ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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A4VKM0 | MNTLLLHCRPGFEGEVCAEISEHAAILEVAGYAKARPDSACAEFICSEPGGAERLMRRLRFADLIFPRQWARGDYLQLPETDRISVLLAHLADYPVCSSLWLEVLDTNDGKELSNFCRKFEAPLRKALVKAGRLDEQGKGPRLLLTFKSGREVFVGIAEANNSALWPMGIPRLKFPRQAPSRSTLKLEEAWHHFIPREQWDTRLAAGMTGVDLGAAPGGWTWQMVNRHIKVSAVDNGPMNADLMDSGLVEHFRADGFTFRPKRPVDWMVCDIVEKPARNAALLETWIGEGLCREAVVNLKLPMKQRYAEVKRLLERIADG... | 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
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C4ZJM0 | MNQHTPAAALACAGLLGYCRAGFEKELAAELDDIAAEAGLIGYVRAEPDSGYVIYETFEPTPLGSFGESTDWRRPVFARQLLPWFARVDDLPERDRATPIVEAVKASGQRFSGVMLETPDTDEAKQRSGFCKRFTEPLAKALEKAGCLRSSRAGLPVLHVLFTSATTAWLAAGQPGQCSTWPMGIPRVRMPSNAPSRSTAKLSEAFMMLLEEGERDSILRAGQRAVDLGAAPGGWTWQLVNRGLRVTAIDNGPLRDSVMATEMVEHLKADGFTWRPHRPVDWMVCDMVEQPSRIASLMAEWVATGRCRYTIFNLKLPMKR... | 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
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Q182S0 | MEKKKIVLKNFTEDELKEFMKTIDEKPFRGSQIFSWIYKGAKTFDDMNNIPKSLRNKLEEVSCIGHIDIELKLESKVDNTKKYLFLLDDGNIIETVMMDYDSRVTVCVSNQVGCRMGCNFCASTMDGLIRNLEPWEILDQVIKIQEDTGKRVSNLVLMGSGEPLDNFENTKQFLKIINEKNGLNIGYRHITLSTCGIVPKMYELADLEIAINLALSLHSPYDEERRKIMPVANAYSIEEILNACRYYIKKTNRRVTFEYSLIKGVNDSEKEAKALAKLLKGMLCHVNLIPINKVEEREYEKPDKAFIYKFRDSLEKNNIP... | 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] +... |
Q0TPL4 | MKNILDFTLEELKEWMKENGESAFRAKQIFDWIYKKEVFNFEEMKNISKALIGKLSENFYIGIPEVIDYLSSSEDGTRKILLGLGDGNIIECVIMRYKYGNSICVSTQIGCRMGCKFCASTLEGMVRNLTAGEILSEVLIGQKLLGERISNIVLMGSGEPLDNYDNVMKFLELVNADYGLNIGQRHITLSTCGLVPKIREMADKEMQVTLAISLHAVSDEKRKTIMPIANKYSISEILDACNYYIEKTGRRITFEYSLVSGVNDTKEDAKSLGRLLKGMLCHVNLIPVNEIKENEFKKSTKKDIETFLNTLKTYGVEATV... | 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] +... |
B2A2K6 | MINHKQSLKDLTLNELQEYFSRKGWQQFRAKQIFDWMYIQQVDSIEVMSNIPKKLRQELMENCTINDLELDSNNIYTSPTDGTIKFLSVLKDGIGVETTIMKYDYGNTVCISSQAGCNMNCVFCASTTGGKERDLSPGEMIDQVLMANKVLPGSESINNIVVMGSGEPLENYQHLIKFLKIVNDGKGLNIGMRHITVSTCGLVPEIYNLAEEELQLNLAISLHAPNDELRNKLIPLNKIYPIHELLEACQVYFQKTGRRITFEYVLIKDFNDSIDLAKELSETLTALKMPVHVNLIPFNPVEETKFTAPPSSRISDFKNN... | 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] +... |
Q82XV4 | MINLLDFNKTELVRFCGEMGEKPYRARQLLRWVHQSGKTDFMEMSDLAKGFRHKLMECAVVQLPEIVSDHTAGDGTRKWLLSTGAGNAVEMVFIPEPSRGTLCVSSQVGCALACSFCSTGRQGFNRNLSVAEIIGQLWWANRLLEAGSHDPFPLDTTRVQTDKPETRRPVTNVVMMGMGEPLANFENLVTALDLMLSDDAYGLSRRRVTVSTSGLVPALDRLRERCPVALAVSLHAPNDALRDQLVPINKKYPIRDLLAACERYLPAAPRDFITFEYVMLKGVNDSVALARELVQLVRNVPCKLNLIPFNAFSGSGYERS... | 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 occurrin... |
