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stringlengths 6
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Q9SE42 | MAAAAAAKIAPSMLSSDFANLAAEADRMVRLGADWLHMDIMDGHFVPNLTIGAPVIQSLRKHTKAYLDCHLMVTNPSDYVEPLAKAGASGFTFHIEVSRDNWQELIQSIKAKGMRPGVSLRPGTPVEEVFPLVEAENPVELVLVMTVEPGFGGQKFMPEMMEKVRALRKKYPSLDIEVDGGLGPSTIDVAASAGANCIVAGSSIFGAAEPGEVISALRKSVEGSQNKS | Cofactor: Binds 1 divalent metal cation per subunit. Active with Co(2+), Fe(2+), Mn(2+) and Zn(2+).
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Mass (Da): 24291
Sequence Length: 228
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-xylulose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.3.1
|
Q16518 | MSIQVEHPAGGYKKLFETVEELSSPLTAHVTGRIPLWLTGSLLRCGPGLFEVGSEPFYHLFDGQALLHKFDFKEGHVTYHRRFIRTDAYVRAMTEKRIVITEFGTCAFPDPCKNIFSRFFSYFRGVEVTDNALVNVYPVGEDYYACTETNFITKINPETLETIKQVDLCNYVSVNGATAHPHIENDGTVYNIGNCFGKNFSIAYNIVKIPPLQADKEDPISKSEIVVQFPCSDRFKPSYVHSFGLTPNYIVFVETPVKINLFKFLSSWSLWGANYMDCFESNETMGVWLHIADKKRKKYLNNKYRTSPFNLFHHINTYEDNGFLIVDLCCWKGFEFVYNYLYLANLRENWEEVKKNARKAPQPEVRRYVLPLNIDKADTGKNLVTLPNTTATAILCSDETIWLEPEVLFSGPRQAFEFPQINYQKYCGKPYTYAYGLGLNHFVPDRLCKLNVKTKETWVWQEPDSYPSEPIFVSHPDALEEDDGVVLSVVVSPGAGQKPAYLLILNAKDLSEVARAEVEINIPVTFHGLFKKS | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Critical isomerohydrolase in the retinoid cycle involved in regeneration of 11-cis-retinal, the chromophore of rod and cone opsins. Catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol which is further oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for use as visual chromophore . Essential for the production of 11-cis retinal for both rod and cone photoreceptors . Also capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid . The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis-retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT (By similarity).
Catalytic Activity: an all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty acid + H(+)
PTM: Palmitoylation by LRAT regulates ligand binding specificity; the palmitoylated form (membrane form) specifically binds all-trans-retinyl-palmitate, while the soluble unpalmitoylated form binds all-trans-retinol (vitamin A) (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 60948
Sequence Length: 533
Subcellular Location: Cytoplasm
EC: 3.1.1.64
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B1YEE3 | MYEQEKKMLAEAAIKQVKNGMILGLGTGSTTRSFIDALGEWVKAGGEVQGVATSNETVEQAKRLNIPLLSLEEATHIDLVIDGIDQIDPRFRVLKGGGGALFREKVVALMSREILYLADASKFVHHLTGPLPVEIDAFARPYVERYLRDKQLDVTLREHDGQPFVTDGGHLILDVDLERVQDVRHFAQELKSLTGVLETGYFERQPDHVLTVEQGKVRQLAHPNLRDGGGLV | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 25745
Sequence Length: 232
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
|
Q7NPM5 | MDLDILKQTAARRAVELVEDGMVVGLGTGSTAAFAVSVLAERVRLGLRVVGIPTSERTARQAEAEGIVLGTLAEQSRVDLTIDGADEVALGELALIKGLGGALLREKIVAAASERLIIIVDATKLVEQLGSHGPLPVEVAPFGWQATARALERLGAEVNLRAQHGQAFLTDGGHYILDCRFGPIARPAELEAAIDRIPGVVESGLFVGMASAVIVADEGGIEVLTPSAAP | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 23868
Sequence Length: 230
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
|
Q5FQ98 | MSGTDMNVHKRTAAREAADMVKSGMVVGLGTGSTAAYMIERLGERVAEGLEIFGIPTSDDSEDKALKAGIPLTDFSAHRRIDIAIDGADEVQRGSLNLIKGLGGALLREKIVAQAAKRFVVIVDGTKPVDLLGERAPVPVEVISFGWECTAERLAACGARGVKPRTDRAGSLFVTDTGNMILDCHFGPIEKPEELAEKIDRIVGVVEHGMFLNMASEVLVATPDGVEHWEP | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 24691
Sequence Length: 231
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
|
P44725 | MNQLEMKKLAAQAALQYVKADTIVGVGSGSTVNCFIEALGTIKDKIQGAVAASKESEELLRKQGIEVFNANDVSSLDIYVDGADEINPQKMMIKGGGAALTREKIVAALAKKFICIVDSSKQVDVLGSTFPLPVEVIPMARSQVGRKLAALGGSPEYREGVVTDNGNVILDVHNFSILNPVEIEKELNNVAGVVTNGIFALRGADVVIVGTPEGAKVID | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 23094
Sequence Length: 219
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
|
Q1GX07 | MSNFVAEKSIAAVRAVDEVRDGMLVGLGTGSTAAYAVKSLSERIKHGLRITAVATSQATEALALRLAVPLVPFQQLSAVDLTIDGADEIDDRFQAIKGGGGALLREKITESASTRVIIIADSSKLVAQLGKFPLPVEVVPFATEFVRARLSALGARVTVREAGGTPFLTDQGNYILDAALDEIPRPREIAAAITTIPGVLEHGLFLDEIDTIMIARGDMVEVRHRGEA | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 24200
Sequence Length: 228
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
|
Q4L8J6 | MKDSKELKIMTVDDAVAQIEDNMVLGIGTGSTIELLIPKLAERIHKEQLNITGVCTSNKSAFIAKKLDINVVDINDVGHVDLAIDGADEVDVNINLIKGGGGALFREKVIDEMAHRFVVLADESKLVNYLGESFKLPVEVDKFNWFHIAKKIEAFDDIITERRMSDDVPFITDNGNYILDCQLNKQIDPYQFHEYLIHLTGVLETGYFLNITDQVIVGTQDGVKIINKSN | Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 25707
Sequence Length: 230
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
EC: 5.3.1.6
|
A3CWI3 | MIPVRCFTCGKVVSTAWKEFKERRDAGEDPKRILDDLGLERYCCRRMLLTHKETVEDLNPYQ | Cofactor: Binds 1 zinc ion.
Function: DNA-dependent RNA polymerase (RNAP) 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): 7362
Sequence Length: 62
Subcellular Location: Cytoplasm
EC: 2.7.7.6
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B8GEG1 | MIPVRCFTCGKVISTAWEEFKQRRDAGEDPGAILDDLGLTQYCCRRMLLTHKEIIDELNPYQ | Cofactor: Binds 1 zinc ion.
Function: DNA-dependent RNA polymerase (RNAP) 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): 7189
Sequence Length: 62
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
O26147 | MIPVRCLSCGKPVSAYFNEYQRRVADGEDPKDVLDDLGLKRYCCRRMLISHVETW | Cofactor: Binds 1 zinc ion.
Function: DNA-dependent RNA polymerase (RNAP) 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): 6434
Sequence Length: 55
Subcellular Location: Cytoplasm
EC: 2.7.7.6
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A6UPX1 | MIFPIRCFSCGNVISEVYDEYKTRLSNVESPEEILNDLGVTKYCCRRMFASHRLENGKELFDDIVEYR | Cofactor: Binds 1 zinc ion.
Function: DNA-dependent RNA polymerase (RNAP) 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): 8044
Sequence Length: 68
Subcellular Location: Cytoplasm
EC: 2.7.7.6
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Q3IQT2 | MMVPVRCFTCGTVVGEHWGEFKERAREGDEDPAEVLDELGVERACCRRMLVSHKDLVDIVSPYQ | Cofactor: Binds 1 zinc ion.
Function: DNA-dependent RNA polymerase (RNAP) 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): 7296
Sequence Length: 64
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
O59298 | MIIPVRCFTCGKVIGDKYYEFKRRVEAGEDPEKVLDDLGLERYCCRRMLLSHVELIDDIMHYKVY | Cofactor: Binds 1 zinc ion.
