ids
stringlengths 6
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stringlengths 11
1.02k
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stringlengths 108
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O69014 | MPDSSTQDKIVMIATDGACKGNPGFGGWGALLRYQGHEKAISGSENPTTNNRMELQAVIEALSCLKKPCQIELSTDSKYVMDGLTRWIHGWQKNGWLTAAKKPVKNADLWKQLLALTRQHDIAWKWVKGHAGHPDNERADQLASDAAIALMQQEKA | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 17251
Sequence Length: 156
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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Q07465 | MKKIVVLLGMLLAPWFSSAVQAKGEAGEFDYYAMALSWSPEHCAIKPADRDQCSRQLGFVLHGLWPQYQRGYPSSCTRERLDPAMEQEFAGLYPSRFLYRHEWEKHGTCSGLSQHDFHQLASDLRQKREDPGRLSVSCRAAAQKPLPAQGGSGQCQRLAGPGQHHGGLRRRWRFLREVYICLNKEGTDAVTCSDEMQKRELPSCGQPDFLLRTVR | Function: One of the few RNases that cleave the phosphodiester bond between any two nucleotide. Shows a preference for adenylic acid.
Sequence Mass (Da): 24410
Sequence Length: 215
Subcellular Location: Periplasm
EC: 3.1.27.-
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P21338 | MKAFWRNAALLAVSLLPFSSANALALQAKQYGDFDRYVLALSWQTGFCQSQHDRNRNERDECRLQTETTNKADFLTVHGLWPGLPKSVAARGVDERRWMRFGCATRPIPNLPEARASRMCSSPETGLSLETAAKLSEVMPGAGGRSCLERYEYAKHGACFGFDPDAYFGTMVRLNQEIKESEAGKFLADNYGKTVSRRDFDAAFAKSWGKENVKAVKLTCQGNPAYLTEIQISIKADAINAPLSANSFLPQPHPGNCGKTFVIDKAGY | Function: One of the few RNases that cleaves the phosphodiester bond between any two nucleotide. Shows a preference for cytidylic or guanylic acid.
PTM: Contains four disulfide bonds.
Catalytic Activity: RNA containing adenosine-cytidine + H2O = an [RNA fragment]-3'-cytidine-3'-phosphate + a 5'-a hydroxy-adenosine -3'-[RNA fragment].
Sequence Mass (Da): 29618
Sequence Length: 268
Subcellular Location: Periplasm
EC: 4.6.1.21
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Q45493 | MKFVKNDQTAVFALGGLGEIGKNTYAVQFQDEIVLIDAGIKFPEDELLGIDYVIPDYTYLVKNEDKIKGLFITHGHEDHIGGIPYLLRQVNIPVYGGKLAIGLLRNKLEEHGLLRQTKLNIIGEDDIVKFRKTAVSFFRTTHSIPDSYGIVVKTPPGNIVHTGDFKFDFTPVGEPANLTKMAEIGKEGVLCLLSDSTNSENPEFTMSERRVGESIHDIFRKVDGRIIFATFASNIHRLQQVIEAAVQNGRKVAVFGRSMESAIEIGQTLGYINCPKNTFIEHNEINRMPANKVTILCTGSQGEPMAALSRIANGTHRQISINPGDTVVFSSSPIPGNTISVSRTINQLYRAGAEVIHGPLNDIHTSGHGGQEEQKLMLRLIKPKFFMPIHGEYRMQKMHVKLATDCGIPEENCFIMDNGEVLALKGDEASVAGKIPSGSVYIDGSGIGDIGNIVLRDRRILSEEGLVIVVVSIDMDDFKISAGPDLISRGFVYMRESGDLINDAQELISNHLQKVMERKTTQWSEIKNEITDTLAPFLYEKTKRRPMILPIIMEV | Cofactor: Binds 1 Ca(2+) cation per subunit. Seen in 1 crystal structure, it is not clear if it is physiologically important.
Function: An RNase that has endonuclease and 5'-3' exonuclease activity, playing a role in both rRNA and mRNA stability and degradation. Endonuclease activity can cleave within 4 nucleotides of the 5'-end of a triphosphorylated RNA. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Preferentially cleaves ssRNA, possibly in AU-rich regions. The 5'-exonuclease activity acts on 5'-hydroxyl and 5'-monophosphate but not 5'-triphosphate ends; it can digest through stem-loop structures if they are not too stable. Required for maturation of 16S rRNA. Acts preferentially on 16S rRNA precursors after association of the 30S and 50S ribosomal subunits. Plays a role in the secondary pathway of 23S rRNA 5' end maturation. Probably also participates in processing of pre-scRNA (the precursor of the signal recognition particle RNA). Major RNase that degrades both RNAs of the type I toxin-antitoxin system BsrE/SR5 .
Sequence Mass (Da): 61517
Sequence Length: 555
Domain: The C-terminal domain (residues 450-555) are required for nuclease activity and dimerization.
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q975G4 | MVIFSYRTRIIYIKKIKNKRDTRAKRYVIFDIISEDNFEIREIEEAVRNSVKELGGKIWLDLSNPKVIMIYNNRGIISTNRIGYKIIIASLPLIKKIKNKEVLLVPRRTTGSLKRAKRLIGIE | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14431
Sequence Length: 123
Subcellular Location: Cytoplasm
EC: 3.1.26.5
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Q9YC00 | MGLIDISVKPQTEQCSEVLRTAGRLGYTAVAIPPESADECMSLEGDGIPRLYRRGYVEASTRRDVRRAAEKLAGVVDFIVVKPLTLEAARYAAANKRVHIIRVDGSNLWAADRGTAEIMAQRGWGALEVSLRNLTLNPGSPAAWRALAVVLRRSFAYGVHVFLASDAEEPHELWSPYSGASLAALLGVPWSHAMLYNSEERLRILLDASRA | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 23083
Sequence Length: 211
Subcellular Location: Cytoplasm
EC: 3.1.26.5
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O27967 | MYDFLRFFPENLPDLGFKSYVFMLEKPKGCGIVIRANSPEELRKKLRGVKRRAIVGIIGKEAVCREAVMRRRVDVILDWEDRELDYATLKLAAEKDVAIELSLSKFLRTEGYKRMHLFERLRQEIMVIRKFDVPFIVTTAAENQYELRTRKQVETFFKFFGAEIPKARLYAQRLVRRYFDENYIMDGFEVEQLSNSGVV | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 23551
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 3.1.26.5
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B0R596 | MYEAVCAHPDGDSTVARLAATAASAGYDGIVVRNWGATSADPDAVGADTDADVVRGTTVSVTDRAGASERIRRRRENAVVVAARASSPSLNRFVAESERVDVLAAPMADGGDVNHVIVKAARTHGVRLEFDFAGVLRASGGDRVQALRGLRKLRELVEHYDAPFVVSGRPASHLHVRSPRELVAVGAEIGFTDAQVRAGLREWTHLAARNRRRLSAEFIAPGVKRGRYEEDP | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 24884
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 3.1.26.5
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Q8TPX2 | MGKPKFYDFCVHAVPDGDSTAQEQVSLGRHFGFSGIALANHSDRLPDRKPILPFIEGFEVFRGIELVEENPSKLHSLIGKFRNSMDVLIVHGGSEAVNRAALENPRVDILNHPAFDRSSGLNQVLAKAAAENGVAIGIILRPLLHSRGSRRIRLLSDLKSNLELARKYDVSLVLCSDAMSCFDLRSPMEMLALAEVCGLEEDEALEAISTVPEKIIAKNRPGPGYIKKGIEVLEGEDLF | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 26214
Sequence Length: 239
Subcellular Location: Cytoplasm
EC: 3.1.26.5
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B5Y9B9 | MRRSLRLQGKKNFSRVYKEGSVVRSDYVVVYFLPASEQRVAVVVSKRFGNAVRRNRIRRLLLEAWQENHDHLPSGYYIILPRSSLLSVEENVWRSKVKELFHEWQWASGKNSPHCSAVL | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13998
Sequence Length: 119
EC: 3.1.26.5
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C3PL13 | MLPAQHKLTSPRQFRRTIKGGRRAGTRTVVVHLRFNDGEDAIAATGPRFGLIVSKAVGNAVVRHRTSRRLRHVCMSLMRDGVKGTMLPANVDIVIRALPASGEATSERLERDIRKALSTWDI | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13523
Sequence Length: 122
EC: 3.1.26.5
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Q6NE96 | MLPSQHKLSNSEQFRATIRKGKRAGRSTVVLHFYAEATAGNLATAGGPRFGLVVSKAVGNAVTRHRVSRQLRHVVIAMKDQFPASSHVVVRALPPAATASSEELRADVQAALDKLNRKR | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 12893
Sequence Length: 119
EC: 3.1.26.5
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Q8NL51 | MLPAQHKLNSSMQFRTVMRKGRRAGSKTVVVHLWDSAESLDGTEKQGEVASFGGPRFGLVVSKAVGNAVVRHRTSRRLRHICASIAEKSPELLSPTHHVVIRALAGAGNATSAELERDIRYGLGKASRVRTNK | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14481
Sequence Length: 133
EC: 3.1.26.5
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Q4JSC2 | MLAPQYRLRSTALFGQTIRNGRKKGSRTVVVHVLAGGSRAEELPLPLQEGATAGPRMGLVVSKAVGNAVTRHNTSRKLRHAFRAVMEEDSLDFPVGTTVVIRALPKSATASFEELVGDVRSCIRRALPR | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13988
Sequence Length: 129
EC: 3.1.26.5
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B1VJ37 | MLAPEHRLRSSALFSTVVKKGARKGSRTLVVHLWTPEPGPDAPLELTGGPRAGLIVSKAVGNAVVRHAVSRKLRAVLATIIDEDATAASPQLQETSFVVVRALPGSAEASSKELESDVRRCLSRLSR | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13530
Sequence Length: 127
EC: 3.1.26.5