A9A3L9 | MTDLYRLLPEEMEKLVIDMGYDRYRADQILLPLYYKFPKDINDIPQLPKKLREEFTEAGYTIGSAKEIHRVVSDDGDTTKLLLELSDGSSVETVLMQYEPTKIGGHPRSTICVSTQIGCAMGCVFCATGQMGFETNLKAEHIVSQVIHFAELLEQRGEHVTNLVFMGMGEPMANYDEMIRAVKILTHDRGFGLGQRHITISTIGITSGIEKLAEENLQIGLAISLHAPNNELRKKLVPTAGPNSVEDIIKSGRDYFKKTGRRVTFEYALMEGVNDSPEIAHELARLLRGNGSHVNIIPINPTAGDFKRPSEKNVLEFEQI... | 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-methyla... |
Q2Y6F3 | MSINLLDFDAKGLTGFCAEIGEKPFRARQLLRWIHRTGEADFDAMSDLAKGLREKLAAAAVIEPPKVISDHTASDGTRKWLLSVGAGNGIETVYIPETSRGTLCISSQVGCALACAFCSTGRQGFNRNLTVAEIIGQLWWANKALTETFTSEAGRERPITNIVMMGMGEPLTNFENVVTSLDLMLDDNAYGLSRRRVTVSTSGIIPAMDRLRERCPVALAVSLHAPNDALRDQLVPINRKYPIRELLGACERYLQSAPRDFITFEYVMLDGVNDSVAQARELVQLVRDIPCKLNLIPFNPFPDSGFRRSSANAVSRFRDV... | 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 occurrin... |
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.-
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Q8ZDG6 | MRKEWLWVGIASVLLSACIDQPPAPQQQVQQTYSGPVEEIGGAEPRYEPFNPNVNQDYKVNGQSYRIIKDPQNFSQIGLASSYGEEARGNTTATGEIFDPNALTAAHPTLPIPSYVRVTNVSNGRQIVVRVNDRGPYTPGRVIDLSRAAADRLNISNNTKVKIDFINVAPDGSLSGPGMVGTTIAKQSYALPSRPDLTSSGMGTPMQQDAPATGAAVQAIDNSQLSGTDATQPVASQSSGFLRAPTPVPAGVLESSEPVIDSAPVTPPVVANPGPVTTTPTSSAISGGYVVQVGALSDAQRAQSWQQSLSQRFGVPGKVS... | 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.-
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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-... |
Q2RSU7 | MTDRLRATYRVKATAASIEARAKGIAVEQSVEMPLSAIDDPAVLDGIVGVVEEITERGEDCFEVRLALSTATIGGDAGQLFNMLFGNTSLQDDTVLLDIDLPDDLLASFGGPNIGAAGLRARVGASADRALTCSALKPQGLPPDRLADLARRMALGGLDFIKDDHGMADQAYAPFASRVGAVAAAVDEVNRQTGGQTRYLPSLSGHLDQLRSQVRTGLDHGIDTFLIAPMIVGPSTFHAVVREFPGAAFFAHPTLAGPSRIAPPAHFGKLFRLLGADAVIFPNSGGRFGYSRDTCQAVAEAALGPWGGLHASLPVPAGGM... | 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-ph... |
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
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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
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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
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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
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A0A0P1AAU8 | MQGVRITILWCIVLATIYAEEGPSTPRDDDPVIQKVRGLRNAGMKANDERMFKDAIEKLRHAISLLHNRVFGEERAAIKDPTVISQDAALYAQILNDYGSVLIRTKQYDEAIEVLEDSVAMIEKIYGDSHPSLGLSLRSLADAYMEKKAFKSAIKRYKTLRKHVKKGLGMTHEAYIEASLKIAEGYKKLNKKDTSRKVLKDTLKAQGGEINGLTIGIAELYMELSSAHVEVGEIDDALRAAETASAIFLQREGKDTMAYAFSLNALAGVKMQQKKVDEAIDLLDRAHNIAVSIYGENDRITLASAKTLQDVKDHKMNLLA... | 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
