ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
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
Subcel... |
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.-
|
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'-... |
Q45493 | MKFVKNDQTAVFALGGLGEIGKNTYAVQFQDEIVLIDAGIKFPEDELLGIDYVIPDYTYLVKNEDKIKGLFITHGHEDHIGGIPYLLRQVNIPVYGGKLAIGLLRNKLEEHGLLRQTKLNIIGEDDIVKFRKTAVSFFRTTHSIPDSYGIVVKTPPGNIVHTGDFKFDFTPVGEPANLTKMAEIGKEGVLCLLSDSTNSENPEFTMSERRVGESIHDIFRKVDGRIIFATFASNIHRLQQVIEAAVQNGRKVAVFGRSMESAIEIGQTLGYINCPKNTFIEHNEINRMPANKVTILCTGSQGEPMAALSRIANGTHRQIS... | 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 ... |
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
|
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
|
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
|
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
|
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
|
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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. ... |
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. ... |
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. ... |
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 Acti... |
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): 1682... |
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 t... |
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 t... |
A7NHM5 | MFEPVATARQRAVACCTFTTEQEDVVQWLVWALPALVIGLAIGAGIGILIYKNSVQSQIRQIEAEARLQLEATRSEQKDLILRATDEALRLRTEAEAQIREARAALAKQEERLQRKEENLDRKIEGLERRERQLQQRERQMEQLHQEAEHLRQQQRAELERISALSQEEARAIILKRVEDETRDEAARRIREIEKTMHEEADKLARKVISMAIQRCASDYVAEVTVSTVALPSEELKGRIIGREGRNIRAFEQLTGVDIIVDDTPEAVTLSCHDPVRREVARLALIKLLKDGRIHPTRIEEVVHKTQQEVDQVMREEGER... | 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.-.-
|
Q1AW41 | MSVLWMVLGLAIGIAVGAAAGYIVCRSRTDRRLAETRADARSIIEDANRQAETLRREAELAAKEAAMRIKDEAEAEVRARRAEISRIEERLDNRDTALDRREVELDERRRRLSETEDELRRREESLAEREQEQLRALEEISGLSRAEAEERLFSRVEAELERRIGRMVRNRISEAEENADLEARRILATTMERLASDLTSESTVKAVELPSDDMKGRVIGREGRNIRAFEAATGVDVIIDDTPETVVLSCFDPVRREVARIAMERLVKDGRIHPGRIEQVVAKVRKEVEKEMKAAGRQALYDAKVSGSMHGDLLRLLGAL... | 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.-.-
|
A8M7V7 | MSGFDAVLLVAVLLLALIVLGAVLVGVRAVRGIAGAPRPEDPAFIAEKDRQEQSLAALRSAADEANSTVDAAKSAAAAARTEAAAARAEAKAARAEARRVLDGARAEADTILERVHKQAEADAEQLRTAARRSGEREAAVLATTTREQAAEVERRAARMDDRERLHSEEVERLAERDRQLSAASAALAARESTLVDRDRELAQAEDRRRRELERVAGITAEAARGELVEAIEAQAKREAALLVREIESEARNTGEERARHIVVDAIQRVASEQTAESVVSVLHLPGDEMKGRIIGREGRNIRAFESVTGVNLIIDDTPEA... | 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.-.-
|
A1U2M9 | MEFTFLGTSAGTPTRSRNVTGLALCLSGPKPWYLVDCGEGTQHQLMRTRYSVMQLRAMFITHIHGDHIFGLPGLLTSASMLGRTEPLDIIAPPQVRRFIDAVIENSDSSLSYPLNFINSEAPDFYWQDDHLGVTNVALSHRVPCRAYVFTERNLERQLQKEKLVADGIEPGPQWGDLQKGKDVLLDDGRLLRSNDYTHIPRTARKIIVGGDNDTPELLKDACQGTHVLIHEATYTQDVADRVGPWPQHSSAQQVARFAQATKLPNLVLTHFSSRYQSAPGGSPHINQLAAEALQHYKGQLFLARDFDTYRLEKDFQLHKV... | 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, gener... |
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, gener... |
