ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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O78484 | MSKLEQYFDYVKINLASPQRIKKWGERRLPNGQVVGEVTKPETINYRTLKPEMDGLFCERIFGPVKDWECHCGKYKRVRYKGIVCERCGVEVAESKVRRHRMGYIELAAPVTHVWYLKSLPSYISILLDIPLKDVEQVVYFNSYVVTKPGNCTNLRYKQLLSEDEWIAIEDQLYQEDSELTGVEVGIGAEAIQKLLRDIDLEVEAESLREEILVVKGIKKDKSIKRLRVIDNFIATRSDPTWMILTVLPVIPPDLRPMVQLDGGRFATSDLNDLYRRVLNRNNRLIRLQEILAPEIIIRNEKRMLQESVDALIDNGRRGRTVMGANNRPLKSLSDIIEGKQGRFRQNLLGKRVDYSGRSVIVVGPQLELNQCGLPREMALELFQPFVIHKLIQQGLVNNIKAAKRLIQKNELIVWNVLEEVIQGHPILLNRAPTLHRLGIQAFEPILVEGRAIKLHPLVCPAFNADFDGDQMAVHIPLSLEAQAEARMLMLAPYNFLSPATGDPIIMPSQDMVLGCYYLTAENPSQQVNRSLYFSNFDDVLLAYETKLIKLHSYVWVRFNGNVDDDDEKIEEKKLDGNKKLHIYPSRIKKLDQDNNLMVQYILTTPGRILLNNVLFDSLQLQF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 71568
Sequence Length: 623
Subcellular Location: Plastid
EC: 2.7.7.6
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Q1KXX1 | MIDRYTHQQLRIGLVSPQQISTWSKKILPNGEIVGEVTKPYTFHYKTNKPEKDGLFCERIFGPIKSGICACGNYRVIGDEKEDPQFCEQCGVEFVDSRIRRYQMGYIKLAYPVMHVWYLKRLPSYIVNLLDKPLNELEDLVYCGFYFARPIDKKPTFLRLRGLLEYEIQPWKYRIPIFFTTRSFDTFRNREMSTGGGSIRQQLANLDLRMIIDYSLVEWKELEEEESTGNEWEDRKVGRRKDFLLRRMELAKHFIRTNIEPKWMVLRLLPVLPPELRPIYHIDEDKLVTSDINEIYRRIIYRNNTLTDLLTTSIATPEELIISQEKLLQEAVDALLDNGICGQPMRDDHNRIYKSLSDVIEGKEGRVRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRDLIRKHLASNIGVAKSQIRKKKPIVWEILQEILDDHPVLLNRAPTLHRLGIQAFLPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPTIGDPISAPTQDMLSGLYVLTSGNRRGICVNRYNPCNRRNYQNEDNNYKYTKKKEPFFCNAYDAIGAYRQKRINLGSPLWLRWRLDQRVIAAREAPIEIHYESLGTYYEIYGHYLIVRSIKKEILYIYIRTTLGHISLYREIEEAIQGFWQGCYNSMLPARIRVSPG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 80198
Sequence Length: 689
Subcellular Location: Plastid
EC: 2.7.7.6
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Q2EEW9 | MKYFIIRSLINKSKNFYNTIIKYNKTKLFALELSIISPQEIQNSAEYKREDGSIVGKVEDSTFYDLEKVNNKNLFSQQIFGPLIDFTCACGKKLNRKNKEINVCTKCGIEFLPSSIRSKRKGYIKLNYAMLHPFYIDYCEKLLMKSKKSLHLLLNMDSFFYFPSYKNWVNFLSEKNHIYLFLLKKILIYNRYSYIYKYSTFFKNRSKFPNNKKMNKLFFYNALGFYGLNSRKTWTVLDFIKGYNFFLGNFSKYYKKLSWYAYQQKISLNKYKSNNISINNFIDNTFNFYKNEVNSLCFKVGGDGIEMFFLQDMAVYSIINKFLKLRVLKLNNLINVNNKYYGKINTIIQNSKNYQYYFKHFYLKKIAPVWMTLRRIPVLPPNLRPILDLSGKNYQKTASSGTLLFMRDIMHEGNLFISDINTFYREIIIHNKKAFNFFSSLPTLYYLNELNIEYVNSKLWLLKYYLMPIQKSITSLFDKNPETINNFSNKKFTDLILDNVKPTSILDSLKGKYGKIRFNLLGKRVDYSGRSVIISAPHLKIYECGIPYEMALTLYYPFLSEYFYKKNNNILKKNYNKSELVLYSKSLIFTKSLQSILLSHPIIINRAPTLHRLGIQSFLPKLTHSKAIELHPLVCPAFNADFDGDQMAIHVPITEIAKLEAIQLMASSLFVYAPASGLPLLIPTQDIILGFNFYTNDLLLKTSREDKSIKQAMNQGFINECHIPYWIKINTKDIFFKFLAYPLRNYIIPIELQLNIKGFSKIIRLNTFKVTNLVFDSLDLLIKKNYISNWLILNNTKFKYLLISFLQNKNLLTNKQVYLRTTLGNIYFNKYLNL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 98313
Sequence Length: 834
Subcellular Location: Plastid
EC: 2.7.7.6
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P36441 | MAKRLLPVGLVVGEITKTDTINYRTFKPETGGL | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 3619
Sequence Length: 33
Subcellular Location: Plastid
EC: 2.7.7.6
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Q06RE0 | MIDRYKHQQLRIGLVSPEQISAWATKILPNGEIVGEVTKPSILHYKTNKAEKGGLFCERIFGPQKSGICACGNYRVIGDEKEDPKFCEQCGVEFVDSRIRRYQMGYIKLACPVTHVWYLKRLPSYIANLLDKPLKELEGLVYRDFSFARPITKKPTFLRLRGLFEYEIKSWKYSIPLFFTIQGFDTFRNREISTGAGAIREQLVDLDLRIILDNSLVEWKELGEEGPTGNEWEDQKVRRRRGFLVRRMELAKHFIRTNIEPEWMVLCLLPVLPPDLRPVIQIAEGKVMSSDITKLYQRVIYRNKILTDLLTRSVSTPGDLVTSQEKLVQEAVDALLDNGTRGQPMRDGQNKVYKSLSDIIEGKEGRFRQTLLGKRVDYSGRSVIVVGPSLSLYRCGLPREIAIELFQTFVIRGLIRQDPASNIKVAKSQIREKEPIVWEILQEVMQGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPISIPTQDMLVGLYVLTSGNRRGICVNRYNPWNHRNYENQRSKNNNYRYTKEPLFSNSYDAIGAYRQKRIKLDSPLWLRWPLDQRVIASRESPIEVHYESLGTYYEIYGHYLIVRSIKKEILFLYIRTTVGHISLYREIEEAIEGFSQACSSSYGTYTKLSNSRI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 79469
Sequence Length: 691
Subcellular Location: Plastid
EC: 2.7.7.6
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Q56P12 | MIDRYTHQQLRIGLVSPQQISTWSKKILPNGEIVGEVTKPYTFHYKTNKPEKDGLFCERIFGPIKSGICACGNYRVIGDEKEDPQFCEQCGVEFVDSRIRRYQMGYIKLAYPVMHVWYLKRLPSYIVTLLDKPLNELEDLVYCNFYFARPIDKKPTFLRLRGLLEYEIQPWKYRIPIFFTTRSFDTFRNREMSTGGGSIRQQLANLDLRIIIDYSLVEWKELEEEEPTGNEWEDRKVGRRKDFLLRRMELAKHFIRTNIEPKWMVLRLLPVLPPELRPIYHIDEDKLVTSDINEIYRRIIYRNNTLTDLLTTSIATPEELIISQEKLLQEAVDALLDNGICGQPMRDDHNRVYKSLSDVIEGKEGRVRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQAFVIRDLIRKHLASNIGVAKSQIRKKKPIVWEILQEILDDHPVLLNRAPTLHRLGIQAFLPVLVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPTIGDPISAPTQDMLSGLYVLTSGNRRGICVNRYNPCNRRNYQNEDNNYKYTKKKEPFFCNPYDAIGAYRQKRINLGSPLWLRWRLDQRVIAAREVPIEIHYESVGTYYEIYGHYLIVRSIKKEILYIYIRTTLGHISLYREIEEAIQGFWQGCCNSMLPTGIRVSPG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 80131
Sequence Length: 689
Subcellular Location: Plastid
EC: 2.7.7.6
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P14564 | MTNEKMIFRNRVVDKGQLRNLISWAFTYYGTARTAVMADKLKDLGFRYATKAGVSISVDDLMVPPTKRLLLEAAEEEIRATETRYQRGEITEVERFQKVIDTWNGTSEALKDEVVVHFKKTNPLSSVYMMAFSGARGNISQVRQLVGMRGLMADPQGEIIDLPIKTNFREGLTVTEYIISSYGARKGLVVQPSRTADSGYLTRRLVDVSQVYYSGFDCGTPELSIRPMTEGAKTLIPLATRLMGRVIGEDVLHPVTKEVIAARNSPISEDLAKKIEKSGVGEVVVRSPLTCEAARSVCQHCYGWSLAHASMVDLGEAVGIIAAQSIGEPGTQLTMRTFHTGGVFTGEVAQQVRSKIDGTVKLPRKLKTRTYRTRHGEDALYVEANGIMLLEPTKVGDVTPENQEVHLTQGSTLYVFDGNKVNKVQLLAEVALGGRTTRTNTEKAVKDVASDLAGEVQFAEVVPEQKTDRQGNTTTTRRTRGLIWILSGEVYNLPPGAELVVKNGDAIASNGVLAETKLASLHGGVVRLPEATPGKSTREIEIITASVVLDQATVTVQSSQGRNNYLVSTGNNQVFNLRATPGTKVQNGQVVAELIDDRYRTTTGGFLKFAGVEVQKKGKAKLGYEVVQGGTCCGSPEESHEVNKDISLLLVEDGQFVEAGTEVVKDIFCQNSGVVEVTQKNDILREVVVKPGELLIVDDPESVIGRDNTFIQPGEEF | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 78244
Sequence Length: 717
EC: 2.7.7.6
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Q0P3M4 | MKTFFCNRTVDKGEMKRLIKWVLLNYGTEKTTRLIDKLKTMGFHYATHAGISLGIDDLSIPPIKSAFLLNAENDIYENDLRLKRGQITSVQRLEKALDIWNTTNDTLKTEVVKYFRSTDIFNPVYMMAFSGARGNISQVRQLVGMRGLMADPQGQILDFPIRRNFREGLTVTEYMISCYGARKGLVDTALRTASSGYLTRRLVDVAQSVIIQQVDCQTTQGLRIVPELEKIESQLIGRVLFEDVVDLETGRMVGYKNQDISPALALKLIKQPALTIRSPLTCRFHAVCQLCYGWNLAQQKLVQLGEAVGVLAAQSIGEPGTQLTMRTFHTGGVFAGEATEKVYSPHNGIVFYSKQARGRKIVSKYGEVAFLTFEPLKVKIKNDNTTSVLEFPSFTLLYIPPGQTVGEHQSLAELSRIENKQNFQQFEVGTENVQKEFMSNCSGQIFLPQRQNALINEDNAGTTTFNYSEMWLLAGKILDSKTLVPGDQIKNALYPIRSKINCEPSRLTTTLPLGYVFPIDSNQTSLSKLQSTDAETLKQLPLLQFSKLSADNLKFARSYALELNKTLFHCDSLSKYRFITSDLEHLPFKSKNLFFNQDTPTKKVPTFKIKFSRFGKADKFNAKEKFLLLRSVTKLVSTQTNPLKTQFANNLFVQNSINKNKKTFLEVVKPLKTFQKKTNFFPSPTHENIKSFNPSLQNGNLMSVDADYVRLNVQYGKGFSSLLNCGEVRATNCMMTEKDQIAFKSPVCDLKMKVGDYARVEDQLTTSTRIPLSGQINFITAENVLFRSVQPYLLVPGSNVVVKHGSLVQENSVLGTLMTSQSTAGDIVQGLPKVDELLEAREPQHKVLTSMHAKLSTLFSQYGKIYGLREGCELSFQKIRQFLVQEVQDVYQSQGVYIGDKHVEIIVRQMTTHVVVVDAGKTGLLPGDIVDIRRIEQLEHTGFFAGVKYRPMLLGITRAALMAESFISAASFQETKRVLSKAALEGQIDWLTGLKENVILGRLIPAGTGLY | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 113458
Sequence Length: 1011
Subcellular Location: Plastid
EC: 2.7.7.6
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Q4L5A4 | MAVFKVFFQHNKDEVIVRENTNTIYVEGETEEQVRRYLKDRNYNIEFITKLEGAHLEYEKEHSDHFNVENAQ | Function: A non-essential component of RNA polymerase (RNAP).