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A9KBT3 | MEKGFSVGWRIRTTAEFRRIYAARQRIIGRYYLLYYRENEIKHSRLGVVASKRNVRKAVWRNRVRRVVKETFRIRKKDLPAFDIVVVAKASSVEADNKELYECINKLFTQLERQSKRSSSV | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14456
Sequence Length: 121
EC: 3.1.26.5
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Q3Z7P1 | MKHSNRLTRREEYSRVLASGGTYIGQLAVMKAVPNSLELSRVGFIVSKKVGGAVERNRAKRILRESLRTTGLKQGWDIVFIARAKAATVKCAEMERVVKHLLGKAQILSKANEKTSSKAD | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13267
Sequence Length: 120
EC: 3.1.26.5
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Q9RSH3 | MRGEREFRKVRAHGAAVRDPLFTLRLTDYRPRYGERWHPRAIIGLVVSKKTLKHAVKRNRARRRVREALRTMPPELLPGGLPACRAILMLNPGVLTVPFPELQAALAQALQRGAGATKRGGAKGKGGKKGGGQVAGERAGNESGSGRVSAEVNPTSASPASPAEKS | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 17773
Sequence Length: 166
EC: 3.1.26.5
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C0QIZ3 | MGSYSFPKTERLLKRADFLKLSRSGRTKQTRYFIAAMLGSETDTTRLGITVSKRVGNAVERNRIKRIVRDYYRLNRDTISGNRDINIIARKYVASLNNREVRDELGKLFKKIVRSDG | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13573
Sequence Length: 117
EC: 3.1.26.5
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B8H8Z3 | MLATRNRLRTSADFSTTVRSGVRNGRRNVVLYTAAIAAGEPSRIGFIVSKSVGNAVVRNLVKRRLREAGAASLREHGTGLAIVVRALPASASASWDQLREDYDAALESTLNRLAGRPQRAAAKGSAGTTQKGTPRA | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14413
Sequence Length: 136
EC: 3.1.26.5
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P0A167 | MSQDFSREKRLLTPRHFKAVFDSPTGKVPGKNLLILARENGLDHPRLGLVIGKKSVKLAVQRNRLKRLMRDSFRLNQQLLAGLDIVIVARKGLGEIENPELHQHFGKLWKRLARSRPTPAVTANSAGVDSQDA | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14922
Sequence Length: 133
EC: 3.1.26.5
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Q3IK52 | MEDFNFGRELRLLTPSHYSRIFNEPARAATPFFTLLAKPNDQDQPRLGLTVAKKRVKKACQRNRIKRLARECFRLNKHNIDNIDIVLMVKSGIDEQSNEELTKQLTKLWRKINERCKPGAPKPPPFKKRPNKSVKSNKQT | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 16339
Sequence Length: 140
EC: 3.1.26.5
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A5WI39 | MTDYCYPKAKRLLKPAEFKPVFNQPLFKVHQTHFMAFAYDSDHLQARLGMAITKKKIPTAVARNTIKRIIREQFRHTHAQLPALDVVFILKKSTKALSNEQMRQEISDILSKVISKQRRATAADVKHKDK | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 15073
Sequence Length: 130
EC: 3.1.26.5
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B2U822 | MGLHAYPKAARLTKTDEFSSVFALRPVRRSRHFVLYVRANGDRPARLGVVIGKKFAKRAVERNLIKRQCRELFRLRQPLLGGRDVLIRLQAKFPRQDVPTVAAFKRICREELAQLFEVATRPLSAPPAATPPQPTAGSTP | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 15769
Sequence Length: 140
EC: 3.1.26.5
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Q1MM57 | MTISEKKHTVGRLKSRPQFLAVREGEKRRGGFFLLEVLDRKEPDSQARVGFTVTKKHGNAVERNRMRRRLKEAVRLHAGFAMQPGHDYVVVARRDVLDASFQELAAELKSRVETRPKHRRSGDGRPRNV | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14870
Sequence Length: 129
EC: 3.1.26.5
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Q7UNR1 | MSRTGGKRPLEFPKSSRVVRSSEFTKALRRGGVAANDCLVVFALPHDVPDADGEPSPDESKTVKCRLGVTIPKKTGNAVVRNRWKRLIREAFRLNQTQLPSGFDYVVRPKKDVTADWKMIEKGFVKLVGRAVRRSQSSADRSSTRS | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 16299
Sequence Length: 146
EC: 3.1.26.5
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C0ZVP7 | MLPEPSRLRRHADFSVAVRRGRRMGRRDLVVHAFDREQVEALVVTNHGPRFGLIVSKAVGPAVIRHRVARRLRHICADFVGQVSPETDVVIRALPGAATASSAELAKQLRGGLTKMNLLVSVSEEP | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13862
Sequence Length: 126
EC: 3.1.26.5
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Q1GXA4 | MRPSNRAPDQLREVEIIRHYTKHAEGSVLVKFGDTHVLCTASVEDKVPPFLRGRNQGWTTAEYGMLPRSTGSRMDREAARGKQSGRTQEIQRLIGRSLRAVIDLGKLGERTIHLDCDVIQADGGTRTASITGAYVALHDAVGFMLANDMIQESPLRDAVAAISVGVYQGTPVLDLDYIEDSACDTDMNVVMTGSGGFVEIQGTAEGEPFQRAAMNRMLELAESGIRTLLLKQKEALGL | Function: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Catalytic Activity: phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n)
Sequence Mass (Da): 25945
Sequence Length: 238
EC: 2.7.7.56
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Q73X87 | MTRREDGRLDDELRPLVITRGFTEHPAGSVLIEFGHTKVMCTASVTEGVPRWRKGSGLGWLTAEYAMLPSATHTRSDRESVKGRLSGRTQEISRLIGRSLRACIDLAALGENTIAVDCDVLQADGGTRTAAITGAFVALADAVTYLSAAGKLSDPRPLSCAIAAVSVGVVDGRIRVDLPYEEDARAEVDMNVVATDTGTLVEVQGTGEGATFPRSTLDKLLDAALAACDKLFAAQREALKLPYPGVLPEGPPPPKAFGS | Function: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Catalytic Activity: phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n)
Sequence Mass (Da): 27375
Sequence Length: 259
EC: 2.7.7.56
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Q83HF6 | MLFCCIICSVLRKNSRAHDEIRPVKIIRGWNIYAEGSALIAFGNTRVLCNATFQRGVPPFLRGQRSGWITAEYAMLPRSGTERSDRESVKGKISGRSHEISRLIGRSMRAILDRYALEENTIILDCDVLQADGGTRTAAITGSYIALYDALVWAKNQKILSKHPLTDSVSAVSVGLVGDQIFLDLDYSEDSNAQADINLVFTGSGKLVEIQGTAEKSPFSYGQFEQMMELAKTGCQALKEIQAASLD | Function: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Catalytic Activity: phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n)
Sequence Mass (Da): 27144
Sequence Length: 247
EC: 2.7.7.56
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Q7SID5 | DFEYLQLVLTWPASFCYANHCERIAPNNFTIHGLWPDNVKTRLHNCKPKPTYSYFTGKMLNDLDKHWMQLKFEQDYGRTEQPSWKYQYIKHGSCCQKRYNQNTYFGLALRLKDKFDLLRTLQTHRIIPGSSYTFQDIFDAIKTVSQENPDIKCAEVTKGTPELYEIGICFTPNADSMFRCPQSDTCDKTAKVLFRR | Function: Self-incompatibility (SI) is the inherited ability of a flowering plant to prevent self-fertilization by discriminating between self and non-self pollen during pollination. In many species of the Solanaceae, self-incompatibility is controlled by the single, multiallelic locus S (By similarity).
Catalytic Activity: a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)
Sequence Mass (Da): 23093
Sequence Length: 196
Subcellular Location: Secreted
EC: 4.6.1.19
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P00684 | MGLEKSLFLFSLLVLVLGWVQPSLGGESRESSADKFKRQHMDTEGPSKSSPTYCNQMMKRQGMTKGSCKPVNTFVHEPLEDVQAICSQGQVTCKNGRNNCHKSSSTLRITDCRLKGSSKYPNCDYTTTDSQKHIIIACDGNPYVPVHFDASV | Function: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity).
Catalytic Activity: an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].
Sequence Mass (Da): 16823
Sequence Length: 152
Subcellular Location: Secreted
EC: 4.6.1.18
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Q9KT97 | MTDKNDALTLKKRFRGYFPVVIDVETAGFNAQTDALLEICAVTLSMDENGDLHPASTIHFHVEPFEGANLEKAALEFTGIYDPFSPLRGAVSEDHALKEIYKLVRKEQKAADCSRAIIVAHNAHFDHSFVMAASERCKLKRVPFHPFATFDTATLSGLAFGQTVLAKACKTAGMEFDNREAHSALYDTQKTAELFCTIVNQWKALGGWPLVNDDEDNNNDADLD | Cofactor: Binds two Mg(2+) per subunit. The active form of the enzyme binds two Mg(2+) ions in its active site. The first Mg(2+) forms only one salt bridge with the protein.
Function: Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis.
Sequence Mass (Da): 24812
Sequence Length: 224
EC: 3.1.13.-
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Q3BV71 | MRMNEPVDAQPAPSFLPMSRRFRGYLPVVVDVETGGFDWNKHALLEIACVPIEMDTDGRFFPGETASAHLVPAPGLEIDPKSLEITGIVLDHPFRFAKQEKDALDHVFAPVRAAVKKYGCQRAILVGHNAHFDLNFLNAAVARVGHKRNPFHPFSVFDTVTLAGVAYGQTVLARAAQAAGLDWNAADAHSAVYDTEQTARLFCKIANAWPGPV | Cofactor: Binds two Mg(2+) per subunit. The active form of the enzyme binds two Mg(2+) ions in its active site. The first Mg(2+) forms only one salt bridge with the protein.
Function: Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis.