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, gener... |
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, gener... |
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 ... |
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
Seque... |
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
Seque... |
P09651 | MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGYGGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFGNYNN... | 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 result... |
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 resulti... |
Q2HJ60 | MEREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYG... | 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 p... |
P22626 | MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGN... | 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 p... |
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... |
Q9USM1 | MESVFGRVRNETSERGKYGLVSVKAGKLQRKPGTNILQADHRKGVIYMQMASDELLHFYWKERARVSREVEDDYIIFPEEAEFIKIDECTTGRVYALKFKSSSQIHFYWMQEYSDEKDKETASLINQLIADPVNTTRTINSHNNSSSRGTDDSSTSQLLQLFGAASQDALQDFNWEVLSPTAEAPAILPRFPNVNESANMYRASSESNLNGPHATAGENGEDHEEATASPLDENIDYTHSRTLELLEQLQPLILNETTFVEPFSIDRESHRVITHPRVYPKIFPHSPSDLLRISGRAELSENRDFFKHLSSLMEAVAKPE... | 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 ... |
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)... |
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... |
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)... |
Q9GZS1 | MAAEVLPSARWQYCGAPDGSQRAVLVQFSNGKLQSPGNMRFTLYENKDSTNPRKRNQRILAAETDRLSYVGNNFGTGALKCNTLCRHFVGILNKTSGQMEVYDAELFNMQPLFSDVSVESELALESQTKTYREKMDSCIEAFGTTKQKRALNTRRMNRVGNESLNRAVAKAAETIIDTKGVTALVSDAIHNDLQDDSLYLPPCYDDAAKPEDVYKFEDLLSPAEYEALQSPSEAFRNVTSEEILKMIEENSHCTFVIEALKSLPSDVESRDRQARCIWFLDTLIKFRAHRVVKRKSALGPGVPHIINTKLLKHFTCLTYN... | 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 inte... |
Q8K202 | MATLESPGMDDQAGDTETEALQSARWLYCGEPDDRQKAVLVQFSNGKLQNPGDMRFTLYNSTDLVNPRQRSHRIVAAETDRLSYVGNNFGTGALKCNALCRHFVGILNKTSGQMEVYDAELFNMQPLFAGMGTEVIKLGGQHLYLLAFCQPSKNLAEAGDLLLSRHRQGHCIAVLLDDDAIEREPPLENQNKTFRDKLDSCIEAFGSTKQKRSLNSRRMNKVGSESLNLSVAKAAESIIDTKGVNALVSDAMQDDLQDGVLYLPPCYADAAKPEDVYRFEDILSPAEYDALESPSEAFRKVTSEDILKMIEENSHCSYVI... | 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 inte... |
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 dephosphoryl... |
P28364 | MSRGTIYTESTMDFQKVRKIQFGLLDPKEIQAMSVVQVENEKIYDNGIPTDGGINDLRMGTMEKAMRCSTCQGDSKECPGHFGHIELAQPVFHIGFIDLVKKILKCVCFNCNKLLITDKHDKYSALKRVKDPKLKLNKVYKVCKDIKVCGKADRKSETYTEGSGQKQPRLRKTGLKIKAEFPIDEDDPSTNDNKRDLSASECLKILGRISPDDCKFLGFDMVLARPEWLIISRLPVAPPPVRPSVCMGSNIRQEDDLTHQYQQILKANNQLRKHLSTANHIINENYQLLQFYCATLIDNEQAGQMVSRHKSGGKAIKAIR... | 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 s... |
P47736 | MIEKMQGSRMDEQRCSFPPPLKTEEDYIPYPSVHEVLGREGPFPLILLPQFGGYWIEGTNHEITSIPETEPLQSPTTKVKLECNPTARIYRKHFLGKEHFNYYSLDAALGHLVFSLKYDVIGDQEHLRLLLRTKCRTYHDVIPISCLTEFPNVVQMAKLVCEDVNVDRFYPVLYPKASRLIVTFDEHVISNNFKFGVIYQKLGQTSEEELFSTNEESPAFVEFLEFLGQKVKLQDFKGFRGGLDVTHGQTGTESVYCNFRNKEIMFHVSTKLPYTEGDAQQLQRKRHIGNDIVAVVFQDENTPFVPDMIASNFLHAYVVV... | 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
