ids
stringlengths 6
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stringlengths 11
1.02k
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stringlengths 108
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A5CQR0 | MWWTPIPEDIVRDPAAFRVGRLTKAHGLKGAVKLELFTDDPDKRFVPGAEFSLQVPESSPWHGRTLTLTELRWYNSHPVGFFDGVADRTAAESLAKAILWMTPPADEAAEPDAWYDHQLVGLTVLRDGVEVGTVSLVDHFPAQDLLHVDTPSGTVLVPFVQAIVPSVDVEAGTLVVTPPLGLFEEIPDETPTAEPTPAEAAEPAPEGDDAR | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 22904
Sequence Length: 211
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
Q60BS2 | MPGNSGNDRSVVVGRVSGAFGVRGWVKAVSFTDPPVNLVGYRPWTLRRGDAERRADVLEGREHGNAVIVRLQGVDTREQAEALKGFEVTVRRSQLPPPAPGEYYRVDLVGLKVVNLGETVLGEVVDVMETGANDVLVVQGDRERLLPFVQGVFVKSVNLEESRIVVDWDPGF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18851
Sequence Length: 172
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
Q1GYT7 | MQIVSELVIMGRIVAPYGVYGWVKVQPATEYVDSLFDYGRWMLGRGDPKQPEQWQSCEVEKAKVHNDLLLVKLQGIDDRDQAFSCKGMYVAVYRDELPEPEEGEYYWSDLIGLQVRNQQEVDFGQVVDVFATGANDVLVVKGDRERLVPFIGQVVLEVDTDGKTMLVDWDPEF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19767
Sequence Length: 173
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
A2SES7 | MLDDEVVWPEDAIEVGRIVDAWGIKGGIKVLPFSSDPQALFSSRRWFLRPPEKPMGPKAAKPLPTLLRITNAREQGDVIVATAQDVADRNAAEALRGCSVFVSRASFPTADVDEYYWIDLIGLAVVNREGQALGNVADLLDTGAHSVLRVTQVETDDQGRSLERERLIPFVAAYIDAVSLEQRCITVDWGLDF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 21279
Sequence Length: 193
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
B1LVU1 | MARRPAGPTSRDGGRRGRTSSAIGKIAPDAATSPKAPAPRPAPPPVPPDPNLVLLGEFGRAHGLTGEVRLKSYTGDPQAIAGYGALQTSDGRTLALADVRPAPGSSPDMLIARVKGVSGRSAAEALNRVALFVPRDRLAAPEDDDEVYAADLIGAAAVDEAGTLVGTIVAVPNYGGGDLLELRPPNGGATALLPFTKAFVPVLDVAQRRVTVAAPEDLFAAPGEKPADDPG | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 23516
Sequence Length: 231
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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B0UCL3 | MARRPQRPAPSGRAGAGRGAAGAAPPGPDARLVVLGEFGRAHGLQGEVRLKSYTAEPMAIGGYGPLLASDGRVVELTALRPAAGTPDILVARVAGVAGRSAAEGLNRLTLSVPRDRLGAPEDEDEFFTADLVGLAAVDAAGTRLGTIRAVPNYGGGDLLEIEPEGGGRPALLPFTRLFVPKVEIAAGRVTIAPPEDLFAPPGPPPEGEG | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 21245
Sequence Length: 209
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
B0JU07 | MEENWLEIGTIVAPQGLEGELRVLSVSDFPERFQKRGMRGIQGPQGGEIREITLLRGRELPGKNVYVIKLEGVENREQAEALRGYKLWANKLEKPRLKADEYHVSELVNLEVYHHLTGEKIGVVVDIFWAGNDILAVQLEANLASVKKKSPSSDSEARALVPFVKEIVPLVDLKAARIEIAPPPGLLEINLS | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 21409
Sequence Length: 192
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
Q2RJV5 | MDTERIGVGKIIGTHGIRGEVKVFPLTDFPERFRPGTRLILEQEGADGREGRTFPVTVISVRPGKGNLILKLAEINDADQAGAVRGATLKVEPWEVEPLPEGHYYIYQLLGSRVYTTGGEFLGILRDILATGANDVYVVRNEDAGEILIPALKTVVRQVDLARKEIRVELPPGLRD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19384
Sequence Length: 176
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
B2HJL4 | MELVIGRVVKAHGITGEVVVEIRTDEPDRRFTPGASLRAKRSRDGGTGRNYVIEGVREHGARLLVRLAGVNDRDTADGLRGSLFVIDSADLPPIDEPDTYYDHQLEGLRVRTTAGQDVGVVAEVLHTGAGELLAVKCDSGEVLVPFVGAIVTSVSLDDRILEIDPPDGLLDLGS | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18606
Sequence Length: 174
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
B1VYW1 | MQLVVARIGRAHGIKGEVTVEVRTDEPELRLGPGAVLATEPAATGPLTVEAGRVHSGRLLLRFEGVRDRTGAEALRNTLLIAEVDPDELPEEEDEFYDHQLIDLDVVLADGTGIGRITEISHLPSQDLFIVERPDGSEVMIPFVEEIVTEIDLEEQRAVITPPPGLIDESEAVVASSRDEETGEAASGDEAEAPKGDA | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 21291
Sequence Length: 198
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
B4SPH2 | MKDNERRILLGRIVGAFGVRGEIKLESWTEPRSAIFRYQPWILRSPNGQESTLEGARGRDSGKHLVARFPGIEDRDTVEAMHGTEVYVARSALPPPNADEYYWVDLEGLDVKTTEGVALGQVSHLFSTGANDVVVVRGDRERMIPFVLPEFVKSVDFEANLVVVDWDPEF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19130
Sequence Length: 170
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
Q8DUN7 | MKYFNVGKIVNTQGLRGEVRVLSVTDFADERFKKGSQLALFDKKDHFAMTVEIASHRKHKNFDIVKFKGLYHINDVEKYRDFTLKVTEDHLADLEDGEFYYHEIIGLDVYENDILIGQVKEILQPGANDVWVVKRKGKKDLLLPYIPSVILKVDVPNGRIDVTVLEGLDDEN | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19823
Sequence Length: 172
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
|
A4WRD4 | MGAMAQNPPNLRPDLAPRLVIDSPRREGQPTIGMVSLGCPKALVDSERILTRLRAEGYAISPDYAGADAVIVNTCGFLDSAKAESLEAIGEALRENGRVIVTGCLGAEPDYITGAHPKVLAVTGPHQYEQVLDAVHGAVPPAPDPFVDLLPATGVRLTPRHFSYLKISEGCNHSCRFCIIPDMRGRLVSRPERAVLREAEKLVEAGVRELLVISQDTSAYGTDWKGPVRFPILPLARELGQLGAWVRLHYVYPYPHVRELIPLMAEGLILPYLDIPFQHAHPEVLKRMARPAAAARTLDEIAAWRRDCPDITLRSTFIVGYPGETEEEFQTLLDWLDEAQLDRVGCFQYENVAGARSNALPDHVAPELKQERWERFMQKAQAISEAKLAARIGQRLEVIVDEVDGEGATCRTKADAPEIDGNLFIDEGFEALSPGDLLTVEVEEAGEYDLWGRAVLV | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50331
Sequence Length: 457
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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A9WDA3 | MKYHIVTLGCPKNAVDSEGMDGLLSTQGHQAVASAEEADVIIVNTCSFIAAARAETLGVLKELAGRKRPGQRLIAAGCMAQSHPHEVAGVQGVDATLGTQQWTQINALVGQLERPVIPLTPGQPVATIPLTTTTNGQPTSYADWRTTQIRRTHQTPSAYLKISDGCNLRCAFCTIPSFKGDMRSKPVGAVLAEAQELVAGGVREIVLVAQHLTDYGRDLGLKDGLATLLAELCQVTPPETWIRLMYAYPHGISERLITTMASYPQICHYLDMPLQHAHPATLRRMRRPPDTDRTLRIIAELRAAMPDIAIRSTFIVGYPGETTAEFHALLEFLQTAQLDRVGAFRYSREPGTPAAELPDQVRPQVIERRWHELMRLQQTISYTRNQRWVGRTIKVLIEGNGTADDGSALSIGRSFRDAPEIDGQVFVWGNYPAGTMIPVQVTQATAYDLWGEALS | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49938
Sequence Length: 455
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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Q3ASP1 | MPTHSLFLLSLGCSKNTVDSERLLAQAAAAAIRSVERVDEADTILINTCAFIEDAKKESIEEMLAALDKKREGVVKQVFVMGCLPELYRRELQEELPEVDAFFGTRELPQILASLGARYRSELFDERLLLTPSHYAYLKISEGCNRICSFCSIPKIRGRYQSQPLEQLLREATRLQQQGVQELNLIAQDISLFGYDTTGHSQLNELLLRLSDMDFLWIRLLYAYPVNFPLEVIDTMRDRSNICNYLDIPLQHCNDRILRAMKRGVTKADTIRLLHEMRQRNPNIRLRTTMLVGFPGETRAEFEELLDFVEEQRFDRLGCFPYNHEEHAPSAMLEDLLSIEEKEERVSELMELQEAVAESLNREFEGKEIEVVVDSFVEEMAFCRSEYDAPEVDNECLLTFGAQNIQAGNFYRALINDSSAHELYGEIVQERSAGNSPQ | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50282
Sequence Length: 438
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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Q9Z8T3 | MTTKSLGSFNSVISKNKIHFISLGCSRNLVDSEVMLGILLKAGYESTNEIEDADYLILNTCAFLKSARDEAKDYLDHLIDVKKENAKIIVTGCMTSNHKDELKPWMSHIHYLLGSGDVENILSAIESRESGEKISAKSYIEMGEVPRQLSTPKHYAYLKVAEGCRKRCAFCIIPSIKGKLRSKPLDQILKEFRILVNKSVKEIILIAQDLGDYGKDLSTDRSSQLESLLHELLKEPGDYWLRMLYLYPDEVSDGIIDLMQSNPKLLPYVDIPLQHINDRILKQMRRTTSREQILGFLEKLRAKVPQVYIRSSVIVGFPGETQEEFQELADFIGEGWIDNLGIFLYSQEANTPAAELPDQIPEKVKESRLKILSQIQKRNVDKHNQKLIGEKIEAVIDNYHPETNLLLTARFYGQAPEVDPCIIVNEAKLVSHFGERCFIEITGTAGYDLVGRVVKKSQNQALLKTSKA | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 52973
Sequence Length: 468
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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Q8KCL7 | MTKTDERKPAIFLLSLGCSKNTVDSERLTAQAVASGLTFTDNVDEADIILINTCGFIKDAKQESIDETLAAIGKKEEGVVREVYVMGCLVELYRKELAEEMPEIDGLFGTRELPEVLAAIGAKYREELFDRRELLTPPHYAFLKIAEGCNRRCSFCSIPKIRGPYVSQPIEQLLREAALLQQQGVKELNLIAQDISVYGYDLYGKSALNDLTLRLSDMGFNWIRLLYAYPLNFPLEVISTMRERPNVCNYIDMPLQHINDRILKSMQRGIGRKATEQLIDDIRQKNPDIRLRTTMIAGYPGETRAEFEELLDFIRQTRFDRLGCFPYRHEEHASAYALEDTVSDEEKEKRVGELMELQEGISASLNRKLEGQTLKVLIDRIEESVAYARTEYDAPEVDNDVIIEIGDEAVEEGDFRQVMIEDSTAYELFGRISG | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49410
Sequence Length: 434
