ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q5M7Z0 | MPLFLLSLPTPPSASGHERRQRPEAKTSGSEKKYLRAMQANRSQLHSPPGTGSSEDASTPQCVHTRLTGEGSCPHSGDVHIQINSIPKECAENASSRNIRSGVHSCAHGCVHSRLRGHSHSEARLTDDTAAESGDHGSSSFSEFRYLFKWLQKSLPYILILSVKLVMQHITGISLGIGLLTTFMYANKSIVNQVFLRERSSKIQCAWLLVFLAGSSVLLYYTFHSQSLYYSLIFLNPTLDHLSFWEVFWIVGITDFILKFFFMGLKCLILLVPSFIMPFKSKGYWYMLLEELCQYYRTFVPIPVWFRYLISYGEFGNVTR... | Function: E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis.
... |
Q6NTV1 | MKHRPVHERQSSTESKNLKETTQLIMQSSSDHTHHQLGSNDSPSACMSLPVPQLSAEGSCTVGDVTVDLSSQDSQHVARSNSRRVRPSTHGRSPSRHGHTHSHDASGPEDANDDSREQSNSISEVFHLYKWLEKSFPYILIFSAKLVVQHITGISVGIGLLTTFLYANKCIVNQVFLRDKCSKLQCLWVLVFLLFSSFLLYYTFSSQALYYSLVFMNPSLGPLHFFDALWVVGITDFIGKFFFMGLKCIILLVPSFVMSHKSKGYWYMALEELAQCYCTLVSTPVWFRYLIDYGNLDSGAEWHFGILLALLYLILKILII... | Function: E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis.
... |
Q11KH2 | MASSQSDSPPLFDLPVRPDFTIEWKIMREGLAPVAGLDEAGRGPLAGPVVAAAVVLDPDRIPEGLDDSKRLTAEARERLVQEIFEVAAAVSVASLCAASIDESNILKASLEAMRRALDGLCVRPAYALADGRDIPPGLPCPCRAVVKGDQRSQSIAAASMVAKVVRDRMMVRTGTLMPHYGFHSHVGYATERHREAITAYGPVTRLHRMSFSPFKTSGEEDRILASGDAAELIASAFSAADGLNGRDAEKEPV | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
A9WIH1 | MLPDLSIEHDLQRRGYANLAGIDEAGRGCWAGPVVAAAVVLSPAVYRQPDLLAGVNDSKQLTAGARERIYTSIQTHALGVGVGIVPAFLIDAYGILPATRLAMIQALLALPCAVDALIIDAVQLPGISLPQTALVRGDERSLSIAAASIIAKVTRDRLMATADHCFPHYGFALHKGYGTAVHRRALAQYGPSPLHRRTFQPVIEALLSLEQS | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q3AP34 | MHTHYEEPLWQHYEFICGIDEVGRGPLAGPVVAAAVVFPRWFQPTEALLTLLNDSKKLSAKERESLVPAIKAQALHWALAEVQHNVIDEVNILQATMLAMNNAVKALPIIPSLLLVDGNRFTTDLAIPYKTIVKGDSHVFSIAAASVLAKVHRDALMCVYATHYPHYGFERHAGYPTSAHIEAIRQHGRCPIHRQSFKLRQLGEKV | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q822M7 | MKTLAIDEEQLFLSKTIFEEEVYGEGFSIIAGVDEVGRGPLAGPVVAGACILPRGKIFAGVNDSKKLTPKERGKIRDILLNDPDVCYGIGVVSVERIDEINILEATKEAMAKAIANLSVHPDFLLIDGLHLPHKIPCKKIIKGDSKSASIAAASIIAKEYRDDLMRELHQRYPNYGFDKHKGYGTAAHLAALRAFGPCDCHRKSFAPIRQVV | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q3B6X8 | MMPMDTVREYLLWNDFLRVCGIDEAGRGPLAGPVVAAAVVFPRWFSPDEGILRRLNDSKKLTPSLRRELAPAIREEAECWAVEAVDHETIDRINILRATMLAMNRAAESLPRQPDLLLIDGNRFTPNIPVPYQTIVGGDALVFSIAAASVLAKTERDRMMEEYAERYPEYGFERNAGYGTREHVEAIRRHGRSPIHRTSFRLRQLGEK | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q9PL10 | MKSIVEQELLFREKSVFEDQAIKQGYSRIAGVDEAGRGPLAGPVVAGACILPGGKLFLGIDDSKKLSPKQRRYLYELLLEDPEVTCGVGVVSVERIDEINILEATKEAMVQAIASLRSTPDFLLVDGLFLPHEIPCLKIIKGDSRSVSIAAASIIAKEYRDELMRKLHSEYPEYGFDKHKGYGTVAHLQALKQFGPCVYHRKSFSPVKESIREGICQ | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
B3QQY0 | MLSTEFETPLWENLSRVCGIDEAGRGPLAGPVVAAAVAFPRHFKPTGILEKLDDSKKLTAELREELAPAIRESAEAWAVAVVDAEIIDRINILQATMLAMNQAVESLAATPELLLVDGNRFRPVLPIPYQTIVKGDSKVFSIAAASVLAKTRRDELMVAYAAEYPAYGFDLHFGYPTARHVEAIARHGRCAIHRKSFKLRKLGEK | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
A4SC35 | MLTDYEEQLWNSMERICGIDEAGRGPLAGPVVAAAVVFPRWFRPGKGILGRMNDSKKLSPSLRREMAPAIQDAALAWSVSVVDAQTIDRINILSATMLAMNRAVGGLGLTPDMLLVDGNRFSPETPVAYRTLVGGDAYIYSIAAASVLAKTARDAIMSSYDRDYPEYGFARHAGYPTAMHISAIRQHGRCPIHRFSFKVRRLNEA | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
B3QRP3 | MDVAFESPYWKKFQYICGVDEVGRGPLAGPVVAAAVIFDRYFEPSGILEQIDDSKALRHETRVLLSSEIKKQALSFSIAEISPEVIDEVNILQATFLAMNQAIEQLSPIPEFLLIDGNRFKTTLPIPFETVVKGDSKVFSIAAASIIAKVHRDNFMINLAERYPEYGFAQHFGYPTKAHIEAIKMFGRSKVHRKSFKLSCLGEK | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q8TPF4 | MMIAGIDEAGKGPVIGPMCIGGVKIEESRAHILKVLGVADSKKLTPKKREQLASQIKKHADGFFILEITPAQIDELRKIMSMNEIMVICFAKVLEQLKPDIVYADAADVKAERFAENLRRQYAKTNPAHAKKIEIISMHQADAIYPVVSAASIIAKVRRDELIEEIKKEWSVDFGSGYPSDPKTKAFLLKWGKEHDGKFPEIVRQSWQTVENIREELEKAGKK | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q0W5R8 | MAKKRTSTIMGIDEAGRGPVIGPLVVCGIIVEEKDLPAIEAMGLKDSKKLSAKKREEFAAALKNKYKYELSVLPPQEIDARFESEDNLNRLEVNCFAGLIRSAKPTIAYLDACDVNAERFGINIKKCLDFELEIVSAHEADSKYPIVSAASIIAKVHRDSLIREISEKMGEDVGSGYPADPVTISFLKNYYMKHKCLPDCARKSWKTSNAVIADCLQARLFQFE | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