Function: DNA-dependent RNA polymerase (RNAP) 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): 7773
Sequence Length: 65
Subcellular Location: Cytoplasm
EC: 2.7.7.6
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Q8ZYQ7 | MISREELLSKLSQVLPQPLYKEVEEAVRDLDDEKALRLVYRVLKLYVTSLIDPGEAIGIVTAQSIGEPGTQMILRSFHYAGLREFSMARGLPRLIEVVDARRTPSTPLMYVYLKPPYNKSREAAESVAKKIQQVTLETLAKEVDVDYVAGTVTITLDQEQLKYRGLTLKDVEKIVAKAKGKDVAISMRGYTITASLTTPDILKIRKIKDKILQIKISGIKGVRKVVLQYDSKNDEWYIVTEGTNLEAVLQLEEVDPTRTYSNDLHEVEEVLGIEATRALVAQEIKRVLEEQGLDVDIRHMYLVADAMTWSGRLRPIGRHGVVGSKESPLARAAFEVTVKTLIEASVRGEDELFKGVVESIIAGKYVPIGTGIVRLLMQF | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 42423
Sequence Length: 379
Subcellular Location: Cytoplasm
EC: 2.7.7.6
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P11514 | MIDEKLKGYIDKRLNEIKDKIPDKLHEDLRAAIMDINGVELTEEDIDRIIDLTIREYQQSLIEPGEAIGVVTAQSVGEPGTQMTLRTFHFAGIRELNVTLGLPRLIEIVDARKVPSTPMMTIYLTDEYKTDKDKALDIARRIEYTRVENVVSSVSVDISNMSITLQFDQEMLKDKGVSIEEIKKIITKLKLGEIRIEDNDEYSFTIYFEKIDSIMALFKMREKILNTKIKGVKGIKRAIVQKKGDEYVIITDGSNLEGIMNVTGVDINKIQTNNIHEVEEVLGIEAARELISREIKKVLEEQGLDVDMRHIVLVSDIMTRTGDIRQIGRHGVTGEKSSVLARAAFEVTVKHLLDAAARGEREEFKGVIENIIIGQPIRLGTGIVELTMKPNMR | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 44444
Sequence Length: 393
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q03586 | MASLLWRDTSKNIAAILEKLPADYAVDYDVPNNVEDGYITINKKNFTYHVVISGVRKYSPDVEAIVKKKSGLKSIITIEKVEKIEPLSFMEFRVGGKTLEAMGSFEVAERQVTEIKEKYGENLSEDVQKVLDDARAMGFTLPESVAEEIARRRTEWGEKAYKNILKRIGEEIGNELIDPYEAVGIIAAQSIGEPGTQMTMRTFHFAGVREMNVTLGLPRLIEIVDARRIPSTPSMTIYLRPEYETNDEVVMDVVKRLENTSISDVADIITDIGELTVTVRPDPRKTKDRLIEMEDIMNAISKIKGITVMEDSGQIIIKPQQESFKKLYLLQEQIKGLTIKGISGIKRAIARVEGKEHRWVIYTQGSNLKDVLEVDEVDPTRTYTNDIVEIANVLGIEAARNAILNEALRTLQEQGLNVDVRHLMLVADMMTFSGSVRAVGRTGISGRKSSVLARAAFEITTKHLLRAGIMGEVDKLAGVAENIIVGQPITLGTGAVDIIYKGYPKTKK | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 56599
Sequence Length: 508
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q85FJ1 | MRKNEMSTSKQAIQWKCLESKIESKRLHYGRFLVSPFKRGQASTVGIAMRRALLQEIEGTSITCARFCGVVHEYSTITGLQETIHDVLVNLKEIVLRGDSKEDIQEAFLSVTGPKEVTAGDLSLPPGVEAIDNSQYIATITQPISLTIELEIEKDCGYRIENLAKSGKGQFPIDAVFMPVRNVNYSIHLFGSGRATQEILFIEIWTNGSLTPHEALRKASEKLMDLLTTFLYVRGGDVSLFENGEDSLDLTKSPSLQPQFGDTNNLEERVLENRFIDQLELPARAFNCLKRAEIYTIADLLNYSREDLSKLKNFGRKSVDQVSEALWDRFAKELPDKKIVLNRRK | 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): 38979
Sequence Length: 345
Domain: The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
Subcellular Location: Plastid
EC: 2.7.7.6
|
Q8KAJ8 | MIYQMQMPTKIDVDEATHTGSFGRFIAQPLERGYGVTLGNAMRRVLLASLPGTAITGIKIDGVFHEFSTIDGVREDVPEIVLNLKKVRFKSNCKRSCKTTLTLAGPKDFLAGDIVAQEGEFEVLNKDLHIATINSEATVTIDIYIGRGRGYVPAEENRSDGMPIGFIAIDSIYTPIKNVKLTVENTRVGQKTDYEKMILDVETDGSITPDDAISLAGKIINDHITFFANFSPTEEEFSEEEYKQLDDEFESMRKLLQTKIEDLDLSVRSHNCLRLAEIDSLGDLVSRREEELLNYKNFGKKSLTELKEQLEKFNLKFGMDITRYQLKG | 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): 36936
Sequence Length: 328
Domain: The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
EC: 2.7.7.6
|
P56298 | MMKTHNLFVSCIESRVQDQGSLYARFHIGTFFRGQALTFGNSIRRALLSEMPGFLMTDVRIQGATHEFAVLPDVEETVLEILLNLKKTVFVPRIPKNQKFETFQGFGFLKNNGPGKVRAADIRLPETVQCVSPEVHIATLTSGAELSLRFNLQFRNFSQLEKREGTFKSKTVAQAKTEDGNVQDTTNELPTLEKNSLFFQQLQNKRNSKDQLFLDTVPMPVQKVNYVIKSLNAKNGSEYIILEIWTDGSLYPQESVEFALRNLTDLFFQFANISKKSN | 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): 31611
Sequence Length: 278
Subcellular Location: Plastid
EC: 2.7.7.6
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Q1R0F0 | MQRSVTEFLRPRDIKVEEINANHAKIVLEPFERGFGHTLGNALRRILLSSMPGCAVVEAEIEGVLHEYSAIEGVQEDVIEILLNLKDVAVKMHGNRDEVVLALSKQGPSVVTAGDIAVDHDVEIVNPDHVIAHLNDSGELKMQLKVVRGRGYEPADTRASEEDESRAIGRLQLDATFSPVRRVSYSVEAARVEQRTDLDKLIIDLETDGTLDPEEAIRRSATILQEQLAAFVDLEADKEQEVEEEEDQIDPILLRPVDDLELTVRSANCLKAENIYYIGDLIQRTEVELLKTPNLGKKSLNEIKDVLAARGLSLGMRLENWPPASLKDDKASA | 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): 37022
Sequence Length: 333
Domain: The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
EC: 2.7.7.6
|
Q09ME5 | MVREKVKVSTRTLQWKCVESRADSKRLYYGRFILSPLMKGQADTIGIAMRRVLLGEIEGTCITRAKSEKIPHEYSTIVGIQESVHEILMNLKDIVLRSNLYGTCDALICVKGPGYVTAQDILLPPSVEIVDNTQHIASLTEPIDLSIGLQIERSRGYNIKTPNTFQDGNCYPIDAVFMPVRNANHSIQSYGNGNEKQEILFLEIWTNGSLTPKEALHEASRSLIDLFIPFLQAEDENLPLENNQYKVTLPFFTFHDRLAKLTKKKKEIALKSIFIDQSEMSPRIYNCLKKSNIHTLFDLLNTRQEDLMKIEHFRIEDVKQIMSILEKK | 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): 37544
Sequence Length: 328
Domain: The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
Subcellular Location: Plastid
EC: 2.7.7.6
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Q8EUD7 | MEKFLRYNIQIGKDQNKDADYGVFVFKPLERGFGHTLGNSLRRVLLSNIIGHSLFAIKIPNVSHEFQSIKGVKEDLTQIILNLKRLVVKIDQEIFGEEEQKETSLEKWPTLKIDFSKGGVLKASDIETPVGFEIINKDMYIATIESGVKFKMELFVKTGRGFTTFSENKELINAINVIAVDSNFSPVLKVGYKVSDIKTTKNEINDVLELEVATNGAVSAAEAVAMSAKILLEHYKPIVTELFDNYNDLRIINEEATVSSSKSSLAISIDELELSVRSYNCLKRAGIHTITQLTDKTKGEIEKIRNLGKKSFKEIIKKIQDRNLKLKEEQN | 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): 37331
Sequence Length: 331
Domain: The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
EC: 2.7.7.6
|
O21260 | MVHKTPSFRPIIHVLKHDFNSIQVLIGPLEKNFSGSFANLLRKIIFRYTSGVSIIGLKINGIDSLHSYSLIPGVKEDVLNVLNNLKHLLIQIDDYDYKPILLTIQKKGPYIIKSKDIICPSNIKILNDDLYICTLENDSQIDLTLIGDIGCGYVLSTYFGNRKSIVYSDTNFCPIKHVSYYVRSYTTYEELIFYIKTNGTCNPLFVMKNAFSFLKDKINITF | 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): 25376
Sequence Length: 222
Subcellular Location: Mitochondrion
EC: 2.7.7.6
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Q925Z2 | MIQKNWQELIKPNKVEFASSGRTKATLVAEPLERGFGLTLGNALRRVLLSSLRGAAVTAVQIDGVLHEFSSIPGVREDVTDIVLNIKEIAIKMDGDDAKRMVVRKQGPGVVTAGDIQTVGDIEILNPNHVICTLDEGAEIRMEFTVNNGKGYVPADRNRSEDAPIGLIPVDSLYSPVKKVSYKVENTREGQVLDYDKLTMSIETDGSVTGEDAIAFAARILQDQLSVFVNFDEPQKETEEEAVTELAFNPALLKKVDELELSVRSANCLKNDNIVYIGDLIQKTEAEMLRTPNFGRKSLNEIKEVLASMGLHLGMEVPSWPPENIEDLAKRYEDQY | 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): 37171
Sequence Length: 336
Domain: The alpha-NTD is essential for RNAP assembly and basal transcription, whereas the alpha-CTD is involved in interaction with transcriptional regulators and with upstream promoter elements (By similarity). The alpha-NTD recognizes upstream AT-rich elements and the alpha-CTD interacts with the transcriptional activator Fis in reconstitution assays in E.coli.
