ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q5M7Z0 | MPLFLLSLPTPPSASGHERRQRPEAKTSGSEKKYLRAMQANRSQLHSPPGTGSSEDASTPQCVHTRLTGEGSCPHSGDVHIQINSIPKECAENASSRNIRSGVHSCAHGCVHSRLRGHSHSEARLTDDTAAESGDHGSSSFSEFRYLFKWLQKSLPYILILSVKLVMQHITGISLGIGLLTTFMYANKSIVNQVFLRERSSKIQCAWLLVFLAGSSVLLYYTFHSQSLYYSLIFLNPTLDHLSFWEVFWIVGITDFILKFFFMGLKCLILLVPSFIMPFKSKGYWYMLLEELCQYYRTFVPIPVWFRYLISYGEFGNVTRWSLGILLALLYLILKLLEFFGHLRTFRQVLRIFFTQPSYGVAASKRQCSDVDDICSICQAEFQKPILLICQHIFCEECMTLWFNREKTCPLCRTVISDHINKWKDGATSSHLQIY | 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.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49710
Sequence Length: 435
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
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Q6NTV1 | MKHRPVHERQSSTESKNLKETTQLIMQSSSDHTHHQLGSNDSPSACMSLPVPQLSAEGSCTVGDVTVDLSSQDSQHVARSNSRRVRPSTHGRSPSRHGHTHSHDASGPEDANDDSREQSNSISEVFHLYKWLEKSFPYILIFSAKLVVQHITGISVGIGLLTTFLYANKCIVNQVFLRDKCSKLQCLWVLVFLLFSSFLLYYTFSSQALYYSLVFMNPSLGPLHFFDALWVVGITDFIGKFFFMGLKCIILLVPSFVMSHKSKGYWYMALEELAQCYCTLVSTPVWFRYLIDYGNLDSGAEWHFGILLALLYLILKILIIFGQRKTSSDCLRLFLSQPNYGTTATKRQCSEADGMCAICQAEFTKPIALICQHVFCEECISSWFNKEKTCPLCRTLISNHSHKWKDGATSLQLRIF | 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.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47122
Sequence Length: 416
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
|
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): 27006
Sequence Length: 253
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 22561
Sequence Length: 212
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 23014
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 23180
Sequence Length: 212
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 23647
Sequence Length: 208
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 24037
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 22536
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 22516
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 22899
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 25052
Sequence Length: 223
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 24892
Sequence Length: 224
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 23082
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 23272
Sequence Length: 212
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 26506
Sequence Length: 230
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 24263
Sequence Length: 210
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 23181
Sequence Length: 212
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 21999
Sequence Length: 200
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 28273
Sequence Length: 270
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 26234
Sequence Length: 249
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 25633
Sequence Length: 234
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 24193
Sequence Length: 215
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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): 29539
Sequence Length: 257
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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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
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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 Location: Cytoplasm
EC: 3.1.26.5
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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 amount of Mg(2+) needed for activity.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14303
Sequence Length: 117
Subcellular Location: Cytoplasm
EC: 3.1.26.5
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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: 120
Subcellular Location: Cytoplasm
EC: 3.1.26.5
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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 Location: Cytoplasm
EC: 3.1.26.5
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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 Location: Cytoplasm
EC: 3.1.26.5
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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 the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13728
Sequence Length: 116
EC: 3.1.26.5
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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 the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 15193
Sequence Length: 131
EC: 3.1.26.5
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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 the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13592
Sequence Length: 118
EC: 3.1.26.5
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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 the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14041
Sequence Length: 121
EC: 3.1.26.5
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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 the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13375
Sequence Length: 114
EC: 3.1.26.5
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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 the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13442
Sequence Length: 113
EC: 3.1.26.5
|
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 the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13140
Sequence Length: 121
EC: 3.1.26.5
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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 the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13363
Sequence Length: 111
EC: 3.1.26.5
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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 the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 14428
Sequence Length: 136
EC: 3.1.26.5
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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 the ribozyme.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13827
Sequence Length: 118
EC: 3.1.26.5
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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. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Catalytic Activity: phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n)
Sequence Mass (Da): 26052
Sequence Length: 243
EC: 2.7.7.56
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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. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Catalytic Activity: phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n)
Sequence Mass (Da): 28871
Sequence Length: 261
EC: 2.7.7.56
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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. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Catalytic Activity: phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n)
Sequence Mass (Da): 25475
Sequence Length: 238
EC: 2.7.7.56
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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 that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Enhances the formation of the ATP-dependent A complex of the spliceosome. Involved in both constitutive splicing and, in association with SRP54 and TRA2B/SFRS10, in distinctive modulation of alternative splicing in a substrate-dependent manner. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Participates in mRNA 3'-end cleavage. Involved in UPF2-dependent nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Also mediates increase of mRNA abundance and translational efficiency. Binds spliced mRNA 20-25 nt upstream of exon-exon junctions (By similarity).
PTM: Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53). Ser-53 phosphorylation site is important for splicing and translation stimulation activity in vitro (By similarity).
Sequence Mass (Da): 34238
Sequence Length: 305
Domain: The RRM domain is required for the formation of the ASAP complex.
Subcellular Location: Nucleus
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P25367 | MDTDKLISEAESHFSQGNHAEAVAKLTSAAQSNPNDEQMSTIESLIQKIAGYVMDNRSGGSDASQDRAAGGGSSFMNTLMADSKGSSQTQLGKLALLATVMTHSSNKGSSNRGFDVGTVMSMLSGSGGGSQSMGASGLAALASQFFKSGNNSQGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQNRY | 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 form, and which forms a parallel in-register beta-sheet in its amyloid form.