A7I9P7 | MICGVDEAGKGSVLGPMVIAGVGVGSTEMIDGFGLRDSKQLSPSERERLFVLIKKKCKVATVVISAAEIDAFRREMTLNTCVARAHAVVIAQLAPEIAYVDACDVNPFRYAETVRGYLSSPCEIVSEHHADSTYPVVSAASIVAKVTRDREIAKLAKKYGQIGSGYPSDPETIAYLNAYIDEHRIPPPIARKSWKTVSTLLAKKTQSSLTSFF | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q2FP80 | MICGVDEAGKGSVLGPMVVAAVGCTDMDDLIALGVADSKKLSSKSREKISADIKAQFPFSIVIRTAHDIDELRRTMTMNEIVARSHAEALIPLNCTCAYVDACDVSEERYEETVSSFSPPDCTIVARHKADSLFPPVSAASIIAKVERDRIIEELSKEYGDIGSGYPSDPVTITYLTKYIRHHNQPPVIARSSWETVKNLLHQKNQSSLLDF | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q57599 | MIIIGIDEAGRGPVLGPMVVCAFAIEKEREEELKKLGVKDSKELTKNKRAYLKKLLENLGYVEKRILEAEEINQLMNSINLNDIEINAFSKVAKNLIEKLNIRDDEIEIYIDACSTNTKKFEDSFKDKIEDIIKERNLNIKIIAEHKADAKYPVVSAASIIAKAERDEIIDYYKKIYGDIGSGYPSDPKTIKFLEDYFKKHKKLPDIARTHWKTCKRILDKSKQTKLIIE | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q8TYV5 | MSGVMGIDEAGRGPVFGPMVVAGVLAPKRELGLGARDSKELTRSARRRLIRALMSDERLRVDLRIVWPWEIDEEGVAKAEFEAIRELVRRAMPDEVILDKPGNYSPERLRRELDLPEGINLIAEERADAKYEVVSAASIVAKTYRDWIVRLLELEYGEVGSGYPSDPRTVDRLRRELRRGGELLKYFRRSWETYKRVESEVKQRKLEDFF | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
A2STJ6 | MTICGVDEAGKGPVLGPMITAGVLVSDMSELEMLGIKDSKKLSPKKRESLFEEITFSWKTYTVVRTPFDIDSREGTMNAFTASCHADVVRALCADFVYLDACDVNAKRFGENVLRLSGSSAHVCSEHKADAKYAVVGAASIVAKVTRDRCIADLKEEYGEIGSGYPSDPATISFLTEYIRTRGEVPLCARRSWQTVQDILDRASQTGLSDFF | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q2S009 | MLSHERRLWADGYERVAGLDEAGRGCLAGPVVAAAVIMPPQVEITAIQDSKALSEGQRLDARATIEDEAVAASIARCSPTEIDDRNILQAALEAMRRAASGCRPPPDFVLVDGNQWDRNLVDAPWPHETVVKGDAKSQSIAAASILAKTERDALMRDLHEAHPEYDWASNVGYPTQQHYDALREHGATPHHRQSFTLFRD | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
A4X4I2 | MLTPPRTVVRRDGGLYALERALQRRGFRQVAGADEAGRGACAGPLVAAAAILPPGRRGEVDGLADSKLLTPASRERVYAEVIARASAYAVVVIPAAEVDLRGLHVCNLAAMRRALASLATPPEYVLTDGFGVDGLDVPGLAVWKGDRVAACVAAASVLAKVTRDRIMVELDLEFPGYGFAEHKGYITAEHSAALRERGPCPEHRFSYVNVATVSGRQGAPPRARRPLVAEADEAMERAGVVKGTVGVALGERPWAGASVGNDVAMEGGMG | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
A7IES2 | MAPRPKAPPQPAEPDPALPRPRGRPPKAGAVTAGWVGLDFTRERALYADGRAPVAGADEVGRGPLAGPVVAAAVVLDPARVPQGLDDSKKLTRAKRESLYLEICATAEVAIALAPPERIDRDNIRQATLWALANAVRGLPCRPAFLLVDGNDPPRVDCEVEAIVGGDGLVASIAAASIVAKVVRDRLMAGVGAAFPAYGFERHMGYGTREHGAALKAHGPCLHHRRSFAPVREQQLGLFPAPGELEEAD | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q9PEI7 | MVSQFDTQHLPSSNTALVAGVDEAGRGPLAGPVVVAAVVFDPSQPRINGLNDSKQLSPACRERLYAHIVERALAYKVVMIDSTQIDTLNIYQATMLGMRLAVEGVAHVAKSARIDGNRLPKNLPCPAEALVGGDARDRTIMAASILAKVTRDRHMVELHLQYPHYGFDKHKGYGTPAHLAALAEHGPCLEHRRSFAPVRKMLTLEAIHARQSTHQHNENSPTKAAFNMLLERDD | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q5NNT2 | MVAGSPKTSKKTLPDLSYEDRIEGVVFGVDEVGRGPLAGPVMAGAVYLHREHIPEGINDSKKLTARRRHLLSDMLHNQADYATGMADVHEIDRINIRQASLLAMKRAVEALIQKIGREPDCILVDGRDIPDWPWPSLPIIKGDSLSLSIAAASIVAKVERDEIMVKASQEYPGYGWEHNMGYPTKEHREAIQRLKPTKFHRRSFSPIRQFYENVD | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
O67644 | MPSLKISPSEAEKIQNYLVSSGFRKINAPYTLWALEGNGVKVYYYKTGSLLIQGKNSEKVLKEVLNLLEKKKLPGCDESGKGDIFGSLVLCCVCIPEENYLKVSSLNPRDTKRLSDKRVERLYLALKPLVKAYCYEIKPEEYNKLYRKFRNLNKMMTHFYKLLIERVKEECGVSEVVVDKYQPSNPFGEDVIFETEAERNLAVAVASIFARYKFLQSLKEVERELGIKIPKGTSKEVKELAKSLKNPERFIKLNFNV | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q72E89 | MSQFDVTVFTDGSCLGNPGPGGWAAIMRCNGCEKELSGGFALTTNNRMEILAVLEALEALRDPCKVTLFTDSQYVRNAVEKKWLAGWQRNGWKTADKKPVKNRDLWERLVPLLAKHSVSFRWVRGHSGHPENERCDVLARAQASRRGLPEDPGFTA | 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): 17414
Sequence Length: 156
Subcel... |
B0R664 | MTTITPESLPRHELLGLHARVAADTDQSRVGIAGRVVDETMQTVVLRTASGVAQVPKKGATFEFRLTDEAAAPDNGVGTAFKPAGGETRQTTGESVAYVTVDGGRLLSRPERRSENGVDSKWR | 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): 13135
Sequence Length: 123
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
A2BMC7 | MKRTAWNIVFHSLIGLRARVLATSDPGLRGLEGVVVEETRHSLVVETRDGRRVRVLKANSIFLFQLPGGSWVVVRGEEIAGSLAERVKRLGRLKGVGWLVRAGEKRRYTRG | 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): 12432
Sequence Length: 111
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
A8AA22 | MKHTPKNVIYHNLVGLRVEVLAHPDPSMKGLKGRIIDESKSFLTIEKDNGELVKVQKLGTFVLVLPSGRKVEVRGELLRGRPEERLKKFLKA | 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): 10427
Sequence Length: 92
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
A6UWU6 | MITPYNILRHELIGLDVEITQSTNKSLVGLKGKIVYETRNTINIERFDNSKEVMIPKDIAVFKFKLNEEYIEVIGELLMGRPEDRLKRKIKNIYPY | 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): 11299
Sequence Length: 96
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
Q12ZU3 | MEALPSNLIFHELIGLYAEVFESTNPKLINICGRVIDETRNMLIIETEDTHEKMVPKNGTTFVFHLPSSSADHDQRVKIFGTLLLSQPENRVKNIRKIRMR | 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): 11649
Sequence Length: 101
