ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A8ERZ9 | MKINIYAILKPTADNFDQIIKEFIKMSSKYAKVEVHYIFNKNIAKAQTIGEKESQLAYSQTYEPLLKGYNIALDVLGKRVDTYAFSSLIDNKNEVNFFIGGAYGFQREFLNKCDSVISLSDLTMAHKVANVVLTEQIFRSLCIQNNHPYHK | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17296
Sequence Length: 151
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
A7H6X6 | MRLRVVAVGRDRSGLYAPAIEEYAKRLGRYVKFELVEVPEARKHAGTAQARDEEAEALLAKLGPRERVIALDERGAEWTSVAFAERVRRWTEGGRDVALVIGGSDGLSRAVLDRAEETLALSRMTLAHRLARLVLVEQLYRAMTILRGEPYHK | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17194
Sequence Length: 153
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q7NKY9 | MRIKLVAVGRLREEAYERACAEYARRLAAYARLELVEVRDARIADSRAGLLKEGQALLDQLHPGEHAVLLDSGGKQFTSVELADWLENHTVQEPVFIVGSSHGVAPMVRERAQMVWSLSKLTFPHELARVIVLEQLYRAVTILAGHPYHHG | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 16944
Sequence Length: 151
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q5FRS9 | MKLVAIGRLKAGPERELFERYAGRIRPALTVTELAPSKGSVQEQKRQDAAALLGACPDNALIVALDEGGKTPDSLRLAEMLSRWQESGRPIHFLIGGAEGLDSSVIQRADSVISLGKLTWPHMLVRVLIAEQVFRAQAINTGHPYHRESRPD | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 16658
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q0BRE3 | MTAPWRIIAVGRMRGSEEEALFQRYAARLRPALTVTEIAEARGSTAEIRRRETSALLAALPPACIVVAMDLGGRAHDSEALATLARRWREQPLPVCFMIGGAEGLEQPVLDRADHVLSLGPMTWPHLLVRPLLAEQLYRAQAIATNHPYHRTGRPSG | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17307
Sequence Length: 157
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q2SA30 | MRIKLIAVGGKMPGWVEQGYNEYVKRMPRDMPLQLIEIPMPRRQKNADPHKLKIQEGESILQSLGSGDHVVALEVEGKSWSTPQLSQQMERWRMSGQDVALLVGGPDGLSDACRARANQQWSLSPLTLPHPLVRVLLAEQLYRAWTILQGHPYHRE | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17724
Sequence Length: 156
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
A1WYZ1 | MRIHLVAVGHKPPRWVRDGHETYAQRLGKGWRLELHEVGAGGRGNDDPQAREREGERLLRALPSRAVCVALDEGGTPRDTRQWARSLERWSHEGGEVAFIIGGADGLSDAVRQRADACWSLSPLTLPHMLVRVLVAEQVYRAWTLLSGHPYHRS | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17282
Sequence Length: 154
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
B8CZR7 | MKINIMAVGKIKEDYINAGIKEFLKRLKPYTEVNVIEVDDERIPPNASGAQIEKVKEKEGERLLKNVPKNSYVIVLDVKGKPMTSEGLAKSIQNLQLQGYSNITFIIGGALGLSQKVLDTGDYILSFSHMTFTHQMIRLILLEQLYRAFKIIKGEPYHK | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 18008
Sequence Length: 159
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q7VGT3 | MQINIYSIAKKDAKYQALLEELCMQCKQFGVEIKILNLLPQAVLKAQKISSAKAQQSYTQTFLPYIALPTALNLILHPTGHNYDSQSFAKLIESQHIVQFFIGGAFGFEESFVRLGKSVSLSAMTFNHKIAKLVLCEQIYRALSILHSHPYHK | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17286
Sequence Length: 153
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
B0TA39 | MLHIRIVAVGKLKEKYLKEGLREYIKRLGAYSRLEIIEVPDEKVPDKPSDTEAALIKRKEGDRLLAAAGDKDYIGVALDPRGEMWSTEDLADKMRRWELYGPNLVVFFIGGTLGLSKEVHAVCKAKWSLSRLTFPHQLVRLILLEQVYRGCKVNRGETYHR | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 18465
Sequence Length: 161
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q3IJ98 | MKIQMIAVGTKMPAWVETGFTEYQRRFAKDMTLELIEIPAGKRGKNADIKRILHIEGEKTLAAIPKGNRIVTLEVTGKPLDTHELAKNMEKWQLDGRDVSLLIGGPEGLAPECIAASEQKWSLSNLTLPHPLVRIIVAESLYRGWSLNNNHPYHRE | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17562
Sequence Length: 156
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q1QDN7 | MKVRILTVGNKMPKWVQTGFDEYHKRIQPMLTTEVVEIAAAKRAKNPSDANLAQYREQEGQAILAAHAVAGREQLWVLDVKGKMLSTENLADKLSDGMQQGDDIALVIGGADGVSPEVLAKADVKWSLSALTLPHPLVRVVLMEQLYRAMSINHNHPYHRGN | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17933
Sequence Length: 162
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q92LB0 | MRIGLFAVGRLKAGPEKDLAGRYLDRFAKAGPAVGLELARVVETAESRAANAETRKREEAGQLEKALADGSLLVLLDERGKALDSEAFARLLGTLRDSGKRDLMIAIGGADGLDPALHARADAVLNLGKMTWPHQLVRILIAEQLYRAVTILSGHPYHRA | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 17274
Sequence Length: 160
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q5NLX2 | MKIHIIARGRIGRSPEGELVERYMKRLSWPYRITELPDRASNAPLPPAPPHSITVAMDEKGKTWRSMEFAQKIGNWQDEGRSEIRFLIGAADGLREEERAAADMYFAFGAATWPHMLARAMLAEQLWRASAILSGHPYHREG | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 16157
Sequence Length: 142
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q8EFW4 | MLNFFAAAPKGFEYSLAQELTEFGATEIKESVAGVYFTAPLTLAYRITLWTRLASRIVLVIYKGPCESAEQLYNAAYCIDWSAHFSNRNTFSIDFHGTGGFINNTQFGALKIKDAIVDRFRDDGDARPNVARIDADIKVDAHFRNGVITIAMNFSGPSLHQRGYRSTTGEAPLKENLAANMLVRSGWKAAPTTLLDPFCGSGTVLIEAALMAADIAPGLQRNRFGFEHWRRHDKATWHEIVEEAKARASLGVKRCEVKFYGSDIDSRLVALAKRNAQNAGVLELIEFNVANALNVEPPAAEGYLITNPPYGERLGSVSELLQLYYQLGDKFKKEFGGWKVAMLCSDIELISALKLKADKQMKMFNGALECAFNLYTLHAQSTRRDTPVLPEGVDIADIAPAFANRIKKNAKQFEKWAQKEGIDSYRLYDADIPEYNVAVDKYLDYVVVQEYMAPASIPEAVTKRRLSDVLLALPAAIGVDPHKIIMKTRERQKGTNQYQKLDERKLELITTEYGAKFKLNLTGYLDTGLFLDHRLTRRLVGQKSKGRRVLNLFSYTGSASVHAALGGAKSVTTVDMSNTYLAWAKENFALNNLSGKQYEFVQADCLQWIRDCNEQYDLIFIDPPTFSNSKRMEDSFDVQRDHVNLLGMLIKLLSPNGELVFSNNKRKFKMDTETLTKMKIKVQNIDDMTLPLDYKRNPHIHNTWLITHADK | Function: Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA.
Catalytic Activity: guanosine(2445) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(2445) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 80049
Sequence Length: 711
Subcellular Location: Cytoplasm
|
B1ZQZ5 | MRPSLAELSVDDLASVLAQWGYKRSHAGRVLREYYARCGELTEAGRPWPAGLLERLRIEFAPGGTALAARQVAADGTTKLLLRLADGRTVEAVLMPDYRADRAAGCLSSQVGCAMGCDFCATAQSGFERNLTAGEMVEQFLALRREAASAGRKLQTVVFMGMGEPLLNLDAVLTAVRRIADNTYGGLGWRQVTVSTVGLVPGIDALTAADLGINLAVSLHAPDDATRAALLPAGRRFAIADILAAVDRFQASRGRPVIIQYCLLKGVNDSAAHARMLAAVIGSRRMHVNLLHYNPTGLSLRGVRYEPSGDEAAAQFLAELRARGVVTHLRRSRGPDIDAACGQLRAKRGELSVQS | 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): 37988
Sequence Length: 355
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
Q6MED6 | MKIPPISILSHTSESYANAISHELGKGFQHAKLVYQEWFRRGNISGLNPAFKNAQALLQNILSLTDFSFLPISQNLTDGQTGKFLIKTIDDLDIKSVLIPMQAGGTLCISSQIGCQMGCAFCETGRMGLLRNLTTQEILSQLFIAKFRLHFSVRNIVFMGMGEPFDNYDTVMHAFRILTDSHGFGLGNNRITISTSGCLEGIYRLLQETTPLPNLAVSLNAPNDELRNKLMPINKKYPLKELYQAIYDFCKQTSKQVLIAYVLIKEQNDSIEHAKQLTNFLSGLNVKINLIPYNPQSRDRFQSPEQSTLENFTSYLREKGFYTLLRQTKGQKIMAACGQLGNLELKRKKPFILPILKE | 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): 40409
Sequence Length: 358
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
B1ZVM5 | MRFLTGNVVVRARGADFFVAIDARSAGGADAWLALTNGAPLLRRFTLSPSAPTNLYDFTRAELRLWLSRRELNPVHAARIWSYLYLDLVEGFGAMTELPARVRARLEAEMCVGNLKIARETDSRDGFTRKYLLELADGAAIETVLMRFAGRATACVSSQVGCAMGCVFCATGQMGYTRHLTAGEIVAQAVHVARALRTAAFEKCHVMRDPSPGREAGEKSRDEADRHRAPPTPRLRNLVLMGMGEPLHNYEAVMRAVDILRDDGGLALGAERITLSTVGVVPGILRLAAEKRPVHLAVSLHAADQEERAALVPVAKKWPLDELMAACRTYSETTGRRVFYEWTLIEGRNDTAAHARAVGRLLRGLPAQVNLIPLNPTAGYDGTPGRTEAARRFQEILSREFALPSTVRQRRGIDIAAGCGQLAVAEQS | 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): 46782
Sequence Length: 428
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
Q6MDD0 | MDYADFDHQKLVEWLKAHGEKEFHAKQILSWIYQKGVLSWDKMSNLSQSLREKLAKHIRLPVLELVRYTESIDQETIKFLWRLRDGNLVESVLILSGIRRTVCVSSQVGCPAKCAFCASGQQGFFRNLRPTEIIEQILQINAWLSSKGEKVSHVVYMGMGEPLKNYESVVASIRVLSHPDFCNISQRRITVSTVGVVEGIKRLSKEGLKVNLVLSLHAPNQHIRKKIIPYARKYPLEEILESMDEYAQKTKRDITFEYTLLAGINDHPDHAHELAHLLKGKQCTVNLIPYNPIPGLRLKRPEKKAIKQFRSVLYGSHIVNTCRYTKGDDIGAACGQLALQEREGQTGLPMLKEVAFGS | 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): 40702
Sequence Length: 358
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
A3DCX9 | MDAKADLLSMTIEELENLMAEMGEQKFRAKQIFQWTNKGIKDIDAMTNLSKDLREKLKERAYINRLEVIKKFVSKIDGTIKYLFKLNDGNIIESVLMQYLHGYSACISSQVGCKMGCKFCASTGVGFVRNLTPGEMLDQILTIQNDTKNRIGNVVIMGIGEPLDNYENVVKFLRLVNHKDGINLGARHISVSTCGLVPEILRLAEEKIPVTLSISLHAPNDEIREKIMPINKRYSIDKIIEACKIYTETTNRRITFEYAMIDGLNDSKENALELAKRIRGMLCHVNLIPVNTVSDTGFKRSSREKITAFKEILERFGVETTVRRELGSDINAACGQLRRNLVENGQLVY | 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): 39515
