ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P11305 | MAESKEARDQEMNLKEESKEEKRRNDWWKIDPQGPLESDQWCRVLRQSLPEEKIPSQTCIARRHLGPGPTQHTPSRRDRWIRGQILQAEVLQERLEWRIRGVQQAAKELGEVNRGIWRELYFREDQRGDFSAWGGYQRAQERLWGEQSSPRVLRPGDSKRRRKHL | Function: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry two recognition sequences that function as Rev responsive element (RRE), that are not present in fully spliced viral mRNAs (early transcripts). This function is essential si... |
P19032 | MAEGFAANRQWIGPEEAEELLDFDKATQMNEEGPLNPGVNPFRVPAVTEADKQEYCKILQPRLQEIRNEIQEVKLEEGNAGKMKKKRQRRRRKKKAFKKMMTDLEDRFRKLFGSPSKDEYTEIEIEEDPPKKEKRVDWDEYWDPEEIERMLMD | Function: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is es... |
Q8A011 | MADNSTILEKLDGLVARFEEISTLITDPAVIADQKRYVKLTKEYKDLDDLMKARKEYIQLLGNIEEAKNILSNESDADMREMAKEEMDNSQERLPALEEEIKLMLVPADPQDSKNAILEIRGGAGGDEAAIFAGDLFRMYAKFCETKGWKMEVSNANEGTAGGYKEIVCSVTGDNVYGILKYESGVHRVQRVPATETQGRVHTSAASVAVLPEAEEFDVVINEGEIKWDTFRSGGAGGQNVNKVESGVRLRYIWKNPNTGVAEEILIECTETRDQPKNKERALARLRTFIYDKEHQKYIDDIASKRKTMVSTGDRSAKIR... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 41662
Sequence Length: 370
Subcellular Location: Cytoplasm
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A1A0I9 | MADEQFPAAVTALEEYHNIEQQMAEPEVASNPDKMRKLGRRHAELGAIVSAYTAYKQVKDDLEAAREMASEDPDFAEEAKRLEGELPAAEEKLRTALIPRDPDDARDTIMEIKAGTGGEEAALFAGDLLRMYMRYAEKRGWSVTVQSENTTELGGVKDVQLAIRAKGTPAPEDGVWASLKYEGGVHRVQRIPVTESQGRIQTSAAGVIVFPEADEDDDEIEIDPKDLKIDIFMSSGPGGQSVNTTYSAVRMTHIPTGITVNMQDEKSQIQNRAAALRVLKSRLLAMKHEQEAAEAADMRHSQVRSLDRSERIRTYNFPEN... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 40213
Sequence Length: 362
Subcellular Location: Cytoplasm
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Q8G3P5 | MADEQFPAAATALEEYQSIEEQMASPEVVSNPDKLRKLGRRHAELGAIVGAYKAWLQVKDDLAAAQEMAGEDADFAEEAKRLEDELPGVEEKLRTALIPRDPDDARDTIMEIKAGTGGEEAALFAGDLLRMYTRYAEKRGWSVNVQSENTTELGGVKDVQIAIRAKGTPAPEDGVWASMKYEGGVHRVQRIPVTESQGRIQTSAAGVIVFPEADEDDDEIEIDPKDLKIDIFMSSGPGGQSVNTTYSAVRMTHLPTGITVNMQDEKSQIQNRAAALRVLKSRLLAMKHEQEAAEAADMRHSQVRSLDRSERIRTYNFPEN... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 40054
Sequence Length: 362
Subcellular Location: Cytoplasm
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Q8R5W0 | MINLRGVKMFDKLEEVVARYDELNKMLVSPEVLADSKKMIECNKAINEITEIVEKYKEYKKYVDDIEFIKESFKTEKDSDMKEMLNEELKEAEEKLPKLEEELKILLLPKDKNDDKNVIVEIRGGAGGDEAALFAADLFRMYSRYAERKKWKIEIIEKQDGELNGLKEIAFTIIGLGAYSRLKFESGVHRVQRVPKTEASGRIHTSTATVAVLPEVEDIQEVTVDPKDLKIDTYRSGGAGGQHVNMTDSAVRITHLPTGIVVQCQDERSQLKNREKAMKHLLTKLYEMEQEKQRSEVESERRLQVGTGDRAEKIRTYNFP... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 41864
Sequence Length: 365
Subcellular Location: Cytoplasm
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Q5FUR9 | MAFDDRLERIVARSEEVQALMSSGELTGEDFTRLSQEYAELEPVVASIQAWKSAEEQKAGAQALLDDPEMRELAQMELAEIEATLPDLQHALRLALLPKDAADERSAILEIRPAAGGDEAGLFAAELFDAYRRFSEQNGWRFEVMEYAENEVAGLKEGMATISGRSVFARLKYESGVHRVQRVPATESQGRIHTSTVTVAVLPEAEEVDVTVNDDDLRIDVYRASGAGGQHVNKTESAVRVTHMPSGIVVAMQEEKSQHKNKAKAMKILRARLYERERAQLHATRAADRKSQVGTGDRSERIRTYNFPQGRVTDHRINLT... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 39444
Sequence Length: 353
Subcellular Location: Cytoplasm
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P43917 | MKDSIIAKLESLKERYEELEALLGDVSVISDQDKFRAYSKEYSQLEEVVKCFNRWTQLNQNIEEAEILLDDPEMKEMAQMEIEESKAEIEEVEQQLQILLLPKDPNDEYNCYLEIRAGTGGDEAGIFAGDLFRMYSRYAESKRWRVEMLSANESEQGGYKEVIVKVTGEGVYGQLKFESGGHRVQRVPKTESQGRIHTSACTVAVMPELPESEMPEINPADLRIDTYRSSGAGGQHVNTTDSAVRITHIPTGIVVECQDERSQHKNKAKAMSVLASRIVQAEQERQAAEQTDMRRNLLGSGDRSDKIRTYNYPQGRVTDH... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1 (By similarity).
Sequence Mass (Da): 40917
Sequence Length: 360
Subcellular Location: Cytoplas... |
Q9X183 | MKEKKKEIEKLLARPDLTPEQMKNYGMEYAKIEEIENITNRIKETQEFIELLREEGENELEIEKYEKELDQLYQELLFLLSPEASDKAIVEIRPGTGGEEAALFARDLFRMYTRYAERKGWNLEVAEIHETDLGGIREVVFFVKGKNAYGILKYESGVHRVQRVPVTESGGRIHTSTATVAVLPEIEEKDIEIRPEDLKIETFRASGHGGQYVNKTESAVRITHLPTGIVVSCQNERSQYQNKQTALRILRARLYQLQKEQKEREISQKRKSQIGTGERSEKIRTYNFPQNRVTDHRINYTSYRLQEILDGDLDEIISKL... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1 (By similarity).