EC: 2.7.7.6
|
Q7UIC5 | MTMHIRWRGMELPSSLEVDRDSLTQTYGKFSAEPFERGFGASIGNSMRRVLLSSLVGSAVTQIKIRGAQHEFTTIPGVLEDVTDIVLNVKSLIVNSNTDSTRVITVERNTAGVVTGADVQTDADVEIINKDHVICTLTDDVPFMMEMVVETGRGYVPSTEHSSVDHEIGIIPIDAVFSPIVRVRYEVEATRVGQKTNYDRLNLEIWTDGTINPEMALTEAAKILRKHLNPFVQYRELGPSIFSAARGGAGSPEAQLEAKLNMTLADLRLSVRANNCLESENIMTVRDLVQRTEDSLLEVRNFGDTTLNEVREKLSQYGLHLGMRVPNQPLF | 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): 36761
Sequence Length: 331
Domain: The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
EC: 2.7.7.6
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Q4MY95 | MNCTVGNNIYHTYINYFVNNIYNSLSRNINSKINKYYNYYKKSKIFKNIKFYFNLLTFESNYCCDSGQNKYLYDGYNSYYFINIPLQIKFNNLKSRFINYNIINIPKINQSGDIILNGYLRLPILYLQLATNNISYIFNEKITRTYFIKIKNNIYLYIYLYDDFITVYINSYKIKNDLFSMYNNVSFKNKYINFSKIDNVIYVMNLKNNNIKYHIFDKTININNFVNNTMFMDILSIVNKFLNLNLKKKFIQSSNNLINKSTNSVLKTIFRQFTKSVTIFDIEKYCDKLLYKKKIFRSFNIVLFKEHLLVNPVIHYTDQLNVLSYLTNKFKINIFGYSNSSNDKFKVSTNLRKIQSDYIGFINIVNTPDGDTCGLISKLANNTILDKFKLKLINCNNEYFENFTKIDITSKNLYNMTSNNFINIKKNSTFKVKQIEVFKNNEFKLINFDKNKTNKNLNVFNTLSITELIIPFLFNNDPCRGLMGSKMHTQALPLIYNEHPYVMTKYNHMNGLLFNKCITSLCEGIIVSVNNYKIIVMDDKNRYLHYYLYPFNVLDYNSFVSYKPIVWVGEKINIGKILALPSDLKHSEFTLGVNNLLNYSFYNGYEHEDAIVINKNLIIEDILTSISFDVYEEYLSINKLDYVELTLRHLLEYNRYNRYLINEVGVSSNQDYMLFGDILSTKIRYELSLSKNKKFFKVFKLIFKENKKLIVYTKPLTIKRGGEGRLIKYEILGYSKFRQLDAMYPEINVSYLTLRFFIFKIDRINIGDKLCGRHGNKGVVSKIVDNIDLPYTFRGLCPYSITSPIGALARINLGQFLEGSCGYFGLNFNCRIKAPINLYNYHLYSNMYLKNIFNSLNVYNNSYINFSIEKYLRDFKTGYQLKNFNLMLMPYFLKLMHTSKSKFQYRTVGKYSSLTQQPVKGKRVNGSQKFGEMEVWALESHGSAYTIRELGYIKTNVKYFKKFEHKGYKGSETFKVLTLELKNVLININRVDNYSYFNQKIKYNY | 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): 118813
Sequence Length: 1005
Subcellular Location: Plastid
EC: 2.7.7.6
|
P52733 | MIDQNKHQQLRIGLASPEQICAWSEKILPNGEIVGQVTKPHTLHYETNKPERDGSFCERIFGPIKSGVCSCGNSPGIGNEKIDAKFCTQCGVEFVDSRIRRYQMGYIKLACPVVHVWYLKRLPSYIANLLAKTRKELEGPVYCDLFLARPIANKPTLLRSRGTFDYEIQSWREIIPHYLSARPYYLFPRGSGTFKEREIATGGDAIGKQLMGLDLQMIIDRSHMEWKNLVELKWNRLEENQESTVDRWEDEKIRRRKDFLVGRMKLAKHFLRTNIEPKWMVLCLLPVLPPEPRPIVQLGEGGLITSSDLNELYRRVINRNNTLTNLLARSGSESFVIYQTKLIQEAVDALLDNGICRQPMRDSHNRPYKSFSDVIEGKEGRFRENLLGKRVDYSGRSVIVVGPFLSLYQCGLPSEIAIELFQAFLIRSLIGRHIAPNLRTAKSMIRDKGPIVWEVLQEVMQGHPILLNRAPTLHKLGIQAFQPILVEGRAIRLHPSVCGGFNADFDGDQMAVHVPLSLEARAEARLLMFSETNLLSPAIGDPISIPTQDMLLGLYISTVQNSQGIYGNRYHPYHSENKSFSCKKPSFYSYDDVLRAYRQKRIDLYSPLWLRWGEVDLRIITSVNQEAPIEVQYESLGTFHEIHEHYRIRKGRMGEILNIYIRTTVGRTRFNREMEEAIQGFACSEHPNKSLPALRI | 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): 79805
Sequence Length: 696
Subcellular Location: Plastid
EC: 2.7.7.6
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P21422 | MIIHNNINFIGLKLNILNPKQIIKWSSIFYKNKIIIGEVLIPNTINFNTGLPILNGLFCEKIFDYMYKWNCNCNKKMYNINNFSFFLYCKFCKNKLIININRKYKLGFIFLNIPILHLWYLTGPLKVASLLLNKNVFYLKFLIYYKYFFSNIKYKQYFYYNKLFSKINLYKKKYKNIIQYLFSHNILYKKLQNINLLTELLNNKELLLINNKYYNKKYLYKKINLFNLFILNNIKPNWIFLDLLPILPAGLRPYFYINNSTYIISTINENYRLIILKNNKLKYWLYLRNNIFFIFEIIEKRLLQQLIDYLLINKLILKNNNTFFNFSKTFQGKYSTIKYKLLGKRVDFSGRSVITVNPSIIYNNIGLPYYISINLFKPFLINILKYNSKLNIIFKSLLINKNLFIIQKFLNRLLQNQFIIINRAPTLHRMNLQSFKPLLTEGYSLKFYPLGCTSFNADFDGDQMSIFLPLIKTSKFESNINLNFDKNIISPSNNKNLFSNLQYYKLGINTLLILNYNNELNIFYFNSIEKIYEYYNNNILFIFNLVWIKYINNNNIFYILTSINRIIINLYMYIY | 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): 69406
Sequence Length: 575
Subcellular Location: Plastid
EC: 2.7.7.6
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Q09G55 | MIDRYKHQQLRIGSVSPQQISAWAKKILPNGEIVGEVTKPYTFHYKTNKPEKDGLFCERIFGPIKSGICACGNYRVIGDEKEDPKFCEQCGVEFVDSRVRRYQMGYIKLACPVTHVWYLKRLPSYIANLLDKPLRELEGLVYCDFSFARPIAKKPTFLRLRGSFEYEIQSWKYSIPLFFTTQGFDTFRNREISTGAGAIREQLADLDLRIITAYSLVEWKELGEEGPTGNEWEDRKIGRRKDFLVRRMELAKHFIRTNVEPEWMVLCLLPVLPPELRPIIQIDGGKLMSSDINELYRRVIYRNNTLTDLLTTSRSTPGESVMCQEKLVQEAVDTLLDNGIRGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQTFVIRGLIRQHLASNIGVAKSKIREREPIVWEILQKVIQGHPVLLNRAPTLHRLGIQAFQPILVEGCAICLHPLVRKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVPTQDMLMGLYVLTIGNRRGICANRYNPRNRRNYQNERIDDNNYRYTKEKEPYFCSSYDALGAYRQKRINLDSPLWLRWRLDQRVIASREVPIEVQYESLGTYHEIYGHYLIVRSVKKEILCIYIRTTVGHISFYREIEEAIQGFCRACSYGT | 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): 78674
Sequence Length: 682
Subcellular Location: Plastid
EC: 2.7.7.6
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P51251 | MTNFEQYFDYVKISLASPEKIRQWGERSLPNGQIVGEITKPETINYRTLKPEMDGLFCEKIFGPVKDWECHCGKYKRFRYKGIVCERCGVEVTESRVRRHRMAYIELASPVTHVWYLKGSTSYIALALDLKVKEVEKIVYFHSYVVTQSSEETNLKYKQLLEGYEWKSLEEEIYQNQDENNQIEVGIGAEAIQKLLKDLDLEYIAETLRLEATNPPKSFKTPSLKFNKKMKRLRLIENFIATGADPSWMVFTVIPVIPPDLRPMVQLDGGRFATADLNEFYRRIINRNNRLSRLKSILAPEIIIRNEKRMLQEAVDSLMDNGRRGRTVVGANNRPLKSLSDIIEGKQGRFRQNLLGKRVDYSGRSVIVVGPHLKLHQCGLPREMALELFQPFVIHRLILQGLVNNIKAAKKMIQKNESSIWNVLNEVIQGHPVLLNRAPTLHRLGIQAFEPILVEGRAIKLHPLVCPAFNADFDGDQMAVHVPLSLEAQAEARLLMLAPHNFLSPATGQPIIMPSQDMVLGCYYLTANNPSQQRGASQYFASLEDVVIAYEKKKVDLHAYIWARFDGVIDSDQVKFPIKIETHHDNSVTKFFDNHIIKEDAEHQRIVQYIRTTPGRIIFNKIIQESLVA | 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): 72179
Sequence Length: 629
Subcellular Location: Plastid
EC: 2.7.7.6
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Q25802 | MYFYFFNKYNLKILEKKLLIIFKYNISFKILHELLYLGYEYSFLYNYSLNIKDFSNFIYLLILYKNKINNIYNNKYYEIKNNYINVFLNNYYYLKVINKIQGILNNNLYNKINPIYSNLFLFFNNKIKIKYSQLQQLIGYKGYISNIKGMIYEKPVINNYINELNIYEYILSCYGSKKGIIDTALKTADSGYLTKRLINITSNFIIKELNCKSPFILKYILNMDIYGNIILPLNILRFKILQNNILNLNNGTFIYTKNTYITKYILNKLLNLYNRRNIYLNIKSVYLCNIYNNICNTCLNYKQLYKYNLGQHIGVISSEAISEPSTQMVLRTFHASSILKDKFNFNKYLIYKIYLYKLNINKIFKLIINFKKYINIKFNLIFLMNKILYNYNNILFEYKYILQNQYIKCNFIYNSISKNFKYNLNNIIIKYLNNVIKYYNYSNIQLLIKNIHNKWILYNIYTYYLYYYHIKFYNLYNKGIILNNNNNKYNVIYFLINYFNLFSNYYYKIYNNNYNFINSNYYFKMNFILKNFNNIQILNKLFYVNNIFIYYKYEKKLFIYLNIINNIIIKKYLNFYKYTYNKLFFIKKYNNFLYLYEIFKYNWYKYLLLNNKYNLYIIYNNYIKYLYKYNININLYFIKNLFYNNNNFIHNHIIYKNNYYIYNNNMNLYQYNKNILINNNLLYNKLFYNYINNNIYNLYLNDITIGLQSINIIFENKNIKDNIFFISNNIYVIFYIKYYNYLNNIIYIYNICNKYNINHYKYKLNFYSYIFEDISSILYSGYSLHTEFYSINKNLKYYFRFLLKSINIYQATKSSYIYVYNILIESILKQYSYQNIYLPSIYFELIIKKMLSCIKIISNNFKIFKYNDIISLQLINIINYSLNLNKHYIYKYEPIILGITKSILANSGFLTNISFQNTFKIISLNILNNKIDWLIDIKSKIILTDLLPVGNGWYRYLVN | 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): 117860
Sequence Length: 959
Subcellular Location: Plastid
EC: 2.7.7.6
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Q6F7G9 | MARVTVEDCLDHVDNRFELVLVASKRARQLARQGIEPTVEWDNDKPTVVSLREIAEGHVTKDILKQRDQDYQTSSLDLALSANSLNLEGFSFQ | 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): 10543
Sequence Length: 93
EC: 2.7.7.6
|
A0LUF4 | MAGTVAVPEGITNPPIDELLKVCDNKYALVIYAAKRARQINAYYAQLGEGLLEYVGPLVETYPTEKPLSIALREINAGLLTAEPIEQ | 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): 9474
Sequence Length: 87
EC: 2.7.7.6
|
Q725M7 | MARITVEDCQKRIDNRFLLVQMAIKRVQQYREGYEPLVDSKNKEVVTALREIAAGKVMPEDLALYRPAEGEEMPVAE | 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): 8851
Sequence Length: 77
EC: 2.7.7.6
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A5EXW8 | MARVTVEDCLIHENSRFRLVLAASKRARQLTLGHQPLVAPENDKPTVLALREIEEGKVTVQGLLDGQDVSEHLARQA | 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): 8540
Sequence Length: 77
EC: 2.7.7.6
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B8E0X9 | MKEVNIDTLISKIPNKYVLTVVISKRARQLFEELKFLKTIARDPLILAMEEIAQEKIAYGEGDDLED | 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): 7708
Sequence Length: 67
EC: 2.7.7.6
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Q1I2S9 | MARVTVEDCLEHVDNRFELVMLSTKRARQLATGGKEPRVAWENDKPTVVALREIAEGIVTPEFIAAEEIVTEDPVFAAFEDENNEAV | 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): 9729
Sequence Length: 87
EC: 2.7.7.6
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C3K482 | MARVTVEDCLEHVDNRFELVMLSTKRARQLATGGKEPLVQWENDKPTVVALREIAEGLMSYEFIANAEIVEDEPLFAAFEDESNEAV | 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): 9827
Sequence Length: 87
EC: 2.7.7.6
|
B5YJ35 | MKKKEQSLDIISLPIELDRTKIESRYRLALIAAQRAAELSLGATAKIDKKGKKVTTTALLEILSNKIDYITGEEAVKAKEKIDQIDVKKLLEDKRKAIPDLSELEKDLKVYLHGKESAEKMLEDLFTEGESNSSNEQE | 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): 15559
Sequence Length: 138
EC: 2.7.7.6
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B8GQN1 | MARITVEDCLTNMDNRFQLVLVAAKRARQLSMGHQPRVAEENDKPTVIALREIADGHVGREVLDEVVAEEHAAVSSRISEDEVRAEL | 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): 9707
Sequence Length: 87
EC: 2.7.7.6
|
O83699 | MIFPMQQLIEFQGNIYEITCAATRRAFQLAAVCDPVLDELGGKVVSAAAQQVFSGTVDYRIEPQELG | 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 (By similarity).