Sequence Mass (Da): 23287
Sequence Length: 213
EC: 3.1.13.-
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A7NHM5 | MFEPVATARQRAVACCTFTTEQEDVVQWLVWALPALVIGLAIGAGIGILIYKNSVQSQIRQIEAEARLQLEATRSEQKDLILRATDEALRLRTEAEAQIREARAALAKQEERLQRKEENLDRKIEGLERRERQLQQRERQMEQLHQEAEHLRQQQRAELERISALSQEEARAIILKRVEDETRDEAARRIREIEKTMHEEADKLARKVISMAIQRCASDYVAEVTVSTVALPSEELKGRIIGREGRNIRAFEQLTGVDIIVDDTPEAVTLSCHDPVRREVARLALIKLLKDGRIHPTRIEEVVHKTQQEVDQVMREEGERVAYEANVQGLHPDLIKLLGRLKYRTSYGQNVLQHSLECALLAAHIAAEIGANINVAKTAALLHDIGKAVDHEVQGPHALIGAEIARRLGKSPAIVHAIAAHHNDEEPQTVEAWLVQAVDAISGGRPGARRETLDLYIKRLEALETVATSFSGVQRAFAVQAGREVRVMVQPDAIDDLGSIHLARDVAKKIEESLQYPGQIKVTVIRETRAVDYAR | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60151
Sequence Length: 535
Subcellular Location: Cell membrane
EC: 3.1.-.-
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Q1AW41 | MSVLWMVLGLAIGIAVGAAAGYIVCRSRTDRRLAETRADARSIIEDANRQAETLRREAELAAKEAAMRIKDEAEAEVRARRAEISRIEERLDNRDTALDRREVELDERRRRLSETEDELRRREESLAEREQEQLRALEEISGLSRAEAEERLFSRVEAELERRIGRMVRNRISEAEENADLEARRILATTMERLASDLTSESTVKAVELPSDDMKGRVIGREGRNIRAFEAATGVDVIIDDTPETVVLSCFDPVRREVARIAMERLVKDGRIHPGRIEQVVAKVRKEVEKEMKAAGRQALYDAKVSGSMHGDLLRLLGALKYRSSYGQNVLAHSVEVANIAGMMAQELGANVKIARRAALLHDVGKAIDHEAEGTHALIGGRFAKKCGESDEVVRAISAHHHEVEMQTVEDVIVATADAVSAARPGARRETTEVYLERLRNLEDIALSHRGVDKAYAIQAGREIRVMVQPSEVDDRIAAKLAYDISRKIEDELEYPGQIKVTVIRESRVSEVAR | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57598
Sequence Length: 514
Subcellular Location: Cell membrane
EC: 3.1.-.-
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A8M7V7 | MSGFDAVLLVAVLLLALIVLGAVLVGVRAVRGIAGAPRPEDPAFIAEKDRQEQSLAALRSAADEANSTVDAAKSAAAAARTEAAAARAEAKAARAEARRVLDGARAEADTILERVHKQAEADAEQLRTAARRSGEREAAVLATTTREQAAEVERRAARMDDRERLHSEEVERLAERDRQLSAASAALAARESTLVDRDRELAQAEDRRRRELERVAGITAEAARGELVEAIEAQAKREAALLVREIESEARNTGEERARHIVVDAIQRVASEQTAESVVSVLHLPGDEMKGRIIGREGRNIRAFESVTGVNLIIDDTPEAVLLSCFDPVRREVGRLTLEKLVLDGRIHPHRIEEVHDLARQEVVQLCQRAAEDALVEVGITEIHPELVSLLGRLRYRTSYGQNVLKHLVETAHIAGIMAAELRLDVPTIKRCAFLHDIGKALTHEVEGSHAIVGADVARKYGESEDVVHAIEAHHNEVPPQTIEAVLTQASDACSGGRPGARRESLEAYVRRLERIEEIAAGKLGVERVFAMQAGREVRVMVRPEDVDDISASVLARDVAKQIEEELTYPGQIRVTVVRESRVTEIAR | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 64289
Sequence Length: 588
Subcellular Location: Cell membrane
EC: 3.1.-.-
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A1U2M9 | MEFTFLGTSAGTPTRSRNVTGLALCLSGPKPWYLVDCGEGTQHQLMRTRYSVMQLRAMFITHIHGDHIFGLPGLLTSASMLGRTEPLDIIAPPQVRRFIDAVIENSDSSLSYPLNFINSEAPDFYWQDDHLGVTNVALSHRVPCRAYVFTERNLERQLQKEKLVADGIEPGPQWGDLQKGKDVLLDDGRLLRSNDYTHIPRTARKIIVGGDNDTPELLKDACQGTHVLIHEATYTQDVADRVGPWPQHSSAQQVARFAQATKLPNLVLTHFSSRYQSAPGGSPHINQLAAEALQHYKGQLFLARDFDTYRLEKDFQLHKVDHN | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 36279
Sequence Length: 323
EC: 3.1.26.11
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Q58897 | MIIMKLIFLGTGAAVPSKNRNHIGIAFKFGGEVFLFDCGENIQRQMLFTEVSPMKINHIFITHLHGDHILGIPGLLQSMGFFGREKELKIFGPEGTKEIIENSLKLGTHYIEFPIKVYEIYTKEPITIYKEENYEIIAYPTEHGIPSYAYIFKEIKKPRLDIEKAKKLGVKIGPDLKKLKNGEAVKNIYGEIIKPEYVLLPPKKGFCLAYSGDTLPLEDFGKYLKELGCDVLIHEATFDDSAKDAAKENMHSTIGDAVNIAKLANVKALILTHISARYDKEEYFNLYKMNVKQYNESFKIIISEDLKSYDIKKDLLG | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 36034
Sequence Length: 317
EC: 3.1.26.11
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Q8TWK0 | MDRELVMRFLGTGGAVPSKDRSHPGLLVEFSGTKLLIDCGEGTQRRAMEQGVTIHDVDAVLLTHHHVDHVAGLLPLATTVDLLHGRRLKVYGPTAGSESALDISDLEVIEYREVNPGDEVEIGDLRVLVYESEHGVPTVDYRIETPKIPGKADPKYIRRVPPSKRREVLLRGERPYSLTKPGKISVYVKGDGRPADPENVRGCQVLVHEACFEDHEEAVRYLHSTHLEAAEVAREAGVDLLVLTHLSTKVDPERMREEAREVFPVVVVARDGLMVRVRR | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 31073
Sequence Length: 279
EC: 3.1.26.11
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O27859 | MMEVTFLGTSSAVPSKNRNHTSIALRIPGEIFLFDCGEGTQRQMALAGISPMKVTRIFITHLHGDHILGIPGMIQSMGFRGREEPLDIYGPPGIHELHECIMKMGYFTLDFDINVHEVRGGTVVEEDDYRVTSAPASHSVFNLAYCFEEKKRPRFLREKAIALGLKPGPAFGKLHRGIPVRVGDRIIMPEEVLGSPRKGVKVCYSGDTRPCESVIKLAEGAELLIHESTLEAGSEDKAAESGHSTAREAAEVARSAGVKRLILTHLSTRYKRTEVILEAARQVFPVTDVADDLMTVEVKAYDSSPDS | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 33757
Sequence Length: 307
EC: 3.1.26.11
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Q49744 | MQAGRQLFLVDCWLGVLQRASAGPTHTPAVCQRCCSTHLHGDRISDLGDLLITHWVTTFALDPPPLPIIGSPDTAETVEAKLKASGHDIEYQITHHTYLNTPPLIEVYEYTKGFVGAPPDGVSIRGSTNHGPVTPTIGFRIESGPTSVVLTGGTVPCASLDELAAEADALVHTIIRKNIVIRVHQQADQGHLQPPLVNRASDSNRGARGHRHPGHNVLCP | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA (By similarity).
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 23634
Sequence Length: 220
EC: 3.1.26.11
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Q13151 | MENSQLCKLFIGGLNVQTSESGLRGHFEAFGTLTDCVVVVNPQTKRSRCFGFVTYSNVEEADAAMAASPHAVDGNTVELKRAVSREDSARPGAHAKVKKLFVGGLKGDVAEGDLIEHFSQFGTVEKAEIIADKQSGKKRGFGFVYFQNHDAADKAAVVKFHPIQGHRVEVKKAVPKEDIYSGGGGGGSRSSRGGRGGRGRGGGRDQNGLSKGGGGGYNSYGGYGGGGGGGYNAYGGGGGGSSYGGSDYGNGFGGFGSYSQHQSSYGPMKSGGGGGGGGSSWGGRSNSGPYRGGYGGGGGYGGSSF | Function: mRNA-binding component of ribonucleosomes. Specifically binds AU-rich element (ARE)-containing mRNAs. Involved in post-transcriptional regulation of cytokines mRNAs.
PTM: Phosphorylated at Ser-84 by MAPKAPK2 in response to LPS treatment, promoting stabilization of GADD45A mRNA.
Sequence Mass (Da): 30841
Sequence Length: 305
Subcellular Location: Nucleus
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Q9CX86 | MENSQLCKLFIGGLNVQTSESGLRGHFEAFGTLTDCVVVVNPQTKRSRCFGFVTYSNVEEADAAMAASPHAVDGNTVELKRAVSREDSARPGAHAKVKKLFVGGLKGDVAEGDLIEHFSQFGAVEKAEIIADKQSGKKRGFGFVYFQSHDAADKAAVVKFHPIQGHRVEVKKAVPKEDIHAGGGGARAARGGRGGGRGRGGGGGGGGRDQNGLAKGGGGGGGGYNSYGGYGGYGAYGGGGGGGGSYGGSDYGNGFGGFGSYSQHQSSYGPMKSGGGGGGGGSWGGRSNSGPYRGGYGGGYGGGSF | Function: mRNA-binding component of ribonucleosomes. Specifically binds AU-rich element (ARE)-containing mRNAs. Involved in post-transcriptional regulation of cytokines mRNAs.
PTM: Phosphorylated at Ser-84 by MAPKAPK2 in response to LPS treatment, promoting stabilization of GADD45A mRNA.
Sequence Mass (Da): 30530
Sequence Length: 305
Subcellular Location: Nucleus
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P09651 | MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGYGGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF | Function: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection . Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform . Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1 . May bind to specific miRNA hairpins .