Sequence Mass (Da): 39657
Sequence Length: 342
Subcellular Location: Cytoplas... |
Q72HB8 | MLDKLDRLEEEYRELEALLSDPEVLKDKGRYQSLSRRYAEMGEVIGLIREYRKVLEDLEQAESLLDDPELKEMAKAEREALLARKEALEKELERHLLPKDPMDERDAIVEIRAGTGGEEAALFARDLFNMYLRFAEEMGFETEVLDSHPTDLGGFSKVVFEVRGPGAYGTFKYESGVHRVQRVPVTETQGRIHTSTATVAVLPKAEEEDFALNMDEIRIDVMRASGPGGQGVNTTDSAVRVVHLPTGIMVTCQDSRSQIKNREKALMILRSRLLEMKRAEEAERLRKTRLAQIGTGERSEKIRTYNFPQSRVTDHRIGFT... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 40093
Sequence Length: 354
Subcellular Location: Cytoplasm
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Q73JU6 | MKERLDNLRKRLVEVEKEVENPNLIKDVAKYKETMREHSYLSKLMEEYDNYLSIEKQIEDSKLLIQEESDAELKEMAREELHSLEAAFEKSEADLKMLLIPPDPLEEKNIIMEIRGGTGGDEAALFAADLFRMYTHYAEMKNWKYEVLSLNETELGGYKEITFSISGKYVYGSLRYESGVHRVQRVPETEGSGRIHTSAVTVAVLPEAEETEIEINQEDLRIDVMRAGGPGGQCVNTTDSAVRITHIPTGLVVICQDEKSQIKNKAKAMRVLRSRLYDLEESKKQAERAQNRKSQVGSGDRSERIRTYNFPQNRVTDHRI... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 41353
Sequence Length: 361
Subcellular Location: Cytoplasm
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B1KFR6 | MFEVNPVKFKIKDLADRTLLLRGIFDYDAKKERLEEVSAELESSEVWNNPENAQALGKERSALELVVKTIDDMDSGLEDVEGLVELAVEEEDEETFADASSELDALEKRLEELEFRRMFSGPHDISDCYLDIQSGSGGTEAQDWANMVLRMFLRWGEAHDYKPELIEVTDGDVAGIKGATIKFTGEYAFGSLRTETGVHRLVRKSPFDSSGKRHTSFCSVFVYPEIDDSIEIDINPSDLRIDTYRASGAGGQHVNKTESAIRITHVPTNTVVQCQNDRSQHKNRDAAMKQLKAKLYELEMLKQNADKQQAEDAKSDIGWG... | Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Sequence Mass (Da): 40996
Sequence Length: 365
Subcellular Location: Cytoplasm
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P27129 | MDSFPAIEIDKVKAWDFRLANINTSECLNVAYGVDANYLDGVGVSITSIVLNNRHINLDFYIIADVYNDGFFQKIAKLAEQNQLRITLYRINTDKLQCLPCTQVWSRAMYFRLFAFQLLGLTLDRLLYLDADVVCKGDISQLLHLGLNGAVAAVVKDVEPMQEKAVSRLSDPELLGQYFNSGVVYLDLKKWADAKLTEKALSILMSKDNVYKYPDQDVMNVLLKGMTLFLPREYNTIYTIKSELKDKTHQNYKKLITESTLLIHYTGATKPWHKWAIYPSVKYYKIALENSPWKDDSPRDAKSIIEFKKRYKHLLVQHHY... | Function: Adds the glucose(II) group on the galactose(I) group of LPS.
Catalytic Activity: UDP-glucose + [lipopolysaccharide] = UDP + D-glucosyl-[lipopolysaccharide].
Sequence Mass (Da): 39040
Sequence Length: 338
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
EC: 2.4.1.58
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P27243 | MLTSFKLHSLKPYTLKSSMILEIITYILCFFSMIIAFVDNTFSIKIYNITAIVCLLSLILRGRQENYNIKNLILPLSIFLIGLLDLIWYSAFKVDNSPFRATYHSYLNTAKIFIFGSFIVFLTLTSQLKSKKESVLYTLYSLSFLIAGYAMYINSIHENDRISFGVGTATGAAYSTMLIGIVSGVAILYTKKNHPFLFLLNSCAVLYVLALTQTRATLLLFPIICVAALIAYYNKSPKKFTSSIVLLIAILASIVIIFNKPIQNRYNEALNDLNSYTNANSVTSLGARLAMYEIGLNIFIKSPFSFRSAESRAESMNLLV... | Function: Adds the O-antigen on the glucose group of LPS.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46878
Sequence Length: 419
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Subcellular Location: Cell inner membrane
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P26471 | MLTTSLTLNKEKWKPIWNKALVFLFVATYFLDGITRYKHLIIILMVITAIYQVSRSPKSFPPLFKNSVFYSVAVLSLILVYSILISPDMKESFKEFENTVLEGFLLYTLLIPVLLKDETKETVAKIVLFSFLTSLGLRCLAESILYIEDYNKGIMPFISYAHRHMSDSMVFLFPALLNIWLFRKNAIKLVFLVLSAIYLFFILGTLSRGAWLAVLIVGVLWAILNRQWKLIGVGAILLAIIGALVITQHNNKPDPEHLLYKLQQTDSSYRYTNGTQGTAWILIQENPIKGYGYGNDVYDGVYNKRVVDYPTWTFKESIGP... | Function: Adds the O-antigen on the glucose(II) group of LPS.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46034
Sequence Length: 404
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Subcellular Location: Cell membrane
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Q9HUF7 | MRLVLEEPFKRLWNGRDPFEAVEALQGKVYRELEGRRTLRTEVDGRGYFVKIHRGIGWGEIAKNLLTAKLPVLGARQEWQAIRRLHEAGVATMTAVAYGERGSDPARQHSFIVTEELAPTVDLEVFSQDWRERPPPPRLKRALVEAVARMVGDMHRAGVNHRDCYICHFLLHTDKPVSADDFRLSVIDLHRAQTRDATPKRWRNKDLAALYFSALDIGLTRRDKLRFLRTYFRRPLREILRDEAGLLAWMERKAEKLYERKQRYGDLL | Function: Catalyzes the phosphorylation of heptose(I) of the outer membrane lipopolysaccharide core. The phosphorylation of the lipopolysaccharide core seems to occur prior to translocation to the periplasm and attachment of O-antigen. Also has protein-tyrosine kinase activity: autophosphorylates on all Tyr residues; i... |
P25742 | MRYHGDMLLTTPVISTLKQNYPDAKIDMLLYQDTIPILSENPEINALYGISNKGAGTFDKIKNVLSLIKTLRANNYDLVINLTDQWMVALLVRCLPARMKISQLYGHRQHGIWKKSFTHLAPIHGTHIVERNLSVLEPLGITDFYTDTTMSYAEDCWKKMRRELDALGVKDHYVVIQPTARQIFKCWDNDKFSKVIDALQQRGYQVVLTCGPSADDLACVDEIARGCETKPITGLAGKTRFPELGALIDHAVLFIGVDSAPGHIAAAVKTPVISLFGATDHVFWRPWTENIIQFWAGNYQKMPTRHELDRNKKYLSVIPA... | Function: Catalyzes heptose transfer to the lipopolysaccharide core. It transfers a heptose, called heptose(III), to the heptose(II) of the inner core (By similarity).
Sequence Mass (Da): 38731
Sequence Length: 344
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
EC: 2.-.-.-
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P27240 | MIQKSKIKDLVVFTDENNSKYLNVLNDFLSYNINIIKVFRSIDDTKVMLIDTDYGKLILKVFSPKVKRNERFFKSLLKGDYYERLFEQTQKVRNEGLNTLNDFYLLAERKTLRFVHTYIMIIEYIDGIELCDMPDIDDALKNKIQQSINALHQHGMVSGDPHRGNFIIKNGEVRIIDLSGKRASAQRKAKDRIDLERHYGIKNEIRDLGYYLLVYRKKMRNFMRRLKGKPAR | Function: Catalyzes the phosphorylation of heptose(II) of the outer membrane lipopolysaccharide core.
Sequence Mass (Da): 27461
Sequence Length: 232
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
EC: 2.7.1.-
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Q9ZIS7 | MITSIRYRGFSFYYKDNDNKYKEIFDEILAYNFKTVKVLRNIDDTKVSLIDTKYGRYVFKVFAPKTKRNERFLKSFVKGDYYQNLIVETDRVRSAGLTFPNDFYFLAERKIFNYASVFIMLIEYVEGVELNDMPIIPENVKAEIKASMEKLHALNMLSGDPHRGNFIVSKDGVRIIDLSGKSCTAERKARDRLAMERHLGIANEIKDYGYYSVIYRTKLRKFIKKLKGKA | Function: Catalyzes the phosphorylation of heptose(II) of the outer membrane lipopolysaccharide core.
Sequence Mass (Da): 26994
Sequence Length: 230
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
EC: 2.7.1.-
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P26472 | MIIEKKIKNYTVFVKKDGEKYIEIFKDFLSYNHQVIKVFRNIEDTKVVLINTDYGKYILKVFSPKVKNTERFFKSLVKGDYYEKLFHQTDRVRREGFAALNDFYLLAEIKTLRYVKTYVMIIEYIEGIELVDMPEISDEVRGKIKQSIYSLHQHGMVSGDPHKGNFILQGNEIRIIDLSGKRPSRQRKAKDRIDLERHYGIKNNVRDIGFYLLIYKKKLRNFLRRIKGKEKR | Function: Catalyzes the phosphorylation of heptose(II) of the outer membrane lipopolysaccharide core.
