ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
A4VKM0 | MNTLLLHCRPGFEGEVCAEISEHAAILEVAGYAKARPDSACAEFICSEPGGAERLMRRLRFADLIFPRQWARGDYLQLPETDRISVLLAHLADYPVCSSLWLEVLDTNDGKELSNFCRKFEAPLRKALVKAGRLDEQGKGPRLLLTFKSGREVFVGIAEANNSALWPMGIPRLKFPRQAPSRSTLKLEEAWHHFIPREQWDTRLAAGMTGVDLGAAPGGWTWQMVNRHIKVSAVDNGPMNADLMDSGLVEHFRADGFTFRPKRPVDWMVCDIVEKPARNAALLETWIGEGLCREAVVNLKLPMKQRYAEVKRLLERIADGLAERGVKASIGCKQLYHDREEVTCHLRRL | Function: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
Catalytic Activity: cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39310
Sequence Length: 349
Subcellular Location: Cytoplasm
EC: 2.1.1.186
|
C4ZJM0 | MNQHTPAAALACAGLLGYCRAGFEKELAAELDDIAAEAGLIGYVRAEPDSGYVIYETFEPTPLGSFGESTDWRRPVFARQLLPWFARVDDLPERDRATPIVEAVKASGQRFSGVMLETPDTDEAKQRSGFCKRFTEPLAKALEKAGCLRSSRAGLPVLHVLFTSATTAWLAAGQPGQCSTWPMGIPRVRMPSNAPSRSTAKLSEAFMMLLEEGERDSILRAGQRAVDLGAAPGGWTWQLVNRGLRVTAIDNGPLRDSVMATEMVEHLKADGFTWRPHRPVDWMVCDMVEQPSRIASLMAEWVATGRCRYTIFNLKLPMKRRVEAVEQCRELIRKRLASVGPYDLRIKHLYHDREEVTAFLTLKR | Function: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
Catalytic Activity: cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40593
Sequence Length: 364
Subcellular Location: Cytoplasm
EC: 2.1.1.186
|
Q182S0 | MEKKKIVLKNFTEDELKEFMKTIDEKPFRGSQIFSWIYKGAKTFDDMNNIPKSLRNKLEEVSCIGHIDIELKLESKVDNTKKYLFLLDDGNIIETVMMDYDSRVTVCVSNQVGCRMGCNFCASTMDGLIRNLEPWEILDQVIKIQEDTGKRVSNLVLMGSGEPLDNFENTKQFLKIINEKNGLNIGYRHITLSTCGIVPKMYELADLEIAINLALSLHSPYDEERRKIMPVANAYSIEEILNACRYYIKKTNRRVTFEYSLIKGVNDSEKEAKALAKLLKGMLCHVNLIPINKVEEREYEKPDKAFIYKFRDSLEKNNIPATVRMSMGSDISGACGQLRRKYK | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39476
Sequence Length: 343
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
Q0TPL4 | MKNILDFTLEELKEWMKENGESAFRAKQIFDWIYKKEVFNFEEMKNISKALIGKLSENFYIGIPEVIDYLSSSEDGTRKILLGLGDGNIIECVIMRYKYGNSICVSTQIGCRMGCKFCASTLEGMVRNLTAGEILSEVLIGQKLLGERISNIVLMGSGEPLDNYDNVMKFLELVNADYGLNIGQRHITLSTCGLVPKIREMADKEMQVTLAISLHAVSDEKRKTIMPIANKYSISEILDACNYYIEKTGRRITFEYSLVSGVNDTKEDAKSLGRLLKGMLCHVNLIPVNEIKENEFKKSTKKDIETFLNTLKTYGVEATVRREMGSDINAACGQLRRSYIKSKGLKL | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39164
Sequence Length: 347
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
B2A2K6 | MINHKQSLKDLTLNELQEYFSRKGWQQFRAKQIFDWMYIQQVDSIEVMSNIPKKLRQELMENCTINDLELDSNNIYTSPTDGTIKFLSVLKDGIGVETTIMKYDYGNTVCISSQAGCNMNCVFCASTTGGKERDLSPGEMIDQVLMANKVLPGSESINNIVVMGSGEPLENYQHLIKFLKIVNDGKGLNIGMRHITVSTCGLVPEIYNLAEEELQLNLAISLHAPNDELRNKLIPLNKIYPIHELLEACQVYFQKTGRRITFEYVLIKDFNDSIDLAKELSETLTALKMPVHVNLIPFNPVEETKFTAPPSSRISDFKNNLQSNNIGVTVRKERGVDVDGACGQLRSKVMR | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39632
Sequence Length: 351
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
Q82XV4 | MINLLDFNKTELVRFCGEMGEKPYRARQLLRWVHQSGKTDFMEMSDLAKGFRHKLMECAVVQLPEIVSDHTAGDGTRKWLLSTGAGNAVEMVFIPEPSRGTLCVSSQVGCALACSFCSTGRQGFNRNLSVAEIIGQLWWANRLLEAGSHDPFPLDTTRVQTDKPETRRPVTNVVMMGMGEPLANFENLVTALDLMLSDDAYGLSRRRVTVSTSGLVPALDRLRERCPVALAVSLHAPNDALRDQLVPINKKYPIRDLLAACERYLPAAPRDFITFEYVMLKGVNDSVALARELVQLVRNVPCKLNLIPFNAFSGSGYERSGAEAIGNFRDVLMQAGIVTTVRKTRGDDIAAACGQLAGQVRDKTRRTSGCGTGQPAVAR | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41646
Sequence Length: 379
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
A9A3L9 | MTDLYRLLPEEMEKLVIDMGYDRYRADQILLPLYYKFPKDINDIPQLPKKLREEFTEAGYTIGSAKEIHRVVSDDGDTTKLLLELSDGSSVETVLMQYEPTKIGGHPRSTICVSTQIGCAMGCVFCATGQMGFETNLKAEHIVSQVIHFAELLEQRGEHVTNLVFMGMGEPMANYDEMIRAVKILTHDRGFGLGQRHITISTIGITSGIEKLAEENLQIGLAISLHAPNNELRKKLVPTAGPNSVEDIIKSGRDYFKKTGRRVTFEYALMEGVNDSPEIAHELARLLRGNGSHVNIIPINPTAGDFKRPSEKNVLEFEQILRKSGVNCTVRVEKGTEISAACGQLRTDIVG | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39021
Sequence Length: 351
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q2Y6F3 | MSINLLDFDAKGLTGFCAEIGEKPFRARQLLRWIHRTGEADFDAMSDLAKGLREKLAAAAVIEPPKVISDHTASDGTRKWLLSVGAGNGIETVYIPETSRGTLCISSQVGCALACAFCSTGRQGFNRNLTVAEIIGQLWWANKALTETFTSEAGRERPITNIVMMGMGEPLTNFENVVTSLDLMLDDNAYGLSRRRVTVSTSGIIPAMDRLRERCPVALAVSLHAPNDALRDQLVPINRKYPIRELLGACERYLQSAPRDFITFEYVMLDGVNDSVAQARELVQLVRDIPCKLNLIPFNPFPDSGFRRSSANAVSRFRDVLMEAGLVTTVRKTRGDDIAAACGQLAGKVLDKTRRVPRNIAEAAG | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40003
Sequence Length: 365
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
Q9KTF4 | MNRIYLYLLIVLILAGCSSPGGRYDMSDDQAPDTPLSVEHIEDAHPQYEPYSFGGNKDYNLRGKSYRIIKNPKGFTESGKASWYGKKFHGHLTSNGEIYDMYSMTAAHKTLPIPSYVKVTNTDNGKSTVVRVNDRGPFHDGRIIDLSYAAAYKIGVVQAGTANVRIEVITVDKPTKPRPKSKNNALEYVIQVVSSQHIERVRTLAQNLGQNLSAPSFVESTNNTHRLFLGPFTDDDLTQTLLEQVKSAGYDSAFIKTINKRAK | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
Location Topology: Lipid-anchor
Sequence Mass (Da): 29290
Sequence Length: 263
Subcellular Location: Cell membrane
EC: 4.2.2.-
|
Q8ZDG6 | MRKEWLWVGIASVLLSACIDQPPAPQQQVQQTYSGPVEEIGGAEPRYEPFNPNVNQDYKVNGQSYRIIKDPQNFSQIGLASSYGEEARGNTTATGEIFDPNALTAAHPTLPIPSYVRVTNVSNGRQIVVRVNDRGPYTPGRVIDLSRAAADRLNISNNTKVKIDFINVAPDGSLSGPGMVGTTIAKQSYALPSRPDLTSSGMGTPMQQDAPATGAAVQAIDNSQLSGTDATQPVASQSSGFLRAPTPVPAGVLESSEPVIDSAPVTPPVVANPGPVTTTPTSSAISGGYVVQVGALSDAQRAQSWQQSLSQRFGVPGKVSNSGSIYRVQLGPFSHRQQAVDLQQRLSNEAQQQSFIVAAP | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
Location Topology: Lipid-anchor
Sequence Mass (Da): 38018
Sequence Length: 360
Subcellular Location: Cell membrane
EC: 4.2.2.-
|
Q9SR62 | MAQKPRTVICVGDIHGYISKLNNLWLNLQSAIDPSDFSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQTHVFLAGNHDFAFSGFLGLLPRPSDGSDLKDTWKEYSKSEETEGWYTGEGFEDMHLQGRRWAGKIKATFNSVKGMAYKGSIYDAGSTFESYGVPHGSSDLMKAVPESHKKFLTNMVWVHEEDDVCIETEEGLKHCKLIAVHAGLEKGNNVEEQLKLLRAKDTSISKIQHLSGRKNVWDIPQELDDKHTVVVSGHHGKLHIDGMRLIIDEGGGFPDKPVAAIVLPSKKIIRDTDNLSS | Cofactor: Binds 2 divalent metal cations per subunit.
Function: Protein phosphatase that dephosphorylates specifically tyrosine-phosphorylated peptides; especially active on dual-phosphorylated substrates containing a phosphothreonine-X-phosphotyrosine motif.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 34425
Sequence Length: 309
Subcellular Location: Cytoplasm
EC: 3.1.3.48
|
Q2RSU7 | MTDRLRATYRVKATAASIEARAKGIAVEQSVEMPLSAIDDPAVLDGIVGVVEEITERGEDCFEVRLALSTATIGGDAGQLFNMLFGNTSLQDDTVLLDIDLPDDLLASFGGPNIGAAGLRARVGASADRALTCSALKPQGLPPDRLADLARRMALGGLDFIKDDHGMADQAYAPFASRVGAVAAAVDEVNRQTGGQTRYLPSLSGHLDQLRSQVRTGLDHGIDTFLIAPMIVGPSTFHAVVREFPGAAFFAHPTLAGPSRIAPPAHFGKLFRLLGADAVIFPNSGGRFGYSRDTCQAVAEAALGPWGGLHASLPVPAGGMSLARVPEMIATYGPDVIVLIGGNLLEARDRLTEETAAFVASVAGAASRGCGLAP | Function: Catalyzes the conversion of 5-methylthio-D-ribulose 1-phosphate (MTRu-1P) to a 3:1 mixture of 1-methylthioxylulose 5-phosphate (MTXu-5P) and 1-methylthioribulose 5-phosphate (MTRu-5P) . Involved in the MTA-isoprenoid shunt of the methionine salvage pathway .
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = S-methyl-1-thio-D-xylulose 5-phosphate
Sequence Mass (Da): 38880
Sequence Length: 374
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway.