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A0A0P1B5K4 | MRLCGVASAFLSTLILIAHIDASTNLNVSVTDVQNISLPGDQIGNFTQSVSGPPSGDEERTSANSAIRKVDLFVEKLITFQVALRAKINRFLAKLKLAWWRLRNVDPNVTFNKLNLHEADNDILSLDNFHTWVKLVESYNLQHPAEQVSILSKLQEQFGEFEVSIMLEQAKNGADKYTEDIALELQHEQISRWRDDNLSLTALYKALQFGKSEPSLLTGPALRVWNIYTSNIESAETSLFDYLYQTIEDAHLSSLLIAAKQSPETVELATKIQNQLRQKWLEILVPPNLVFQHYKLDTNPTHLLDRPETKLWVRYQKMYW... | 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
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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... |
Q8P682 | MSDQSSEPLDSSLRQAVVPDSAAGRRFDAVLAELFPEFSRSRLSEWIKSGDALLDGETARPRDTLRGGETVQVQVVLETQTHAAPQDIPLNVLYEDDHVLVIDKPAGLVVHPGAGNPDGTLVNALLFRDPNLAAVPRAGVVHRLDKDTSGVMVVARTLQAQTALVEQLSARDVHRQYLAVVVGALVSGGTADAPIDRHPRDRLKMAVRDDGRDAVTHYRLRERFRAHTALECRLETGRTHQIRVHMAHLKSPIVGDPLYGGALKLPKGATDTLVAELRGFKRQALHAETLEFLHPVSGEPIRASAPVPEDLQRLMSALRE... | 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
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Q8ZBV7 | MAQQVQLSATVAESQLGQRLDQALAELFPDYSRSRIKEWILDSRVTVNGKKINKPKEKVLGGELVAIDAQIEEDARWAPQEIPLDIVYEDNDILVINKPRGLVVHPGAGNPDGTVLNALLHYYPEIMDVPRAGIVHRLDKDTTGLMVVAKTVPAQTRLVEALQAREITREYEAVAIGNMTAGGRVDEPISRHSTKRTHMAVHPMGKPATTHYRIMEHFRAHTRLRLRLETGRTHQIRVHMSHINHPLVGDQLYGGRPRPPKGASDSFIAILRGFDRQALHATMLRLYHPIRGIQMEWHAALPEDMVELINALKADTEEFK... | 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
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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
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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
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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
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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
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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
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A3LZU8 | MSKYKILDSHIHLYSLANIPLLHWDEGNPLHGNRRLDEYIENSQSTQFDVEGVVWIECDAKIDLTQGLKGLENPIEEYLYICRNINGKLLPEEGVSTPFKRRLIKAMIPFAPMPLGSAGVEEYVKALKTRNSSEFHLVKGFRYLIQDKPPLTISDPHFVSSFQWLDSNGYVFDLGIDMRSGGLWQFKETLEVFKKVPNLKYIINHLTKPCLDFDPETIDSNPDFLSWKRLVTEMYITTPNSYMKLSGGFSEVEQDVALDVTSTSRHVYPWFKVVYELWGPERTIFASNWPVCAIPAGQNLTEKWFQVCETLFDSIGMDED... | 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