Sequence Length: 349
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
B1H070 | MQLLKQNYKKYILDLNDAQFNRAVKPIIEQDYRINQIIEWIYAKKAVSFESFTNIPKELRNKLDEKFFLRTLKIVKKEKSLIDSTIRYTFRTADKKYFFAVFLPANGKNSVCISSQIGCPIMCAFCSSGKTKLARNLSRGEIIEQILQVENDTKEKISGILFMGMGEPMLNFNNLISVLNSLLSSKEFGIGKRHITVSSVGIVPAVKKLADDNFGVRLALSLHAVDERQRKKLVPDNLGFSIEDILKAGKYYLKKTNSHLTIEYVLVKGINISSADAHKLARLLKRCDLINSDVQVNLIPFNPVTDVQFQRPDKKSINKFKSILKLNGITVNVRQSKGANINAACGQLGY | 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): 39572
Sequence Length: 350
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
B0S143 | MQNKIILENMTVDELKEFFVNNGEKPFRALQYFQAIHKNRIFNPDEMTNFSNSLRGKLNQYNDIKNCSIIKRIDSKLDNTKKYLIEMSDGNIVETVFMQYKTHTSICLSTQIGCKMGCKFCASTKKSFVRNLQPYEMCAQIYLVENDLDIRINNIVLMGIGEPLDNYDNVSRFIDLITDKDGQDMSIRNITLSTCGLVDKIIRLANDDIGINITISLHNPFDNERNKLMPIGNKYSIEEILDACDYYFKKTKRRIGFEYTVIENVNDSKKYMDKLVSLLKNRNCLLNLITLNPIEEFNQKSPDRYKMTEFMEYMNKNNVNTTIRRKQGIDIDGACGQLRINNMTKRGVK | 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): 40597
Sequence Length: 349
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
A6H1B8 | MQIEKKDIRALSKDQLRDFFVINKDKAFRGNQVYEWLWSKGAHSFEDMTNVSKGTRQMLVENFVINHIKVDTMQRSSDGTVKNAVRLHDGLIVESVLIPTETRTTACVSSQVGCSLDCNFCATARLKRMRNLEPGEIYDQVLAIDRESKLYFNRPLSNIVFMGMGEPLMNYNNVIKAIDMITSSEGLGMSPKRITVSTSGVSKMIKKMADDEVKFKLAVSLHSAVEEIRNKIMPFTKSFPLPELREALQYWYHKTKSKITYEYVVWKGINDNKESVDALVKFCKHVPCKVNLIEYNPIDDGEFQQASPESINAYIKALEANGIIAKVRHSRGKDIDAACGQLANKEI | 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): 39359
Sequence Length: 347
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
Q0RDQ8 | MTAESDSPDGPVSAGTGRPVRLSLTRRAARPARHLADLSRDERRQVAVALGQPAFRADQVSRHYFARLVDADETDAMTDLPENARGPLLEALLPRLLVPARTLSCDDGLTRKTAWRTADGALLESVIMRYPDRATVCVSSQAGCGMGCPFCATGQGGLTRNLSTAEIVEQVVHAARVLRRQELAGGQGRLSNVVFMGMGEPLANYTAVTAALRRLIAPSPEGLGLSARGLTVSTVGLVPAMRRLAGEGLPVTLAVSLHAPDDELRDELVPINTRWPVAEVLAAAWEYAEVTGRRVSIEYALIDGVNDDVARADALATLLAGRLAHVNLIPLNPTEGSSWQASAPAGQRAFVRRLRERGIATTVRDTRGREIAAACGQLAAEPAGRARRVESARPVESARPVGVAGAASGSPAHGSRVLR | 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): 44374
Sequence Length: 419
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
A8M6B6 | MTSLPLTPVNLDAPARRAAMPPRHLADLDLAGRQALVAELGEPRFRARQVSTHYFGRLVRDSGQMTDLPAAAREKLTDRLLPTLLTPVRELTCDDGATHKALWRLHDGSLVESVLMGYPDRVTACLSSQAGCGMACPFCATGQAGLTRNLSTAEIVDQAVYLAGVAASGAVAGSPPRLSRVVFMGMGEPLANYNRVVAAIRRLVAPAPEGLGLSQRHVTVSTVGLVPAIRRLASEDLSVTLALSLHAPDDGLRDELVPVNQRWKVSEVLETAWEYAARTGRRVSIEYAMIKDVNDQPWRADLLGRLLAGKLAHVNLIPLNPTPGSRWDASPKPVEREFVRRLRDAGVSTTVRDTRGREIDGACGQLAAAEGDEIVGPGAP | 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): 40812
Sequence Length: 380
Subcellular Location: Cytoplasm
EC: 2.1.1.192
|
Q2S0P9 | MPDVKTASHTVGTAEDRVDLKTMGRAGLKDFVAEHGAPRYRGDQLFNWVYGKGVSDFDRMSNLPKRMRRGLQRDATVEDIEIVEQQQAADRTVKALFELPSGREAETVLIPAIDERGEARRLTVCVSSEVGCAMGCEFCATGRMGFRENLTPGAIFDQVWHMNEVAQEHFGRPVTNIVFMGMGEPLLNYDAVLDSISILTDEDSLNLSAQKITVSTVGLARRIKDLADDQLRTNLAVSLHAPDNETRSRIMPVNEAEKTSLPALKEALQYYFDKTGRQITYEYCLFKGVNDSETDARNLADVTRWAPSKVNLLMYNPVEGLNFERTSEAQLDRFVQVLVQEGVTVTVRRSRGQDIDAACGQLANEGEDA | 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): 41087
Sequence Length: 369
Subcellular Location: Cytoplasm
EC: 2.1.1.192
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A4X4J7 | MTSLPLTPVNPDAPARRAAMPPRHLADFDLAGRQTLVTELGEPRFRARQVSTHYFGRLVRDPEQMTDLPAATREKLADQLLPTLLTPVRELACDDGATHKALWRLHDGSLVESVLMGYPDRVTVCLSSQAGCGMACPFCATGQAGLTRNLSTAEIVDQAVYLAGVAASGAVAGSPPRLSRVVFMGMGEPLANYNRVVAAIRRLVAPSPEGLGLSQRHITVSTVGLVPAIRRLASEDLSVTLALSLHAPDDELRDELVPVNQRWKVSEVLEAAWEYAARTGRRVSIEYAMIKDVNDQPWRADLLGRLLADRLAHVNLIPLNPTPGSRWDASPKPVEREFVRRLRAAGVSTTVRDTRGREIDGACGQLAAAEGP | 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): 40317
Sequence Length: 372
Subcellular Location: Cytoplasm
EC: 2.1.1.192
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A7ICB3 | MMSTPETATEATAPEAAPAPSLGADAPAPLPSLIGLDRDKLGAALDAIGVRGSDRRMRVNQLWHWIYLRGATDFAEMTNVSKHLRADLAAAYSLARPEIVMEQVSQDGTRKWLLRFPADHPGERPHDIETVYIPESDRGTLCVSSQVGCTLNCSFCHTGTQRLVRNLTAAEIVAQVMVARDRLGDYPGRDRATGPGLPTEGDRLVTNIVFMGMGEPLYAYDSVKEAIETLSDGDGLGLGKRRITVSTSGVVPEIERLGAEVGPMLAISLHAVRDKLRDELVPINKKYPIAELMEACRTYPAASNAKRITFEYVMLKGVNDSPADARALVKLLEGVPAKINLIPFNPWPGTQYECSDWETIERFSDIVFRAGYASPVRTPRGRDILAACGQLKSESEKLSARERLALRAMMAQDE | 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): 45275
Sequence Length: 414
Subcellular Location: Cytoplasm
EC: 2.1.1.192
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P0CU92 | MRASTILFVLGAAILAVIGVTTALDSGEIDKSTQENHRLLRSGSMEQEPDEERKFIKVPSFMNKAAREAKKAKKKAEIANLVWLKLQKYSDSYALNYVDDMVKSGRSADDEIKFLKKHMKVSNNLQRVIEGHFRSHAELGRVLAKPKYK | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 16864
Sequence Length: 149
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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P0CV09 | MRLYTQVVAASLVATLAIVDSKVSNAIAGQGNNLRFLRQDNATVARVSEDGERGGLLADEKDIMAIADHLIRLNYSLSYARKVLGKFANYEYAIAKVEEKIKKRTVSYMFLDEKFLTQEEAEGKFIEWILEGKTQEQLEREFDIFTRPESKRAKKIQEVNKFAIRAYLDWLRNLRARSFRMTMMEYTNPSNAFATFDRHGHSRNKILSMFDAWVAKGTLLDVVKDRLGFNKPMKPADMFHSDNFVAYATYAQMLREKNNSLRPPRLDSVSTPSN | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 31528
Sequence Length: 274
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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P0CV10 | MLGFVTGVLAISAHVIVSQPNEHSPVVVARETYGLRDVIFRRLRSYETDTASARAEEGTSDIEERSDHEIPPDFYKRLASTSTPYVANLSHKAQIAAQALRKDAERSKGALELLKKYAELEGKMDAPKEEKNHVDRLKAAAFKEWNEKGLNLDQVRVLFADNKRRTSKYENLIEKIVGEYEKS | Function: Secreted effector that dos not suppress the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 20718
Sequence Length: 183
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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P0CV11 | MKVTMALAALCVALQAPCIGSESTPSNLNNRHLRHEHDSNTPLQRRDEALVPAHRVYDPVSGLACSLVGKCMVCPTSEKDESYCRETGYRQELDCPRVEDDVVHTKSVNQRTTRFRPCSFAEPARPGVAFVKFEVGNLRTLLQKL | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 16183
Sequence Length: 145
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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P0CV12 | MSIFIFISLVLGLAHQHKRSSIIVRLYSKDGFQKCSLTIRAVSAYALACKLQLEHRPLRAQRLRQIRLAQKSRVFPFIFYQCPHKKKSARIHALTFTKEAELSKLSIETLRCIHLQLISCTRSPVVTNSSY | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 15100
Sequence Length: 131
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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P0CV13 | MICLLPLIAVMLFVFATHTVLALEIATGIDAPETEFSASTQTTRVSFRRITSVDNKRFLRQETTFEEKPSVNDVHAEERSSFYRKFLYRLFGDRMDVEAKVLARDSNWLINIFRRKFLRWAGREEHPHKATTFDTTCCQVAPYDPVTSS | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 17270
Sequence Length: 149
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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P0CV14 | MCCVSWNWVLACTFLLIFLSWWNCCNDRISVNSGVPGMAARVAGAHHVVLTEQDELLRLLRVNLAANAEVLTHEIEEEKGGIVARPLSWGIEHTKEYLARYGDEKIDVILSCDCIYEPLYGTSWKGLAQTMELLCLANPKSVVLLAVERRNEDGIDKFLAFVEKETMLLYRRDEVTVGSSKNRLEVYHLHLENILKN | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 22408
Sequence Length: 197
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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A0A182BSS2 | MIRRSPLVAVILFVAITHVVLALDDATRIDSSEIVPSEPTRRTRVSPHYISSGGSKRSLRQQAFRPVAYLKNKLNWFLSRFFGTPTDAFTQMNSPRSSRIANIFRKIYMHTAKDDEYFSRLRSV | 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): 14276
Sequence Length: 124
Domain: Has a conserved RxLR motif that acts to carry the protein into the host cell cytoplasm. Lacks the 'so-called' EER motif, which is found closely behind the RxLR motif in most of RxLR effector family members, but the presence of an EER motif is not always essential for the translocation of every RxLR effector into host cells, or for inducing a hypersensitive response.