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 7349
Sequence Length: 67
EC: 2.7.7.6
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B3E4R5 | MARVTVEDCLEKVDNRFMLVMMASKRVKQLYKGAKPLIDPKNNRHVVTSLREIAAGKLSAELSSKRSA | 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): 7631
Sequence Length: 68
EC: 2.7.7.6
|
A1WQL7 | MARITVEDCLEKIPNRFQLVLAATYRARMLNQGHAPRIESRNKPGVTALREIAAGKVGLEMLKKVPG | 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): 7429
Sequence Length: 67
EC: 2.7.7.6
|
A5CX12 | MARVTVEDCLDHVENRFELVLIAAKRAHQLSSGGYKPLLNAGKDKPTVVALREIEAGLIDSSILSEIYVIDEQLSAQQKVLDSVKMSEIKDELSVTAVDKVIDEITEIEE | 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): 12166
Sequence Length: 110
EC: 2.7.7.6
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Q17632 | MDLNVKQSGIHSVALHTTYFQNRSGKVYKRAEERYLRNDLSCGLAQCGTCKDFGTNPLLKIENPVRNAKVGRHALIVDSTSLIRFYDLFDSSLLRDLIVTQTVWEGVKAKAVPAYKKMNSLCYEDAKDRFHVFMNEFHCETFSESSKFEDLSRGEELLLSTALYLKTHWQKHNVAPVVLVFDEDSKKRMENHYQHVMYLKEYIQNLEDPGKQALLDQMAAYESSGNGNEKQIFDEYLSHDRIMEGIASGTIKRGNFSVSRENYREATVIIDDQLTSWFITGNNCNRAVNGDTVAVQLLPEDQWTAPEKKIRLRDVEEYVKTADDMGNEDEENDDENDEPKAKKSKKMTVSTAKVVGIIKRNWREYCGMLLPSTVKGARRHLFCPAERLIPRIRIETEQAETLSQQRIVVAIDHWPRDSKYPLGHYVRSIGEMGSRETENEVLLLEHDIPHAPFSESVLDCLPREEWEPDLTENRGPLPRVDLRDLTICSVDPLGCTDIDDALHCKQIGEDLFEVGVHIADVTHFVRPGTAIDDEAALRGTTVYLCDRRIDMLPCLLSSNLCSLRGEEERYAFSCIWTMTSSADIQSVKYHKSLIKSKAALTYEKAQEIIDDPKEQNDVALGLRGLMKLSKVLNARRTGNGALTLASSEVRFDMDWESRTPKKVMEKQHLDTHSMVEEFMLLANISVAEKILEEYPDCALLRRHPVPLKESYKPLVEAARHRGFEIIVESGKGLADSLNRCVDKKNPMLNRLLRMLTTRCMTQAVYFSAGTVPVPQYQHFGLACAIYTHFTSPIRRYADVIVHRLLAAAIGADDIQSGLLNQARCTKICTNINYRHKQAQYAGRASVQLNVVRYFKGKVETCEGFVMGVRNNGIQVFVPKYGLESIIVLQTSAASGTTIDVEEMSVKVNGDVVIKELEPVTVRISVNEKNQQRPRVELQLIKPAIPGLSVDFDLSSSEGLGL | Function: Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. dis-3 has both 3'-5' exonuclease and endonuclease activities (By similarity).
Sequence Mass (Da): 108786
Sequence Length: 961
Subcellular Location: Cytoplasm
EC: 3.1.13.-
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Q9Y2L1 | MLKSKTFLKKTRAGGVMKIVREHYLRDDIGCGAPGCAACGGAHEGPALEPQPQDPASSVCPQPHYLLPDTNVLLHQIDVLEDPAIRNVIVLQTVLQEVRNRSAPVYKRIRDVTNNQEKHFYTFTNEHHRETYVEQEQGENANDRNDRAIRVAAKWYNEHLKKMSADNQLQVIFITNDRRNKEKAIEEGIPAFTCEEYVKSLTANPELIDRLACLSEEGNEIESGKIIFSEHLPLSKLQQGIKSGTYLQGTFRASRENYLEATVWIHGDNEENKEIILQGLKHLNRAVHEDIVAVELLPKSQWVAPSSVVLHDEGQNEEDVEKEEETERMLKTAVSEKMLKPTGRVVGIIKRNWRPYCGMLSKSDIKESRRHLFTPADKRIPRIRIETRQASTLEGRRIIVAIDGWPRNSRYPNGHFVRNLGDVGEKETETEVLLLEHDVPHQPFSQAVLSFLPKMPWSITEKDMKNREDLRHLCICSVDPPGCTDIDDALHCRELENGNLEVGVHIADVSHFIRPGNALDQESARRGTTVYLCEKRIDMVPELLSSNLCSLKCDVDRLAFSCIWEMNHNAEILKTKFTKSVINSKASLTYAEAQLRIDSANMNDDITTSLRGLNKLAKILKKRRIEKGALTLSSPEVRFHMDSETHDPIDLQTKELRETNSMVEEFMLLANISVAKKIHEEFSEHALLRKHPAPPPSNYEILVKAARSRNLEIKTDTAKSLAESLDQAESPTFPYLNTLLRILATRCMMQAVYFCSGMDNDFHHYGLASPIYTHFTSPIRRYADVIVHRLLAVAIGADCTYPELTDKHKLADICKNLNFRHKMAQYAQRASVAFHTQLFFKSKGIVSEEAYILFVRKNAIVVLIPKYGLEGTVFFEEKDKPNPQLIYDDEIPSLKIEDTVFHVFDKVKVKIMLDSSNLQHQKIRMSLVEPQIPGISIPTDTSNMDLNGPKKKKMKLGK | Function: Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. DIS3 has both 3'-5' exonuclease and endonuclease activities.
Sequence Mass (Da): 109003
Sequence Length: 958
Subcellular Location: Cytoplasm
EC: 3.1.13.-
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Q08162 | MSVPAIAPRRKRLADGLSVTQKVFVRSRNGGATKIVREHYLRSDIPCLSRSCTKCPQIVVPDAQNELPKFILSDSPLELSAPIGKHYVVLDTNVVLQAIDLLENPNCFFDVIVPQIVLDEVRNKSYPVYTRLRTLCRDSDDHKRFIVFHNEFSEHTFVERLPNETINDRNDRAIRKTCQWYSEHLKPYDINVVLVTNDRLNREAATKEVESNIITKSLVQYIELLPNADDIRDSIPQMDSFDKDLERDTFSDFTFPEYYSTARVMGGLKNGVLYQGNIQISEYNFLEGSVSLPRFSKPVLIVGQKNLNRAFNGDQVIVELLPQSEWKAPSSIVLDSEHFDVNDNPDIEAGDDDDNNESSSNTTVISDKQRRLLAKDAMIAQRSKKIQPTAKVVYIQRRSWRQYVGQLAPSSVDPQSSSTQNVFVILMDKCLPKVRIRTRRAAELLDKRIVISIDSWPTTHKYPLGHFVRDLGTIESAQAETEALLLEHDVEYRPFSKKVLECLPAEGHDWKAPTKLDDPEAVSKDPLLTKRKDLRDKLICSIDPPGCVDIDDALHAKKLPNGNWEVGVHIADVTHFVKPGTALDAEGAARGTSVYLVDKRIDMLPMLLGTDLCSLKPYVDRFAFSVIWELDDSANIVNVNFMKSVIRSREAFSYEQAQLRIDDKTQNDELTMGMRALLKLSVKLKQKRLEAGALNLASPEVKVHMDSETSDPNEVEIKKLLATNSLVEEFMLLANISVARKIYDAFPQTAMLRRHAAPPSTNFEILNEMLNTRKNMSISLESSKALADSLDRCVDPEDPYFNTLVRIMSTRCMMAAQYFYSGAYSYPDFRHYGLAVDIYTHFTSPIRRYCDVVAHRQLAGAIGYEPLSLTHRDKNKMDMICRNINRKHRNAQFAGRASIEYYVGQVMRNNESTETGYVIKVFNNGIVVLVPKFGVEGLIRLDNLTEDPNSAAFDEVEYKLTFVPTNSDKPRDVYVFDKVEVQVRSVMDPITSKRKAELLLK | Function: Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. DIS3 has both 3'-5' exonuclease and endonuclease activities. The exonuclease activity of DIS3 is down-regulated upon association with Exo-9 possibly involving a conformational change in the catalytic domain and threading of the RNA substrate through the complex central channel. Structured substrates can be degraded if they have a 3' single-stranded extension sufficiently long (such as 35 nt poly(A)) to span the proposed complex inner RNA-binding path and to reach the exonuclease site provided by DIS3. Plays a role in mitotic control.