|
A2ALS5 | MIEKMQGSRMDEQRCSFPPPLKTEEDYIPYPSVHEVLGREGPFPLILLPQFGGYWIEGTNHEISSLPETEPLQSPTTKVKLECNPTARIYRKHFLGKEHFNYYSLDTALGHLVFSLKYDVIGDQEHLRLLLRTKCRTHHDVIPISCLTEFPNVVQMAKLVCEDVNVDRFYPVLYPKASRLIVTFDEHVISNNFKFGVIYQKLGQTSEEELFSTNEESPAFVEFLEFLGQKVKLQDFKGFRGGLDVTHGQTGTESVYCNFRNKEIMFHVSTKLPYTEGDAQQLQRKRHIGNDIVAVVFQDENTPFVPDMIASNFLHAYVVV... | 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
|
Q684P5 | MFGRKRSVSFGGFGWIDKTMLASLKVKKQELANSSDATLPDRPLSPPLTAPPTMKSSEFFEMLEKMQGIKLEEQKPGPQKNKDDYIPYPSIDEVVEKGGPYPQVILPQFGGYWIEDPENVGTPTSLGSSICEEEEEDNLSPNTFGYKLECKGEARAYRRHFLGKDHLNFYCTGSSLGNLILSVKCEEAEGIEYLRVILRSKLKTVHERIPLAGLSKLPSVPQIAKAFCDDAVGLRFNPVLYPKASQMIVSYDEHEVNNTFKFGVIYQKARQTLEEELFGNNEESPAFKEFLDLLGDTITLQDFKGFRGGLDVTHGQTGVE... | 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
Seq... |
Q9N1T2 | MGEPEEVMPGSGAVFTFGKTQFAENIPSKFWFRNDVPTFLSCGDEHTAVVTGNNKLYMFGSNNWGQLGLGSKSTVSKPTCVKALKPEKVKFAACGRNHTLVSTEGGKVYAAGGNNEGQLGLGDTEERSTFHLISFFTSQRKIKQLSAGSNTSAALTEDGELFMWGDNSEGQIGLENVTNVCVPQQVTVGKPISWISCGYYHSAFVTTEGQLYTFGEPECGKLGLPNQLLVNHRMPQPVPGIPGKVVQVACGGGHTVVLTEKAVYTFGLGQFGQLGLGTFLFETSVPKAIEHIKDQKISFIACGENHTALITDMGLMYTFG... | 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 integ... |
Q92834 | MREPEELMPDSGAVFTFGKSKFAENNPGKFWFKNDVPVHLSCGDEHSAVVTGNNKLYMFGSNNWGQLGLGSKSAISKPTCVKALKPEKVKLAACGRNHTLVSTEGGNVYATGGNNEGQLGLGDTEERNTFHVISFFTSEHKIKQLSAGSNTSAALTEDGRLFMWGDNSEGQIGLKNVSNVCVPQQVTIGKPVSWISCGYYHSAFVTTDGELYVFGEPENGKLGLPNQLLGNHRTPQLVSEIPEKVIQVACGGEHTVVLTENAVYTFGLGQFGQLGLGTFLFETSEPKVIENIRDQTISYISCGENHTALITDIGLMYTFG... | 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 processe... |
Q9R0X5 | MAESESLVPDTGAVFTFGKTKFAENIPSKFWFKNDIPICLSCGDEHTAIVTGNNKLYMFGSNNWGQLGLGSKAAIIKPTCIKALKPEKVKLAACGRNHTLVSTDTGGVYAAGGNNEGQLGLGDTDDRDTFHQIVFFTPADTIKQLSAGANTSAALTEDGKLFMWGDNSEGQIGLEDKSNVCIPHEVTVGKPISWISCGYYHSAFVTMDGELYTFGEPENGKLGLPNELLMNHRSPQRVLGIPERVIQVACGGGHTVVLTEKVVYAFGLGQFGQLGLGTFLFETSEPKIIERIKDQKICHISCGENHTALMTELGLLYTFG... | 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... |
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
|
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
|
P39956 | MTKLIAPSEIVGGVPVFKPTYEQFEDFYAYCKAINKYGMKSGVVKVIPPKEWKDKLDLPYSAETLQKIKIKSPIQQHISGNKGLFMVQNVEKNKTYNIIQWKDLSKDYVPPEDPKARRNSRKGSVSKSTKLKLKNFESSFNIDDFEQFRTEYTIDLSDFQNTERLKFLEEYYWKTLNFTTPMYGADTPGSIFPEGLNVWNVAKLPNILDHMETKVPGVNDSYLYAGLWKASFSWHLEDQDLYSINYIHFGAPKQWYSIPQEDRFKFYKFMQEQFPEEAKNCPEFLRHKMFLASPKLLQENGIRCNEIVHHEGEFMITYPY... | 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 Locat... |
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
|
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 fo... |
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
Seque... |
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-phos... |
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-phos... |
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-phos... |
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-... |