Subcellular Location: Cytoplasm
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Q6NQJ6 | MMSVRAINGCSIIRTATSAGGPPVSLFRHRIQRLRASHLREFSKLRLNFPLIRADRRFLGNSDAPSCSTCIHSLVESVSEELESISRRKGSRMRVRASVKVKLTSYGEVLEDKLVNQELEAGLLLEFKKDADRVLLAVLHRRDGKKNWMVFDQNGVSCSIKPQQITYIVPNVYNFDHTGLTDFLQRAQDNLDPQLLEFAWMELLEKNKPVTPEELAEMIYGRADPLESYCAHFLLSQDEIYFSILESKGSRSIYSPRPTEQVEELLRRQRVKEAEDKEFQEFIQLLKSAKKAPSHAKPPKSSWLADDKVQDRIGSLEAYAIDAWASTDQQKLAGTILKSMGLQKTSVSALNLLIDIGYFPVHVNLELLKLNLPTHHSEAITEAAEALLSESSDIDAVRRIDLTHLKVYAIDVDEADELDDALSATRLQDGRIKIWIHVADPARYVTPGSKVDREARRRGTSVFLPTATYPMFPEKLAMEGMSLRQGENCNAVSVSVVLRSDGCITEYSVDNSIIRPTYMLTYESASELLHLNLEEEAELKLLSEAAFIRSQWRREQGAVDTTTLETRIKVVNPEDPEPLINLYVENQADLAMRLVFEMMILCGEVVATFGSQHNIPLPYRGQPQSNIDVSAFAHLPEGPVRSSSIVKVMRAAEMNFRCPVRHGVLGIPGYVQFTSPIRRYMDLTAHYQIKAFLRGGDNFPFSAGELEGIAASVNMQSKVVRKLSNTGLRYWVIEFLRRQEKGKKYTALVLRFVKDRIASLLLVEVGFQATAWVSEGKQVGDEIEVRVEEAHPRDDLILFKEVI | 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 nucleoside 5'-phosphates.
Sequence Mass (Da): 90679
Sequence Length: 803
Subcellular Location: Mitochondrion
EC: 3.1.13.1
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Q9CH00 | MSIREVIMDYLENSSKKALSVEELSVALHMNKAKDYKVFVKTLASLEAEHLLNFTAKGKVELAEKEEAKVVISGIFRANAAGFGFVSIDAEEPDVFVARGQTAFALDGDEVFIEIDKNANALKGTSAEGHVVEIIRHDVHQVVGTFVALNDDEKEQTGLIGFVKSRNKKIPYRVYLENEGLIPENKAIVRVEITHYPDKEFPQTMQGLVTEIIGQADDQGIDVLEVLASMDIVSEFPKEVLDQAEAVPEEVPENEIVGRVDYRNEITFTIDGADAKDLDDAVHAKRLENGNYELGVHIADVSHYVTENSPLDKEAYERGTSVYVTDRVVPMLPERLSNGICSLNPRINRLTQSCVMEISPEGRVINYQISQSIIKTTERMTYDAVNQMIAGDEAALENYAKIADSVKIMVELHHILEAMRKRRGAIDFDTVEAKIIVNEKGLPIEIRKRTRGIAERMIESFMLEANETVATHFEAHGLPFIYRIHEQPKADRLQRFIDFAATFGMQIEGTSNGIDQKVLQAFMKKIKGQPGEMVLSTMLLRSMQQARYSENNEGHFGLAAENYTHFTSPIRRYPDLLVHRLIREIGEGKTPANILQKWEDKIPEIAEHSSHRERRAVDAEREVEKMKKAEFMEEHVGEEYEGIIASVTRFGMFIELENTIEGLVHISTLKGDYFNYQERMLALIGERSGLTFKIGQPIKIKVVKADRMTGEIDFEYLPSELDLIDKAAKAKKKPDHKGRKKSNQSLKVKSVAPKSTDKSANKSKNGRRADEKFEFDKKKKKSAKKPFYSKAAKGKFTDKKDNGKKFTDGRKKPHKRG | 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: 3.1.13.1
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Q02146 | MVQLSELASALNQTESKGVFSKHPKGFGFVHPEDATDKTNDIYIGKNDTKFAMDGDKVTVKVTYPKTEKRGASGQITKINERAVVDTVGTYRSLSNRQVKALGYKGRIELYNDRISDTLYIKQPLSGVQEEDVVSLKITQYPTNTKTFEGKITGIIGHKGEVGLDILEVLCAMKIPQEFSSETLAEAEAFSEKLTDSDLQDREDYRNEITYTIDGDDSKDLDDAIHVKKLSNWHFELGVHIADVSHYVTEGSSLDEEAYSRATSVYVTDRVVPMLPVKLSNNLCSLNEAQERLTMSCLMEIDDKGKIVSYKISPSVIKTTYRMTYNNVNKMIHQGQEGHREALENFFKITDSIKVAVELHEILETMRKDRGMIEFDESEAKIILDEKGHPIEIVKRDRDTAERMIESFMLMANETVALDFQKKKLPSLYRVHDNPKEKSFAKLMEAAANAGFSLNSDSHQAINFFADEIKGTSSEKALTYQLRHTMSTAVYSEKNTKHFGLAATNYTHFTSPIRRYPDLIIHRLLHLYPSDHSNHTKDEWKERLPEIASHSSDMEHRAVVTERIIDAMKKAEYMSERIGEVYTGTITGLQKFGIFVALDNTVEGLIRVPNLHTGTTEELEFDEEASIFKGKKSETVYQIGQEIKIRVIAANKRKGTVDFEQIAPE | 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: 3.1.13.1