PTM: Arg-194, Arg-206 and Arg-225 are dimethylated, probably to asymmetric dimethylarginine.
Sequence Mass (Da): 38747
Sequence Length: 372
Subcellular Location: Nucleus
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P49312 | MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF | Function: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform. Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1. May bind to specific miRNA hairpins.
PTM: Sumoylated.
Sequence Mass (Da): 34196
Sequence Length: 320
Subcellular Location: Nucleus
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Q2HJ60 | MEREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY | Function: Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (By similarity). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (By similarity). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity).
PTM: Sumoylated in exosomes, promoting miRNAs-binding.
Sequence Mass (Da): 36006
Sequence Length: 341
Domain: The disordered region, when incubated at high concentration, is able to polymerize into labile, amyloid-like fibers and form cross-beta polymerization structures, probably driving the formation of hydrogels. In contrast to irreversible, pathogenic amyloids, the fibers polymerized from LC regions disassemble upon dilution. A number of evidence suggests that formation of cross-beta structures by LC regions mediate the formation of RNA granules, liquid-like droplets, and hydrogels.
Subcellular Location: Nucleus
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P22626 | MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY | Function: Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs . Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm . Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts . Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs . Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs . Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform . Also plays a role in the activation of the innate immune response . Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6 . In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production .
PTM: Sumoylated in exosomes, promoting miRNAs-binding.
Sequence Mass (Da): 37430
Sequence Length: 353
Domain: The disordered region, when incubated at high concentration, is able to polymerize into labile, amyloid-like fibers and form cross-beta polymerization structures, probably driving the formation of hydrogels. In contrast to irreversible, pathogenic amyloids, the fibers polymerized from LC regions disassemble upon dilution. A number of evidence suggests that formation of cross-beta structures by LC regions mediate the formation of RNA granules, liquid-like droplets, and hydrogels.
Subcellular Location: Nucleus
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Q9Y7Y6 | MSLITFKAGKLRRVPGTKLLRADPEKGYIVMNRDAYGLIHFQWAKRNDLENPEDDIIVFSSECTFEKVTECTTGRAYMLKYPSSAHSLFYWMQEASDDNDTSYAERINSYIKDQDLLDPARSDVATVSDMMEVDTVEQSEPIAQPTESSKESSEIGAPNSDEINSSEAVRNLLATISAQAGFGGSTVDLCEILKPSNLTDLLCQEGVIDRLMPYMPPDTPNNLEGVLAIVSSPQYAQALRSFSQALNSPGGVNIISALGLSLDESANPNEGGALQFLKAIARFVSRNNGSE | Function: Ccomponent of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required . Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Within the complex, functions as a proteasomal ubiquitin receptor (Probable).
Sequence Mass (Da): 31821
Sequence Length: 291
Domain: The Pru (pleckstrin-like receptor for ubiquitin) domain mediates interactions with rpn2 and ubiquitin.
Subcellular Location: Cytoplasm
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Q9USM1 | MESVFGRVRNETSERGKYGLVSVKAGKLQRKPGTNILQADHRKGVIYMQMASDELLHFYWKERARVSREVEDDYIIFPEEAEFIKIDECTTGRVYALKFKSSSQIHFYWMQEYSDEKDKETASLINQLIADPVNTTRTINSHNNSSSRGTDDSSTSQLLQLFGAASQDALQDFNWEVLSPTAEAPAILPRFPNVNESANMYRASSESNLNGPHATAGENGEDHEEATASPLDENIDYTHSRTLELLEQLQPLILNETTFVEPFSIDRESHRVITHPRVYPKIFPHSPSDLLRISGRAELSENRDFFKHLSSLMEAVAKPESESLREICNLSLEQVQSASGAELFLHALYDRLVNEGVIVISHITQEGSDGEVEEEGDVEMRESNEKDE | Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required . Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Within the complex, functions as a proteasomal ubiquitin receptor (Probable).
Sequence Mass (Da): 43903
Sequence Length: 388
Domain: The Pru (pleckstrin-like receptor for ubiquitin) domain mediates interactions with rpn2 and ubiquitin.
Subcellular Location: Cytoplasm
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P21967 | MSLFNTNAYLPVVIQPHELNLDLMDNIKKAVINKYLHKETSGFMAKKIQIVEDTPMPLAELVNNEIVVHVTCNIDYKYYKVGDIVSGILTITDESDISVVCSDLICKIRSDSGTVSYDNSKYCFIKNGKVYANESTVTVMLKEAQSGMESSFVFLGNIIEK | Function: Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF) thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase (By similarity).
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 18014
Sequence Length: 161
Subcellular Location: Virion
EC: 2.7.7.6
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Q76ZS0 | MSSFVTNGYLPVTLEPHELTLDIKTNIRNAVYKTYLHREISGKMAKKIEIREDVELPLGEIVNNSVVINVPCVITYAYYHVGDIVRGTLNIEDESNVTIQCGDLICKLSRDSGTVSFSDSKYCFFRNGNAYDNGSEVTAVLMEAQQGIESSFVFLANIVDS | Function: Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates . Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 17911
Sequence Length: 161
Subcellular Location: Virion
EC: 2.7.7.6
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Q05569 | MDNSMDINDILLSDDNDYKSYDEDDDSISDIGETSDDCCTTKQSDSRIESFKFDETTQSPHPKQLSERIKAIKQRYTRRISLFEITGILSESYNLLQRGRIPLLNDLTEETFKDSIINIMFKEIEQGNCPIVIQKNGELLSLTDFDKKGVQYHLDYIKTIWRNQRKL | Function: Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF) thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase (By similarity).
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 19500
Sequence Length: 167
Subcellular Location: Virion
EC: 2.7.7.6
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Q9GZS1 | MAAEVLPSARWQYCGAPDGSQRAVLVQFSNGKLQSPGNMRFTLYENKDSTNPRKRNQRILAAETDRLSYVGNNFGTGALKCNTLCRHFVGILNKTSGQMEVYDAELFNMQPLFSDVSVESELALESQTKTYREKMDSCIEAFGTTKQKRALNTRRMNRVGNESLNRAVAKAAETIIDTKGVTALVSDAIHNDLQDDSLYLPPCYDDAAKPEDVYKFEDLLSPAEYEALQSPSEAFRNVTSEEILKMIEENSHCTFVIEALKSLPSDVESRDRQARCIWFLDTLIKFRAHRVVKRKSALGPGVPHIINTKLLKHFTCLTYNNGRLRNLISDSMKAKITAYVIILALHIHDFQIDLTVLQRDLKLSEKRMMEIAKAMRLKISKRRVSVAAGSEEDHKLGTLSLPLPPAQTSDRLAKRRKIT | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors . Appears to be involved in the formation of the initiation complex at the promoter by mediating the interaction between Pol I and UBTF/UBF .
PTM: Acetylated at Lys-373 by CREBBP/CBP, leading to decreased RNA polymerase I transcription . In normal conditions, deacetylated by SIRT7, promoting the association of RNA polymerase I with the rDNA promoter region and coding region . In response to stress, SIRT7 is released from nucleoli leading to hyperacetylation of POLR1E/PAF53 and decreased association of RNA polymerase I with the rDNA promoter region .
Sequence Mass (Da): 47260
Sequence Length: 419
Subcellular Location: Nucleus
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Q8K202 | MATLESPGMDDQAGDTETEALQSARWLYCGEPDDRQKAVLVQFSNGKLQNPGDMRFTLYNSTDLVNPRQRSHRIVAAETDRLSYVGNNFGTGALKCNALCRHFVGILNKTSGQMEVYDAELFNMQPLFAGMGTEVIKLGGQHLYLLAFCQPSKNLAEAGDLLLSRHRQGHCIAVLLDDDAIEREPPLENQNKTFRDKLDSCIEAFGSTKQKRSLNSRRMNKVGSESLNLSVAKAAESIIDTKGVNALVSDAMQDDLQDGVLYLPPCYADAAKPEDVYRFEDILSPAEYDALESPSEAFRKVTSEDILKMIEENSHCSYVIEMLKSLPIDEVHRNRQARSIWFLDALIRFRAQKVIKGKRALGPGIPHIINTKLLKQFTCLTYNNGRLQNLISSSMRAKITSYAIILALHINNFQVDLTALQKDLKLSEKRMIEIAKAMRLKISKQKVSLADGREESHRLGTLSVPLPPAQNSDRQSKRRKMN | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors . Appears to be involved in the formation of the initiation complex at the promoter by mediating the interaction between Pol I and UBTF/UBF .
PTM: Acetylated at Lys-436 by CREBBP/CBP, leading to decreased RNA polymerase I transcription. In normal conditions, deacetylated by SIRT7, promoting the association of RNA polymerase I with the rDNA promoter region and coding region. In response to stress, SIRT7 is released from nucleoli leading to hyperacetylation of POLR1E/PAF53 and decreased association of RNA polymerase I with the rDNA promoter region.
Sequence Mass (Da): 54034
Sequence Length: 482
Subcellular Location: Nucleus
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Q31S42 | MKPRILVIDDDSAILELVAVNLEMSGYDVRKAEDGIKGQALAVQLVPDLIMLDLMLPRVDGFTVCQRLRRDERTAEIPVLMLTALGQTQDKVEGFNAGADDYLTKPFEVEEMLARVRALLRRTDRIPHAARHSEILSYGPLTLIPERFEAIWFNRTVKLTHLEFELLHCLLQRHGQTVAPSEILKEVWGYDPDDDIETIRVHIRHLRTKLEPDPRHPRYIKTVYGAGYCLELPAETELHQHADQFPSAS | Function: Response regulator of 2 two-component regulatory systems SasA/RpaA and CikA/RpaA involved in genome-wide circadian gene expression. The histidine kinases have opposing effects modulated by the clock oscillator proteins; SasA phosphorylates RpaA (stimulated by fully phosphorylated KaiC) while CikA dephosphorylates phospho-RpaA (stimulated by the phospho-Ser-431-KaiC-KaiB complex) . A very robust clock is reconstituted with KaiA, KaiB, KaiC, SasA, CikA and RpaA; output is measured by transcription from an appropriate reporter . Phosphorylation by SasA is maximal when KaiC phosphorylation is active during the circadian cycle . Functions downstream of LabA .