Sequenc... |
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 complementa... |
O00237 | MWLKLFFLLLYFLVLFVLARFFEAIVWYETGIFATQLVDPVALSFKKLKTILECRGLGYSGLPEKKDVRELVEKSGDLMEGELYSALKEEEASESVSSTNFSGEMHFYELVEDTKDGIWLVQVIANDRSPLVGKIHWEKMVKKVSRFGIRTGTFNCSSDPRYCRRRGWVRSTLIMSVPQTSTSKGKVMLKEYSGRKIEVEHIFKWITAHAASRIKTIYNAEHLKEEWNKSDQYWLKIYLFANLDQPPAFFSALSIKFTGRVEFIFVNVENWDNKSYMTDIGIYNMPSYILRTPEGIYRYGNHTGEFISLQAMDSFLRSLQ... | 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 prot... |
Q6ZNA4 | MSQWTPEYNELYTLKVDMKSEIPSDAPKTQESLKGILLHPEPIGAAKSFPAGVEMINSKVGNEFSHLCDDSQKQEKEMNGNQQEQEKSLVVRKKRKSQQAGPSYVQNCVKENQGILGLRQHLGTPSDEDNDSSFSDCLSSPSSSLHFGDSDTVTSDEDKEVSVRHSQTILNAKSRSHSARSHKWPRTETESVSGLLMKRPCLHGSSLRRLPCRKRFVKNNSSQRTQKQKERILMQRKKREVLARRKYALLPSSSSSSENDLSSESSSSSSTEGEEDLFVSASENHQNNPAVPSGSIDEDVVVIEASSTPQVTANEEINVT... | 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 SM... |
Q99ML9 | MSQWTPEFNELYTLKVAMKSGTPDAPTTQESLKAVLLHPQPLGATKSFPAEVEMINSKVGNEFSHLCDDSQKQEKDMTGNQQEQEKSGVVRKKRKSQQAGPSYVQNCVKENQEILGRRQQLETPSDEDNDSSLSECLSSPSSSLHFGGSDTVTSDEDKEVSVRHTQPVLSAKSRSHSARSHKWPRTEADPVPSLLMKRPCFHGSALRRVTCRKRLVKSSSSQRTQKQKERMLVQRKKREALAQRKYALLSSSSSSSENDLSSDSSSSSSTDGEEDLCASASENPSNPAAPSGSIDEDVVVIEASFTPQVTANEEINVTST... | 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 the... |
Q08DF2 | MPRSALSVISFCHRLGKQERKRSFMGNSSNSWSHTPFPKLELGLGSRPTAPREPPACSICLERPREPISLDCGHDFCPRCFSTHRVPGCGPPCCPECRKTCKRRKGLRGLGERMRLLPQRPLPAAALQETCAVRAEPLLLVRINASGGLILRMGAINRCLKHPLARDTPVCLLAVLGGPHSGKTFLLNHLLQGLPGLASGEGSWPRSAGSGQGFRWGANGLSRGIWMWSHPFLLGKEGRKVAVFLVDTGDVMSPELSRETRTRLCALTSMLSSYQILTASQELKDTDLEHLETFVHVAEVMGRHYGMVPIQHLDLLVRDS... | 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 regulator... |
Q96DY5 | MPRPVLSVTAFCHRLGKRESKRSFMGNSSNSWVLPREEAQGWMGQAVQGGTRTSRSHASFPKLELGLGHRPSPTREPPTCSICLERLREPISLDCGHDFCIRCFSTHRIPGCELPCCPECRKICKQRKGLRSLGERMKLLPQRPLPPALQETCAVRAERLLLVRINASGGLILRMGAINRCLKHPLARDTPVCLLAVLGEQHSGKSFLLDHLLSGLPSLESGDSGRPRAEGSLPGIRWGANGLTRGIWMWSHPFLLGKEGKKVAVFLVDTGDVMSPELSKETRVKLCALTMMLSSYQILNTSQELKDTDLGYLEMFVHVA... | 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 regulator... |
O17917 | MDLFRKPKKRNAPVVRKKESSSDEDQDSEVKDVIQKRRRTNPMVQSTKQLDASTRRADNSSDDSDDSDDNQDIAVATHSFAASGDAGPSGPRDQGATATLEVDTDYSHDAQAQFERVQQQLKEGVEKDGKILYKGSALYGAKEAKDTAKGNAASGYNRVGPVRAPQFLRQTVRWDFAPDICKDYKETGFCTFGDSCKFVHDRSDYKHGWEIDEEYEAGKYGAEDDANYEIHEGDDTFPEDCFICGNPFVDPIVTKCKHYFCTGCALKSFQKSSKCPICQQNTENIMNTAKELLTYLKRKKQQQKQEAEKQEEEKDSDDDE... | 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 Activit... |