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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
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P54084 | MPETQEPASLNERDPMFEREKEKYERPIVSREYILSYLEGTGRPLTLEDIIAELEVAEDDQEALRRRLRAMERDGQLVRNRRGAYGIVAAMELVRGTVSAHPDGFGFLIPEAGGKDLFLSPREMRKVFHGDTILGRAVGEDRRGRIEGAVVRILERALKHIVGRYYADNGVHYVVPEDRRIPQEFAVVEGEGEGLTPVHGQIVILEITQYPDGRNMPQGHVVEILGEHMAPGMEVEIAVRNYGLPHQWPDEVLAEIKQFSETVPETMKAGRRDLRDLPLVTIDGADAKDFDDAVYAEVIENGFRLTVAIADVATYVCPDSALDREAVTRGNSVYFPRRVIPMLPEILSNGLCSLNPHVDRLCMFCEMEMDAAGRSTGFRFDRGIIGSQRRFTYDEVAAILAGDAELRAQDAAMVPHLEALHSLYESFAKARERRGTIEF | 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: 3.1.13.1
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O67834 | MDKEKLEKEVIKLLSKKKKPLHFLQIAKALGLGKKERKTLKKVMRKLKKEGKVKVVKGKYEYTGEEVVTGTVIAYPGGFGFLEVEGGKDIYIPPFEMVKVFHGDVVKAKVTEFKGKKEVRIIKVLKRAKKDIVAKVVFEDEQCYVVPLDENAHHRILLSKKDCQKLKEGEVVVLKITQFPTKKSPARGKVIEVLGNPKEKFIAIDVIIRKYNLPTSYPEKVIKEVEAIPEEIPEEEIKRRRDLREQLCFTIDPEKAGDFDDAVAIELTPEGYYKLYVHIADVSYYVREGTETDKEAYKRGFTYYFPDRALHMLPEKLSAKLCSLRPNEDKLAFTVEMVFDESGNLKAYDIYESVIRSKARLTYNEALALIVGDPALEKKFPNLVEPLRMMETLYRILSRKRWEMGSIDFDLPEAEVIVDEYGEPTAIYPYERHVAHRIIEHFMISANETVALHLEHAGYPCLYRVHEPPDEEKVENLLEILEGLGYKVKRPHEYTPKFFQKIIEDFEGRPEENLVRFLTLRAMARAKYSPHNVGHFGLALEHYAHFTSPIRRYPDIIVHRLLKKALRGEEIDYEKTLAYLEEAGNHLSKQERIADEAEMEAIDYLKARYMKGRIGEEFIGIITGVVAFGFFVELEENLVEGLVKINTLTDDEYVFDEPAHRLVGVRTGKVFRLGDHVKVRCIAVDEERARVEFELIEKLEKHETL | 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: 3.1.13.1
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O32231 | MEKEAFMEKLLSFMKEEAYKPLTVQELEEMLNITEAEEFKELVKALVALEEKGLIVRTRSDRYGIPEKMNLIKGKISAHAKGFAFLLPEDTSLSDVFIPPNELNTAMNGDIVMVRLNSQSSGSRQEGTVIRILERAIQRVVGTYTETRNFGFVIPDDKKITSDIFIPKNGKNGAAEGHKVVVKLTSYPEGRMNAEGEVETILGHKNDPGIDILSVIHKHGLPGEFPADAMEQASSTPDTIDEKDLKDRRDLRDQVIVTIDGADAKDLDDAVTVTKLDDGSYKLGVHIADVSHYVTENSPIDKEALERGTSVYLVDRVIPMIPHRLSNGICSLNPKVDRLTLSCEMTINSQGQVTEHEIFQSVIKTTERMTYSDVNKILVDDDEELKQKYEPLVPMFKDMERLAQILRDKRMDRGAVDFDFKEAKVLVDDEGAVKDVVIRERSVAEKLIEEFMLVANETVAEHFHWMNVPFIYRIHEEPNAEKLQKFLEFVTTFGYVVKGTAGNIHPRALQSILDAVRDRPEETVISTVMLRSMKQAKYDPQSLGHFGLSTEFYTHFTSPIRRYPDLIVHRLIRTYLINGKVDEATQEKWAERLPDIAEHTSSMERRAVDAERETDDLKKAEYMLDKIGEEFDGMISSVTNFGMFVELPNTIEGLVHVSFMTDDYYRFDEQHFAMIGERTGNVFRIGDEITVKVVDVNKDERNIDFEIVGMKGTPRRPRELDSSRSRKRGKPARKRVQSTNTPVSPAPSEEKGEWFTKPKKKKKKRGFQNAPKQKRKKKK | 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.