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 8735
Sequence Length: 72
EC: 2.7.7.6
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A5CRX2 | MVDKTQGIIDPPIDELLSKVDSKYALVIFASKRARQINDYYADLHEGSLFDNVGPLVDSTIDDKPLSVAMHEINEDKLVATPIVEPAAS | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 9769
Sequence Length: 89
EC: 2.7.7.6
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B2THR8 | MNNSMINPSIVDLLTKVGDRYSLVILTSKRAREIIEGAEPLTKVDSHKPLTIAINEVNEDIVKYEE | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 7426
Sequence Length: 66
EC: 2.7.7.6
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Q92AI2 | MLYPSIDNLLLKIDSKYSLVTVAAKRARYMQLENDKGVLPSYQSDKFVGKALEEIHAGKLVLQNDEK | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 7598
Sequence Length: 67
EC: 2.7.7.6
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A0L486 | MARVTVDDCVQHVSNRFELVILAAKRARQLAKGAEPEVSVDRDKNTVVALREIAESKLNMDDLRRMEETVVEEEVVDEVIRFEIADLAVSDDLADGDAANDLQGEEDDLGLGLDEAEDLGF | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 13372
Sequence Length: 121
EC: 2.7.7.6
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Q2W519 | MARVTVEDCVLKVPNRFELVLIAGQRARDISAGAKLTVERDNDKNPVVALREIADDTVPLDALQNALIQNLQKHVEVDEPEEDEMEGFIADRDLAFENVANEDEMIEDGMSINDTGADFDVDSGDE | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 13944
Sequence Length: 126
EC: 2.7.7.6
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Q0APB9 | MARVTVEDCIEKIPNRFRLVLMAAHRARNISAGSELTIDRDNDKNPVVALREIADETLDMDSLKDSLVNGLQRVLPSEDEEDAAREERGQQMEALPAPPVELDEAEMLKALQNDRDGAPDGRL | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 13706
Sequence Length: 123
EC: 2.7.7.6
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A1TYB4 | MARVTVEDCLENVDNRFQLVMLATKRARQIATKGAEPMVAEENDKPTVIALREIAEGKVTRDLLLEEDDD | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 7886
Sequence Length: 70
EC: 2.7.7.6
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Q9MUL7 | MRNKIPYDSKKILYDSELLLNSASNRYILTMKVANRANLRRYEEFETMNHSSIKPIARTIIEMVDDKNFLVVKKK | Function: May be involved in RNA polymerase activity.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 8907
Sequence Length: 75
Subcellular Location: Plastid
EC: 2.7.7.6
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Q606J4 | MARITVEDCLDKVENRFQLVLLASKRARVLARHPEEAKVTWDNDKPTVVALREIAEGHITPAYMKEKVKTDRYPIERPMPAPRDDLADLDDDI | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 10711
Sequence Length: 93
EC: 2.7.7.6
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C4XRE2 | MARITVEDCLEKINNRFLIVQMAIKRVHQYREGYDPLVECKNKEVVTALREIAAGEVMPADSIEEAGVFLPATK | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 8363
Sequence Length: 74
EC: 2.7.7.6
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Q1GSQ7 | MARVTVEDCVDKVPNRFDLVLLSAHRAREISGGSELTVDRDRDKNPVVALREIAEQTIRPKDLHEALVGSLQKVVIDDDDTPDEISSISRSAEALRLTAAAPPRSPAGGGGDFE | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 12317
Sequence Length: 114
EC: 2.7.7.6
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Q6XPR3 | MAQLLNSILSVIDVFHKYAKGNGDCALLCKEELKQLLLAEFGDILQRPNDPETVETILNLLDQDRDGHIDFHEYLLLVFQLVQACYHKLDNKSHGGRTSQQERGQEGAQDCKFPGNTGRQHRQRHEEERQNSHHSQPERQDGDSHHGQPERQDRDSHHGQSEKQDRDSHHSQPERQDRDSHHNQSERQDKDFSFDQSERQSQDSSSGKKVSHKSTSGQAKWQGHIFALNRCEKPIQDSHYGQSERHTQQSETLGQASHFNQTNQQKSGSYCGQSERLGQELGCGQTDRQGQSSHYGQTDRQDQSYHYGQTDRQGQSSHYSQTDRQGQSSHYSQPDRQGQSSHYGQMDRKGQCYHYDQTNRQGQGSHYSQPNRQGQSSHYGQPDTQDQSSHYGQTDRQDQSSHYGQTERQGQSSHYSQMDRQGQGSHYGQTDRQGQSSHYGQPDRQGQNSHYGQTDRQGQSSHYGQTDRQGQSSHYSQPDKQGQSSHYGKIDRQDQSYHYGQPDGQGQSSHYGQTDRQGQSFHYGQPDRQGQSSHYSQMDRQGQSSHYGQTDRQGQSSHYGQTDRQGQSYHYGQTDRQGQSSHYIQSQTGEIQGQNKYFQGTEGTRKASYVEQSGRSGRLSQQTPGQEGYQNQGQGFQSRDSQQNGHQVWEPEEDSQHHQHKLLAQIQQERPLCHKGRDWQSCSSEQGHRQAQTRQSHGEGLSHWAEEEQGHQTWDRHSHESQEGPCGTQDRRTHKDEQNHQRRDRQTHEHEQSHQRRDRQTHEDKQNRQRRDRQTHEDEQNHQR | Function: Involved in the cornified cell envelope formation. Multifunctional epidermal matrix protein. Reversibly binds calcium.
PTM: Potential substrate of transglutaminase. Some arginines are probably converted to citrullines by peptidylarginine deimidase.
Sequence Mass (Da): 90731
Sequence Length: 784
Domain: Can be divided into a N-terminal domain with significant homology to S100-like calcium-binding proteins, a central domain containing a series of short tandem repeats, and two flanking segments with low homology to the consensus sequences of the central repeats.
Subcellular Location: Secreted
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Q9C5Z6 | MIAEVAAGGALGLALSVLHEAVKRAKDRSVTTRFILHRLEATIDSITPLVVQIDKFSEEMEDSTSRKVNKRLKLLLENAVSLVEENAELRRRNVRKKFRYMRDIKEFEAKLRWVVDVDVQVNQLADIKELKAKMSEISTKLDKIMPQPKFEIHIGWCSGKTNRAIRFTFCSDDS | Function: Disease resistance (R) protein that induces localized, salicylic acid-dependent defenses . Confers resistance to powdery mildew (e.g. Erysiphe cichoracearum UCSC1) .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19973
Sequence Length: 174
Subcellular Location: Membrane
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Q9RRH3 | MPLTPGTLLAGRYELLALLGEGGSAQVYRAQDGLLGREVALKVMHDYLPESDRSRFLREVRTLARLTHPGVVPVLDLGQEPEAGRPFFTMPLLTGGPITRLGPLEDAPGPLARFLTAAAFASRALHHVHSHGIVHRDLTPGNVLLDDTGLPRIMDFGLVALSEQTRHLTRSGVTLGTPAYMAPEQAKGGGVDARSDLYALGAVLYRVACGSPPFVGDSDQSVLYQHVYEPVPDPRDLNPAVPDAVARVLLWLLAKRADRRPQSGAALAHLWALARRDLWTTHARGQYRGGRARTGEHPDGPARVSDMQELWSVALPGEVTWPAAVVGEGDLVAVGTRGGQLVLTHTSGRPFATYAARDEVTAPATLIGGHVLYGAWDGTLRRVELQSGSEVWRHQARAEFTGAPTVWGGRLLAPSRDGHLHALSLRTGELAWAYRAGGSLAASPLVWAGAALQCDETGWLHALDARSGTPLWKVEVGTVHATPALLPGPPGTATLVIATWEGEVHAIGLEVQNGRAALAGEDAIRWTYDVEDEVWASPALTALDLPPDSGAAPDASAAPGGVVVVAGWGGKVRGLRLADGEDLWERTLDGRVTASPVISAGLVFLATEGGELLALDVRNGEVRWTCRERSGVQATPLAASGTLYVAFMDGTLRAYRNAHPEWRSEQEG | Function: Plays an important role in radiation resistance and DNA double-strand break (DSB) repair. Involved in transcriptional regulation of genes important for bacterial stress response. Phosphorylates PprA in vitro.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 71126
Sequence Length: 668
Domain: Contains an N-terminal catalytic kinase domain and a C-terminal PQQ binding domain.