PTM: Phosphorylated by SasA; phosphorylation is maximal when KaiC phosphorylation is active during the circadian cycle . Dephosphorylated by CikA. CikA and SasA cooperation generates RpaA activity oscillation that is distinct from that generated by CikA or SasA alone and offset from the rhythm of KaiC phosphorylation .
Sequence Mass (Da): 28492
Sequence Length: 249
Subcellular Location: Cytoplasm
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P28364 | MSRGTIYTESTMDFQKVRKIQFGLLDPKEIQAMSVVQVENEKIYDNGIPTDGGINDLRMGTMEKAMRCSTCQGDSKECPGHFGHIELAQPVFHIGFIDLVKKILKCVCFNCNKLLITDKHDKYSALKRVKDPKLKLNKVYKVCKDIKVCGKADRKSETYTEGSGQKQPRLRKTGLKIKAEFPIDEDDPSTNDNKRDLSASECLKILGRISPDDCKFLGFDMVLARPEWLIISRLPVAPPPVRPSVCMGSNIRQEDDLTHQYQQILKANNQLRKHLSTANHIINENYQLLQFYCATLIDNEQAGQMVSRHKSGGKAIKAIRARLKGKEGRLRGNLMGKRVDFSARTVITCDPTLDLDQLGVPRSIAENITIPEVVTPQNIDEMRKLVINGPNKWPGAKYIKGEGGKMIDLSYAKTTETFIDYGYVIERHLKNDDFVLFNRQPSLHKMSIMGHRVKVLPYSTFRLNLSVTAPYNADFDGS | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing (By similarity).
PTM: Phosphorylation activates POL II.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 54026
Sequence Length: 478
Subcellular Location: Nucleus
EC: 2.7.7.6
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P47736 | MIEKMQGSRMDEQRCSFPPPLKTEEDYIPYPSVHEVLGREGPFPLILLPQFGGYWIEGTNHEITSIPETEPLQSPTTKVKLECNPTARIYRKHFLGKEHFNYYSLDAALGHLVFSLKYDVIGDQEHLRLLLRTKCRTYHDVIPISCLTEFPNVVQMAKLVCEDVNVDRFYPVLYPKASRLIVTFDEHVISNNFKFGVIYQKLGQTSEEELFSTNEESPAFVEFLEFLGQKVKLQDFKGFRGGLDVTHGQTGTESVYCNFRNKEIMFHVSTKLPYTEGDAQQLQRKRHIGNDIVAVVFQDENTPFVPDMIASNFLHAYVVVQAEGGGPDGPLYKVSVTARDDVPFFGPPLPDPAVFRKGPEFQEFLLTKLINAEYACYKAEKFAKLEERTRAALLETLYEELHIHSQSMMGLGGDEDKMENGSGGGGFFESFKRVIRSRSQSMDAMGLSNKKPNTVSTSHSGSFAPNNPDLAKAAGISLIVPGKSPTRKKSGPFGSRRSSAIGIENIQEVQEKRESPPAGQKTPDSGHVSQEPKSENSSTQSSPEMPTTKNRAETAAQRAEALKDFSRSSSSASSFASVVEETEGVDGEDTGLESVSSSGTPHKRDSFIYSTWLEDSVSTTSGGSSPGPSRSPHPDAGKLGDPACPEIKIQLEASEQHMPQLGC | Function: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 73361
Sequence Length: 663
Subcellular Location: Golgi apparatus membrane
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A2ALS5 | MIEKMQGSRMDEQRCSFPPPLKTEEDYIPYPSVHEVLGREGPFPLILLPQFGGYWIEGTNHEISSLPETEPLQSPTTKVKLECNPTARIYRKHFLGKEHFNYYSLDTALGHLVFSLKYDVIGDQEHLRLLLRTKCRTHHDVIPISCLTEFPNVVQMAKLVCEDVNVDRFYPVLYPKASRLIVTFDEHVISNNFKFGVIYQKLGQTSEEELFSTNEESPAFVEFLEFLGQKVKLQDFKGFRGGLDVTHGQTGTESVYCNFRNKEIMFHVSTKLPYTEGDAQQLQRKRHIGNDIVAVVFQDENTPFVPDMIASNFLHAYVVVQAEGGGPDGPLYKVSVTARDDVPFFGPPLPDPAVFRKGPEFQEFLLTKLINAEYACYKAEKFAKLEERTRAALLETLYEELHIHSQSMMGLGGDDDKMENGSGGGGFFESFKRVIRSRSQSMDAMGLSNKKPNTVSTSHSGSFTPNNPDLAKAAGISLIVPGKSPTRKKSGPFGSRRSSAIGIENIQEVQEKRESPPAGQKTPDSGHVSQEPKSENSSTQSSPEMPTTKNRVESAAQRTEVLQGFSRSSSSASSFTSVVEETEGVDGDDTGLESVSSSGTPHKRDSFLYSTWLDDSVSTTSGGSSPGLTRSPHPDVGKSGDPACPEIKIQLETSEQHTPQMGC | Function: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 73433
Sequence Length: 663
Subcellular Location: Golgi apparatus membrane
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Q684P5 | MFGRKRSVSFGGFGWIDKTMLASLKVKKQELANSSDATLPDRPLSPPLTAPPTMKSSEFFEMLEKMQGIKLEEQKPGPQKNKDDYIPYPSIDEVVEKGGPYPQVILPQFGGYWIEDPENVGTPTSLGSSICEEEEEDNLSPNTFGYKLECKGEARAYRRHFLGKDHLNFYCTGSSLGNLILSVKCEEAEGIEYLRVILRSKLKTVHERIPLAGLSKLPSVPQIAKAFCDDAVGLRFNPVLYPKASQMIVSYDEHEVNNTFKFGVIYQKARQTLEEELFGNNEESPAFKEFLDLLGDTITLQDFKGFRGGLDVTHGQTGVESVYTTFRDREIMFHVSTKLPFTDGDAQQLQRKRHIGNDIVAIIFQEENTPFVPDMIASNFLHAYIVVQVETPGTETPSYKVSVTAREDVPTFGPPLPSPPVFQKGPEFREFLLTKLTNAENACCKSDKFAKLEDRTRAALLDNLHDELHAHTQAMLGLGPEEDKFENGGHGGFLESFKRAIRVRSHSMETMVGGQKKSHSGGIPGSLSGGISHNSMEVTKTTFSPPVVAATVKNQSRSPIKRRSGLFPRLHTGSEGQGDSRARCDSTSSTPKTPDGGHSSQEIKSETSSNPSSPEICPNKEKPFMKLKENGRAISRSSSSTSSVSSTAGEGEAMEEGDSGGSQPSTTSPFKQEVFVYSPSPSSESPSLGAAATPIIMSRSPTDAKSRNSPRSNLKFRFDKLSHASSGAGH | Function: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state.
PTM: In vitro phosphorylated by cGMP-dependent protein kinase 1 (cGKI) at Ser-7; the phosphorylation probably does not regulate GAP activity.
Sequence Mass (Da): 80056
Sequence Length: 730
Subcellular Location: Cytoplasm
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Q9N1T2 | MGEPEEVMPGSGAVFTFGKTQFAENIPSKFWFRNDVPTFLSCGDEHTAVVTGNNKLYMFGSNNWGQLGLGSKSTVSKPTCVKALKPEKVKFAACGRNHTLVSTEGGKVYAAGGNNEGQLGLGDTEERSTFHLISFFTSQRKIKQLSAGSNTSAALTEDGELFMWGDNSEGQIGLENVTNVCVPQQVTVGKPISWISCGYYHSAFVTTEGQLYTFGEPECGKLGLPNQLLVNHRMPQPVPGIPGKVVQVACGGGHTVVLTEKAVYTFGLGQFGQLGLGTFLFETSVPKAIEHIKDQKISFIACGENHTALITDMGLMYTFGDGRHGKLGLGLENSTNQFIPTLCSNFLRFIVQLVSCGGCHTLVFATPRLGGTEEMELKEINKSCFSAATSLSLSNLSSGIVLHQTLSARVRRREREKSPDSFQMTRTLPPIDGIPMPPVCFSPSPIPFYMAASNWSGKMTPEKEGLTQPEPDYFRDNMAKGKETDNSSATDSESLGETTDVLNMTHMMSLNSNDKSLKLSPIDKQKKQETIEKLKQHTAHFGNDDSKGCASEEMSKTVKEGKAYKQLLAKGIYMTQAAMTMEAFSDEDIGNDSGQPGPRADTHAEGVQRKIFSCESKHGLYPPDFKAIAKESDGGQSQKDPEAEETVSEKENELAEMAGLQARRQSEENLRNINMFFDDLPNRDVNIEDEESKDFVKDSRRNKQDVIFDSERESIEEPDSYLEGESESQQGTTDGFEQPESVEFSSGEKEDDDEVETDQNLWYSRKFIEQGHKEETEHILSKFMAKYDFKCDHLSEIPEEQEGAEDSEGSGIEEQEVEANENVEVPAGKEEKEIEILSDDLTDRAEDHEFSEDEEPEDMAEELDEDLESKKNVPADVASDNSLKKDETTKQEKRAICEYNENPKGNMHYHAKSSSSEVLNDSESTPNKDVKKSKKIFLFKRMSLMSQKSMQSNNEPLPEIKPIGDQIAFKGNKKDANQNHMGQNHQDTSPPDMERRSKSCTIL | Function: Could be a guanine-nucleotide releasing factor. Plays a role in ciliogenesis. Probably regulates cilia formation by regulating actin stress filaments and cell contractility. May be involved in microtubule organization and regulation of transport in primary cilia. Plays an important role in photoreceptor integrity. May play a critical role in spermatogenesis and in intraflagellar transport processes.
PTM: Prenylated.