Sequence Mass (Da): 27740
Sequence Length: 232
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
EC: 2.7.1.-
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Q48475 | MSIKMKYNLGYLFDLLVVITNKDLKVRYKSSMLGYLWSVANPLLFAMIYYFIFKLVMRVQIPNYTVFLITGLFPWQWFASSATNSLFSFIANAQIIKKTVFPRSVIPLSNVMMEGLHFLCTIPVIVVFLFVYGMTPSLSWVWGIPLIAIGQVIFTFGVSIIFSTLNLFFRDLERFVSLGIMLMFYCTPILYASDMIPEKFSWIITYNPLASMILSWRDLFMNGTLNYEYISILYFTGIILTVVGLSIFNKLKYRFAEIL | Function: May form an ATP-driven O-antigen export apparatus, in association with RfbB.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30036
Sequence Length: 259
Subcellular Location: Cell inner membrane
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Q8PV94 | MLKQRFVLDTTALTDLQTREVMGYTSLCEGMKTILDLIAEARLHFGISCYVPYPSVYKEMYEFASRNGCDREVVAKIDTWLVKKSPDRYRVDVTSQIFHEYVSYMRERINRGMGVAEDAIWEAATECLFMENPQNKKKEYREEVEREVIGGIIGKFRNKYRAALRYGILDSAPDIDVLILAKELDAAVIASDYGIEKWAEQLGVRFVPANTFPMMIKEYLRHGPEVVKEQEDEDRKRIDYSDDADFI | Function: RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 28672
Sequence Length: 247
EC: 3.1.26.5
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O26345 | MLAKQRFVLDTTAFTDNQLRELLGDGDLNLSVDRMLDLIARSRIKLNISCHMPPITYKEFTDYMTRYDCPEETLIKAETWIVKKTPNRYDTQIPSQIFYEYVHDIRERMNKGLRISETLLWEAGIQSIIMASRDVKKTEIESEVLGKAIKDLRKKYRSALRKGTLDSAPDLDVLLLAKELGAGVVAADDGIRVWAERLGLRFLNATSFPKMLKEYLKYYE | Function: RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 25461
Sequence Length: 220
EC: 3.1.26.5
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O59517 | MIKFVLDTSIFVNPDVRKKFGETPTEAMKTFLHYAENLFGKVEFYMPPGIYRELMHFVEEEEVSPDIELYIIKKPPNVHDIKIPAFVVYELIEDIRRRVDKGLRVAEKAVRESVIDTSNVDKIIQKLRRNYRKALREGILDSKEDFELILLAKEIDGIIVSADVGILTWAEKMGIKWVDAFKFKEVLSELVEKFKRSESEKERK | Function: RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 23896
Sequence Length: 204
EC: 3.1.26.5
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A3DL59 | MPLIYVLDTSAVTDPRLREIFGVKTLDGVVREYARLLIRSHIVLGAEFYTTPSTALELRSFLERNNVSREAIDMLMGAITIRSPDLYTTRIPAIIMSDWIHDMLIRITKGLRVAEDSVRRAARRGYDYGVAQDKKGFEESVAETIHELREKYREATRKGVIDTRVDFDLVVLAHEINGELVTNDTGIMKLCMQIGVKYIEPPRFINKLFLLLRERTGRV | Function: RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 25113
Sequence Length: 219
EC: 3.1.26.5
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Q09697 | MISSFSNGFWSKDYATGVKKLFDCLDNGVEENEQVKNLLKLYKEANEEFGEKLQEITKECLKGKKPENTEDGATSNKAFEGLRSEIANQGKQHIRIAKDLETLIIAPFSKMSIDHSQKLQTSQQVLTNQIKSYEKKYYTLKKTKSAYYNKCRNLEDYEEESKESNETTSEAITDLTTVSSPQQQSLLENDDDLIQLGFMEFRPEELKEVLAQVLQEIPLQDYRVPILGTYPNTCSGNIIVSWLQENLPVPTLVAAEAFGQDLIAQGFLRHMGVGGSFVNSTNFHYQWKDKAFQFAGLNSVDSLVENAKALPLVGEYLSDY... | Function: Acts in signal transduction. Negatively regulates the pak1/shk1 control pathway.
PTM: Phosphorylated by pak1/shk1.
Sequence Mass (Da): 88208
Sequence Length: 777
Subcellular Location: Cytoplasm
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Q9H0H5 | MDTMMLNVRNLFEQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMKAETERSALDVKLKHARNQVDVEIKRRQRAEADCEKLERQIQLIREMLMCDTSGSIQLSEEQKSALAFLNRGQPSSSNAGNKRLSTIDESGSILSDISFDKTDESLDWDSSLVKTFKLKKREKRRSTSRQFVDGPPGPVKKTRSIGSAVDQGNESIVAKTTVTVPNDGGPIEAVSTIETVPYWTRSRRKTGTLQPWNSDSTLNSRQLEPRTETDSVGTPQSNGGMRLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCR... | Function: Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Plays key roles in controlling... |
Q03336 | MSSIKIECVLRENYRCGESPVWEEASKCLLFVDIPSKTVCRWDSISNRVQRVGVDAPVSSVALRQSGGYVATIGTKFCALNWEDQSVFILAMVDEDKKNNRFNDGKVDPAGRYFAGTMAEETAPAVLERHQGSLYSLFPDHSVKKYFDQVDISNGLDWSLDHKIFYYIDSLSYTVDAFDYDLPTGQISNRRTVYKMEKDEQIPDGMCIDVEGKLWVACYNGGRVIRLDPETGKRLQTVKLPVDKTTSCCFGGKDYSEMYVTCARDGMSAEGLLRQPDAGNIFKITGLGVKGIAPYSYAG | Cofactor: Binds 1 divalent metal cation per subunit. Most active with Zn(2+) and Mn(2+) ions. The physiological cofactor for gluconolactonase activity is most likely Ca(2+) or Mg(2+). Mg(2+), Mn(2+) and Co(2+) are equally efficient for the hydrolysis of diisopropyl phosphorofluoridate.
Function: Gluconolactonase with l... |
Q6DF62 | MSSIKIECVVSETYKIGESPVWEEKDGTLLFVDITGQKVCRWDPGTKKVQSVSLEAPVGSVVLRKSGGYVMAMGNTFSALNWQDQSVTTLTCVDEDKPNNRFNDGKVDPEGRFLAGTMSQEIRPAVVERNQGSLFTLYPDHSVVKHFDMVDISNGLDWSLDHKTLYYIDSLSFKVDALDYDMKTGKSSNRRTLYKLQQDEGIPDGMCIDAEGKLWVACYNGGRVIRIDPETGKQIQTVKLPVDKTTSCCFGGPDYSEMYVTSACEGMDEEWKKRQPQSGGIYKITGLGVKGIAPTAFAG | Cofactor: Binds 1 divalent metal cation per subunit. Most active with Zn(2+) and Mn(2+) ions. The physiological cofactor is most likely Ca(2+) or Mg(2+).
Function: Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Catalyzes a key step in ascorbic acid (vitami... |
Q9SRT9 | MVEPANTVGIPVNHIPLLKDELDIVIPTIRNLDFLEMWRPFLQPYHLIIVQDGDPSKTIAVPEGFDYELYNRNDINRILGPKASCISFKDSACRCFGYMVSKKKYIFTIDDDCFVAKDPSGKAVNALEQHIKNLLCPSTPFFFNTLYDPYREGADFVRGYPFSLREGVSTAVSHGLWLNIPDYDAPTQLVKPKERNTRYVDAVMTIPKGTLFPMCGMNLAFDRELIGPAMYFGLMGDGQPIGRYDDMWAGWCIKVICDHLGLGVKTGLPYIYHSKASNPFVNLKKEYKGIFWQEDIIPFFQSAKLTKEAVTVQQCYMELS... | Function: UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides. Catalyzes the interconvertion of UDP-L-arabinopyranose (UDP-Arap) and UDP-L-arabinofuranose (UDP-Araf) in vitro. Preferentially catalyzes the formation of UDP-Arap from UDP-Araf. At thermodynamic equilibrium in vi... |
P80607 | MAGTVTVPGSSTPSTPLLKDELDIVIPTIRNLDFLEMWRAFFQPYHLIIVQDGDPTKTIKVPEGFDYELYNRNDINRILGPKASCISFKDSACRCFGYMVSKKKYIYTIDDDCFVAKDPSGKDINALEQHIKNLLSPSTPFFFNTLYDPYREGADFVRGYPFSLREGAHTAVSHGLWLNIPDYDAPTQLVKPKERNERYVDAVMTIPKGTLFPMCGMNLAFDRDLIGPAMYFGLMGDGQPIGRYDDMWAGWCVKVICDHLSLGVKTGLPYIWHSKASNPFVNLKKEYKGIFWQEDIIPFFQNVTIPKDCDTVQKCYIYLS... | Function: Probable UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides (By similarity). Was initially shown to possess an autoglycosylating activity which is dependent on the presence of UDP-glucose and manganese .