EC: 2.7.11.1
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Q9FT74 | MKDQDLELEKVRLISLATKLGFDEDSAKKCLDRFVDLYGDDGRDFITVELCGDDFLAALADFEEGTEEWDDIQAIESEAQGNLAEMFDKSTNPSDNGFDTDDDDDDSRVEVHVIEDSPEPKKKPEIVELDSSSDLEDVETRFKVPRRSQTCSRSMDYSMEDSVSTISGRKPSVQISNKDHETPSYEELQALDDLEFANLVIFGNKVFRPLQHQACRASMERKDCFVLMPTGGGKSLCYQLPATLKAGVTIVISPLLSLIQDQIVALNLKFGIPATFLNSQQTSSQAAAVLQELRRDNPSCKLLYVTPEKIAGSSSFLETLRCLDRKGLLAGFVVDEAHCVSQWGHDFRPDYRELGCLKQNFPRVPVMALTATATESVCQDVLKSLRIPRAPVLKMSFDRINLKYEVIVKTKEPLKQLQELLRDRFKDQSGIVYCLSKSECVDVAKFLNEKCKVKTVYYHAGVPAKQRVDVQRKWQTGEVRIVCATIAFGMGIDKADVRFVIHNTLSKAVESYYQESGRAGRDGLQAQCICLYQKKDFSRVVCMLRNGQGRNMDRFKSAMAQAKKMQQYCELKTECRRQMLLEYFGESFDRMICKSSLNPCDNCERS | Function: 3'-5' DNA helicase that may play a role in the repair of DNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 68501
Sequence Length: 606
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q85FU7 | MQNMNEQQEQWQERVIQIRRVAKVVKGGKKLSFRVLVVVGNLNGCVGVGMGKAADVMSAVTKAVVDAKKQLINITLTPTNSIVHASQGRFSAAVVFLKPAASGSGVIAGGAVRSVMELAGIQNVLSKQLGGSNPLNNAKAALLALKSSSANAR | Function: With S4 and S12 plays an important role in translational accuracy.
Sequence Mass (Da): 15907
Sequence Length: 153
Domain: The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.
Subcellular Location: Plastid
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P40389 | MILEDTDLPLSHEQPSYSQIKDVLDKIPTGEHLWDLPKYEEKIILNWLIKLLATNLEWITVEEERDYLVSTICERIAERSGRLAAPTRKREFSLSNGVSVVLREPTMTYNTLGFKTWGSAPLLSANLPKWEDLSNSINALELGAGTGLVGISAAIQLGWQVVCTDLPDIVENMQYNVDYNSELIQQYAGSVSCHVLDWMNPPDDDNRPSWLIKPFQRIIASDCIYETHFGELAIALFRKYLAKDGIVITEYPLRETHLEEIGVFEKGMDAAGFERQMGEEIGEEDFGSLYPVTCRWSRWKYHG | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 2 and elongation factor 3A.
Sequence Mass (Da): 34534
Sequence Length: 303
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q12167 | MAQNFGKIPSHKSYVLSLYRTVLRNIPKCCHSYAFQYEIKKTLSIQLFKHKHDKSSWSVYTLLNEFSLLNNCLLEGKLQEIKNLMKPLKKMKKQLKTTKILNSLTSLGDVKTNDPEEVRRFHVLSAYIKRKQDLGLLPAYIPKTYQHKLLLPLALNEHACLKLFHIQQKLKNGPPSAGLSYTKEGRNQIWFVRSPINKGRQQSKKLGILIRKERKDSQKNIDNLNFCEINAAWALHEAIWEEYLESKKIIKVNLPKYLEYAANIPKSTKCNPSSQYQKVKEWVDPVREIMFELHSKSFQRVEYFNKYKEKLLKNGGQLAYFDKKSKEMYAKRLTLFRKMSKETLPYVTLFIEGRDLPSVLAKYGF | Function: Essential for respiratory growth and required for mitochondrial protein synthesis. Required for vacuolar acidification.
PTM: N-glycosylated. Glycosylation is important for correct localization of the protein.
Sequence Mass (Da): 42829
Sequence Length: 365
Subcellular Location: Mitochondrion
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Q0CIQ3 | MSKNSSRDSSPEEVSPDTETPSTTTAPKTFRELGVIDSLCEACEELGYTAPTPIQERCIPIALEGRDLIGLAETGSGKTAAFVLPMLQALMDKPQQFHSLILAPTRELAQQIAHTVEALGARISVRCTLLIGGMDMISQAIALGKKPHVIVATPGRLLDHLENTKGFSLRTLKYLVLDEADRLLDLDFGPILDKLLRLLPKRKTYLFSATMSSKVESLQRASLSDPVRVSVSTKNQTASKLLQSYLFIPHKFKDFYLVYLLNERAGQMGIIFTRTVHETQRLSIMLRNLGFPAIPIHGQLSQSARLASLNKFRARSRNLLIATDVAARGLDIPAVDYVLNYDLPQDSKTYIHRVGRTARAGKSGIAFSFVTQYEVELWLRIEDALGKKVEEYKPEKDEVMIFAERVNDAQRVAALTMRDMQDKDNKGRGPRNRKRTRDDLDQDDG | Function: ATP-dependent rRNA helicase required for pre-ribosomal RNA processing. Involved in the maturation of the 35S-pre-rRNA and to its cleavage to mature 18S rRNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 49698
Sequence Length: 445
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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P50943 | MSMKSHLELFKQKKSTAYILLTVLFGIGWATLDLPVMVAMNIRPSISMRPIKPYISWLDSLLKPLPFNSAFGTNSTAHVDLREFLLFIGLNTSPCVSETIAIFLVCCFDRSIFIATEYLFLILLPLRGLCHQFCEQKYVETI | Function: Identified in a screen for mutants with decreased levels of rDNA transcription.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16168
Sequence Length: 142
Subcellular Location: Membrane
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Q4V398 | MCKMEKFLYHRKLWEMNVKLLGESKVEKLKNSFVSRPRMSLWMIRAVTVLLLWSCFVHLMALGEMWGPRLFKGWPSCFNHHQLSTAAEMTSLPTKIALPPKRVYVNNGYLMVSCNGGLNQMRAAICDMVTVARYMNVTLIVPELDKTSFWNDPSEFKDIFDVDHFISSLRDEVRILKELPPRLKKRVELGVYHEMPPISWSNMSYYQNQILPLVKKHKVLHLNRTDTRLANNGLPVEVQKLRCRVNFNGLKFTPQIEELGRRVVKILREKGPFLVLHLRYEMDMLAFSGCSHGCNPEEEEELTRMRYAYPWWKEKVINSELKRKDGLCPLTPEETALTLTALGIDRNVQIYIAAGEIYGGQRRMKALTDAFPNVVRKETLLESSDLDFCRNHSSQMAALDYLVALESDIFVPTNDGNMARVVEGHRRFLGFKKTIQLNRRFLVKLIDEYTEGLLSWDVFSSTVKAFHSTRMGSPKRRLVIPNRPKEEDYFYANPQECLQLLDEPLRVI | Function: Glycosyltransferase involved in the formation of rhamnogalacturonan I (RG-I) oligosaccharides in the seed coat mucilage, which is a specialized cell wall with abundant RG-I . Transfers the rhamnose residue from UDP-beta-L-rhamnose to RG-I oligosaccharides . Prefers RG-I oligosaccharides with a degree of polymerization of 5 or larger than 5 . Does not act on oligosaccharides with a degree of polymerization of 4 or smaller than 4 . Does not require metal ions for its activity .
Catalytic Activity: alpha-D-galacturonosyl-[(1->2)-alpha-L-rhamnosyl-(1->4)-alpha-D-galacturonosyl](n) + UDP-beta-L-rhamnose = [(1->2)-alpha-L-rhamnosyl-(1->4)-alpha-D-galacturonosyl](n+1) + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 59041
Sequence Length: 508
Pathway: Glycan metabolism; pectin biosynthesis.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.351
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P38192 | MILFKNLVFLPSILIGYISIRVSLLVWVNWVLVWSSCFQVAFIFSLWYFILSIYTFFYSKKIKQIISYEPSYFVFSYRAIDLCPERVLLYFFCIFNNVVFPML | Function: Identified in a screen for mutants with decreased levels of rDNA transcription.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12447
Sequence Length: 103
Subcellular Location: Membrane
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Q6E279 | MSVVVGDRSESTLMRSDYKAPPSQAIPKARLQVWFFRVCSCILVWTCLIQLFWHSQIFTGLTNHISRFSLPVQSVPLPPPLPPRNYTSNGILLVSCNGGLNQMRAAICDMVTVARLLNLTLVVPELDKKSFWADTSDFEDIFDIKHFIDSLRDEVRIIRRLPKRYSKKYGFKLFEMPPVSWSNDKYYLQQVLPRFSKRKVIHFVRSDTRLANNGLSLDLQRLRCRVNFQGLRFTPRIEALGSKLVRILQQRGSFVALHLRYEMDMLAFSGCTHGCTDEEAEELKKMRYAYPWWREKEIVSEERRVQGLCPLTPEEAVLVLKALGFQKDTQIYIAAGEIFGGAKRLALLKESFPRIVKKEMLLDPTELQQFQNHSSQMAALDFIVSVASNTFIPTYYGNMAKVVEGHRRYLGFKKTILLDRKRLVELLDLHNNKTLSWDQFAVAVKDAHQGRRMGEPTHRKVISVRPKEEDYFYANPQECIS | Function: Glycosyltransferase involved in the formation of rhamnogalacturonan I (RG-I) oligosaccharides in the seed coat mucilage, which is a specialized cell wall with abundant RG-I (By similarity). Transfers the rhamnose residue from UDP-beta-L-rhamnose to RG-I oligosaccharides .