Subcellular Location: Secreted
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P0CV15 | MRSSTVLYVLGAAILAVNGVTTALISDGVDKGSQEQTRWLRSNAMEHETDDEERVLEFKLPSSISTWRAERFERLESLEKQKEMERQAVLELVDKYAPLLLTDRMFAGFTKLDQEGIPLPSMIALLREHGKDITSEMEAYLINSYKTTHKIPLELNTAR | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 18115
Sequence Length: 159
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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P0CV16 | MRSSTILFVLGVAMVAVNGVTTALISDGTGKGTQGKHRLLRSNSGKHKTDEERLKLSARIYGTKAYKKRQVRNRESARKFQKALLNMADGNDIARLLKKRNTTLKGLFALLARNKAGLPKEAKNHITTVYNTRRGGVL | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 15248
Sequence Length: 138
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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P0CV17 | MIFTLLGLALVATKSACIAHVFILQLGALDMEALATPLAKVIATSARALHTRSLRASERDKCTNLTARSTRALLAHGPRLRHAVQQQAVAALFTIAVARRRRTA | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 11197
Sequence Length: 104
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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A0A182BSS3 | MAASRSSITTLLLLIVAVALGYGILPISAKTSVARQLREQVDFVDAAALSESATSSSSSSALDHKSSAPGEATNASETEHSAASTASEPKHEGPTMMSFVGPAAAGVLAILLIGAVIAFKKRMNK | 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12700
Sequence Length: 125
Domain: Has a conserved RxLR motif that acts to carry the protein into the host cell cytoplasm. Lacks the 'so-called' EER motif, which is found closely behind the RxLR motif in most of RxLR effector family members, but the presence of an EER motif is not always essential for the translocation of every RxLR effector into host cells, or for inducing a hypersensitive response.
Subcellular Location: Secreted
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P0CV18 | MHRKRLRVVLSATLLDLITCVQLMLDPLVRSHVIARLVRWRHHRLLLAELVLSETRVRILRLALEQGALESGAMSSRALARIVIPRSSSRPNWKLSRVVSELSDNSKTNVYKNQLFIHCARYLLHVLP | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 14762
Sequence Length: 128
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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A0A182BSS4 | MAFQLRIVQHLLHITFLRLPLAYPSQIHQRENERMFLLRIHRQDVQHLSHRRLRQLNEHRSLLPKGFPFKLLRPLPQLQRLLSQVCRGSVRIDACCCIPSCH | Function: Effector that partially suppresses the tobacco programmed cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 12219
Sequence Length: 102
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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A0A172M490 | MQRFPYSLLLLLLSATNRSRRHHITRPGRSIHWCLVRPTRPNRMLRAIRTCGARYWRNWPLNWPRKAGLTRRSSARIGLSDALRPCPTLFGCFKRRYARQAMSCYCRTEWRVNWLKKKRRGSSRWRRESSVWRCWK | Function: Effector that partially suppresses the tobacco programmed cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 16589
Sequence Length: 136
Domain: Has a conserved RxLR motif that acts to carry the protein into the host cell cytoplasm. Lacks the 'so-called' EER motif, which is found closely behind the RxLR motif in most of RxLR effector family members, but the presence of an EER motif is not always essential for the translocation of every RxLR effector into host cells, or for inducing a hypersensitive response.
Subcellular Location: Secreted
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A0A182BSS5 | MMSPPMTTTLMFILNYAIISFHGQPSGISWGNHIETAEAAAILAMANRELRSRELLLWTSGSTHLLLQPILPLPLCLPFPLVPASIFKKMMLPLSAFSFWM | 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11272
Sequence Length: 101
Domain: Has a conserved RxLR motif that acts to carry the protein into the host cell cytoplasm. Lacks the 'so-called' EER motif, which is found closely behind the RxLR motif in most of RxLR effector family members, but the presence of an EER motif is not always essential for the translocation of every RxLR effector into host cells, or for inducing a hypersensitive response.
Subcellular Location: Secreted
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A0A172M476 | MHLRLLMSTVITATLIVSNNALTSPSDKTKTRALRGASTVGIAADNLLAAHFSPTLKHKESRGDYNNIQTERHRKRRLYDAPHHPEFYDIAVHQVPSDKSYGGGPAIAIFAGVAATFILIDYLIRHFTEN | 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14395
Sequence Length: 130
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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A0A172M477 | MRLYILVLAAIAVTLVFASSGPAITYHEVGTRALRQASITDEKSDDSLNAQAPPLSKSEKRLSRSFRTTSRRLPYTNYYHPQYYHPQNYHPHYNYPQYHSSPHVYVHQESKKSWFVRMILEAGIFWAVFHCLSAAFC | Function: Effector that partially suppresses the tobacco programmed cell death induced by cell death-inducing proteins.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15897
Sequence Length: 137
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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A0A172M4N1 | MRCVCASIRRTRIIEFLMFFALSSSTASCAPFSVSNVTHASPRPRWLRWHEKTSMAGNPVSLSIATPNGAKSSSICSANTVGFTPDTYTCPDIRDSSTDTLSRSKRISSLSLTKPISSSSESETKVLSAS | 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): 14013
Sequence Length: 130
Domain: Has a conserved RxLR motif that acts to carry the protein into the host cell cytoplasm. Lacks the 'so-called' EER motif, which is found closely behind the RxLR motif in most of RxLR effector family members, but the presence of an EER motif is not always essential for the translocation of every RxLR effector into host cells, or for inducing a hypersensitive response.
Subcellular Location: Secreted
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A5PJU7 | MAAPTDSLSVSGPTAVRLPRSPPIKVLAEQLRRDAEGGPGSWRLSRAAVGREPLELRAVWMQGTVVEAGGGVARLRDPSGSFSVRGLERVPRGRPCLVPGKYVMVMGVIQACSPEPCLQAVKMTDLSDNPLHESLWELEVEDLHRHIYSLDDVGTGD | Function: Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates. It is required to regulate sister chromatid segregation and to limit DNA crossover. Essential for the stability, localization, and function of BLM, TOP3A, and complexes containing BLM. In the RMI complex, it is required to target BLM to chromatin and stress-induced nuclear foci and mitotic phosphorylation of BLM.
PTM: Phosphorylated during mitosis.
Sequence Mass (Da): 16948
Sequence Length: 157
Subcellular Location: Nucleus
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Q96E14 | MAAAADSFSGGPAGVRLPRSPPLKVLAEQLRRDAEGGPGAWRLSRAAAGRGPLDLAAVWMQGRVVMADRGEARLRDPSGDFSVRGLERVPRGRPCLVPGKYVMVMGVVQACSPEPCLQAVKMTDLSDNPIHESMWELEVEDLHRNIP | Function: Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates. It is required to regulate sister chromatid segregation and to limit DNA crossover. Essential for the stability, localization, and function of BLM, TOP3A, and complexes containing BLM. In the RMI complex, it is required to target BLM to chromatin and stress-induced nuclear foci and mitotic phosphorylation of BLM.
PTM: Phosphorylated during mitosis.
Sequence Mass (Da): 15865
Sequence Length: 147
Subcellular Location: Nucleus
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Q8WU17 | MAAVGPPQQQVRMAHQQVWAALEVALRVPCLYIIDAIFNSYPDSSQSRFCIVLQIFLRLFGVFASSIVLILSQRSLFKFYTYSSAFLLAATSVLVNYYASLHIDFYGAYNTSAFGIELLPRKGPSLWMALIVLQLTFGIGYVTLLQIHSIYSQLIILDLLVPVIGLITELPLHIRETLLFTSSLILTLNTVFVLAVKLKWFYYSTRYVYLLVRHMYRIYGLQLLMEDTWKRIRFPDILRVFWLTRVTAQATVLMYILRMANETDSFFISWDDFWDLICNLIISGCDSTLTVLGMSAVISSVAHYLGLGILAFIGSTEEDDRRLGFVAPVLFFILALQTGLSGLRPEERLIRLSRNMCLLLTAVLHFIHGMTDPVLMSLSASHVSSFRRHFPVLFVSACLFILPVLLSYVLWHHYALNTWLFAVTAFCVELCLKVIVSLTVYTLFMIDGYYNVLWEKLDDYVYYVRSTGSIIEFIFGVVMFGNGAYTMMFESGSKIRAFMMCLHAYFNIYLQAKNGWKTFMNRRTAVKKINSLPEIKGSRLQEINDVCAICYHEFTTSARITPCNHYFHALCLRKWLYIQDTCPMCHQKVYIEDDIKDNSNVSNNNGFIPPNETPEEAVREAAAESDRELNEDDSTDCDDDVQRERNGVIQHTGAAAEEFNDDTD | Function: E3-ubiquitin ligase; acts as a negative regulator of cell proliferation through mechanisms involving G2/M arrest and cell death . Required for MHC class I ubiquitination in cells expressing the cytomegalovirus protein US2 before dislocation from the endoplasmic reticulum (ER) . Affects SREBP processing by hindering the SREBP-SCAP complex translocation from the ER to the Golgi, thereby reducing SREBF2 target gene expression . Involved in the sterol-accelerated degradation of HMGCR . This is achieved through binding of RNF139 to INSIG1 and/or INSIG2 at the ER membrane . In addition, interaction of RNF139 with AUP1 facilitates interaction of RNF139 with ubiquitin-conjugating enzyme UBE2G2 and ubiquitin ligase AMFR, leading to ubiquitination of HMGCR . The ubiquitinated HMGCR is then released from the ER into the cytosol for subsequent destruction . Required for INSIG1 ubiquitination . May be required for EIF3 complex ubiquitination .
PTM: Autoubiquitinated. Ubiquitination is induced by sterol and leads to ist degradation via the ubiquitin-proteasome pathway.