Sequence Mass (Da): 88750
Sequence Length: 779
Subcellular Location: Cytoplasm
EC: 3.1.13.1
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P57628 | MVVDPYQKREAKRYKNPIPSREYISSCLRTSQDLISQKNLEKKFGINNQESKKALRRRLRAMERDGQVIYTSNRCYVAPESLKIVKGKVIGHRDGYGFLRTETLKEDLWLSSEQMKSCIHGDIILAHIVETHGKRRSSARFLKLLQPNNILIVGRYYIDDKIKFVIPDDTRFNFKIFIFSAIKDDISIGSIVSVKLKQHPIRNSRVQGFIVEILGKEMGTNLAIEIALRTHLIPSLWSKEVKKQVYEISRKINQYDFKNRTDLRHFPFFTIDDEDARDFDDAVFCKRKANPEEGWILWVAIADVSCYVQPNTPLDKAALERGTSVYFPSLVIPMLPEKISTDLCSLKPNVERLCLICEMSLSKQGELISYKHYEGIICSHGRFTYNEIFKIWNGDIFLRSKYKKFLKDIENLSCLQNIFNKDNISKKGIYFENIEPKFVLDSNLRIKSIYQNIRNDAHKFIESCMILANVASARFVEKYKYPVLFRNHDRPKKDNVVSLRLFLNELGFTLLGGDSPESVHYSNLLKNVSDRPEYEMIQTVLLRSMTQAVYSPDNRGHFGLSLSSYVHFTSPIRRYPDLILHRVIKYLLFKDKNTSKSNYNFYSAHLYSTGEIKKIGAHCSITERRADEANRDVIDWLKCDFMYKKIGCILNGVISNVTTFGFFVRLNQFFIDGLVHINSLNDDYYYFDSLGLKLIGKSTKNTYCLGDALKVKVISVNLNEKKIELSLYKSS | 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: 3.1.13.1
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O84402 | MGKAKNKKKFLKNRKQVLVPGTLFVHSRKGFGFVSPDQPELYPFDIFISASDLKGALDGDHVLVALPFSLRGGEKRKGVIHKVLSRGKTVLVGTIVSLINPTLAMVYVNTIGPEHPLKAELLPKRTYKLGDRLLLKTPVWKENYPSREPPPLAMLEFIGNISNAKTDFPVIKAEFSITEEFPDAVVQEASQFLQKHVTQALHSRKDLRDLLCFTIDSSSAKDFDDAVSLTYDHEGNYILGVHIADVSHYVTPNSALDREAAKRCNSIYFPGKVIPMLPSALSDNLCSLKPNVDRLAVSVFMTFSKEGFLSDYRILRSVIRSKYRMTYDEVDEIIEKKQTHPISKTILKMAELSRIFSDIREQRGCTRLVLPSFTMSLDNLQEPVALIENKQTAAHKLIEEFMLKANEVIAYHISHQGITMPFRTHEPPNEESLLVFQETAKAMGFTITQTPAQEPDYQYLLQETTAGHPLEPILHSQFVRSMKTASYSTENKGHYGLCLDYYTHFTSPIRRYVDLIVHRLLFHPLSVEEEHLEQIVRACSSQERIAAKAEGAFVNIKKARFLKKFIEEQPATLYKAFIITASPEGISFVLPEFCHEGFIPAAKLPQAYVLQTKIGLEELPEHLRPGAVISVQLASVTLLTQSIEWTLVEATTKAKAKRTSKKKKTESVTTKEKKKSPAKKKKGATKTKKGSGKN | 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: 3.1.13.1
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P21499 | MSQDPFQEREAEKYANPIPSREFILEHLTKREKPASRDELAVELHIEGEEQLEGLRRRLRAMERDGQLVFTRRQCYALPERLDLVKGTVIGHRDGYGFLRVEGRKDDLYLSSEQMKTCIHGDQVLAQPLGADRKGRREARIVRVLVPKTSQIVGRYFTEAGVGFVVPDDSRLSFDILIPPDQIMGARMGFVVVVELTQRPTRRTKAVGKIVEVLGDNMGTGMAVDIALRTHEIPYIWPQAVEQQVAGLKEEVPEEAKAGRVDLRDLPLVTIDGEDARDFDDAVYCEKKRGGGWRLWVAIADVSYYVRPSTPLDREARNRGTSVYFPSQVIPMLPEVLSNGLCSLNPQVDRLCMVCEMTVSSKGRLTGYKFYEAVMSSHARLTYTKVWHILQGDQDLREQYAPLVKHLEELHNLYKVLDKAREERGGISFESEEAKFIFNAERRIERIEQTQRNDAHKLIEECMILANISAARFVEKAKEPALFRIHDKPSTEAITSFRSVLAELGLELPGGNKPEPRDYAELLESVADRPDAEMLQTMLLRSMKQAIYDPENRGHFGLALQSYAHFTSPIRRYPDLTLHRAIKYLLAKEQGHQGNTTETGGYHYSMEEMLQLGQHCSMAERRADEATRDVADWLKCDFMLDQVGNVFKGVISSVTGFGFFVRLDDLFIDGLVHVSSLDNDYYRFDQVGQRLMGESSGQTYRLGDRVEVRVEAVNMDERKIDFSLISSERAPRNVGKTAREKAKKGDAGKKGGKRRQVGKKVNFEPDSAFRGEKKTKPKAAKKDARKAKKPSAKTQKIAAATKAKRAAKKKVAE | 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 helicase activity, which is independent of its RNase activity. RNases 2 and R (rnb and this entry) contribute to rRNA degradation during starvation, while RNase R and PNPase (this entry and pnp) are the major contributors to quality control of rRNA during steady state growth . Required for the expression of virulence genes in enteroinvasive strains of E.coli.
PTM: Acetylated at Lys-544 by PatZ during exponential growth phase. Acetylation alters RNase R structure and enhances binding of SsrA/tmRNA and SmpB, leading to instability and degradation of RNase R. Not acetylated and stable in stationary phase cells.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 92109
Sequence Length: 813
Subcellular Location: Cytoplasm
EC: 3.1.13.1
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Q5AK94 | MLSILSIAALLIATVQAADFSSSCPIDSPISCSSNGDTSNSCCYENPGGIILFTQFWDYNPASGPADSFTIHSIWNDYCSGGYPQFCDTSLEIDSTGSTIESIVVDQFGDQTLYDNMNKYWTDINGNNKKFWAHEFNKHGTCLNTLNPSCYSNYKQNENVYDYYSLVYQLFQKLPTYQWLVSAGIKPSTTATYTLSQIQSALKSKFGAEVYIACDSNNAINEVWYFYNIKGSILQQNYLPIDTVSKTNCPSSGIKFPPKGNSGANTLTTKTTGTTTSGSGSTSVPATSYINLTGKSGCLISNGKYYTSGTCATYHFNAGSSGNTQITSSKGNCGIDSSNQFTCSSSTSATDFQVSGGSIGYNGNFDWCLGAVTGSGSTAQTSVKLSDGSCSSFKLTLSS | 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 salt concentration (By similarity).