Sequence Mass (Da): 111097
Sequence Length: 1003
Domain: The RCC1 repeat region mediates interactions with RPGRIP1.
Subcellular Location: Golgi apparatus
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Q92834 | MREPEELMPDSGAVFTFGKSKFAENNPGKFWFKNDVPVHLSCGDEHSAVVTGNNKLYMFGSNNWGQLGLGSKSAISKPTCVKALKPEKVKLAACGRNHTLVSTEGGNVYATGGNNEGQLGLGDTEERNTFHVISFFTSEHKIKQLSAGSNTSAALTEDGRLFMWGDNSEGQIGLKNVSNVCVPQQVTIGKPVSWISCGYYHSAFVTTDGELYVFGEPENGKLGLPNQLLGNHRTPQLVSEIPEKVIQVACGGEHTVVLTENAVYTFGLGQFGQLGLGTFLFETSEPKVIENIRDQTISYISCGENHTALITDIGLMYTFGDGRHGKLGLGLENFTNHFIPTLCSNFLRFIVKLVACGGCHMVVFAAPHRGVAKEIEFDEINDTCLSVATFLPYSSLTSGNVLQRTLSARMRRRERERSPDSFSMRRTLPPIEGTLGLSACFLPNSVFPRCSERNLQESVLSEQDLMQPEEPDYLLDEMTKEAEIDNSSTVESLGETTDILNMTHIMSLNSNEKSLKLSPVQKQKKQQTIGELTQDTALTENDDSDEYEEMSEMKEGKACKQHVSQGIFMTQPATTIEAFSDEEVGNDTGQVGPQADTDGEGLQKEVYRHENNNGVDQLDAKEIEKESDGGHSQKESEAEEIDSEKETKLAEIAGMKDLREREKSTKKMSPFFGNLPDRGMNTESEENKDFVKKRESCKQDVIFDSERESVEKPDSYMEGASESQQGIADGFQQPEAIEFSSGEKEDDEVETDQNIRYGRKLIEQGNEKETKPIISKSMAKYDFKCDRLSEIPEEKEGAEDSKGNGIEEQEVEANEENVKVHGGRKEKTEILSDDLTDKAEDHEFSKTEELKLEDVDEEINAENVESKKKTVGDDESVPTGYHSKTEGAERTNDDSSAETIEKKEKANLEERAICEYNENPKGYMLDDADSSSLEILENSETTPSKDMKKTKKIFLFKRVPSINQKIVKNNNEPLPEIKSIGDQIILKSDNKDADQNHMSQNHQNIPPTNTERRSKSCTIL | Function: Could be a guanine-nucleotide releasing factor. Plays a role in ciliogenesis. Probably regulates cilia formation by regulating actin stress filaments and cell contractility. Plays an important role in photoreceptor integrity. May play a critical role in spermatogenesis and in intraflagellar transport processes (By similarity). May be involved in microtubule organization and regulation of transport in primary cilia.
PTM: Prenylated.
Sequence Mass (Da): 113387
Sequence Length: 1020
Domain: The RCC1 repeat region mediates interactions with RPGRIP1.
Subcellular Location: Cytoplasm
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Q9R0X5 | MAESESLVPDTGAVFTFGKTKFAENIPSKFWFKNDIPICLSCGDEHTAIVTGNNKLYMFGSNNWGQLGLGSKAAIIKPTCIKALKPEKVKLAACGRNHTLVSTDTGGVYAAGGNNEGQLGLGDTDDRDTFHQIVFFTPADTIKQLSAGANTSAALTEDGKLFMWGDNSEGQIGLEDKSNVCIPHEVTVGKPISWISCGYYHSAFVTMDGELYTFGEPENGKLGLPNELLMNHRSPQRVLGIPERVIQVACGGGHTVVLTEKVVYAFGLGQFGQLGLGTFLFETSEPKIIERIKDQKICHISCGENHTALMTELGLLYTFGDGRHGKLGLGMENFTNQFFPTLCSNFLRFAVQLIACGGCHMLVFATPRLGTIDEPKFEDVYEPYISTGSFSINDLSPRSSLNRSLSARLRRRERERPPCSASMVGTLPPLEGTSASTSAYFYPSSPPFHLSVNNYPEKSPSESMEPLDSDYFEDKMNKDTETENSSAVDSENFGETNDILNMTHMMTTSSNEKLLDFSPIQKQQNQDTFEKVMESTPCTENEDSYEYEEMSKIKEVTVYKQYLAKGIYMIRPAEILEAFSDEEVGNGLDQVEEPRVFTDGKGLQSKQVGKESDEEIVSEKKTEVMEVADVKKIRESEENSKSDSLFDDLPDKTMNSESEDNKDIAEERRSSEQNMTFDSETELVEEPDSYMECERHSEQDSAEELEQPKLVEYSSEEKDEKDEKDDDEVETENLWYDRNCTEQETENVFRATRFFPKFDLKHDHLSGIPEEQEGPEDSEGNVVVEQVVQAQKENLEFEGDRKEAKAEAPSDVITEKEAPQLSETVKPEEGEMDEEISILNVEDTVEEERKEGEKEIVEEGSIPETEGSETIDITDEKLDEVLKEEDSASLLQRALREYNENPKGHMYDRVKSSSSEILGGNDPTSKDIKKAKKISFFNRMSLTGQKLMQNTNDPLPEIKPIGDQIALQSDKKDANQNHMGQNLQDSTTPNMEGKSKSCTIL | Function: Could be a guanine-nucleotide releasing factor (By similarity). Plays a role in ciliogenesis (By similarity). Probably regulates cilia formation by regulating actin stress filaments and cell contractility (By similarity). May be involved in microtubule organization and regulation of transport in primary cilia (By similarity). Plays an important role in photoreceptor integrity. Isoform 5 may play a critical role in spermatogenesis and in intraflagellar transport processes.
PTM: Prenylated.
Sequence Mass (Da): 111801
Sequence Length: 1001
Domain: The RCC1 repeat region mediates interactions with RPGRIP1.
Subcellular Location: Golgi apparatus
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Q9ZU82 | MSWSLCSTHGVSSSIALTYGFRHRRRSTFRIFATSDGLEPKDDPPESPLPSSSSALGKDLKKVVNKTAATFAPRASTASKNPALPGTTLYKVFEVQGYASMFLGGVLSFNLLFPSSEPDLWRLMGMWSIWMFTIPSLRARDCPSKEKEALNYLFLIVPLLNVAIPFFWKSFALVWSADTVAFFAMYAWKLGWLERTE | Function: Plays a positive role in the immune response to the oomycetes P.brassicae, including induced oxidative burst (e.g. H(2)O(2)) and enhanced expression of defense-related genes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22094
Sequence Length: 197
Subcellular Location: Plastid
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M1C5M7 | MNSATTMSASVLNYQILKFFPPQKNGFLKSPLIRGKICRFCVSASSNELNKQVIEDPKEETQEKSDGVIVNSTEEEEERSGENSTSTGPSTVLDNKELKKAVLKTASTFAPRASTATKNPAKPGTVLYTVFEVQAYASMLIGGALSFNLIFPSTEPDIWRLMGMWSIWMFTIPSLRARDCSKDEKEALNYLFLLVPLLNVAIPFFLKSFAVVWSADTVAFLGMYAWKLGWLQKER | Function: Plays a positive role in the immune response to the oomycetes P.infestans, including induced oxidative burst and enhanced expression of defense-related genes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26243
Sequence Length: 235
Subcellular Location: Plastid
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P39956 | MTKLIAPSEIVGGVPVFKPTYEQFEDFYAYCKAINKYGMKSGVVKVIPPKEWKDKLDLPYSAETLQKIKIKSPIQQHISGNKGLFMVQNVEKNKTYNIIQWKDLSKDYVPPEDPKARRNSRKGSVSKSTKLKLKNFESSFNIDDFEQFRTEYTIDLSDFQNTERLKFLEEYYWKTLNFTTPMYGADTPGSIFPEGLNVWNVAKLPNILDHMETKVPGVNDSYLYAGLWKASFSWHLEDQDLYSINYIHFGAPKQWYSIPQEDRFKFYKFMQEQFPEEAKNCPEFLRHKMFLASPKLLQENGIRCNEIVHHEGEFMITYPYGYHAGFNYGYNLAESVNFALEEWLPIGKKAGKCHCISDSVEIDVKKLAKSWRDNNKESKGTPPLNQLPNPAMPLLHRPTLKEMESSSLRSTSPDVGHFSNFKSKSSGVSSPLLSRMKDYSNIVEPTLEDPTLKLKRISSFQEQPLNKLLKRETSQTAMLTDHEDNIVAMSLTSMANSAASSPRLPLSRLNSSNELSNAQPLLDMTNNTLAFPRPNGPSGLNPLLYISNKNISGISHSAPHSPVNPNISLIKRVKSPNIVTLNISRESSRSPIALNYEARQQHSQQHSFSTPSTVSNLSTSVLGPLSDTNDIKTPHPERPNHKTANRILKKESPVETSKSNLILSKVASTRQEDSFTSRNDDLDKEQGSSPLNSKFAPEEIVLSGKNKIYICKECQRKFSSGHHLTRHKKSVHSGEKPHSCPKCGKRFKRRDHVLQHLNKKIPCISNETTVDAPIMNPTVQPQDGKAAINQQSTPLN | Function: Transcriptional repressor of photolyase PHR1. Recognizes and binds the sequence AG(4) in the upstream repressing sequence of PHR1. Derepresses PHR1 transcription when phosphorylated.
PTM: RAD53-dependent phosphorylated in response to DNA damage.
Sequence Mass (Da): 90211
Sequence Length: 796
Subcellular Location: Nucleus
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Q58D79 | MADTIFGSGCDQWVCPNDRQLALRAKLHTGWSVHTYQTEKQRKSQSLSPAEVEAILQVIQRAERLDILEQQRVGRLVERLETMRRNVMGNGLSQCLLCGEVLGFLGSSSVFCKDCRKKVCTKCGIEASPSQKRPLWLCKICSEQREVWKRSGAWFYKGIPKFILPLKIPGQADHPSFRPLPVEPAEQEPRSTETSRVYTWARGRVVSSDSDSDSDLSSSSLDDRLRPAGVRDPKGNKPWGESGGSVESLKMGPTRPASCLSGSQSSLASETGTGSADPQGGPRTLAGPRGPR | Function: Rab GTPase effector involved in the late steps of regulated exocytosis, both in endocrine and exocrine cells.