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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A6LAJ6 | MRKNKVDIITLGCSKNLVDSEQLMRQFVANGYTVEHDPHKINGEIVVVNTCGFIGDAQEESINMILELGEQKQKGRIGKLFVMGCLSERFLKDLEKELPEVDRFYGKFNWKELISDLGKSYHQELATDRVLTTPRHYAYVKIGEGCNRTCSYCSIPIITGAYQSRPMDEIVDEVRGLVAQGVKEFQMIAQDLTFYGLDRYKRMALPELVERVSDIPGVEWIRLHYGYPSHFPYDLLPVMRERDNVCKYMDIALQHISDPMLKMMRRNITKAETYELLERMRREVPGIHLRTTLMVGHPGETEQDFEELIRFVKDIRFERMGAFAYSHEEGTYAYQHYKDEIPQEVKQDRLDYLMRVQEGISADVNASKVGQTFRVIVDREEEDFYVGRTQYDSPEVDPEILISKDTPLSPGSFYQVKVIDAQAFDLYGKVLN | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50112
Sequence Length: 432
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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A1B3K8 | MPAMSQNPPLLRPDLAPAPIFDTSRREGQPTIGMVSLGCPKALVDSERILTRLRAEGYAISPDYKGAGAVIVNTCGFLDSAKAESLQAIGEALAENGKVIVTGCLGAEPEYITGAHPSVLAVTGPQQYEQVLDAVHHAVPPSPDPFVDLLPASGVKLTPRHYSYLKISEGCNHACKFCIIPDMRGKLVSRPAHAVIREAEKLVEAGVRELLVISQDTSAYGLDRKFATERGHRAHITDLARDLGQLGAWVRLHYVYPYPHVRDLIPLMAAHGESGGLVLPYLDIPFQHAHPDVLKRMARPAAAARTLDEIAAWRAVCPDITLRSTFIVGYPGETEAEFQTLLDWLDEAQLDRVGCFQYENVKGARANDLPDHVPDDVKQDRWDRFMQKAQAISEAKLAAKVGHRIEVIVDAVDGDGATCRTKADAPEIDGNLFIDEGFEDLAPGDIVSVTVDEAGEYDLWGRL | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50455
Sequence Length: 463
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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Q6MBU9 | MLPILKNQGVKKDQNHIALKNDSCESSSPCFDHEGNKINFISLGCPRNLVDSEVMLGILLKAGYEVAPTLEEADYLVINTCGFLEASRQESMDTVEEVLSQRKKTAKLIVTGCMVQTHSDALKTTFPSIDYLLGSGDVEGILKAVQSTQKGQIISSARSYLEAGEVPRRLSTPKHYAYLKIAEGCRKRCAYCVIPTIKGPLKSKGKEQILKEFNLLLSQGVKEVILIAQDLGDYGKDQGAKKLTALLNLLQSMLEIKQAFWLRLLYLYPDEITDELIALMKSDSRICPYLDMPIQHVNNQILKSMRRATSKEDIIEIITKLRREIPNVAIRTSLIVGFPGETEEQFQELIQFVQDYPLENVGIFKFSREPGSHAYDLPNQISDEMKEDRYHRLMQVQKKVVKKNLKKMIGKKIAVVVEGYHPETELLMIGRHTGQCPDIDGQVLINDGRKVKAFGEIYTVEITDVADYDLVGHVI | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53462
Sequence Length: 475
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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A9BEU9 | MKKFHIVKLGCPKNDADMEIFKGLLQSKGYKYESNPQLANYIFIDTCGFIEEAKKESIETIFEYVSLKDNNKNLKVIPIGCLTQRYFDDILKDIPEIDGLYGVLSPKTIVEKIENGEYFFKRDIPETLYDCKIRAIPDSHYAYVKIGDGCSRNCAFCSIPTFKGKPKSRSIEEINEEVEFLVSKGVKEIILVSQDNTLYGIDNYQKQALPDLLDKLNNIKGKFWIRVMYLHPDFLSEEIIESIHRNEKVLNYFDVPIQHISDKILQSMGRHKKRNELIKLFEKIRKEPSAIRTTLMVGFPGEKAEDFEELVDFVKEIKFERMGSFIFSKEENTKSFTLPEQIDEQIKKQRQNELMTVQSEISKNIMEKYIGETLEVLLEEKEDNVYVGRSYLDAPEIDGNVYIKNFGDKELTFGNFVKVTITGSYEYDLEGEIVE | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50507
Sequence Length: 435
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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P36602 | MFVYKRDGRQEKVAFDKITARVSRLCYGLDSDHVDPVEITQKVISGVYPGVTTIELDNLAAETAATMTTKHPDYAILAARIAVSNLHKQTEKVFSTVVQQLHDYVNPKTDKPAPMISDKIYDIVMKHKDELDSAIIYDRDFTYNFFGFKTLERSYLLRIDGKVAERPQHMIMRVAVGIHGEDIEAAIETYNLMSQRYFTHASPTLFNAGTPRPQLSSCFLVTMKDDSIEGIYDTLKMCAMISKTAGGIGINIHNIRATGSYIAGTNGTSNGIVPMIRVYNNTARYVDQGGNKRPGAFAAYLEPWHADVMDFLELRKTHGNEDFRAREMFYALWIPDLFMQRVERNEQWTFFCPNEAPGLADVWGDEFVALYEKYEKENRGRRSLPAQKVWYAILQSQVETGNPFMLYKDSCNRKSNQKNVGTIRCSNLCTEIVEYSSPDEVAVCNLASVALPTFIKDGKYNFQKLHDVVKVVTRNLNKIIDVNYYPVPEARRSNMRHRPVGLGVQGLADAFFALRLPFESAGAKKLNIQIFETIYHAALEASCEIAQVEGTYESYEGSPASQGILQYDMWNVNPTDLWDWAELKEKIAKHGIRNSLLVAPMPTASTSQILGFNECFEPYTSNMYQRRVLSGEFQIVNPWLLKDLVERDLWNEDMKNKLVMLDGSIQAIPEIPQDLKDLYKTVWEISQKTVIDYAADRGPFIDQSQSLNIHLKDPSYGKITSMHFYGWKKGLKTGMYYLRTMAASAAIKFTVDPVALRARNEESNEENKKPVIKNGKAEISAEPTKEEIDIYNEKVLACSIKNPEACEMCSA | Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 91999
Sequence Length: 811
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P50643 | MPPRAPRPAGAVSPPFPPLAGPPLKARAPRARDSPLTSPCRAHAAMASVVAPAASSSAAAPGADAFLDAACPEDVARALAAELEALRALGHDVGAPAPGASRREAALFITRAVDGLKAFSRVDERVYVACGKLVHLRVRSREADLDAWLASPELALIPAVAAAVRRHRARVEAALRWFWREAYPALYARGLQSALKYEEMYLARLEHGRCEAMDQFFVRLAAAAATATRRPMALVLCGSDAWPEVFDAYFRALATQAIVPATPLMLFAGRARGSLASCYLLNPLPRTTEEAVRAITDEVAPILLRRGGVGLSLQSFNRTPSGDCTRGIMAVLKALDSMTAAINSDSERPTGVCVYVEPWHADVRAVLNMRGMLAADESLRCDNIFSCLWTPDLFFQRYQRHLDGERAVKWTLFDDRASHLASLHGPDFAREYERLERLGLGVESLPIQDMAFLIVRSAVMTGSPFLMMKDACNRHFHTDTRGAALATSNLCTEIVQRATPGENGVCNLASVNLPACLAGGAFDFAALRRAARVAAVFVNAMMRIGNYPTGASVEGVRRSRSLGIGLQGLHTTVLALDMDMADPAARRLNAAIAEELLYGVMDASVELCERGLRPFDGFEHSRYARGVMPFDAYERVSLREPMRWDALRVRIAEHGVYNAQFVALMPTVSSSQVTESSEGFSPTFTNMFSKVTISGELLRPNLPLMETLRRLFPRECARRDAVARLERAQWSVAAAFGELPAGHPLAKFKTAFEYDQELLIDMCADRAPFVDHSQSMSLFLTEPADGKLHASRVMGLLMRAYNLGLKTGMYYCKIRKATNNGVFTGGDLVCTSCHL | Function: Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 91060
Sequence Length: 835
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P74240 | MHPTLISAPISSSANDAHAGTSQGSHQGHRIQVIRRDGSSTPLNIGKIRAVVDWACLGLEVNSIALEAGLTTRLREGISTREIQDNLISCALEMCSPNEPDWRYVAGRLHVWSLWKDTLVRRGYQYGQYLRTVQTKVTNGEYDSRILTYSEGELQEAGCWINSDWDTDYDYAGAVLLTSRYLLPNELPQEALLTCALLLASVEAPDRRLQWARRFYESIAARRISLATPILANLRVPGGSLTSCFIVAMEDNLESIFGEITNAARISKNGGGVGVNVSRIRATGSWVMGKPNASGGVIPWTKLLNDTAIAVNQGGRRAGAVTVGLDVWHLDVPEFLEMQAENGDQRRKAYDIFPQLILPDEFMRRVINKEDWTLVDPYEVREKMGIELAELWGEQFEGAYREIESNLDTTITLYKRINARELFKQIMRTQVETGMPYLSFKDTINKANPNKHLGYIPGTNLCCESFSNVTPGQDAHCCNLVSLNLANLDLQDIAGVSQIAVRMLDNTIELTAPPFADAKSHNNKYRTIGVGAMGLADWLAKRRLNYDELADINRLFEEIGYWCTQSSMELAKERGAYPAFPGSDWQKGLLIGSKPVSWFQANAAKPERWEKLSNDIQTHGIRNSHITAIAPNTSSSLVQGCTASILPVYSRFFYDKWAKGTVPIAPPFIGNCFWFYPENKTMDQRKVVKAVAAIQQWTDTGISMELLFNLNAGIYFPEEPERSLNAKDIFDTLVMAWEAGCKAIYYIRTVQKDDFKDSSDGCVACAN | Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 85637
Sequence Length: 767
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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O83972 | MHIIKRNGEPQPYMREKIIVAISAAFRSVQNPLAPEVPAIITDLAAEVERQLFEMNRAGVPVHVEKIQDFVEKTLTKYNHSDEVKSFILYRDDRTKKRIAREQIACCFTDSSVLGVLKEIQQDFPFPEYSLDALASKFLLFKKEVTDERRSMQLLIKAAVELTAQEAPQWELIAARLLMLDFSLALGTSLEKLNIHSFYEKITYLEEAGLYGVYIRTHYSRAEIEEAATYLECSRDKLFTYSSLDMILRRYVIRTRAHVPLETPQEMFLGIALHLAMNETQDRMQWVKRFYTVLSKLQVTVATPTLSNARKPFHQLSSCFVDTVPDSLDGIYRSIDNFSQVSKFGGGMGLYFGKVRAVGAPIRGFQGAAGGILRWIKLANDTAVAVDQLGVRQGSVAVYLDVWHKDIPEFLQLRTNNGDDRMKAHDVFPAVCYPDLFWKTVRDNLGASWYLMCPHEILTVKGYALEDFYAEEWEKRYWDCVKDARISKRTIPIKELVRLVLKSVVETGTPFAFYRDHANRANPNGHRGIIYCSNLCTEIAQNMSAINLVSVKITEVDGQKVVVQTTRPGDFVVCNLASLVLSNIDLSDDKELREVVRVAVRALDNVIDLTYYPVPYAQVTNAYYRAIGLGVSGYHHVLAQQGIDWESDEHLAFADRIFERINRAAIEASMTIAREKGAYGCFTGSDWCTGAYFRKRGYVSEDWQRLQREVATHGMRNGYLLAVAPTSSTSIIAGTTAGVDPIMKQYFLEEKKGMLMPRVAPSLSQKTCPLYKSAHAVEQRWSIRAAGLRQRHIDQAQSVNLYITTDFTLKQVLDLYVYAWEVGMKSLYYVRSQSLEIDLCGYCAS | Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 95987
Sequence Length: 845
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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O15909 | MLETVKLVTKRDGSVEPYDEKVVRSRIVNLMSGIDSYYVDVDDLVRVVGEGVREGMSTSMLDELLAETAAYCVTKHPDYGLLAGRLAVTALHKTTTESVLDSFRVLHEHVSQATKRHAPLISEELWDIANKHSAALQQIINYERDFDFEYFGYKTLERSYLLRVHKGRGVMEVVERPQQMFLRVALGIHGEDLERVKETYDYMSQGFFTHATPTLFNAGTPFPQMSSCFLVAMREDSIDGIYDTLKQCAIISKSAGGIGIHMHNIRAAGSYIAGTNGTSNGLVPMLRVWNNTARYVDQGGGKRKGAFAIYLEPWHADIFGFLLLKKNTGKEDQRARDLFYGLWIPDLFMERVESHGTWTLMDPNTAPFLSDCYGQEFTDLYERYEREGRGVRTIQAQELWFLILESQVETGVPFMLYKDACNFKSNQKNLGTIKCSNLCTEIVEYTSRDEVAVCNLASIALPRFVKDGAFDYVALKEVTKVVTRNLNRVIDRNHYPVCEARYSNLRHRPVGIGVQGLADAFALLSLPFAHPEAKKLNRQIFETIYIAAVEASTELAEKDGPYETFKGSPASEGKLQFDLWDEERRIRGMNEDSVHSHCGLWDWDSLKERVVKVGMRNSLLIAPMPTASTSQILGNNECIEPFTSNIYVRRVLSGEFPVVNKHLVKELIRLRLWNDDMRRKIIALNGSVSGIKEIPERIRELYKVVWEIRQKDLIDMAADRGRYIDQSQSLNLFLATPTSSQLTSMHFYSWKKGLKTGMYYLRSQPAADAIKFTLDPKAMKELPKPDKQSKEEVHGSVGRGKRKRVGEKPTANHSNAGAPNLNGPPDTDGDGGCLNCGS | Function: Provides the precursors necessary for DNA synthesis. Catalyzes the rate limiting step in the de novo synthesis of deoxyribonucleotides by directly reducing ribonucleotides to the corresponding deoxyribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 94619
Sequence Length: 838