EC: 5.3.3.23
|
A0A0P1A544 | MQFHLLVMTTIAASFAATGSALPHTNVLPKIGTLRGAINNDAATFNGRALRNTENRGLIGDDSDSSISDSDSEAKEYRAYKSHKEHFGYQMP | Function: Secreted effector that suppresses pattern-triggered immunity (PTI) in plant host.
Sequence Mass (Da): 10000
Sequence Length: 92
Domain: Has the canonical translocation RxLR motif, but lacks the canonical EER motif, which characterizes most oomycete effectors identified so far.
Subcellular Location: Secreted
|
A0A0P1B6Y2 | MRLSYIFVVVATIITNCDIASASLRAIMSDTASGNGLGTRILRQTNDSDDLEPIRHAMLDMELLEKIAKDPKYAEEVFGNWRHNGQTKAEMENRLQSNGLLGKYRFIIDRYAEHLANSE | Function: Secreted effector that suppresses pattern-triggered immunity (PTI) in plant host.
Sequence Mass (Da): 13460
Sequence Length: 119
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular Location: Secreted
|
A0A0P1AFH7 | MRGAFYVATAFLIASSTRTAAESVQIKSEITQDLDKLPVGDSDTKSLPRRSLKGSGDRLEIPVAEEERVIPTGVLEGAGKDVSEAILRLEKSGDDLNKMVKVGEGVGSSATSKGKRIQIFQKSHKDAVAEHQQVFDTYKHAIKKNEALELERDTALIKSHNWKLLSDYFSAQAAKDTKNYHNYHTIFSQLDSVVTPATASYKGIKNTREKYLALLEESFSRANAAKHAGNMDEYNEIQVTVAEL | Function: Secreted effector that suppresses pattern-triggered immunity (PTI) in plant host.
Sequence Mass (Da): 26933
Sequence Length: 244
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular Location: Secreted
|
A0A0P1AXF0 | MRIQLLWLSFAVLSTILSTCDATSDKLDPQRVQPNQNGSGHNQSIRSALKTSHGKTIADDEERFISLSGMSEKIAKYYKAIVAKLSKYFRDYHERREIRKQRILNKSFAEMMAGQKSVEDIGRNQDASFMSSSFLWTPEAFKSILHKYALFLYKYGNGHLATVPVKTG | Function: Secreted effector that suppresses pattern-triggered immunity (PTI) in plant host.
Sequence Mass (Da): 19129
Sequence Length: 168
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular Location: Secreted
|
A0A0P1AAU8 | MQGVRITILWCIVLATIYAEEGPSTPRDDDPVIQKVRGLRNAGMKANDERMFKDAIEKLRHAISLLHNRVFGEERAAIKDPTVISQDAALYAQILNDYGSVLIRTKQYDEAIEVLEDSVAMIEKIYGDSHPSLGLSLRSLADAYMEKKAFKSAIKRYKTLRKHVKKGLGMTHEAYIEASLKIAEGYKKLNKKDTSRKVLKDTLKAQGGEINGLTIGIAELYMELSSAHVEVGEIDDALRAAETASAIFLQREGKDTMAYAFSLNALAGVKMQQKKVDEAIDLLDRAHNIAVSIYGENDRITLASAKTLQDVKDHKMNLLAAKDEL | Function: Secreted effector that suppresses pattern-triggered immunity (PTI) in plant host.
Sequence Mass (Da): 36122
Sequence Length: 325
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular Location: Secreted
|
A0A0P1B5K4 | MRLCGVASAFLSTLILIAHIDASTNLNVSVTDVQNISLPGDQIGNFTQSVSGPPSGDEERTSANSAIRKVDLFVEKLITFQVALRAKINRFLAKLKLAWWRLRNVDPNVTFNKLNLHEADNDILSLDNFHTWVKLVESYNLQHPAEQVSILSKLQEQFGEFEVSIMLEQAKNGADKYTEDIALELQHEQISRWRDDNLSLTALYKALQFGKSEPSLLTGPALRVWNIYTSNIESAETSLFDYLYQTIEDAHLSSLLIAAKQSPETVELATKIQNQLRQKWLEILVPPNLVFQHYKLDTNPTHLLDRPETKLWVRYQKMYWGKTKKEVTLKEMIEDFYKADEIAIIIKSATTDYGKHLAKKLPQCDSKHFKTFHNLTILPLLFVFHYTIGAEDDLSSEKNLISQYNHVPTSCETANCVAGGCLFENCASPLLCRGGLCYFRKCKDATCEGGACIFDNTAEASCPGGGCQFVNVPVTLADGYCDGGGCTLDGDDHPSSLAGSLAE | Function: Secreted effector that suppresses pattern-triggered immunity (PTI) in plant host.
Sequence Mass (Da): 56185
Sequence Length: 503
Domain: Has the canonical dEER motif, but lacks translocation RxLR motif, which characterizes most oomycete effectors identified so far.
Subcellular Location: Secreted
|
A0A172M421 | MRVLNFVLTTTVVLLTSSEGIASSPQVRHIKPNVAIDHLSIRSLRATENPGSDESRLNEKDTGFDPDGSSSKEDEDIGEPTFWEKVRFRYWKTMGKTPGDLRKEYFEGMDEAVIKNNPNYKLVQQYEVYYDEKSSE | Function: Effector that acts as a broad suppressor of cell death to interrupt plant immunity. Inhibits cell death induced by cell death-inducing proteins, including the PAMP elicitor INF1 from P.infestans.
Sequence Mass (Da): 15597
Sequence Length: 136
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular Location: Secreted
|
Q8P682 | MSDQSSEPLDSSLRQAVVPDSAAGRRFDAVLAELFPEFSRSRLSEWIKSGDALLDGETARPRDTLRGGETVQVQVVLETQTHAAPQDIPLNVLYEDDHVLVIDKPAGLVVHPGAGNPDGTLVNALLFRDPNLAAVPRAGVVHRLDKDTSGVMVVARTLQAQTALVEQLSARDVHRQYLAVVVGALVSGGTADAPIDRHPRDRLKMAVRDDGRDAVTHYRLRERFRAHTALECRLETGRTHQIRVHMAHLKSPIVGDPLYGGALKLPKGATDTLVAELRGFKRQALHAETLEFLHPVSGEPIRASAPVPEDLQRLMSALREDSARAAELARR | Function: Responsible for synthesis of pseudouridine from uracil at positions 1911, 1915 and 1917 in 23S ribosomal RNA.
Catalytic Activity: uridine(1911/1915/1917) in 23S rRNA = pseudouridine(1911/1915/1917) in 23S rRNA
Sequence Mass (Da): 36150
Sequence Length: 331
EC: 5.4.99.23
|
Q8ZBV7 | MAQQVQLSATVAESQLGQRLDQALAELFPDYSRSRIKEWILDSRVTVNGKKINKPKEKVLGGELVAIDAQIEEDARWAPQEIPLDIVYEDNDILVINKPRGLVVHPGAGNPDGTVLNALLHYYPEIMDVPRAGIVHRLDKDTTGLMVVAKTVPAQTRLVEALQAREITREYEAVAIGNMTAGGRVDEPISRHSTKRTHMAVHPMGKPATTHYRIMEHFRAHTRLRLRLETGRTHQIRVHMSHINHPLVGDQLYGGRPRPPKGASDSFIAILRGFDRQALHATMLRLYHPIRGIQMEWHAALPEDMVELINALKADTEEFKDQMDW | Function: Responsible for synthesis of pseudouridine from uracil at positions 1911, 1915 and 1917 in 23S ribosomal RNA.
Catalytic Activity: uridine(1911/1915/1917) in 23S rRNA = pseudouridine(1911/1915/1917) in 23S rRNA
Sequence Mass (Da): 36706
Sequence Length: 325
EC: 5.4.99.23
|
P50513 | MPTEQVTLTEEMIGWRLDRALASLITRLSRERLKNLISSGCVSNSQGALVRDPAFKIKSLDCFTVDIPLPRPAHNEPQDIPLEIVFEDEHLLVVNKPAGMVVHPAAGNYDNTLVNALLYHCAGKLSGIGGVARPGIVHRIDKDTSGLLVVAKTDPAHAGLAAQFADHSINRRYRAIVDGHPSLQGHVDAPLARSSVNRQKMAIVSDGRGKRAVTHYRMITPLKNASLIECRLETGRTHQVRVHMSSIGHSLLGDPVYGRSKKAHHALLQSLAFQRQALHAAHLGFIHPISGKQVDFDAEMPQDMQLLFKMLMISNRN | Function: Responsible for synthesis of pseudouridine from uracil at positions 1911, 1915 and 1917 in 23S ribosomal RNA.
Catalytic Activity: uridine(1911/1915/1917) in 23S rRNA = pseudouridine(1911/1915/1917) in 23S rRNA
Sequence Mass (Da): 34862
Sequence Length: 317
EC: 5.4.99.23
|
P75966 | MRQFIISENTMQKTSFRNHQVKRFSSQRSTRRKPENQPTRVILFNKPYDVLPQFTDEAGRKTLKEFIPVQGVYAAGRLDRDSEGLLVLTNNGALQARLTQPGKRTGKIYYVQVEGIPTQDALEALRNGVTLNDGPTLPAGAELVDEPAWLWPRNPPIRERKSIPTSWLKITLYEGRNRQVRRMTAHVGFPTLRLIRYAMGDYSLDNLANGEWREVTD | Function: Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA.
Catalytic Activity: uridine(2457) in 23S rRNA = pseudouridine(2457) in 23S rRNA
Sequence Mass (Da): 24880
Sequence Length: 217
EC: 5.4.99.20
|
Q9CKK7 | MKPNTKFNQKTKPRPSSLRSVNKRKAAEIKPQKRPLSFRQKKTVNFAETQVILFNKPYDVLTQFSDEEGRATLKAFIPIPHVYPAGRLDRDSEGLVLLTNNGEIQHRLAVPKFNTEKTYFAQVEGIPQETDLAQLRQGVVLNDGKTLPAKVRLVPEPNWLWQRNPPIRERKQIPTSWLEIKIHEGRNRQVRRMTAHIGFPTLRLIRYQMALFNLANLEQGQYRQLSEVELTALYQQLKLKK | Function: Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA.
Catalytic Activity: uridine(2457) in 23S rRNA = pseudouridine(2457) in 23S rRNA
Sequence Mass (Da): 28058
Sequence Length: 241
EC: 5.4.99.20
|
Q9HX48 | MAKAPPSEPKLLLFNKPFDVLTQFNDEQGRSTLKDFIPVPGVYPAGRLDRDSEGLLLLTNDGRLQARIADPRHKLPKTYWVQVEGTPDEEQLRRLREGVTLNDGPTLPAEARLLDEPTLWERVPPVRFRKSVPTHWLELVIREGRNRQVRRMTAAVGLPTLRLVRVRIGPWSLDGLGLGEWREVPARLD | Function: Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA.
Catalytic Activity: uridine(2457) in 23S rRNA = pseudouridine(2457) in 23S rRNA
Sequence Mass (Da): 21576
Sequence Length: 189
EC: 5.4.99.20
|
Q8ZPZ1 | MRQLISSENTMQKTSFRNHYVKRFSSRQASKSRKENQPKRVVLFNKPYDVLPQFTDEAGRRTLKDFIPVQGVYAAGRLDRDSEGLLVLTNDGALQARLTQPGKRTGKIYYVQVEGIPDNAALQALRTGVTLNDGPTLPAGIEIVAEPDWLWPRTPPIRERKNIPTSWLKVTLYEGRNRQVRRMTAHVGHPTLRLIRYSMGDYTLNGLDNGQWREIAQEKDR | Function: Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA.