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): 75994
Sequence Length: 664
Domain: The RING-type zinc finger domain mediates ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
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Q5RBT7 | MAAVGPPQQQVRMAHRQVWAALEVALRVPCLYIIDAIFNSYPDSSQSRFCIVLQIFLRLLGIFVSSIVLILSQRSLFKFYMYSSAFLLAATSVLVNYYASLHIDFYGAYNTSAFGIELLPRKGPSLWMALIVLQLTFGIGYVTLLQIHSIYSQLIILDLLVPVIGLITELPLHIRETLVFTSSLILTLNTVLVLAVKLKWFYYSTRYVYLLVRHMYRIYGLQLLMEDTWKRIRFPDILRVFWLTRVTAQATVLMYILRMANETDSFFISWDDFWDLICNLIISGCDSTLTVLGMSAVISSVAHYLGLGILAFIGSTEEDDRRLGFVAPVLFFILALQTGLSGLRPEERLIRLSRNMCLLLTAVLHFIHGMTDPVLMSLSASHVSSFRRHFPVLFVSACLFILPVLLSYVLWHHYALNTWLFAATAFCVELCLKVIVSLTVYTLFMIDGYYNVLWEKLDNYVYYVRSTGSIIVFIFGVVMFGNGAYTMMFESGSKIRAFMMCLHAYFNIYLQAKNGWKTFMNRRTAVKKINSLPEIKGSRLQEINDVCAICYHEFTTSARITPCNHYFHALCLRKWLYIQDTCPMCHQKVYIEDDIKDNSNVSNNNGFTPPNETPEEAVREAAAESDRELNEDDSTDCDDDVQRERNGVIQHTGAAAEEFNDDTD | Function: E3-ubiquitin ligase; acts as a negative regulator of cell proliferation through mechanisms involving G2/M arrest and cell death. Required for MHC class I ubiquitination in cells expressing the cytomegalovirus protein US2 before dislocation from the endoplasmic reticulum (ER). Affects SREBP processing by hindering the SREBP-SCAP complex translocation from the ER to the Golgi, thereby reducing SREBF2 target gene expression. Involved in the sterol-accelerated degradation of HMGCR. This is achieved through binding to INSIG1 and/or INSIG2 at the ER membrane. In addition, interaction of RNF139 with AUP1 facilitates interaction of RNF139 with ubiquitin-conjugating enzyme UBE2G2 and ubiquitin ligase AMFR, leading to ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Required for INSIG1 ubiquitination. May be required for EIF3 complex ubiquitination.
PTM: Autoubiquitinated. Ubiquitination is induced by sterol and leads to ist degradation via the ubiquitin-proteasome pathway.
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): 75941
Sequence Length: 664
Domain: The RING-type zinc finger domain may be essential for ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
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Q8WVD5 | MGQQISDQTQLVINKLPEKVAKHVTLVRESGSLTYEEFLGRVAELNDVTAKVASGQEKHLLFEVQPGSDSSAFWKVVVRVVCTKINKSSGIVEASRIMNLYQFIQLYKDITSQAAGVLAQSSTSEEPDENSSSVTSCQASLWMGRVKQLTDEEECCICMDGRADLILPCAHSFCQKCIDKWSDRHRNCPICRLQMTGANESWVVSDAPTEDDMANYILNMADEAGQPHRP | Function: May be involved in spermatogenesis.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25535
Sequence Length: 230
Subcellular Location: Membrane
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Q95Y82 | MEGVMENVGGLMQNIRRRHMSITEMTEESVRLGVAQMDTGFKKIKEMSIMVLETGLRLPGLLFIELLWRYQGFSFEDISDDMMKQTPLSYFDIPTMLDFVHRRNFDHHAAIILSYFVIFISLMFLTLPLSRLIRMYSHFLSVFLFGVAYKLSAIYVDLEMKTGEEELKLDGLIKLERHGFHFLAQMLLVVLQSMLLEVDGEPWRVALPVFALPIVARMCGCPMDKLKNAHNYACTGTMIFIATYMLYRAPSLIKSTKTALRQIKAVFMVHGLADGVAVLWRKLRILELLTFTWITMFLMVLYVELIDKGRTWSEVGRILLTGVAETTNTPITLAALAVSVSYVCKWIADLTKLITGGTRSHGHVLAHSGYTEAVSVVILCIQTGFLGMQVEQKTILLALVLYIVISALLQSLFEIIEVVLLNLPSSPTASRARHARCICIALLLVVIPFFTTKTMLALLPIDIYTAIIIANSATVTARAIGVILKYIVLIVETKSEEPWEGIDDLTYYIDCANKGIELLAAKVVMVFGCMQVVKVGFSFATFAILLFHVIVNIYKRLEHTVSFIKNRNAAVKNINRLSKADVVQLREREDVCAICFIEMKEEARITPCKHYFHGPCLRKWLAVKMVCPLCYTYMKEDDFDSKSSSSGTLNEVQQNEEGAAVEENPENPEEQPEAPNAERAPGDMFDWDDLFGFRAERETRNRNEQRIHGARDMWPLLVDNDAYESDSDAGSEELVIEEENNN | Function: E3 ubiquitin ligase that catalyzes the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate (By similarity). Acting downstream of probable Golgi transport protein eas-1, involved in inhibition of activation of transcription factor sbp-1, thereby playing a role in regulating AMsh glial cell size .
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): 83994
Sequence Length: 742
Subcellular Location: Membrane
EC: 2.3.2.27
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Q96MT1 | MAAKEKLEAVLNVALRVPSIMLLDVLYRWDVSSFFQQIQRSSLSNNPLFQYKYLALNMHYVGYILSVVLLTLPRQHLVQLYLYFLTALLLYAGHQISRDYVRSELEFAYEGPMYLEPLSMNRFTTALIGQLVVCTLCSCVMKTKQIWLFSAHMLPLLARLCLVPLETIVIINKFAMIFTGLEVLYFLGSNLLVPYNLAKSAYRELVQVVEVYGLLALGMSLWNQLVVPVLFMVFWLVLFALQIYSYFSTRDQPASRERLLFLFLTSIAECCSTPYSLLGLVFTVSFVALGVLTLCKFYLQGYRAFMNDPAMNRGMTEGVTLLILAVQTGLIELQVVHRAFLLSIILFIVVASILQSMLEIADPIVLALGASRDKSLWKHFRAVSLCLFLLVFPAYMAYMICQFFHMDFWLLIIISSSILTSLQVLGTLFIYVLFMVEEFRKEPVENMDDVIYYVNGTYRLLEFLVALCVVAYGVSETIFGEWTVMGSMIIFIHSYYNVWLRAQLGWKSFLLRRDAVNKIKSLPIATKEQLEKHNDICAICYQDMKSAVITPCSHFFHAGCLKKWLYVQETCPLCHCHLKNSSQLPGLGTEPVLQPHAGAEQNVMFQEGTEPPGQEHTPGTRIQEGSRDNNEYIARRPDNQEGAFDPKEYPHSAKDEAHPVESA | Function: E3 ubiquitin ligase that catalyzes the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. In response to bacterial infection, negatively regulates the phagocyte oxidative burst by controlling the turnover of the NADPH oxidase complex subunits. Promotes monoubiquitination of CYBA and 'Lys-48'-linked polyubiquitination and degradation of CYBB NADPH oxidase catalytic subunits, both essential for the generation of antimicrobial reactive oxygen species. Involved in the maintenance of cholesterol homeostasis. In response to high sterol concentrations ubiquitinates HMGCR, a rate-limiting enzyme in cholesterol biosynthesis, and targets it for degradation. The interaction with INSIG1 is required for this function. In addition, triggers ubiquitination of SCAP, likely inhibiting its transport to the Golgi apparatus and the subsequent processing/maturation of SREBPF2, ultimately down-regulating cholesterol biosynthesis.
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): 75617
Sequence Length: 663
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
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Q5SWK7 | MAAKEKLEAVLNVALRVPSIMLLDVLYRWDVSSFFQQIQRSSLNNNPLFQYKYLALNMHYVGYILSVVLLTLPRQHLVQLYLYFVTALLLYAGHQISRDYVRSELESAYEGPMYLEPLSMNRFTTALIGQLVVCTLCSCVMKTKQIWLFSAHMLPLLARLCLVPLETIVIINKFAMIFTGLEVLYFLGSNLLVPYNLAKSAYRELVQVVEVYGLLALGMSLWNQLVVPVLFMVFWLVLFALQIYSYFSTRDQPASRERLLFLFLTSIAECCSTPYSLLGLVFTVSFVALGVLTLCKFYLQGYRAFMNDPAMNRGMTEGVTLLILAVQTGLIELQVVHRAFLLSIILFIVVASILQSMLEIADPIVLALGASRDKSLWKHFRAVSLCLFLLVFPAYMAYMICQFFHMDFWLLIIISSSILTSLQVLGTLFIYVLFMVEEFRKEPVENMDDVIYYVNGTYRLLEFVVALCVVAYGVSETIFGEWTVMGSMIIFIHSYYNVWLRAQLGWKSFLLRRDAVNKIKSLPVATQEQLEKHNDICAICYQDMKSAVITPCSHFFHAGCLKKWLYVQDTCPLCHCHLKNSSQLPGLGTEAAPQPPAGAEQNIVLQEGPEPPDHESPPGTGTQEGSGDSSEHINRGSASQEGAADAGEGPQIPEGEVCPVESA | Function: E3 ubiquitin ligase that catalyzes the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. In response to bacterial infection, negatively regulates the phagocyte oxidative burst by controlling the turnover of the NADPH oxidase complex subunits. Promotes monoubiquitination of CYBA and 'Lys-48'-linked polyubiquitination and degradation of CYBB NADPH oxidase catalytic subunits, both essential for the generation of antimicrobial reactive oxygen species . Involved in the maintenance of cholesterol homeostasis. In response to high sterol concentrations ubiquitinates HMGCR, a rate-limiting enzyme in cholesterol biosynthesis, and targets it for degradation. The interaction with INSIG1 is required for this function . In addition, triggers ubiquitination of SCAP, likely inhibiting its transport to the Golgi apparatus and the subsequent processing/maturation of SREBPF2, ultimately down-regulating cholesterol biosynthesis .
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): 74648
Sequence Length: 663
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
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Q7ZUK0 | MASCGEVNLTVDSLTSGKKVSGEAVPEGSGSPSSPSLPVPECPICLQSCVHPVRLPCRHIFCFLCVKGASWHSKRCALCRREVPEDFLERPTLLSPEELKASATGGCGTGSSGHAWYYEGRNGWWQYDERTSRELEDAFSKGKKSAEMLIAGFLYVADLENMVQYRRNEHGRRRRMKRDVVDIPKKGVAGLRLDPDPNSSAGAVPAPAVVDVSVDGAAAERESSADGADTGVSGGRPQGTFVPAPIRPPTILGGHLTSPASSSDIQLVQTLAQLNISPNEQEPEEEDAEDEDDSAAPDASGYDSESGTSDDDEQVEDEDENEHTDGSQGKHRLQQLNRPPPGGGPANSGDRSGCPDGQCTVTKV | Function: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of poly-ADP-ribosylated proteins. Neuroprotective protein. Protects against cell death induced by DNA damaging agents and rescues cells from G1 arrest. Promotes cell survival after gamma-irradiation. Facilitates DNA repair.