Catalytic Activity: a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)
Sequence Mass (Da): 42733
Sequence Length: 399
Subcellular Location: Vacuole lumen
EC: 4.6.1.19
|
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 salt concentration (By similarity).
Catalytic Activity: a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)
Sequence Mass (Da): 33434
Sequence Length: 292
Subcellular Location: Vacuole lumen
EC: 4.6.1.19
|
Q4WXZ5 | MLQSIPGPQHILKALTGSLGLSTIFEPDHEASQNSFQCSKPELSCHAQYHGQDTCCFNYPGGQMLQTQFWDADPAVGPVDSWTIHGLWPDFCDGGFDQYCDSKRRYSNISLILVDSGRADLLEYMSDFWKDFRGDDEDLWEHEWNKHGTCISTLETTCYADYYPQQEVVDYFNKTVEIFQKLPTYQTLANAGIVPSHTETYTLDEIQAALAKAHAAPVTIRCRNRALNEVWYHFNIAGSLQTGTFVPSEPDGLKTNCPATGIHYIPKKHREPSRTTDTPSQPTTTGTPFKGRGNLIVSSMGGRRGCIISRGKWFASGTCATFKAKKATDDTFTLQSSKGICAFEGDAFSCGPHVTAPEEFSVQDGKLSYRGNTTFFADKAPKGRTQSTIFASQDEHLIDLAITWKERR | 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 salt concentration (By similarity).
Catalytic Activity: a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)
Sequence Mass (Da): 45499
Sequence Length: 408
Subcellular Location: Vacuole lumen
EC: 4.6.1.19
|
Q6MNQ3 | MEIVISAIIGLLIGGTVVFVIKRLQDNNKKKSARFEAERIVNKANSEAAKIKKESENKAKDFESRARKNVEQDIHKQKSTLKNKESQLERRLKEVEDQFKQKMEENERYLNSLKDREEKIAISENRIKDLEKKGEAHIGELKQKLESVAAMSQDEARRQLLTALEDEAKQEAAKKIAQIEEEANKESEKKAKRILATALSRFASEYTSERTVSVLALPNDEMKGKIIGREGRNIRTLEAHCGVDLIVDDTPEAVVISGFDPVRRELARRTIEKLMEDGRVHPARIEEVAEKQRNELMKSMKEEGERHVMELGIPNMHPELVKIIGGLKYRSYQGQNALNQSLEVATIAGLLAAELGVSVKLARRAGLLHNIGKAIDHTVEGSYAFVGAEAAKKYNESEDVCHAIRAHDEEEKPHSILAWIVHAAYTLSSSRPGARRPQMDTFIHRLEDLESIGNSFDGVLKTLALQAGKDIRVLVESSRVTDDQAVMLSRDIARKIEREMPQAGQVKVTVVRETRSVEHAR | 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.-.-
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Q6FP42 | MILASVLKAFQGLQTGLQHSYQDGSPSCPINLPLSCGNETAISDLCCFEYPGGILLMTQFWNYAPSKPNLNRTELEEELGPVDSFTIHGLWPDDCMGGYPQFCKRDLFIDDVDYLLKSDAFNNDDTLPIQGEELLNNLNKYWKSNNGNHESLWIHEYNKHGTCLSTLQPQCYSRWNPTTSQKGPKYYKKKAVYDYFRISYDLFQKLNTYEMLAKHNITPSNDTSYTKSEILSALSSEFQGTQAHINCNSQNALTEVWYYHQLNGSILNEDFIPLDPLRSMSRCKDQGIKYYPKGYQRRDNRGPNKKPISRGTIRISQYGGFLIKTGRWMKRGTPANFELIESKYGNYLLKSRMGYCTVHNDKSQLDCSSRSPDYATQFDYNEEKGILGYSGSFEWGAESAPKNGRTSRSVVFAVSNEKNSNLKYKFQLKFNRK | 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 salt concentration (By similarity).
Catalytic Activity: a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)
Sequence Mass (Da): 49674
Sequence Length: 433
Subcellular Location: Vacuole lumen
EC: 4.6.1.19
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Q6BHB1 | MLALILTISICIFLKGSTCSYINLGSEGIVFGAPNCPVDIPLTCTNSTPIDNSCCFESPGGILLSTQFWDYYPPIGGNESFTLHGLWPDNCDGTYEQFCDDSLNIRSATDIVLNQFGDKVLYGKMSEFWKNFNGNDESLWIHEFNKHATCVKTIRPTCYDNQRYVKNKNVYDFYNITMNLYEKLPTFQFLAAEGIVPSLTQKYSKKQINDALTKYFGKAVYFKCNKYKALQEVWYYHYLQGSLKEENFSPIDTIINSNCPEENIQFIPKNGFNPGPQPPKSPRKGYLESPGKKGCLISNGLWYEAGTCATYAISQQEFGGYKIRSSKGYCGMNSQGQFTCNKQVDPTKNQFQYNKDTRKIGYGGNFAWCLDTEHKHGDGKTAQTPIKISDGQCDSFPVQYGGK | 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 salt concentration (By similarity).