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 transcriptio... |
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 ... |
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... |
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): 1749... |
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... |
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 o... |
O74919 | MAYNHFSIPKNIEEKENSFFDVTFQDEPDETTSTATGIAKVSIPTPKPSTPLSTLTNGSTIQQSMTNQPEPTSQVPPISAKPPMDDATYATQQLTLRALLSTREAGIIIGKAGKNVAELRSTTNVKAGVTKAVPNVHDRVLTISGPLENVVRAYRFIIDIFAKNSTNPDGTPSDANTPRKLRLLIAHSLMGSIIGRNGLRIKLIQDKCSCRMIASKDMLPQSTERTVEIHGTVDNLHAAIWEIGKCLIDDWERGAGTVFYNPVSRLTQPLPSLASTASPQQVSPPAAPSTTSGEAIPENFVSYGAQVFPATQMPFLQQPK... | 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
Subcellu... |
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 o... |
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
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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 o... |
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 o... |
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'-pho... |
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 o... |
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 o... |
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 o... |
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 o... |
A7HYE5 | MEIITTNEALRAACDRLSTAGFVTVDTEFMRDATFWPILCLIQLAGPSDELIVDPLAPDLDLAPFYALMKNRNVVKVFHAARQDIEIFCHEGKAIPDPLFDTQVAAMVCGFGDSVGYETLVRKLAGGSVDKSSRFTDWSRRPLSDKQLQYAMADVTYLRTIYEVLAKRLTHTKRAHWVAEEMAVLQDPETYAMRPENAWKRVKARFRGQRGLAVLVEVAAWRERQAQERDLPRSRVMKDDALAEIATQIPRTISDLDGLRAVPKGFSNSRSAASLMEAVERGLAMKEEDIPVVEGPEPLPPGIGPLVELLKVLLKIKCEE... | 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 (D... |
A6V8R6 | MFVTAPEIQWIRDDASLAQQCREWRTQPYLALDTEFMRVDTFYPAAGLVQVGDGRREWLIDPLLVRDWGPFAELLEDPRVVKVLHACSEDLEVFLRLTGSLPVPLFDTQLAAAYLGMAHSMGYSKLVKEVLDIDLPKDETRSDWLQRPLTEMQMRYAADDVQHLAQVYLALDARLSEEKRAWLLEDGAELVANLCRESDPREAYREVKLGWRLRPQQLAVLRELCAWREEQARLRNRPRNHVLRERTLWPLARLLPKNKTDLAAIEDMHPRTVRQDGDFLIELIAEAARLPQSEWPEALPEPLPPEVTPLLKSLRAIGQR... | 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 (D... |
A1SVE6 | MQFEIITTTAQLHDFIATLDGSPISLDTEFVRTRTYAANLGLLQISQNTQITLIDPIAVGDLSSFWQAIDNKNIILHASSEDLEIIRDHKGDLNFTLFDTQIACSFLNMGASLGYAKMVETLEAVIVDKGESRTDWCARPLSEKQINYAGVDVLYLQPCLEKLQQQLENKKMFPFFEQECQSVLAQKMVKQDPDKAYKLLNNLFKLDRQGLAIIKALAKWRLLTAQERNLALNFVVKADHLWLLAYYQPTSLDDLRRLNLLPNEIRIHGQQILTIMTQVISQDESTYPPLVNRLVDFPAYKSTVKSMRDKIQLCAEKYDL... | 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 (D... |