Catalytic Activity: uridine(2457) in 23S rRNA = pseudouridine(2457) in 23S rRNA
Sequence Mass (Da): 25330
Sequence Length: 221
EC: 5.4.99.20
|
A3LZU8 | MSKYKILDSHIHLYSLANIPLLHWDEGNPLHGNRRLDEYIENSQSTQFDVEGVVWIECDAKIDLTQGLKGLENPIEEYLYICRNINGKLLPEEGVSTPFKRRLIKAMIPFAPMPLGSAGVEEYVKALKTRNSSEFHLVKGFRYLIQDKPPLTISDPHFVSSFQWLDSNGYVFDLGIDMRSGGLWQFKETLEVFKKVPNLKYIINHLTKPCLDFDPETIDSNPDFLSWKRLVTEMYITTPNSYMKLSGGFSEVEQDVALDVTSTSRHVYPWFKVVYELWGPERTIFASNWPVCAIPAGQNLTEKWFQVCETLFDSIGMDEDTRRKIYYSNAFKAYNI | Cofactor: Divalent metal cation.
Function: Hydrolase with high substrate specificity for L-rhamnono-1,4-lactone. Catalyzes the second step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.
Catalytic Activity: H2O + L-rhamnono-1,4-lactone = H(+) + L-rhamnonate
Sequence Mass (Da): 38836
Sequence Length: 336
EC: 3.1.1.65
|
Q7LYJ6 | MVKLVATLGTSPGGVIESFLYLVKKGENIDEVRVVTTSNAEVKKAWRIVRLMFVCCIQEKFPKVEISEHPLDIEDIYSEDDLRKVREFVEKQLGEGDYLDITGGRKSMSVAAALAAKNKGVKIITSIIPQDDYNKISKKVRELKEIPEIKNRGECRQEMKETYCSLIVQDARSIEFEI | Cofactor: Does not require a metal cofactor.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (Probable). A nuclease that degrades cyclic oligoadenylates (cOA), second messengers that induce an antiviral state important for defense against invading nucleic acids. Destruction of cOA deactivates the Csx1 ribonuclease, preventing uncontrolled degradation of cellular RNA. Degrades cA4 (a tetraadenylate ring) into a linear diadenylate product with 5'-OH and 2',3'-cyclic phosphate termini. Is 10-fold more active than SSO1393, suggesting this is the major cA4 degradation enzyme. Is highly specific for cA4; it has very poor activity on cA6 and no discernible activity against a number of cyclic dinucletides. There may be 2 active sites per homodimer .
Catalytic Activity: cyclic tetraadenylate = 2 5'-hydroxy-diadenylate 2',3'-cylic phosphate
Sequence Mass (Da): 20213
Sequence Length: 178
Subcellular Location: Cytoplasm
EC: 4.6.1.-
|
O00237 | MWLKLFFLLLYFLVLFVLARFFEAIVWYETGIFATQLVDPVALSFKKLKTILECRGLGYSGLPEKKDVRELVEKSGDLMEGELYSALKEEEASESVSSTNFSGEMHFYELVEDTKDGIWLVQVIANDRSPLVGKIHWEKMVKKVSRFGIRTGTFNCSSDPRYCRRRGWVRSTLIMSVPQTSTSKGKVMLKEYSGRKIEVEHIFKWITAHAASRIKTIYNAEHLKEEWNKSDQYWLKIYLFANLDQPPAFFSALSIKFTGRVEFIFVNVENWDNKSYMTDIGIYNMPSYILRTPEGIYRYGNHTGEFISLQAMDSFLRSLQPEVNDLFVLSLVLVNLMAWMDLFITQGATIKRFVVLISTLGTYNSLLIISWLPVLGFLQLPYLDSFYEYSLKLLRYSNTTTLASWVRADWMFYSSHPALFLSTYLGHGLLIDYFEKKRRRNNNNDEVNANNLEWLSSLWDWYTSYLFHPIASFQNFPVESDWDEDPDLFLERLAFPDLWLHPLIPTDYIKNLPMWRFKCLGVQSEEEMSEGSQDTENDSESENTDTLSSEKEVFEDKQSVLHNSPGTASHCDAEACSCANKYCQTSPCERKGRSYGSYNTNEDMEPDWLTWPADMLHCTECVVCLENFENGCLLMGLPCGHVFHQNCIVMWLAGGRHCCPVCRWPSYKKKQPYAQHQPLSNDVPS | Function: Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway.
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): 79405
Sequence Length: 685
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
|
Q6ZNA4 | MSQWTPEYNELYTLKVDMKSEIPSDAPKTQESLKGILLHPEPIGAAKSFPAGVEMINSKVGNEFSHLCDDSQKQEKEMNGNQQEQEKSLVVRKKRKSQQAGPSYVQNCVKENQGILGLRQHLGTPSDEDNDSSFSDCLSSPSSSLHFGDSDTVTSDEDKEVSVRHSQTILNAKSRSHSARSHKWPRTETESVSGLLMKRPCLHGSSLRRLPCRKRFVKNNSSQRTQKQKERILMQRKKREVLARRKYALLPSSSSSSENDLSSESSSSSSTEGEEDLFVSASENHQNNPAVPSGSIDEDVVVIEASSTPQVTANEEINVTSTDSEVEIVTVGESYRSRSTLGHSRSHWSQGSSSHASRPQEPRNRSRISTVIQPLRQNAAEVVDLTVDEDEPTVVPTTSARMESQATSASINNSNPSTSEQASDTASAVTSSQPSTVSETSATLTSNSTTGTSIGDDSRRTTSSAVTETGPPAMPRLPSCCPQHSPCGGSSQNHHALGHPHTSCFQQHGHHFQHHHHHHHTPHPAVPVSPSFSDPACPVERPPQVQAPCGANSSSGTSYHEQQALPVDLSNSGIRSHGSGSFHGASAFDPCCPVSSSRAAIFGHQAAAAAPSQPLSSIDGYGSSMVAQPQPQPPPQPSLSSCRHYMPPPYASLTRPLHHQASACPHSHGNPPPQTQPPPQVDYVIPHPVHAFHSQISSHATSHPVAPPPPTHLASTAAPIPQHLPPTHQPISHHIPATAPPAQRLHPHEVMQRMEVQRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQAPERSAWELGIEAGVTAATYTPGALHPHLAHYHAPPRLHHLQLGALPLMVPDMAGYPHIRYISSGLDGTSFRGPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYKKVTTDWFSQRKLHCKQDGEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQLPSES | Function: E3 ubiquitin-protein ligase . Required for mesoderm patterning during embryonic development (By similarity). Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP . Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP . In addition to enhance transcription of SMAD2/SMAD3 effectors, also regulates their turnover by mediating their ubiquitination and subsequent degradation, coupling their activation with degradation, thereby ensuring that only effectors 'in use' are degraded (By similarity). Activates SMAD3/SMAD4-dependent transcription by triggering signal-induced degradation of SNON isoform of SKIL . Associates with UBE2D2 as an E2 enzyme . Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates . Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair . Mediates ubiquitination and degradation of sumoylated PML (By similarity). The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) (By similarity).
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.
Sequence Mass (Da): 108862
Sequence Length: 994
Domain: The SUMO interaction motifs (SIMs) mediates the binding to polysumoylated substrate.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
|
Q99ML9 | MSQWTPEFNELYTLKVAMKSGTPDAPTTQESLKAVLLHPQPLGATKSFPAEVEMINSKVGNEFSHLCDDSQKQEKDMTGNQQEQEKSGVVRKKRKSQQAGPSYVQNCVKENQEILGRRQQLETPSDEDNDSSLSECLSSPSSSLHFGGSDTVTSDEDKEVSVRHTQPVLSAKSRSHSARSHKWPRTEADPVPSLLMKRPCFHGSALRRVTCRKRLVKSSSSQRTQKQKERMLVQRKKREALAQRKYALLSSSSSSSENDLSSDSSSSSSTDGEEDLCASASENPSNPAAPSGSIDEDVVVIEASFTPQVTANEEINVTSTDSEVEIVTVGESYRSRSTLGHSRSHWSQGSSSHTGRPQESRNRSRISTVIQPLRQNAAEVVDLTVDEDEPTIVPTTSARMDSQTTSASINNSNPSTSEQASDTTSTVASSQPSTVSETEATLTSNSATGSSVGDDVRRTASSAVPESGPPAMPRLPSCCPQHSPCGGTSQSHHALAHPHSSCFQQHGHHFQHHHHHHHTPHPAVPVSPSFSDPACPVERPQVQAPCGANSSSGSSYHDQQALPVDLSNSALRTHGSGGFHGASAFDPCCPVTSSRAAVFGHQAAAAPTQPLSIDGYGSSMVAQPQPQPPPQPSLSSCRHYMPPPYASLTRPLHHQASACHHSHGNAPPQTQPPPQVDYVIPHPVHAFHSQISSHAASHPVAPPPPTHLGSTAAPIPQHLPPAHQPISHHIPAPAPSAQRLHPHEVMQRMEVQRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQAPERTAWELGIEAGVTAATYTPGALHPHLAHYHAPPRLHHLQLGALPLMVPDMAGYPHIRYISSGLDGASFRGPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYKKVTTDWFSQRKLHCKQDGEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQLPSES | Function: E3 ubiquitin-protein ligase required for mesoderm patterning during embryonic development . Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP . Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP . In addition to enhance transcription of SMAD2/SMAD3 effectors, also regulates their turnover by mediating their ubiquitination and subsequent degradation, coupling their activation with degradation, thereby ensuring that only effectors 'in use' are degraded (By similarity). Activates SMAD3/SMAD4-dependent transcription by triggering signal-induced degradation of SNON isoform of SKIL (By similarity). Associates with UBE2D2 as an E2 enzyme (By similarity). Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates . Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair (By similarity). Mediates ubiquitination and degradation of sumoylated PML . The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) .
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.
Sequence Mass (Da): 107896
Sequence Length: 989
Domain: The SUMO interaction motifs (SIMs) mediates the binding to polysumoylated substrate.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
|
Q08DF2 | MPRSALSVISFCHRLGKQERKRSFMGNSSNSWSHTPFPKLELGLGSRPTAPREPPACSICLERPREPISLDCGHDFCPRCFSTHRVPGCGPPCCPECRKTCKRRKGLRGLGERMRLLPQRPLPAAALQETCAVRAEPLLLVRINASGGLILRMGAINRCLKHPLARDTPVCLLAVLGGPHSGKTFLLNHLLQGLPGLASGEGSWPRSAGSGQGFRWGANGLSRGIWMWSHPFLLGKEGRKVAVFLVDTGDVMSPELSRETRTRLCALTSMLSSYQILTASQELKDTDLEHLETFVHVAEVMGRHYGMVPIQHLDLLVRDSSHPSKAWQGHVGDVIQKSSGKYPKVQGLLQGRRARCYLLPAPGRRWASRGHGSSGDDDAGRLRAYVADVLSAAPQHAKSRCPGYWSEGRPAARGDRRLLTGQQLAQEVKNLSGWMGRTGPSCASPDEMAAQLHDLRTVEAAKKEFEEYVRQQDAATKRIFSALRVLPDTMRNLLSAQKDTLLARHGATLLCTGREQTLEALEAELQAEAKAFMDSYTVRFCGHLAAVGGAVGAGLMGLAGGVVGAGMAAAALAAEAGMVAAGAAVGATGAAVVGGGVGAGLAATVGCMEKEEDERVQEGDREPLLQEE | Function: E3 ubiquitin-protein ligase that plays an important role in neuronal differentiation, including neurogenesis and gliogenesis, during brain development. During embryonic development initiates neuronal differentiation by inducing cell cycle arrest at the G0/G1 phase through up-regulation of cell-cycle regulatory proteins. Plays a role not only in the fetal period during the development of the nervous system, but also in the adult brain, where it is involved in the maintenance of neural functions and protection of the nervous tissue cells from oxidative stress-induced damage. Exhibits GTPase and E3 ubiquitin-protein ligase activities. Regulates dendritic spine density and synaptic neurotransmission; its ability to hydrolyze GTP is involved in the maintenance of dendritic spine density.