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): 38786
Sequence Length: 364
Domain: The WWE domain mediates non-covalent poly(ADP-ribose)-binding.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q9NTX7 | MMAGCGEIDHSINMLPTNRKANESCSNTAPSLTVPECAICLQTCVHPVSLPCKHVFCYLCVKGASWLGKRCALCRQEIPEDFLDKPTLLSPEELKAASRGNGEYAWYYEGRNGWWQYDERTSRELEDAFSKGKKNTEMLIAGFLYVADLENMVQYRRNEHGRRRKIKRDIIDIPKKGVAGLRLDCDANTVNLARESSADGADSVSAQSGASVQPLVSSVRPLTSVDGQLTSPATPSPDASTSLEDSFAHLQLSGDNTAERSHRGEGEEDHESPSSGRVPAPDTSIEETESDASSDSEDVSAVVAQHSLTQQRLLVSNANQTVPDRSDRSGTDRSVAGGGTVSVSVRSRRPDGQCTVTEV | Function: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation . May regulate many important biological processes, such as cell survival and DNA damage response . Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex . Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2 . Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination, leading to their degradation . Different ubiquitin linkage types have been observed: TNKS2 undergoes ubiquitination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48' . May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location . Neuroprotective protein . Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos (By similarity). Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner (By similarity). Does not affect PARP1 activation (By similarity). Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest (By similarity). Promotes cell survival after gamma-irradiation . Facilitates DNA repair .
PTM: Ubiquitinated; autoubiquitinated. Polyubiquitinated in the presence of UBE2D1, UBE2D2 and UBE2D3. Multimonoubiquitinated in the presence of UBE2E1. Not ubiquitinated in the presence of UBE2H, CDC34, UBE2L3, UBE2L6, nor UBE2C. In the absence of PAR, autoubiquitination occurs on Lys-85, Lys-95 and Lys-176 via 'Lys-11' and 'Lys-48' ubiquitin linkages. In the presence of PAR, Lys-131 and Lys-176 are ubiquitinated via 'Lys-6', 'Lys-33' and 'Lys-48' ubiquitin linkages. Autoubiquitination is enhanced upon PAR-binding.
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): 38950
Sequence Length: 359
Domain: The WWE domain mediates non-covalent PAR-binding.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q97YD2 | MEVHVCSVGTSLLKNSLDDDNVRKEIERLGLKDWDRLKFDDDRQNRIKENFDSLRKMLLKFIRSKGRRASAELDSLFSTFEKLKHNKSEIYVFLYSTNTSNSQLAGEVIRDYLIEEGIRSELVTVKTISSEENFYEGIVDLFDKVIYRILKFKEQDNEVYINATPGLKPESIFLTLAGLLAGADLIYYKYQEFNDVVILPSPPITIRPKYLDWLIRFAISGYTLSEKRAEELGIPVRLLEAKMLVERKGEDAYRLKDWVRKLLGIYLPIGAQNKYYRVIVEGEGERTFDNEVEAYNYMESKRKEGKNVRVEVPDRVYFLGL | 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. Slowly degrades cA4 (a tetraadenylate ring) into first a linear tetraadenylate product and secondly into a linear diadenylate product with 5'-OH and 2',3'-cyclic phosphate termini. Is 10-fold less active than SSO2081, suggesting it plays a minor role in cA4 degradation. There may be 2 active sites per homodimer .
Catalytic Activity: cyclic tetraadenylate = 2 5'-hydroxy-diadenylate 2',3'-cylic phosphate
Sequence Mass (Da): 37448
Sequence Length: 321
Subcellular Location: Cytoplasm
EC: 4.6.1.-
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Q05823 | MESRDHNNPQEGPTSSSGRRAAVEDNHLLIKAVQNEDVDLVQQLLEGGANVNFQEEEGGWTPLHNAVQMSREDIVELLLRHGADPVLRKKNGATPFILAAIAGSVKLLKLFLSKGADVNECDFYGFTAFMEAAVYGKVKALKFLYKRGANVNLRRKTKEDQERLRKGGATALMDAAEKGHVEVLKILLDEMGADVNACDNMGRNALIHALLSSDDSDVEAITHLLLDHGADVNVRGERGKTPLILAVEKKHLGLVQRLLEQEHIEINDTDSDGKTALLLAVELKLKKIAELLCKRGASTDCGDLVMTARRNYDHSLVKVLLSHGAKEDFHPPAEDWKPQSSHWGAALKDLHRIYRPMIGKLKFFIDEKYKIADTSEGGIYLGFYEKQEVAVKTFCEGSPRAQREVSCLQSSRENSHLVTFYGSESHRGHLFVCVTLCEQTLEACLDVHRGEDVENEEDEFARNVLSSIFKAVQELHLSCGYTHQDLQPQNILIDSKKAAHLADFDKSIKWAGDPQEVKRDLEDLGRLVLYVVKKGSISFEDLKAQSNEEVVQLSPDEETKDLIHRLFHPGEHVRDCLSDLLGHPFFWTWESRYRTLRNVGNESDIKTRKSESEILRLLQPGPSEHSKSFDKWTTKINECVMKKMNKFYEKRGNFYQNTVGDLLKFIRNLGEHIDEEKHKKMKLKIGDPSLYFQKTFPDLVIYVYTKLQNTEYRKHFPQTHSPNKPQCDGAGGASGLASPGC | Cofactor: Manganese or magnesium. Required for optimal RNA cleavage rates.
Function: Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. In the crosstalk between autophagy and apoptosis proposed to induce autophagy as an early stress response to small double-stranded RNA and at later stages of prolonged stress to activate caspase-dependent proteolytic cleavage of BECN1 to terminate autophagy and promote apoptosis . Might play a central role in the regulation of mRNA turnover . Cleaves 3' of UpNp dimers, with preference for UU and UA sequences, to sets of discrete products ranging from between 4 and 22 nucleotides in length.
Sequence Mass (Da): 83533
Sequence Length: 741
Domain: The nine ankyrin repeats also called 2-5A sensor constitute the N-terminus 2-5A binding domain.
Subcellular Location: Cytoplasm
EC: 3.1.26.-
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P59107 | MFQDNPLLAQLKQQLHSQTPRAEGVVKATEKGFGFLEVDAQKSYFIPPPQMKKVMHGDRIIAVIHSEKERESAEPEELVEPFLTRFVGKVQGKNDRLTIVPDHPLLKDAIPCRAARGLNHEFKEGDWAVAEMRRHPLKGDRSFYAELTQYITFGDDHFVPWWVTLARHNLEKEAPDGVATEMLDEGLVREDLTSLDFVTIDSASTEDMDDALFAKALPDDKLQLIVAIADPTAWIAEGSKLDKAAKIRAFTNYLPGFNIPMLPRELSDDLCSLRANEVRPVLACRMTLSADGTIEDNIEFFAATIESKAKLVYDQVSDWLENTGDWKPESEAIAEQVRLLAQICQRRGEWRHNHALVFKDRPDYRFILGEKGEVLDIVAEPRRIANRIVEEAMIAANICAARVLRDKLGFGIYNVHMGFDPANADALAALLKTHGLHVDAEEVLTLDGFCKLRRELDAQPTGFLDSRIRRFQSFAEISSEPGPHFGLGLEAYATWTSPIRKYGDMINHRLLKAVIKGETATRPQDEITVQMAERRRLNRMAERDVGDWLYARFLKDKAGTGTRFAAEIVDISRGGMRVRLVDNGAIAFIPAPFLHAVRDELVCSQENGTVQIKGETVYKVTDVIDVTIAEVRMETRSIIARPVA | Function: Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 72465
Sequence Length: 644
Subcellular Location: Cytoplasm
EC: 3.1.13.1
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Q7MEL4 | MFQDNPLLAQLKQQIQENLPKKEGTIKATEKGFGFLEVDSKTSFFIPPAYMKKCMHGDKVIAIIRTENEREVAEPQELVEQMLNRFIGRVKMFKGKLNVVPDHPQLKKMSLKAKTKKGLNPQEFAEGDWVVGHLIRHPLKDDNGFFVEISEKITDADDKIAPWWVTLAENDLPNSEPAGIDDWQIKDDADLERIDMTHIPFVTIDGESTKDMDDALYAKKNDAGDFELTIAIADPTAYITPDDEMDKVARERGFTIYLPGRNIPMLPRDLADELCSLIEGEIRPALCCTVTVSKDGVIGDDIQFFAANIKSHARLAYDNVSDWLETGSCEKWQPSEEIAAIVRDLYEFSQARAEWREKNAVVFPDRPDYRFELSEDNDVVAIHADMRRSANRLVEESMITANICAGKTLQAHFGTGVFNCHAGFKPEKIADVVELVNPEGTLEFTAESIATREGFAALRRWLSKQETTYLDNRIRKFQTYSEVSNQPLPHYAMGLDIYATWTSPIRKYGDMINHRMLKALILNKEPVQKPDDSVGEELALHRKHHKIAERNVADWLYARTLADAPENQTLFTGEIFDINRAGMRIRLLENGAAAFIPGSLIIDNKERIECNGDLGTVSIDKEVVYKLGDVLEVVLADVNQENRSLVAKPTQVFAELPVVEETQN | Function: Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 75069
Sequence Length: 664
Subcellular Location: Cytoplasm
EC: 3.1.13.1
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Q6GZP5 | MEGWLGNLLAKSVKDKYIPVIVGRRDLWNKVFTPKSVNPDDNYEALEIVGDGVASYFFPSYFLKRFPQLNSPKGVKTVARLKIYYGSKKSFSSIADSLGFWKFIRSGPVPVNPSTRESLLEDTFEAFLGAVCMAVDDEYSIDGLGAVVAYKIMADIFDDMDISLEYTALFDTVTRLKELMDVKKDVLGGDAVYNHRGDTTVITLKGRVIGKATGAIKRDRAKEAAGQALDLLRREGHFREHDDDAVVKVAKGPAGDGLVVAQSALGGFTVFGAESGVVEGSGGTVAQALSRVVGTKRPSAVEVAGGDYKSLLKEYLESVGETDSVNYIHEGVTVTMTRKGKPVATANHLVKKVREQLASRDYYRTVHAKGV | Function: Digests double-stranded RNA.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 40362
Sequence Length: 371
EC: 3.1.26.3
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Q8RGX3 | MKNLLDLEHKLNYYFNDRNLLKNALLHKSLGNERKEYKNQTNERLELLGDAVLDLIVAEYLYKSYKNASEGPIAKLKAMIVSEPILAKISRQIGVGKFLMLSRGEVMSGGRNRESILADSFEAILGAVYIDSNLDEARVFALSHIKQYIDHIEENEDILDFKSILQEYVQKEFKTVPTYELVAERGPDHMKEFEIQVIVGNYKEKAVARNKKKAEQLSAKALCIKLGVKYNEAL | 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): 26756
Sequence Length: 234