PTM: Reversibly glycosylated by UDP-glucose, UDP-xylose and U... |
O04300 | MASLPKPTPLLKDELDIVIPTIRNLDFLEMWRPFFEQYHLIIVQDGDPSKVIKVPEGFDYELYNRNDINRILGPKASCISFKDSACRCFGYMVSKKKYIYTIDDDCFVAKDPTGHEINALEQHIKNLLSPSTPFFFNTLYDPYREGTDFVRGYPFSLREGVPTAVSHGLWLNIPDYDAPTQLVKPHERNTRFVDAVLTIPKGSLFPMCGMNLAFNRELIGPAMYFGLMGDGQPIGRYDDMWAGWCIKVICDHLGYGVKTGLPYIWHSKASNPFVNLKKEYKGIFWQEEIIPFFQAATLSKDCTSVQKCYIELSKQVKEKL... | Function: Probable UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides (By similarity). Was initially shown to possess an autoglycosylating activity which is dependent on the presence of UDP-glucose and manganese .
PTM: Reversibly glycosylated by UDP-glucose, UDP-xylose and U... |
P85413 | TIKVPEGFDYELYNRNDINRYVDAVLTIPKVICDHLGLGVKTGLPYIWHSKASNPFVNLK | Function: Probable UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides.
Catalytic Activity: UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose
Sequence Mass (Da): 6847
Sequence Length: 60
Subcellular Location: Secreted
EC: 5.4.99.30
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Q7FAY6 | MSLEIQDSEVDIVIAALQPNLTTFFEAWRPFFSRFHIIVVKDPDMAEELQIPTGFDLKVYTKSDMGVLGATSIDFSGHSCRYFGYLVSRKKYVISIDDNCLPAKDNGGLTVDAVAQHMSNLKTPATPFFFNTLYDPFRKGADFVRGYPFSLREGVECMLSCGLWLHNADYDPMTHVVKRNQRNTTYVDAVMTVPLGAMMPVSGINVAFNREVLGPVMFPALRLRKEGKHRWDTLEDVWNGLCAKVVCDRLRYGVKTGLPYVMRSDAEAGKALESLKEWEGVKVMDVVLPFFESLKLSSTSVTVEDCVKELTSIVKEKLGP... | Function: Probable inactive UDP-L-arabinose mutase. Inactive in vitro, but associates with UAM1 and UAM3.
PTM: Is not reversibly glycosylated in vitro by UDP-glucose, UDP-xylose and UDP-galactose.
Sequence Mass (Da): 38907
Sequence Length: 347
Subcellular Location: Golgi apparatus
|
Q8LA13 | MSASWADVADSEKAVSQSKPPYVPPHLRNRPSEPVAAPLPQNDHAGYGGQPAGSRWAPPSSGGGGASGGGYRNDGGRTGYGYGAGGGGGGGGGWNNRSGGWDRREREVNPFGDDAELEPVFTEQENTGINFDAYEDIPVETSGGDVPPPVNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVERPRGSRAVYPFAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGF... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 66026
Sequence Length: 612
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
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Q9M2E0 | MNTNRGRYPPGVGTGRGAPPNPDYHQSYRQQQPPQDQQYVQRGYSQNPQQMQLQQQHQQQQQQQQWSRRPQLPGNASNANEVVQQTTQPEASSDANGQDWKATLRLPPPDTRYQTADVTATKGNEFEDYFLKRDLLKGIYEKGFEKPSPIQEESIPIALTGSDILARAKNGTGKTGAFCIPVLEKIDPNNNVIQAMILVPTRELALQTSQVCKELSKYLNIQVMVTTGGTSLRDDIMRLHQPVHLLVGTPGRILDLTKKGVCVLKDCAMLVMDEADKLLSAEFQPSLEELIQFLPQNRQFLMFSATFPVTVKAFKDRHLR... | Function: ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 56775
Sequence Length: 498
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP bind... |
Q93Y39 | MVTGDKESSLMKKRNKRSHKRKREEDFERIDSLPWSSSIPIGEDDEGESFSTLFSGSGQLDGGFLSLEEIDEADYHLTLPTIESEITERKQSPEDDDDTNETVDEMIEGEEAEEDGEGRDDEDDEDDEETRKKKEKKAKRNKEKKKEKKKKKQKKINEAAKNQDASAVSCDGDDTVEEQVEEEEIPPEFSAWSSMRLHPLLMKSIYRLDFKEPTKIQKACFNVAAYQGKDVIGAAETGSGKTLAFGLPILQRLLDEREKVGKLYALKGEEAQKYAADGYLRALIITPTRELALQVTEHLENAAKNLSVKVVPIVGGMFSE... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 93986
Sequence Length: 826
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
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Q8H136 | MAATAAASVVRYAPEDHTLPKPWKGLIDDRTGYLYFWNPETNVTQYEKPTPSLPPKFSPAVSVSSSVQVQQTDAYAPPKDDDKYSRGSERVSRFSEGGRSGPPYSNGAANGVGDSAYGAASTRVPLPSSAPASELSPEAYSRRHEITVSGGQVPPPLMSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRNDSRMGPTILVLSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMG... | Function: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 67728
Sequence Length: 619
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases an... |
Q5VQL1 | MASAAAAAATARGPRYAPPDPTLPKPWRGLIDGNTGYLYFWNPETKAVQYDRPTAPPPSSPPAQQPPERPRNSDPAESQAQAGASRTQNAAPADDRARNDHLNDHFERRTEAAGSHAQNVPFTEQNTRSNPSSQPCSAAGVYPAQNVFSEAASGDRTSPEAYRAKHEITIVGNEAPAPFMTFQSTGFPPEILREVQQAGFSAPTPIQAQSWPIALRNRDIVAVAKTGSGKTLGYLIPGFILLKRLQHNSRDGPTVLVLSPTRELATQIQDEAKKFGRSSRISSVCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMR... | Function: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 77297
Sequence Length: 708
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases an... |
Q56XG6 | MGDARDNEAYEEELLDYEEEDEKVPDSGNKVNGEAVKKGYVGIHSSGFRDFLLKPELLRAIVDSGFEHPSEVQHECIPQAILGMDVICQAKSGMGKTAVFVLSTLQQIEPSPGQVSALVLCHTRELAYQICNEFVRFSTYLPDTKVSVFYGGVNIKIHKDLLKNECPHIVVGTPGRVLALAREKDLSLKNVRHFILDECDKMLESLDMRRDVQEIFKMTPHDKQVMMFSATLSKEIRPVCKKFMQDPMEIYVDDEAKLTLHGLVQHYIKLSEMEKNRKLNDLLDALDFNQVVIFVKSVSRAAELNKLLVECNFPSICIHS... | Function: ATP-dependent RNA helicase involved in pre-mRNA splicing. Required for the export of mRNA out of the nucleus. In addition to ssRNA and dsRNA, binds dsDNA, but not ssDNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 48337
Sequence Length: 427
Domain: The Q motif is unique to and c... |
Q9SW44 | MGKTKLKPVEDVNSEVVDEVEKAEEVEEQRNDREQEEEQKEEEAPKSFEELGLDSRLIRALTKKGIEKPTLIQQSAIPYILEGKDVVARAKTGSGKTLAYLLPLLQKLFSADSVSKKKLAPSAFILVPSRELCQQVYTEVSSLIELCRVQLKAVQLTSSMSASDMRNALAGLPEILVSTPACIPKCFAAGVLEPTAVSESLSILVLDEADLLLSYGYEDNLRSVTSIIPRRCQCLLMSATTSSDVEKLKKLILHNPIVLTLTEDNDKEEAVPSNVQQFWISCSAQDKLLHILALLKLEVVQKKILIFINTIDMGFRLKLF... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 69502
Sequence Length: 626
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
