ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
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 ... |
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 ... |
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 ... |
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 ... |
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 ... |
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 ... |
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 ... |
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 ... |
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 ... |
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 ... |
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 ... |
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 ... |
A4WRD4 | MGAMAQNPPNLRPDLAPRLVIDSPRREGQPTIGMVSLGCPKALVDSERILTRLRAEGYAISPDYAGADAVIVNTCGFLDSAKAESLEAIGEALRENGRVIVTGCLGAEPDYITGAHPKVLAVTGPHQYEQVLDAVHGAVPPAPDPFVDLLPATGVRLTPRHFSYLKISEGCNHSCRFCIIPDMRGRLVSRPERAVLREAEKLVEAGVRELLVISQDTSAYGTDWKGPVRFPILPLARELGQLGAWVRLHYVYPYPHVRELIPLMAEGLILPYLDIPFQHAHPEVLKRMARPAAAARTLDEIAAWRRDCPDITLRSTFIVG... | 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 ... |
A9WDA3 | MKYHIVTLGCPKNAVDSEGMDGLLSTQGHQAVASAEEADVIIVNTCSFIAAARAETLGVLKELAGRKRPGQRLIAAGCMAQSHPHEVAGVQGVDATLGTQQWTQINALVGQLERPVIPLTPGQPVATIPLTTTTNGQPTSYADWRTTQIRRTHQTPSAYLKISDGCNLRCAFCTIPSFKGDMRSKPVGAVLAEAQELVAGGVREIVLVAQHLTDYGRDLGLKDGLATLLAELCQVTPPETWIRLMYAYPHGISERLITTMASYPQICHYLDMPLQHAHPATLRRMRRPPDTDRTLRIIAELRAAMPDIAIRSTFIVGYPG... | 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 ... |
Q3ASP1 | MPTHSLFLLSLGCSKNTVDSERLLAQAAAAAIRSVERVDEADTILINTCAFIEDAKKESIEEMLAALDKKREGVVKQVFVMGCLPELYRRELQEELPEVDAFFGTRELPQILASLGARYRSELFDERLLLTPSHYAYLKISEGCNRICSFCSIPKIRGRYQSQPLEQLLREATRLQQQGVQELNLIAQDISLFGYDTTGHSQLNELLLRLSDMDFLWIRLLYAYPVNFPLEVIDTMRDRSNICNYLDIPLQHCNDRILRAMKRGVTKADTIRLLHEMRQRNPNIRLRTTMLVGFPGETRAEFEELLDFVEEQRFDRLGCF... | 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 ... |
Q9Z8T3 | MTTKSLGSFNSVISKNKIHFISLGCSRNLVDSEVMLGILLKAGYESTNEIEDADYLILNTCAFLKSARDEAKDYLDHLIDVKKENAKIIVTGCMTSNHKDELKPWMSHIHYLLGSGDVENILSAIESRESGEKISAKSYIEMGEVPRQLSTPKHYAYLKVAEGCRKRCAFCIIPSIKGKLRSKPLDQILKEFRILVNKSVKEIILIAQDLGDYGKDLSTDRSSQLESLLHELLKEPGDYWLRMLYLYPDEVSDGIIDLMQSNPKLLPYVDIPLQHINDRILKQMRRTTSREQILGFLEKLRAKVPQVYIRSSVIVGFPGE... | 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 ... |
Q8KCL7 | MTKTDERKPAIFLLSLGCSKNTVDSERLTAQAVASGLTFTDNVDEADIILINTCGFIKDAKQESIDETLAAIGKKEEGVVREVYVMGCLVELYRKELAEEMPEIDGLFGTRELPEVLAAIGAKYREELFDRRELLTPPHYAFLKIAEGCNRRCSFCSIPKIRGPYVSQPIEQLLREAALLQQQGVKELNLIAQDISVYGYDLYGKSALNDLTLRLSDMGFNWIRLLYAYPLNFPLEVISTMRERPNVCNYIDMPLQHINDRILKSMQRGIGRKATEQLIDDIRQKNPDIRLRTTMIAGYPGETRAEFEELLDFIRQTRFD... | 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 ... |