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
Q57903 | MITPHNILRHELIGLKVEIVEAKNKAMIGIKGKVVDETRNTLVIEKEDGREVVIPKDIAVFLFQLKGCKVKVDGRLLIGRPEERLKKKIKILYPY | 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): 10888
Sequence Length: 95
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
Q8TGY6 | MPITPRNIVRHELIGLECRVVKSLGPPYEGLEGRIVDETKNTLVLKTESGEKVIVKDQVLLELKLPSGERVRVDGALLVGRPEERLSKRIKYAEVVRGRFDPEDYLD | 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): 12135
Sequence Length: 107
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
P60832 | MSQNILRHELIGLNLEVVKSTDSGLISTKGRVINETRNTLVLEKENGKEITLVKEISTFRIQFESENVVKIDIDGRLLVGRPEDRLKRKIKQLYSY | 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): 11069
Sequence Length: 96
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
A5UL80 | MITVNNLVHHEFIGLSVSVTSVSNESLRLKGTVIDETKNTIKIEVDDNVEKIIPKKGSIFVFELPTGEKVEINGNILSIRPEDRIKKRFKKI | 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): 10402
Sequence Length: 92
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
O26119 | MITPRNIFRHELIGLSVRIARSVHRDIQGISGRVVDETRNTLRIEMDDGREITVPKGIAVFHFRTPQGELVEIDGRALVARPEERIKKKFRKP | 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): 10740
Sequence Length: 93
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
A9A5I7 | MITADNITSHEFIGLNTEIVQSTNPQVIGLNGRIENETKSMFTINTENGMKSIAKSTSNWKFSIDSNDVIVEGSRIAKRPFDRIGGKA | 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): 9687
Sequence Length: 88
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
Q6KZ41 | MNIALKRINYLINISRVSDNPERCIDLMEKISKRMDITLNHDIKLQYCKVCKMPYRNPVIRLKNGFVLIHCDHCGNTRRIKIRDHSVSSSK | Cofactor: Binds 1 zinc ion per subunit.
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): 10727
Sequence Length: 91
Subcellular Loc... |
Q8U0H6 | MAKYNEKKEKKRIAKERIDILFSLAERVFPYSPELAKRYVELALLVQQKAKVKIPRKWKRRYCKKCHAFLVPGINARVRLRQKRMPHIVVKCLECGHIMRYPYIKEIKKRRKEKMEY | Cofactor: Binds 1 zinc ion per subunit.
Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. The RNA is catalytic, but its KM for pre-tRNA is 170-fold decreased in the presence of the 4 known protein subunits (Rnp1-4). The protein subunits also decrease the... |
O59248 | MVDIVKRRDWEKKEKKKIAIERIDTLFTLAERVARYSPDLAKRYVELALEIQKKAKVKIPRKWKRRYCKRCHTFLIPGVNARVRLRTKRMPHVVITCLECGYIMRYPYLREVKQKRKKAT | Cofactor: Binds 1 zinc ion per subunit.
Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Binds RNase P RNA.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14589
Sequence Length:... |
Q97WJ1 | MRRKNQIKKRIIELIELAYNTAKSGNLELAREYVKLAEMYSRKGKVEIPLKYKRMFCRKCYTPLIIGVTERRRMRSKILIRTCLICNWQRRYVLSGNKRSDKENES | Cofactor: Binds 1 zinc ion per subunit.
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): 12788
Sequence Length: 106
Subcellular Lo... |
Q9HLQ1 | MLITKKDVEYTARKRIEKLYDFAIRTGDRRYIIEMEHIAQRMDITLPANIKRGYCKKCKTPYRNQVVRIKKNLVTVKCPVCDDIRRFQISR | Cofactor: Binds 1 zinc ion per subunit.
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): 10965
Sequence Length: 91
Subcellular Loc... |
A9NE63 | MKRVYSIKSKNELDLVFKEKKSVGNGYFVIYFIPHETPHFKYAISIGKKFGNAVERNQAKRRLRYIVSNYSNYINPKYRFVIVVRPQSNLLPYDLIKENITKLLIKAKLIEKEAQN | 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... |
Q6F6K8 | MMTLYSFSTEVRLRCAADYQGVFDGALFKVHQPHFLFLAKPSEQLQSRLGVIVAKKKVRRAHERNRIKRLARESFRLHQQQLGLLDIVVMPKIGIEAVSNADLHQQLEFAWQKLQRQAKKYQKVAVSPSLH | 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... |
Q82YV0 | MKKSYRVKKEKEFQQVFNKKQSCANRRFVVYVLEKPQQAHFRVGISVGKKIGNAVTRNAVKRKIRASLFQLKDRISPEIDFIVIARPGLEKLSSEEVKANLTHVLNLAKILDVREGIE | 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... |
Q2N7X0 | MTDKPAVIRKRADFLAANRGLRVARPGFVLLAHPNQGQGQRYGITVTKKIGNAVVRNRMKRRFRELLWELLPQQGLADHDHILIGREGGIERDFGKLREELMLALRRAREGKGDPRRRRRR | 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... |
C4KZZ5 | MKKEYRLQKNEEFQAVFREGRSVANRQFVVYTLKADQTHFRVGLSVSKKLGNAVERNRMKRLMRESLRLLEPNVAPNDYVIIARKPATALTQSEVTESLKHVFKRAKVWQKQGR | 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... |
B0S3V6 | MDKSVRLRDNREYNVVYKRGKTYYNRNFSLVVYNSKKGTRIGFSVTKKYGNAVERNRIKRKLREIVRLNFSEFDKGLDMVIIPKKNTEDLTYKQLESALLHVCRKASNKKCQK | 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... |
A8L8W2 | MLPRGSRVRTRQEHALVGRSGRRVRAGSIVVHSVQTDVDGPPRAGFVVGRRVGNAVVRNRVRRRLREQTRSRLSSLPPGTAVLIRALPDAAGSSSADLGRSLDSAFRTVRSPRPQRSARSG | 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... |