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P12848 | MFVIKRNGYKENVMFDKITSRIRKLCYGLNTDHIDPIKIAMKVIQGIYNGVTTVELDTLAAEIAATCTTQHPDYAILAARIAVSNLHKETKKLFSEVMEDLFNYVNPKNGKHSPIISSITMDIVNKYKDKLNSVIIYERDFSYNYFGFKTLEKSYLLKINNKIVERPQHMLMRVAVGIHQWDIDSAIETYNLLSEKWFTHASPTLFNAGTSRHQMSSCFLLNMIDDSIEGIYDTLKRCALISKMAGGIGLSISNIRASGSYISGTNGISNGIIPMLRVYNNTARYIDQGGNKRPGVMAIYLEPWHSDIMAFLDLKKNTGNEEHRTRDLFIALWIPDLFMKRVKDDGEWSLMCPDECPGLDNVWGDEFERLYTLYERERRYKSIIKARVVWKAIIESQIETGTPFILYKDACNKKSNQQNLGTIKCSNLCTEIIQYADANEVAVCNLASVALNMFVIDGRFDFLKLKDVVKVIVRNLNKIIDINYYPIPEAEISNKRHRPIGIGVQGLADAFILLNYPFDSLEAQDLNKKIFETIYYGALEASCELAEKEGPYDTYVGSYASNGILQYDLWNVVPSDLWNWEPLKDKIRTYGLRNSLLVAPMPTASTAQILGNNESVEPYTSNIYTRRVLSGEFQVVNPHLLRVLTERKLWNDEIKNRIMADGGSIQNTNLPEDIKRVYKTIWEIPQKTIIKMAADRGAFIDQSQSMNIHIADPSYSKLTSMHFYGWSLGLKTGMYYLRTKPASAPIQFTLDKDKIKPPVVCDSEICTSCSG | Cofactor: Maximal ribonucleotide reductase activity requires the presence of Mg(2+) ions.
Function: Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 87738
Sequence Length: 771
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P21524 | MYVYKRDGRKEPVQFDKITARISRLCYGLDPKHIDAVKVTQRIISGVYEGVTTIELDNLAAETCAYMTTVHPDYATLAARIAISNLHKQTTKQFSKVVEDLYRYVNAATGKPAPMISDDVYNIVMENKDKLNSAIVYDRDFQYSYFGFKTLERSYLLRINGQVAERPQHLIMRVALGIHGRDIEAALETYNLMSLKYFTHASPTLFNAGTPKPQMSSCFLVAMKEDSIEGIYDTLKECALISKTAGGIGLHIHNIRSTGSYIAGTNGTSNGLIPMIRVFNNTARYVDQGGNKRPGAFALYLEPWHADIFDFIDIRKNHGKEEIRARDLFPALWIPDLFMKRVEENGTWTLFSPTSAPGLSDCYGDEFEALYTRYEKEGRGKTIKAQKLWYSILEAQTETGTPFVVYKDACNRKSNQKNLGVIKSSNLCCEIVEYSAPDETAVCNLASVALPAFIETSEDGKTSTYNFKKLHEIAKVVTRNLNRVIDRNYYPVEEARKSNMRHRPIALGVQGLADTFMLLRLPFDSEEARLLNIQIFETIYHASMEASCELAQKDGPYETFQGSPASQGILQFDMWDQKPYGMWDWDTLRKDIMKHGVRNSLTMAPMPTASTSQILGYNECFEPVTSNMYSRRVLSGEFQVVNPYLLRDLVDLGIWDEGMKQYLITQNGSIQGLPNVPQELKDLYKTVWEISQKTIINMAADRSVYIDQSHSLNLFLRAPTMGKLTSMHFYGWKKGLKTGMYYLRTQAASAAIQFTIDQKIADQATENVADISNLKRPSYMPSSASYAASDFVPAAVTANATIPSLDSSSEASREASPAPTGSHSLTKGMAELNVQESKVEVPEVPAPTKNEEKAAPIVDDEETEFDIYNSKVIACAIDNPEACEMCSG | Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 99561
Sequence Length: 888
Pathway: Genetic information processing; DNA replication.
Subcellular Location: Cytoplasm
EC: 1.17.4.1
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P50651 | MGSLKEGQGRDMEEGESEEPLLMAQNQRFTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARFLNDVQVPEARAFYGFQIAMENIHSEMYSLLLETFIKDSKEKDRLFNAIETIPCISKKAKWCLDWIQSPMSFAVRLVAFACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPLEKVYQIVHEAVEIETEFVCKALPCDLIGMNSNLMSQYIQFVADRLLVTLGCERTYKAENPFDWMEFISLQGKTNFFEKRVGEYQKASVMSNLQNGNQNYEFTTEEDF | Cofactor: Binds 2 iron ions per subunit.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 39370
Sequence Length: 341
Pathway: Genetic information processing; DNA replication.
Subcellular Location: Cytoplasm
EC: 1.17.4.1
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Q7LG56 | MGDPERPEAAGLDQDERSSSDTNESEIKSNEEPLLRKSSRRFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRKSTFGERVVAFAAVEGVFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEERVREIIVDAVKIEQEFLTEALPVGLIGMNCILMKQYIEFVADRLLVELGFSKVFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDADF | Cofactor: Binds 2 iron ions per subunit.
Function: Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 40737
Sequence Length: 351
Pathway: Genetic information processing; DNA replication.
Subcellular Location: Cytoplasm
EC: 1.17.4.1
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P11998 | MNIIQGNLVGTGLKIGIVVGRFNDFITSKLLSGAEDALLRHGVDTNDIDVAWVPGAFEIPFAAKKMAETKKYDAIITLGTVIRGATTHYDYVCNEAAKGIAQAANTTGVPVIFGIVTTENIEQAIERAGTKAGNKGVDCAVSAIEMANLNRSFE | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. Is able to use the non-natural R enantiomer of 3,4-dihydroxy-2-butanone 4-phosphate as a substrate, but with less efficiency than the natural S enantiomer. Cannot use unphosphorylated 3,4-dihydroxy-2-butanone, 3,4-dihydroxy-2-butanone 3-phosphate or diacetyl as substrates.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16287
Sequence Length: 154
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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Q89ZW8 | MKFGIVVSEWNFNITGALLNGAVNTLKKHGVKDENILVKTVPGSFELTFGANQMMENCDVDAIIAIGCVIKGDTPHFDYVCMGATQGITELNATGDIPVIYGLITTNTMEQAEDRAGGKLGNKGDECAISAIKMIDFVWSLNK | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 15360
Sequence Length: 143
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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Q9REF4 | MTIEICKKLHVLIVEARFYDGISDALLTGAVSTLQKAEATYDIVTVPGALEIPGAIAFAEKNSKIYYDGYVALGCVIRGETYHFEIVANDSCRALMDLTIHKHLAIGNGILTVENEKQAWARAKQDEKNKGGFAAQAALCMIALKKRFGEIIKYG | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16953
Sequence Length: 155
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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C1DB32 | MNPDIVNLESNLNGEGLRIGVVMARFNLPVCEGLRDACLDELLALGVEPTDITFVTVPGALEIPLALQAMAQNEDDSYDALVALGAVIRGETYHFELVSNEAGAALTRVGLDFDIPVANGVLTCDTDEQAEARMAEKGRDCARCAVEMANLQKAFYD | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16847
Sequence Length: 157
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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B1MYJ5 | MIYTGKLTGHEERRIAIVVSRFNALVTEPLLKGARDTLNMHGVDEHHISVFWVPGALEITMVSSQLAESGMFDGIVTLGAVIKGDTDHYNLVINGVANGVSQVSLSTNTPIVFGVLTTDTLEQAQQRAGAKAGNKGAEVTVSLLEILSLYDDIKQLS | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16819
Sequence Length: 157
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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A5VJX0 | MKEFTGKFNVQSAEIGIVVADFNETVTKQLVQGATEMLAKFDLENVDVYHVPGAFEIPFMTKQLLAKKEYDGILTLGAVIKGETDHYDLICQNVASGVMNLNLKSNIPITFGILTTDNIEQAMQRAGLKAGNEGAITAQSLLEMISLNRQIN | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16637
Sequence Length: 152
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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A0L3Z9 | MGDIIELEGHLTVDGKKFCLLLSRFNSFITERLLEGAIDCIVRHGGKREDITVARVPGAFELPLVAQKAAKSGKYDGIVCLGAVIRGSTPHFDYVSSEVTKGVASISLAYDMPIGFGVLTTDTVEQAIDRAGTKAGNKGWEATISVIEMINLLDGM | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16701
Sequence Length: 156
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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Q2W4S6 | MAKVLIIEARFYDHIADGLLAGARAEFDKAGVAHDLLVVPGIFELPAALKLVLTAAEQGNDKARYDGFVTLGCAIRGESDHYHHVGTECMRGIADLSMAYDLALGNGVLTVHNEAQALARSDPARKNLGGQAARACLRMMAVKRELGLSS | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 15987
Sequence Length: 150
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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Q2FFX3 | MNFEGKLIGKDLKVAIVVSRFNDFITGRLLEGAKDTLIRHDVNEDNIDVAFVPGAFEIPLVAKKLASSGNYDAVITLGCVIRGATSHYDYVCNEVAKGVSKVNDQTNVPVIFGILTTESIEQAVERAGTKAGNKGAEAAVSAIEMANLLKSIKA | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16396
Sequence Length: 154
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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P0CV49 | MRGAYYVITALLVVASSQTSADSGHRLHVYDHDVVAAENAAAKTLPQQSLRGSRDVPDDLAHEERAIISELVEEGAKLIPRAAENVEEMPRVTEAVGKRPRVAEKDALEKASGADEASKKPRNTATDDAFQGMSTEWELELPFKEWNTEIEPMREMPEPKWSWEKRKLVHEAFVKLCAEDLNPTVYETARLWSLFDGKAKSRPATFHRQVLIQLAKENVRRDVLIMKSVESEWDRWNEVSILSRVDVLNMLLNVHFQRWKRMYNAFGEQRSKLIAL | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 31594
Sequence Length: 276
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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P0CV50 | MRGAYYVLIALLVVASSQTSAESGHQLQVYDHDFVAADTAAATTLPRQFLRGSRNVPGDLAHEERAITSELVEEGAKLIPRAAENVEEISRVAEAVGKRPRVAEEDVLNKASGANEAFKKPRNTATDDAFQGISTEQLLPLSYKQWDTEIKSMRIPKPEKYQNNIQSVYDAFVDVCDEDLKPTISETARLWNLFDRSFKPLTTRLHQQALAQFAKEYVLRDELRLKTEWARMNERTMPNRAGMLNMKLNWHFQRWVRMYNKFGERRSELIGTPLNVARSRGGTTGASRGTALHRHSIVPLNAASTSKGKSSVFTERSQRTFDDNTDIASPPSKHIKGQSSELVEPEGHRSKP | Function: Secreted effector that acts as an elicitor that induces cell death in host plant cells.