A6LAJ6 | MRKNKVDIITLGCSKNLVDSEQLMRQFVANGYTVEHDPHKINGEIVVVNTCGFIGDAQEESINMILELGEQKQKGRIGKLFVMGCLSERFLKDLEKELPEVDRFYGKFNWKELISDLGKSYHQELATDRVLTTPRHYAYVKIGEGCNRTCSYCSIPIITGAYQSRPMDEIVDEVRGLVAQGVKEFQMIAQDLTFYGLDRYKRMALPELVERVSDIPGVEWIRLHYGYPSHFPYDLLPVMRERDNVCKYMDIALQHISDPMLKMMRRNITKAETYELLERMRREVPGIHLRTTLMVGHPGETEQDFEELIRFVKDIRFERM... | 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 ... |
A1B3K8 | MPAMSQNPPLLRPDLAPAPIFDTSRREGQPTIGMVSLGCPKALVDSERILTRLRAEGYAISPDYKGAGAVIVNTCGFLDSAKAESLQAIGEALAENGKVIVTGCLGAEPEYITGAHPSVLAVTGPQQYEQVLDAVHHAVPPSPDPFVDLLPASGVKLTPRHYSYLKISEGCNHACKFCIIPDMRGKLVSRPAHAVIREAEKLVEAGVRELLVISQDTSAYGLDRKFATERGHRAHITDLARDLGQLGAWVRLHYVYPYPHVRDLIPLMAAHGESGGLVLPYLDIPFQHAHPDVLKRMARPAAAARTLDEIAAWRAVCPDI... | 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 ... |
Q6MBU9 | MLPILKNQGVKKDQNHIALKNDSCESSSPCFDHEGNKINFISLGCPRNLVDSEVMLGILLKAGYEVAPTLEEADYLVINTCGFLEASRQESMDTVEEVLSQRKKTAKLIVTGCMVQTHSDALKTTFPSIDYLLGSGDVEGILKAVQSTQKGQIISSARSYLEAGEVPRRLSTPKHYAYLKIAEGCRKRCAYCVIPTIKGPLKSKGKEQILKEFNLLLSQGVKEVILIAQDLGDYGKDQGAKKLTALLNLLQSMLEIKQAFWLRLLYLYPDEITDELIALMKSDSRICPYLDMPIQHVNNQILKSMRRATSKEDIIEIITK... | 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 ... |
A9BEU9 | MKKFHIVKLGCPKNDADMEIFKGLLQSKGYKYESNPQLANYIFIDTCGFIEEAKKESIETIFEYVSLKDNNKNLKVIPIGCLTQRYFDDILKDIPEIDGLYGVLSPKTIVEKIENGEYFFKRDIPETLYDCKIRAIPDSHYAYVKIGDGCSRNCAFCSIPTFKGKPKSRSIEEINEEVEFLVSKGVKEIILVSQDNTLYGIDNYQKQALPDLLDKLNNIKGKFWIRVMYLHPDFLSEEIIESIHRNEKVLNYFDVPIQHISDKILQSMGRHKKRNELIKLFEKIRKEPSAIRTTLMVGFPGEKAEDFEELVDFVKEIKFE... | 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 ... |
P36602 | MFVYKRDGRQEKVAFDKITARVSRLCYGLDSDHVDPVEITQKVISGVYPGVTTIELDNLAAETAATMTTKHPDYAILAARIAVSNLHKQTEKVFSTVVQQLHDYVNPKTDKPAPMISDKIYDIVMKHKDELDSAIIYDRDFTYNFFGFKTLERSYLLRIDGKVAERPQHMIMRVAVGIHGEDIEAAIETYNLMSQRYFTHASPTLFNAGTPRPQLSSCFLVTMKDDSIEGIYDTLKMCAMISKTAGGIGINIHNIRATGSYIAGTNGTSNGIVPMIRVYNNTARYVDQGGNKRPGAFAAYLEPWHADVMDFLELRKTHGN... | 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 (D... |
P50643 | MPPRAPRPAGAVSPPFPPLAGPPLKARAPRARDSPLTSPCRAHAAMASVVAPAASSSAAAPGADAFLDAACPEDVARALAAELEALRALGHDVGAPAPGASRREAALFITRAVDGLKAFSRVDERVYVACGKLVHLRVRSREADLDAWLASPELALIPAVAAAVRRHRARVEAALRWFWREAYPALYARGLQSALKYEEMYLARLEHGRCEAMDQFFVRLAAAAATATRRPMALVLCGSDAWPEVFDAYFRALATQAIVPATPLMLFAGRARGSLASCYLLNPLPRTTEEAVRAITDEVAPILLRRGGVGLSLQSFNRTP... | 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 Act... |
P74240 | MHPTLISAPISSSANDAHAGTSQGSHQGHRIQVIRRDGSSTPLNIGKIRAVVDWACLGLEVNSIALEAGLTTRLREGISTREIQDNLISCALEMCSPNEPDWRYVAGRLHVWSLWKDTLVRRGYQYGQYLRTVQTKVTNGEYDSRILTYSEGELQEAGCWINSDWDTDYDYAGAVLLTSRYLLPNELPQEALLTCALLLASVEAPDRRLQWARRFYESIAARRISLATPILANLRVPGGSLTSCFIVAMEDNLESIFGEITNAARISKNGGGVGVNVSRIRATGSWVMGKPNASGGVIPWTKLLNDTAIAVNQGGRRAGA... | 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
... |