Q8RHA6 | MNTLKKNGEFQNIYNLGNKYFGNYSLIFFNKNKLEYSRFGFIASKKVGKAFCRNRIKRLFREYIRLNINKINDNYDIIIVAKKKFGENIEDLKYKDIEKDLNRVFKNSKII | 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... |
A4XDK4 | MLTAAQRLRRSTDFAAAVRGGRRVGRGVVVVHLTLPGTLPDVSSSKPARDTGAEQTSAPARAGFVVSKAVGNAVVRNAVRRRLRHLVRERLPGLPAGSTLVVRALPTAAHRSYQRLGVDLDAAIAAARAPRGRRSR | 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... |
Q8EKT4 | MTSYTFTRELRLLTPAQFKSVFSNPIKASSAEITLLAIPNSEQHPRLGLTVAKRYVKRANQRNRIKRVIRDSFRLNQHNIPHLDIVVLVRNGVMEMENAELNKLIEKLWRKLSRRYNG | 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... |
A3MML4 | MTNSSLRPSGRRADQLRDVRITRHYTKHAEGAVLVEFGDTKVICTASVAERVPEFLRERGQGWLTAEYGMLPRATHTRSDREAARGKQTGRTQEIQRLIGRALRAVFDLNALGPRTLHLDCDVIQADGGTRTASITGAFVAAHDAVTKLVAAGRIARSPITDYVAAISVGVFGGTPVLDLDYDEDSACDTDMNVVMTGAGGFVEVQGTAEGAPFSRTEMNALLDLAQAGIGELVRLQRAALEA | 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. ... |
C0QTN9 | MRPDGRKPTQLRPVKIIRDFNIYAEGSVLIEMGNTKVIITASIEEKVPPFLRGTGQGWITAEYAMLPRSTESRSIREVVRGAPSGRTQEIQRLIGRSLRGVVDLKKLGERTLWVDCDVIQADGGTRVASITGAFIAVADAMIKLTESGKVRQNPLKDYVAAISTGIVGNEVVLDLNFKEDSSAKVDMNLVMTGSGNFVEVQATGEEYSFTQQEFDKMLEYGKLGINKLIHIQKKFIEGMPSIGHWKRLSIKEFSYTDTGGN | 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. ... |
B4RC87 | MRPSDRRPDLLRPVTLETGVNRYAEGSCLASFGHTKVLVTASLEEGVPPFLRGKGQGWVTAEYGMLPRATHTRGRREAAQGKQSGRTQEIQRLIGRSLRAVVDLKALGERQITVDCDVVQADGGTRTAAITGAWVALRLATRYLLEEGVIATDPILDQVAAISCGVFSGTPVLDLDYEEDSNAEADANFVLTGAGDIVEIQATGEKRGFSEAEFEALFALARKGIGELCELQRAATGG | 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. ... |
Q6AYK1 | MDLSGVKKKSLLGVKENNKKSSTRAPSPTKRKDRSDEKSKDRSKDKGTTKESSEKDRGRDKTRKRRSASSGSSSTRSRSSSTSSSGSSTSTGSSSGSSSSSASSRSGSSSTSRSSSSSSSSGSPSPSRRRHDNRRRSRSKSKPPKRDEKERKRRSPSPKPTKVHIGRLTRNVTKDHIMEIFSTYGKIKMIDMPVERMHPHLSKGYAYVEFENPDEAEKALKHMDGGQIDGQEITATAVLAPWPRPPPRRFSPPRRMLPPPPMWRRSPPRMRRRSRSPRRRSPVRRRSRSPGRRRHRSRSSSNSSR | Function: Part of pre- and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors... |
P25367 | MDTDKLISEAESHFSQGNHAEAVAKLTSAAQSNPNDEQMSTIESLIQKIAGYVMDNRSGGSDASQDRAAGGGSSFMNTLMADSKGSSQTQLGKLALLATVMTHSSNKGSSNRGFDVGTVMSMLSGSGGGSQSMGASGLAALASQFFKSGNNSQGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQG... | Function: Transferable epigenetic modifier which forms a prion responsible for the non-Mendelian trait [PIN+]. The native function of the soluble protein is unknown.
Sequence Mass (Da): 42580
Sequence Length: 405
Domain: The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble... |
Q6NQJ6 | MMSVRAINGCSIIRTATSAGGPPVSLFRHRIQRLRASHLREFSKLRLNFPLIRADRRFLGNSDAPSCSTCIHSLVESVSEELESISRRKGSRMRVRASVKVKLTSYGEVLEDKLVNQELEAGLLLEFKKDADRVLLAVLHRRDGKKNWMVFDQNGVSCSIKPQQITYIVPNVYNFDHTGLTDFLQRAQDNLDPQLLEFAWMELLEKNKPVTPEELAEMIYGRADPLESYCAHFLLSQDEIYFSILESKGSRSIYSPRPTEQVEELLRRQRVKEAEDKEFQEFIQLLKSAKKAPSHAKPPKSSWLADDKVQDRIGSLEAYA... | Function: 3'-5' exoribonuclease that catalyzes 3' maturation of chloroplast and mitochondrion ribosomal RNAs; degrades short nucleotidic extensions to generate the mature 3'-ends. Involved in the maturation of 23S, 16S and 5S rRNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleos... |
Q9CH00 | MSIREVIMDYLENSSKKALSVEELSVALHMNKAKDYKVFVKTLASLEAEHLLNFTAKGKVELAEKEEAKVVISGIFRANAAGFGFVSIDAEEPDVFVARGQTAFALDGDEVFIEIDKNANALKGTSAEGHVVEIIRHDVHQVVGTFVALNDDEKEQTGLIGFVKSRNKKIPYRVYLENEGLIPENKAIVRVEITHYPDKEFPQTMQGLVTEIIGQADDQGIDVLEVLASMDIVSEFPKEVLDQAEAVPEEVPENEIVGRVDYRNEITFTIDGADAKDLDDAVHAKRLENGNYELGVHIADVSHYVTENSPLDKEAYERGT... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 92250
Sequence Length: 817
Subcellular Location: Cytoplasm
EC: 3.1.13... |
Q02146 | MVQLSELASALNQTESKGVFSKHPKGFGFVHPEDATDKTNDIYIGKNDTKFAMDGDKVTVKVTYPKTEKRGASGQITKINERAVVDTVGTYRSLSNRQVKALGYKGRIELYNDRISDTLYIKQPLSGVQEEDVVSLKITQYPTNTKTFEGKITGIIGHKGEVGLDILEVLCAMKIPQEFSSETLAEAEAFSEKLTDSDLQDREDYRNEITYTIDGDDSKDLDDAIHVKKLSNWHFELGVHIADVSHYVTEGSSLDEEAYSRATSVYVTDRVVPMLPVKLSNNLCSLNEAQERLTMSCLMEIDDKGKIVSYKISPSVIKTT... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 75274
Sequence Length: 665
Subcellular Location: Cytoplasm
EC: 3.1.13... |
P08056 | MKAVLALATLIGSTLASSCSSTALSCSNSANSDTCCSPEYGLVVLNMQWAPGYGPDNAFTLHGLWPDKCSGAYAPSGGCDSNRASSSIASVIKSKDSSLYNSMLTYWPSNQGNNNVFWSHEWSKHGTCVSTYDPDCYDNYEEGEDIVDYFQKAMDLRSQYNVYKAFSSNGITPGGTYTATEMQSAIESYFGAKAKIDCSSGTLSDVALYFYVRGRDTYVITDALSTGSCSGDVEYPTK | Function: This is a base non-specific ribonuclease.