PTM: Auto-ubiquitinated.
Location Topology: Multi-pass membrane protein
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.
Sequence Mass (Da): 67392
Sequence Length: 628
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
EC: 2.3.2.27
|
Q96DY5 | MPRPVLSVTAFCHRLGKRESKRSFMGNSSNSWVLPREEAQGWMGQAVQGGTRTSRSHASFPKLELGLGHRPSPTREPPTCSICLERLREPISLDCGHDFCIRCFSTHRIPGCELPCCPECRKICKQRKGLRSLGERMKLLPQRPLPPALQETCAVRAERLLLVRINASGGLILRMGAINRCLKHPLARDTPVCLLAVLGEQHSGKSFLLDHLLSGLPSLESGDSGRPRAEGSLPGIRWGANGLTRGIWMWSHPFLLGKEGKKVAVFLVDTGDVMSPELSKETRVKLCALTMMLSSYQILNTSQELKDTDLGYLEMFVHVAEVMGKHYGMVPIQHLDLLVRDSSHHNKSGQGHVGDILQKLSGKYPKVQELLLGKRARCYLLPAPERQWVNKDQASPRGNTEDDFSHHFRAYILDVLSTAPQHAKSRCQGYWSEGRAVARGDRRLLTGQQLAQEIKNLSGWMGKTGPSFNSPDEMAAQLHDLRKVEAAKKEFEEYVRQQDIATKRIFSALRVLPDTMRNLLSTQKDAILARHGVALLCKEREQTLEALEAELQAEAKAFMDSYTMRFCGHLAAVGGAVGAGLMGLAGGVVGAGMAAAALAAEAGMVAAGAAVGATGAAVVGGGVGAGLAATVGCMEKEEDERVQGGDREPLLQEE | Function: E3 ubiquitin-protein ligase that plays an important role in neuronal differentiation, including neurogenesis and gliogenesis, during brain development. During embryonic development initiates neuronal differentiation by inducing cell cycle arrest at the G0/G1 phase through up-regulation of cell-cycle regulatory proteins . Plays a role not only in the fetal period during the development of the nervous system, but also in the adult brain, where it is involved in the maintenance of neural functions and protection of the nervous tissue cells from oxidative stress-induced damage . Exhibits GTPase and E3 ubiquitin-protein ligase activities. Regulates dendritic spine density and synaptic neurotransmission; its ability to hydrolyze GTP is involved in the maintenance of dendritic spine density .
PTM: Auto-ubiquitinated.
Location Topology: Multi-pass membrane protein
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.
Sequence Mass (Da): 71275
Sequence Length: 654
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
EC: 2.3.2.27
|
O17917 | MDLFRKPKKRNAPVVRKKESSSDEDQDSEVKDVIQKRRRTNPMVQSTKQLDASTRRADNSSDDSDDSDDNQDIAVATHSFAASGDAGPSGPRDQGATATLEVDTDYSHDAQAQFERVQQQLKEGVEKDGKILYKGSALYGAKEAKDTAKGNAASGYNRVGPVRAPQFLRQTVRWDFAPDICKDYKETGFCTFGDSCKFVHDRSDYKHGWEIDEEYEAGKYGAEDDANYEIHEGDDTFPEDCFICGNPFVDPIVTKCKHYFCTGCALKSFQKSSKCPICQQNTENIMNTAKELLTYLKRKKQQQKQEAEKQEEEKDSDDDEKPHECDDHHHHDHEDEPEEPENDSNVPEAEEKSDEEQEIMMEDVEGLEGGENDSESDDDDAEKD | Function: May function as E3 ubiquitin-protein ligase that catalyzes the transfer of ubiquitin onto target proteins. May play a role in DNA repair via its role in the synthesis of 'Lys-63'-linked polyubiquitin chains that recruit proteins involved in repair to sites of DNA damage by alkylating agents.
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.
Sequence Mass (Da): 43428
Sequence Length: 384
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
|
Q9Y508 | MAAQQRDCGGAAQLAGPAAEADPLGRFTCPVCLEVYEKPVQVPCGHVFCSACLQECLKPKKPVCGVCRSALAPGVRAVELERQIESTETSCHGCRKNFFLSKIRSHVATCSKYQNYIMEGVKATIKDASLQPRNVPNRYTFPCPYCPEKNFDQEGLVEHCKLFHSTDTKSVVCPICASMPWGDPNYRSANFREHIQRRHRFSYDTFVDYDVDEEDMMNQVLQRSIIDQ | Function: E3 ubiquitin-protein ligase that promotes the ubiquitination of various substrates . In turn, participates in the regulation of many biological processes including cell cycle, apoptosis, osteoclastogenesis as well as innate or adaptive immunity . Acts as negative regulator of NF-kappa-B-dependent transcription by promoting the ubiquitination and stabilization of the NF-kappa-B inhibitor TNFAIP3 . May promote the ubiquitination of TRAF6 as well . Acts also as a negative regulator of T-cell activation . Inhibits cellular dsRNA responses and interferon production by targeting MAVS component for proteasomal degradation . Ubiquitinates the CDK inhibitor CDKN1A leading to its degradationand probably also CDKN1B and CDKN1C . This activity stimulates cell cycle G1-to-S phase transition and suppresses cellular senescence. May play a role in spermatogenesis.
PTM: Autoubiquitinated. Polyubiquitinated in the presence of E2 enzymes UBE2D1, UBE2D2 and UBE2D3, but only monoubiquitinated in the presence of UBE2E1.
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.
Sequence Mass (Da): 25694
Sequence Length: 228
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
|
Q9ET26 | MAAAQPESRDGAAQSAKPASETDPLSRFTCPVCLEVFEKPVQVPCGHVFCSACLQECLKPKKPVCGVCRSALAPGVRAVELERQIESIETSCHGCRKNFILSKIRAHVTSCSKYQNYIMEGVKATTKDASLQPRNIPNRYTFPCPYCPEKNFDQEGLVEHCKLTHSTDTKSVVCPICASMPWGDPSYRSANFMEHIQRRHRFSYDTFVDYDVDEDDMINQVLQRSIIDQ | Function: E3 ubiquitin-protein ligase that promotes the ubiquitination of various substrates. In turn, participates in the regulation of many biological processes including cell cycle, apoptosis, osteoclastogenesis as well as innate or adaptive immunity. Acts as negative regulator of NF-kappa-B-dependent transcription by promoting the ubiquitination and stabilization of the NF-kappa-B inhibitor TNFAIP3. May promote the ubiquitination of TRAF6 as well. Acts also as a negative regulator of T-cell activation. Inhibits cellular dsRNA responses and interferon production by targeting MAVS component for proteasomal degradation. Ubiquitinates the CDK inhibitor CDKN1A leading to its degradationand probably also CDKN1B and CDKN1C. This activity stimulates cell cycle G1-to-S phase transition and suppresses cellular senescence. May play a role in spermatogenesis.
PTM: Autoubiquitinated. Polyubiquitinated in the presence of E2 enzymes UBE2D1, UBE2D2 and UBE2D3, but only monoubiquitinated in the presence of UBE2E1.
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.
Sequence Mass (Da): 25745
Sequence Length: 229
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
|
V9GZ92 | GILSSFKGVAKGVAKDLAGKLLETLKCKITGC | Function: Antibacterial peptide with amphipathic alpha-helical structure. Active against E.coli ATCC 25726 (MIC=4-5 uM) and S.aureus ATCC 25923 (MIC=8-10 uM). Has a weak hemolytic activity on human erythrocytes (LC(50)=150-160 uM).
Sequence Mass (Da): 3250
Sequence Length: 32
Domain: The structure is characterized by a full length helix-turn-helix conformation between residues Ile-2-Leu-21, Leu-22-Leu-25 and Lys-26-Thr-30, respectively.
Subcellular Location: Secreted
|
Q8SPN4 | MALDKSVILLPLLVVVLLVLGWAQPSLGRESRAKKFQRQHMDSGSSPSSSSTYCNQMMKRRNMTQGRCKPVNTFVHEPLVDVQNVCFQEKVTCKNGQTNCFKSNSKMHITDCRLTNGSKYPNCAYRTSPKERHIIVACEGSPYVPVHFDASVEDST | Function: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity).
Catalytic Activity: an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].
Sequence Mass (Da): 17498
Sequence Length: 156
Subcellular Location: Secreted
EC: 4.6.1.18
|
O18937 | MVPKLFTSQICLLLLLGLLGVEGSLHAAPQKFTRAQWFSIQHIQTTPLRCTNAMRAINKYQHRCKNQNTFLHTTFAAVVNVCGNTNITCPRNASLNNCHHSRVQVPLTYCNLTGPPTITNCVYSSTQANMFYVVACDNRDQRDPPQYPVVPVHLDTTI | Function: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities.
Catalytic Activity: an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].
Sequence Mass (Da): 17714
Sequence Length: 158
Subcellular Location: Lysosome
EC: 4.6.1.18
|
Q8Z023 | MYKLLMFRDDKLLRRALTHRSYVNENPEEGEHNERLEFLGDAILNFLSGEYLYRSHPDRGEDELTRRRSALVDEKQLAKFAIEVGLDFKMRLGKGAIRDGGYQNPNLLSSTFEAVIGAYYLDNNSNIEAVRAIIEPLFESVPEQIVVVRSNVDSKNRFQEWVQRNIGPTPPKYLTEQIGGFSHAPEFKATVLVGEKEYGEGIGKNKKDAEKAAAENALANLNKQELLP | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 25872
Sequence Length: 228
Subcellular Location: Cytoplasm
EC: 3.1.26.3
|
O74919 | MAYNHFSIPKNIEEKENSFFDVTFQDEPDETTSTATGIAKVSIPTPKPSTPLSTLTNGSTIQQSMTNQPEPTSQVPPISAKPPMDDATYATQQLTLRALLSTREAGIIIGKAGKNVAELRSTTNVKAGVTKAVPNVHDRVLTISGPLENVVRAYRFIIDIFAKNSTNPDGTPSDANTPRKLRLLIAHSLMGSIIGRNGLRIKLIQDKCSCRMIASKDMLPQSTERTVEIHGTVDNLHAAIWEIGKCLIDDWERGAGTVFYNPVSRLTQPLPSLASTASPQQVSPPAAPSTTSGEAIPENFVSYGAQVFPATQMPFLQQPKVTQNISIPADMVGCIIGRGGSKISEIRRTSGSKISIAKEPHDETGERMFTITGTHEENEKALFLLYQQLEMEKDRRSH | Function: Binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression suppresses the Cl(-) sensitivity of calcineurin deletion.
PTM: Phosphorylated by pmk1. Phosphorylation causes enhancement of the RNA-binding activity.