Sequence Mass (Da): 113707
Sequence Length: 1001
Subcellular Location: Cytoplasm
EC: 3.1.13.-
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P62280 | MADIQTERAYQKQPTIFQNKKRVLLGETGKEKLPRYYKNIGLGFKTPKEAIEGTYIDKKCPFTGNVSIRGRILSGVVTKMKMQRTIVIRRDYLHYIRKYNRFEKRHKNMSVHLSPCFRDVQIGDIVTVGECRPLSKTVRFNVLKVTKAAGTKKQFQKF | 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 .
PTM: Citrullinated by PADI4.
Sequence Mass (Da): 18431
Sequence Length: 158
Subcellular Location: Cytoplasm
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P08708 | MGRVRTKTVKKAARVIIEKYYTRLGNDFHTNKRVCEEIAIIPSKKLRNKIAGYVTHLMKRIQRGPVRGISIKLQEEERERRDNYVPEVSALDQEIIEVDPDTKEMLKLLDFGSLSNLQVTQPTVGMNFKTPRGPV | 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 .
PTM: Ubiquitinated at Lys-103 by RNF14 and RNF25 in response to ribosome collisions (ribosome stalling).
Sequence Mass (Da): 15550
Sequence Length: 135
Subcellular Location: Cytoplasm
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Q6QAP6 | MGPQGFYWSHPRKFGQGSRSCRVCSNRHGLIRKYGLNMCRQCFRQYAKDIGFIKLD | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Sequence Mass (Da): 6600
Sequence Length: 56
Subcellular Location: Cytoplasm
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P46791 | IPVTKLGRLVKDMKIKSLEEIYLFSLPIKESEIIDFFLGASLKDEVLKIMPVQKQTRAGQRTRFKAFVAIGDYNGHVGLGVKCSKEVATAIRGAIILAKLSIVPVRRGYWGNKIGKPHTVPCKVTGRCGSVLVRLIPAPRGTGIVSAPVPKKLLMMAGIDDCYTSARGCTATLGNFAKATFDAISKTYSYLTPDLWKETVFT | 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 (By similarity). Plays a role in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity).
PTM: Citrullinated by PADI4 in the Arg/Gly-rich region.
Sequence Mass (Da): 22047
Sequence Length: 202
Subcellular Location: Cytoplasm
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P25443 | MSAPEAQQQKRGGFGGRNRGRPNRRGPRNTEEKGWVPVTKLGRLVKAGKITTIEEIFLHSLPVKEFQIIDTLLPGLQDEVMNIKPVQKQTRAGQRTRFKAVVVVGDSNGHVGLGIKTAKEVAGAIRAGIIIAKLSVIPIRRGYWGTNLGQPHSLATKTTGKCGSVTVRLIPAPRGSGIVASPAVKKLLQLAGVEDVYTQSNGKTRTLENTLKAAFVAIGNTYGFLTPNLWAEQPLPVSPLDIYSDEASAQKKRF | 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 . uS5 is important for the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly .
PTM: N-terminally acetylated by acetyltransferase NatA.
Sequence Mass (Da): 27450
Sequence Length: 254
Subcellular Location: Cytoplasm
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Q2PQM1 | MKLNVSYPATGCQKLFEVNDEHKLRVFYEKHMGQVVEADILGDEWKGYMLRISGGNDKQGFPMKQGVLTHDRVRLLLKKGHSCYRPRRTGERKRKSVRGCIVDANMSVLALVIVKKGEKDIPGLTDTSVPRRLGPKRASKIRKLYNLSKVDDVRPYVIRRPLPAKDNKKAISKAPKIQRLITPVVLQRKRRRIALKKKRQAASKEAAADYAKLLAQRKKESKAKREEAKRRRSASMRESKSSISSDKK | Function: Component of the 40S small ribosomal subunit. Plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA. 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: Ribosomal protein S6 is the major substrate of protein kinases in eukaryote ribosomes.
Sequence Mass (Da): 28370
Sequence Length: 248
Subcellular Location: Cytoplasm
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Q6G7P4 | MQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNVGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIGPYDKNENIDFLREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNGERVEIS | Function: Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 17920
Sequence Length: 159
EC: 2.7.11.1
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P17906 | MIQVEENEHIQTLVYQLNKEGKSICGDSFFMKADDKELICAVADGLGSGSLANESSAAIKDLVENYASEDVESIIERCNQAMKNKRGATASILKINFEQRQFTYCSVGNVRFILHSPSGESFYPLPISGYLSGKPQKYKTHTATYEKGSKFIIHTDGLNVPDIRSHLKKGQSVEEISNSLKMYTTSRKDDLTYILGQLS | Function: Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.
Catalytic Activity: H2O + O-phospho-L-serine = L-serine + phosphate
Sequence Mass (Da): 22144
Sequence Length: 199
EC: 3.1.3.3
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Q2SBB3 | MAKRKLSKQQKWRIQKIQDERTKRATRKETQLESQLSGGELSAEQEGLIIAHYGQQLAVEALEPPHAGQIFRCYVRANIDSLVTGDLVIWRAGPDNSGVIVARQPRESALKRPDKFGQLKPIAANIDQILIVIAAEPEPHHNLVDRYLVASEAVGIPPLIILNKQDLINDANRDALQQFKDQYQQLGYEWIDASTNTQSGLDDLKQHLAHKTSIFVGQSGVGKSSLIKMLLPEEDVKVGDLSENVRKGTHTTTTAKLFHLPSGGDLIDSPGIREFGLWHIDEHTLEDGFVEFRPHLGHCRFRNCRHIQEPGCALQSAQESGEILTSRMESFLRIRESLQEQDIHEENL | 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): 39143
Sequence Length: 348
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q5FJH9 | MKLAQGTVVGLIAGYYDVETATGIVRTRARGVFRQKKQKPAVGDRVEIQIDDKGMSYLVEILPRINRIGRPAVANVSHVLLVISAVEPDFSLELLDRFLTFFSWQKVNVTIYLSKADLISEQRLNEIKESLDYYQKIGYPVFIDYHHLEEKIGDMIKDNQIWTLAGQSGAGKSTLLNHLKKDANQTTGAISTSLNRGKHTTRKVELFKLGHGFLADTPGFSSIDLTPIKLNELCNYFIEFKRASKKCKFRGCQHIKEPGCEVKKLLEEGKILHSRYDDYLAMRTEINEGRMPEYLK | 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): 33657
Sequence Length: 296
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q044G6 | MNKAQGTIVSAISGYYDVEIENEVVRTRARGVFRDRKQKPLVGDRVVVQLDNQGMNYLIEILPRTNEIGRPAVANVSKVLLVISAVEPDFSLELLDRYLTFFAWKNVGVVIYLSKADITPTEKLKAIKCKLDYYQKIGYSVFEDAEELERQLPTMIQKDQIWTLAGQSGAGKSTLLNKLENEANQETGAISTALNRGKHTTRQVKLFKYSSGFIADTPGFSAIDLFKIKVDELENYFYDLKDASVKCKFRRCQHIKEPGCEVKKLIEEGKIAKSRYDSYLKIRQEISENRMPEYLKK | 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): 33911
Sequence Length: 297
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q8EZ61 | MSQPNSILMSYGWDPSIYLEEPKLLEGLKPGRVLAVYGEYSKIIIEQGEKKGIFSGALMASGESIVTGDWVLIREIEGDELCIVEKILPRKTFLRRSNPGKRKGSQAIASNIDLLLVIMGLDNDYSPRRIERYLFLAKVSGAQVTIVLNKKDLCMDPENKFMEIKTIAGETPIEMISALDLKQTRTILQWIDPGKTITFLGSSGAGKSTIINSLLGGEIQKTNEVKVSDGTGKHTTTRRELFLLPSGGVLMDNPGIREVGLFSEGSEDELEEVFPEIAVAAEECRFNDCSHNEEPNCGVVAAVKDGRISEARYFSYLKLSKELMAYQALNDPEEARKKKQKDKQMSKALQKRLKDKGRK | 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): 39938
Sequence Length: 359
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q8YG65 | MMRQYELVERVQRYKPDVNEALLNKAYVYAMQKHRSQKRASGDPYFSHPLEVAAILTDMHLDEATIAIALLHDTIEDTTATRQEIDQLFGPEIGKLVEGLTKLKKLDLVSKKAVQAENLRKLLLAISEDVRVLLVKLADRLHNMRTLGVMREDKRLRIAEETMDIYAPLAGRMGMQDMREELEELAFRYINPDAWRAVTDRLAELLEKNRGLLQKIETDLSEIFEKNGIKASVKSRQKKPWSVFRKMESKGLSFEQLSDIFGFRVMVDTVQDCYRALGLIHTTWSMVPGRFKDYISTPKQNDYRSIHTTIIGPSRQRIELQIRTREMDEIAEFGVAAHSIYKDRGSANNPHKISTETNAYAWLRQTIEQLSEGDNPEEFLEHTKLELFQDQVFCFTPKGRLIALPRGATPIDFAYAVHTDIGDSCVGAKVNGRIMPLMTELKNGDEVDIIRSKAQVPPAAWESLVATGKARAAIRRATRSAVRKQYSGLGMRILERAFERAGKPFSKDILKPGLPRLARKDVEDVLAAVGRGELPSTDVVKAVYPDYQDTRVTTQNNPAKAGEKGWFNIQNAAGMIFKVPEGGEGAAAKVDPAATTPKPGKRALPIRGTNPDLPVRFAPEGAVPGDRIVGILQPGAGITIYPIQSPALTAYDDQPERWIDVRWDIDDQMSERFPARISVSAINSPGSLAEIAQIAAANDANIHNLSMVRTAPDFTEMIIDVEVWDLKHLNRIISQLKESASVSSAKRVNG | Function: Functions as a (p)ppGpp synthase. In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. It is necessary for persistence in mice, essential for intracellular growth of Brucella and required for expression of the type IV secretion system VirB and therefore plays a role in adaptation of Brucella to its intracellular host environment.