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Q6ATJ8 | MAAAAAASSMAKRKQRKAATEQEVENHDEATVAAEAGPENDGHTAHAAEEAAAAEEGVEREGGGEGGAEGEEGPDAAARGGEEGKEEEEREVSFDELGLDEQLKRALRKKGLDKATPIQREAIPLILEGKDVVAKAKTGSGKTFAYLLPMLHELLKLSAEGRIRKSAPNVFILVPTRELCQQVHNEASSLLEFCTSKLKVVQVNASMSDKDIKVALSGPPNILVTTPACVASCISKGIIRGSSIKESLSMMILDEADLLLSYRCEDDIKALVPHIPRSCQSILMSATSSADIEKLTKLLLHNPFILTLTEVGHAKDDLIP... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 74332
Sequence Length: 670
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
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Q7XJN0 | MKRAQQSARETKQEAKDASKAKSGLFASCSFSSLGLDTKLSDQLKERMGFEAPTLVQAQAIPVILSGRDVLVNAPTGTGKTIAYLAPLIHHLQGHSPKVDRSHGTFALVIVPTRELCLQVYETLEKLLHRFHWIVPGYVMGGEKKAKEKARLRKGISILIATPGRLLDHLKNTASFVHKNLRWVIFDEADSILELGYGKEIEQIIKLLGSGQNEQGEEDDIVPKGIQKQNLLLSATLNDKVNDLAKLSLDDPVMIGLDNTKLQQNLSIESPAAPDSDAEDMVIHVNKSANPLSEDYGIPSQLVQRYLRVPCGARLVALLS... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 68214
Sequence Length: 609
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
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Q0DLB9 | MAKKLGKSPVAKEEDKEGLFASCSFTDLGLHPTLCAHLQDKMGFQAPTRIQAQAIPVAMSGQHMLVKAATGTGKTLAYLAPIVHLLQMREPRVERTDGTFALVLVPTRELCLQVYGIAQQLVHRFHWLVPGYIMGGENRAKEKARLRKGISILIATPGRLLDHLQHTSSFVYPNMRWIVFDEADSILELGFGKALEDILEHLGSRNDTSNQNKNKMEPMKRQNLLLSATLNEKVNRLAKISLKNPVMIGLDEQNSSAHGKNHTSLLSDDEEEILEKHNVTVEQAVDDFKLPAQLVQRYVKVSCGSRLAILLTILKSLFER... | Function: May play a role in organellar ribosome biogenesis and suppress 16S rRNA maturation.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 66904
Sequence Length: 591
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hyd... |
Q761Z9 | MSSSSSSLAAAAARKRALTEQRFSELSPALSPEVVKALKGGGFRRCTPVQAAAIPLLLSHKDVAVDAATGSGKTLAFVVPVVEILRRRPSPPKPHEVLGIIISPTRELSSQIYNVAQPFFATLKGVSSMLLVGGFDIKAELKKLEEEGANILVGTPGKLFDVMERLDTLNYKNLEILILDEADRLLDLGFQKQITSIISKLPKLRRTGLFSATQTEAVKELAKAGLRNPVRVEVKTEVKPTGKDGAQQELGPSKTPLGLRLEYMICEASNKSSQLVDFLVQNNGKKIMVYFATCACVDYWAIVLPLLDSLKGSPIIPYHG... | PTM: Phosphorylated.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 72217
Sequence Length: 647
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
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Q7FGZ2 | MGRDKEDKTEMDSVVPWMRAPVDVSNVENCALDTLPCLNPKLKKALENMGISSLFPVQVAVWHETIGPGGFERDICVNSPTGSGKTLSYALPIVQLLASRPVRCLRALVVLPTRDLALQVKDVFDAIAPAVGLSVGSAVGQSSIAGEISQLIKTPKLDAGICYDPDDLSQNLESAVDILVATPGRLMDHINNTKGFTLEHLRYLVVDETDRLLREAYQSWLPTVLQLTQTSDDSLFPSFTPFVPSAFGSLQTVRRQSVERGFKGKPYPRLVKMVLSATLTQDPSKLIQLDLHHPLFMTTGGSRYRLPEKLECLRLICETG... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 57716
Sequence Length: 522
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
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P85441 | RELLMGIFEKNGTGKTAAFVIPLLQK | Function: ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 2875
Sequence Length: 26
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP bindin... |
O05262 | MIYTAIDVGASSGRIMVGELNEGKLDIQEIHRFANGFSQRDGHCLWDIDHLLKQILQGLQKVKTLGYEHCTVGIDTWAVDYVLLDEKGDRLREAISYRDRRTDHTIDKLEHTLSKAAIYQKTGIQFQPFNTIYQLFEEDRELLKKTDKIMMIPDYLGYCLTGKAVTEITNVSTTQLLNVSTGNLDPELLEAVSVLEQQFAPLTEPGCELGKLRNEWFPDYDLPACKVMTVATHDTASAVIAAPGVNDGWAYISSGTWSLIGVENKTPIITDLALENNYTNERGANNTIRFLKNIIGMWVIQEVKQQLQADYSFQQLAEEA... | Function: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate.
Catalytic Activity: ATP + L-rhamnulose = ADP + H(+) + L-rhamnulose 1-phosphate
Sequence Mass (Da): 54736
Sequenc... |
Q8A1A3 | MKQNFFAVDLGATSGRTILGSFIEGGLNLEEINRFPNHLIEVGGHFYWDIYALYRHIIDGLKLVAHRGESIASIGIDTWGVDFVLLGKDGNLLRQPYAYRDPHTVGAPEAFFSRISRSEVYGKTGIQVMNFNSLFQLDTLRRNHDSALEAADKVLFMPDALSYMLTGKMVTEYTIASTAQLVNAHTQRLEPELLKAVGLQEENFGRFVFPGEKIGTLTEEVQKITGLGAIPVIAVAGHDTGSAVAAVPALDRNFAYLSSGTWSLMGVETDAPVITAETEALNFTNEGGVEGTIRLLKNICGMWLLERCRLNWGDTSYPEL... | Function: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate.
Catalytic Activity: ATP + L-rhamnulose = ADP + H(+) + L-rhamnulose 1-phosphate
Sequence Mass (Da): 53403
Sequenc... |
Q7BSH1 | MTLEKHAFKMQLNPGMEAEYRKRHDEIWPELVDLLHQSGASDYSIHLDRETNTLFGVLTRPKDHTMASLPDHPVMKKWWAHMADIMATNPDNSPVQSDLVTLFHMP | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12292
Sequence Length: 106
Pathway: Carbohydrate degradation; L-rhamnose degradation.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
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Q2HIJ8 | MGGCCSSSRKSHLVGTPVYYYCPESFEELVPSGTRAGVGSAFTTGLLVDIGLETSIPDTFCAPAPLPYDLLLGRPQCTDSESIKGRMSGSSFETLATCEDLGESDCKTLASSVILSPRKSDFSKHQGLKILVDEEEDCCPICFEDYDVENPRLTTKCEHEFHLSCLLEWIERSDRCPICDKEVVFDDRLN | Function: Probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass... |
O94363 | MAPIKSRRIAVLGSRSVGKSSLTVQYVENHFVESYYPTIENTFSKNIKYKGQEFATEIIDTAGQDEYSILNSKHSIGIHGYVLVYSITSKSSFEMVKIVRDKILNHTGTEWVPIVVVGNKSDLHMQRAVTAEEGKALANEWKCAWTEASARHNENVARAFELIISEIEKQANPSPPGDGKGCVIA | Function: Regulates entry into stationary phase when extracellular nitrogen levels are adequate for growth.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20515
Sequence Length: 185
Subcellular Location: Cell membrane
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P59555 | MKLTKISEAKLPTSFGEFLMIVFEESKTDKNHIALVYGDIKDTNNSVLSRIHSECLTGDALFSIRCDCGFQLKSALMEIVKEGSGILIYHRQEGRNIGLSNKIRAYALQDIGLDTVEANHHLGFSADERDFSVCIDIFNTLNIKKIKLLTNNPSKVTVLNNAGIQITERISLIVGRNAKNSKYLNTKAHKMGHFLPIEY | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (... |