Catalytic Activity: alpha-D-galacturonosyl-[(1->2)-alpha-L-rhamnosyl-(1->4)-alpha-D-galacturonosyl](n) + UDP-beta-L-rhamnose = [(1->2)-alpha-L-rhamnosyl-(1->4)-alpha-D-galacturonosyl](n+1) + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 55631
Sequence Length: 481
Pathway: Glycan metabolism; pectin biosynthesis.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.351
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Q6NQ51 | MEVRSESNITQARSDKLPLPPAVPKPRVQVWFVRVCSSILVWTCLVQLFAAGELWHSRIFTGLTNQISRFSAPVEPVPLPPPLPPPRNYTSNGILLVSCNGGLNQMRSAICDMVTVARLLNLTLVVPELDKTSFWADPSGFEDIFDVRHFIDSLRDEVRILRRLPKRFSRKYGYQMFEMPPVSWSDEKYYLKQVLPLFSKHKVVHFNRTDTRLANNGLPLSLQWLRCRVNFQGLKFTPQLEALGSKLVRILQQRGPFVALHLRYEMDMLAFSGCTHGCTEEEAEELKKMRYTYPWWREKEIVSEERRAQGLCPLTPEEVALVLKALGFEKNTQIYIAAGEIYGSEHRLSVLREAFPRIVKKEMLLESAELQQFQNHSSQMAALDFMVSVASNTFIPTYDGNMAKVVEGHRRYLGYKKTILLDRKRLVELLDLHHNKTLTWDQFAVAVKEAHERRAGAPTHRRVISDKPKEEDYFYANPQECLCEGTNCHDLFGHRNLTH | Function: Glycosyltransferase involved in the formation of rhamnogalacturonan I (RG-I) oligosaccharides in the seed coat mucilage, which is a specialized cell wall with abundant RG-I (By similarity). Transfers the rhamnose residue from UDP-beta-L-rhamnose to RG-I oligosaccharides .
Catalytic Activity: alpha-D-galacturonosyl-[(1->2)-alpha-L-rhamnosyl-(1->4)-alpha-D-galacturonosyl](n) + UDP-beta-L-rhamnose = [(1->2)-alpha-L-rhamnosyl-(1->4)-alpha-D-galacturonosyl](n+1) + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 57571
Sequence Length: 499
Pathway: Glycan metabolism; pectin biosynthesis.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.351
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Q3E7X9 | MDNKTPVTLAKVIKVLGRTGSRGGVTQVRVEFLEDTSRTIVRNVKGPVRENDILVLMESEREARRLR | Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
PTM: N-terminally acetylated by acetyltransferase NatB.
Sequence Mass (Da): 7592
Sequence Length: 67
Subcellular Location: Cytoplasm
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P62081 | MFSSSAKIVKPNGEKPDEFESGISQALLELEMNSDLKAQLRELNITAAKEIEVGGGRKAIIIFVPVPQLKSFQKIQVRLVRELEKKFSGKHVVFIAQRRILPKPTRKSRTKNKQKRPRSRTLTAVHDAILEDLVFPSEIVGKRIRVKLDGSRLIKVHLDKAQQNNVEHKVETFSGVYKKLTGKDVNFEFPEFQL | Function: Component of the small ribosomal subunit . The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell . Required for rRNA maturation . Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome .
PTM: Phosphorylated by NEK6.
Sequence Mass (Da): 22127
Sequence Length: 194
Subcellular Location: Cytoplasm
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P62241 | MGISRDNWHKRRKTGGKRKPYHKKRKYELGRPAANTKIGPRRIHTVRVRGGNKKYRALRLDVGNFSWGSECCTRKTRIIDVVYNASNNELVRTKTLVKNCIVLIDSTPYRQWYESHYALPLGRKKGAKLTPEEEEILNKKRSKKIQKKYDERKKNAKISSLLEEQFQQGKLLACIASRPGQCGRADGYVLEGKELEFYLRKIKARKGK | Function: Component of the small ribosomal subunit . The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell . Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome .
Location Topology: Lipid-anchor
Sequence Mass (Da): 24205
Sequence Length: 208
Subcellular Location: Cytoplasm
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Q8WXG1 | MWVLTPAAFAGKLLSVFRQPLSSLWRSLVPLFCWLRATFWLLATKRRKQQLVLRGPDETKEEEEDPPLPTTPTSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQDRGEYLGKLVRFCKVELRLPSVSIVSNGSLIRERWFQNYGEYLDILAISCDSFDEEVNVLIGRGQGKKNHVENLQKLRRWCRDYRVAFKINSVINRFNVEEDMTEQIKALNPVRWKVFQCLLIEGENCGEDALREAERFVIGDEEFERFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCRKGRKDPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYIWSKADLKLDW | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Interferon-inducible antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon . Catalyzes the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) via a SAM-dependent radical mechanism . In turn, ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple viruses and directly inhibits viral replication . Therefore, inhibits a wide range of DNA and RNA viruses, including human cytomegalovirus (HCMV), hepatitis C virus (HCV), west Nile virus (WNV), dengue virus, sindbis virus, influenza A virus, sendai virus, vesicular stomatitis virus (VSV), zika virus, and human immunodeficiency virus (HIV-1) . Promotes also TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating 'Lys-63'-linked ubiquitination of IRAK1 by TRAF6 . Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins.
Catalytic Activity: AH2 + CTP + S-adenosyl-L-methionine = 3'-deoxy-3',4'-didehydro-CTP + 5'-deoxyadenosine + A + H(+) + H2O + L-methionine
PTM: Acetylated by HAT1. HAT1-mediated acetylation of Lys-197 in turn recruits UBE4A that stimulates RSAD2 polyubiquitination leading to proteasomal degradation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42170
Sequence Length: 361
Domain: The N-terminal region (1-42) is necessary for its localization to the endoplasmic reticulum membrane and lipid droplet.
Subcellular Location: Endoplasmic reticulum membrane
EC: 4.2.-.-
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Q8CBB9 | MGMLVPTALAARLLSLFQQQLGSLWSGLAILFCWLRIALGWLDPGKEQPQVRGEPEDTQETQEDGNSTQPTTPVSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGEYLDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRRWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENSGEDALREAERFLISNEEFETFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYVWSKADLKLDW | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Interferon-inducible antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Catalyzes the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) via a SAM-dependent radical mechanism. In turn, ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple viruses and directly inhibits viral replication. Therefore, inhibits a wide range of DNA and RNA viruses (By similarity). Promotes also TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating 'Lys-63'-linked ubiquitination of IRAK1 by TRAF6. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins (By similarity) .
Catalytic Activity: AH2 + CTP + S-adenosyl-L-methionine = 3'-deoxy-3',4'-didehydro-CTP + 5'-deoxyadenosine + A + H(+) + H2O + L-methionine
PTM: Acetylated by HAT1. HAT1-mediated acetylation of Lys-198 in turn recruits UBE4A that stimulates RSAD2 polyubiquitination leading to proteasomal degradation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41524
Sequence Length: 362
Domain: The N-terminal region (1-43) is necessary for its localization to the endoplasmic reticulum membrane and lipid droplet.
Subcellular Location: Endoplasmic reticulum membrane
EC: 4.2.-.-
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O93384 | MFLQRCMSFLQCIFAAVLAWIGVRGQQVHGASQFSSTGKVNPATIKVVNNVISQASATPSSVNYHFTRQCNYKCGFCFHTAKTSFVLPIEEAKRGLQLLKESGLEKINFSGGEPFIHDRGDFLGKLVQYCKHDLQLPSVSIVSNGSMIREKWFQTYGEYLDILAISCDSFDEDTNQTIGRAQGRKSHLDNLFKVRDWCRKYKVAFKINSVINTFNVDEDMRENITELNPVRWKVFQCLLIDGENAGENSLREAERFLISDQQFQDFLERHSSISCLVPESNQKMRDSYLILDEYMRFLDCREGRKDPSKSILDVGVEEAIQFSGFDEKMFLKRGGKYVWSKADMRLEW | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Interferon-inducible iron-sulfur (4FE-4S) cluster-binding antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40002
Sequence Length: 348
Subcellular Location: Endoplasmic reticulum membrane
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P46187 | MIKEWATVVSWQNGQALVSCDVKASCSSCASRAGCGSRVLNKLGPQTTHTIVVPCDEPLVPGQKVELGIAEGSLLSSALLVYMSPLVGLFLIASLFQLLFASDVAALCGAILGGIGGFLIARGYSRKFAARAEWQPIILSVALPPGLVRFETSSEDASQ | Function: May play a role in reduction of the SoxR iron-sulfur cluster. May work together with the RsxABCDGE complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16639
Sequence Length: 159
Subcellular Location: Cell inner membrane
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P0AEH2 | MLSFLWDLASFIVALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDKLGTEYVIALIPLGGYVKMLDERAEPVVPELRHHAFNNKSVGQRAAIIAAGPVANFIFAIFAYWLVFIIGVPGVRPVVGEIAANSIAAEAQIAPGTELKAVDGIETPDWDAVRLQLVDKIGDESTTITVAPFGSDQRRDVKLDLRHWAFEPDKEDPVSSLGIRPRGPQIEPVLENVQPNSAASKAGLQAGDRIVKVDGQPLTQWVTFVMLVRDNPGKSLALEIERQGSPLSLTLIPESKPGNGKAIGFVGIEPKVIPLPDEYKVVRQYGPFNAIVEATDKTWQLMKLTVSMLGKLITGDVKLNNLSGPISIAKGAGMTAELGVVYYLPFLALISVNLGIINLFPLPVLDGGHLLFLAIEKIKGGPVSERVQDFCYRIGSILLVLLMGLALFNDFSRL | Function: A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49071
Sequence Length: 450
Domain: The 2 circularly premutated PDZ domains act to negatively regulate protease action on intact RseA.
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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D0ZKX9 | MLSILWNLAAFIIALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDRYGTEYVIALIPLGGYVKMLDERAEPVAPELRRHAFNNKTVGQRAAIIAAGPVANFIFAIFAYWLVFIIGVPGVRPVIGEITPNSIAAQAQIAPGTELKAVDGIETPDWDAVRLQLVSKIGDQQTTVSVAPFGSDQRQDKTLDLRHWAFEPDKQDPVSSLGIRPRGPQIEPVLSEVQANSAASKAGLQAGDRIVKVDGQPLTQWMKFVTFVRDNPGKPLALEIERQGSALSLTLTPDTKSVNGKAEGFAGVVPKIIPLPEEYKTIRQYGPFSAILEATDKTWQLMKLTVSMLGKLITGDVKLNNLSGPISIAQGAGMSAEFGVIYYLMFLALISVNLGIINLFPLPVLDGGHLLFLAIEKLKGGPVSERVQDFSYRIGSILLVLLMGLALFNDFSRL | Function: A site-2 regulated intramembrane protease that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49184
Sequence Length: 450
Domain: Deletion of the PDZ domains leads to dis-inhibition of protease activity and almost complete loss of RseA even under non-inducing conditions.