Sequence Mass (Da): 43377
Sequence Length: 398
Subcellular Location: Cytoplasm
|
P74368 | MNHPDFPPIGDPQLKLEALTHRSYCNEHPGTPSYDRLEFLGDAVLGFVVGRILFERYPHFTEAELTRLRSQLVNQNQLAYLARFLHIAPEIRLSQSLARDDGQSSPSILADVFESLLGAALLDRGLTAVEDFIQELFVPILEQWEKSQDGRSPKLVPTMDVKSMLQQWALAKTKQLPEYELINTSGPPHAQEFTFTVKVAGKIHGQGSGPSKQIATKQAALEALKSLGLLQ | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 25712
Sequence Length: 231
Subcellular Location: Cytoplasm
EC: 3.1.26.3
|
P00652 | MLYNKLITIAALLVPALAAPQGLDVRDCDYTCGSHCYSASAVSDAQSAGYQLYSAGQSVGRSRYPHQYRNYEGFNFPVSGNYYEWPILSSGSTYNGGSPGADRVVFNDNDELAGLITHTGASGNGFVACSGW | Catalytic Activity: [RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment].
Sequence Mass (Da): 14064
Sequence Length: 132
Subcellular Location: Secreted
EC: 4.6.1.24
|
Q55637 | MSLLPHRQTQLKALLRRLGLTDNTPVDWNLVDLALTHASQSPEQNYQQLEFVGDAVVRLASAEVLMKHYPQTSVGEMSALRAILVSDRTLAGWGELYGLDRFLWITPAVLADKNGRVSLMADSFEALLGALYLSVGDLSLIRPWLSEHLLAKATEIRQDPALHNYKEALQAWTQAHYKCLPEYRVEPLDQNLPQQSGFQATVWLGDQPLGSGSGSSKKSAEQAAAQQAYQDFIAKEILPMPKIN | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 27106
Sequence Length: 244
Subcellular Location: Cytoplasm
EC: 3.1.26.3
|
Q2GFE4 | MIESISKIIKYNFKNPQLLNEALTHPSLVSKDTLKFNYERLEFLGDAVLNIVISEMLFNIFPKDTEGNLAKKKTALVCGNKLVEVAQSINLGQFIMMSDGERACGGINNFRNLENALEALIGAIYLDGGFTAAQDFIYLFWEHSATHMNVPPQDAKTILQELVQGKRLPAPAYHTIDKSGPDHNPTFTVEVRIPSYQAIQATGHNKKLAEQKAASLMLNQIHNKTK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 25200
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 3.1.26.3
|
A0Q7W6 | MVPEYSRFYNILGYNFKDYTLLIRALTHRSKTKKNYERLEFLGDSVLSFVIAEVLYKQFTDLAEGKLSQLRSKLVKGTTLAQLASSLKMDEYIILGASEQGGHKREKILEDVFEAVIGAIYLDSDFATVKKVILKWYQPIISSINLDTIKVKDSKSKLQEILLQNALSLPEYSIETIDGKDHEQQFTVVAMSKDLNLRVKAQGTSRKKAEQKAAEKMIEMLSQQGLHEKK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon (By similarity).
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 26229
Sequence Length: 230
Subcellular Location: Cytoplasm
EC: 3.1.26.3
|
A6U7A8 | MKGRSLNAEDRARLEAAIGYQFAEKERLDRALTHSSARSGRAINYQRLEFLGDRILGLCVAELLFQTFSDANEGELSVRLNQLVSAESCAKVADELSLHEFIRTGSDVKKITGKHMMNVRADVVESLIAAIYLDGGLEAARRFVLEHWTHRAASADGARRDAKTELQEWAHARFGVAPKYRTEDRSGPDHDPRFTVTVEVDGIDPETGVDRSKRGAEQVAAMKLLEREGVWQKRSAGN | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 26522
Sequence Length: 238
Subcellular Location: Cytoplasm
EC: 3.1.26.3
|
Q027L3 | MRAEPALLELKLDYRFNDPELLRRALTHSSLANENRPGAGVGSPLNDNEQLEFLGDSVLGFLIAEALVRRFPEYHEGDLSRLKAHLVSAAHLHGVARRLDLGSYLELGRSEEMSGGRTKKTLLVDGLEAIMAAIYLDGGVDAARAFVATHVLDAPFFGDEEAGTDIQPAITNFKSALQELAQTRRLPQPRYSVVRERGPEHSKTFTVEVRVGKEWTAQAEGRTKKIAAQRAARGLYERLMGDPIVPLPDDSPGDSPDDSGDAAESGVISAT | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 29496
Sequence Length: 271
Subcellular Location: Cytoplasm
EC: 3.1.26.3
|
Q1GTU3 | MSDPLNTEALADIIGCIPDDLTLYDLALTHGSTGRADYQRLEFLGDRVLGLVLASELYTRFPAASEGEMSSRLHVLASGATCAAIAQRLDLPALIRFGAQARSDGGRHSDNIAADAIEALIGALFLERGIEAARTFILAQWGALIDGQQAAPKHPKAALQEWALARGRRPPEYEIVSREGPDHAPRFRIAVSIGKLARAEAQGASKQAAEKAAAAALLAELEGQEK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 24045
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 3.1.26.3
|
Q53844 | MQFINKQSEQLFIELKAFFKQYHVFIKERQYYLEALTHNSYANEHNLSYTYQRMEFLGDAILAKEISLYLFLSFPDKNEGEITNLRSKIVREGTLAELVRRMNWAPFLLLGKGEIKTKGYEKNRILADIYESMIAALYLDLGEDVVRTFINNTLIRMVSNPGFFDKIRDYKTELQEFLQAGDARTLEYKLIKESQPLEGNRVLYTVVAEIGGIRYGEGCGYTHKEAEQLAARDALQKLATKSKYHFEK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 28931
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 3.1.26.3
|
A7HYE5 | MEIITTNEALRAACDRLSTAGFVTVDTEFMRDATFWPILCLIQLAGPSDELIVDPLAPDLDLAPFYALMKNRNVVKVFHAARQDIEIFCHEGKAIPDPLFDTQVAAMVCGFGDSVGYETLVRKLAGGSVDKSSRFTDWSRRPLSDKQLQYAMADVTYLRTIYEVLAKRLTHTKRAHWVAEEMAVLQDPETYAMRPENAWKRVKARFRGQRGLAVLVEVAAWRERQAQERDLPRSRVMKDDALAEIATQIPRTISDLDGLRAVPKGFSNSRSAASLMEAVERGLAMKEEDIPVVEGPEPLPPGIGPLVELLKVLLKIKCEEHDVAQKLVANVADLELIAAHSEADVGALKGWRRELFGEDALRLKRGELAIGVKGKRIVLIETKR | Function: Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
Catalytic Activity: Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
Sequence Mass (Da): 42837
Sequence Length: 384
Subcellular Location: Cytoplasm
EC: 3.1.13.5
|
A6V8R6 | MFVTAPEIQWIRDDASLAQQCREWRTQPYLALDTEFMRVDTFYPAAGLVQVGDGRREWLIDPLLVRDWGPFAELLEDPRVVKVLHACSEDLEVFLRLTGSLPVPLFDTQLAAAYLGMAHSMGYSKLVKEVLDIDLPKDETRSDWLQRPLTEMQMRYAADDVQHLAQVYLALDARLSEEKRAWLLEDGAELVANLCRESDPREAYREVKLGWRLRPQQLAVLRELCAWREEQARLRNRPRNHVLRERTLWPLARLLPKNKTDLAAIEDMHPRTVRQDGDFLIELIAEAARLPQSEWPEALPEPLPPEVTPLLKSLRAIGQREAETLGMAPELMLRKKILEALLKSGYPHGPYELPDSLRGWRRERMGQALLNALESA | Function: Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
Catalytic Activity: Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
Sequence Mass (Da): 43331
Sequence Length: 376
Subcellular Location: Cytoplasm
EC: 3.1.13.5
|
A1SVE6 | MQFEIITTTAQLHDFIATLDGSPISLDTEFVRTRTYAANLGLLQISQNTQITLIDPIAVGDLSSFWQAIDNKNIILHASSEDLEIIRDHKGDLNFTLFDTQIACSFLNMGASLGYAKMVETLEAVIVDKGESRTDWCARPLSEKQINYAGVDVLYLQPCLEKLQQQLENKKMFPFFEQECQSVLAQKMVKQDPDKAYKLLNNLFKLDRQGLAIIKALAKWRLLTAQERNLALNFVVKADHLWLLAYYQPTSLDDLRRLNLLPNEIRIHGQQILTIMTQVISQDESTYPPLVNRLVDFPAYKSTVKSMRDKIQLCAEKYDLPLELLASKRVINEYLSWLWKLTNLQRQTANKPKLLTGWRFELIGHQFEH | Function: Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
Catalytic Activity: Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
Sequence Mass (Da): 42462
Sequence Length: 369
Subcellular Location: Cytoplasm
EC: 3.1.13.5
|
A0KXU5 | MSRLLFLWTVLNPQELEKNLSVFQYVSDEASLNALVAQYQQSPLLVLDTEFVRTRTYYAKLGLIQAYDGKTLALIDPVALPDLSAFWSLLDNPNIIKLVHSCSEDLEVFAHYGQRQPTPLFDSQIAASLCGMGHGLGYAKLVETCLGEVIDKGESRTDWMRRPLTEAQLSYAANDVLYLYQLYPQLADKLKAQDRLGWLYEEGERMTEGRLATPDMDTAYLRVKNAFQLTEHQLAYLKVLAKWRLEKALARDLALGFVIKDHGLIALAKKQPKSMGDLLKLNDLTEQEKRIHGKDILRVMQTADLSNPPELVDVLALKPGYKSAFKNIKTCLSELCEQHAIPMEMLGSKRHIHEYLQWRWDKQQGELPTVLSGWRGQIAAESLAKLDV | Function: Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
Catalytic Activity: Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
Sequence Mass (Da): 44034
Sequence Length: 388
Subcellular Location: Cytoplasm
EC: 3.1.13.5
|
D4Z694 | MQIHPLITDSKTLAQFCARIAKSPYIAVDTEFMRENSYWPDLCLVQVADEHEAAAIDPKAPGLDLSPLLDLMVDNEDVLKVFHAGGQDLEIIYNLTGKTPHPLFDTQIAAMALGLGEQIGYGNLVDAWLGVQLDKGARFTDWARRPLDKRQIDYAIGDVTYLIQIFPKMLEELRRTGRGDWLDQEMERISDPSNYENKPEEAWQRVRIASRKADVLGRLKALAAWREMEAQDKNLPRGRIVKDETLADIASHPPRTQEDLGKVRGLSATWKTNDIGNRLMLALASHAPLAKEEMPERDPKRPGLGKDGALVADLLKLLLKIRSRDINVAARLIARSDDIDALAAGVREDLAILEGWRYEQFGRDAVDLVEGRLAFAVKNGRLKMTRTQ | Function: Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
Catalytic Activity: Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
Sequence Mass (Da): 43562
Sequence Length: 388
Subcellular Location: Cytoplasm
EC: 3.1.13.5
|
Q5GZ75 | MPHWITHPSELTDRLQAARPARIGLDTEFIRERTYWPQLALVQMAIGEEILLIDPLIPGMNAALKEWLTATDIVKVMHSASEDLVTFKCACGVLPRPLFDTQIAAALAGVGGGMGYQKLVQEVTGTLLTKGETRSDWMRRPLSPSQLEYAADDVRYLFAIHDELTRRLTEQNRLGWLAEDAERLLATVEHDDGERWPHVSLRTAQFLEPAAQRRLLRLLRWRDLQARQSDRPRSWILDNEVASQLARFPPADLDALLQQFDKFPKAPRKLANAVWDALNTPLPDEEHAPLAQAATDGNKAVLKRLQDTVAQRSHELGLPDGLLASRRHLETLIEQRSWPAALGQWRRAVLEAQVMPLLEASEA | Function: Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
Catalytic Activity: Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
Sequence Mass (Da): 40983
Sequence Length: 363
Subcellular Location: Cytoplasm
EC: 3.1.13.5
|
F4IV66 | MDVTEVPWRRLPQFSVSSRASWLVSSGFPLSSYMFSHVERGKTFRLTLCFGVSRLRPRSAIPLRFLLSVFSEQPPSRLKGLCEVVWIVEADLAANEHLYVTGDPSTLGSWEPDCAISMYPTENDNEWEAKVKIASGVNFRYNYLLKAGYGSSSDVIWRPGPQFSLSVPSSVNQDRKIIIRDSWMSMSISSKSQESYGWGSWIDDAYLFPNCVTPAQSEDECTSADSAIEVPRTHLNDKQVGAESFLCDELAAFSSENSNLSALFSDNYQPIEEPWLIQESITLQHERNMQTDSEQDVESCDDNENNLNTDEQNHQLTETLLPDGGFFQSESIATTILINSSICTVQRIAVLEGGKLVELLLEPVKTNVQCDSVYLGVITKFVPHMGGAFVNIGSARHSFMDIKSNREPFIFPPFCDGSKKQAADGSPILSMNDIPAPHEIEHASYDFEASSLLDIDSNDPGESFHDDDDEHENDEYHVSDHLAGLVNGTVVNHGAVEVGSENGHIPMERGHSADSLDSNASVAKASKVMSSKDNKWIQVRKGTKIIVQVVKEGLGTKGPTLTAYPKLRSRFWVLLTRCKRIGVSKKISGVERTRLKVIAKTLQPQGFGLTVRTVAAGHSLEELQKDLDGLLLTWKNITDEAKSAALAADEGVEGAIPALLHRAMGQTLSVVQDYFNDKVEKMVVDSPRTYHEVTHYLQDMAPDLCNRVELHDKGIPLFDLYEIEEEIEGILSKRVPLSNGGSLVIEQTEALVSIDVNGGHGMFGQGNSQEKAILEVNLAAARQIAREIRLRDIGGIIVVDFIDMADESNKRLVYEEVKKAVERDRSLVKVSELSRHGLMEITRKRVRPSVTFMISEPCSCCHATGRVEALETTFSKIEQEICRQLAKMEKRGDLENPKSWPRFILRVDSHMSSFLTTGKRTRLAILSSSLKVWILLKVARHFTRGTFEVKPFMDEKTVNERQHQVAISLLKKADAIADSSGKKKLTLIPIKKEKTSGKQRR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in intercistronic processing of primary transcripts from chloroplast operons. The endonucleolytic activity of the enzyme depends on the number of phosphates at the 5' end, is inhibited by structured RNA, and preferentially cleaves A/U-rich sequences.