Catalytic Activity: a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)
Sequence Mass (Da): 25635
Sequence Length: 238
EC: 4.6.1.19
|
P54084 | MPETQEPASLNERDPMFEREKEKYERPIVSREYILSYLEGTGRPLTLEDIIAELEVAEDDQEALRRRLRAMERDGQLVRNRRGAYGIVAAMELVRGTVSAHPDGFGFLIPEAGGKDLFLSPREMRKVFHGDTILGRAVGEDRRGRIEGAVVRILERALKHIVGRYYADNGVHYVVPEDRRIPQEFAVVEGEGEGLTPVHGQIVILEITQYPDGRNMPQGHVVEILGEHMAPGMEVEIAVRNYGLPHQWPDEVLAEIKQFSETVPETMKAGRRDLRDLPLVTIDGADAKDFDDAVYAEVIENGFRLTVAIADVATYVCPDS... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 49332
Sequence Length: 439
Subcellular Location: Cytoplasm
EC: 3.1.13... |
O67834 | MDKEKLEKEVIKLLSKKKKPLHFLQIAKALGLGKKERKTLKKVMRKLKKEGKVKVVKGKYEYTGEEVVTGTVIAYPGGFGFLEVEGGKDIYIPPFEMVKVFHGDVVKAKVTEFKGKKEVRIIKVLKRAKKDIVAKVVFEDEQCYVVPLDENAHHRILLSKKDCQKLKEGEVVVLKITQFPTKKSPARGKVIEVLGNPKEKFIAIDVIIRKYNLPTSYPEKVIKEVEAIPEEIPEEEIKRRRDLREQLCFTIDPEKAGDFDDAVAIELTPEGYYKLYVHIADVSYYVREGTETDKEAYKRGFTYYFPDRALHMLPEKLSAK... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 81538
Sequence Length: 705
Subcellular Location: Cytoplasm
EC: 3.1.13... |
O32231 | MEKEAFMEKLLSFMKEEAYKPLTVQELEEMLNITEAEEFKELVKALVALEEKGLIVRTRSDRYGIPEKMNLIKGKISAHAKGFAFLLPEDTSLSDVFIPPNELNTAMNGDIVMVRLNSQSSGSRQEGTVIRILERAIQRVVGTYTETRNFGFVIPDDKKITSDIFIPKNGKNGAAEGHKVVVKLTSYPEGRMNAEGEVETILGHKNDPGIDILSVIHKHGLPGEFPADAMEQASSTPDTIDEKDLKDRRDLRDQVIVTIDGADAKDLDDAVTVTKLDDGSYKLGVHIADVSHYVTENSPIDKEALERGTSVYLVDRVIPM... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs (By similarity). Involved in degradation of type I toxin-antitoxin system bsrG/SR4 RNAs .
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
... |
P57628 | MVVDPYQKREAKRYKNPIPSREYISSCLRTSQDLISQKNLEKKFGINNQESKKALRRRLRAMERDGQVIYTSNRCYVAPESLKIVKGKVIGHRDGYGFLRTETLKEDLWLSSEQMKSCIHGDIILAHIVETHGKRRSSARFLKLLQPNNILIVGRYYIDDKIKFVIPDDTRFNFKIFIFSAIKDDISIGSIVSVKLKQHPIRNSRVQGFIVEILGKEMGTNLAIEIALRTHLIPSLWSKEVKKQVYEISRKINQYDFKNRTDLRHFPFFTIDDEDARDFDDAVFCKRKANPEEGWILWVAIADVSCYVQPNTPLDKAALE... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 84807
Sequence Length: 731
Subcellular Location: Cytoplasm
EC: 3.1.13... |
O84402 | MGKAKNKKKFLKNRKQVLVPGTLFVHSRKGFGFVSPDQPELYPFDIFISASDLKGALDGDHVLVALPFSLRGGEKRKGVIHKVLSRGKTVLVGTIVSLINPTLAMVYVNTIGPEHPLKAELLPKRTYKLGDRLLLKTPVWKENYPSREPPPLAMLEFIGNISNAKTDFPVIKAEFSITEEFPDAVVQEASQFLQKHVTQALHSRKDLRDLLCFTIDSSSAKDFDDAVSLTYDHEGNYILGVHIADVSHYVTPNSALDREAAKRCNSIYFPGKVIPMLPSALSDNLCSLKPNVDRLAVSVFMTFSKEGFLSDYRILRSVIR... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 78065
Sequence Length: 694
Subcellular Location: Cytoplasm
EC: 3.1.13... |
P21499 | MSQDPFQEREAEKYANPIPSREFILEHLTKREKPASRDELAVELHIEGEEQLEGLRRRLRAMERDGQLVFTRRQCYALPERLDLVKGTVIGHRDGYGFLRVEGRKDDLYLSSEQMKTCIHGDQVLAQPLGADRKGRREARIVRVLVPKTSQIVGRYFTEAGVGFVVPDDSRLSFDILIPPDQIMGARMGFVVVVELTQRPTRRTKAVGKIVEVLGDNMGTGMAVDIALRTHEIPYIWPQAVEQQVAGLKEEVPEEAKAGRVDLRDLPLVTIDGEDARDFDDAVYCEKKRGGGWRLWVAIADVSYYVRPSTPLDREARNRG... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs (rRNAs, tRNAs and SsrA/tmRNA). In stationary phase, involved in the post-transcriptional regulation of ompA mRNA stability. Shortens RNA processively to di- and trinucleotides. In vitro, exhibits ... |
Q5AK94 | MLSILSIAALLIATVQAADFSSSCPIDSPISCSSNGDTSNSCCYENPGGIILFTQFWDYNPASGPADSFTIHSIWNDYCSGGYPQFCDTSLEIDSTGSTIESIVVDQFGDQTLYDNMNKYWTDINGNNKKFWAHEFNKHGTCLNTLNPSCYSNYKQNENVYDYYSLVYQLFQKLPTYQWLVSAGIKPSTTATYTLSQIQSALKSKFGAEVYIACDSNNAINEVWYFYNIKGSILQQNYLPIDTVSKTNCPSSGIKFPPKGNSGANTLTTKTTGTTTSGSGSTSVPATSYINLTGKSGCLISNGKYYTSGTCATYHFNAGS... | Function: Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high ... |
Q75BW5 | MAKTASAMLFLYLLLSRCLLSHAFQEFITKFPMPMMYNFPSCSSTIPSTCRNETAIADTCCFEYPGGLILHSQFWNAPYRKRSYRDFGPDDSFTIHGLWNDRCDGSWDQFCRRGSSIRSVVDILSKDSLNRGGLPITGKALLRQMSMYWKGDRGDENLWVHEYNKHGLCLNTLRPECYQRWGSVASAEDQAIYDYFRIAMNLHLKIDAYHALSRQGIKPRCDAPYDAVRMQNALADDFGREVQMQCTGNRLTGVTYYYLLRGGILSENFQPVDPTQSSSCRGKIYWIPKSGC | Function: Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high ... |
Q4WXZ5 | MLQSIPGPQHILKALTGSLGLSTIFEPDHEASQNSFQCSKPELSCHAQYHGQDTCCFNYPGGQMLQTQFWDADPAVGPVDSWTIHGLWPDFCDGGFDQYCDSKRRYSNISLILVDSGRADLLEYMSDFWKDFRGDDEDLWEHEWNKHGTCISTLETTCYADYYPQQEVVDYFNKTVEIFQKLPTYQTLANAGIVPSHTETYTLDEIQAALAKAHAAPVTIRCRNRALNEVWYHFNIAGSLQTGTFVPSEPDGLKTNCPATGIHYIPKKHREPSRTTDTPSQPTTTGTPFKGRGNLIVSSMGGRRGCIISRGKWFASGTCA... | Function: Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high ... |
Q6MNQ3 | MEIVISAIIGLLIGGTVVFVIKRLQDNNKKKSARFEAERIVNKANSEAAKIKKESENKAKDFESRARKNVEQDIHKQKSTLKNKESQLERRLKEVEDQFKQKMEENERYLNSLKDREEKIAISENRIKDLEKKGEAHIGELKQKLESVAAMSQDEARRQLLTALEDEAKQEAAKKIAQIEEEANKESEKKAKRILATALSRFASEYTSERTVSVLALPNDEMKGKIIGREGRNIRTLEAHCGVDLIVDDTPEAVVISGFDPVRRELARRTIEKLMEDGRVHPARIEEVAEKQRNELMKSMKEEGERHVMELGIPNMHPEL... | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58704