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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Q8ZH59 | MMSILWSLAAFIVALGILITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDRQGTEYVIALIPLGGYVKMLDERVEAVAPELRHQSFNNKTVLQRAAIVSAGPIANFLFAIVAYWLVFIIGVPSVRPVIGDISPQSIAAQANISSGMELKSVDGIETPDWDSVRLALISRIGDKQMQVGVAPFGSDNVVEKTLDLRQWQFEPDKQDPVVALGIIPRGPQIESVLAEVQPGSAAQKAGLQAGDRIVKVNGQLLDRWQTFVLQVRDNPGQPLVLDIERESTPLSLTLIPDTKSVGENRSEGFAGVVPKVIPLPDEYKTIRQYGPFTAVYQAGDKTWQLMRLTVSMLGKLITGDVKLNNLSGPISIAQGAGLSAEYGLVYYLMFLALISVNLGIINLFPLPVLDGGHLLFLAIEKLKGGPVSERVQDFSYRIGSILLVLLMGLALFNDFSRL | Function: A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49429
Sequence Length: 451
Domain: The 2 circularly premutated PDZ domains act to negatively regulate protease action on intact RseA.
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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Q87VI5 | MAKRQLNRRQNWRIEKIQGERAARAAKRESVTLETLEGGDLGPEQTGLVIAHFGVQVEVEAQEGEDVGKVFRCHLRANLPALVTGDRVVWRAGNQGIGVIVAQLPRTTELRRPDSRGQLKPVAANVDLIVIVFAPMPEPHANLIDRYLVAAEHAGIHPLLLLNKADLIDEQNAPALNALLAVYRTLGYPVLEVSAHQGDGMQSLQSQLDGHISVFVGQSGVGKSSLVNSLLPETDTRVGPLSEVSGQGTHTTTTARLFHFPRGGDLIDSPGIREFGLGHVSRADVEAGFIEFNDLIGTCRFRDCKHDREPGCALLKGLEDGRVQQQRMNSYRSIIASLPQDSY | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
Sequence Mass (Da): 37444
Sequence Length: 343
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q8Y0V3 | MTRGKPGRAGHDRRHASTGEHGLVIAAHGRHYLVERKGGGLLQCFPRGKRSECAVGDRVIFEATAVDQGVVVRVEERRNLLHRSDQFKSKQLAANIDQVLIMLGTEPGFSEDLLGRALVAAESLGITPLILLNKIDLTARLETARARLALYRALGYAVVELSVHAAPEAAHAVLAAHVAGRSSILIGQSGMGKSSLLNLLIPGVDAQTREISEKLDSGKHTTTFTRLYHLPSGWGHGGTLIDSPGFQEFGLHHLTEGMLERAFPEFRPRLTECRFYNCRHLQEPGCGILGAMAEGKIDPRRHALYAQLLHESEQQKPW | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
Sequence Mass (Da): 34854
Sequence Length: 318
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q98JM4 | MPLVEAVTASSPSLADLGWSEFFGDQLEASDANLIPTRIAMVHRDRLSGLSQTGQTDLSLAPQATTGDYAVGDWVLVEPHSHLVQRRLTRKTVLERRVQGGRGPQLAAANVDTLFIVTSCNADFNIARLERYLALANEAGTTPVILLTKADTAEDAEAYRKQAAALQRELAVVTLNPRIPGAASALAAWCGAGQTVALIGSSGVGKSTLVNTLAGSAQQSPQQTGAIREHDAKGRHTTTARSLHAIAGGGWVIDTPGMRTLQVSDVGYGIDTLFAEITELAPLCKFRDCTHVHEPGCAVQAALKAGTLDPERLARWRKLSDENQHNTPVQSGPRGAKSPAGRGKRR | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
Sequence Mass (Da): 36745
Sequence Length: 346
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q7UUZ6 | MSVDEDNLLQGRVLSVHGLQSKVLGDNGVLYACAVRQVLKSLSTSQRNVIVAGDRVWFRSESRDGVSLKSEADGMIERVEPRTGMISRTSRGRQHVLVSNIDAMLIIASAEQPGIKPALIDRMILTAHQCQIEPIVIINKVDLIDLVDLQPLIGVYSSLGYRVLPTSAETGQNVAYLRALLKDRQTALAGQSGVGKSSLLNAVQPGLGLAIGAVSSDNDKGKHTTTASQLIPLADGGAVFDTPGIRQFQLWDISAGEVAGLMPDLRPYVSGCRYPDCLHLAEDDCAVKTAVADARIDARRYDAYCHLLEEELM | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
Sequence Mass (Da): 33789
Sequence Length: 313
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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B8I262 | MQLGIILKGIGGFYYVKQEKTEDIFECKPRGVFRKNSVTPLPGDRVGFSIIDGDKKLGNIDEILPRSSELVRPAVANVDQIAIIVAAKAPNPDYMLLDKLLITAETRNIRVLICVNKIDLDDDTAKIVRNAYSPAGYDVIEISSVRNIGYKRLKEELKGHITVFAGQSGVGKSTILNHIMESWVMETGSVSNKIERGKHTTRHAELLELKYGGYVADTPGFSSFEIIDIPYNQLERYYPEFLPYINTCRFNSCSHITEPGCRVIEALERSEIDNNRYQRYIQLYKALKDIPQYKGKKTESRRVIK | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
Sequence Mass (Da): 34583
Sequence Length: 305
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q21H92 | MAKRRLSKRQVDRIRERQSQRLDTSVAAPDGKQLGSEQAGLVIAHHGKQVQVETLDNSDDSPRRLRCHLRATLGSVVTGDRIVFQEDDSSGIIVAIQPRSSTLVRPDSYGKLKPVAANVDQLLITIACAPEPFSGLIDRYLAVAENLHIRPVLLFNKLDLLQSDEIDSAIANKVAKLRTLYTSLGYRCIDTCAKNGDGLDELRNTLQDNTSVFVGQSGVGKSSIIKKLLPDQEIAIGALSDAIDKGRHTTTHSELFHFPFGGDCIDSPGIREFGLWHLSPKEVTYGFIEIRDIAGLCKFRDCSHTHEPSCAVLNAVEDGSLHPERYENFQRIVQSLDDVNMQG | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
Sequence Mass (Da): 37866
Sequence Length: 343
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
A8EQW4 | MEKVKAKKQYGQNFLKDSTILDKIIQSMPNNNNHIVEIGPGLGDLTKNLVKYKDLTAYEVDTDLIGILKSKFAIEIEKGNLKLIHTDVLEAWDKLKNLHDGKYDLIANLPYYIATNIILRAFEDELCEHIIVMVQKEVAEKFTAKTNDKEYSSLGIITELISINSKILFDVPAEAFDPPPKVTSSILYIKKDMSKSLDKDFNKFLKACFIQPRKKLSKNLTTIFDKNIIFEIYKELNINDNVRPHEVSSSLYSQMYTKVKNGRNK | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 30411
Sequence Length: 265
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
A6TJK9 | MDKIVSPSKTKAIVEKYKFRFSKSLGQNFLIDQNILEDIVDGADIQPDDCVIEIGPGIGTLTQFIAEKAHKVVAIEIDRNLIPILKHTLADYQNVEVINQDVLKVDLHQLIADKFEGKPVKVIANLPYYVTTPIVMRFLEEKVPVDSLVIMIQKEVAVRMQAGPGTKDYGALSIAVQYYCNPEILLKVPPSVFIPQPKVESIVIKLQVYPEPKVKVERDDLMFALVKDAFGKRRKTLLNALSSGLLQLSKEIVRESLEAANIDENRRGETLTIEEYATLTKEVAARQ | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 32212
Sequence Length: 287
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
Q2GK91 | MKITKYRTKKSLGQCFILDPAIAEKIVSYAGCLEQYNVIEVGPGLGIMTQSILNKEVRRLTAIEKDRRLSNIHSKLKEAHAEYDCIFEDILDVNIEQLLSQSPLKMISNLPYNISVILLLKLLPYIHRFEKLILMFQKEVADRIVAQPNTKSYSILSILVQLLCDVRKVEDFPPEIFSPSPKVYSSVIEITPLLSPRFSVDNSYFAQVLKKLFHCRRKTIRNSLKSCIKDADALFIGCNIDPNARAESLTIEQLCSLTNALKARNINII | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 30615
Sequence Length: 269
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
O67680 | MVRLKKSFGQHLLVSEGVLKKIAEELNIEEGNTVVEVGGGTGNLTKVLLQHPLKKLYVIELDREMVENLKSIGDERLEVINEDASKFPFCSLGKELKVVGNLPYNVASLIIENTVYNKDCVPLAVFMVQKEVAEKLQGKKDTGWLSVFVRTFYDVNYVMTVPPRFFVPPPKVQSAVIKLVKNEKFPVKDLKNYKKFLTKIFQNRRKVLRKKIPEELLKEAGINPDARVEQLSLEDFFKLYRLIEDSGE | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 28355
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
O28491 | MKLRKSLGQHMLVDRRVISRIVGYAELSEDDVVLEVGCGTGNLTSALLRKCSVVGIEKDPLMVKRLRERFSDFIGKGRFRLIQGDALKVDFPYFTKFVANIPYKISSPLTFKLLKTDFRLAVVMYQREFAERLCGEDNRLGVISKTYCKAEILEIVKPSSFNPPPKVESAIVRIVPEPEVFVENRELFEKFVTFAFSMRRKRMGKIVQEFRKRYGVELAVNKNLAEKRPEELGARKFAEIVVGE | Function: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Sequence Mass (Da): 28017
Sequence Length: 244
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q5P7J1 | MSEHRARKRFGQNFLSDPNIIRKIIDAIHPVPGETVVEIGPGLGAMTDPLVERLGHLHVVEIDRDLIARLHERYSPERLTIHEGDALKFDFATLGAPLRVVGNLPYNISTPLLFHLAEFAARVRDMTFMLQKEVVMRMVAEPGTEDYGRLSVMLQYRFRMGRLFDVPPGAFRPAPKVTSSIVRMVPLPAEQRTAKDEALLERVVAAAFGQRRKTLRNTLREWLDEADFPALGIDPGLRGERLTVADYVAITNYIAAKSPRALANA | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 29742
Sequence Length: 265
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