Sequence Mass (Da): 32043
Sequence Length: 292
Domain: The N-terminus of the RabBD domain is necessary and sufficient for interaction with RAB27A.
Subcellular Location: Cytoplasm
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Q9UNE2 | MADTIFGSGNDQWVCPNDRQLALRAKLQTGWSVHTYQTEKQRRKQHLSPAEVEAILQVIQRAERLDVLEQQRIGRLVERLETMRRNVMGNGLSQCLLCGEVLGFLGSSSVFCKDCRKKVCTKCGIEASPGQKRPLWLCKICSEQREVWKRSGAWFYKGLPKYILPLKTPGRADDPHFRPLPTEPAEREPRSSETSRIYTWARGRVVSSDSDSDSDLSSSSLEDRLPSTGVRDRKGDKPWKESGGSVEAPRMGFTHPPGHLSGCQSSLASGETGTGSADPPGGPRPGLTRRAPVKDTPGRAPAADAAPAGPSSCLG | Function: Rab GTPase effector involved in the late steps of regulated exocytosis, both in endocrine and exocrine cells (By similarity). Acts as a potential RAB3B effector protein in epithelial cells.
Sequence Mass (Da): 34464
Sequence Length: 315
Domain: The N-terminus of the RabBD domain is necessary and sufficient for interaction with RAB27A.
Subcellular Location: Cytoplasm
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Q768S4 | MADTIFSSGNDQWVCPNDRQLALRAKLQTGWSVHTYQTEKQRRSQCLSPGELEIILQVIQRAERLDILEQQRIGRLVERLETMQRNVMGNGLSQCLLCGEVLGFLGSSSVFCKDCRKKVCTKCGIEASPGQKRPLWLCKICSEQREVWKRSGAWFYKGLPKYILPLKTPGRADDPHFRPLPVEPTETQPPSAETSRVYTWARGRVVSSDSDSDSDLSSSSLEDRPLPSGVKGTKGDKPRGDSGASMESPRLGPARPPSHLSGSQSSLGSEAGTGATEPQGGTPAQPEPRVPGKRHTWATPRY | Function: Rab GTPase effector involved in the late steps of regulated exocytosis, both in endocrine and exocrine cells. Regulates the exocytosis of dense-core vesicles in neuroendocrine cells through interaction with RAB27A. Acts as a potential RAB3B effector protein in epithelial cells.
Sequence Mass (Da): 33259
Sequence Length: 302
Domain: The N-terminus of the RabBD domain is necessary and sufficient for interaction with RAB27A.
Subcellular Location: Cytoplasm
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Q9HJT5 | MADYEKQKMNAAIKAAEYVRSGMIVGLGTGTTSYYLINEIGRRVREEGLKIRAVCTSRRTEDLAKQNGIEVIQGTKDQIDLTIDGADQVGMYGTLIKGGGGALLREKIVAYNSKEMYVIVDSRKIEAAHFGSFPLPVEIVPFMHMRTLENLRGICTQTDLRMNEKGEPFVTDNGNYIADMHMGMIDDPINLERSLKSIPGVVEVGLFNGIAKRIFEGTDEGCNIYSITNSGIKKEEVYFDP | 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): 26729
Sequence Length: 241
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
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Q5JH26 | MNVEEMKKAVAKEALKFIEDEMVVGLGTGSTTAYFINYLGKLLMEGELEDVYGVPTSHQARLLALEAGIPVVSLDEVDAIDIAVDGADEVDPHMNLIKGRGAALTMEKIIEYRAGMFIVLVDESKLVEYLGQKMPVPIEVIPAAWRAIAEELEVFNATAELRMAVKKDGPVVTDNGNFILDAKFARIEDPLDLEIELNTIPGVVENGIFADIADIILVGTPEGVKRMER | 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): 25014
Sequence Length: 229
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
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B9KYD3 | MGTERAKERAARFAASLVEDGMIVGLGSGSTAELAVRALGERLHDGLRLIGVATSQRTAALARRVGIELRDPDSVDRIDLAIDGADEVEERSLGLLKGRGGALVREKLVARMARRLVIIIDDSKLVAALGARFPLPVEVVPFGWRWCARWLEDLGGRPTLRCRPTGHPFRSDNGNLILDVAFGAIADPAWLDRTIKMLPGVIDHGLFLDMADLVIVGSETGIRLLERSRTVSETSKS | 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): 25694
Sequence Length: 237
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
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Q72J47 | MERPLESYKKEAAHAAIAYVQDGMVVGLGTGSTARYAVLELARRLREGELKGVVGVPTSRATEELAKREGIPLVDLPPEGVDLAIDGADEIAPGLALIKGMGGALLREKIVERAAKEFIVIADHTKKVPVLGRGPVPVEIVPFGYRATLKAIADLGGEPELRMDGDEFYFTDGGHLIADCRFGPIGDPLGLHRALLEIPGVVETGLFVGMATRALVAGPFGVEELLP | Function: Involved in the first step of the non-oxidative branch of the pentose phosphate pathway. It catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. Can also act on D-ribose-5-diphosphate and D-ribose-5-triphosphate as substrate.
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 24039
Sequence Length: 227
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
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Q73M68 | MDTSQLKERVAYHAIDTLFSEGKIFDGMKIGLGTGSTAMPAVHRLAQLLSSGKLKKIYAVPTSFQTSIECEKLGIPIYSLSSQQIGGSLDLAIDGADEIDPDKNLIKGGGAALLKEKIIAYNSKEFVVIADERKKVKSMGKGFALPIEIIPEARLSITKALEAQGIEVFLREGVKKMGPVVTDNGNFIIDVKWPKAADVDPKALEESLNKITGVVENGFFTKNTPRVFIVHQDGNIEDL | 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): 25917
Sequence Length: 239
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
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O83625 | MHERNTTTNTPLDVTAQKLLVAQRSVDTLVQEGVLHAHMSIGLGTGSTAMPAVKRIADHLARGTLSDIAAVPTSFQTALICERYNIPLFSLSSKRIGGKLDVTIDGADEIDTQNFVIKGGGAALLQEKIAAYNSAHFVIIVDETKVVETLGTRAALPIEVVPEARMSVMRTLQDWGLSVHIREAVRKKGPVVTDHGNFILDARWQSLPTRTPQDMERALNALPGVIENGLFTERTVRVFVAHADGSVEERSASF | 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): 27573
Sequence Length: 254
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
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Q5V2C7 | MDLRVIDKSDTELSIEIAGEDHTFMNVIKGALLETEGVTAATYDVNPEQSGGQTDPVLTIKTEEGVDALEALEDGTDAVIEKADNFTDAFEAAA | 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): 9989
Sequence Length: 94
Subcellular Location: Cytoplasm
EC: 2.7.7.6
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B1L7Q7 | MEIEVVDVSRNEIRVLIRGETHTLLSPLVEELNSLDEVEFAGYDVPHPLKEESVLFLRVKEGMNPREVLKGAIRRLMEKYEIIGNSFIEELSSLKVNH | 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): 11288
Sequence Length: 98
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q8TSS4 | MELNILNKTNNELEVELRGETHTLLNLLKDLLIKDERVEAAFYDMKHVSISDPILYIKTDGTDPILVLKETAAIIIAQCDEFIDVFSKAANA | 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): 10374
Sequence Length: 92
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q46C10 | MELNILSKTDNELEVKLKGETHTLLNILKDLLIKDQRVEIAFYDMKYVSISDPILYIKTDGTNPIEVLKDAASQIISQCDEFTDVFSKAVNA | 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): 10420
Sequence Length: 92
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q57832 | MEIKILERKDNLVEIELINEDHSLPNLLKDILLTKEGVKMASYSIDHPLLHPETGRYISNPKITIITEEGTDPLEVLKEGLRDIIKMCDTLLDELKEKK | 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): 11392
Sequence Length: 99
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q8TZ81 | MKLPEVEVVVKKYDKDEVLLELPGEDHTLCNLLRWALNRQDGIIATYRIEHPILGKEHKVDEERYVPPKMRIRAVDEDADAREALERAIEELLELVEEAKEEFSGALEEKES | 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): 13024
Sequence Length: 112
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q8PVT0 | MELNILNKTNNELEVELRGETHTLLNLLKDLLIKDERVVTAFYDMKYVSISDPVLYIKTDGADPILVLKDVVAIIVSECDEFIDVFSKAANA | 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): 10371
Sequence Length: 92
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
O27372 | MEVILDKRNEMEIVFEGETHTLCNVLRSILMEDEKVKAAAYSIDHPIVGEPQLYIRAGSPKKSLKAAAETLRDRCDEFRRLIESL | 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): 9732
Sequence Length: 85
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
A0B533 | MNLKVLKKTEDELRIEFEGERHTLLNLLRSELLEDERVVIATYDAKFPIMDNPVFRLKTRGVDPLDVIRDASARIADLCDEFLREYEEAVR | 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): 10707
Sequence Length: 91
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
O74105 | MPEAVYRCAKCGREVKLDLSTTRDLRCPYCGSKILYKPRPKIPRRVKAI | 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): 5681
Sequence Length: 49
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
B1Y9C5 | MAEERKLYMCMRCGRVFSKPEMEILPGIRCPYCNFKIIMKVRSPTVKRIPAV | 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): 6122
Sequence Length: 52
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q4JAE8 | MAKYRCGKCWKELDDDQLKTLPGVRCPYCGYRIIYMVRKPTVKIVKAI | 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): 5652
Sequence Length: 48
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q980B8 | MVSGMSTDEEKEGTSDEEVNEEKEVEETSEDEFPKLSIQDIELLMRNTEIWDNLLNGKITLEEAKKLFEDNYKEYEKRDSRRKAKKAVSKKVKKTKKKEKSVEG | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Probably binds dsDNA.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 12176
Sequence Length: 104
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
B8YB65 | MVSGMSTEEEKEGTNDEEVSEEREVEETSEEEFPKLSIQDIELLMKNTEIWDNLLNGKISVDEAKRLFEDNYKDYEKRDSRRKAKKAASKKVKKTKKKEKSVEG | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (Probable). A molten-globule protein, it binds dsDNA in the RNAP, in vitro binds dsDNA but not ssDNA (Probable) . Its position in RNAP implies it functions in both transcription initiation and elongation (Probable).