Sequence Mass (Da): 111552
Sequence Length: 1001
Subcellular Location: Plastid
EC: 3.1.26.-
|
P57429 | MKRMLINATQQEELRVALVDGQRLYDLDIEHSGSEQKKSNIYKGKITRIEPSLEAAFVDYGEEKNGFLPLKEISKNYFPENHIETLGFNIKNVLQEGQEVIVQISKEERGTKGAALTTFISLAGSYLVLMPNSPKSGGISRRIEGNDRIALKELLTLLELPEEMSLIIRTAGAGKSIESLRWDLSLRLQHWKTIQIIAKSRTAPFLIHQESNIIVRAFRDYLRQDIGEILIDNPKILDLARKHITFLGRPDFVNKIKLYSGEVPLFSYFQIETQINSAFQRKVRLPSGGSIMVDSTEALTAIDINSSRSTSGTDIASTAFNTNLEAVDEISRQLRLRDLGGLIVIDFIDMSAISHQRAIENRLREIARDDRARIQIGQISRFGLLEMSRQRLSSSLGESSHHICPRCTGTGTIRDNESLSLSILRLIEEEALKENTYEVRAIVPVEIACYLLNEKRDAVHAIEKRQAGGKTIIVPSKKMKTPHYSVSRIRKSESKNYTRYGLSNIRQSKITSFLKKNLLKKKQKEILDVANFNFYDNCYNKIQEAQENILKKNNYNNILLKVLSNNRNFIFKMITWFKNSFFIKNMLITSDIFKKNTLKNTNNIFFKKKYSSLNKKNNNQKKRVILSKLFEANIENIPLKNKKLDTSSANYLYDNIERKKNITKKNDLIQKNIHENSYLKHVLMNRYNVINIINNNYIFYKIFNRTKIFKNQNTNNSFLKFSSVTSPIFIFSSVFSLELALGKVWIKYPIAILDETKKQKKLNRKQILHISSISETNTIVNKNNYSGIKKIKHETYSFKKYVKNNIQNQEVTQSQLIKRTKKRNVFILDKKNFLYKRTCNRKNKIHQSSAPITKISKQSDLNKKEKEFHYNLSMMKSSLRGKNSAGVHSATNFSNSPVSKLK | Cofactor: Binds 2 Zn(2+) ions per homotetramer.
Function: Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.
Catalytic Activity: Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 104007
Sequence Length: 902
Subcellular Location: Cytoplasm
EC: 3.1.26.12
|
Q89AH3 | MRRMLINAIEIKKLRIALIDGQQLYDLNVENIDKKQRKSNIYKGKIVRIEPSLEAAFVDYGEKKNGFLPLKEISRNYFPNNCSNYRHLHIKNILKEGQECIVQIDKEERGTKGALLTTFISLAGNYLVLMPNCPHLEGISRKIEGIDRFHLKKIISMLMVPENMGIIIRTSGVGRSIETLQLDLNFRVKNWYTIKKSAEINTAPCLIHKESNIVIRTLRDYLKKDIQEIIVDNPEILELARDYMFNMNCSYFEKKIKLYTGSDPLFSYYKIESQINALLRRIVKLPSGGSIIIDYTEALTAIDINSSQSTKGVNIEETAFNTNYEAVREIARQLRLRDLGGLIVIDFIDMSVLKHQKMIELHLHQVLQKDRARVQVGSISQFGLLEMSRQCLGSPLKKINHNYLFEMQKC | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs (By similarity).
Catalytic Activity: Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47312
Sequence Length: 410
Subcellular Location: Cytoplasm
EC: 3.1.26.12
|
O78453 | MSFNIIILKELGFSLVFSQSKCEYIIFQKEQCGLNDIYFGFIPRQSIYPTLNAAFVTLDSERNQGFIPFTLLIKKSNQQFVIPNSVFLIQVIKEPTINKPATLTSHIFLNSFNLNLQFSGIDCKYLNLYPNIKFLHICLITLLIPSGLDINFDHSMKDILYLDLIGQSKILYYSFSNLFTKLLRIKKMPQFIFRNSNFFLPILNKLSLSSINDFFVSSYQRAVYLRHFLITHYFTIKQTDYRILFYPTAYKSMQLYYLDMLFYRSLKPIVYTLYGIFIVICKTEALISIDVNSGSHSSRVSQNLSLHTNLIASKSIIKEIKLRNLAGVIVIDFVDMIHQKDQIHLLAFFRYLLNINSVMITLIQLSDIGLLELTRKRQDQSIYDVFQIGNISKSSFLYDRILSLNKNLFKTNLLINYTLFSNVKLIYNY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in intercistronic processing of primary transcripts from chloroplast operons. The endonucleolytic activity of the enzyme depends on the number of phosphates at the 5' end, is inhibited by structured RNA, and preferentially cleaves A/U-rich sequences.
Sequence Mass (Da): 50078
Sequence Length: 429
Subcellular Location: Plastid
EC: 3.1.26.-
|
P44443 | MKRMLINATQKEELRVALVDGQRLFDLDIESPGHEQKKANIYKGKITRVEPSLEAAFVDYGAERHGFLPLKEIAREYFPDDYVFQGRPNIRDILVEGQEVIVQVNKEERGNKGAALTTFVSLAGSYLVLMPNNPRAGGISRRIEGDERTELKEALSSLDVPDGVGLIVRTAGVGKSPEELQWDLKVLLHHWEAIKQASQSRPAPFLIHQESDVIVRAIRDYLRRDIGEILIDSPKIFEKAKEHIKLVRPDFINRVKLYQGEVPLFSHYQIESQIESAFQREVRLPSGGSIVIDVTEALTAIDINSARSTRGGDIEETALNTNLEAADEIARQLRLRDLGGLVVIDFIDMTPIRHQREVENRIRDAVRPDRARIQISRISRFGLLEMSRQRLSPSLGESSHHICPRCQGTGKVRDNESLSLSILRLLEEEALKENTKQVHTIVPVQIASYLLNEKRKAISNIEKRHNVDIIVAPNEAMETPHFSVFRLRDGEEVNELSYNLAKIHCAQDENTEESLLSRNVETTAVIEQPAVESAVVALSISEAAPTPVERKSNEPSLLAKIIAKIKGLFATKSEENKPKNNRTSRNPNRNQRRSQDRRSSRRPRSENNETERTEEQVRNVRERNQRRPRRNLVEESIAESAVNSTPVFEAKEERTEPVTQRRQRRDLRKRVRVEDNETVVENNFSTTEKMPEVDVITVQNNDEKPVHQNQRSERQERQRRTPRHLRAANNQRRRRDQEPKSPMPLFAAVVSPELASGKAWIDYSTVNLPKENHFLSVDELLEQEKTKKGFITPAMGIVVEEKSPDVKPALDFITQPANESVQKKVQESLDRLSSYKPQEVVESIDPAINVDEPETLEKVSKFVRTYEFNGRLGTISSVPHTKAEMTLAKANDEMPEDFPIRAWQDSRYYFYGKGAAGHHCAISHVYSEPTRTKSE | Cofactor: Binds 2 Zn(2+) ions per homotetramer.
Function: Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.
Catalytic Activity: Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 106584
Sequence Length: 935
Subcellular Location: Cytoplasm
EC: 3.1.26.12
|
Q9TL10 | MLVVGNRIVDVSRHTSIGTIVIATVDKLAPGLGIAFVSWTHGQGKGGLPSTKKHYGILPLRSWRGRGPLDFATTHELTGENLILQHGDFVLVQIVQDGNHAKVHLVSGHIALTTSRLVVWPGLSSKDWIFSHQIGQKINNYLHVRKLVSYMRRDQILCTGPQRWMKEQYALEHQWENFVLEFIEQPTGISYLTSMTEKFVSPVCAEWFQHPLSVWIIGCNLQIRESMTKWMITHVPHKSRHIEITTLDAWKNWYNLHRAAIVQPQIPLRSGGTMIIEFTEIGWSFDINSGIGLEIGSKTCANEEAIYAIAQQILLRSMHGFILIDFIGDIDLEKLRVNLIQFTSLLEQDSYHIRIISISADGLVCVIRHRRSKLI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in intercistronic processing of primary transcripts from chloroplast operons. The endonucleolytic activity of the enzyme depends on the number of phosphates at the 5' end, is inhibited by structured RNA, and preferentially cleaves A/U-rich sequences.