Q62BG3 | MTLVATATLPTRYGTFTSYAFRVAGGDAEHLALVMGDVAEQPSVLTRLHSECLTGDVFGSYRCDCGEQLDLSLRYIAAEGRGVLLYLRGHEGRGIGLSNKIRAYALQEQGRDTVEANLDLGLPDDAREYDSAAAILRILKVTSVRLMSNNPKKFDTLARHGIPVCERVALAVPVREENERYIRTKQLKFGHYYFDENE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (... |
A0RR75 | MEIIKSNIANLPSRFGKFQIKSYKEGCCKEHLTIFSPNLDVTKTVNVRIHSECLTGDAIGSLKCDCRDQLEASLKYINKHGGMVIYLRQEGRNIGLLNKVNAYALQDNGLDTIEANHQLGFKADERTYEIVDFILKDFGIKSINLLTNNPLKLASLTCVNIEKRIPIEIESNEFNKDYLKVKKEQMGHMLDEFTR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (... |
Q8TT89 | MNESTVYECLKYGNENINRALEVLRAGKMIQIYDSDSREGETDLVIPAKAVTYKDVKWMRKDAGGLICVAVDPVASKQLKLPFMADLVREASRTSESLGEVVEKDGDLKYDSHSSFSIWVNHRDTRTGIPDLERALTIRKIGEITEKSLSGNGIRFGNEFRTPGHVALLRAAEGLLDERMGQTELSVALARMAGITPAMVVCEMLDDESGRALSKENSKDYGKDHGLVFLEGQEILEAYMLWTGSEC | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 27396
Sequ... |
Q60364 | MNNVEKAIEALKKGEIILVYDSDEREGETDMVVASQFITPEHIRIMRKDAGGLICTALHPDICNKLGIPFMVDILEFASQKFKVLRELYPNDIPYDEKSSFSITINHRKTFTGITDNDRAFTIKKLAELVKEGRFNDFGKEFRSPGHVTLLRAAEGLVKNRQGHTEMTVALAELANLVPITTICEMMGDDGNAMSKNETKRYAEKHNLIYLSGEEIINYYLDKYLKD | Cofactor: Requires divalent metal ions, preferentially magnesium, for activity (Probable). Binds 2 divalent metal cations per subunit . Zinc and calcium, which are present in the crystals do not support the enzymatic reaction.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-b... |
A2SQG6 | MFTFNTIEEALKSLQNGEMIIVTDDENRENEGDLICAAEYATTENVNFMAKYGRGLICMPMGRSLVEKLCLPPMVLKNTDNHETAFTVSIDHVDTTTGISAVERGITARKCIDPNARPEDFRRPGHMFPLQAKDNGVFEREGHTEATVDLMKLAGLREAGLCCEIMADNGEMMRTPELISMAKQYNLTFVTIKDLQAYRRKQEASALAVEQKNMSPMDC | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 24522
Sequ... |
O27543 | MEIVIMIQEALKALRRGEIVLVFDADNRERETDMIVAAEKIKPEHIRIMRNDAGGLICVPVSWENSEKLGIPYMTDIMEEASGRYPVLGKLSPHDIPYDEKSAFSITVNHRKTFTGITDNDRALTIGELAGICRDDRHESFGDLFRSPGHVTLLRAADGHVLRRGGHTEMSIALMEMAGLTGVAVCCEMMDDRTGNSLSTEDAMKYAREHDLIFMSGAELIESYMEFRS | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 25638
Sequ... |
Q9JZ77 | MSHISPIPEILADIKAGKMVIITDAEDRENEGDLLMAAQFVTPEAINFMIKHARGLVCLPMDGEMVEKLGLPMMTQKNGAQYGTNFTVSIEAAHGITTGISAADRALTIQTAVSPTAKPEDIVQPGHIFPLRAQKGGVLVRAGHTEAGVDLAQMNGLIPASVICEIINDDGTMARMPELMKFAEEHKLKIGTIADLIEYRSRTESLLEDMGNAPVQTPWGEFQQHVYVDKLSGETHLALVKGTPAADTETLVRVHEPFSVMDFIQANPRHSWSLPKALEHIQQAESGVVILLHRTEDGASLLDRTLPKGANQAYKWDSKS... | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 39335
Sequ... |
Q8CWF6 | MNELSKIEQAIEDLRNGKLIIVADDADREAEGDLVGLSEFVTPEKVNFMTKYGRGLICVPITEERALELDLHAMATNNTDTYGTQFTVSVDYYTNSTGISTADRADTIRALAEPLSKAADFKRPGHMFPLIAKNAGVLERRGHTEAAVDLARLSNSIPSAYICEILNDDGTMARYPALETLAKDWDLTLITVEDLVQYREKEIAIEN | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 22928
Sequ... |
Q7N0C8 | MNQTLLSEYGTSSERVEHAINALRDGKGVMVLDNEDRENEGDIIFAAETMTVEQMALTIRYGSGIVCLCLTEERRQQLQLPMMVENNSSPFQTAFTVTIEAAQGVTTGVSAADRITTIRAAIADNAKPSDLNRPGHVFPLRAQPGGVLVRQGHTEAAIDLVSLAGFKPAGVLCELTNDDGSMARTLEVVQFAKLHNMPVVTIEDLVIYRQAIEQKAS | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 23558
Sequ... |
Q2FT79 | MIRVVATGTFDILHPGHLWYLEESAKLGDELYVIVARDANIRHKPRPVIPEEQRLVMVAALKPVTHAVLGDLEDMFRPIREIKPDIITLGCNQHFDPETLQKALEKQNIRAQVVRISEHSSSPFTSSRDIVRKIAELTHQRSQTRETKEQRECGAV | Function: Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Mass (Da): 17822
Sequence Length: 156
Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/... |
Q58579 | MKKRVVTAGTFDILHPGHYEILKFAKSLGDELIVIVARDETVKKLKGRKPIIPEEQRREMVEALKPVDKAILGSLKNKLEPILELKPDIIVLGPDQTTFDEETLKKELAKYNLYPEIVRFRGYKKCPFHSSFDIVKEIIRRFCNKEIKI | Cofactor: Divalent metal cations. The best activity is observed with Co(2+), where the activity is 4 and 2.5 times greater than that with Mg(2+) and Mn(2+), respectively.
Function: Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme. To a... |
Q8TXT2 | MGKRVLAGGVFDILHPGHVAFLEEARKIAGKNGELVVVVARDETVRRLKRTPIVPEEQRVRMVSALKPVDRAILGHPRDFSITLKTVKPDVVVLGPDQDIDEKEVERWAERAGVDCEVRRIEKYERCPLDSTIKIVKRVIELWKRGELRV | Function: Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Mass (Da): 17107
Sequence Length: 150
Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/... |
Q7CP78 | MSKTIATENAPAAIGPYVQGVDLGSMVITSGQIPVDPKTGAVAEDVSAQARQSLENVKAIVEAAGLKVGDIVKTTVFVKDLNDFATVNATYEAFFTEHNATFPARSCVEVARLPKDVKIEIEAIAVRR | Function: Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of rea... |
Q8GUU2 | MSSYSSDSTAARDQHAPLLRPRHDGSFSSSSSSARPTALAVLLGRITGHRAPSMLVRETAARALEERRIDWGYSKPVVAADILWNAALVLASAVMLVGTVEERPNEPIRVWICVYGLQCLFHVVLVWSEYWRRNSTRRARDLESYDHEDYNIEYDYEQDSDDNSTTYSFVKRCESINTVISFIWWIIGFYWVVEGGDKLLGEAPNLYWLSVIFLAIDVFFAVFCVVLACLVGIALCCCLPCIIALLYAVAGTEGVSEAELGVLPLYKFKAFHSNEKNITGPGKMVPIPINGLCLATERTLLAEDADCCICLSSYEDGAEL... | Function: Probable E3 ubiquitin-protein ligase required for embryo development.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Location Topology: Multi-pass membra... |
O52547 | MNVFDVETYLQRIGCGGETGVDLETLAKLQKSHLMAIPYSSLAYELRDAVNVVDLDEDDVFVTSIAEGQGGACYHLNRLFHRLLTELGYDVTPLAGSTAEGRETFGTDVEHMFNLVTLDGADWLVDVGYPGPTYVEPLAVSPAVQTQYGSQFRLVEQETGYALQRRGAVTRWSVVYTFTTQPRQWSDWKELEDNFRALVGDTTRTDTQETLCGRAFANGQVFLRQRRYLTVENGREQVRTITDDDEFRALVSRVLSGDHG | Function: Catalyzes the release of the completed linear polyketide from the rif PKS by forming an intramolecular amide bond, in this way terminating polyketide assembly and forming the macrocyclic compound proansamycin X, an intermediate in the rifamycin B biosynthesis.