O83972 | MHIIKRNGEPQPYMREKIIVAISAAFRSVQNPLAPEVPAIITDLAAEVERQLFEMNRAGVPVHVEKIQDFVEKTLTKYNHSDEVKSFILYRDDRTKKRIAREQIACCFTDSSVLGVLKEIQQDFPFPEYSLDALASKFLLFKKEVTDERRSMQLLIKAAVELTAQEAPQWELIAARLLMLDFSLALGTSLEKLNIHSFYEKITYLEEAGLYGVYIRTHYSRAEIEEAATYLECSRDKLFTYSSLDMILRRYVIRTRAHVPLETPQEMFLGIALHLAMNETQDRMQWVKRFYTVLSKLQVTVATPTLSNARKPFHQLSSCF... | 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
... |
O15909 | MLETVKLVTKRDGSVEPYDEKVVRSRIVNLMSGIDSYYVDVDDLVRVVGEGVREGMSTSMLDELLAETAAYCVTKHPDYGLLAGRLAVTALHKTTTESVLDSFRVLHEHVSQATKRHAPLISEELWDIANKHSAALQQIINYERDFDFEYFGYKTLERSYLLRVHKGRGVMEVVERPQQMFLRVALGIHGEDLERVKETYDYMSQGFFTHATPTLFNAGTPFPQMSSCFLVAMREDSIDGIYDTLKQCAIISKSAGGIGIHMHNIRAAGSYIAGTNGTSNGLVPMLRVWNNTARYVDQGGGKRKGAFAIYLEPWHADIFG... | 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 = [... |
P12848 | MFVIKRNGYKENVMFDKITSRIRKLCYGLNTDHIDPIKIAMKVIQGIYNGVTTVELDTLAAEIAATCTTQHPDYAILAARIAVSNLHKETKKLFSEVMEDLFNYVNPKNGKHSPIISSITMDIVNKYKDKLNSVIIYERDFSYNYFGFKTLEKSYLLKINNKIVERPQHMLMRVAVGIHQWDIDSAIETYNLLSEKWFTHASPTLFNAGTSRHQMSSCFLLNMIDDSIEGIYDTLKRCALISKMAGGIGLSISNIRASGSYISGTNGISNGIIPMLRVYNNTARYIDQGGNKRPGVMAIYLEPWHSDIMAFLDLKKNTGN... | 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 correspond... |
P21524 | MYVYKRDGRKEPVQFDKITARISRLCYGLDPKHIDAVKVTQRIISGVYEGVTTIELDNLAAETCAYMTTVHPDYATLAARIAISNLHKQTTKQFSKVVEDLYRYVNAATGKPAPMISDDVYNIVMENKDKLNSAIVYDRDFQYSYFGFKTLERSYLLRINGQVAERPQHLIMRVALGIHGRDIEAALETYNLMSLKYFTHASPTLFNAGTPKPQMSSCFLVAMKEDSIEGIYDTLKECALISKTAGGIGLHIHNIRSTGSYIAGTNGTSNGLIPMIRVFNNTARYVDQGGNKRPGAFALYLEPWHADIFDFIDIRKNHGK... | 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 (D... |
P50651 | MGSLKEGQGRDMEEGESEEPLLMAQNQRFTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARFLNDVQVPEARAFYGFQIAMENIHSEMYSLLLETFIKDSKEKDRLFNAIETIPCISKKAKWCLDWIQSPMSFAVRLVAFACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPLEKVYQIVHEAVEIETEFVCKALPCDLIGMNSNLMSQYIQFVADRLLVTLGCERTYKAENPFDWMEFISLQGKTNFFEKRVGEYQKA... | 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 ribon... |
Q7LG56 | MGDPERPEAAGLDQDERSSSDTNESEIKSNEEPLLRKSSRRFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRKSTFGERVVAFAAVEGVFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEERVREIIVDAVKIEQEFLTEALPVGLIGMNCILMKQYIEFVADRLLVELGFSKVFQAENPFDFMENISLEGK... | 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 ribonucleotid... |
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 subs... |
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 = ... |
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 = ... |
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 = ... |
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 = ... |
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 = ... |
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 = ... |
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 = ... |
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 = ... |
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.