Sequence Length: 521
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q6FP42 | MILASVLKAFQGLQTGLQHSYQDGSPSCPINLPLSCGNETAISDLCCFEYPGGILLMTQFWNYAPSKPNLNRTELEEELGPVDSFTIHGLWPDDCMGGYPQFCKRDLFIDDVDYLLKSDAFNNDDTLPIQGEELLNNLNKYWKSNNGNHESLWIHEYNKHGTCLSTLQPQCYSRWNPTTSQKGPKYYKKKAVYDYFRISYDLFQKLNTYEMLAKHNITPSNDTSYTKSEILSALSSEFQGTQAHINCNSQNALTEVWYYHQLNGSILNEDFIPLDPLRSMSRCKDQGIKYYPKGYQRRDNRGPNKKPISRGTIRISQYGG... | Function: Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high ... |
Q6BHB1 | MLALILTISICIFLKGSTCSYINLGSEGIVFGAPNCPVDIPLTCTNSTPIDNSCCFESPGGILLSTQFWDYYPPIGGNESFTLHGLWPDNCDGTYEQFCDDSLNIRSATDIVLNQFGDKVLYGKMSEFWKNFNGNDESLWIHEFNKHATCVKTIRPTCYDNQRYVKNKNVYDFYNITMNLYEKLPTFQFLAAEGIVPSLTQKYSKKQINDALTKYFGKAVYFKCNKYKALQEVWYYHYLQGSLKEENFSPIDTIINSNCPEENIQFIPKNGFNPGPQPPKSPRKGYLESPGKKGCLISNGLWYEAGTCATYAISQQEFGG... | Function: Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high ... |
Q5B3K6 | MSSISGFLGAIPGAQQILQTMAGSLGLAPLSHPEIASSGSTFQQCGKLELSCQTSYHGQDTCCFNYPGGQMLQTQFWDADPAVGPENSWTIHGLWPDHCNGGFDQFCDSHRKYSNISLILIDAGRRDLLDEMSTYWKDYRGDDPNLWEHEWNKHGTCVSTLETHCYSEYYPQQEVVDYFDKTVELFHDLPTYMTLANAGIVPSYTQTYTRHEVEDALSKAHGATVTVRCRSQRLQEVWYFFNVEGPLQTGKFVPSEPDGQTSNCPAKGIIYQPKTPNKDPGHGHEPTKTRHPHGPTGAPFIGKGNLVVSTMGQQRGCIIG... | Function: Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high ... |
Q03R31 | MSVPIVILAIIAIVVGVVGGYYLRKSVHERKLDAAKYTAAGVLAEAKKQAETATKEALLEAKEDSHKYRAEVETELKERRAEVQKQEDRLIQREETLDRKDNSLEKRENSLNRRDKKLSAEEQNLVKKQQQADSLIEKRQAAVEAVAALSQDDARELIISEAKTALASERAKMIKESEETARKTAQANAKDLIVSAIQRSAADMVTETTITVVTLPNDDMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVVLSGFDPLRREVAKIALEKLIQDGRIHPARIEEMVAKAKKELDEHVRELGEQATFDLGIHSMHPELVK... | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57405
Sequence Length: 519
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q03EQ6 | MIILYIILAIIAIVVGYCAGFFMHKRLIEKQTANASNSADVIVENARKQAETERREKLLEAKDESHRYRAKVEKELKERRAELQKQEDRLLQREDSLDRKDNSFEKRENSLERKEQKLALDQKHIDEQQQKASSLVEERQQELERVSNLTQEDAKNLIISETEAKLEKERALIIKEGLEDAEAEADQTARKLIAEAIQRSAADMASETTITVVSLPNDDMKGRIIGREGRNIRNFQNVTGVDLIIDDTPEAVVLSSFDPIRREIARIALDKLIQDGRIHPARIEEMVEKAKKEMDDNIRKTGEQAVFDLGIHSMNPELIK... | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58362
Sequence Length: 519
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q6CAV7 | MQFSLATIATVAAAVSALVCPYTKRDAVAAFTSPPLSSADHKSCPADTPVSCSSGAGSADLCCTESPGGVLVLTQFWDWTPAIGPDDLFTLHGLWPDNCDGSYAQFCDKSMEVQSVAAVLQQLGETELLDKMNKIWIPNRGSTDSFWTHEWNKHATCMSTLKDKCYSSDAPQYQSLADWAHTVVNVFETVNTYKFLEAAGITPDSSKTYAKTDFLNALNSNFDGKQVHISCKSGYISEVWYYFHLKGSVVSGQYLPIDDIGSSSCPDQIKFPPKDGSGGTPPPTDPSDPPTGGSKGFINISGQSGCLISNGNWYTSGTCA... | Function: Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high ... |
Q02933 | MLLKNLHSLLQLPIFSNGADKGIEPNCPINIPLSCSNKTDIDNSCCFEYPGGIFLQTQFWNYFPSKNDLNETELVKELGPLDSFTIHGLWPDNCHGGYQQFCNRSLQIDDVYYLLHDKKFNNNDTSLQISGEKLLEYLDLYWKSNNGNHESLWIHEFNKHGTCISTIRPECYTEWGANSVDRKRAVYDYFRITYNLFKKLDTFSTLEKNNIVPSVDNSYSLEQIEAALSKEFEGKKVFIGCDRHNSLNEVWYYNHLKGSLLSEMFVPMDSLAIRTNCKKDGIKFFPKGYVPTFRRRPNKGARYRGVVRLSNINNGDQMQG... | Function: Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high ... |
Q6ML54 | MIAMIATAIIGIVAGGGLGWALHKFFRARTLRLAREEAQDILDEANEVVELRNLEERERIQEIEMELWTKVEPEMLKSEGRIEDLQEVANERKAKADAIVQEEKKKLQDREADVKVQEQALRGQEAELGKLKEAQKALNQELVQKLTERLGTSAEEFKTQLKNQMEEESRRRAARMIQETEADTKEHAESEAKRILSLVIDRFARPYCAERGIGAVNFPDAHIRKLFCDPAGNNIKAVQDACGCDIIVEEGMEMVGVAGFDPVRRELTRRTLERIFKEKKNINPDFIRKIAENQKKELFKNIKHDGDSLAKELKLEGLNA... | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59273
Sequence Length: 527
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q03NQ6 | MLITGLIIGCLLIGLVIGYVVRQHQHRQELLAVQKQARDIIASATAETQQKIAKLTADSRRETLTYQQSVKDELAEQTSDIAVREQRRQQREQLLGQMGVRLADQTAILDERSQANRDQRQKIRDLKAQALQLRTDRDEMLAQQAGIDEQAAKDHVLADTELDLKRDRDVEIKALNDNAVANAERWAKDVVLSATESGPQDLPKEHLEHTVTVPNGEIRSKIIGRDGQHIRLLETLTGTDLIFVPDDNTTLFISTHDPIRREVARVALTNLVASRRISSNQIETQVENAQRDVNHSLWETGEQTVSGLHVGWMHPDLMKL... | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59402
Sequence Length: 535
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q03E93 | MATILIVVLLLASIGVGYGLRAKKHSETLAQARKAAEKIIEHERQKTKAEVAEYEKNSVQETQQYQETIDQELADDLHDNQRKEAWIEQRMNLLNQKKIVLTNRADALAKKRQSLLQERDNVRTTLGEAKQLITDRWNKLQEVADLEEQAASKLVLKETKQDAIRSKDEFVNNAQTELESSCEREAEDLIALAMEHSDVPRGQAENHRSFIAENAEYLGKLIGNSGQNVRAIEALTGVDIVIDDQEKEVILNGYDPVRRAVAMETMEMIKTEKRVVPDTIERLVNKANKVIDQRIRQYGEDAVRELKLKYVAPDLIKFIG... | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58704
Sequence Length: 520
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
A0PTY0 | MIEITLLGTGSPIPDPDRAGPSTLVRAGGQVFLVDCGRGVLQRAAAVGVGAAGLSAVLLTHLHSDHIAELGDVLITSWVTNFAADPAPLQVIGPPGTAETVEAMLKAFGRDIGYRIAHHADLNAPPPIEVHEYTDGTVWDRDGVAIRVAPTDHRPVAPTIGFRVEFDGASAVLAGGTVPCPSLDELAAGAGALVHTVIRKDIITNFPQQRVKDICDYHSSVQEAAATAARAGVGTLVMTHYVPAIIAGQEDQWRALAATEFGGRIELGNDLHRVEVHAR | 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... |