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-phos... |
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-phos... |
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... |
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.... |
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.... |
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.... |
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.... |
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... |
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.... |
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... |
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.... |
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... |
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... |
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... |
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 Loc... |
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 transcri... |
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... |
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... |
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
... |
A0Q4K8 | MSNNNSKQEFVPNIQLKEDLGAFSYKVQLSPVEKGMAHILGNSIRRVLLSSLSGASIIKVNIANVLHEYSTLEDVKEDVVEIVSNLKKVAIKLDTAIDRLDLELSVNKSGVVSAGDFKTTQGVEIINKDQPIATLTNQRAFSLTATVSVGRNVGILSAIPTELERVGDIAVDADFNPIKRVAFEVFDNGDSETLEVFVKTNGTIEPLAAVTKALEYFCEQISVFVSLRVPSNGKTGDVLIDSNIDPILLKPIDDLELTVRSSNCLRAENIKYLGDLVQYSESQLMKIPNLGKKSLNEIKQILIDNNLSLGVQIDNFRELV... | 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 f... |
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 f... |
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 f... |
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 f... |
Q2GEB6 | MSAVLDKGSLVDVFSSPSVVFNQIREGYCAEFIVEPLRVGFGLTIGNAMRRVLLSSLSGFAISAVGIKGLTHEFSCIPGVREDFADLALNLKKVVLKSISGATCGNLHLSVTDGGAVFSNMISPSHDFEVVNGDLLICNVAEGVSLEMEMKVSSGFGYVSSVSVRKDEYDLEGAVPIDAIYNPVRAVNFTVKPTSAGSFAGHDKLILYVETNGAMDPKTAVLEASKILSTQARCFLNIADPEHRVHGVPCGVSTSDRNDASDLLSARIDRLYLSARARKCLNGENIVYIRDLVSRTEADLLKAPNFGRRSLEEVKKELFS... | 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 f... |
Q9TL28 | MPYIKHIETKRISARTYYGRFCVLPLPAGQGITLGNALRRILLGDLVGFAATSANLAGASHEFDTLPGIRESVLEILLNIKQLVFKQISSRPKDTNRFAMRASLNLTGPATVTAKDLVLPSWMKVVDPSQYIATLASGASLEFEIQLSQGSGYRLRRTSLVPPGFTLPPPRDPLEPENDSKSETKSKSKGKSKNTSTSDVQLADTDVNAQIIDTDSNSTETEKEAPHIPSMRDDHMTLHIDAVFFPVTRVNYRVEEEVINGRRREELVIDIWTNGSLSPRKALDQAAVILIRMLASLQAPPPLLIEPEKKPTTKTIAKEI... | 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 f... |
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 f... |
A6BM51 | MIDSQKEHQKLKITLVSPEQIRVWSETILPNGKRIGEVTNPKTIDLATNKPERNGSFCERIFGPVKSKKCACENKFGEDKKGFAFVDRKKTNDSGLCEHCGVEFMDSRIRRYRMGYIKLASPVTHIWYIKRVPSYIATLIGKQNSEIKDLVYCNLFLARPAVNKPTILRFRGLLQHGEITSWMEILVPYISGWNFVEFQERELATGGTSIQKQLIGLNLRALLNHSYMEWRKLLKNHRIQKRKNKIEKRKNFLVKRIKFAKNLIQAKINPEWMVLCLLPVLPPELRPIFVLGEQVVVESDFNKLYQKVNLRNKNLQNSFE... | 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
Su... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.