Catalytic Activity: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
Sequence Mass (Da): 83999
Sequence Length: 750
EC: 2.7.6.5
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O05403 | MDKRLQQLREEYKNVQIPKELDIIVEKALQQEPKKKRIVMWPTSAAIAAAILFTALVNINPDAAQAMSKIPVIGKIVKAITFIEIKEEKDQSSIDVKTPALSGLSNKELENSINEKYLKESQQLYKEFIQSTSKNKKGHLSIYSDYETVTDTPDLLSIRRNIETTQASSYTQSRYITIDKKNDILLTLKSLFKDERYIKVISQNIKEQMKQQMKEDPNKIYWLTDEDAEPFKTILPDQTFYITEDHKLVISFDEYEVAPGYMGVTEFTIPTGVISNLLVGERYIR | Function: Anti-sigma factor for SigV. Negatively regulates SigV activity through direct interaction.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32868
Sequence Length: 285
Subcellular Location: Cell membrane
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Q5WLH2 | MKTCHSHDELIHIYLDGDATKEQKEELYAHLQSCPSCREHLQELKKSIAFIQSSSHIEAPEGFTAGVMAKLPKTKKTAKWKLKAKRHPILVAAAIFLIMMSAAFFSAWSHTTDGIAVSGNGPFVIDKEAGVVVVPEGEVIDGDLVVRNGTLVLEGEVRGNVLLINSRFNKDTLYASPNQVTGEIEEVDKALSWAWYNMKEFFNEVVAVFDAGEDDPHSTDN | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: Is the anti-sigma factor for SigW. The presence of RsiW leads to the inactivation of SigW, and its proteolytic destruction to sigma-W activation (By similarity).
PTM: Is processed by three successive proteolytic events. First, the extracellular region of RsiW is cleaved by PrsW (Site-1 cleavage) in response to cell envelope stresses. Next, it undergoes cleavage at an intramembrane site (Site-2 cleavage) mediated by RasP. This cleavage uncovers a cryptic proteolytic tag with conserved alanine residues in the transmembrane segment, that is recognized mainly by the ClpXP protease, which completely degrades the protein in the cytoplasm and leads to the induction of the sigma-W-controlled genes (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24429
Sequence Length: 221
Subcellular Location: Membrane
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Q45588 | MSCPEQIVQLMHMHLDGDILPKDEHVLNEHLETCEKCRKHFYEMEKSIALVRSTSHVEAPADFTANVMAKLPKEKKRASVKRWFRTHPVIAAAAVFIILMGGGFFNSWHNDHNFSVSKQPNLVVHNHTVTVPEGETVKGDVTVKNGKLIIKGKIDGDVTVVNGEKYMASAGQVTGQIEEINQLFDWTWYKMKSAGKSVLDAFNPNGEE | Cofactor: Binds 1 Zn(2+) ion per subunit. Absence of the Zn(2+) (in a residue 1-80 fragment) does not prevent interaction with SigW, nor does it change the overall conformation of RsiW, although a disulfide bond can form between Cys-3 and Cys-37 .
Function: The anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-W (SigW). Holds SigW, its cognate ECF sigma factor, in an inactive form until released by regulated intramembrane proteolysis (RIP). SigW and RsiW mediate cell response to cell wall stress . RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, PrsW) , then within the membrane itself (site-2 protease, S2P, RasP) , while cytoplasmic proteases finish degrading the anti-sigma factor, liberating sigma-W .
PTM: Is processed by successive proteolytic events. First, the extracellular region of RsiW is cleaved by PrsW (site-1 cleavage) in response to cell envelope stresses . In a reconstituted E.coli system PrsW cuts between Ala-168 and Ser-169 followed by trimming by E.coli Tsp; the endogenous extracellular exopeptidase responsible for the event in B.subtilis has not been identified . Next, it undergoes cleavage at an intramembrane site (site-2 cleavage) mediated by RasP . This cleavage uncovers a cryptic proteolytic tag with conserved alanine residues in the transmembrane segment, that is recognized mainly by the ClpXP protease, which completely degrades the protein in the cytoplasm and leads to the induction of the sigma-W-controlled genes .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23341
Sequence Length: 208
Domain: The cytoplasmic domain is able to inactivate SigW and the extracellular and transmembrane domains are crucial for sensing and transducing the signal that triggers SigW activation . The N-terminus binds the zinc ion and is followed by a long helix (about residues 40-80) that fits into a hydrophobic surface groove on SigW, probably blocking its ability to interact with the -10 and -35 promoter elements .
Subcellular Location: Cell membrane
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Q9KG49 | MSCEQHYRTLIDKYIDGEATAEERQELNEHLETCDACFEYMLEVRKVVAFVQSASHVQAPEGFTENVMKNLPKRKQTNRFKVWMRRYPLAVAAAVFVLLMSTSLFSMWSSDGEHVTVTGTGNVSIDQESGRVIVPEGEVIQGDLVVRNGELIIEGEVQGNVLLVNSSQYLASPGSVSGEIDEVNQILDWIWYHTKKFLTKVIDISDEKNSPSS | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: Is the anti-sigma factor for SigW. The presence of RsiW leads to the inactivation of SigW, and its proteolytic destruction to sigma-W activation (By similarity).
PTM: Is processed by three successive proteolytic events. First, the extracellular region of RsiW is cleaved by PrsW (Site-1 cleavage) in response to cell envelope stresses. Next, it undergoes cleavage at an intramembrane site (Site-2 cleavage) mediated by RasP. This cleavage uncovers a cryptic proteolytic tag with conserved alanine residues in the transmembrane segment, that is recognized mainly by the ClpXP protease, which completely degrades the protein in the cytoplasm and leads to the induction of the sigma-W-controlled genes (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23947
Sequence Length: 213
Subcellular Location: Membrane
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Q8ETN0 | MSCSKDYLNLMHIYLDGDITREDESKLSRHLEDCESCQKHFHELNRTITLMRSAERVEAPDGFTENVMANLPSEKKTVKYRRWFKLHPMWTAAAIFLVLMAGGMISTWTHSSDQLVVSAQNELIVDGDTVIVPAGVTVPGDVLVKNGDLLLLGTVDGDVTIFNGKILDNDSEMNGEGLMASVGGVNGELETIDRMFEWIWYNIKNFFKGVFSF | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: Is the anti-sigma factor for SigW. The presence of RsiW leads to the inactivation of SigW, and its proteolytic destruction to sigma-W activation (By similarity).
PTM: Is processed by three successive proteolytic events. First, the extracellular region of RsiW is cleaved by PrsW (Site-1 cleavage) in response to cell envelope stresses. Next, it undergoes cleavage at an intramembrane site (Site-2 cleavage) mediated by RasP. This cleavage uncovers a cryptic proteolytic tag with conserved alanine residues in the transmembrane segment, that is recognized mainly by the ClpXP protease, which completely degrades the protein in the cytoplasm and leads to the induction of the sigma-W-controlled genes (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23927
Sequence Length: 213
Subcellular Location: Membrane
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P35166 | MMKSEWNEEQIKELLSQLPAVKDHRSPQDIYKRLTMAKRKNKPAVRWIGPACAAAIAVYIAFIISPHFFDQAQPQQKEASQENAVTKTETEDSPKAASSLDQTSFVVPEKEQDNYITVAVADADTSAIIPVSIQKTNADQTIQDMLFESSELGILDHAITIPTFIDEVEIKEKPKQKELSIRVHQPATAFSIKDDTLLKKLLKESLKWSPYEKVKFLSDQNETGVRIGSYGTFTEISIPKQSKRSYYLYQNKQGQDFLVPSNHSFDTVKEAIKEMESSSQEDTTPLIQAGAVQSVTKKQKHLYIRFSKESEVDDSIAGILMIEGLLLTAKEFGFTEVTFTETRTKKIGKYDISDAIPVPAAPNPISLN | Function: The anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigX, inhibits SigX activity and stabilizes it.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41295
Sequence Length: 368
Subcellular Location: Cell membrane
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Q7U1Z7 | MTEHTDFELLELATPYALNAVSDDERADIDRRVAAAPSPVAAAFNDEVRAVRETMAVVSAATTAEPPAHLRTAILDATKPEVRRQSRWRTAAFASAAAIAVGLGAFDLGVLTRPSPPPTVAEQVLTAPDVRTVSRPLGAGTATVVFSRDRNTGLLVMNNVAPPSRGTVYQMWLLGGAKGPRSAETMGTAAVTPSTTATLTDLGASTALAFTVEPGTGSPQPTGTILAELPLG | Function: An anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigK. ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). However, in M.bovis this protein is probably dysfunctional, due to at least 1 of the 2 naturally occurring polymorphisms in its gene, when compared to M.tuberculosis. This leads to an increased expression of SigK-regulated genes, such as mpb70 and mpb83. RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, Rip1), while cytoplasmic proteases finish degrading the regulatory protein, liberating the sigma factor.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24013
Sequence Length: 232
Domain: The cytosolic domain interacts with sigma factor SigK.
Subcellular Location: Cell membrane
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A3Q5U1 | MTEPNNTDLLDLATPYALHAVSIDERFEIDRWLATAPPEVADAFTDEVRSVQETMAVLSAATATEPPAHLRDNVLAMVADDPVRDLGSARRRRGGESRWRTAVLAAAAVAVVGLGALGVGLALRPAVSPTTADQVFAAPDVQTVSGPIPGGGTATVVFSKERDAGVLVMNDVAPPKPGTVYQMWLVGSDGPHSAGTMDDKAISPSTTAVLSDIGTSQALAFTVEPPGGSQRPTSPAFAELPLT | Function: An anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigK. ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, Rip1), while cytoplasmic proteases finish degrading the regulatory protein, liberating the sigma factor (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25147
Sequence Length: 243
Domain: The cytosolic domain interacts with sigma factor SigK.