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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Q74AX1 | MRETDEQPVAGGAASTEGLETSIGYRFTDRRFLDEALTHRSWLNEVRSPTVPDNERLEFFGDAILGFCIGKMLLRHYPESREGALARMKSALVGEETLADLAAAVELGSYLRLGRGEERSGGRHRRSLLANALEALLAAMYLDGGMAPVERLVDAWFGPRLAGVAAGIKGRDFKTDFQELAQAQYGGLPRYVLVDTSGPAHDLRFTVAAYVGERLLGQGTGRSKKEAEQAAARQCLERLETGRCSAAP | 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): 27017
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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Q7NH89 | MAESALTPLRLAQLRRFAARFALSEPEALSWELLHRALIHPSWSAQEGGEDNDRLEFLGDEILRLLAAEFLYRADPELTVGEMTAVRSVLVSDVALAELAEGYDLGEFLVVGRSASGDERGRITRLADGFEAVIGALYLSTGDLGLIRPWLLPHLAHLAESVMADPTRGNHKSALQELTQKLAAGELPEYRLVDPGPPFRYEVWALGRLWGSGEGPSKKLAQQRAARGAYAALRSAFDTALQ | 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): 26473
Sequence Length: 242
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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Q9KA05 | MPHSKNQRKHRHHSHSERRRQPKRLTLTAKQQQMFDELLRTLNLTFANKKLLVQAFTHSSYVNEHRIQSCKDNERLEFLGDAVLELAVSQYLYKAFEQMSEGDMTKLRASIVCEPSLAQLAEELHFGELVLLGKGEEMTGGRKRPALLADVFESFVGALYLDQGMDAVYLFLERTIYPKISEGAFSHMMDFKSQLQEFIQRDNLGHIHYEIVQERGPAHNREFVSEVVLNNETLGVGTGRSKKEAEQHAAQQALITLSQKKEQ | 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): 30224
Sequence Length: 263
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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Q7VIA9 | MSKSILPKSPQLLEKKLGYVFQNQQLLLEALTHKSCKKQYNNERLEFLGDAVLDLLVGEYLFKKFPLAKEGELSKLRACIVNEKGFMKLAQSLDLGAYLYISQSEENNNGRQKASILSNAFEALIGAIYLESSLTYVQSIIYDLLEYNYIKIDLDSLFMDYKTALQEITQAFYGEIPTYTLISESGPDHKKSFEIALSVQGKEYARASGNSKKEAQQKSAQIAYKKLYSKMNKTHHKGEK | 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): 27283
Sequence Length: 240
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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Q8Y0I1 | MSLEALQQRLGYRFSKPELLQQALTHRSHNAMHNERLEFLGDSILNCAVADMLYGMFGKLDEGDLSRVRANLVKQQALYEIAQMLLLPDELRLGEGELKSGGFRRPSILADALEAIFGAVFLDGGFDAARTLIRKLYIPILEQVDPRTLGKDAKTLLQEYLQGHKIALPQYAVVATHGAAHNQQFEVECTIPKLEIRVSGSGASRRAAEQSAAKLALEEAHRLVPQLVKRSRAERTGKTRKQATPPDPQLSLRLKE | 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): 28502
Sequence Length: 256
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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Q7UGZ7 | MDASSSSNPDDGLQAIRLVDASDDEPYADAVAKIERCQEILGYDFRDLDLLRSALTHASGASHRLASNERLEFLGDSVLGLTVCEWLFNEYPEYSEGDLTKIKSAVVSRRSCGKVACKLGLDQCLIVGRGVTRNRSYPKSLVSDVFEAVIAALYIDGGPEIVRDRLKLWLAEEVNLAVDTQGSGNHKSVLQQFAQRELSATPVYKLIRETGPDHRKMFLMGAMVDDRRFAPAWGNNKKDAEQRAAANALAELHNAKVPYDSEQPPA | 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): 29313
Sequence Length: 266
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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Q52698 | MKVAADLSAFMDRLGHRFTTPEHLVRALTHSSLGSATRPDNQRLEFLGDRVLGLSMAEALFHADGRASEGQLAPRFNALVRKETCAAVARDIDLGAVLKLGRSEMMSGGRRKDALLGDAMEAVIAAVYLDAGFEVARALVLRLWAARIQSVDNDARDPKTALQEWAQARGLPPPRYETLGRDGPDHAPQFRIAVVLASGETEEAQAGSKRNAEQAAAKALLERLERGA | Function: Digests double-stranded RNA. Involved in the processing of ribosomal RNA precursors and of some mRNAs. Complements an E.coli disruption mutant, but the E.coli enzyme does not cleave R.capsulatus rRNA precursor, showing substrate recognition is different. Probably also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Probably 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): 24663
Sequence Length: 228
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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Q6N6C1 | MTDDVTNVEQPSTASEQQPQDVPAAEPSAAKKRRANKAKSKATAAAIEQRLGHSFADPSLLTTAFTHVSALKSARRTDSYQRLEFLGDHVLGLIVSDMLYRAFPDADEGELSKRLADLVRKETCADVARSLDLVEGIKLGTVGAGAGAKLRKSVLGDICEAVIGAIYLDGGYEAASDFVRRNWTERMRKPARSLRDPKTVLQEWAQARGLPTPVYREVERTGPHHDPQFRVAVILPGLEPAEGLGGSKRAAEKVAASAMLAREGVGTGGNDG | 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): 29186
Sequence Length: 272
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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Q9ZE31 | MESFEKLETLLGYSFKNKELLIEALSHPSLRQYHEYKYDKDYERLEFLGDAVLNLLITEILFKNFENYKEGNLAKIRSYLVCKETICIVGTKLALKDYIIMTHGEEVAGGRDNPNNIENATEALIAAIYLDSNIEITHNIIEKLWAEFMKVQNLTDYDPKTALQEWAQANSHHLPIYRLIKREGAAHSSIFTVLVKVKDYEQTCTGYSIKEAEKKAARSLLHRLK | 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): 26006
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 3.1.26.3
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Q9UBS8 | MSSEDREAQEDELLALASIYDGDEFRKAESVQGGETRIYLDLPQNFKIFVSGNSNECLQNSGFEYTICFLPPLVLNFELPPDYPSSSPPSFTLSGKWLSPTQLSALCKHLDNLWEEHRGSVVLFAWMQFLKEETLAYLNIVSPFELKIGSQKKVQRRTAQASPNTELDFGGAAGSDVDQEEIVDERAVQDVESLSNLIQEILDFDQAQQIKCFNSKLFLCSICFCEKLGSECMYFLECRHVYCKACLKDYFEIQIRDGQVQCLNCPEPKCPSVATPGQVKELVEAELFARYDRLLLQSSLDLMADVVYCPRPCCQLPVMQEPGCTMGICSSCNFAFCTLCRLTYHGVSPCKVTAEKLMDLRNEYLQADEANKRLLDQRYGKRVIQKALEEMESKEWLEKNSKSCPCCGTPIEKLDGCNKMTCTGCMQYFCWICMGSLSRANPYKHFNDPGSPCFNRLFYAVDVDDDIWEDEVED | Function: E3 ubiquitin-protein ligase that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes . Recruited to stalled ribosomes by the ribosome collision sensor GCN1 and mediates ubiquitination of EEF1A1/eEF1A, leading to its degradation . In addition to EEF1A1/eEF1A, RNF14 catalyzes ubiquitination of other translation factors on stalled ribosomes: mediates ubiquitination and degradation of ETF1/eRF1 and ubiquitination of ribosomal proteins RPL0, RPL1, RPL12, RPS13 and RPS17 . Independently of its function in the response to stalled ribosomes, acts as a regulator of transcription in Wnt signaling via its interation with TCF transcription factors (TCF7/TCF1, TCF7L1/TCF3 and TCF7L2/TCF4) . May also play a role as a coactivator for androgen- and, to a lesser extent, progesterone-dependent transcription .
PTM: RING-type zinc finger-dependent and UBE2E2-dependent autoubiquitination.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Mass (Da): 53837
Sequence Length: 474
Domain: The N-terminal destruction box (D-box) acts as a recognition signal for degradation via the ubiquitin-proteasome pathway.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.31
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Q9JI90 | MSAEDLEAQEDELLALASIYDADEFRKAESVQGGETRIYLDLPQNFKIFVSGNSNESLQNSGFEYTICFLPPLVLNFELPPDYPSSSPPSFTLSGKWLSPTQLSALCKHLDNLWEEHRGRVVLFAWMQFLKEETLTYLNIVSPFELKMGSQKKVQRRATAQASSSTELGVGGAAAADVDQEETVDERAVQDVESLSSLIQEILDFNQARQTKCFNSKLFLCSICFCEKLGSDCMYFLECKHVYCKACLKDYFEIQIKDGQVKCLNCPEPQCPSVATPGQVKELVEADLFARYDRLLLQSTLDLMADVVYCPRPCCQLPVMQEPGGTMAICSSCNFAFCTLCRLTYHGLSPCKVTAEKLIDLRNEYLQADEATKRFLEQRYGKRVIQKALEEMESKDWLEKNSKSCPCCGTPIQKLDGCNKMTCTGCMQYFCWICMGSLSRANPYRHFTDSESPCFNRLFHAVDINGDMWEDEIEEDDDDEDDDDD | Function: E3 ubiquitin-protein ligase that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes (By similarity). Recruited to stalled ribosomes by the ribosome collision sensor GCN1 and mediates ubiquitination of EEF1A1/eEF1A, leading to its degradation (By similarity). In addition to EEF1A1/eEF1A, RNF14 catalyzes ubiquitination of other translation factors on stalled ribosomes: mediates ubiquitination and degradation of ETF1/eRF1 and ubiquitination of ribosomal proteins RPL0, RPL1, RPL12, RPS13 and RPS17 (By similarity). Independently of its function in the response to stalled ribosomes, acts as a regulator of transcription in Wnt signaling via its interation with TCF transcription factors (TCF7/TCF1, TCF7L1/TCF3 and TCF7L2/TCF4) (By similarity). May also play a role as a coactivator for androgen- and, to a lesser extent, progesterone-dependent transcription (By similarity). May regulate the expression of both mitochondrial and immune related genes in skeletal muscle .