Q1DEJ2 | MSLLRLTFLGTSAAQPTLHRNLSGLAVKAHSDLLLFDCGEGSQRQMVRYGTGFTVDAVFFTHFHADHYLGIIGFLRTLGMTGRSEPIHLYGPPSAKRLLHQAVHLGVESMSFPVEIHELKDGDVVPRKGYAVHAVGVDHRINALGYALVEDDRPGRFNLDVARSLGVPEGPSFGKLQRGEPVTLEDGRTVKPEDVLGAPRPGRRLVISGDTRPCPALVKAAKDADLLVHESTFSDDEQERAVETRHSTAREAARVAREAGARRLVLTHLSSRHDTDPSKLLTQAREEYQGPVEVAFDGFTVELPLRD | 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... |
Q74MH2 | MIYILGTGGNMPTKYRQTLSIFVNYMGKGILFDAGENTQRQMRLLNLSPTQIDYIFLTHIHGDHILGLPGILLSLSNQDYNRELTIFGPKGIKEVIEKIIDSFAININFPLKIKEIGETKIDFGPFYIESIYGIHQVPVLAYSFKEKDKIKINKEKLAKYNIRSNPKLAKLKEGKSVTINGITLDPKEFTYIQKGLKFTLITDTLFREQFIDFARDSDIIFHELAFLDKDKDKAIEHYHSTISDAFRIRDESNSKLLVFIHVSPRYQGSLFEIYQYLYNKKDWIIAEDLDYIEYKKGTIIYKRNDIVLYEYAIWRS | 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... |
A9A3X2 | MKLVFLGTSAAQPTENRGLSCICLEREGEVLMFDAGEAAQISYMKSGLGWNKKMKIFVTHLHGDHCVGILGLLQTMSMQNRTESLEIFGPSGIEEFIAANIKVLNFGLSFPILINTIKDEKIFEDEKFLIRTCKANHSIIAFSYLFEEKDKPGRFNVEKAKELGIPEGELWNKLQNGNEITVNEKIIKPEQVLGERRPGKKIGISGDTMPTKELEEFFEECDYLVFDSTFLEAEKQKAQDTCHSTAKQAATVAKNAKVKNLVLTHFSARYRDEVEHLREAKEIHDSVITAKDLLEIEIK | 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... |
Q5YQ00 | MSQRELVVLGTASQVPTRQRNHNGYLLRWGREGVLFDPGEGTQRQMAFAGVAATDITRIALTHFHGDHCLGLPGIVQRINLDRVAHPVDAYYPASGQEYFDRLCSASSFYRRVDLRTHPIAGPGPLDAPDAPFTIEAVALSHPVEAFGYRLTEPAGVRMLPDRLAALGIHGPRIGELQRAGSLLVDGRTVTVAEVSEPRPGQSFAFVMDTRLCPGVAELAAGVDMLVIEATFLDADAHLAEEYGHLTAGQAARVAADADVRTLVLTHFSQRYRTLDDHRAEAEKHFSGEVVVAEDLHRIPLPPRR | 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... |
Q8YLZ0 | MQITFLGTSSGVPTRARNVSSVALRLPQRAELWLFDCGEGTQHQILRSDLKVSQLSRIFITHLHGDHIFGLMGLLASCGLAGNVQRVDIYGPSGLNDYIQSASRYSHTHFSYPIKVHTVRPGVIYENDEFTVTCGLLHHRITAFGYRVAEKDRAGRFDIEKAKELQIPPGRIYGQLKRGETVTLEDGRVINGAELCGPTEIGRKMAYCTDTIYCDGAVELAQDADVLIHEATFAHQDSEMAFQRLHSTTTMAAQTALAAGVRRLLMTHFSPRYAPGNTIELKDLLQEARAIFPRTDMAYDFMTYEVPRRREPVFSSVSSS... | 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... |
Q8EQ58 | MELVFLGTGAGLPSKTRNVSAVALNMTQEINEVWLFDCGEATQHQILHTNLKPRKITKIFITHLHGDHIYGLPGFLSSRSFQSGENQPLCIYGPIGIKEFVESTLRLSQTNLTYPITIKEITEDGNLFETNEMMVETKKLQHGIDSYGYRIKEKDKPGELLVDKLKQIGIAPGPIYQQIKENEITTLDNGSIIYRNDVLGPAKKGKVISILGDTRYSIDHIPFIKFSDILVHESTFTQDKELLAFEYNHSTNVQAAKLAKEANINKLYLTHVSSRYQAEDIDSIIEEARKIFPSTWLANDFSVYEI | 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... |
Q8Z4P3 | MNTEATHDQNEAQTTGVRLRNAREQLGLSQQAVAERLCLKVSTVRDIEEDKAPSDLASTFLRGYIRSYARLVHVPEEELLPGLEKQAPLRAAKVAPMQSFSLGKRRKKRDGWLMSFTWLVLFVVVGLTGAWWWQNHKAQQEEITTMADQSTAELNADKDSGQSVPLDTSAATSQDTTPAQTAPAPATPVDSTAATQNTVVAPSQANVDTAATSAAPAATETPSALPTSQAGVAAPAADPNALVMNFTADCWLEVTDATGKKLFSGMQRKDGNLNLTGQAPYKLKIGAPAAVQIQYQGKPVDLSRFIRTNQVARLTLNAEP... | Function: Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34779
Sequence Length: 324
Domain: The helix-turn-helix (HTH) motif in the cytoplasmic domain of the N-terminus is involved... |
A1XQR6 | MPVAVGPYGQSQPSCFDRVKMGFVMGCAVGMAAGALFGPFSCLRIGMRGRELMGGIGKTMMQSGGTFGPFMAIGMGIRC | Function: Has antibacterial activity against a variety of bacteria including S.aureus, P.aeruginosa and M.tuberculosis. Acts by inducing bacterial membrane breakage (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8175
Sequence Length: 79
Subcellular Location: Mitochondrion inner mem... |
Q4V7T9 | MPVAVGPYGQSQPNCFDRVKMGFMMGFAVGMAAGALFGTFSCLRFGMRGRELMGGVGKTMMQSGGTFGTFMAIGMGIRC | Function: Has antibacterial activity against a variety of bacteria including S.aureus, P.aeruginosa and M.tuberculosis. Acts by inducing bacterial membrane breakage (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8306
Sequence Length: 79
Subcellular Location: Mitochondrion inner mem... |
A4QNF3 | MPVAVGPYGQSQPSCFDRVKMGFMMGFAVGMAAGALFGTFSCLRFGMRGRELMGGVGKTMMQSGGTFGTFMAIGMGIRC | Function: Has antibacterial activity against a variety of bacteria including S.aureus, P.aeruginosa and M.tuberculosis. Acts by inducing bacterial membrane breakage (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8279
Sequence Length: 79
Subcellular Location: Mitochondrion inner mem... |
B6VJS4 | MDLANGVISAELLHAQAHVWNHIFNFIKSMSLKCAIQLGIPDIIHNHGKPMTLPELVAKLPVHPKRSQCVYRLMRILVHSGFLAAQRVQQGKEEEGYVLTDASRLLLMDDSLSIRPLVLAMLDPILTKPWHYLSAWFQNDDPTPFHTAYERSFWDYAGHEPQLNNSFNEAMASDARLLTSVLLKEGQGVFAGLNSLVDVGGGTGKVAKAIANAFPHLNCTVLDLSHVVAGLQGSKNLNYFAGDMFEAIPPADAILLKWILHDWSNEECVKILKRCREAIPSKENGGKVIIIDMIMMKNQGDYKSTETQLFFDMTMMIFAP... | Function: Catalyzes the biosynthesis of pterostilbene from resveratrol. Pterostilbene has both antifungal and pharmacological properties. Also has activity toward resveratrol monomethyl ether (RME).