Sequence Mass (Da): 39609
Sequence Length: 352
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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P62750 | MAPKAKKEAPAPPKAEAKAKALKAKKAVLKGVHSHKKKKIRTSPTFRRPKTLRLRRQPKYPRKSAPRRNKLDHYAIIKFPLTTESAMKKIEDNNTLVFIVDVKANKHQIKQAVKKLYDIDVAKVNTLIRPDGEKKAYVRLAPDYDALDVANKIGII | Function: Component of the large ribosomal subunit . The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell . Binds a specific region on the 26S rRNA . May promote p53/TP53 degradation possibly through the stimulation of MDM2-mediated TP53 polyubiquitination .
PTM: N-terminus is methylated by METTL11A/NTM1.
Sequence Mass (Da): 17695
Sequence Length: 156
Domain: The N-terminal beta-like import receptor binding (BIB) domain mediates interaction with IPO5, IPO7, KPNB1 and TNPO1.
Subcellular Location: Cytoplasm
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P35679 | MAAARPTVSIYSKDGSVSSETIALPFVFKAPIRPDLVRSVHTAVAKNKRQPYAVSEKAGHQTSAESWGTGRALARIPRVGGGGTHRSGQAAFGNMCRSGRMFAPTKTWRKWHVKVNQNEKRYAISSAVAASGVPSLLLARGHRIEEIPEVPLVVDDAVQSFQKTKEAVALLKEIKAYRDVVKVANSRKLRAGKGKLRNRRHVQRRGPLVVFNEDAGIVKAFRNIPGVEIVNVRRLNLLQLAPGGHLGRFVIWTKSAFGLLDSVFGSTTEAAQLKKNYFLPENIISNADVTRLINSDEIQSIVKAAGPSRVKRAHVQKKNPLKNKAVLARLNPYAKAYKANVKLNTGKTPKAAGEKFLTVLHEN | Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uL4 participates in the regulation of the accumulation of its own mRNA.
Sequence Mass (Da): 39767
Sequence Length: 363
Domain: The eukaryote-specific C-terminal extension harbors a nuclear import signal and delivers the ACL4-uL4/RPL4 complex to the pre-ribosome, triggering uL4 release from ACL4 and incorporation into the 60S ribosomal subunit.
Subcellular Location: Cytoplasm
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Q28346 | MACARPLISVYSEKGESSGKNVTLPAVFKAPIRPDIVNFVHTNLRKNNRQPYAVSELAGHQTSAESWGTGRAVARIPRVRGGGTHRSGQGAFGNMCRGGRMFAPTKTWRRWHRRVNTTQKRYAICSALACLSLPALVMSKGHRIEEVPELPLVVEDKVEGYKKTKEAVLLLKKLKAWNDIKKVYASQRMRAGKGKMRNRRRIQRRGPCIIYNEDNGIIKAFRKHPGITLLNVSKLNILKLAPGGHVGRFCIWTESAFRKLDDLYGTWRKAASLKSNYNLPMHKMLNTDLSRILKMPRDPRALRAPRKKIHRRVLKKNPLKNLRIMLKLNPYAKTMRRNTILRQAKNHKLRMDKAAAALEAKSEEKGVPGKKPRRKKGKKTVGVKKPKKPVVGKKAAATKKPAADKKPAEKKPTTEEKKPAA | Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
PTM: Citrullinated by PADI4.
Sequence Mass (Da): 47515
Sequence Length: 421
Subcellular Location: Cytoplasm
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Q6YRK2 | MFSKNKHNTKFIVIACVIVVLILILFCLDFQNIQEIIETINQLTNNQNPSQNTASEMSGMRRKIIFFIFNFFGKIILASFVISFLLHIKKNAQIKRLKNKLSLWSKLSFHVSQIGEEVLNELPIGIVLIDISSQEIQWLNPYASFILKNPEINSPLAQINENMAQLISTSDAIPKTIITLENKKFECFYKKDLNVFYLFDATEKEQIKHLFLQKTLALAMITFDNLAESLIRYDLSEQSQIQGEYLSALSDYIEPYEGYLKQLIDDRFLLLLNRQNLDKMLENKFIILDTIRNISYKYQLKVTLSMGIACWNLSYEKLATYSQNAIELAQKRGGDQVVVNIENEKIKYFGAKIASLSKQSKVHARINAQNLVDILKKHPHCFIMGHTHTDLDALGSVIAFYKIATTIHPESNNYIILDEEKLDKSLIPVYNQLIKTEAKTSLNIITTQQASKMIKDNSLIAVLDTQTKDMVNSPELLSLTSNVVVVDHHRATEEIIPSIFSYVESSASSTVELLVEVMGFLEKEVHITAFEASIMYAGILIDTNAFIYRTSSRTFEVASKLKDLGADAIEVKSWLRKDFDKVLEINKLISEMEIFMDRFAIIQSSEIYENRSFLAQVAEGVLNIRNVDAAFMIAQIADNKIAISARSYNEINVQTIMEQMEGGGHLNSAATQLEGTNIKTVTDTLKHFLKLEYEKGEKNMEIILLTDIPNKGKKHEIIKVNNGYGNFLIQNKKALLADKTNLAAIKQSQMLEQEQKRNHELLMHKLKQEIDDKKITLDIQLGPKGKIYGKITLKQIAEEFLKVHNITLDRKKISLEGEIIAIGIYPVDVFLTDQIKATFFLNVTERKSK | Function: Binds to the 23S rRNA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96795
Sequence Length: 849
Subcellular Location: Cell membrane
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Q9LIG2 | MEYHPQAIRLCALIFISFYALLHLVEAQDQKGFISLDCGSLPNEPPYNDPSTGLTYSTDDGFVQSGKTGRIQKAFESIFSKPSLKLRYFPDGFRNCYTLNVTQDTNYLIKAVFVYGNYDGLNNPPSFDLYLGPNLWVTVDMNGRTNGTIQEIIHKTISKSLQVCLVKTGTSSPMINTLELRPLKNNTYNTQSGSLKYFFRYYFSGSGQNIRYPDDVNDRKWYPFFDAKEWTELTTNLNINSSNGYAPPEVVMASASTPISTFGTWNFSWLLPSSTTQFYVYMHFAEIQTLRSLDTREFKVTLNGKLAYERYSPKTLATETIFYSTPQQCEDGTCLLELTKTPKSTLPPLMNALEVFTVIDFPQMETNPDDVAAIKSIQSTYGLSKISWQGDPCVPKQFLWEGLNCNNLDNSTPPIVTSLNLSSSHLTGIIAQGIQNLTHLQELDLSNNNLTGGIPEFLADIKSLLVINLSGNNFNGSIPQILLQKKGLKLILEGNANLICPDGLCVNKAGNGGAKKMNVVIPIVASVAFVVVLGSALAFFFIFKKKKTSNSQDLGPSSYTQVSEVRTIRSSESAIMTKNRRFTYSEVVTMTNNFERVLGKGGFGMVYHGTVNNTEQVAVKMLSHSSSQGYKEFKAEVELLLRVHHKNLVGLVGYCDEGENLALIYEYMANGDLREHMSGKRGGSILNWETRLKIVVESAQGLEYLHNGCKPPMVHRDVKTTNILLNEHLHAKLADFGLSRSFPIEGETHVSTVVAGTPGYLDPEYYRTNWLNEKSDVYSFGIVLLEIITNQLVINQSREKPHIAEWVGLMLTKGDIQNIMDPKLYGDYDSGSVWRAVELAMSCLNPSSARRPTMSQVVIELNECLSYENARGGTSQNMNSESSIEVSMNFDIGATPDAR | Function: Probable receptor with a dual specificity kinase activity acting on both serine/threonine- and tyrosine-containing substrates.