PTM: RING-type zinc finger-dependent and UBE2E2-dependent autoubiquitination.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Mass (Da): 54926
Sequence Length: 485
Domain: The N-terminal destruction box (D-box) acts as a recognition signal for degradation via the ubiquitin-proteasome pathway.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.31
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Q9Y225 | MSSDFPHYNFRMPNIGFQNLPLNIYIVVFGTAIFVFILSLLFCCYLIRLRHQAHKEFYAYKQVILKEKVKELNLHELCAVCLEDFKPRDELGICPCKHAFHRKCLIKWLEVRKVCPLCNMPVLQLAQLHSKQDRGPPQGPLPGAENIV | Function: May play a role in TRPCs intracellular trafficking.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17210
Sequence Length: 148
Subcellular Location: Golgi apparatus membrane
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Q8BGI1 | MSSDFPHYNFRMPNIGFQNLPLNIYIVVFGTAVFVFILSLLFCCYLIRLRHQAHKEFYAYKQVILKEKVKELNLHELCAVCLEDFKPRDELGICPCKHAFHRKCLVKWLEVRKVCPLCNMPVLQLAQLHSKQDRGPPQEPLPGAENIV | Function: May play a role in TRPCs intracellular trafficking.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17254
Sequence Length: 148
Subcellular Location: Golgi apparatus membrane
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Q7SXJ6 | MAAESDVLSEIEVLQSIYLDELNVTQNDEGGWTVSLVLHPSTAEDCLSQFVRLTLTMDLDSQYPYSSPYISIHNPRGLSDDKLLSLQKSLQMEAEECVGTPVLYQLIERAKEILTDSNIPHGNCVICLYDFKEGEVFTKTSCYHYFHSHCLGRYITHSEMELKDRERELEEDKTRDRTEEEELAVVCPVCRESLTYDLDALLSSPAPVLCQQEDAVIGGEFKKKWEALQKILERQKEKGGVIDPEAESNRFLIHINEAPVNLSDTPGMTDSSGAESSQSLPSSSPDSTSTTQTSQNQHTAGQPQRKHTGDFKRGRRGRGAGRGGPARHMVPAPGEERLGKHIQSSDKINSANSGPTNTTSQVESTAQRQACELSENTAQLRQPLTNEENKPVSQDMLTSEPKDGQEVSQQKECISKEVTQTILQEGHPEREHVGRGDKRGSRGSARHHGHWQDRNYKGPGHWDNSGSAGHRGGAYRTREGGAGRGHRGGGAYRGGGRGMHQRVEKEFRKEGVL | Function: E3 ubiquitin-protein ligase that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes (By similarity). May also acts as a positive regulator of the Wnt signaling .
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): 56887
Sequence Length: 513
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q96BH1 | MAASASAAAGEEDWVLPSEVEVLESIYLDELQVIKGNGRTSPWEIYITLHPATAEDQDSQYVCFTLVLQVPAEYPHEVPQISIRNPRGLSDEQIHTILQVLGHVAKAGLGTAMLYELIEKGKEILTDNNIPHGQCVICLYGFQEKEAFTKTPCYHYFHCHCLARYIQHMEQELKAQGQEQEQERQHATTKQKAVGVQCPVCREPLVYDLASLKAAPEPQQPMELYQPSAESLRQQEERKRLYQRQQERGGIIDLEAERNRYFISLQQPPAPAEPESAVDVSKGSQPPSTLAAELSTSPAVQSTLPPPLPVATQHICEKIPGTRSNQQRLGETQKAMLDPPKPSRGPWRQPERRHPKGGECHAPKGTRDTQELPPPEGPLKEPMDLKPEPHSQGVEGPPQEKGPGSWQGPPPRRTRDCVRWERSKGRTPGSSYPRLPRGQGAYRPGTRRESLGLESKDGS | Function: E3 ubiquitin-protein ligase that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes . Catalyzes ubiquitination of RPS27A in response to ribosome collisions, promoting activation of RNF14 . RNF25 catalyzes ubiquitination of other ribosomal proteins on stalled ribosomes, such as RPL0, RPL1, RPL12, RPS13 and RPS17 . Also involved in ubiquitination and degradation of stalled ETF1/eRF1 . Independently of its function in the response to stalled ribosomes, mediates ubiquitination and subsequent proteasomal degradation of NKD2 (By similarity). May also stimulate transcription mediated by NF-kappa-B via its interaction with RELA/p65 .
PTM: Ubiquitinated; autoubiquitinated.
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): 51219
Sequence Length: 459
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q9QZR0 | MAASASTAAGEEDWVLPSEVEVLESIYLDELQVMKGNGRSPWEIFITLHPATAEVQDSQFVCFTLVLRIPVQYPHEVPQISIRNPRGLSDEQIHKISQALGHVAKEGLGTAMLYELIEKGKEILTDNNIPHGQCVICLYGFQEKEAFTKTPCYHYFHCHCLARYIQHMEQELTTQEQEQERQHVVTKQKAVGVQCPVCREPLVYDLASLKAAPEPQQPMELYQPSAESLRQQEELKLLYQRQQEKGGIIDLEAERNRYFISLQQPPAALEPESAVDVSREPQPPNALSAEQSTSLADQSTLPTSLPMTTQYTYEKTSGAGPNQQRPGETQKSVLDPPRHGRGSWRQYDRRHPKGGECCTPKGTSEIHELPPPEKPLKETVDLKAEPRNKGLTGHPQEKGPGSWQGPSARRTRDCARWERSKNRTPGSCYPHLPRGQGAYRSGTRREPLGLESEEGS | Function: E3 ubiquitin-protein ligase that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes (By similarity). Catalyzes ubiquitination of RPS27A in response to ribosome collisions, promoting activation of RNF14 (By similarity). RNF25 catalyzes ubiquitination of other ribosomal proteins on stalled ribosomes, such as RPL0, RPL1, RPL12, RPS13 and RPS17 (By similarity). Also involved in ubiquitination and degradation of stalled ETF1/eRF1 (By similarity). Independently of its function in the response to stalled ribosomes, mediates ubiquitination and subsequent proteasomal degradation of NKD2 . May also stimulate transcription mediated by NF-kappa-B via its interaction with RELA/p65 (By similarity).
PTM: Ubiquitinated; autoubiquitinated.
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): 51227
Sequence Length: 456
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q9BY78 | MEAVYLVVNGLGLVLDVLTLVLDLNFLLVSSLLASLAWLLAFVYNLPHTVLTSLLHLGRGVLLSLLALIEAVVRFTCGGLQALCTLLYSCCSGLESLKLLGHLASHGALRSREILHRGVLNVVSSGHALLRQACDICAIAMSLVAYVINSLVNICLIGTQNLFSLVLALWDAVTGPLWRMTDVVAAFLAHISSSAVAMAILLWTPCQLALELLASAARLLASFVLVNLTGLVLLACVLAVTVTVLHPDFTLRLATQALSQLHARPSYHRLREDVMRLSRLALGSEAWRRVWSRSLQLASWPNRGGAPGAPQGDPMRVFSVRTRRQDTLPEAGRRSEAEEEEARTIRVTPVRGRERLNEEEPPGGQDPWKLLKEQEERKKCVICQDQSKTVLLLPCRHLCLCQACTEILMRHPVYHRNCPLCRRGILQTLNVYL | Function: E3 ubiquitin-protein ligase that plays a key role in endosome organization by retaining vesicles in the perinuclear cloud . Acts as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1 through interaction with the ubiquitin conjugating enzyme UBE2J1 . Ubiquitinated SQSTM1 attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport . Also acts as a regulator of type I interferon production in response to viral infection by mediating the formation of 'Lys-11'-linked polyubiquitin chains on TMEM173/STING, leading to stabilize TMEM173/STING . Also required to limit type I interferon response by promoting autophagic degradation of IRF3 .
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): 47737
Sequence Length: 433
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
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Q8BUH7 | MEAVYLVVNGVGLVLDLLTLMLDLNFLLVSSLLATLAWLLAFIYNLPHTVLTSLLHLGRGFLLSLLALVEAVVRFTFGGLQALGTLLYSCYSGLESLKLLGHLASHGALRSREFLNRGILNMVSNGHALLRQACDICAIAMSLVAYVINSLVNICLISTQNFFSLVLALWDAVTGPLWRMTDVVAAFLAHISSSAVAMAILLWTPCQLALELLASAARLLASCVVFHLTGLVLLACVLAVILIVLHPEQTLRLATQALSQLHARPSYHRLWEDIVRLTRLPLGLEAWRRVWSRSLQLASWPNRGGAPGAPQGGPRRVFSARIQPQDTPPEAEEEVIRTAPARGREQLNEDEPAAGQDPWKLLKEQEERKKCVICQDQSKTVLLLPCRHLCLCQACTEILMRHPVYHRNCPLCRRSILQTLNVYL | Function: E3 ubiquitin-protein ligase that plays a key role in endosome organization by retaining vesicles in the perinuclear cloud. Acts as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1 through interaction with the ubiquitin conjugating enzyme UBE2J1. Ubiquitinated SQSTM1 attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport. Also acts as a regulator of type I interferon production in response to viral infection by mediating the formation of 'Lys-11'-linked polyubiquitin chains on TMEM173/STING, leading to stabilize TMEM173/STING. Also required to limit type I interferon response by promoting autophagic degradation of IRF3.