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 12148
Sequence Length: 104
Domain: Forms a helix-turn-helix motif with helix 1 (residues 38-56) nearly parallel to helix 2 (residues 61-82); helix 1 contacts both Rpo5 and Rpo1N. The C-terminal region (residues 81-104) is required for DNA-binding.
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q4JAJ6 | MSEDDSKKEPEPEETEAEIKHEEISREEDDEGGEFSTVTISDIEMLLKDTEIWDKLLRNELSIEEAKKMFDDVARSYSKADKKKRRVEKKPKKGKVTKKSDEEEE | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (Ref.2). In vitro binds dsDNA but not ssDNA .
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 12308
Sequence Length: 105
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
B8YB59 | MMESKAQEIILSCEINSIERGSLKNLSIIHMSCNDFNISFDIIDSINIFSQKEKVKAFISKNRLSYTNDDFCGHGYIVTELKDSSSNNGNRYITIISLFGLLVKIISNKESFLKIHQLNVMDHIYFCVKKNT | 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): 15120
Sequence Length: 132
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
Q4JAY4 | MMQGTCKISSIEKGALKNLYVVKMDCDNDLKIEFDITKELSIFSKDEEVTFIISREKPEYSEKDFCAHGYLFLERQQEDGSFIDEISLYGLIVKILSKNGLINSKLFKMMDHVYYCVKKKA | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
PTM: This subunit is phosphorylated.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 14054
Sequence Length: 121
Subcellular Location: Cytoplasm
EC: 2.7.7.6
|
A0Q4K8 | MSNNNSKQEFVPNIQLKEDLGAFSYKVQLSPVEKGMAHILGNSIRRVLLSSLSGASIIKVNIANVLHEYSTLEDVKEDVVEIVSNLKKVAIKLDTAIDRLDLELSVNKSGVVSAGDFKTTQGVEIINKDQPIATLTNQRAFSLTATVSVGRNVGILSAIPTELERVGDIAVDADFNPIKRVAFEVFDNGDSETLEVFVKTNGTIEPLAAVTKALEYFCEQISVFVSLRVPSNGKTGDVLIDSNIDPILLKPIDDLELTVRSSNCLRAENIKYLGDLVQYSESQLMKIPNLGKKSLNEIKQILIDNNLSLGVQIDNFRELVEGK | 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): 35387
Sequence Length: 323
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
|
Q2A4H7 | MALENLLHPTNIKIDEYAKNATKFSFEALERGVGYTLGFALKQTMLYSIAGACVTSIKINDGKVTSLEDVIPCDETVADIILNVKSLSVTLAEDVETGTITFELSGSEEEIFSEEAKLSEGLAITEEVFICSYNGGKKLKIEAKVEKGVGFRPAQDNFKDGEFLLDATFSPVVFCDFEIKDARVGRRTDLDKLELNIKTNGNVNCEEALRLAATKIQNQLRNIVDIEEINKGIFVEDPKDINPILLKHVEELNLTARSSNCLKAVNIRLIGELVQKTENELLKAPNFGKKSLTEIKDKLSELGLSLGTLIENWPQDL | 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): 35074
Sequence Length: 317
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
|
Q18CI5 | MIEIEKPKVDIVELSEDYRYGKFVIEPLERGYGITIGNALRRILLSSLPGVAVNAIKIDGVLHEFSTIPGVKEDVTEIILTLKELSATIDGEGSRTLKIEAQGPCSITGADIICPPDVEILSKDLAIATLDDNAKLNMEIFVDKGRGYVSAEENKTENVPIGVLPVDSIYTPVEKVSYHVENTRVGQKTDYDKLVLEVWTNGSINPQEGISLAAKVLVEHLNLFIDLTEHVSSVEIMVEKEEDQKEKVLEMTIEELDLSVRSYNCLKRAGINTVEELANKSEDDMMKVRNLGKKSLEEVIQKLEELGLGLKPSEE | 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): 34920
Sequence Length: 315
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
|
Q890R0 | MLEIEKPKIECIEMTENGSYGKFVVEPLERGYGITLGNALRRILLSSLPGVAVNSIKIENVLHEFSTVKGVKEDVTEIILNIKLLALKMTGEGPKTIYIDAKGPGVVTAADIKTDSDVEIINKDLHIATLDDDGKLYIEMTVDRGRGYVSQNRNKVEGMPIGTIPIDSIYTPVKRVNFTVANTRVGQITDYDKLTLEIWTNGTIMPDDAISLSAKILIEHFKLFMTLTDHADDVEIMVEKEEDKKEKVLEMTIEELDLSVRSYNCLKRAGINTVQELTERTVEDMMKVRNLGRKSLEEVEQKLEALELGLKQSEE | 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): 35344
Sequence Length: 315
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
|
Q2GEB6 | MSAVLDKGSLVDVFSSPSVVFNQIREGYCAEFIVEPLRVGFGLTIGNAMRRVLLSSLSGFAISAVGIKGLTHEFSCIPGVREDFADLALNLKKVVLKSISGATCGNLHLSVTDGGAVFSNMISPSHDFEVVNGDLLICNVAEGVSLEMEMKVSSGFGYVSSVSVRKDEYDLEGAVPIDAIYNPVRAVNFTVKPTSAGSFAGHDKLILYVETNGAMDPKTAVLEASKILSTQARCFLNIADPEHRVHGVPCGVSTSDRNDASDLLSARIDRLYLSARARKCLNGENIVYIRDLVSRTEADLLKAPNFGRRSLEEVKKELFSKGLSLGMNLDSHG | 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): 35796
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
|
Q9TL28 | MPYIKHIETKRISARTYYGRFCVLPLPAGQGITLGNALRRILLGDLVGFAATSANLAGASHEFDTLPGIRESVLEILLNIKQLVFKQISSRPKDTNRFAMRASLNLTGPATVTAKDLVLPSWMKVVDPSQYIATLASGASLEFEIQLSQGSGYRLRRTSLVPPGFTLPPPRDPLEPENDSKSETKSKSKGKSKNTSTSDVQLADTDVNAQIIDTDSNSTETEKEAPHIPSMRDDHMTLHIDAVFFPVTRVNYRVEEEVINGRRREELVIDIWTNGSLSPRKALDQAAVILIRMLASLQAPPPLLIEPEKKPTTKTIAKEIALTPIESLDLSVRSFNCLKRANITNVGKLIAYTRQELLQLKNFGTKSASEVVDVLNSRFKLALKGEEVTDQEQVVNQPSSQIATKKGARKKVNRASRPIDSKETRRSRNPVKSTASEVPEKMLRKSSKTKVKAPKSETLPKPSKSANLQQAEESLQVPKLRRKSELSSSQNPEET | 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): 54763
Sequence Length: 495
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
|
Q0AUK9 | MLEMEKPRIDCVEKNSSSNYGRFVIEPLERGYGTTLGNSLRRVLLSSLPGAAVTSIKIDGVLHEFSTIPGVLEDTTEIILNIKKLVLSYTGSERKIIRLEQQGPKEVKASDITPDAEVEILNPDLHLASLDEDGKVEIEMTVERGRGYVSSDQQPQKNDDIVGLIPIDSIFTPVSRVNYTVENARVGKRTDYDRLNLEVWTNGSISPEEAISLSAQILIEYLKLFTEIDDTYAEVEILVEKEEEKKDKILEMSIEELELSVRASNGLKRASINTVGDLIAKNREEMSKIRNLGQKSLEEIERKLKELNLSFRKSED | 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): 35581
Sequence Length: 316
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
|
A6BM51 | MIDSQKEHQKLKITLVSPEQIRVWSETILPNGKRIGEVTNPKTIDLATNKPERNGSFCERIFGPVKSKKCACENKFGEDKKGFAFVDRKKTNDSGLCEHCGVEFMDSRIRRYRMGYIKLASPVTHIWYIKRVPSYIATLIGKQNSEIKDLVYCNLFLARPAVNKPTILRFRGLLQHGEITSWMEILVPYISGWNFVEFQERELATGGTSIQKQLIGLNLRALLNHSYMEWRKLLKNHRIQKRKNKIEKRKNFLVKRIKFAKNLIQAKINPEWMVLCLLPVLPPELRPIFVLGEQVVVESDFNKLYQKVNLRNKNLQNSFEIQGGPFYSTGDFLTLQKRLLQEAVDALLDSGKSGQPRKDHFRNRPYKSFSDVIAGKEGRFRANLLGKRVDYSARSVIVVGPSLALHQCGLPRELAIKLFQPFLIRNLIGQGVVANIRAAKLLIQRRIPVVWKILQQILLGHPVLLNRAPTLHKFGILAFQPILVKERAIRLHPAVCTGFNADFDGDQMAVHLPLSIEAILESRLLMFSHTNLLSPSNGSPITKPTQDMLLGLYILTTEKPRNISQFRCRPSNPTKKFLPEANLCFCNYDDVFIAYQKNRVSLKNPLWFRWKVVNGTILTSVDQEVPIEFQYQSLGTSQQIYEHYTIQRARSGKVLTIYIRTTVGRIIFNREIENAFLAFSKLSESPRAMPVFLNKSDTMFLMILNSCSAKQNCGKPAKRGLKYFVNSAEKILEVSLYETKKTSPFLQ | 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): 85648
Sequence Length: 747
Subcellular Location: Plastid
EC: 2.7.7.6
|
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