PTM: Autophosphorylated on Tyr and Thr residues.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 100195
Sequence Length: 899
Subcellular Location: Cell membrane
EC: 2.7.10.1
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F4I2N7 | MAPSLRNFNFFHRFSTFLVFSLFSVVSSDDLQVLLKLKSSFADSNLAVFDSWKLNSGIGPCSFIGVTCNSRGNVTEIDLSRRGLSGNFPFDSVCEIQSLEKLSLGFNSLSGIIPSDLKNCTSLKYLDLGNNLFSGAFPEFSSLNQLQFLYLNNSAFSGVFPWKSLRNATSLVVLSLGDNPFDATADFPVEVVSLKKLSWLYLSNCSIAGKIPPAIGDLTELRNLEISDSGLTGEIPSEISKLTNLWQLELYNNSLTGKLPTGFGNLKNLTYLDASTNLLQGDLSELRSLTNLVSLQMFENEFSGEIPLEFGEFKDLVNLSLYTNKLTGSLPQGLGSLADFDFIDASENLLTGPIPPDMCKNGKMKALLLLQNNLTGSIPESYANCLTLQRFRVSENNLNGTVPAGLWGLPKLEIIDIEMNNFEGPITADIKNGKMLGALYLGFNKLSDELPEEIGDTESLTKVELNNNRFTGKIPSSIGKLKGLSSLKMQSNGFSGEIPDSIGSCSMLSDVNMAQNSISGEIPHTLGSLPTLNALNLSDNKLSGRIPESLSSLRLSLLDLSNNRLSGRIPLSLSSYNGSFNGNPGLCSTTIKSFNRCINPSRSHGDTRVFVLCIVFGLLILLASLVFFLYLKKTEKKEGRSLKHESWSIKSFRKMSFTEDDIIDSIKEENLIGRGGCGDVYRVVLGDGKEVAVKHIRCSSTQKNFSSAMPILTEREGRSKEFETEVQTLSSIRHLNVVKLYCSITSDDSSLLVYEYLPNGSLWDMLHSCKKSNLGWETRYDIALGAAKGLEYLHHGYERPVIHRDVKSSNILLDEFLKPRIADFGLAKILQASNGGPESTHVVAGTYGYIAPAEYGYASKVTEKCDVYSFGVVLMELVTGKKPIEAEFGESKDIVNWVSNNLKSKESVMEIVDKKIGEMYREDAVKMLRIAIICTARLPGLRPTMRSVVQMIEDAEPCRLMGIVISKESDVKVKEIS | Function: Plays a role in pattern-triggered immunity (PTI) signaling induced by pathogen-associated molecular patterns (PAMPs). Acts as a receptor for PIP1 defense peptide. PIP1 is an endogenous secreted peptide that acts as elicitor of immune response and positive regulator of defense response . Involved in the control of seed germination speed, in tolerance to oxidative stress and in maintaining seed longevity .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 107450
Sequence Length: 977
Subcellular Location: Membrane
EC: 2.7.11.1
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Q9LVI6 | MRLFFTPSMSNLSIFFSILLLSLPLPSIGDLAADKSALLSFRSAVGGRTLLWDVKQTSPCNWTGVLCDGGRVTALRLPGETLSGHIPEGIFGNLTQLRTLSLRLNGLTGSLPLDLGSCSDLRRLYLQGNRFSGEIPEVLFSLSNLVRLNLAENEFSGEISSGFKNLTRLKTLYLENNKLSGSLLDLDLSLDQFNVSNNLLNGSIPKSLQKFDSDSFVGTSLCGKPLVVCSNEGTVPSQPISVGNIPGTVEGSEEKKKRKKLSGGAIAGIVIGCVVGLSLIVMILMVLFRKKGNERTRAIDLATIKHHEVEIPGEKAAVEAPENRSYVNEYSPSAVKAVEVNSSGMKKLVFFGNATKVFDLEDLLRASAEVLGKGTFGTAYKAVLDAVTLVAVKRLKDVTMADREFKEKIEVVGAMDHENLVPLRAYYYSGDEKLLVYDFMPMGSLSALLHGNKGAGRPPLNWEVRSGIALGAARGLDYLHSQDPLSSHGNVKSSNILLTNSHDARVSDFGLAQLVSASSTTPNRATGYRAPEVTDPRRVSQKADVYSFGVVLLELLTGKAPSNSVMNEEGMDLARWVHSVAREEWRNEVFDSELMSIETVVSVEEEMAEMLQLGIDCTEQHPDKRPVMVEVVRRIQELRQSGADRVG | PTM: Autophosphorylation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70406
Sequence Length: 647
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cell membrane
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Q5SI81 | MLGPVLRLVVKAGKERKLRNFYPNLYRDEIAAPPEGVGVAEAVDAEGHFLAVGYYDPRSRVPFRAFRFDPGPLNRAFFQGRFARALRRRQGLGESHRLVHGEADGLPGLVVDRFGEVLVLQVRSRGMEALREVWLPALLEVVAPKGVYERSDVEARRQEGLPERVGVVYGEVPEVLEVEEDGLRFPIPLALAQKTGYYLDQRENRRLFEAMVRPGERVLDVYSYVGGFALRAARKGAYALAVDKDLEALGVLDQAALRLGLRVDIRHGEALPTLRGLEGPFHHVLLDPPTLVKRPEELPAMKRHLVDLVREALRLLAEEGFLWLSSCSYHLRLEDLLEVARRAAADLGRRLRVHRVTYQPEDHPWSLHIPESLYLKTLVLQDDPL | Function: Specifically methylates the cytosine at position 1942 (m5C1942) of 23S rRNA.
Sequence Mass (Da): 43563
Sequence Length: 385
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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F4I594 | MASSSSSASRTWRYRVFTSFHGSDVRTSFLSHFRKQFNNNGITMFDDQRILRGETISPALTQAIRESRISIVLLSKNYASSGWCLDELLEILKCKDDMGQIVMTVFYGVDPSDVRKQTGEFGIAFNETCACRTEEERQKWSQALNYVGNIAGEHLLNWDNEAKMIEKIARDVSEKLNVTPCRDFDGMVGIEAHLRKIQSLLDLDNDEVKMVAISGPAGIGKSTIGRALHSLLSNRFHHTCFVDNLRGSHPIGLDEYGLKLRLQEQLLSKILNQDGSRICHLGAIKERLCDMKVFIILDDVNDVKQLEALANESNWFGPGSRIIVTTENKELLKQHGINNTYYVGFPSDEEAIKILCRYAFRQSSSRHGFKKLTRSVTELCGKLPLGLRVVGSSLHGKNEEEWEYVIRRLETIIDRDIEQVLRVGYESLHENEQSLFLHIAIFFNYEDGDLVKAMLAENDLDIEHELNILVNKSLIYISTDGRIRMHKLLQLVGRQANQREEPWKRRILIDAQEICHVLENDIGTGAVSGILFDTSGINEVSISNKALRRMCNLRFLSVYKTKHDGYNRMDIPEDMEFPPRLRLLHWDAYPSKCLPLKFRAENLVELDMKDSRLEYLWPGTQLLTKLKKLNLEGSYNLKELPDLSNATNLEMLDLSVCLALAELPSSIKNLHKLDVIYMDLCESLHMIPTNINLASLETMYMTGCPQLKTFPAFSTKIKRLYLVRTGVEEVPASITHCSRLLKIDLSGSRNLKSITHLPSSLQTLDLSSTDIEMIADSCIKDLQRLDHLRLCRCRKLKSLPELPASLRLLTAEDCESLERVTYPLNTPTGQLNFTNCLKLGEEAQRVIIQQSLVKHACFPGSVMPSEFNHRARGNSLKILVKSSASFAFKACVLISPRQLQCERNQRRVKIRCRVTDGRGRFVGSKVVSLEHPNHSTGIRTKHLCFFNGVLTEVSCDALCFVFKISAYNPLDNYEISECAVQILTNEPERRSCDGGSE | Function: TIR-NB-LRR receptor-like protein that confers resistance to the pathogen Leptosphaeria maculans (blackleg disease).
Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
Sequence Mass (Da): 113174
Sequence Length: 997
Domain: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
EC: 3.2.2.6
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Q9CAK1 | MASPSSFSSQNYKFNVFASFHGPDVRKTLLSHIRLQFNRNGITMFDDQKIVRSATIGPSLVEAIKESRISIVILSKKYASSSWCLDELVEILECKKAMGQIVMTIFYGVDPSDVRKQIGKFGIAFNETCARKTEEERQKWSKALNQVSNIAGEDFLRWDNEAIMIEKIARDVLDKLNATPSRDFDGMVGIEAHLREIKSLLDLDNVEVKIVAIAGPAGIGKTTIARALYGLLSKRFQLSCFVDNLRGSYHSGFDEYGFKLHLQEQFLSKVLNQSGMRICHLGAIKENLSDQRVLIILDDVNKLKQLEALANETTWFGPGSRIVVTTENKELLQQHGINNTYHVGFPSDEDALKILCSYAFKQTSPRHGFEELSESVTKLCGKLPLGLCVVGSSLRGKKEDEWEDVVTRLETILDQDIEDVLRVGYESLDENAQTLFLHIAIFFNKEDGDLVKTMFAESDLDVKYGLKILENRSLIKMKIFSNGDTKIVMHRLLQQMGKRAIQKQEPWERQILIDAREICHVLEHAKGTGWNVHGMSFDISRISEVSIRKKAFKRMPNLQFLKVYKSKDDGNNRMHVPEEMDFPCLLRLLDWKAYPSKSLPPTFNPEHLVELNMHSSQLEYLWQGTQPLKNLKKMDLSQSKNLKQLPDLSNATNLEYLYLMGCESLIEIPSSISHLHKLEMLATVGCINLEVIPAHMNLESLQTVYLGGCSRLRNIPVMSTNIRYLFITNTAVEGVPLCPGLKTLDVSGSRNFKGLLTHLPTSLTTLNLCYTDIERIPDCFKSLHQLKGVNLRGCRRLASLPELPRSLLTLVADDCESLETVFCPLNTLKASFSFANCFKLDREARRAIIQQSFFMGKAVLPGREVPAVFDHRAKGYSLTIRPDGNPYTSFVFCVVVSRNQKSDKTIPPSLLWRRIIAQDEGYPVEVWNRIGDVFKYRTEHLLIFHFDFLEFDNRDIVFEFSSESHDFDIIECGAKVLAEKSIKESYESGSDQAFEDDVVFEPSKAFGDEKYGDCCIL | Function: TIR-NB-LRR receptor-like protein that confers resistance to the pathogen Leptosphaeria maculans (blackleg disease).
Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
Sequence Mass (Da): 115415
Sequence Length: 1017
Domain: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
EC: 3.2.2.6
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Q12224 | MGRRKIEIQRISDDRNRAVTFIKRKAGLFKKAHELSVLCQVDIAVIILGSNNTFYEFSSVDTNDLIYHYQNDKNLLHEVKDPSDYGDFHKSASVNINQDLLRSSMSNKPSKSNVKGMNQSENDDDENNDEDDDDHGNFERNSNMHSNKKASDKNIPSAHMKLLSPTALISKMDGSEQNKRHPENALPPLQHLKRLKPDPLQISRTPQQQQQQNISRPYHSSMYNLNQPSSSSSSPSTMDFPKLPSFQNSSFNGRPPPISISPNKFSKPFTNASSRTPKQEHKINNSGSNNNDNSNYTQSPSNSLEDSIQQTVKARRKLSARPVLRVRIPNNNFSSNSAIPSEPSSASSTSANGNSMGSSQIMKENKTSRSSKISPLSASASGPLTLQKGNNGRMVIKLPNANAPNGSNNGNGSNNNNHPYPFGSGSSPLFSATQPYIATPLQPSNIPGGPFQQNTSFLAQRQTQQYQQMSFKKQSQTVPLTTTLTGRPPSTFSGPETSNGPPTGSLPSKFVHDLMSNSPNVSSISMFPDWSMGPNSAKPGNTNNPGTFPPVQTAVNNGNSSNISSTNNTNNNNNNNNNNSSNNNSNNGNDNNSNNSNNSYYSNNEDAPVNGAAISEHTTDGDSNNQSNSSTYDAAATAYNGNTGLTPYINTAQTPLGTKFFNFSTDISGEKNSSKI | Function: May function as a transcription factor downstream of MPK1 that is subject to activation by the MPK1 mitogen-activated protein kinase pathway. Binds to the DNA sequence 5'-CTA[TA](4)TAG-3'. At least some RML1 target genes are involved in cell wall biosynthesis.
PTM: Phosphorylated by SLT2.
Sequence Mass (Da): 73484
Sequence Length: 676
Subcellular Location: Nucleus
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Q9FT77 | MKSSSSQSYDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNRIERSRKITPELLLAIENSRISLVVFSKNYASSTWCLDELVKIQECYEKLDQMVIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEKRKWMRALAEVAHLAGEDLRNWRSEAEMLENIAKDVSNKLFPPSNNFSDFVGIEAHIEALISMLRFDSKKARMIGICGPSETGKTTIGRALYSRLKSDFHHRAFVAYKRKIRSDYDQKLYWEEQFLSEILCQKDIKIEECGAVEQRLKHTKVLIVLDDVDDIELLKTLVGRIRWFGSESKIVVITQKRELLKAHNIAHVYEVGFPSEELAHQMFCRYAFGKNSPPHGFNELADEAAKIAGNRPKALKYVGSSFRRLDKEQWVKMLSEFRSNGNKLKISYDELDGKGQDYVACLTNGSNSQVKAEWIHLALGVSILLNIRSDGTTILKHLSYNRSMAQQAKIWWYENLERVCKKYNICGIDSSTDGGGSTYGQCSNSQFQRNMDASPGGNKTSNQSTKDSPRASQVEKEKIEYCEPHVYITPAIFSDGTRAPKYVESSSRRVTQVHHAKTWWPENCEKVYENHNNIYGIDRSIDGGDKFEGKSKVSDGGLDGKDQGSMYGQSSNSELQINMDADNRRCEPVSEMLFKNYNVCSPNGLTDVNCSNPQSQRKLDASLKKDKIVHEWIRTGSGFFFDFQGPKSIVSAAQVDEKNFEYCEQGVYITLGILSGGIIVLKHLEFSRRMAQQAKVWWSENWIKVYQEHNICGIDKSFDGRFDDRRVIRQLRPN | Function: TIR-NB-LRR receptor-like protein that confers resistance to the pathogens Leptosphaeria maculans (blackleg disease), Botrytis cinerea, Alternaria brassicicola and Alternaria brassicae. Required for efficient callose deposition downstream of RLM1 during infection with L.maculans.
Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
Sequence Mass (Da): 91154
Sequence Length: 796
Domain: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
EC: 3.2.2.6
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Q9S1M6 | MRKNVVRYLRCPHCAAPLRSSDRTLRCENGHTFDVARQGYVNLLRRPTKLAADTTDMVAARAALLDSGHYAPLTERLAGTARRAAGAGAPDCVVDIGGGTGHHLARVLEEFEDAEGLLLDMSKPAVRRAARAHPRASSAVADVWDTLPLRDGAAAMALNVFAPRNPPEIRRILRPGGTLLVVTPQQDHLAELVDALGLLRVRDHKEGRLAEQLAPHFEAVGQERLRTTLRLDHDALGRVVAMGPSSWHQDPDELARRIAELPGIHEVTLSVTFTVCRPLP | Function: Specifically methylates the guanosine in position 748 of 23S rRNA. Confers resistance to the macrolide antibiotic tylosine.
Catalytic Activity: guanosine(748) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(748) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30543
Sequence Length: 280
EC: 2.1.1.188
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Q4WX78 | MGRRKIEIKAIKDDRNRSVTFLKRKGGLFKKAHELAVLCSVDVAVIIFGHNKKLYEFSSCDMRETLGRYQYYGPPHEHKGPEDFNGKRDDDDDEDETTPAPEEMQPTTQNPPAVVPAHIPSHPGFQHVNHAPSASPPISNGIPFDPRHGTPQPQGASRPSSRNHLRRVSSNLGPQQHHGTPPPPPQNGFAYIPNPSMYHPNANPNIAQQPRPPQFAHYGPQQPLPPHAIPPHPMPQPVPPHHQAPQHLPQHPHPLAQQTPAMGLSQPPHASIPQVAQPFLPEQGRNSIPPAFPTEQSQPPRPVSLPDVSSADQMVGPLKVETSPSPPHQRSLSSKSRSIFTPIDDRGSVLARHFGLGPPTCESPRTESADVKAEAKQNDSKEIKPPAQPVAPPPPPRTTADAARSQSAPDIKPPPRTNSGQLPSKRPQLKVQIPSENSDRGSATADSSSSTGNQTVTPAKANPDTNHSGVVLPPPSPSAGAILSAGATGPPNPFARPPPPGTASQNSNAYNSNNNIETPISALPSRFVSDALLPSPSSFFPEWGFGRSGPDTNMLPSPLTFPTPAVQTGPGFAREDEQEKKRKSPDSGPSIEGTAKKSKT | Function: Transcription factor; part of cell wall integrity (CWI) signaling pathway composed of pkcA, the bck1-mkk2-mpka MAPK cascade and the downstream rlmA transcription regulator . The CWI signaling pathway regulates cell wall integrity and pyomelanin formation . CWI controls also oxidative stress response, gliotoxin production, iron adaptation and asexual development . Finally, CWI is constitutively required for A.fumigatus to cope with the temperature increase found in the mammalian lung environment, during infection . Positively regulates the phosphorylation of mpkA . Involved in tolerance to oxidative damage and transcriptional regulation of genes related to oxidative stress adaptation . Finally, CWI is constitutively required for A.fumigatus to cope with the temperature increase found in the mammalian lung environment, during infection . Directly regulates the expression of regulators of conidiation, including flbB, flbC, brlA, abaA, and rasB, as well as genes involved in cell wall synthesis and remodeling . Specifically associates with the target fumiquinazoline (fmq) cluster genes promoters at conserved motifs (5'-TAWWWWTA-3') during conidiation to supplement mature conidia with fumiquinazoline C . Controls also the DHN-melanin production via binding the promoter of pksP .
PTM: Phosphorylation during asexual development.
Sequence Mass (Da): 64379
Sequence Length: 600
Subcellular Location: Nucleus
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P36999 | MSFSCPLCHQPLSREKNSYICPQRHQFDMAKEGYVNLLPVQHKRSRDPGDSAEMMQARRAFLDAGHYQPLRDAIVAQLRERLDDKATAVLDIGCGEGYYTHAFADALPEITTFGLDVSKVAIKAAAKRYPQVTFCVASSHRLPFSDTSMDAIIRIYAPCKAEELARVVKPGGWVITATPGPRHLMELKGLIYNEVHLHAPHAEQLEGFTLQQSAELCYPMRLRGDEAVALLQMTPFAWRAKPEVWQTLAAKEVFDCQTDFNIHLWQRSY | Function: Specifically methylates the guanosine in position 745 of 23S rRNA.
Catalytic Activity: guanosine(745) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(745) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30419
Sequence Length: 269
EC: 2.1.1.187
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Q6FF50 | MAKPEYYYGVHSVESLLELEPERVLTLFTLKGRDDQRLQKILELAEPFGISVQKASRDSLEKLAGLPFHQGVVAAVRPHPVLNEKDLDQLLQNNDQALLLALDQVTDPHNLGACIRTAAAMGIAAVIVPRDRSASLTPTARKVAAGGAEKVKFIQVTNLARTLAHIKAHFFVKVVGTMLDEKALPIQKYDFSGNVAIVMGAEDTGLRPITQSQCDQTVYIPMSGNLQSLNVSVAAGMALYEACRQRLG | Function: Specifically methylates the ribose of guanosine 2251 in 23S rRNA.
Catalytic Activity: guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26984
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 2.1.1.185
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Q7VQP0 | MSELVYGIHTVESIVNQSPNRILIVYIVSNPRDLRLKSLIYRIRKMNINIQECTRRVLNIKSMKSAHQGIIAEVIPMPALNEDYLLHFLKTKNNIIPLLLVLDGITDPHNLGACIRSADAAGVHMIIVPRDRSANVNATVRKVASGSSDRVPFVRVTNLSRTLKLLKKYNIYIVGSVLRSNQILFNTRLIDPIALVMGSESSGIRRLTRENCDKLVHIPTLQSTVSLNVSVATGIFLFETVRQRKYQNGFINYS | Function: Specifically methylates the ribose of guanosine 2251 in 23S rRNA.
Catalytic Activity: guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28590
Sequence Length: 254
Subcellular Location: Cytoplasm
EC: 2.1.1.185
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Q7WKX5 | MASTQVLAGFHAVVARLRHAPESIKEIYVEASRRDKRMQTFLEQAERAGRRVHPVAAERLDGLARGTRHQGVVAVAEERSLAVGIDEVLDVIEGPALLLILDGVTDPHNLGACLRTADAAGVHAVIAPRDRAVGLNATVQRVACGAADTVPYLTVTNLARTMRELKERDVWLVGTDDQAGESMHQVDARRSMAWVMGAEGEGMRRLTRETCDQLVRIPMLGSVESLNVSVASAVCLYESVRQRQG | Function: Specifically methylates the ribose of guanosine 2251 in 23S rRNA.
Catalytic Activity: guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26621
Sequence Length: 245
Subcellular Location: Cytoplasm
EC: 2.1.1.185
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Q9RED7 | MPRLKLLHGFHAITARLRAFPATVNEVWYDPARQDARMRAFLHLAASANARLIAADASRLNALSGEKRHQGVVARVTEATRAHSLETLLDTIEGQPLLLALDGVTDPHNLGACLRVADGAGAHAVIAPRRRAAGLTAAAAKAANGAAETVPYLTVINLARALRALKNAGIQVIGTADDATTSLFDIQLDGALALVMGAEGAGMRRLTREACDEVVRIPLAGHVQSLNVSVASGICLFEAVRQRLKRL | Function: Specifically methylates the ribose of guanosine 2251 in 23S rRNA.
Catalytic Activity: guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26118
Sequence Length: 247
Subcellular Location: Cytoplasm
EC: 2.1.1.185
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B4SRK6 | MARSRSRIDRTPFQTEILDLSHDGRGVARREGEGGKVTFVSGALPGEVVMAEQTARSRHFDEARTVEVLKASPQRVTPKCPHFGTCAGCVLQHLDEDQQIVAKQRVLMDNLERIGHVKPGTVLAPLVGESWGYRRKGRFSVRRVEKKDKTLVGFREQDPRFVADLSQCLTVIPEIGTKVEALSTFIESLDGKRDIPQIEFIAGDQAVVLTVRHLQPLSDADRAAWATFGQQHGFVIYLQSGGVDTVQPLDGQGVPLSFRLAPWDVELAFRPLDFIQVNAKLNEKMIAHALDLLEPGEDERVLDLFCGLGNFTLPLARRVREVVGVEGDAGLVARARENAERNGLANAQFFSADLTQDQRSTAWMRQGFDKLLLDPPRSGAIEVLQQLPLKQFKRIVYVSCHPGSLARDAGYLVNEQGFTLVSAGAMDMFPHTAHVESIAVFEKR | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49223
Sequence Length: 444
EC: 2.1.1.190
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C4LBR5 | MVQFFQPKPKALPTQAVEITIDNLDHHLTGVGRYQGKACFVEGVLPGEKVSVQITEQKKQYAHARLRQVIEPSADRCEPFCPAFKQCGGCNAQMMPQAMQCQAKQQGVQRLFRQLAKIDLPAPLWIESSAPQAYRRVCRLAVKYDKNKRCVLVGFRQKQSQALVEINSCPVLTAALSALIVPLRTLINELSSARDVGHIELYETESGLAMLLRHNGRPPVKDKELLLAFALQHDCALYLQTTGYPEPLADVKPSFYQLDGLRLYFQPGDFLQVNPQVNQRLVNYVREWLAPTATDNVLDLFCGIGNFTLPLAREAASVTGIEGVDEMVQRATHNAEQNQLVNTGFHRADLTKMAEYANAGWQQQCYDLVLLDPGRTGAEAVMPWLAKSGARRIVYVSCNPVTAARDCALLQPGYTLKQWGLLDMFPHTGHVESLFLFERK | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49224
Sequence Length: 440
EC: 2.1.1.190
|
A5CXB2 | MRRRRKLEHKTYKLNIESFSHEGRGIAHFEDKIIFVSDALPGELVIANRTFSCAKFEEADAKEILKPADNRMKPKCDVFGICGGCSFQNLSSEDQIQIKSRWLKKVFARQAKVEPETWLKSLQFQSWGYRRKARLGIRYVAKKDKVLIGFRERKSSFITNMSRCEVLHPSIGEHLEVLANCIERLSIKSSIPQFEVVISESGIALILRHLESLSVKDEKILADCAQELNITFYTQSGGLDSVKPLDEPTILTYSHSNYNIIMEFLPTDFVQVNFKLNQQMVSLAVELLELNESDKVIDLFCGLGNFTLPIARYAKYVVGIEGDLGLVERAKYNAEKNSINNVDFYRSDLCKEVVGFEWFKGKTYNKALIDPSRSGAIEIVELLPKLGVTRLVYVSCNPATLARDTLKLIKLGFTLETAGVIDMFPQTSHVESIALFVKR | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49838