Catalytic Activity: a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)
Sequence Mass (Da): 45472
Sequence Length: 403
Subcellular Location: Vacuole lumen
EC: 4.6.1.19
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Q5B3K6 | MSSISGFLGAIPGAQQILQTMAGSLGLAPLSHPEIASSGSTFQQCGKLELSCQTSYHGQDTCCFNYPGGQMLQTQFWDADPAVGPENSWTIHGLWPDHCNGGFDQFCDSHRKYSNISLILIDAGRRDLLDEMSTYWKDYRGDDPNLWEHEWNKHGTCVSTLETHCYSEYYPQQEVVDYFDKTVELFHDLPTYMTLANAGIVPSYTQTYTRHEVEDALSKAHGATVTVRCRSQRLQEVWYFFNVEGPLQTGKFVPSEPDGQTSNCPAKGIIYQPKTPNKDPGHGHEPTKTRHPHGPTGAPFIGKGNLVVSTMGQQRGCIIGRGTWYSSGTCADFRAKRASGDTFTLSSRKGPCAFKDDIFTCGSYISSPAEFSAEDGKLSYHGNTTFFADKAPKGKVQSDIFVSEADHPIELSIAWRG | 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 salt concentration (By similarity).
Catalytic Activity: a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)
Sequence Mass (Da): 46091
Sequence Length: 417
Subcellular Location: Vacuole lumen
EC: 4.6.1.19
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Q03R31 | MSVPIVILAIIAIVVGVVGGYYLRKSVHERKLDAAKYTAAGVLAEAKKQAETATKEALLEAKEDSHKYRAEVETELKERRAEVQKQEDRLIQREETLDRKDNSLEKRENSLNRRDKKLSAEEQNLVKKQQQADSLIEKRQAAVEAVAALSQDDARELIISEAKTALASERAKMIKESEETARKTAQANAKDLIVSAIQRSAADMVTETTITVVTLPNDDMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVVLSGFDPLRREVAKIALEKLIQDGRIHPARIEEMVAKAKKELDEHVRELGEQATFDLGIHSMHPELVKLVGRLNFRISHGQNALAHSIEVAKITGVLAAELGEDVTLAKRAGLLHDIGRAAEHEDDNSYITTGMELTKKYRESSVVVNAIAAQAEETAAQSVIAELVSTADIISATRPGARSDSLESYIHRLDKLETIANEFDGVDHSFAIQAGREVRVIVRPDRISDTDAVVLARDIKQQIEGDLDYPGHVKVSVIREVRSVEYAK | 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.-.-
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Q03EQ6 | MIILYIILAIIAIVVGYCAGFFMHKRLIEKQTANASNSADVIVENARKQAETERREKLLEAKDESHRYRAKVEKELKERRAELQKQEDRLLQREDSLDRKDNSFEKRENSLERKEQKLALDQKHIDEQQQKASSLVEERQQELERVSNLTQEDAKNLIISETEAKLEKERALIIKEGLEDAEAEADQTARKLIAEAIQRSAADMASETTITVVSLPNDDMKGRIIGREGRNIRNFQNVTGVDLIIDDTPEAVVLSSFDPIRREIARIALDKLIQDGRIHPARIEEMVEKAKKEMDDNIRKTGEQAVFDLGIHSMNPELIKLIGQLKYRTSYGQNVLNHSIEVANLAGVLAAELGEDVTVAKRAGLLHDIGKAVQHETDTSHAQLGVELAKKYKESATVINAIAAHHDGVEAQHVISVLVAAANSISAARPGARSDTLQSYIHRLEKLEQISNNFDGVKKSYAIQAGREVRVIVKPNKINDLKAVMLTHNIRKAIEKELEYAGKVKVTVVREVRAVDYAK | 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.-.-
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Q6CAV7 | MQFSLATIATVAAAVSALVCPYTKRDAVAAFTSPPLSSADHKSCPADTPVSCSSGAGSADLCCTESPGGVLVLTQFWDWTPAIGPDDLFTLHGLWPDNCDGSYAQFCDKSMEVQSVAAVLQQLGETELLDKMNKIWIPNRGSTDSFWTHEWNKHATCMSTLKDKCYSSDAPQYQSLADWAHTVVNVFETVNTYKFLEAAGITPDSSKTYAKTDFLNALNSNFDGKQVHISCKSGYISEVWYYFHLKGSVVSGQYLPIDDIGSSSCPDQIKFPPKDGSGGTPPPTDPSDPPTGGSKGFINISGQSGCLISNGNWYTSGTCATYTLGESQYGGVTLTSSKGPCDVVNGKFSCASGNNAGQFTQDGSNIVYGGKSDWSAPSVPSGSQQVGVSPGSAGGSVSFNLVFAAK | 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 salt concentration (By similarity).
Catalytic Activity: a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)
Sequence Mass (Da): 42796
Sequence Length: 406
Subcellular Location: Vacuole lumen
EC: 4.6.1.19
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Q02933 | MLLKNLHSLLQLPIFSNGADKGIEPNCPINIPLSCSNKTDIDNSCCFEYPGGIFLQTQFWNYFPSKNDLNETELVKELGPLDSFTIHGLWPDNCHGGYQQFCNRSLQIDDVYYLLHDKKFNNNDTSLQISGEKLLEYLDLYWKSNNGNHESLWIHEFNKHGTCISTIRPECYTEWGANSVDRKRAVYDYFRITYNLFKKLDTFSTLEKNNIVPSVDNSYSLEQIEAALSKEFEGKKVFIGCDRHNSLNEVWYYNHLKGSLLSEMFVPMDSLAIRTNCKKDGIKFFPKGYVPTFRRRPNKGARYRGVVRLSNINNGDQMQGFLIKNGHWMSQGTPANYELIKSPYGNYYLRTNQGFCDIISSSSNELVCKFRNIKDAGQFDFDPTKGGDGYIGYSGNYNWGGDTYPRRRNQSPIFSVDDEQNSKKYKFKLKFIKN | 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 salt concentration.
PTM: N-glycosylated.