Q2NIH8 | MHHTNKKKYGQNFLTDVNLLNKIVTKASITDKNVLEIGPGKGALTKIIVPQAKNVLAYEIDATLKPFLNFENHNNVNIIYDDFLKRDLLKDFDHYFSPNSQLSLIGNLPYYITSPILFKIIDTPQINDATIMIQKEVGMRLLAQPNNKNYNALSVIIQFLFSIEKIQEVKRHMFFPTPKVDSIVIKLTKNNNILPTFLKQFIKFVKNSFKQKRKTLLNNLSCQFLLSKETIIPFFLQHHIPLQIRAEQVTLETFQKLTVKWFIFLNMS | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 31156
Sequence Length: 268
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
A6GVR5 | MEAVKAKKHLGQHFLKDESIAKDIADTLNLEGYDNVLEIGPGMGVLTKYLLAKEVTTYVIEIDTESVTYLDQNYPKLKDKIISKDFLKYNINEIFEGKQFAIIGNFPYNISTQIVFRALEYRNQIPEFAGMFQKEVAQRICEKKGTKAYGILSVLVQAFYDAEYLFTVDETVFIPPPKVKSGVLRLRRKKDYSLPCGEKLFFTVVKTAFQQRRKTLRNSLKTLNLSDILREDEVFNLRPEQLDVQQFIELTKKIEADGI | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 29870
Sequence Length: 259
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
B0TZ54 | MQYKTKAKKSLGQNFLQDENIIRKIVQLANIKKDDIVLEIGPGLGALTRYILKCSDNVNVVEFDASVIDTLLQNCQKYGEPKVFNEDFLKFDLDIVRADSQQKLKLIGNLPYNISSPILFKVIEQSDKIIDAHFMLQKEVVERIISQPNSKTYGRLSVILQYHFDCSMILNIPPEVFYPQPKVDSAILRLKPKANKLVINDYIFFENIVKQSFAQRRKTLHNNLKGILKELDIDPNTLPVDTKLRAENLSMEDFVSLVNFLK | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 30131
Sequence Length: 262
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
Q8R6B1 | MEFKHKKKYGQNFLNNKDEILNKIIEVSNIDDNDEILEIGPGQGALTSLLVERVKKITCVEIDKDLENTLRKKFSSKENYTLVMEDVLEVDLRRYINQGTKVVANIPYYITSPIINKIIENKDLIDEAYIMVQKEVGERICAKSGKERGILTLAVEYYGESEYLFTIPREFFNPIPNVDSAFISIKFYKDDRYKNKISEDLFFKYVKAAFSNKRKNIVNNLVTLGYSKDKIKEILNQIEISENERAENISIDKFIELIKIFEGR | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 30764
Sequence Length: 264
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
Q8ZTJ4 | MKRRRLAQHFLRDPSVAEYIAGLVPSGLDVIEVGPGAGALTIPLAKRSKTVYAIEIDKALAERLRGIAPPNVVIIVGDALEVEWPRADFFVSNVPYSITSPLLFKLIRHRLPAVLTIQREVAERLVARPGSEDYGRLTVAVQCFYDVEILRVLPPYVFDPPPKVYSAVVRLMPKAPCVDNFDEFEKFSAWLFSARRKTLRRLKLADSTKRVYQLTLEELVELFKRHKA | Function: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Sequence Mass (Da): 25838
Sequence Length: 228
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
O59487 | MRDRLFFLLSKYGIRPRDSIGQHFLIIEDVIEKAIETANVNENDVILEVGPGLGFLTDELAKRAKKVYTIEIDQKIIEILKKEYSWNNVKIIQGDAVRVEWPKFNKVVSNIPYKISSPFTFKLLKTDFERAVVMYQLEFALRMVAKPGSRNYSRLSLMAQALGNVEIVMKIGKGAFYPRPKVDSALVLIEPRKDKIVLNENLVKALFQHRRKTVPRALKDSIHMLGVSKDEIRGIINNVPHSNKRVFQLYPEEVKDIEEYLKKHGIIS | Function: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Sequence Mass (Da): 30906
Sequence Length: 268
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q92QZ1 | MAALDGLPPLRDVIQRHGLDAKKALGQNFLLDLNLTQKIARTAGPLEDVTVIEVGPGPGGLTRAILALGAKKVVAIERDSRCLPALAEIGAHYPGRLDIIEDDALKVDFEALADGPVRIIANLPYNVGTQLLVNWLLPGLWPPFWQSMTLMFQREVGLRIVAGADDDHYGRLGVLCGWRTKARLAFDVPPQAFTPPPKVTSTVVHLEPVEAPIPCSPAVLEKVTQAAFGQRRKMLRQSLKPLGGEALLAKAGIDPQRRAETLTVEEFCRLANCL | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 29733
Sequence Length: 274
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
Q7UIR4 | MRPVSKYGQNFLIDLNLVELIARSAEIGPSDIVLEIGTGVGSLTSIMASQAGAILTVEIDQNLFQLASEELAPFPHVKMIQGDALKNKSTFRDDIMESIREAKSRLPDDSKFMLVANLPYNVATPIVSNLLHQDPPPDRIVVTIQKELGERMVAGPGSKDYGALSIWIQATCRAEIVRILPPTVFWPRPKVDSAIVRLDVDHERGNAIPDLKYFHQTVRALFFHRRKFLRSVVISAMKGRLDKPAIDEILGRLGHGETARAEELNLEQISDLVEALRQAELANE | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 31578
Sequence Length: 284
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
Q0S4T6 | MSEAEVPPVARGQAALLGPAEVRALAEEFGVRPTKQLGQNFVHDANTVRRIVATAGVGREDTVLEVGPGLGSLTLALLDVVDKVIAVEIDPNLAARLPVTVADRAPELADRLTVVGADAMRVKPSEIPGEPTALVANLPYNVAVPVLLHLFSELPSLRTALVMVQAEVADRLAASPGSKIYGVPSVKANFFGAVRRAGAVGRAVFWPVPKVESGLVRIDRYAEPPWPVDDAHRRRVFAVIDAAFAQRRKTLRAALGGWAGSPAEAERRLLEAGIAPSARGETLDAAAFVRLAATQP | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 31277
Sequence Length: 296
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
B5ZCB6 | MNKTVIKNKLKQESFVPSKKMGQNFLLSNEIKNKIVNVANISKDDLILEIGPGWGAITELLVQKTDTLVAIELDKRLYAHLKTYIKAPNFHIINNDVLCVDLDKLILDYTNTKKNQKIKVVANLPYAISSKIVLKIIQSKLINDAYIMVQKEMAERIGAKVNTRGYNAFTVLVQLFCKTKILFQVNAKEFHPQPKVQSAVIHLENLHNKVDFDIEQVSKFLRICFLNKRKKLKNNLSNIYDIKLVNEMFIDYNLDMNLRAENIEPKMFLELFNYLNKSNNE | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 32516
Sequence Length: 281
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
Q8D3I1 | MHKPIKKLGQNFLKDKKIIKKIINFINPKYKDKIIEIGPGLGALTIPISKISKSITAIEIDKNLVYFLNKNKNIKNNLNIINIDIMKLNLKKFFSSFCDPVRIFGSLPYNISVSLMFNFIENYNKIIDMHFVIQKEVAQRILARPNNKHYGYISVIMQYYFYVEKLIDISNCAFKPIPKVQSSLIRMRPHKVCPFPFCDIDKMKVLLKSAFNQRRKMLKNSLKKYFSVEQIILYKINPKLRAENLSIENYCNLSNNMIIKK | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 30634
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
B3CPY6 | MRKFLLKPKKSLGQNFILSNEIIKRIVALAGSLKDFNVIEIGPGYGALTREILAYNPKFLLSIEKDSSLVKHHEQLLNEHQGKYRIIEADALNVVEKELVECPVKVIANLPYNISVALFLKWLNNIKFFTNLTLMFQKEVAERITAEPNSKDYGSLSVLSQLLCDIKKEFDIEPKEFFPRPKVYSSVITVKPLPTPRFAVNLETLTKLTRAVFAQRRKMLRNSLQSITSDVSTTLENAKLSGDERPESLTIEQFCLLANNIIMR | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 30082
Sequence Length: 264
Subcellular Location: Cytoplasm
EC: 2.1.1.182
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Q8PP25 | MNSSFSAPAKKSLGQHFLADRYYIDRIVQAVDPRAGQHLVEIGPGQGAITFPLLRKHGALTVIEFDRDLIAPLTEAAAPIGALRIIHRDVLSVDFTALADGTPIRLVGNLPYNISSPILFHALDHAAAVADMHFMLQKEVVDRMAAGPGSKVYGRLSVMLQAYCEVTALFVVPPGAFRPPPKVDSAVVRLVPRDPATVLINDRRRFADVVRAGFGQRRKTLRNALSAICEPAHFDAAQVRPDARAEQLEVADFIRLANVELA | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
Sequence Mass (Da): 28554
Sequence Length: 262
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
P44453 | MISLESQVLERHISFFDGKSVLFAGGISDSFPQTLASKCSSIQIWSCYFDYARTQSAVNFSVEFQGQADLIVYYWTKNKQEVNFQLIQLLAQASIGQEILIIGENRCGVRSVEKTLSPYGEIAKIDSARRCGLYHFSLQNKPHFELKNFWRTYQHSTLENLTIYSLPGVFSAAELDTGTELLLSTIDNKIKGKVLDLGCGAGVIGSMIKKRTPNAQITMTDIHAMALESARKTLSENQLQGEVYASDVFSDIEGKFDLIISNPPFHDGIDTAYRAVTELITQAKWHLNQGGELRIVANSFLPYPELLRQHFNDYQVLAQTGKFKVYSVKN | Function: Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
Catalytic Activity: guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37061
Sequence Length: 330
Subcellular Location: Cytoplasm
EC: 2.1.1.172
|
Q2SJX3 | MSQLSNPSQAFLRQRGQLSGRILLCSPPADAIAAELRQTGVEVSVLSWDHTAVNACRGAVAEEWLFTDLALPADAQWDQIALFMPKARELLDLMLSVVAPALKHAQHIWLVGEKREGVESAAKRLAKEDWDATKVDSARHCQVWSLTPPADWKPKQNDFWRAYELAQEKVDTLQLFTLPGVFSAGRLDEGTEVLLQSLPELHGRRLLDFGCGCGVIGATLKKRYPKASVELTDINLLALKSAARTAEANGVELNVYASDGLAEVQPGVDAIITNPPFHQGVKQDTRVTQQFLRDCARVLKPGGSLTLVANRFLPYPDWIEAHVGPVRVLFENSRFKVYHAVR | Function: Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
