSWAKAVGDERWNYANMLKYFQKTETQISTTAAARIYPLREPIRNAMVAAGLDYNPDPNGGNPLGFGPFTENWKNALRQPASKAYDLSKATVLTNSVIARVDFDDPKTTATGVTLTDGTQYTATSEVLVTCGALKTPQLLMLSGIGPQQHLAQHNIPIIADLPVGENYHDKISATFFWKLRHPEKGYALGSPRFNKPEFRHGNPIEWVATVPTPHAELIKATQQDQIDSDDPYLQKPRGNVEVMVAYAPIAGGGSEFRLPMDGTHISSPVVLLLPTSRGRITLASADPTADPVLDPGYLDTETDRAAIRAGMRVALRLMETESAKEVIDGETPPPGHEPLTSACSDADLDRRVQIVGSSFFQNGGTAAMGTVVDTQCRVKGVRNLRVCDASVLSVPLAGHYQAPMYALGEAVADMLLAQ
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GMC-type oxidoreductase; part of the gene cluster that mediates the biosynthesis of aculins (PubMed:26374386). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) acuA via condensation of acetate and malonate units (PubMed:26374386). The 6-methylsalicylic acid decarboxylase acuB then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol) (Probable). These first reactions occur in the cytosol (By similarity). The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase acuC converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase acuD (Probable). Gentisyl alcohol is further oxidized by the oxidoreductase acuE that probably catalyzes hydroxylation of the aromatic ring (Probable). The aromatic system might then be opened by oxidation through a Baeyer-Villiger type of oxidation, which could be catalyzed by acuF, with the carboxylic acid at C-1 subsequently reduced to an aldehyde by acuG (Probable). Subsequently, a hemiacetal is formed, before the dehydrogenase acuH would reduce the double bond between C-4 and C-6 (Probable). Finally, keto-enol tautomerism results in formation of aculinic acid, which exists as two diastereomers (both R/S configurations at C-1) by non-enzymatic hemiacetal formation (Probable). The carboxypeptidase acuI could be involved in the linking of aculinic acid to an aculene A moiety produced by the aculene biosynthesis cluster and which leads to the production of aculin A (Probable). AcuI may also be involved in the attachment of proline to aculinic acid to form epi-aculins A and B (Probable). Secondary metabolite biosynthesis. Belongs to the GMC oxidoreductase family.
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P9WEZ9
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MHFRTVNTPARLQFISRFVLQPLRPLLHYKDHTIRTAAEAGLDVAELAVGPAFVVARGYFTLRQADTSSAESRDPTKQQQLWEKTLEWLGMTEEQGAL
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Dehydrogenase; part of the gene cluster that mediates the biosynthesis of aculins (PubMed:26374386). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) acuA via condensation of acetate and malonate units (PubMed:26374386). The 6-methylsalicylic acid decarboxylase acuB then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol) (Probable). These first reactions occur in the cytosol (By similarity). The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase acuC converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase acuD (Probable). Gentisyl alcohol is further oxidized by the oxidoreductase acuE that probably catalyzes hydroxylation of the aromatic ring (Probable). The aromatic system might then be opened by oxidation through a Baeyer-Villiger type of oxidation, which could be catalyzed by acuF, with the carboxylic acid at C-1 subsequently reduced to an aldehyde by acuG (Probable). Subsequently, a hemiacetal is formed, before the dehydrogenase acuH would reduce the double bond between C-4 and C-6 (Probable). Finally, keto-enol tautomerism results in formation of aculinic acid, which exists as two diastereomers (both R/S configurations at C-1) by non-enzymatic hemiacetal formation (Probable). The carboxypeptidase acuI could be involved in the linking of aculinic acid to an aculene A moiety produced by the aculene biosynthesis cluster and which leads to the production of aculin A (Probable). AcuI may also be involved in the attachment of proline to aculinic acid to form epi-aculins A and B (Probable). Secondary metabolite biosynthesis.
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