Catalytic Activity: a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)
Sequence Mass (Da): 50171
Sequence Length: 434
Subcellular Location: Vacuole lumen
EC: 4.6.1.19
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Q6ML54 | MIAMIATAIIGIVAGGGLGWALHKFFRARTLRLAREEAQDILDEANEVVELRNLEERERIQEIEMELWTKVEPEMLKSEGRIEDLQEVANERKAKADAIVQEEKKKLQDREADVKVQEQALRGQEAELGKLKEAQKALNQELVQKLTERLGTSAEEFKTQLKNQMEEESRRRAARMIQETEADTKEHAESEAKRILSLVIDRFARPYCAERGIGAVNFPDAHIRKLFCDPAGNNIKAVQDACGCDIIVEEGMEMVGVAGFDPVRRELTRRTLERIFKEKKNINPDFIRKIAENQKKELFKNIKHDGDSLAKELKLEGLNAEIRQMMGSLRYRYSFTQNQYFHCGEVGWLAGLMAAELGIDIKKARRVGMLHDIGKSMDHTVEGGHAVIGADFIAARGEAPDVVHAVKAHHFDEQPSTDHAFLVIAADAVSGARPGARRSTIESYNQKVSELQDIARSFPGVTDCFVLSGGRECRVMVNGKKVDDTQAMDLSRKIAARIEEECNYPGSIKVVVVRETVVTEQTRKELA | 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.-.-
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Q03NQ6 | MLITGLIIGCLLIGLVIGYVVRQHQHRQELLAVQKQARDIIASATAETQQKIAKLTADSRRETLTYQQSVKDELAEQTSDIAVREQRRQQREQLLGQMGVRLADQTAILDERSQANRDQRQKIRDLKAQALQLRTDRDEMLAQQAGIDEQAAKDHVLADTELDLKRDRDVEIKALNDNAVANAERWAKDVVLSATESGPQDLPKEHLEHTVTVPNGEIRSKIIGRDGQHIRLLETLTGTDLIFVPDDNTTLFISTHDPIRREVARVALTNLVASRRISSNQIETQVENAQRDVNHSLWETGEQTVSGLHVGWMHPDLMKLIGRLKYRTSYGQNVLLHSIEVAQLTGAMAARLGYNTRLARRAGLLHDLGKAIDHEVEGTHVEIGTEFAQKYGEDDVVINAIAAHHGDVEKTSPLAELVAAADAISGARPGARSESVEDYINRLRALEKIANDQSGVAESYAIQAGRELRIIVKPQELDDTAAANLTQEVAQQIESTLTYPGKIKVTTIRKSTAVEYVGDEKKKKSKKKKKKAANA | 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.-.-
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Q03E93 | MATILIVVLLLASIGVGYGLRAKKHSETLAQARKAAEKIIEHERQKTKAEVAEYEKNSVQETQQYQETIDQELADDLHDNQRKEAWIEQRMNLLNQKKIVLTNRADALAKKRQSLLQERDNVRTTLGEAKQLITDRWNKLQEVADLEEQAASKLVLKETKQDAIRSKDEFVNNAQTELESSCEREAEDLIALAMEHSDVPRGQAENHRSFIAENAEYLGKLIGNSGQNVRAIEALTGVDIVIDDQEKEVILNGYDPVRRAVAMETMEMIKTEKRVVPDTIERLVNKANKVIDQRIRQYGEDAVRELKLKYVAPDLIKFIGRMHYRTSYGQNILEHSIETAKLAGIFAVELGEDATLARRAGLLHDIGKSIDRDIEATHVELGVELTTKYRESPVIVNTIASHHGDVEARYVIANLVEAADAISGARQGARSESVADYIQRIKSLEEIANKHPEVKESYAIQAGRELRVIVQPKETDDKTIHSLATNVKNQIEEDVTYPGQVKVTVVRKLEIVEYVEKKQA | 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.-.-
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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, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 29247
Sequence Length: 279
EC: 3.1.26.11
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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, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 33673
Sequence Length: 307
EC: 3.1.26.11
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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, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 36885
Sequence Length: 316
EC: 3.1.26.11
|
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, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 33758
Sequence Length: 299
EC: 3.1.26.11
|
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, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 33304
Sequence Length: 305
EC: 3.1.26.11
|
Q8YLZ0 | MQITFLGTSSGVPTRARNVSSVALRLPQRAELWLFDCGEGTQHQILRSDLKVSQLSRIFITHLHGDHIFGLMGLLASCGLAGNVQRVDIYGPSGLNDYIQSASRYSHTHFSYPIKVHTVRPGVIYENDEFTVTCGLLHHRITAFGYRVAEKDRAGRFDIEKAKELQIPPGRIYGQLKRGETVTLEDGRVINGAELCGPTEIGRKMAYCTDTIYCDGAVELAQDADVLIHEATFAHQDSEMAFQRLHSTTTMAAQTALAAGVRRLLMTHFSPRYAPGNTIELKDLLQEARAIFPRTDMAYDFMTYEVPRRREPVFSSVSSSSV | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 35884
Sequence Length: 322
EC: 3.1.26.11
|
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, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Mass (Da): 34606
Sequence Length: 306
EC: 3.1.26.11
|
Q8Z4P3 | MNTEATHDQNEAQTTGVRLRNAREQLGLSQQAVAERLCLKVSTVRDIEEDKAPSDLASTFLRGYIRSYARLVHVPEEELLPGLEKQAPLRAAKVAPMQSFSLGKRRKKRDGWLMSFTWLVLFVVVGLTGAWWWQNHKAQQEEITTMADQSTAELNADKDSGQSVPLDTSAATSQDTTPAQTAPAPATPVDSTAATQNTVVAPSQANVDTAATSAAPAATETPSALPTSQAGVAAPAADPNALVMNFTADCWLEVTDATGKKLFSGMQRKDGNLNLTGQAPYKLKIGAPAAVQIQYQGKPVDLSRFIRTNQVARLTLNAEPTPAQ | 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 in the formation of spirals to maintain the rigid rod shape. As this protein is anchored in the cytoplasmic membrane, the HTH motif may contribute to protein-protein interactions to form the RodZ helix, which is localized beneath the cytoplasmic membrane. The C-terminal domain may be critical for determination of the rod shape by probably interacting with enzymes required for synthesis of the peptidoglycan layer, including PBPs in the periplasm.