A0KXU5 | MSRLLFLWTVLNPQELEKNLSVFQYVSDEASLNALVAQYQQSPLLVLDTEFVRTRTYYAKLGLIQAYDGKTLALIDPVALPDLSAFWSLLDNPNIIKLVHSCSEDLEVFAHYGQRQPTPLFDSQIAASLCGMGHGLGYAKLVETCLGEVIDKGESRTDWMRRPLTEAQLSYAANDVLYLYQLYPQLADKLKAQDRLGWLYEEGERMTEGRLATPDMDTAYLRVKNAFQLTEHQLAYLKVLAKWRLEKALARDLALGFVIKDHGLIALAKKQPKSMGDLLKLNDLTEQEKRIHGKDILRVMQTADLSNPPELVDVLALKPG... | 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 (D... |
D4Z694 | MQIHPLITDSKTLAQFCARIAKSPYIAVDTEFMRENSYWPDLCLVQVADEHEAAAIDPKAPGLDLSPLLDLMVDNEDVLKVFHAGGQDLEIIYNLTGKTPHPLFDTQIAAMALGLGEQIGYGNLVDAWLGVQLDKGARFTDWARRPLDKRQIDYAIGDVTYLIQIFPKMLEELRRTGRGDWLDQEMERISDPSNYENKPEEAWQRVRIASRKADVLGRLKALAAWREMEAQDKNLPRGRIVKDETLADIASHPPRTQEDLGKVRGLSATWKTNDIGNRLMLALASHAPLAKEEMPERDPKRPGLGKDGALVADLLKLLLK... | 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 (D... |
Q5GZ75 | MPHWITHPSELTDRLQAARPARIGLDTEFIRERTYWPQLALVQMAIGEEILLIDPLIPGMNAALKEWLTATDIVKVMHSASEDLVTFKCACGVLPRPLFDTQIAAALAGVGGGMGYQKLVQEVTGTLLTKGETRSDWMRRPLSPSQLEYAADDVRYLFAIHDELTRRLTEQNRLGWLAEDAERLLATVEHDDGERWPHVSLRTAQFLEPAAQRRLLRLLRWRDLQARQSDRPRSWILDNEVASQLARFPPADLDALLQQFDKFPKAPRKLANAVWDALNTPLPDEEHAPLAQAATDGNKAVLKRLQDTVAQRSHELGLPD... | 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 (D... |
F4IV66 | MDVTEVPWRRLPQFSVSSRASWLVSSGFPLSSYMFSHVERGKTFRLTLCFGVSRLRPRSAIPLRFLLSVFSEQPPSRLKGLCEVVWIVEADLAANEHLYVTGDPSTLGSWEPDCAISMYPTENDNEWEAKVKIASGVNFRYNYLLKAGYGSSSDVIWRPGPQFSLSVPSSVNQDRKIIIRDSWMSMSISSKSQESYGWGSWIDDAYLFPNCVTPAQSEDECTSADSAIEVPRTHLNDKQVGAESFLCDELAAFSSENSNLSALFSDNYQPIEEPWLIQESITLQHERNMQTDSEQDVESCDDNENNLNTDEQNHQLTETL... | 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... |
P57429 | MKRMLINATQQEELRVALVDGQRLYDLDIEHSGSEQKKSNIYKGKITRIEPSLEAAFVDYGEEKNGFLPLKEISKNYFPENHIETLGFNIKNVLQEGQEVIVQISKEERGTKGAALTTFISLAGSYLVLMPNSPKSGGISRRIEGNDRIALKELLTLLELPEEMSLIIRTAGAGKSIESLRWDLSLRLQHWKTIQIIAKSRTAPFLIHQESNIIVRAFRDYLRQDIGEILIDNPKILDLARKHITFLGRPDFVNKIKLYSGEVPLFSYFQIETQINSAFQRKVRLPSGGSIMVDSTEALTAIDINSSRSTSGTDIASTAF... | 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... |
Q89AH3 | MRRMLINAIEIKKLRIALIDGQQLYDLNVENIDKKQRKSNIYKGKIVRIEPSLEAAFVDYGEKKNGFLPLKEISRNYFPNNCSNYRHLHIKNILKEGQECIVQIDKEERGTKGALLTTFISLAGNYLVLMPNCPHLEGISRKIEGIDRFHLKKIISMLMVPENMGIIIRTSGVGRSIETLQLDLNFRVKNWYTIKKSAEINTAPCLIHKESNIVIRTLRDYLKKDIQEIIVDNPEILELARDYMFNMNCSYFEKKIKLYTGSDPLFSYYKIESQINALLRRIVKLPSGGSIIIDYTEALTAIDINSSQSTKGVNIEETAF... | 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-st... |