Catalytic Activity: 2 S-adenosyl-L-methionine + trans-resveratrol = 2 H(+) + pterostilbene + 2 S-adenosyl-L-homocysteine
... |
Q9F0J6 | MQATKIIDGFHLVGAIDWNSRDFHGYTLSPMGTTYNAYLVEDEKTTLFDTVKAEYKGELLCGIASVIDPKKIDYLVIQHLELDHAGALPALIEACQPEKIFTSSLGQKAMESHFHYKDWPVQVVKHGETLSLGKRTVTFYETRMLHWPDSMVSWFADEKVLISNDIFGQNIAASERFSDQIPVHTLERAMREYYANIVNPYAPQTLKAIETLVGAGVAPEFICPDHGVIFRGADQCTFAVQKYVEYAEQKPTNKVVIFYDSMWHSTEKMARVLAESFRDEGCTVKLMWCKACHHSQIMSEISDAGAVIVGSPTHNNGILP... | Cofactor: Binds 1 FMN per monomer.
Function: Catalyzes the four-electron reduction of one oxygen molecule to two water molecules.
Sequence Mass (Da): 44796
Sequence Length: 402
Pathway: Energy metabolism; electron transfer.
EC: 1.-.-.-
|
Q9HAT0 | MAQTDKPTCIPPELPKMLKEFAKAAIRVQPQDLIQWAADYFEALSRGETPPVRERSERVALCNRAELTPELLKILHSQVAGRLIIRAEELAQMWKVVNLPTDLFNSVMNVGRFTEEIEWLKFLALACSALGVTITKTLKIVCEVLSCDHNGGSPRIPFSTFQFLYTYIAKVDGEISASHVSRMLNYMEQEVIGPDGIITVNDFTQNPRVQLE | Function: Important for male fertility. With ROPN1L, involved in fibrous sheath integrity and sperm motility, plays a role in PKA-dependent signaling processes required for spermatozoa capacitation.
PTM: Sumoylated, sumoylation decreases upon spermatozoa capacitation conditions.
Sequence Mass (Da): 23893
Sequence Lengt... |
Q3T024 | MPLPDTMFCAQQIHIPPELTDILKQFTKAAIRTQPADVLQWSAGYFSALSRGDPLPVKDRIEMPMATQKTDTGLTQGLLKVLHKQCSHKEYVDLADLEQKWKNLCLPVEKFRALLQLDPCEDKIEWIKFLALGCSMLGGSLNTAMKHLCEILTTDPEGGPARIPFGTFSYVYRYLSGLDSDIPESDTEAYLSSLKENAAARKNGMIGLSDFFVLKRKI | Function: Functions as part of axonemal radial spoke complexes that play an important part in the motility of sperm and cilia. Important for male fertility. With ROPN1, involved in fibrous sheath integrity and sperm motility, plays a role in PKA-dependent signaling processes required for spermatozoa capacitation.
PTM: ... |
Q96C74 | MPLPDTMFCAQQIHIPPELPDILKQFTKAAIRTQPADVLRWSAGYFSALSRGDPLPVKDRMEMPTATQKTDTGLTQGLLKVLHKQCHHKRYVELTDLEQKWKNLCLPKEKFKALLQLDPCENKIKWINFLALGCSMLGGSLNTALKHLCEILTDDPEGGPARIPFKTFSYVYRYLARLDSDVSPLETESYLASLKENIDARKNGMIGLSDFFFPKRKLLESIENSEDVGH | Function: Functions as part of axonemal radial spoke complexes that play an important part in the motility of sperm and cilia. Important for male fertility. With ROPN1, involved in fibrous sheath integrity and sperm motility, plays a role in PKA-dependent signaling processes required for spermatozoa capacitation.
PTM: ... |
Q9EQ00 | MPLPDTMFCAQQIHIPPELPDILKQFTKAAIRTQPADVLQWSAGYFSALSRGDPLPVKDRIEMPVATQKTDTGLTQGLLKVLHKQCSHKQYVELADLEKKWKNLCLPVEKLRTILELDPCEDKIEWIKFLALGCSSLGRTLNTAMKNVCEILTSDPEGGPARIPFETFAYVYQYLSGLDPELPAVETENYLTSLRLMSESRKNGMIGLSDFFVGKKII | Function: Functions as part of axonemal radial spoke complexes that play an important part in the motility of sperm and cilia . Important for male fertility. With ROPN1, involved in fibrous sheath integrity and sperm motility, plays a role in PKA-dependent signaling processes required for spermatozoa capacitation.
PTM:... |
A9C3R9 | MVSRLEHPAGGYKKVFESCEELAEPIPAHVSGKIPAWLSGSLLRMGPGLFEIGDEPFNHLFDGQALIHKFDLKDGRVTYHRKFIRTDAYVRAMTEKRVVITELGTAAYPDPCKNIFSRFFTYFQGTEVTDNCSVNIYPIGEDFYACTETNFITKVNPDTLETIKKVDLCNYLSVNGLTAHPHIEADGTVYNIGNCFGKNMSLAYNIVKIPPLQEEKSDPLAMSKVLVQFPSSERFKPSYVHSFGMTENHFVFVETPVKINLLKFLTSWSIRGSNYMDCFESNDRMGTWFHLAAKNPGKYIDHKFRTSAFNIFHHINCFED... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Specifically generates 13-cis retinol, a stereoisomeric form of retinoic acid. Capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid (By similarity).
Catalytic Activity: an all-trans-retinyl ester + H2O = 13-cis-retinol + a fa... |
P32561 | MVYEATPFDPITVKPSDKRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHPRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVAR... | Function: Catalytic component of the RPD3 histone deacetylase (HDAC) complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression... |
P40117 | MHATELNTGHGSQRAIRLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVPNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPLFAKAGANIISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLGWLDHTLDQLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARIDRQVDAGGRPVWLEIDGGVKADNIAAIARAGADTFVAGSAVFGAPDADGGYSSILYRLREAATVT | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Mass (Da): 25501
Sequence Length: 241
Pathway: Carbohydrate degradation.
EC: 5.1.3.1
|
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