Subcellular Location: Cell inner membrane
|
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 membrane
|
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 membrane
|
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 membrane
|
B6VJS4 | MDLANGVISAELLHAQAHVWNHIFNFIKSMSLKCAIQLGIPDIIHNHGKPMTLPELVAKLPVHPKRSQCVYRLMRILVHSGFLAAQRVQQGKEEEGYVLTDASRLLLMDDSLSIRPLVLAMLDPILTKPWHYLSAWFQNDDPTPFHTAYERSFWDYAGHEPQLNNSFNEAMASDARLLTSVLLKEGQGVFAGLNSLVDVGGGTGKVAKAIANAFPHLNCTVLDLSHVVAGLQGSKNLNYFAGDMFEAIPPADAILLKWILHDWSNEECVKILKRCREAIPSKENGGKVIIIDMIMMKNQGDYKSTETQLFFDMTMMIFAPGRERDENEWEKLFLDAGFSHYKITPILGLRSLIEVYP | 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
Sequence Mass (Da): 40100
Sequence Length: 357
EC: 2.1.1.240
|
Q9F0J6 | MQATKIIDGFHLVGAIDWNSRDFHGYTLSPMGTTYNAYLVEDEKTTLFDTVKAEYKGELLCGIASVIDPKKIDYLVIQHLELDHAGALPALIEACQPEKIFTSSLGQKAMESHFHYKDWPVQVVKHGETLSLGKRTVTFYETRMLHWPDSMVSWFADEKVLISNDIFGQNIAASERFSDQIPVHTLERAMREYYANIVNPYAPQTLKAIETLVGAGVAPEFICPDHGVIFRGADQCTFAVQKYVEYAEQKPTNKVVIFYDSMWHSTEKMARVLAESFRDEGCTVKLMWCKACHHSQIMSEISDAGAVIVGSPTHNNGILPYVAGTLQYIKGLRPQNKIGGAFGSFGWSGESTKVLAEWLTGMGFDMPATPVKVKNVPTHADYEQLKTMAQTIARALKAKLAA | 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 Length: 212
Domain: The RIIa domain mediates interaction with AKAP3.
Subcellular Location: Cell projection
|
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: Sumoylated, sumoylation decreases upon spermatozoa capacitation conditions.
Sequence Mass (Da): 24426
Sequence Length: 218
Subcellular Location: Cell projection
|
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: Sumoylated, sumoylation decreases upon spermatozoa capacitation conditions.
Sequence Mass (Da): 26107
Sequence Length: 230
Subcellular Location: Cell projection
|
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: Sumoylated, sumoylation decreases upon spermatozoa capacitation conditions.
Sequence Mass (Da): 24516
Sequence Length: 218
Subcellular Location: Cell projection
|
A9C3R9 | MVSRLEHPAGGYKKVFESCEELAEPIPAHVSGKIPAWLSGSLLRMGPGLFEIGDEPFNHLFDGQALIHKFDLKDGRVTYHRKFIRTDAYVRAMTEKRVVITELGTAAYPDPCKNIFSRFFTYFQGTEVTDNCSVNIYPIGEDFYACTETNFITKVNPDTLETIKKVDLCNYLSVNGLTAHPHIEADGTVYNIGNCFGKNMSLAYNIVKIPPLQEEKSDPLAMSKVLVQFPSSERFKPSYVHSFGMTENHFVFVETPVKINLLKFLTSWSIRGSNYMDCFESNDRMGTWFHLAAKNPGKYIDHKFRTSAFNIFHHINCFEDQGFIVVDLCTWKGHEFVYNYLYLANLRQNWEEVKKAALRAPQPEVRRYVLPLDIHREEQGKNLVSLPYTTATAVMCSDGTVWLEPEVLFSGPRQAFEFPQINYSKFNGKDYTFAYGLGLNHFVPDRICKLNVKSKETWIWQEPDAYPSEPLFVQSPDAEDEDDGVLLSIVVKPGVSQRPAFLLILKATDLTEIARAEVDVLIPLTLHGIYKP | 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 fatty acid + H(+)
PTM: Palmitoylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 60613
Sequence Length: 532
Subcellular Location: Cytoplasm
EC: 3.1.1.90
|
P32561 | MVYEATPFDPITVKPSDKRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHPRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKDLPYNEYYEYYGPDYKLSVRPSNMFNVNTPEYLDKVMTNIFANLENTKYAPSVQLNHTPRDAEDLGDVEEDSAEAKDTKGGSQYARDLHVEHDNEFY | 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, DNA damage response, osmotic stress response and developmental events. Is involved in rDNA and telomere silencing and in double strand breaks repair. Required for both full transcription repression and activation of many genes including cell type-specific genes (STE6, TY2 and HO), cell differentiation-specific genes (SPO13), genes that respond to external signals (PHO5) and TRK2. The RPD3 complexes regulate also chromosomal replication timing.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 48904
Sequence Length: 433
Domain: The ESA1-RPD3 (ER) motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity.
Subcellular Location: Cytoplasm
EC: 3.5.1.98
|
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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