Catalytic Activity: guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37819
Sequence Length: 342
Subcellular Location: Cytoplasm
EC: 2.1.1.172
|
Q5R049 | MSAAILSMLGRQSAQPWANGSLLVIHPGGGELSALPNASAWSFHAGHAAYWKAAGRPVFCQIQPPNLSHYDGVLFLVAKEKELNQYLLEQLASLPTGTPVWFAGEKRSGIQPLMKHLPAWLQPPQKLASANHCLLFASERNEQVHQSASIEDYAKNITYELNQQQESFVTLPGVFSREHIDPATLLLLQHIKDLPKGRGMDFACGAGVIAKQLASVATELMACDVSPIAIAASEITLANEPVKTELRLADGIPDNAGQFDFIVSNPPFHTGQRTDYEIAREFISNARQHLNKQGVFRVVANRFLPWPEVIESVFGNCSVIADDGRYRVYHATCR | Function: Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
Catalytic Activity: guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36704
Sequence Length: 334
Subcellular Location: Cytoplasm
EC: 2.1.1.172
|
A6VRG3 | MNLNSTSQLLVRNEEGLVGKILFANPEDTYPLDLSRKADVYAWCQSKTYYDALLRVGFADEKLFLSEQWALEHGSDFDHIVIYQPKAKELLDYLLASVLPLLKEGGQIWLVGDNKSGVKSSMKRLEAGLDEVGKRDGAKHCLLYTGYKRRPTKPFVFEDWITTWKQEVAGQTLTLCSLPGVFGHGKLDKGTDILLNQLNQHRFMSDVASARILDFGCGDGIIALWLHNKTGARITALDDSVMALKATELTFAANQVSDAVTLIASNGLDEVKGRFNYVVTNPPFHSGVNTDYSIAESFFMMVKQHLTLNGELFVVANDFLRYPPILDAALGSHTRLYRDRGFAIYHGRQPKKK | Function: Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
Catalytic Activity: guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39511
Sequence Length: 353
Subcellular Location: Cytoplasm
EC: 2.1.1.172
|
A1U204 | MSALPNTHEVLLRNAHLLNGRPALLGVSDASLLPRCPVPGIAMTEHAGLWQILSHDTDWAGCFGYEPDRQQQGSCDTVVVFLPKARAECELRLALARYLGKPGAALVVIGEKKEGIAGAIKQFSVVAGEVVKVDSARHCQVWCGRNTQPLTEFRLTDWLSWTELSCAGVALSVAGLPGVFSLGRLDDGTRMLLETLAESPLGVDRVFDFACGAGVIGSWLHGFHQLAGKMPIRVDGTDVQAQAVFCARESYRKAGVNGEIFAADGLAVVQGNWPAVISNPPFHTGVKTDTSMTEQFLAQVAAHLAHGGELRLVANSFLPYEALIRQHIGPVEKLAQDRRFTVYRAFRKKSG | Function: Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
Catalytic Activity: guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37919
Sequence Length: 351
Subcellular Location: Cytoplasm
EC: 2.1.1.172
|
Q6D984 | MSALTPASEVILRHSDEFLSRRVLFAGDLQDTLPAQFEAASVRVHCNQYHHWQQMAKPLGDNAQYSLVADAELVADSDTLIYYWPKSKQEAEFQLCNLLSLLPVGAEIFVVGENRSGVRSAETVLSDFVELVKIDSARRCGLYHGRIDKQASFTLDDWWDEYVTEGVTVKTLPGIFSRDGLDPGSRLLLSTFEPHMKGKVLDIACGAGVLASVLAKQSPKIRLTLSDVSAAAVESSNATLAANALEGSVIASNVYSDIDGRFDMIVSNPPFHDGLQTSLQAVEMLIRGAVTHLPIGGQLRIVANAFLPYPALLDAAFGSHEVLAQTGRFKVYQATVGRPPRTGKGRRR | Function: Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
Catalytic Activity: guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37926
Sequence Length: 348
Subcellular Location: Cytoplasm
EC: 2.1.1.172
|
Q7MZN0 | MSALTPASEVILRHREQFSSHHLLFAGDIQDTLATQIDAASVRVHTNQYHHWQSLIRTLGESAWFGLVAEKAFTQGCDTLIYYWPKSKQEARFQLRSLFSVLPKGINIFIVGENRSGVRSVDKLMDGMATFRKIDSARRCSLFYGQLEHEVQFEQDNWWNSYQVENVIVNTLPGVFSQDELDVGSRLLLSTFDKPLSGNLLDIACGAGVLAAVLGKKNPELALTLSDVNAAAIASSKATLKANKLEGHVVVSNVYSNIEDKFDWIISNPPFHEGLKTSLLATDDLIRQAPNHLKPGGKLRIVANAFLPYPDLLDKTFGTHEVIAQTGKFKVYQATKKF | Function: Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
Catalytic Activity: guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37646
Sequence Length: 338
Subcellular Location: Cytoplasm
EC: 2.1.1.172
|
Q9KRY1 | MHPNISLPEPFIASMAKILPDPTQLADFIAACQRPLRKSIRVNTLKISVAEFCQRAAEKEWQLTPVPWCENGFWIDADESLVPLGNTAEHMAGLFYIQEASSMMPVSALFMGNAHYDSVLDMAAAPGSKTTQMAALMDNQGVLVANEFSASRVKVLHANIERCGIRNTALSNFDGCVFGGWLPERFDAVLIDAPCSGEGTIRKDPDAMKNWSLESIQSIANTQKALIESAFQALKVGGTLVYSTCTLSREENQQVCWHLKQTYGDAVSFESLGNLFEHASLALTEEGFLHIFPQMYDCEGFFVAKIRKLASVPTPEVNKRLGKFPFNKASHKQQAEIAQQLHKSLGIELPSDAQVWLRDNDVWLFPEALEPLLGELRFSRMGIKIAEAHKSGYRWQHQVATCLASSSASHSVELDTTQAREWFMGRDVRPEGQSGQGEVIIRYANDVIGLGKWVGNRVKNGLPRELVRDKNLF | Function: Specifically methylates the cytosine at position 1407 (m5C1407) of 16S rRNA.
Catalytic Activity: cytidine(1407) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(1407) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 52559
Sequence Length: 473
Subcellular Location: Cytoplasm
EC: 2.1.1.178
|
Q6MQY9 | MSEHFEKRRPVFLQLGFNEAALPQLKAYLDLLWSSNEELNLISRKMTYEELIDNHVIDCLLPIKDFPKDVKVAADFGSGGGLPGVIYAIQFPNVEYHLFEKSKLKQDFLNRCVSIAPNLRIHGEIPPKLEKIEVVTSRAFKPVDVILEFSRDYYKKGGKYFLLKGRKEKIDEEVALARKKFKDLKVTVQPLSSPVLEVERHLVLI | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23598
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
A0LLH7 | MRETPSPQTLRAFLNGHGIAVSPQQAEMLFEHVRLMLEWNLRSNLTRITEFDRILTAHLLDSLLPARWLPLTGKTLDVGTGAGFPGVPLKILHPETQMYLLESNRKKVSFLKVLLAGLSLPGIHVLHGRWEEPEGWFTEEDERFTAVIMRAVRVEPGHLTRLAPRVLRPGGVFASWAGSGTETALENRRTHAYPAPAETRSYELPGMSAPRRLYLWRMEG | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24850
Sequence Length: 220
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q6MMJ3 | MGRHKKPETIYDIHEANDRLADVFRNHGFDLVSHSQRQQLAHFYRLLMLNQEKENFTRLLKLRDVAIKHFIDSIIIMKYTDLQFPLLDVGTGPGFPGIPLKIMYPDQQILLGEGVQRRVEFLKHVRSEMNLKNLDILGRNINKHCVYPVRGAITRAVEDIGNTLGNVMSCLEIGGRVYFMKGPGVGPEIEAAKKDWGEYYKLVQDVAYSLPQTPHERRLVVYEKIKNMPLPEEDEGEELLMDELSNEEKRRWAKY | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29619
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
A0LHE3 | MRNGTIRYPGSDAAPGPDEMSAILRRCGIRLAPARIGQLWTYHQLLREFNPELNLTRIHNFANMVLKLYVDSLLPMNLVELPSPLMDLGTGPGMPGIPIKIAMPELEIVLAESRQKRAAFLKMAVERLKLEKVEVVGKSVGSSFEVPVKGVITRAVESVGATLERIAGCLDRDGLAIFMKGPQCDAEIGEALKRFRGEYRLWRDIHYTIPHTRNERRLVVFQRLGPPTRIRKETAMKRHGFRKIESENNDLYRDIRKLLTSRGIRKQQRALVSGSKQVHETLRDFPDDCLAWIAPGQEMPPPEGAPGHMSWYQMAPALFETLDVFGTRTPLLLIKVGEIETWDPVEGFPAGCSVLVPFQDPENVGAVIRSAAAFGAVQVILLRESAHPFHPKALRASGGAVLRMKLRNGPPLENLPENLPILPLSAEGRDITRHVFPAAFGLLPGLEGPGLPDNWRRKSFAIPICKDVESLNAATAAAIALYAWSRSGSQTKHSPAPA | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 55106
Sequence Length: 498
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q6MGL7 | MKDNQEQAAPIVYWRIDEWFPDLSPDLRTRLKTYHEELLKFNRTLNLISAKTVFVADALHFADSIMASQAIMKSNPSLDKIYDLGSGNGFPGMIFALLYPKVQVVLVEFDQKKCEFLNHVAGVLKLSNVTVENRTIESFPDGSMKYVMARGLANISKSIMMTRKVVPKGGVFYHLKSEEWGIEVGDIPTQLCSVWAPSLVGEYKLPIGAIKFSVVKTDKIA | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24819
Sequence Length: 221
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
A3DHY6 | MDEKELKLRKLLIEGASGFGVNLDDEQIDKFFAYKDVLKEWNQKMNLTAIEDDEEIILKHFIDSISICPIIKDKNLALIDVGTGAGFPGIPVKIVFPELKVKLLDSLEKRTKFLNEVIERLDLKDISTVHARAEEKGVDPDYREKYDISVARAVASLPVLLEYCLPFVKVGGCFIAMKGNSTEEVENSKKALEILGGKIEDILEFNLPFSDIKRNVIVIKKFRQTPTKYPRKSGKPSKNPLT | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 27353
Sequence Length: 242