Subcellular Location: Cell membrane
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Q8RDC8 | MKAKKKWGQNFIFDKNLLSKIVRASGVGEEDFVLEVGTGHGGLTEELAKKVKKVVSFEIDKELFEMSREKLKIYKNVVIINEDILEVDLLEIAQEHFDGNSFKVVANLPYYITSPIIMKMLDCKLVKEMTVLVQKEVAERICALPGTKDYGMLTVFVNFKAKPEILFNLPPKVFVPPPKVESSLLKLKVYDKPLVEVKDEKLFSEVVRAAFGQRRKVLSNSLKVLGFSKEVLHETLLKVGISPQARGETLSIDQFANLANALYLLIKE | 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): 30287
Sequence Length: 268
Subcellular Location: Cytoplasm
EC: 2.1.1.182
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Q7VGZ3 | MEEYRSKKRFGQNFLQDSHFLHKIIQSIPDIPIQCIEIGVGLGDLTQELLKIESLIAYEVDLDLCSLLNKKFSNQIQSGRLNIIYKDILNLPSQQAWLHTHEYKVVSNLPYYIATHIILRLLRDRFCRAFLVMTQKEVAQKFCATTGQKEFCALSVLVESFGKAKMLFEVPKEAFSPMPKVTSSVFVIHKYSQQNQIEDSFLCDLESFLKIAFYAPRKTLFKNLSQVFDKKLLEEVFENENIKSNARAHEVKTKSFHHILQFLKKRNDNGKQTLTRTTKQRPS | 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): 32926
Sequence Length: 283
Subcellular Location: Cytoplasm
EC: 2.1.1.182
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O25972 | MVVAKKSLGQHFLTDESFLDRIVNALPPLNPLKLVEIGVGLGDLTLKLLDRYPLKTYEIDSHLCEKMRSKLKAQKKPFKLELVEKDALFLKEEEPYFLISNLPYYIATRLVLNAFKDPKCRGLLVMTQKEVALKFCAKDSQNALSVLAHTIGNATLLFDVPPSAFSPPPKVFSSVFEVIKEPLKEKALASLAQAPFFEEALQKGFEMLEDFLKACFSSPRKTLSNNLKKSVSYREKLDKVLDFLALENQPTSVRASEIKDYLKLLNYLLKG | 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): 30644
Sequence Length: 271
Subcellular Location: Cytoplasm
EC: 2.1.1.182
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B4U9C8 | MLKPKKTFGQNFLKSKNIAHSIVELLDVKEDDTVIEIGPGLGALTEFLYQKPKKELILVELDKDIFGLLEKKYKNATLLNEDASLVDLSSYKNLKIIGNLPYNMYASILINMINQEKHISKMVFMLQKEVGERLITDSKDKSWLWAYANTYFNIHYAFSVPGRFFEPVPKVTSCVLVFDKKEDTPSFEKQNYMDFLKKMFSNRRKMLKHKLNNIEDKYALKRVEELSLEDIKYIYNTLSCFNKNIFTSTPAL | 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): 29381
Sequence Length: 252
Subcellular Location: Cytoplasm
EC: 2.1.1.182
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Q28RD6 | MVAIDGLPPLRDVIAAHGLSARKALGQNFLLDLNLTAKIARLAGDLTSVDVLEVGPGPGGLTRGLLAEGARRVVAVEKDPRCLPVLAEIEAIYPGRLKVLNADALELDWAADLQAPRKIVANLPYNVGTELLVRWLTPASWPPPWESLTLMFQREVAERIVAQPGSKTYGRLAILSQWRADPRIVMGLPPEAFTPPPKVHSAVVHFTALPAPRFPADARVLTRVVAAAFGQRRKMLRAALKGLAPDIEDRLVAAGLKPTDRAEQVPLEGFCALARVMEDVITPSHGREA | 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): 31219
Sequence Length: 289
Subcellular Location: Cytoplasm
EC: 2.1.1.182
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Q1ILA1 | MPKMAAEKNSKPAKKAKLGQNFLSDASGALKIVEALGDISDATVVEIGPGRGAITDHLAKRAKRLIAVEIDRVLAAQLRLRYSRLENVEILEADILAVELSTVLAQRIGPLRDLRPTKPEKVRIIGNLPYYITSDILLRLFEAHALIDFAVIMVQKEVADRIAAKPGTRDYGLLSATSQLYTHVEKLFTLPPGSFNPAPQVHSTVLKLQMEPKLEALGVDEEGFDSFLKLIFGQKRKTLFNNLRVAYDMAKAREAMKAVGLKSDVRAEAVALEKTAQLYNELRKG | 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): 31454
Sequence Length: 285
Subcellular Location: Cytoplasm
EC: 2.1.1.182
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Q92GV0 | MLPSIAKHAALHQVNPLKKHGQNFIFDSSLCDKIVRASNLAENSRVLEIGPGTGGLTRSILQKNPESLTVIETDARCLPLLNEIKEYYPNLNIIKQDALKINLTDLSYDIVNSVGFAYKKREVKPITNRRANDIGESKSIDYKVTIISNLPYHIGTELVIRWLKEARLITSMTLMLQKEVVERICAIPSTKAYGRLSVICQLIAKVEKCFDVAPTAFYPPPKVYSAIVKLIPLENPPSIALINKVEQITKLAFAGRRKMIKSSLKNLVPNIYEVLTQLKINDNYRAENLAPQDYLRIAEIL | 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): 33866
Sequence Length: 301
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
Q1AXL9 | MSPSLSGRTPRPKKRLGQHFLKDANTARIVAAGLTERDVVLEIGPGRGFLTAFLAERAGLVHAVEIDPDVLPELRRAVGARGNVRIHEADALRFDYGALSPPPNRLAANLPYNIASPLVLRLLEEVPSLERMRFMVQLEVALRMTARPGSKDYGAYAVLIQLLSRPEVAHRVSPRVFDPPPRVRSAVVELERRRDAPEDYRGVKELVAAAFRSRRKRLPNNLPGPLRERAEEALAGLGHGPDARAEELSPEDFVALYRRISP | 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): 29070
Sequence Length: 262
Subcellular Location: Cytoplasm
EC: 2.1.1.182
|
Q9I7A9 | MNPRLAACQALAAVLAGRASLSGALPPQLDKVAPRDRGLTQELAFGAARWQPRLQALAARLLQKPFKAADTDIHALLLIGLYQLLYTRIPPHAAIGETVGCADKLKKGWAKGVLNAVLRRAQREGETLLAEVDRDPSARLGHPRWLLKALKQAWPEQLDALCAANNAHPPMTLRVNRRHGERDAYLAELAEAGIKARACDYSRDGIQLAAPRDVRELPGFAEGRVSVQDEAAQLAAEQLESAPGQRVLDACCAPGGKTCHLLETQPELAEVVAVDLEESRLVRVRENLQRLGLQASLVAADARATGEWWDGKPFQRILLDAPCSATGVIRRHPDIKLARKPEDIAALAHLQGELLDALWPTLEVGGVLLYATCSVMPAENSDSIAAFLARTPGARELDLPGPWGMKQPHGRQLLPQVEGHDGFYYAKLIKISAR | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 47154
Sequence Length: 434
Subcellular Location: Cytoplasm
EC: 2.1.1.176
|
P17136 | MTVGKSSKMLQHIDYRMRCILQDGRIFIGTFKAFDKHMNLILCDCDEFRKIKPKNSKQAEREEKRVLGLVLLRGENLVSMTVEGPPPKDTGIARVPLAGAAGGPGIGRAAGRGIPAGVPMPQAPAGLAGPVRGVGGPSQQVMTPQGRGTVAAAAAAATASIAGAPTQYPPGRGGPPPPMGRGAPPPGMMGPPPGMRPPMGPPMGIPPGRGTPMGMPPPGMRPPPPGMRGLL | Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (By similarity). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). As part of the U7 snRNP it is involved in histone pre-mRNA 3'-end processing (By similarity).
PTM: Methylated by PRMT5 (By similarity). Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine (By similarity).