Sequence Mass (Da): 42619
Sequence Length: 375
Subcellular Location: Plastid
EC: 3.1.26.-
|
Q8YP69 | MPKQIIIAEQHQIAAVFSEDQIQELVVATGHHQIGDIYLGVVENVLPGIDAAFVNIGDPERNGFIHVTDLGPLRLKRTAAAITELLAPQQKVLVQVMKEPTGTKGPRLTGNITLPGRYVVLMPYGRGVNLSRRIKSESERNRLRALAILIKPAGMGLLVRTEAEGKPEEAIIEDLEVLQKQWEAIQQEAQSTRAPALLNRDDDFIQRVLRDMYGADVNRIVVDSSTGLKRVKQYLQNWSGGQTPQGLLIDHHRDRSPILEYFRINAAIREALKPRVDLPSGGYIIIEPTEALTVIDVNSGSFTRSATARETVLWTNCEAATEIARQLRLRNIAGVIVVDFIDMESRRDQLQVLEHFNKALRADKARPQIAQLTELGLVELTRKRQGQNIYELFGDTCPACGGLGHTVRLPGETENRLPTPAAEVPERFVSLPTREPRLPTARTTEPRETYDGFGEAFENDSDLGALNLINHPSYQELNDNNKRRARTRRSRIGINGTNGKDEQRITANPLAFISESDLDLDGDVELSAPPELPTPNLGKSGWIERAERTKVIKTEPVKPVVEPPEIRTVEMTPEEQDIFALMGISPLIKLEQEVKNPKSVIINIVQPGQTPTIPTEITPEPVAKVTPSVEVNTPKVKLESKSVSVAATEPIKLTETMEESEVNAASTANRRRRRRSSASDSDTGEDS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endoribonuclease that plays a central role in rRNA and tRNA processing and mRNA decay. Has been shown to act on 9S rRNA (the precursor of 5S rRNA).
Catalytic Activity: Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions.
Sequence Mass (Da): 76169
Sequence Length: 687
Subcellular Location: Cytoplasm
EC: 3.1.26.12
|
A0L5G7 | MLEAVSAVMSLGGMALFAGLGLGYAAKKFHVEADPVVEKLEALLPATNCGMCGHPGCGPYAQAITEGEAINLCTPGGKAVMESIAAMLGVSPAAMDDEGPKVAYIDEEACIGCTACIKVCPVDAIVGANKQSHTVIVAECTSCQLCLEPCPTDCITMQPVPENIYDWTWDKPAGPNSKALH | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Sequence Mass (Da): 18729
Sequence Length: 181
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
|
Q8TSX9 | MSSVLINSIAVLAGLGFAVGVMLVIASKVFKIDSNPLIDDVASLLPGANCGGCGFAGCAACAEAIVEQGAPVNSCPVGGFEVAKQIGALLGQEVTESEKEFPFVRCQGGNQHCTTLYDYHGVENCKVALMLCDSRKGCTYGCLGLGTCVQACQFGALSMGEDGFPVVNKALCTSCGNCIAACPNGVLTFARDSEKVHVLCRSHDKGKDVKAVCEVGCIGCKKCEKECPAGAIRVTEFLAEIDQEKCTACGACVAICPQKAIELR | Cofactor: Binds 5 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Catalyzes Na(+) transport, most probably coupled to electron transfer from reduced ferredoxin to methanophenazine and heterodisulfide reductase. Involved in heterodisulfide reduction during methanogenesis from acetate.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27352
Sequence Length: 264
Subcellular Location: Cell membrane
EC: 7.2.1.-
|
Q02QX9 | MNGVFLAIGALLPICLAGGALLGYAAVRFRVQGDPVAEQVNALLPQTQCGQCGYPGCKPYAEAIAAGDKINKCPPGGEATIRALADLLDLEPEPLDAAEETPPRVAYIREAECIGCTKCIQACPVDAIVGAARLMHTVIADECTGCDLCLEPCPVDCIEMRETPDDVRHWKWPQPSPRLIASDRERAA | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Sequence Mass (Da): 20013
Sequence Length: 188
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
|
P0CZ14 | MIAAAASMSALGLGLGYLLGAAARKFHVETPPIVEEIAKILPGTNCGACGFPGCNGLAEAMAEGNAPVTACTPGGRDVALALAEIVTVEAGADAGPIAEIEPMVAFVFEDHCTGCQKCFKRCPTDAIVGGAKQIHTVVMDACIGCDACIEVCPTEAIVSRVKPKTLKTWYWDKPQPGLVAASAETAA | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required for nitrogen fixation. Involved in electron transfer to nitrogenase .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19090
Sequence Length: 187
Subcellular Location: Cellular chromatophore membrane
EC: 7.-.-.-
|
Q8EE80 | MSTMLIAVILLTLLALFFGVLLGFAALKFKVEGNPIVDELEAILPQTQCGQCGYPGCRPYAEAIANGDKVNKCPPGGTATMEKLASLMGVEPEPLNAEAQSQVKKVAYIREDECIGCTKCIQACPVDAIIGAGKLMHTVLTADCTGCDLCVEPCPVDCIDMVPVTQNLKNWNWRLNAIPVTLIQETPHEEKRG | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Sequence Mass (Da): 20762
Sequence Length: 193
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
|
H6LC30 | METKEKVQIDWKVVFKLGLILFVISAVAACALALTNYVTAGTIEEMNVQTNTVARQEVLPKAADFEAVPAKDVEKIASEIGMEKPEELLEVYIGKSNGEVVGYTVKTGPTSGYAGEVQVLTGISADGVITGITIIKSNETPGLGAKASGVWNDQFTGKSAKEELVVVKGTTKEGSNEIQAITGSTITSKAVTSGVNMSIQVYQNLSK | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Couples electron transfer from reduced ferredoxin to NAD(+) with electrogenic movement of Na(+) out of the cell. Involved in caffeate respiration.
Catalytic Activity: H(+) + Na(+)(in) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = Na(+)(out) + NADH + 2 oxidized [2Fe-2S]-[ferredoxin]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21832
Sequence Length: 207
Subcellular Location: Cell membrane
EC: 7.2.1.2
|
Q5E6C0 | MLTTMKKSSLVLALFAIAATALVTITYALTKDQIAYQQQQQLLSVLNQVVPKEQHDNELYKACVLVKNKDALGSKQAMPIYLASLNGQHSGAAIEAIAPDGYSGNIKIIVGVDSDAMVTGVRVLSHQETPGLGDKIDIRITRWVDGFLGKTVENAEDKNWAVQKDGGQFDQFTGATITPRAVVKAVKRAVWFYKTHQEELQTLPLNCETK | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23001
Sequence Length: 210
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
|
Q8KA18 | MKSFKETIINACLMGFFSFFSLSSVIFVKNITNNQIKNIKEKQKNTLIQQVIPRVMYHSFEKKYFLIKDKLLGDQKKHNLWLLFKNKQAKVAVVESIAPDGYSGSISILVAAYLNGKIIGVRVLSHKETPGIGDKIEISISNWITKFQDMNVIDLKDKKFLLKKYGGKIEQFTGATITPQSVSNAVKRTVVFIKKIPLIFSL | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22948
Sequence Length: 202
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
|
Q89AW6 | MLKKNNKRKIFCSALVLGSFGFLAASFVSIIYVITKNKIQYQEQRYKNIIFNHIVPSNLHDNDIQRSCLILNNKLLGDKKNHYLWLAKKKQDITAVIFETIAPDGYSGIIKMVISLDIKNGKILGVRVLSHNETPGLGDKIDVNISNWITKFSGVKIFSLDERDLSLKKYGGNIDQFTGATITPLAVVNSIKRTIVLVKMLLSSKFSELTSCDNYE | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24344
Sequence Length: 216
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
|
D8GR68 | MAKDKDQNSIFAITKNLTITCFISGIIIAAVYYITSPVAAQKQVQIQNDTMRVLVNDADKFNKVNGKKDWYAAQKGNKTIAYVVPAESKGYGGAIELLVAVTPDGKVIDFSIVSHNETPGLGANASKDSFRGQFKDKKADALTVVKDKSNTKNIQAMTGATITSKAVTKGVKEAVEQVTTFTGGK | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Couples electron transfer from reduced ferredoxin to NAD(+) with translocation of H(+) out of the cell. Essential for energy conservation during autotrophic growth. Contributes to ATP synthesis during heterotrophic growth.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19810
Sequence Length: 185
Subcellular Location: Cell membrane
EC: 7.1.1.-
|
Q819W9 | MQTMTIKEAENVLKEIMNEEDDRFQLLMKDDRKGVQKLVLKWYKQKELEQKEKEKFFEMSKYENALREKGVTYIAGIDEVGRGPLAGPVVTAAVVLPEDFYIPGLNDSKKLSEAKRERFYDEIKVQAIAIGVGIVSPQVIDDINIYQATKQAMLDAVANLSCTPQHLLIDAMKLPTPIPQTSIIKGDAKSVSISAASIIAKVTRDRMMKELGGKYPEYGFEQHMGYGTKQHLEAIEVHGVLDEHRKSFAPIKDMIQK | 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): 29015
Sequence Length: 257
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q65JP3 | MKTLTVKEIKEHLQSVSDEKDPFIEQCKNDERKSVQALVDAWLKKNERLSAMREEWQAMTSFERSLRARGYQYIAGIDEAGRGPLAGPVVAAAVILKEDCEILGLTDSKKLSKQKREDYYSYIMEEAAAVGVGIADAHEIDELNIYEASKAAMLKAVQALDVAPDYLLIDAMSLAVDTEQSSIIKGDAKSASIAAGACIAKVTRDRLMDEYAEKYPLYGFEKHKGYGTKEHLNALAKYGPSPIHRRSFAPVKAHE | 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): 28301
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
O31744 | MNTLTVKDIKDRLQEVKDAQDPFIAQCENDPRKSVQTLVEQWLKKQAKEKALKEQWVNMTSYERLARNKGFRLIAGVDEVGRGPLAGPVVASAVILPEECEILGLTDSKKLSEKKREEYYELIMKEALAVGIGIVEATVIDEINIYEASKMAMVKAIQDLSDTPDYLLVDAMTLPLDTAQASIIKGDAKSVSIAAGACIAKVTRDRMMSAYAETYPMYGFEKNKGYGTKEHLEALAAYGPTELHRKTFAPVQSFR | 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): 28355
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q8A293 | MLLPYLNKDLIEAGCDEAGRGCLAGSVYAAAVILPKDFKNELLNDSKQLTEKQRYALREVIEKEALAWAVGVVSPEEIDEINILRASFLAMHRAVDQLSVRPQHLLIDGNRFNKYPDIPHTTVIKGDGKYLSIAAASILAKTYRDDYMNRLHEEYPFYDWNKNKGYPTKKHRAAIAEHGTTPYHRMTFNLLGDGQLNLNF | 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): 22708
Sequence Length: 200
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
A1URV4 | MSRNIRNVLNMSDLPPQPNFSYELDLQNQGFFHIAGVDEVGRGPLAGPVVTAAVILSKDHSLDGLNDSKKLSVQKRNRLYCEILQSALAISIASICARAIDQSDIRKATLEAMRRCVMGLAVPAHYALIDGRDIPPHLPCPAKALVKGDQRSVSIAAASIVAKVTRDRMMEHAGQVYQGYGLEKHVGYATVAHRAAIAEYGPVIGLHRYSFALIKRYKEDIS | 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): 24275
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
A9IQL1 | MYVFCICDLSKRFSLSFQPNFLCELGLQKQGFFHVAGVDEVGRGPLAGPVVTAAVILDKDRIPDGLNDSKKLSFLQRNRLYHEILQSALAASIASLCARTIDQSNIRKATLEAMRRCIIGLAVPAHYVLVDGRDIPSELPCPAMALIKGDQRSVSIAAASIIAKVTRDRMMECAGQVYTNYGLEKHVGYATLAHRRALDKYGPIVGLHRYSFAPLKERYRNDVS | 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): 24770