Sequence Length: 439
EC: 2.1.1.190
|
Q7MHP7 | MARFFQPKKKLQPESKHQQVLVEKLDHQGAGIAYLNKKPLFIDGTLPGEEVVTQLTESKSKFARGKLIKLLKPAAERVEPFCSHFNQCGGCDMQHMDYQAQLAYKQRTLLQLMKKFSGSEILLSPPVTGLEKAYRRRARVSLMWDKKSRQLQFGFRRKQSKQIENVTQCPVLVAELECLLPELKAILSHFHHPEHLGHVELVAADNGAVITLRHTGPLLDEDVAKLRQCAEQHQATLYLMPASDQLERISGEAPYYQEIGFKVPFEPNNFIQVNQKVNQQMVVQALEWLDPQSSDRVLDLFCGLGNFSLPIASKAKSVTGVEGVDDMVQKAALNASLNQINNAQFFHANLEQDFVGQPWASEKFDKILLDPARAGASGIIEQVSALGAKRVVYVSCNPATLARDSQSLLEQGYRLTKLGMLDMFPYTSHLESMALFEK | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49216
Sequence Length: 438
EC: 2.1.1.190
|
Q8PMU6 | MARTRNRLDRTPFQTAVTDLSHDGRGVARRDGEGGKVTFISGALPGELVRAEPTARSRHFDEAKTVGVLEASPQRVTPRCPHFGVCAGCVLQHLEESQQIVAKQRVLMDNLERIGHVTPQAVLPALTGDNWGYRRKGRFSVRRVEKKDKTLVGFRELDPRFVADLSVCYTVIPQIGEKIPLLAALIEGMDGKRDIPQIEFIAGDDAVALTIRHMQPLSERDRQAWITFAQEHGFAIFLQPGGVDSVQPLWPQEVPLSFRLPQWDVELAFRPLDFIQVNASLNQKMIAHAVALLEAKPDDRVLDLFCGLGNFTLPLARVVREVVGVEGDAGLVARAKENAQRNGLDNAQFYAADLTQDQRSAPWMRQGFDKLLLDPPRSGALEVLQQLPLKTFQRIVYVSCHPGSLARDAGYLVNEQGFTLVSAGAMDMFPHTAHVESIAVFERR | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49346
Sequence Length: 444
EC: 2.1.1.190
|
Q3YRW8 | MDNKFSIFKKGQYVLDLGSFPGGWSQFAAQKVSHGNNNLVFSVDIQNMDAIPNVIFIKCDISNEIEILNDKFHNKKFDVILSDMAPKACGNKQVDHANIINLCEMSLDIVIKFARENGTFITKILQGEYEKEFYQSMKSNFKLVKYFKPKASRKDSSEIYLVGLGFKKDFQ | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 19554
Sequence Length: 171
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
A9FQE4 | MPAERPSVSQKPKNPYKRPDAFTKAAKAQGYPARSVFKLEEIDRRVRLLRPGQRVLDLGAAPGSWSMYAAQRIGAGGKLLAVDLSPITAAFGPQATVVQGDALSLTNEALAQFAPYDVVLSDMAPATSGSKIADQARSYELFMRAVAVAEALLAPGGAFVGKIFMSEDFVKARDALRNLCEEVRSIRPEGTRASSVEIFLVGLKRKAAGKTG | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22652
Sequence Length: 212
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
A4VNP3 | MKRSKSSRRWLDEHVNDPFVKRAQKDGLRSRSSYKLIELNEKDKLIRPGMLVMDLGSAPGGWSQVAGGIVGEKGRVLATDILPMGGLDNVDFVQGDFTEDAVFQQILDMLDGRQPDLIVSDIAPNISGVAAADQAASMYLVELTLDMVRQVLKPGGNYVVKVFQGEGSDEFLKDVRSSFEKVVIRKPEASRPRSREVYLVAKGFKG | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22742
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
A0LGZ0 | MSYTVRDHYFHKAKKEHYLARAVYKLQEIQDRYKILKPGNRVLDLGAAPGSWMQFAREIVGPSGLVVGVDLKGVEHRFPEGVVVLQGDVTDPELARSLSVEHGPFDVVLSDMAPSTSGIRVADSARSALLFESALEMARSALRPGGHFVAKLFQGAEFHVLLQAVKRDFEWVKVTKPDASRKQSKEIYVIGMRLRKS | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22003
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
Q97C13 | MTGDRRDEYYWKAKKEQLRSRAAFKLEFLLDRYRVVRKGDAVIEIGSSPGGWTQVLNSLARKIISIDLQEMEEIAGVRFIRCDIFKETIFDDIDRALREEGIEKVDDVVSDAMAKVSGIPSRDHAVSYQIGQRVMEIAVRYLRNGGNVLLKQFQGDMTNDFIAIWRKNFSSYKISKPPASRGSSSEIYIMFFGFKAP | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22604
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
Q3SJR5 | MAQKPKRTKSGSAWMHEHVTDAYVKKAQQDGFRSRAAYKLLEIDSRDHLLHPGMTVVDLGAAPGSWCQVAVQKMKRQGRVLAIDLLPVAPLPGVEALQGDFTAPDTLAWLENTLQAARVDLVLSDMAPNMSGVMLRDQARHYELCELALDFAVNWLKPDGAFLVKVFQGSGFEDFRNAMRRAFDQVVIRKPDASRDRSSEVYLLGRRPVKLESVAATGAS | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24376
Sequence Length: 220
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
Q73L97 | MAKNKYSEPDYWSKKAFAENYPARSVYKLEEMNKKFNLFSPNDKVLDLGAAPGSWTVYVLRFLNKEGRVTAVDLKPLDSSVYDERLNFFQGDMFDKGIIKSVKELGPYDAVICDAAPATTGNKTVDTARSSGLVELALYYAQEQLKQGGSFVVKIFQGGDQQIHLNNLRKCFKTARAFKPEACRSSSFETYLIGLDFKG | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22359
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
O83687 | MNVYKRADFWAKKAAAAGYRARSVYKLAALDKKYSLLSRASRVLDLGAAPGSWTQYVLGTAAACTAVCAVDVQPIASDIQDARLQRVQGDLCAADTRARVACNAPFDLILSDAAPRTTGNRTVDTSASACLAAGVCAYVNFLSSDGGLVFKVFQGSEHLAILTHLRAHFGAVCSFKPPASRPRSCELYVVARFFRGTCGK | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 21318
Sequence Length: 200
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
Q8KTR0 | MGRTSEWYARHVGDSFVRTSKAWGYRARAACKLKRLDAKYGLMSRQCDVLELGSSPGVWSQYISYERRVSGMAWRTVSVDTRAMVRVRGVSFIHGDITEAETMAEVSSRLPSGVGLILSDICPHPSCERYLDSIATAKVAETLLMVSRRFLLDGGALLHKTFVIRAEHIASVMERHFSSVEVYRDASSRSFNSEAYLLCVGD | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22594
Sequence Length: 202
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
A1WEE7 | MKVKTRSKKVNKAWLDQHVNDPYVQRARKEGYRARAAYKLREIDEQLGLIRPGYTVVDLGATPGAWSQYLRRRMAAEGAIIALDILPMEPLEGVTCLHGDFRAPDVQQRLEQALAGRVVDVVVSDMAPNLSGIACADAARMADLVELAVAFSCRHLKPDGALLVKLFHGSGYSDLAALFKQTFLRVVPLKPKASRDKSSETFLLGRGLKKASPNGLDSRSGTAAEPAPLVPIGTNSMPANGD | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26246
Sequence Length: 242
Subcellular Location: Cytoplasm
EC: 2.1.1.166
|
B2VDD5 | MSQLELSNRMLTLHRFPQMREESPLQAWDAADEYLLNHLDNLPVNGPTLIFNDTFGALACALAGEGVWSISDSWLNQQATRQNLALNQLDEGDVRLLDSLAPLPGAPARVLIKVPKTLALLEKQLRALRAVVTPETQIVAAGKAKEIHTSTLQLFEKILGPTTTSLAWKKARLIYATFTQPELAESEVISRWPLDGTPWQIHNHANVFARGGLDIGARFFMQHLPDDIDGEIVDLGCGNGVIGLMALRQNPLAQVHFLDESYMAVASSRMNVELNCPDDLARCEFRVNNALAGYPSDRLHAVLCNPPFHQQNAVTDHIAWQMFRDARRCLQYGGELRIVGNRHLDYYHKMKKLFGNCTTVATHQKFVILRSVKMP | Function: Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA.
Catalytic Activity: guanosine(1835) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1835) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41976
Sequence Length: 375
Subcellular Location: Cytoplasm
EC: 2.1.1.174
|
A0L9S5 | MQHLNIHGHTLTLRRFPHKPGCPLQAWDAADALALTNHALPDGEILILNDHFGALACGLAYPERTLEWVNDSYMAHQALAQNLQLNRIETPLHRTPALAASPTNPVGILIKLPRMLQLLSSQLDWLNLHLPKGTPVVIAARQKDMPSTLPDLTRRLLDDVHPSRAEKKARLIFGQLSGRQSGQAEITAWHCAELDCLLSHYPNVFGRQKLDLGARVLLQNLGTIPDQVVDLGCGNGVLSIAALQRNPNSHVLAVDESWQATRSCQINLERVRTPEHFKVVWGHSLSFIEGMQADLVLCNPPFHQHQTLTDDIAWCMFKDAHRVLKPGGRLRMVGNRHLGYHAKLHKLFGHCRSIAATPKFVVLESVKSS | Function: Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA.
Catalytic Activity: guanosine(1835) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1835) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41088
Sequence Length: 369
Subcellular Location: Cytoplasm
EC: 2.1.1.174
|
Q48DT7 | MPLLISPFAELDLIRQPEQQDEPLQAFDAADEYLLNHVAETGLSLQSRVLVLNDSFGALAASLASHATVVSSTDSFLAAQGLEKNLARNGMSYDAVPHIPASEPLSGPFDWVLIRVPKTLALLEEQLIRLQGQLAPGARVVAAAMVKHLPRSAGDLLEEYVGPVQASLAVKKARLLFATPQPMEVRTSPYPTRYRLDEPAIELLNHANVFCRDGLDIGTRAFLPYLPKNLGTARVADLGCGNGVLAIASALDNPQAHYTLVDESFMAVQSAAENWRATLGERVVEVRAADGLDTQEPDSLDVVLCNPPFHQQQVVGDFLAWRMFLQARAALVNGGALYIVGNRHLGYHTKLSRLFRGVEQVAATPKFVILKARK | Function: Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA.
Catalytic Activity: guanosine(1835) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1835) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40697
Sequence Length: 374
Subcellular Location: Cytoplasm
EC: 2.1.1.174
|
Q15YR1 | MKTELTLLDHSYELLRYPAENQHVSWQAWDSADEYLMEYVAQNITDLNGLNIHIYNDDFGALGVWFATNNAPLWISDSFVAHKALALNLERNHLPIENVNVQNSLYKANQKADLVLIKVPKTLALLEQQLIDLQSSVTPETRIIAAGKANAIQKSTLALFEKHLGLTTTSLAKKKSRLIFCQYDGVKQSVSPYPTKWKTDNTQFIMSNLANVFSRQQLDIGARVLLAHLPDANHKCIVDLGCGNGVLGLHVLHKSPGAHVIFVDESFMAIASAKMNIEQNMPDKLDQCKFIVSNCLDECLSSGENEATVDIVLCNPPFHQQNTITDHIALQMFKDSKRILKHAGELRVVGNRHLDYPQTIKRLFGHYKVLASDRKFSILSAIKK | Function: Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA.