Sequence Mass (Da): 29192
Sequence Length: 260
Pa... |
Q9YA27 | MDCGVFEGTVFSGLGHGSFYVSIYARNLRRALGYTPYPGTLNLRVGDAAERLAGCIERARGVRIEPPPIPGERLASVLAFPVEIEGGVRGHIVRPEITVYKGDVVEIVADVYLRDVLKISDGDKVRFRLLDP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Mass (Da): 14456
Sequence Length: 132
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN fro... |
O52552 | MNARKAPEFPAWPQYDDAERNGLVRALEQGQWWRMGGDEVNSFEREFAAHHGAAHALAVTNGTHALELALQVMGVGPGTEVIVPAFTFISSSQAAQRLGAVTVPVDVDAATYNLDPEAVAAAVTPRTKVIMPVHMAGLMADMDALAKISADTGVPLLQDAAHAHGARWQGKRVGELDSIATFSFQNGKLMTAGEGGAVVFPDGETEKYETAFLRHSCGRPRDDRRYFHKIAGSNMRLNEFSASVLRAQLARLDEQIAVRDERWTLLSRLLGAIDGVVPQGGDVRADRNSHYMAMFRIPGLTEERRNALVDRLVEAGLPAF... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the dehydration and aromatization of 5-amino-5-deoxy-3-dehydroshikimate (aminoDHS) to 3-amino-5-hydroxybenzoate (AHBA), a compound that then serves as the starter unit for the assembly of a polyketide during the biosynthesis of rifamycin B and other... |
O28174 | MVRDIKTFKFFEVLLIYEMLEVLKALAMMNATRKVVKISSKELAEHIGQSLQTAARKLKELEDEGLIDRTLTKDGQFVVITEKGKQLLYKEYMDYKKIFDDEGTIKIKGEVFSGVGEGRYYVSLEGYRKQFREKLGFDPYPGTLNLRIPKEEMYFRRRLDEERGILIEGFSTEDRTFGEVKAFKCRINGIEGAIVIPKRTHYPAEILEVISPVKLRDKLGLKDGDFVEVEVIL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Mass (Da): 26975
Sequence Length: 233
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN fro... |
Q75DY2 | MARRPVDIPIPASPVQPFPILTEYVDIVAGFGRGSAELGIPTANVPIEQLPSEVNEMATGVYFGWARLRPNMDQEAQVHHRNDGSEVIYNFGSKLSETERGVFPIVLSVGWNPFYNNSKKTVELHILNDFEEDFYGAKIKFSFLGYIRPELNYTTKEALIEDIHTDIKIASEVLHTEPYSSLKNQL | Cofactor: Zinc or magnesium.
Function: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Mass (Da): 20984
Sequence Length: 186
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP ... |
A1C603 | MRPDGPRDPVVGPDSGPEPPYPVRLSGPVIKGFGRGSKELGIPTANIPAEELAEHPDLQVGVYYGVVALDPAKFQYHGDASRKGEDSQAAILPAVLSIGYNPFYKNKTRSIEIHIMPPLSSPSPTAEVTTQGQGHGQVKFHKLPDFYGTQLKLLILGYIRPEFDYVSLEALVEDIRVDCEVARASLQRPAYERYLAGGQGLDAVEKQRRWLVSF | Cofactor: Zinc or magnesium.
Function: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Mass (Da): 23496
Sequence Length: 214
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP ... |
Q4WHD2 | MRPDGPRDPVAGPDSGPEPPYPVRLSGPVIKGFGRGSKELGIPTANIPAEGLEEYPDLQVGVYYGVVALDPAKFQYQEGQGSTSTSSTGGAEAAVLPAVLSIGYNPFYKNKTKSIEIHIMPPLSSPSPTADGAGEVKFHKLPDFYGTQLKLLILGYIRPEYDYVSLEALIEDIRVDCEVARKSLQRPAYACYIDGDEKECSDVVREQRRWLVTF | Cofactor: Zinc or magnesium.
Function: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Mass (Da): 23367
Sequence Length: 214
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP ... |
Q493M2 | MKHDEYSINKEDVMIPPLHPVVIGRIIGAYGILGWVRILSFTEKNDNIFYYSPYFIIVQSTWKEIFLDKWKLIGKRYIVKIRGVSNRNSAQSLSRCNIIIDETQFPCINDDEYYWKDLIGCVVITVQGVLLGDIISIIETTANDVLVVKMCQNNLYKIKNCLIPFLIKRVIKNINLVTRTVTVDWDPNF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
Q2KY81 | MSERTLPDDLVELGRVASAYGVKGWIKVQPHSAQADVLRAAKQWWLAATPKSAPRVYAVQQCRVHGATAVAQLEGIADRDQAEALRGATVWVSRALFPAAAEDEYYWIDLVGCAFYSSVSGSDVRVGVVEEVFDNPAHAILRVVCQDAEGKALLDAKGRAREMLVPFVSAHIQAVDIAARRIDSDWPLED | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
Q7WHM0 | MSEAAHSGAAPADLVELGRIASAYGVKGWVKVQPHSAQAEVLRTVSHWWLTRPAPQAARGVVASVPRAYQVLQARVHGGAVVAQLAGIDDRDQAEALRGCLVQAARSAFPAPADDEYYWVDLIGCALYSDADGESRLLGVVDEVFDNGAHAVLKVLRQQLQPGQPGPVPLVDPKGRPLEELVPFVRAHIRHVDLAARRIDSDWPLDY | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
O51640 | MFIKGVILSSYGVNGYARVKSISNNFCDFINLKNNKVLLKKSNSSSVEVKVVDVNIKGNSLFLKFEEIDTPEAVRPLIGFELWVDDSLASSLKEGEYYLGKLIGYAIVNNNKKLGEVVAFFEYLNSVFLEVRVGIKFFFIPFLSIYIGDINTQEKTIELKVLDLLK | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A4YK99 | MMSKLICVARIGAAHGVRGEVRLWTFTEDPLAVLHYGPLTTKDGSRSFEVTKAREAKDHLVASFKGITDRNAAERLNGVELYVPRDRLPETDDDEYYHADLIGLAAETTAGAPLGRVLAIHNFGAGDIIEIAPPSGSTLMLPFTNAVVPTVDLAGGRVIIELPDEIDGEDRASADESASAEDDAAAPNSARHPRESGDP | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
B2S869 | MPRPENPIQLAVIGAAHGTRGEVRVKTFTGDPLAIADYGLLYDEQGKAYEILEARVAKTVVIVRFKGVNDRNAAEALNGTELFIDRSQLPDEELDEDEFFQTDLIGLEAVDGDGKSYGVVSAIFDFGGGDLIELSEKGKRPMLIPFTEAAVPEIDFDKGIIKVEPHAAGLIADEHDNPPHESGKKPKKP | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A6WXG0 | MPRPENPIQLAVIGAAHGTRGEVRVKTFTGDPLAIAEYGLLYDEQGKSYEVLEARPAKTVVVVRFKGINDRNAAEALNGTELFIDRSQLPDDELDEDEFFQTDLIGLLAVDAEGKTYGVVSALFDFGGGDLIELSEKGKRPMLIPFTEAAVPEIDLDKGTLLVEPYAAGLIADDEDERPQNEKKKPKKS | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
Q31HX9 | MMSSKQDEKIILGQINGIYGVQGWVKIFSHTDPRQNILSYSPWLVKVKNEWRTFQVEEGRAQQGGKSVVAKLEGIDDRDLAREYIGCEIAILPEQLPATEEGFYWMQLIGCQVTSVEGEDLGQVTEIVETGAHDVLRVEKQSDAGLVSTLIPFVMETFILDVDVESKQIQVDWQLEDATES | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