O78453 | MSFNIIILKELGFSLVFSQSKCEYIIFQKEQCGLNDIYFGFIPRQSIYPTLNAAFVTLDSERNQGFIPFTLLIKKSNQQFVIPNSVFLIQVIKEPTINKPATLTSHIFLNSFNLNLQFSGIDCKYLNLYPNIKFLHICLITLLIPSGLDINFDHSMKDILYLDLIGQSKILYYSFSNLFTKLLRIKKMPQFIFRNSNFFLPILNKLSLSSINDFFVSSYQRAVYLRHFLITHYFTIKQTDYRILFYPTAYKSMQLYYLDMLFYRSLKPIVYTLYGIFIVICKTEALISIDVNSGSHSSRVSQNLSLHTNLIASKSIIKEI... | 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... |
P44443 | MKRMLINATQKEELRVALVDGQRLFDLDIESPGHEQKKANIYKGKITRVEPSLEAAFVDYGAERHGFLPLKEIAREYFPDDYVFQGRPNIRDILVEGQEVIVQVNKEERGNKGAALTTFVSLAGSYLVLMPNNPRAGGISRRIEGDERTELKEALSSLDVPDGVGLIVRTAGVGKSPEELQWDLKVLLHHWEAIKQASQSRPAPFLIHQESDVIVRAIRDYLRRDIGEILIDSPKIFEKAKEHIKLVRPDFINRVKLYQGEVPLFSHYQIESQIESAFQREVRLPSGGSIVIDVTEALTAIDINSARSTRGGDIEETALN... | 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... |
Q9TL10 | MLVVGNRIVDVSRHTSIGTIVIATVDKLAPGLGIAFVSWTHGQGKGGLPSTKKHYGILPLRSWRGRGPLDFATTHELTGENLILQHGDFVLVQIVQDGNHAKVHLVSGHIALTTSRLVVWPGLSSKDWIFSHQIGQKINNYLHVRKLVSYMRRDQILCTGPQRWMKEQYALEHQWENFVLEFIEQPTGISYLTSMTEKFVSPVCAEWFQHPLSVWIIGCNLQIRESMTKWMITHVPHKSRHIEITTLDAWKNWYNLHRAAIVQPQIPLRSGGTMIIEFTEIGWSFDINSGIGLEIGSKTCANEEAIYAIAQQILLRSMHG... | 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... |
Q8YP69 | MPKQIIIAEQHQIAAVFSEDQIQELVVATGHHQIGDIYLGVVENVLPGIDAAFVNIGDPERNGFIHVTDLGPLRLKRTAAAITELLAPQQKVLVQVMKEPTGTKGPRLTGNITLPGRYVVLMPYGRGVNLSRRIKSESERNRLRALAILIKPAGMGLLVRTEAEGKPEEAIIEDLEVLQKQWEAIQQEAQSTRAPALLNRDDDFIQRVLRDMYGADVNRIVVDSSTGLKRVKQYLQNWSGGQTPQGLLIDHHRDRSPILEYFRINAAIREALKPRVDLPSGGYIIIEPTEALTVIDVNSGSFTRSATARETVLWTNCEAA... | 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
... |
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.-.-.-
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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 hete... |
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.-.-.-
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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):... |
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 r... |
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.-.-.-
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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.-.-.-
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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 duri... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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
Subcel... |
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
Subcel... |
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
Subcel... |
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