Sequence Mass (Da): 23656
Sequence Length: 231
Subcellular Location: Cytoplasm
|
O51333 | MKQIVLDENCLAGNFIIVKDAKIYHHLVNVRRLKKGDKLNILLKDKELRASEIVKIGSNFIKFTTNKIDKIEKNNFEISIFISSLKGRKIDLVLRQVVEIGVSEINIINADRSVSKIDINNASAKILRFSKIIDEALKQSGNKIVPKINFYNNFFYLPYSFCTTRYYVAHPSGMILSKNESFDNFGKIGIIIGPEGCFSESEIVFFKEKGFNFVRFNTPILRADTAIIYSLAYFKALLEDYNG | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27769
Sequence Length: 243
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
O66552 | MHVFYSEERRGNLLILREGEVKHFRVRRIEKDEEFGVIHEGKIYVCKVRREDKREISCEIVEELETKLPPKDITLYQSVTVDLKTMDTIVRQATELGVLTFVPIISERSFQKEEAILKKTEKWKRIVIEAMKQSRRPIPMEIKKPVRLSDLIPESEENIILDNFYEGVKPKDVNLEAKTYSVVVGPEGGFSKRESQILREKGFKSVLLEPYTLRTETAVVSIVSILMNF | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26683
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
P54461 | MQRYFIELTKQQIEEAPTFSITGEEVHHIVNVMRMNEGDQIICCSQDGFEAKCELQSVSKDKVSCLVIEWTNENRELPIKVYIASGLPKGDKLEWIIQKGTELGAHAFIPFQAARSVVKLDDKKAKKKRERWTKIAKEAAEQSYRNEVPRVMDVHSFQQLLQRMQDFDKCVVAYEESSKQGEISAFSAIVSSLPKGSSLLIVFGPEGGLTEAEVERLTEQDGVTCGLGPRILRTETAPLYALSAISYQTELLRGDQ | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28802
Sequence Length: 256
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
P57488 | MFTSTAIKNKKIPRIYIEDDLDLNQFYFLSDENRHYVTKVLRMKIEDILEIFNNTHYIFFAKIIDISKKIIKIQTFKKILKNLESPLHIHLGQVISKNEKMDFTIQKSIEIGVKTITPLFFENDHFQKKRINFSNKIKRWEKIAISACRQCNRNIIPKIKIPMNVFHWCENNQNNDKKIIFHPKSTLTMKCLTEPIKYIQIIIGSERGFFNDEFQKIIKYGFIPIRLGPRILRTETASVVAITALQTMFGDFK | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29962
Sequence Length: 253
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
P37995 | MRIPRIFHPDTLTPQGGETDLSEDAANHVGRVLRMSAGQALQLFDGSNQVFDAEIVQAGKKNVRVRYAAGQTENRESPLHLHLGQVMSRGEKMEFTIQKSIELGVNVITPLLSERCGVKLDGERLEKKIAQWQKIAIAACEQCGRNRVPEIRPVQTLESWCAEPDNGLKLNLHPRAAHSINTLPLPVSRIRLLIGPEGGLSADEIAMTATQGFTDILLGPRVLRTETTALTAITALQVRFGDLG | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26740
Sequence Length: 244
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
P0AGL8 | MRIPRIYHPEPLTSHSHIALCEDAANHIGRVLRMGPGQALQLFDGSNQVFDAEITSASKKSVEVKVLEGQIDDRESPLHIHLGQVMSRGEKMEFTIQKSIELGVSLITPLFSERCGVKLDSERLNKKLQQWQKIAIAACEQCGRNRVPEIRPAMDLEAWCAEQDEGLKLNLHPRASNSINTLPLPVERVRLLIGPEGGLSADEIAMTARYQFTDILLGPRVLRTETTALTAITALQVRFGDLG | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26978
Sequence Length: 243
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
Q9ZKD2 | MRFVYHPLAKEPTLKIEGESYIHLYRSRRIKSASRLDLRNLKDGFLYTYEHAEIAKKHALLRLVGVQPLEIMANKKTHLILSVIEIKNIEKILPFLNQLGVSKLSLFYADFSQRNEKIDSAKLERFQKILIHSCEQCGRSVLMELEAFSNTKEALKAYPKASVLDFNGETLPASADFEKGVIIGPEGGFSEQERGYFKEREIYRIPLDMVLKSESACVFVASIAQI | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25827
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
O50188 | MYRFFVNEKQENFFILTNLTLNHIKTVRIKNENFICVYQNEFYLVRLVPNSNKAEIIEKIKGNNEPKNKVVLALAILKTKSFEFAIQKAVEIGVNEIWPFYSKNVSQKLSGDLEKKLKRWEQICLHSAQQSFRNLIPKINLPINYKDLLEQAKNFPVKLISFERAKNNINIPDNPQNTIIIIGPEGGFDDVEIQQAEKLGFQSITLGKRILRSETAAIFLLTKCIKD | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26286
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
P67203 | MVAMLFYVDTLPDTGAVAVVDGDEGFHAATVRRIRPGEQLVLGDGVGRLARCVVEQAGRGGLRARVLRRWSVPPVRPPVTVVQALPKSERSELAIELATEAGADAFLAWQAARCVANWDGARVDKGLRRWRAVVRSAARQSRRARIPPVDGVLSTPMLVQRVREEVAAGAAVLVLHEEATERIVDIAAAQAGSLMLVVGPEGGIAPDELAALTDAGAVAVRLGPTVLRTSTAAAVALGAVGVLTSRWDASASDCEYCDVTRR | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27653
Sequence Length: 262
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
Q92J59 | MKYNRIYINSRLAENSKIELASDHHVHYVKTVLRLKVNDGLRLFNGTDGEFLAQINDIGKNNLSVRLKEQLKKPYTKSTLTLAVAIIKQDKLMLAINMATQLGITKIIPLITRWCQFRSVNIERLTKCVIEATEQSERLTPPIIEKAITIQDYLKKNNNLMLYANEHEKEENSILRISSSLSNSDITIIVGPEGGFTNDELELLASYKNTKSISLGSNILRAETAAITAIAQVRLLGSHCEEIA | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27437
Sequence Length: 244
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
Q9ZDZ5 | MKYNRIYINSNLAENSKLELARDYVHYVKTVLRLKIHDSLRIFNGSDGEFLAQITQIGKNNLSVVLKEQLKKAYIESALTLAVAIIKSDKLMLTINMATQLGITKIIPLITRRCQFRTVNIERLMKCVIEATEQSERLNPPIIEQAITLKDYLKKNNNLILYANEHEKVKHSILHISSLLSKDIAIIIGPEEGLLMMS | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22603
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
P72667 | MLAKAFAGSKSHKILINAWFTTLPGQCQKPIVQFVLSPILVSTNLTPSILSLPVQEKSSSSFVMAYRLVVAPEQIIEATVTLTTAQLHYLQRVLRLQKGDGFMVLDGGGGVWRAQLNDLAHGTAQLLETVSEQNELPLPVTLAIALPKGSGFEEIIRPCTELGATAFQPLLTERTLLKPSQNKLERWQRIVTEAAEQSERQWLPPVAAPLTFGQFVEKVAGPETLALLCVTRLNSPMLGAYLKQSNLPAQIVLATGPEGGWTDNEISLAIAKGFQPVSLGKRILRAVTAPTVALAQINALLES | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32775
Sequence Length: 303
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
O83075 | MNIVLFEQEEVVHGCAVLSFRDSRFCHIKRVLKLSAGACFKAGIINGVKGSARISLATEKYLVAVFEKLEYEDCALFPLHLVIGFPRPIQLRRILRDVSSLGISSIHLVGTELGERSYLDSGLAHMEKMHTYLIRGLEQAGGTKLPLITVSESVRTFCSQHTHILGDSTHQKLILDTKNTLTDLGSAALRGDVLWIAIGSERGWTESERLLFSAMGFRAVDMGRRTLRTETAACAACAVVLANAHAWKRKIPRPGKRSSPISRKNP | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29379
Sequence Length: 266
Subcellular Location: Cytoplasm
EC: 2.1.1.193
|
Q62FS7 | MTVQQRRRPPIASRETLQALLSEGAQALGVALSDAQRGALLDYVALLAKWNAVYNLTAIRDPRQMLIQHILDSLSIVPHLGAHGAAAAALDVGSGGGLPGVVLAIALPGWRVTLNDIVHKKSAFQNQAKAELKLGNLSVVTGRVETLRPGADVPAKFDVIVSRAFADLADFVTLARHLVAPGGSIWAMKGVRPDEEIGRLPDGARVKQMIRLTVPSLDAERHLIEVELDEAI | 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): 24796
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
B9MQF1 | MELLDKVLEYYKVKNPLVVKHLLIKYMNLVLEKNKLFNLTAIENEEEFVIKHIADSLSLLKFIEQENSNQNPVAIDIGSGFGAPGLFVKIAMPSVNVFLNDSNKKKCKFMNEAKESLGISGVNVVCERAEVLGRKEEFREKFDFVFARAVDRLNVLCEYAIPLLKVGGAFLAQKGFECEDEIDLAKNAIEILGGEIYSIEKFVLPYSDEKRSIIIIKKLRQTPSNFPRNTKQIVKKPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 27045
Sequence Length: 238
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q8R6L0 | MKQKSIEMLVQGASSLGITLEMFHVEHFQKFYSLLLEWNQKMNLTAITEEEEVVIKHFLDSLSVIKSGKIKGGEKVIDIGTGAGFPGIPLKIVFPEIGLTLLEASKKKVNFLNFLSQVLLFEGIEVIHGRAEELGKVERFREKFDIATARAVAPLNILLEYAVPFVRVGGHFIAMKGRDIEEVYQCKNALEELKCEIEDVIEVRLPFSDILHHLIVVKKVDVLPSKYPRREKAIRTKPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 27081
Sequence Length: 239
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A0RR76 | MNLPDNFWNKVSEFEIILKQFNKIHSLTNYRDIKPVVEDSMKPLEFLDFNPKIVIDVGSGAGFPAIFLSLILNSSEFHLYEPIAKKSSFLSYVGAALNLKNITVHPSKIESCQKIKADLITSRALSKTLFLIEICRGFYDENTTFLLYKGDGAKEEISNLKCKNSIISSGKRNYLFLKGVKC | 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): 20594
Sequence Length: 182
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
A7I3X1 | MIIKKPENFNEQIEQFGKCLEKFNKIHSITNYNDLSAVIEDSLEGLKFITEMPKVAIDIGSGAGFPAIFLAMVLPYTKWHLFEPNTKKAAFLTYAKVNLKLKNIIIHNTKIENETPFIADLITSRAVMKVPDLIKISHGFFDTHTKFLFYKGSNVKDELGNLKAEIFENNMRKYALLKGNDVC | 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): 20861
Sequence Length: 183
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
B0JYE6 | MILPELFDLWQETLEWQPDGAQQARFQQLYDLILEGNQRFNLTRITQPEEFWEKHLWDSLSGLAWLQKSQPDLLTKSLSVIDLGTGAGFPGVPIAIAYPHWSVTLLDSTQKKINFLEEVIDKLELNNTKTRLGRAEIVGKNLKHNCAYDIVCLRAVGNVDICVNYALPFLKKTGIAILYRGQWSAQDSLSLEENLGKAGGKILEIASFTTPLSESVRHCLYISKK | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 25445
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q2RFJ0 | MRDRDRLLAAFSKDTGITLKPEQIAMIEAYTGLLLDYNQRVNLTAITDREEIWRKHVLDSLLLFLALEIPPAAKVIDIGTGAGIPGLILKIYRPDLEMALLESQNKKVAFLKKAVATLGLQGIECLWGRAEDIGRQKNYRESFDLAVSRGLAGMNTLAEYCLPFVRVGGFMIAYKGPGGEGELNAAARAIEILGGGTKKVWRGSLTGGQEVRQLIIIQKEHPTPPVYPRRPGLPAKRPLQ | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 26444
Sequence Length: 240
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q9KX67 | MLKLIKDSLGKFNLTLTDKQIEDIAFFLEEIYHSNQLFNLTGYKTKELIAEMLGVKTILLAQSLSYIFSNQSLNVIDIGTGAGIPGLIIKIIYPQLNVYLVDSNAKKITFINEVIKKLNFTGVFAILSRVEDNFFLKKYHGYFDYVFSQAVSKIAVLNELGTQLLKINGQIIHFKSRDYQEEIEFAKKHLSDLGLAFNNLYHYQFNSYFLVNVFYNKKAIAPQKYPREWSKIKRELIDDAKH | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 27999
Sequence Length: 242
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
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