Q0C668 | MSADTKTQRLIPMGVLKGAHGVRGEVRVKSFTADPDALFTYGPLMDEAGKVLLTPITARPGKDHFIVRPKENLQKEDWDALRGCLLHASRDQLPEADEDEFYFEDLIGMPVYTVGEEPEARVRAVQNFGSGDLLEIEIPGAPATIYVPLTRADVPVIDMAAHRIVIPELSLWANQDEDDAS | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A6SVI5 | MKVPEDLVLVGYISGAYGLNGWVRVRPYSADADALLTAKTWWLDKPEFHDVEMMQSKIHTGDVVAKLMGVAGRDAAEALKGATVQIPRSHFPALSDNEFYWVDLIGLEVENLQGEHLGQVSDMMDNGAHPILRVAVPQAAETTDPKAAPQELLIPFVEQFVITVDRTAKKITVDWGLDY | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
Q28UE7 | MTNPDHTCVGAISGSFGVRGEVRLKSFCAEPSDIGSYGPLSTEDGAQTYTITLTRPVKAGYAAMLSGVATKEDADALRGTRLYAPRSALPSLPDDEFYHADLVGLTVLDTGGEVIGTVASVANHGAGDILELSGPGLPSGLLIPFTLAVVPTVDIAAGRVIVDMPDGLIGGDKPDTSDTAPLGQDFD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A6W7U9 | MEYVVARVGRPHGVRGEVTVEVRTDDPDTRFAPGAVLRTDPDRGPLTVATARWHNGTLLLTFQGVEDRTAVEGLRNTRLVVDLDDEADPDDDAWYPHQLQGLAAVTTTGTPLGTVKDLLTGGAQDVLVVTGTDGREVLVPFVTPLVPRVDVKRGKVVLSPPGGLFVELPGEPEE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
B2GFY3 | MSVRVARIGKPHGVRGEVTVELFTDDPQARFAPGSVLSIQHARGGRRGQGSAADAREPLAVQSLTVTGHRWNKDVLVARFEEISDRNAAEAARGLELFAEVADLPLEDDEWHQDDLLGLVAVDLTRGEARIGTVKALIQGSAQDLLEITPQGGGRTVLVPFVEEIVPEVDLDRGLVLVSPPPGLLELGEGE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
Q1IMM5 | MSSTSSTNTDDFITIARIQKTQGRVGEVFSELFTDFPELFEQRHHLYVLPEKGERRELELEDHWFHKGGVVLKFQGIETIDDAEKLLRSEVQIPRQDRAQLEEGATYVSDLVGCELFEIHGSEARKVGVVADVDFSAGEAPLLVVKGDREHLIPYVESFLKSTDFKAKRIEMVLPQGMLELDAPLSKAEKERQKSEADETREAGERRKR | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
C5CEB5 | MIKEFRDLIDSMIPVGKVVKPHGLRGEVKMKSLTNQLKVFETLKKVLLYDEKAGTVVRAEIDTIRRAGKGYIVHFKGFKSVEAAERIRGFYVYAPLNVLPPLKEGEYYFYQLLDCEVYDPEGEYIGKVTDIIETGANDVIVVTKELPDFTVEEELIPVIKDYIVEFRFKDKKIVAKRLEYLTLEGKEDNDDENQRIDDIS | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
Q5FJK6 | MQYFDVARILTTHGLHGEVKVNVITDFPEDRFAEGMQLELKDDIDRVLTIKKSRPFKQFWLLQFDEITDIDEAEKLRGKILVISEKDRGELPDGVYYYKDIFDCGVIDNETGKRLGKITDIQSPGANDIWLVHEDNGKEYWIPNIADVVKKIDIADKKVYVELMEGLRDED | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
Q9CFB6 | MEKFYKVGTIVNTQGLQGEVRVMPSTDFAQERFSKGSVLALFDDKDNYIQDLKVKSGRPQKNFYVVKFEGFYHINDVEKYKGYIVKIAEENQEDLDDGEFYYHEIIGSDVYENDILIGQISEILQPGANDVWVVKRKGKRDLLLPYIPPVILNVDVNQHRVDVSIMEGLDD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A7NJT6 | MEDRPSADEVLLIGTVVDAFGLHGEIKVRSVTDRVDHLRHHVQTVFVGEERRPFPLQRIREPKTGVLILTLGGVTDRTMAEALRGAEVTIRECDAAPLEADEYFIHQLYGLRVVESSGAEIGIVREVLQTGANDVIVVERHGRSDTLLPMIHDVVESLDVAAGQIVVRLLPGLIDEEG | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
Q1AW75 | MGELADPVVIGTITAPHGVRGTVRVRPAGEGRHLREGLSPLVGGRRRRILRARRTPKGFLVDLEGVPDRFRAAELRGEDLLLDRSELDAPEEDEFYVADLVGLEAVDERGGALGEVIETFPTPAHEVLVVRGEGGLLYVPFTREHVPEVDPRAGRAVVRPPEE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A1AXN8 | MKNVLLPNNQERKRSLSNSEIFTFDDKRLLIGQINSLFGVQGWVKIFSHTHPRENILFYQPWHINVDANWQTLEIIQGCVQAKTIVAQIKDVFDKEQARAYIGIDLYIKKSQLPQLKSGEYYWDDLIGLEVINKAKIILGKVSNLVDTGSNNVLVINGEREHWVPYISPFLIKVDIDNQIILVDWDENF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
Q21LG3 | MFTPVEAKKSNLITVGRITGVFGIKGWVKLKSFTDPQDNVLEYSPLLLKTKHGVKECEIAEYQFRPQGLVVRLKGVDDRNAAEALAPVDVAIDKSLLPELDDDDFYWHQLEGLRVVTIYEGNTQDLGVVSKVMATGANDVLEVKPDAQSIDDRDRLVPYVLDLYVKKVDLSAECITVDWDPEF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A4FME9 | MDDKQPLTLAVGRIVRPHGVRGELVVEVRTDSPELRFAPGSVLGMRRRGAHASENFTVAAARPHAGRLLVRAEGVEGREAAEELRGALLTVTADELESTDDPDEFHDHQLEGLRVVFPAGEEAGVVAEVVHTPAGELLAVRTPDDREVLVPFVSEMVPEIDLEAGRIVVDPPEGLFDAEE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0LV11 | MPASRTVRLIRLGCARNDVDAEELAARLVDAGWRLTEAPSADVTVVNTCGFIEAAKQESIDTLLEAADGSTRVVAVGCLAERYGAALADAMPEATILSFDDYPVIAQRLEDVLAGRPPAPHTPRDRRTLLPLTPVDRPRAAAEVGIPGHLGGPRVLRHRLDDSPVAPLKIASGCDRRCTFCAIPSFRGAFVSRPPADILREAQWLADHGAREIVLVSENSTSYGKDLGDPFALEKLLAAFGGVDGLVRVRVTYLQPAEVRPALIDVIATAPHVAPYFDLSFQHASPRVLRRMRRFGGSEEFLNLLAEIRRRNPRAAVRSN... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen ... |
B2ULZ9 | MPLTVGLISLGCPKNLVDSEIMIGHLQKAGMTMTPEPELADVMVVNTCAFIDQAKQEAIDAILDIVRARENGAYPENQKLIVAGCLSQRFRKELPALLPEVDAFIGPDQITKLPEIITQVMDRTIQDRNFIEGKCRYVPDWNTPRYRLTPPHTAYIKIAEGCNHGCAYCIIPMIRGRHRSRSQQDVVREAETLIRSGVKEICLIAQDITYYGMDKWTDARPNRRSAVDSSRGESLASLLRALNAIEGEFWIRLLYTHPAHWSDELTAAIAECPKVARYVDIPLQHISDNMLDAMQRVTDGNYIRTLLRNIRKAVPGIAIR... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen ... |
A6TRJ4 | MPLSVYVESLGCSKNLIDAEVMLGILNQYGYKLTNNEVKADVIIVNTCGFIEAAKEESINKIIELGQLKKDKLKLLIVAGCLGERYQKDLLEELPEVDAIVGTGGYHEIVKVIHQTMKGQRIVEIGDINRPYDETLPRIQTTASHSAYIKISDGCDNYCTYCIIPKLRGKYRSRKMENIIQEAQTLANNGVKEIILIAQDTTRYGIDLYDEYRLSALLDKLSEVEGIQWIRILYCYPEMITDELIATIKNNDKVCKYIDIPIQHCSTKILKLMNRRTSKEEIVSLIEKLKKNVPNIVIRTSIIVGFPGESEEDFNELKAF... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen ... |
A8MLX7 | MNVGFISLGCSKNLVVTEEIIGLFKSNHFNIVNKKEDAEIIVINTCGFIESAKQEAINTILEMAKLKNNKCKYLIVAGCLVQRYKKELEKAIPEVDLFISISEYKQIWKEIENLLDLETGKESNLDYHNRVLTTGSNMAYLKIGEGCDNHCTYCAIPNIQGPYISRTMEDILKEARNLAKQGIKELIVIAQDTTKYGLDIYGEARLPQLLEELCKIEDIEWVRFLYVYPESITDELIKVVGENDKICNYFDIPIQHISDSVLKRMNRKSDGASVRNIIEKIRREIPDVIIRTTLIVGFPGETEEDFKELYEFVEETKFDK... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen ... |
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