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): 46914
Sequence Length: 424
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
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A1TZ60 | MSTKTSSEIIKDGLWHNNPALVQVLGLCPLLAVTSTVVNAIGLGLATLLVLMGSNLSVSLIRNFVSESVRLPAFVMIIASFVTCAELLMQAFTYELYQILGIFIPLIVTNCAILGRADAFASKNPPLPAILDGAMMGIGFLAVLMTLGAMRELIGQGTLFADMHLLLGPMAADWVIRPLEQYPDMLFMVLPPGAFVGLGLLIALKNGIDNHLKERRKAAEPAPASTGSKRVRVTGTIS | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25388
Sequence Length: 238
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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Q8TSY1 | MYPHRRADMNPISEFIRGITKDNPTFGLVLGLCPTLAVTTSVENGIGMAMGTLFVLVGSNMMVSAIRKGIPGTVRLPVEIIVIATFVTIVDMVMEAFTPDLYTSLGVFIPLIVVNCIVIGRAEAYALKNGVFYSIIDALGEGTGFLLVLILIGGIRELLGTGIIDPFGMTLINLSGVINPAMFMTMSPGAFLTIAVLMTIVNYRRQQKAAKGG | 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: Multi-pass membrane protein
Sequence Mass (Da): 22745
Sequence Length: 213
Subcellular Location: Cell membrane
EC: 7.2.1.-
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P97055 | MSESYAKIARDGLWDKNIVTGQMLALCPTLAITGTATNGLGMGLATTVVLILSNVVISALRKTIAPEIRIPAFILIIAAIVTVVDLALNAWLHDLHKVLGLFIALIVTNCAILGRAEAFASRFGVLASALDGLMMGIGFTLALVVVGAIREILGSGTLFAQASLLLGPHFAFMELQIFPDYPGFLIMILPPGGFLVVGGLFALKRIIDARKPTIEQEIKQMRTERVFTAAGVLKPKLETGEEA | 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: Multi-pass membrane protein
Sequence Mass (Da): 25867
Sequence Length: 243
Subcellular Location: Cellular chromatophore membrane
EC: 7.-.-.-
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O70338 | MRWLLPLSRTVTLAVVRLRRGICGLGMFYAVRRGRRTGVFLSWSECKAQVDRFPAARFKKFATEDEAWAFVRSSSSPDGSKGQESAHEQKSQAKTSKRPREPLGEGEELPEPGPKHTRQDTEPAAVVSKDTFSYMGESVIVYTDGCCSSNGRKRARAGIGVYWGPGHPLNVGIRLPGRQTNQRAEIHAACKAIMQAKAQNISKLVLYTDSMFTINGITNWVQGWKKNGWRTSTGKDVINKEDFMELDELTQGMDIQWMHIPGHSGFVGNEEADRLAREGAKQSED | 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. Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 31805
Sequence Length: 285
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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Q9UST8 | MGGNKRAYYAVARGRNTGIYSTWDEASDQVKGYGGNRYKKFDSYEAAQEFCRTEGSRYSSSSGPYRRSTTSYGYSPYSSSSSNYSARHSDKYRKKISRSYSTEKDIEIFSNDTHEKSIACSDRQVVYADGSSLRNGKKGAVAGCGVFFGNDDPRNISVPLAGEEQTNNRAELQAIILALENTSGDLTIRSDSNYSIKSLTTWLPKWKKNDFKTSNSQPVKNLDLINRASDLMSDRNVSLEYVKGHSTDYGNQQADMLARRGASE | 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): 29421
Sequence Length: 264
EC: 3.1.26.4
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Q04740 | MARQGNFYAVRKGRETGIYNTWNECKNQVDGYGGAIYKKFNSYEQAKSFLGQPNTTSNYGSSTHAGGQVSKPHTTQKRVHRRNRPLHYSSLTSSSACSSLSSANTNTFYSVKSNVPNIESKIFNNWKDCQAYVKHKRGITFKKFEDQLAAENFISGMSAHDYKLMNISKESFESKYKLSSNTMYNKSMNVYCDGSSFGNGTSSSRAGYGAYFEGAPEENISEPLLSGAQTNNRAEIEAVSEALKKIWEKLTNEKEKVNYQIKTDSEYVTKLLNDRYMTYDNKKLEGLPNSDLIVPLVQRFVKVKKYYELNKECFKNNGKFQIEWVKGHDGDPGNEMADFLAKKGASRR | 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): 39431
Sequence Length: 348
EC: 3.1.26.4
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Q67PD4 | MKRLQALMAEQGPDIYPEVIAALKDDPREGAQRLVRQCQTYLKERERQRAVLQRMYNYERQLWSMGYRHIAGIDEVGRGPLAGPVVAAAVILPGEVELPGIEEAKRLSDRRRMELYRRIREVAVAVGVGLVQPEGIDEASVVVATYKAMMKAVADLPVTPDYLLIDGVHLPNVSQPQVPVVGGETLSCSIAAAAVVAKVVRDEYMVEMDAKYPAYGFAHHKGYGTPEHRLALERYGPCPIHRKPSDGTPAGAVLLFTEG | 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): 28540
Sequence Length: 259
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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Q67MS9 | MADLRLERVLWRHGCQVIGVDEAGRGPLAGPVVAAACILPPDAALPGVDDSKRMTEKRREAAFAAIQAVAVGWGIGIVDAARIDEINILQATFEAMAQAVEGARAMAAARPGRTAEAALLVDGNRPLPLWPGWQRTVVGGDHKSLSIAAASILAKVTRDRMMIEYDAHYPEYGFARNKGYGSREHWDALERYGPCPLHRRTFIGPRQIRFF | 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): 23038
Sequence Length: 211
Subcellular Location: Cytoplasm
EC: 3.1.26.4
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Q9SEZ6 | MESECLTPEWASQPCLMGIDEAGRGPVLGPMVYGCMYCPISYQSSLASLHFADSKTLKEEKREELYESLKLDKSLGWAVDVIDPRELSAKMLAKNKTNLNEISHNSAMGLIKRVLDMGVLLTEAYLDTVGDPDKYRIKLSERFPSIKFVVSKKADSLFPIVSGASIVAKVTRDRALKEWLVEETGEDINRNFGSGYPGDPETKAWLVQHKHSVFGFPSLVRFSWGTCTTHLKGEVEVAWEADENEESGNGSSSKRQAKLSSFGFKTCEKRSEEIESSGKGRCKFLQARKIQQLTQF | 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: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes (By similarity).
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 33078
Sequence Length: 296
EC: 3.1.26.4
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Q9U6P6 | MSLKCETERSKTWNNFGNGIPCVLGIDEAGRGPVLGPMVYAAAISPLDQNVELKNLGVDDSKALNEAKREEIFNKMNEDEDIQQIIAYALRCLSPELISCSMLKRQKYSLNEVSHEAAITLIRDALACNVNVVEIKVDTVGPKATYQAKLEKLFPGISICVTEKADSLFPIVSAASIAAKVTRDSRLRNWQFREKNIKVPDAGYGSGYPGDPNTKKFLQLSVEPVFGFCSLVRSSWKTASTIVEKRCVPGSWEDDEEEGKSQSKRMTSWMVPKNETEVVPKRNVYFKERHMSNILTF | 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: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes (By similarity).
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 33191
Sequence Length: 297
EC: 3.1.26.4
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Q54D13 | MDNKIIYLTELDSSVDKSEPFVMGIDEAGRGPVMGPMVYGCCYAPISKSTTLKSMKFNDSKKLTEQQRDQLFDKMGESNKILAYETDVITAEILSEKMLYKKPISLNVISHESAIGLIRSVLKKGVNVQELYLDTVGPPDKYQLMLKKLFPEIGKIIVSKKADSLYPIVSAASIAAKVVRDFEITNKNFDYLNIYDQDEQLSTDFGSGYPSDPLSKKWLVKNRDKVFGYPNFIRFSWKTTETAMRGACFGVDWVLENDKLKQHFQENQNDKKRFMFFKENNIENCINDF | 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. Participates in DNA replication (By similarity).
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 33083
Sequence Length: 289
EC: 3.1.26.4
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Q9VPP5 | MSDQEDVVVKKEKKCIENIDENDEEPDDVDFKDSGKISSLKALGPFIAGKENSRNTVYLSDVPDICKDKPCMLGVDEAGRGPVLGPMVYGISYCPLESNKALEDLGCADSKQLTEGKRDIIFNDINTKEYATSCVGWAVEIISPNTISTSMYRRSKCSLNEVSMDSAMGLIQQAIDAGVNIAEVYVDTVGPPEKYQEKLLKRFPSFKITVAKKADSTYPIVSAASICAKVTRDHALKVWSFPEGLVIKDNEFGSGYPGDPVTRRFLTEYIDLVFGFPRLVRFSWSTAENALADKAYDMEFDEPDSEKPKYAGTKLTKFFKGTTKSGEIIREECRFFKQRHLESVMEF | 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: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes (By similarity).
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 38750
Sequence Length: 347
EC: 3.1.26.4
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O75792 | MDLSELERDNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGPVLGPMVYAICYCPLPRLADLEALKVADSKTLLESERERLFAKMEDTDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTATGLIQYALDQGVNVTQVFVDTVGMPETYQARLQQSFPGIEVTVKAKADALYPVVSAASICAKVARDQAVKKWQFVEKLQDLDTDYGSGYPNDPKTKAWLKEHVEPVFGFPQFVRFSWRTAQTILEKEAEDVIWEDSASENQEGLRKITSYFLNEGSQARPRSSHRYFLERGLESATSL | 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: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 33395
Sequence Length: 299
Subcellular Location: Nucleus
EC: 3.1.26.4
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Q9CWY8 | MDLSELERDNTGRCRLSSPVPAVCLKEPCVLGVDEAGRGPVLGPMVYAICYCPLSRLADLEALKVADSKTLTENERERLFAKMEEDGDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTAAGLIQYALDQNVNVTQVFVDTVGMPETYQARLQQHFPGIEVTVKAKADSLFPVVSAASIFAKVARDKAVKNWQFVENLQDLDSDYGSGYPNDPKTKAWLRKHVDPVFGFPQFVRFSWSTAQAILEKEAEDVIWEDSEAEEDPERPGKITSYFSQGPQTCRPQAPHRYFQERGLEAASSL | 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: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 33513
Sequence Length: 301
Subcellular Location: Nucleus
EC: 3.1.26.4
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Q9P5X8 | MADIQDEAGPFLPPTISPPALLSGVSQTYFSPIPPQLLADNTPCCLGVDEAGRGPVLGPMVYSAFYLPLTLSDPLLKQKHSFDDSKVLTPAVRLSLMKELCTKDTELHDNCGYATSSLSPLSISSGMLKASKAQIYNLNQQAMDATIALIKGIYERGVNVTDIFIDTIGQPAAYQKKLERVFPTAKITVAKKADSLYPVVSAASVVAKVTRDIALEVLWADRTMAWGSGYPSDSKCVSWLKQNMHPVFGWGPECRFSWGTAKDMLETKGGVKVDWPEEEEEETQKLTDFFMAKRDQAEVDVDDLGTWFGAPAGVECF | 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. Participates in DNA replication.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 34627
Sequence Length: 317
EC: 3.1.26.4
|
Q10236 | MKDDHDAWEPEELVSDNNSSENELQEDQNSSITFLPPSVNKSNPAKSNYYHSTVTDDISKSQPYRLGVDEAGRGPVLGPMVYAVAYCPVDFDLTNYGFADSKTLASLKREELLKLICNKSNELGKNVGWSTMSISARELAAGMLRYRNKYNLNLQAHDTTIDLIKKVYESGINVTEIYVDTVGPPISYQEKLQAHFPQAKVTVTKKADSLFPIVSLASICAKVTRDIQLECARESIRTENWGSGYSSDARTTEWLKVNVDKIFGWKGDIVRYSWKTAKDLLELPSKSQSSIEIDWHEDDDTPTLNFTQKKKPNPASRSWFGSEFYF | 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. Participates in DNA replication.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 36808
Sequence Length: 326
EC: 3.1.26.4
|
P53942 | MVPPTVEASLESPYTKSYFSPVPSALLEQNDSPIIMGIDEAGRGPVLGPMVYAVAYSTQKYQDETIIPNYEFDDSKKLTDPIRRMLFSKIYQDNEELTQIGYATTCITPLDISRGMSKFPPTRNYNLNEQAHDVTMALIDGVIKQNVKLSHVYVDTVGPPASYQKKLEQRFPGVKFTVAKKADSLYCMVSVASVVAKVTRDILVESLKRDPDEILGSGYPSDPKTVAWLKRNQTSLMGWPANMVRFSWQTCQTLLDDASKNSIPIKWEEQYMDSRKNAAQKTKQLQLQMVAKPVRRKRLRTLDNWYR | 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: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 34875
Sequence Length: 307
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
Q8KAA5 | MLSTDFEYPLWESLSQVCGIDEAGRGPLAGPVVAAAVVFPRHFRPTGIFAKLDDSKKLTAELRDELALAIRESAESWALGVVDAETIDRINILQATMLAMNLAVESLGSTPEFLLVDGNRFRPVLPIPYQTIVKGDSKVFSIAAASVLAKTHRDELMTTSAAEYPEYGFEVHFGYPTARHVEAIARHGRCAIHRQSFKLRKLGEK | 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): 22583
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
O84032 | MKSTVEQAMLFEEKSIFENQAIEQGYSQVAGVDEAGRGPLAGPVVAGACILPRGKVFLGIDDSKKLTPKQRRYLYELLLEDPEVDCGVGVISVERIDEINILEATKEAMVQAIASLRSTPDFLLVDGLFLPHKVPSLKIIKGDARSVSIAAASIIAKEYRDELMRKLHVEYPEYGFDKHKGYGTAAHLQALKHFGPCVYHRKSFSPVKESIQEGVCQ | 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): 23961
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 3.1.26.4
|
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