Sequence Length: 224
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q6MLA0 | MLFPSIIAGLKHRGIRMAKKEKIEFPKIEWRDFSPAPIIGVDEVGRGCLAGPVYAAAVIFKSDALNDLVTDSKLLSEKRREELADLILKEHIVGIGSASVEEIDEINILNASLLAMKRAVEKLGVKSGHVLVDGNKKIPNLKGFEQSTIVKGDLRVAPISAASIVAKVTRDRLMKDLGVKYPHYGFEIHKGYSTPVHKQSIVDHGPCIAHRRSFAGVKEYV | 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): 24285
Sequence Length: 221
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q7VRD2 | MCTRKYFLSKKATIVAGVDEVGCGSLVGAVVASAVLMLYPDQEQLFSGLIDSKALSNKKRLRFCNYIQKYSLHWSIGMVNVTEIDQLNIFQARLLSIKRAICNLSMIPDLVLIDGKHAPSLNKNILYQCFVKGDSRIPVISAASIIAKVTRDQAMMMLHTQYPKYGFHRNKGYATVFHLKQLDLYGPTIYHRKTFAPVKYMLSMC | 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): 23148
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
C4K435 | MTSDFIYPEAQSIAGVDEVGRGPLAGPVVTAAVILDPKNPIIGLADSKTLSKKKRMALYEEITHKALAWSLGRAESKEIDEINIFHATLLAMQRAVNALGIKTDHVLIDGHICPILSIPSSSIVKGDSKVPEISAASILAKVTRDREMEALDKVFPGYGFAQHKGYPTAFHLEKLALLGPTEQHRRSFRPVRRALISLTG | 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): 21730
Sequence Length: 200
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
P56121 | MGCVSMTLGIDEAGRGCLAGSLFVAGVACNEKTALEFLKMGLKDSKKLSLKKRFFLEYKIKTHGEVGFFVVKKSANEIDSLGLGACLKLAVQEILENGCSLVDEIKIDGNTAFGLNKRYPHIQTIIKGDETIAQIAMASVLAKAFKDREMLELHALFKEYGWDKNCGYGTKQHIEAIIKLGATPFHRHSFTLKNRILNPKLLEVEQRLI | 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): 23176
Sequence Length: 209
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
A2BL34 | MQRRRCRYAIGIDEAGRGPVIGPMVVVGVAVCSNDIDKLVALGVRDSKQLTPVVRAKLYGEILRVALHSVIVKLPPALLDAVNLNQLEVETFEYIASRIAGVHDSPEAVYVDAVGSPEKLAARLSGRLGVRVIAEPGADKTYPIVSAASIVAKVVRDAEIRMLRRLYGVRGSGYPTDPETIAWLAEEYRRNPANPPWFVRRTWSTLKRIAPGWYVEKQATTQPPRGQRSLLDYLLGEKQS | 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): 26481
Sequence Length: 240
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q5QZK7 | MICGTDEAGRGPIAGPVVAAAVILDPDNPIEGLNDSKKLSEKKREKLSLEIKEKALYWAIAQSDPDEIEAINILWASMKAMQRAVEALPVKPDMVLVDGNRVPELKVPAKAIVGGDASEQCIAAASILAKVERDRQMLKWHELYPQYEFDKHKAYGTPKHLELLEKHGPCPIHRKGFNPVKRLLANL | 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): 20690
Sequence Length: 187
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q28VF4 | MGPDFEIERELGGLVAGVDEVGRGPWAGPVTACAVVLDPMQVPDGLNDSKKLSEARRDALAMQILRVADVSLGWASVEEIDALNIRQATFLAMRRAMDGLTTPPTHALIDGNAIPPGLSCPATCVVKGDGRSVSIAAASIVAKVRRDALMKELAVMHPGYGWETNMGYGTAKHAAGLHHLGVTQYHRRSFAPIAKILCG | 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): 21062
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
A6W7V4 | MSPAGGRVPPSLRLERQFLRAGHALVAGVDEVGRGSLAGPVSVGVLVVDAATRTAPTGLRDSKLLTPAAREALAPKVRRWAVASAVGHAEPGEIDAVGIVAALRLAGRRALAQLPVPPDLVILDGNHDWLSDPREPSLLDALDGLGDPAAGLPCPAPAVTTRVKADVTCAAVAGASVLAKTTRDALMTARHEEFPHYGWAGNKGYSAPDHLEALAAHGACPQHRRSWRLPGVAAAAGVPAPRSGPGDALVDVTSDTSSPRGA | 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): 26746
Sequence Length: 262
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q2KBV7 | MKRRTPPDSPLLFDTVPLVPDFKLELKARKAGHWPVAGADEAGRGPLAGPVVAAAVILDPKRIPEGLNDSKQLSAQRREELFVQILATATVSIASSSSTRIDETDIRKASLDAMRRAICSLAIPASYVLTDGLDVPPGLDCPGQAVVKGDARSVSIAAASIVAKVTRDRMMARAHNVFPDYGFAAHAGYGTAQHRAGIEKHGPCSLHRMSFRPLRKGEDGPEMDELIPE | 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): 24535
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q92RM4 | MSRRKQPDSPLFPLQAPVPDFTFERAAHRDGFWPVAGADEAGRGPLAGPVVAAAVILDPDAIPAGLNDSKLLTAEQREALFEEILATSTVSIASSSSARIDTTDILKASLDAMRRAVHGLELAARIVLVDGRDVPPGLSCHAKAIVKGDSRSVSIAAASIVAKVTRDRMMARADATFPLYGFAHHAGYATVKHRTAIESHGPCSLHRMSFRPFRQV | 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): 23084
Sequence Length: 216
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
A5VF46 | MAGPSFDLEIAHPLPLAGVDEAGRGPLAGPVVAAAVILDRGRVPAGIDDSKKLGAEARADLCGKIREVAHVGVGIATVEEIDEINILWASMLAMERAVAALGVEPAMVLVDGNRCPRWTRPSQWVIGGDALCLSIAAASIVAKEERDRMMADYDVHHPGYGWAKNKGYGTPAHLDALARLGPSPLHRRSFAPVAQFSLFPAA | 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): 21300
Sequence Length: 202
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q2RPE1 | MPDLSLERACGGRVAGVDEVGRGPLAGPVVAAAVVIDAGRADPALLARLDDSKKLSAALRQRLATALLADPGVEVGLGEASVAEIDRINILQATFLAMGRALAKLAPPVDLALVDGNRLPPLPCPGQAVVRGDGLSLSIAAASIVAKVHRDAAMATLAQALPGYGWERNAGYGTAEHLAALDRLGATPHHRASFAPVREALARSALPGHKCVTALTFS | 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): 22260
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
A8GMJ0 | MEVDLLHFEKKYHNYIVAGIDEAGRGPLAGPVVASAVIIDNANIIHGIKDSKKLSKKKRALLYEQITSNYVWAVAIITHTEIDKINILEATKKACSIAAANLNVKPEIVLVDGNMQFSDERFISIVNGDNLSLSIAAASIIAKVTRDRLMLELSAKFPQYLWHKNSGYGTKEHLEAINKYGLSPYHRKSFKCC | 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): 21470
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
A8GVS9 | MEIDILHFEKKYPNFILAGIDEAGRGPLAGPVVAAAVIVDQNNIIAGIKDSKKLSKKKRELLYEQITANYIWATGIISHTEIDKINILEATKKACILAAENLSTKPEIVLVDGNMQFSDKRFISIINGDNLSLSIAAASIIAKVTRDRLMLELSNEFPQYLWHKNSGYGTKEHAQAIKEYGLSPYHRLSFTKALYK | 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): 21876
Sequence Length: 196
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q8EPH7 | MSQQVIVTTKEQIQKMKKYYLSQLTSTPQGAIFRAKTNNAVITAYQSGKVLFQGSAPESEASKWGNVPLNDKKKHSLEQKHSYSPQAELFTDNHIGSDEAGTGDYFGPITVAALFATKEQQLKLKQIGVRDSKHLNDTKIKQIAKEIAHLQIPYSLLLLPNGKYNKLQAKGWSQGKMKAMLHHHAIDKLLQKIDVRSLKGIVIDQFCQPPVYKKYLQSEKKTLHPNTTFITKAESHSISVAAASILARARFVNAMDELSEEAKMELPKGASAKVDQTAARLIRSKGFEELDKYAKTHFANTQKAQKLL | 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): 34433
Sequence Length: 308
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q6MDE6 | MSSLPPFVTTLDLKLAEKLLKDLQQQGFSITIPAYTRFSASKKGLTCTLYTSGKLVVQGKEQAHFIEFYLEPEILESFGFSHPTTKIDLTPHIGIDESGKGDFFGPLCIAGVYIQANQFSKLQALGVKDSKTLSDKTIRQLASQIKNLCLYHIVKINPAKYNEIYQDFKNLNHLLAWGHATTIEQLILQSGCQTVIVDQFADEKVVLLALKRKKLDVNLTQRHRAEDDLAVAAASILARQAFIDGLEQLSKEIQIPLPKGSSSATQKAGKEVLRKWGEERLRSICKQHFKTLDAILGKVGK | 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): 33525
Sequence Length: 301
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
B3R0F3 | MKNYSFTFDIPQLRKLKKIYKSFLIEKEINNNSIYFFLKKDNIQMIAYNNGTFFIKGENIQEEILNIKEILNIKDYSAIGSDEVGTGDVFGSIVVCSSYVSAENIPFLENLNIKDSKKLTDEKIIQLVPKIINKITYSLISINPYKYNILTNKGFNLNKIKAILHNDMILKNLIKIKKNVNVILDKFTSSKNYFNYLKNEKKVYKKIFFCNKAEKVHISVAAASIIARYAFLKNIFALSKKIGINLKLGASTEVDKQINFIYKKYGMNILKKIAKCNFKNITKQFIKN | 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): 33316
Sequence Length: 288
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q8CPL8 | MGNVVYKLTSKEIQSLMAQTTFETTKLPQGMKARTRYQNTVINIYSSGKVMFQGKNADQLASQLLPDKQSTTGKHTSSNTTSIQYNRFHCIGSDEAGSGDYFGPLTVCAAYVSQSHIKILKELGVDDSKKLNDTKIVDLAEQLITFIPHSLLTLDNVKYNERQSIGWSQVKMKAVLHNEAIKNVLQKIEQDQLDYIVIDQFAKREVYQHYALSALPFPDKTKFETKGESKSLAIAVASIISRYAFVKHMDHISKKLHMEIPKGASNKVDLIAAKVIQKYDIQQLDTISKKHFKNRDKAIHLMNQKYNK | 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): 34875
Sequence Length: 308
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q5FG88 | MKDELNKVVVYTDGACSGNPGPGGWGAVLLFDNGEKTICGGHPNTTNNRMELTAVVQALKFLDVTYVIDLYTDSVYVKSGITSWIKKWKINGWRTADKLPVKNLELWLELDKIVKYHKITWYWVKAHSGNLYNEKADMLARSQIVK | 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): 16549
Sequence Length: 146
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q14IN1 | MEIFKKKNRVIAYTDGACKGNPGIGGWGAILSYNGVDKEIYGSEKDTTNNRMELMAAIKTLQALKRKCDITIYTDSKYLQNGINEWLANWKANGWKTAAKKEVKNKDLWQELDSLTNKHNVTWGWVKGHSGNAGNEKADELANKAIAELIGK | 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): 16976
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q9PBI6 | MKSINAYTDGSCLGNPGPGGWAVLLRYKNNEKELVGGELDTTNNRMELMAAIMALERLSEPCQIKLHTDSQYVRQGITEWMSGWVRRGWKTAAGDPVKNRDLWERLCAATQRHMVEWCWVKAHNGDSDNERVDVLARGQAMAQRSTVASR | 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): 16921
Sequence Length: 150
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.