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A9NEC5 | MLNTYITNILGIKLTEQQNGQFDAYYNLLVAYNKHTNLTRITSRDDADIKHFLDSVLISKLVDLNKVVTLCDMGAGAGFPSIPLLIVFPNIQVTIVESQIKRVQFLQELKQALGLEFNIVHDRAENFSSKNYQQFDIVTARALGELRLILEFGVPMLKVGGHFIAPKGSKFEEELTSAAHAIKVLNVELITQDLFELPLESGFRANLLFRKEKHVSGYPRPFPIIKKKPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 25982
Sequence Length: 230
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A1TI79 | MTVAADALSAPLRAGAEALGLDLSEAHLGQLLEFLALLQKWNQVYNLTAVRDPQEMLTHHLLDSLAAVAPLQRHLRGMQDLPGSAGDGAKLRLLDVGSGGGLPGVVFAICCPALDVSCVDTVAKKAAFIQQAAVSLRLRNLRGIHARVENLAGPFDVVSCRAFASLPDFVAWSQAAIAANGVWLAMKGRDPSDEITGLPPIAEVFHVEQLAVPGLDAERCIVWMRPRKGAEAGADGVGGPALP | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25501
Sequence Length: 243
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q6F9W7 | MHPFLQELKQGSQALGLDLSDEVLGLLLKYQDALVLWNKAYNLTAIRDPKEMLVKHLLDSLSILKDLPQGRLLDVGTGGGMPGMIIALCQPERNCVLLDSNGKKIRFLKQFIADLKLKNVVAVQTRVENEESIQELGKFDVITSRAFASLLDFVDAARPYMYESTIIAAMKGLVPTEEMQQLKAEFSCQVIGLQVPRLDEQRHLLLLQQIKN | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23802
Sequence Length: 212
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q1QSC0 | MTPACEARLDAGLAELGLEVDATARERLLALLALLHKWNRAYNLTAVRDPEQMVTRHLLDSASVATAVRGPRLLDVGAGAGLPGLVLAILDPSLEVTMLDGNGKKVRFQRQAVLELGLENVTPVQARVEHFTTRDFDQIVSRAFAQLATFVELTRPLLAEGGEWLAMKGRDAASELAELPPDVTLIERRDLEVPGDAAQRVLLRLRRA | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22714
Sequence Length: 208
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q97CW4 | MKYFDIMSLECKKIGIEFTEEKYGKFMRYKELLQEWNKVMNLTSIVDDEEIVKKHFIDSIKIFECEHIVKAKRIIDVGTGAGFPGLPIAIMNDDIEVVLLDSLQKRVNFLNEVIKELNLKNISTVHGRAEDFGVDKDYREKFDVAVSRAVANMAVLSEFCLPFARVGGYLVALKGPGINDEISTAKKAIKVLGGTLDKVINVEFENEDFQHNLVVIKKQNGTPKKYPRKAGKVSKNPII | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 27055
Sequence Length: 239
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A0LE46 | MENFRYEIESMLQLVGVDMDVISVDPYSDEKLAEFVSELLLWNKKINLIGKSTEKSIWSRHIAESLILLPYVQGSTVLDMGTGAGLPGLPLQIVSGSNIEMHLVEKDQKKVSFLKHVSANLNLKNIRIYNKQFTEKGFDGAPLVNVVTSRALAEINQLVAWADPCLVNGGSLVLIKGPVCKAELEKFEESDLSDKYENGEIVEYKIDSHDVNIVIIKKK | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24447
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q2WBG8 | MGPEELLTKSGVSRETLERLRLYADLLVKWQARINLVGPDTVPDLWSRHMLDSVQLFPLIKVGARRLVDLGSGAGFPGLVLAVMGAPDVHLVESDSRKCAFLREVARVTETPVTVINKRIEQVAPLGADVVTARALAPLDRLLGWAFPHLAEGGECLFLKGRGAEDELTASAKEWNITASRVPSLTDPGGLVLHLREVSRGRAQP | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22283
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q8EUW9 | MNLKDLIKLLEVKFPQIDSNEVESKITIYKNYLQQENKIHNLTRLDKEEEIYQKYFYESILNFHNDLFDNKNINLLDIGSGSGVPGIFLKILFPHINLYIVESNTKKVNFLNNLVDKLELENVFISNQRCEDYIKDKIEFFDLITCRAVAELRILLELSFPGLKINGIGFFLKSNNYLVELDNAKNISSKLKIEEEPKIETIEYDGKTFVSLKYIKKNKVNNIFPRTWKEILNNDKN | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 27880
Sequence Length: 237
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q0AKF0 | MDRETFGRETGVSRETLDGFETWRALLVETNAHTNLVGRSTLDQFWARHAMDSYQLLEHVGADVTKIADLGAGAGFPGIALALGLRDRQQAAHVTLVDSVGKKVAFLRKTIAALALDADARSVRVETLDPAEGFDLITARAFAPLNKLLGYASPLLKNRAQGLFFKGQNYRDELTEARKHWTFDCEVIPSRTSDGVILRIHEVERAN | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22890
Sequence Length: 207
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
A1U7I4 | MSYPQWPGQLRDGLAAMNLSLSDSQQQQLLAFLALLNKWNKAYNLTAVRDERVMVSRQLLDSLSILPWVTTDHLLDVGAGGGLPGIPLAIVVPEKRFTLLDSNGKKTRFLNQCVLELGLDNVEVIHGRAEDCQPDQPFTQISSRAFTALENLVTWCGGLLANDGEFLAMKGQYPDDEVAALPAGWQVESSHSLTVPGADGERHLLIVARAERHR | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23540
Sequence Length: 214
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q6F0F5 | MWTMFNNWKIFEDNLGFVPSEEIKDKLNEYYKILVEENLKYNLTRITNEEDVYEKHFLDSLLFTKETKIDNQKIIDIGTGPGFPGIVLKIFFPETDITLIDSNNKKINFLNIVIKKLNLKQIEAKHARAEELARIENEKYDIAISRAVAYLDVILELAVRFLKIQGKLILLKGPRADEEIKNSKNIDQKLKIKLTNKQSLADTGFGERINLFYEKEKSTPELYPREYAKIVKESGKK | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 27662
Sequence Length: 237
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q5ZZN1 | MYKRLVQEFFPKLDFENLEKYVNLIEFSNKNFNLTAFSGDILWKEGIFESIFTMNFIVGLVNNKENKKLKILDIGAGSGFPSIPFLITNPEIELTISESMQKRCQFLKDISEKLDLKFNLICKPVQEINPQKFDIITARAVANLEKLEKITKKIHFPKTLLAFIKGPKVFNEVQNCKNCNYKIIKVNNNINKKIFIAFKQVS | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 23434
Sequence Length: 202
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q6KH77 | MSPFQNFMILEEKQLLILMKTNSEICKELVSNPEKFNKLEQFVSLVEEWNKKINLTGFEGENLWKEGINESFFCFEKILETKNLNDFENKSWVDIGSGAGFPIIPFAIIYPKINFYIIESNSKRVRFLELVNEKLNLKIKIFNTRAENFSELKFDFVSARAVAHLDLLIKYFMKITKQDATGYFIKGPKIFEEKEEINNKKISIETLKIDKIKEKNVFVVKMNRI | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 26487
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q60CS4 | MLERGLSELGSDAGGDQRERLLRFLELLRKWNRVYSLTAIEDPCEGVRLHLLDSLSIASFLHGRRVLDVGTGPGLPGIPLAIVQPERRFVLLDCNAKKIRFVRQAVIELGLANVVPVQARIESFTDAEGFDCVLARAYASLAEIWTDAAPLLRTGGTVLALKGRRPEAELGDLPAGVAVGIHRLRVPGVEAERHLAELKPTGQDS | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22343
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q1GXM0 | MQQKLETGIRQLGLDLPAEVTEKLLAYLALLAKWNKVHNLTAVRDPEDMVTLHLLDSLSVLPHVPSGSLLDVGSGAGLPGIVLAICRPDLQVTTIDAVQKKASFMRQAKAELQIDNLQVVAGRVEQFEPEAPFDTVISRAFSEIALFVKLTRHLMAEDGLWLAMKGQMPQEELGAVALKPAKIMSLIVPGLDAQRHLVFLPARQF | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22473
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
B8IHZ7 | MSASDRDRVLAAAAVSRETAAALDLYVAQLARWQTVKNLVGPSTLPEVWTRHIADSLQLLDAAPGATRWLDLGSGAGIPGLILAIAGREARPQMQVDLVESNARKGAFLQETARLTGASARIHVSRIESVIGRFTGVEVVCARALAPLPQLLAWTAPLLKSGTIGLFPKGREAQSELTAARETWTFEADVIPSRTDSSAGIVRISSLSGQLP | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22486
Sequence Length: 212
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
A2SMF0 | MTVAPFDAKALAQGLEQGAQALRLELTAVQQQQLLQHLALIDRWNRVYNLTAVREPAQMLTQHLLDSLAVVAPLRRQTRATAIALLDVGSGAGLPGVAIAVACPEIHVSCVDTVSKKASFIRQVGVELGLTHFQALHARVESLASSNFDVITSRAFASLADFVTLTEAALAPDGVWMAMKGQVPHEEMAVLPSSIEVFHVEPLQVPGLDAERCIVWMHRKG | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23869
Sequence Length: 221
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q01NF9 | MTFAEELQQILPPDLPHRDAVIASAARHLDLIVETNQHFNLTRIVSPREAAIKHIADSVIPWRLFSGAPHVVDAGSGAGFPGIPLALVLPETRFTLLESTQKKARFIESAAADLGLANVEVRPDRAEDWLKTHRASIVTARAVAPLTRAVGLFAHALRAGARILLYKGPDAEAEIAEAASEAAKRRVHLRVVERYELPDSLGARTIVEIR | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 22915
Sequence Length: 210
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
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