Catalytic Activity: guanosine(1835) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1835) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 43112
Sequence Length: 384
Subcellular Location: Cytoplasm
EC: 2.1.1.174
|
B9MR74 | MIKIISVGTIKEKYFLQACEEYKKRLSRWVKVEEIEIKEEDENKYFNIETLLEKEADKILKHVKEGEFIIVCDINGIELSSEEFSEILRKNINSSKNITFIIGSSNGLSNEVKRRADLLLSFSKLTFPHQLFRVLLYEQIYRGLSIIYGTKYHK | 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): 18128
Sequence Length: 154
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
A0RMM1 | MQILVHCIQKKDDDFDNIKEYIKMSSKWADIKDINKFNSQIAKAQSASKEQAHKAYDLAYEHCLNGYCIGLDEKGYHLDSVEFADLLKNSSQISFFIGGAYGLSPQFKTKMNRLISLSKMTLAHKIAKLMLFEQIFRGLCINANHPYHK | 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): 17096
Sequence Length: 149
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
A7I0T3 | MSEIFVNSIQKNKNDFAMQIAEYIKMSQKFAALKDNVFFNQKIAKAQSIGKDEALKSYDEVYFAHKKGYLIALDERGEMIDSLQFAEILSKNSQISFFIGGAYGLSENFKQKMDKIISLTKLTLAHKIAKLMLFEQIFRGLCINAGHPYHK | 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): 17271
Sequence Length: 151
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q9PJ01 | MENNLQVNIFCIQKSDEFKTCSEKYSKLISKYATLKEINVFNKKIALAQNLNAIEAKKSYEEAFMPYKKGYCIALDEKGKDLTSIEFAKLIQDKNELSFFIGGAYGLREEFNQSLDFRLSLSKLTLAHQFVKTLLLEQIYRAFCINNNHPYHK | 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): 17783
Sequence Length: 153
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q9A2X3 | MMKITILTVGKLGRMVEAQLALDYASRATASGRALALGPVDILEVEARKPGKAAEAEVLRPHLEGAYVVACDEHGKAWKSRAFADHLARLRDDGNRRVVFLIGGADGLDPSILAAANETMAFGVQTWPHALARAMLAEQIYRAATILSGSPYHRD | 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): 16690
Sequence Length: 155
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
B3PKN1 | MRIRIIAVGTKMPEWVEQGYAEYAKRMPRDLAVEMVELPLAQRSKNSDVAKAMEKEGEAMLAAIGKGEQVIALDVKGKPWSTEQLAEQLASWKMSGSNFCLLIGGPDGLAPAALAQATIKWSLSPLTLPHPLVRILLIEQLYRACTILQNHPYHK | 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): 17148
Sequence Length: 155
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
O25603 | MRCVVYSIAKSSPLELVKIYQKQCRQFDCELELVDLFPKNTANAQKVSKKLAQKSYSLAFEPYLNPKAKNIALHPKAQRGDSFAFSKMLENHLNINFFIAGAYGFEENFLKDCQAWSLSEMTFSHEVAKIVLCEQIYRALSIIFKHPYHK | 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): 17331
Sequence Length: 150
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q0C5F9 | MRLQILAVGRLKDGPERDLTDDYIRRASAMARGLGFKGPEEAEIASGGGMDAEGARLLARIPEGARIIRLDEGGENLTSEAFASRLSRWRDDGERDTCFLIGGAEGYAPDVRAAAPQTLAFGVQTWPHRLVRAMLAEQLYRAMTILAGTPYHKA | 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): 16785
Sequence Length: 154
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q5QYD9 | MQIQLLAVGTKMPTWVTEGFNEYKKRFPADCKLVLHEIAAQKRTRKADLNRVMQQEGKSLLQAIPKGNRIVTLEVKGQAWDTPKLAQQLEKWQMDGRDVTLLIGGPEGLSDECLAAAEQRWSLSKLTLPHPVVRLIVAESLYRAWSLNNNHPYHRE | 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): 17797
Sequence Length: 156
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q28VG7 | MIDDYLRRFDKTGRGLGLSLGQVVEVENRKGGGMAAEADLIRARLPGGVFWVMDERGDVMTSPGFADRLGAQRDRGAGDLTMVIGGADGIDPTLRDEAGMAISFGKMVWPHMLARVMLSEQLYRAASILAGGPYHRV | 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): 14809
Sequence Length: 137
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q1IVS1 | MKLRVVWIGKTKESAIQTLTGEYLKRLSRYVATEGLEIGSEEALLKLKDRPGRTAPVLVLMDERGKQVGSEELANFLGYHRDQGVQDLIFAIGPSDGWQKETLKSATQVLSMGKMTLPHELARVVLLEQLYRGYTILTGHPYHGGH | 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): 16332
Sequence Length: 146
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
C5CFQ6 | MNLEIYLTGKVKTKFILEGVEQYLKWIRPYHKIKITSFPLAGSTSANRDQIKKKEGERYLKALQNEKNVVVLHERGEELSSMEFATFIKKWQNSGTRKLIFIIGGPLGFSDNVLSQNWKKLSLSRMTFTHEMALLVLLEQLYRAETINRGMIYHY | 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): 18115
Sequence Length: 155
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q5FMT8 | MNIKIVCVGKLKEKYFKDAIAEYQKRLSRFAKVTIVQVPDEKAPEKFSEAEDEKVKEIEGQRILSKIKDKEYVYVTAIKGKQRSSEEFAKEIQDLGTYGHSDITFVIGGSLGTSDAVNKRADDLISFGKLTMPHQLMRVVLIEQIYRAFMINSGSPYHK | 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): 18109
Sequence Length: 159
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q1G7S5 | MNIKIVCVGKLKEKYFKDGIAEYQKRLSRFAKVEIVQVPDEKAPESLSPAQMEEVKKREGERILSKIKDKEYVYVLAIKGKERASEEFAKELKNLGTYGHSDITFVIGGSLGTSDAVNKRANDLFSFGKLTMPHQLMRLVLIEQIYRAFMINSGSPYHK | 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): 18118
Sequence Length: 159
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q8EHP8 | MKLQLIAVGTRMPDWVTRGFEEYQRRFPRDMALELIEIPAGKRGKNADIVRILQKEGEQMLAAIPKGNHIVTLDLPGKNWTTPELASAMNKWQLDGRDVSLLVGGPEGLAPACKEAAHQSWCLSALTLPHPLVRIVVAESLYRAWSVNTNHPYHRE | 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): 17514
Sequence Length: 156
Subcellular Location: Cytoplasm
EC: 2.1.1.177
|
Q0VP88 | MHSDLLNSQSETLLALCRPGFEADLAAELNFHAADQMVAGYPRATANSGYVLWHSQQGSLASLQESGLIFARTLSVCEGEFSDIGDDRISALWPLLEAAGPFSELYLEHPDTNEGRELQRFLRGFRKALEPRLKKVGLLRRQAKQRLHLFFSDSHNGWVGTSPSAVPLVEGGVLRLRLPAEAPSRSALKVEEALIRFFGSADALNAKTAVDLGAAPGGWSWQLARRGIRVQAVDHGKMAPRLLDEYPVQHVYGDAFTWRPRSKVDLVVCDVVDKPARTLQHMEKWLTQGWATAALFNLKLPMKRRFQETWQLLEKLTAAMERMDHLGEPVIKAAHLYYDREEITVWASFHRSY | Function: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
Catalytic Activity: cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39698
Sequence Length: 353
Subcellular Location: Cytoplasm
EC: 2.1.1.186
|
Q0A8J8 | MTERDPIPTRHATRWLLQCRPGFGADLAAELAAWSSDAGVAGWPRVENDQGRVDFHSADGRPLPTPPALTFARQAWPVVADCPQLPERDRVGALLEALAPHLPEALAGVWLEHPDTNDGKALGRFCRKFRPHLERALRERGVALERAGAPRLHLWFADSRQVVAGLAPAGSGRPWPMGIPRLRLPRAAPSRSALKLEEAVGWLLTPVEREAALRPGMSAVDLGAAPGGWTWVLRQAGLHVTAVDNGPLAESLRADRAVRHLREDGFRYRPPHRVDWLVCDMVEQPHRVARLVRHWLVSGWCGRALFNLKLPMRRRWQCVAECRALVTGGSGELGWRSAQLYHDREEITVLAWRPAAGSRG | Function: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
Catalytic Activity: cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39961
Sequence Length: 360
Subcellular Location: Cytoplasm
EC: 2.1.1.186
|
B4RSU6 | MSDTSILAYCRPGYENDTANELTSRYGEAGFYGYPVSKKNSGFAHYHLYDAAQLEQTVTQFAVHDSIFPRQLVAVFAAINDVEKEDRVGQVLDALKEVEKPFSIFGAVDVEYPDTEEGKTLAKFCRKFTVPLRQALRKAGWLTAKENLGKPKLHIFFASFEICYIGFTLPSHASRDHLGICRLKFPSDSPSRSTLKLEDALVNMLSNKQQSKVLRSGGRAVDLGACPGGWTYQLVKRGMYVEAIDNGLIADSLMSTGLVEHHAADGFTYRPQFGRVDLLVCDMIEQPDRVAKLMGDWLVKHWATHAIFNIKLPMKRRYETVVEAMTSLNSRLDALDDAFAVKVRHLYHDRDEVTVTIVRTSKDEV | Function: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
Catalytic Activity: cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41052
Sequence Length: 365
Subcellular Location: Cytoplasm
EC: 2.1.1.186
|
B3PKB3 | MNQLFLHCRPGFEKECAAEITELAAAQGIYGYSKTKDNAAFVVFITQDERGAETLIRQLPFQSLIFVRQWFAGFGNLSDLPVTDRVSPLLEAARALPKTSDLTGETVDTNEGKALSALVKKFLLPFGKALDAHKCLDRKSPWRLHLVFLSGTEAYLGVAPVNNSSAWPMGIPRLRLPKSAPSRATLKLEEAWHHFIPAADWDRRLAPGMRAVDLGAAPGGWTWQLVQRSIYVEAIDNGPMDKDLLDSGLVTHVLADGFLFEPKKPVDWLVCDIVDKPARVSSMVIKWFSKGHCRQAIFNLKLPMKQRYMEVQKCRTRILGELGSLGMRAELDFKQLYHDREEVTGYLRVF | Function: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
Catalytic Activity: cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39342
Sequence Length: 350
Subcellular Location: Cytoplasm
EC: 2.1.1.186
|
Q1QUU9 | MAVCPHEWLLYCRPGFEKDLSAELADKTAHAGQGGYPIAARDSGHVRFVLDPETPANEVHRALPLEALVFARQSLVAFPPLEALPRDDRLSAIVDLVVASGWSFESIWQETPDTNEEKALAGLMKALRKPLESTLKKRGALRRKAGGRRLHLFWTAGDRVQLAMSFPGNRAEHLGGIPRLKFPREAPSRSTLKLEEAWHVFVPREAWPTRLSDSMQAADLGAAPGGWTYQLVRKGMYVYAIDNGPMDDALMASGQVEHLCEDGFVWQPPMRLDWLVCDIVDKPMRVIDMVERWLVAPWCHEAIFNLKLPMKKRWDEVSRCLERLASSLDQAGIRARIRCRHLYHDREEVTVHVCLLD | Function: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
Catalytic Activity: cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40425
Sequence Length: 357
Subcellular Location: Cytoplasm
EC: 2.1.1.186
|
Q47YA5 | MTSIVLFCRPGFEKECGAEIQEKAAWNEMYGYLELKINQGLVFFHLHESAHGEALMNKLPLKRLIFARQWFVTVTDKIDLPDYNRVEAITEALGNDWQYSDLRMEMADDNDGKSLSKFCRKLSVPLRQALRKNKVLTQKGNNSADDPEGAILHALFLSGQEVILGFSLARNSSPHVMGIPRLKFPSASPSRSTLKLDEAFLHFIPRDEWDERLTSGMNAVDLGSAPGGWTYQLVRRGMMVTAIDNGLMAESLMETGQVKHKMMDGFKYVPLKQNVYWLVCDMIEKPQRVAKLMSEWLLHGHCKEAMFNLKLPMKGRYQQVTNDLQTIKDAFTKHNVKYELYAKHLYYDREEVTVHARLLSPAPLRAKE | Function: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
Catalytic Activity: cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42158
Sequence Length: 368
Subcellular Location: Cytoplasm
EC: 2.1.1.186
|
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