Subcellu... |
P0CV50 | MRGAYYVLIALLVVASSQTSAESGHQLQVYDHDFVAADTAAATTLPRQFLRGSRNVPGDLAHEERAITSELVEEGAKLIPRAAENVEEISRVAEAVGKRPRVAEEDVLNKASGANEAFKKPRNTATDDAFQGISTEQLLPLSYKQWDTEIKSMRIPKPEKYQNNIQSVYDAFVDVCDEDLKPTISETARLWNLFDRSFKPLTTRLHQQALAQFAKEYVLRDELRLKTEWARMNERTMPNRAGMLNMKLNWHFQRWVRMYNKFGERRSELIGTPLNVARSRGGTTGASRGTALHRHSIVPLNAASTSKGKSSVFTERSQRT... | 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: Secr... |
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-ter... |
P35679 | MAAARPTVSIYSKDGSVSSETIALPFVFKAPIRPDLVRSVHTAVAKNKRQPYAVSEKAGHQTSAESWGTGRALARIPRVGGGGTHRSGQAAFGNMCRSGRMFAPTKTWRKWHVKVNQNEKRYAISSAVAASGVPSLLLARGHRIEEIPEVPLVVDDAVQSFQKTKEAVALLKEIKAYRDVVKVANSRKLRAGKGKLRNRRHVQRRGPLVVFNEDAGIVKAFRNIPGVEIVNVRRLNLLQLAPGGHLGRFVIWTKSAFGLLDSVFGSTTEAAQLKKNYFLPENIISNADVTRLINSDEIQSIVKAAGPSRVKRAHVQKKNP... | 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 t... |
Q28346 | MACARPLISVYSEKGESSGKNVTLPAVFKAPIRPDIVNFVHTNLRKNNRQPYAVSELAGHQTSAESWGTGRAVARIPRVRGGGTHRSGQGAFGNMCRGGRMFAPTKTWRRWHRRVNTTQKRYAICSALACLSLPALVMSKGHRIEEVPELPLVVEDKVEGYKKTKEAVLLLKKLKAWNDIKKVYASQRMRAGKGKMRNRRRIQRRGPCIIYNEDNGIIKAFRKHPGITLLNVSKLNILKLAPGGHVGRFCIWTESAFRKLDDLYGTWRKAASLKSNYNLPMHKMLNTDLSRILKMPRDPRALRAPRKKIHRRVLKKNPLK... | 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 | MFSKNKHNTKFIVIACVIVVLILILFCLDFQNIQEIIETINQLTNNQNPSQNTASEMSGMRRKIIFFIFNFFGKIILASFVISFLLHIKKNAQIKRLKNKLSLWSKLSFHVSQIGEEVLNELPIGIVLIDISSQEIQWLNPYASFILKNPEINSPLAQINENMAQLISTSDAIPKTIITLENKKFECFYKKDLNVFYLFDATEKEQIKHLFLQKTLALAMITFDNLAESLIRYDLSEQSQIQGEYLSALSDYIEPYEGYLKQLIDDRFLLLLNRQNLDKMLENKFIILDTIRNISYKYQLKVTLSMGIACWNLSYEKLAT... | 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 | MEYHPQAIRLCALIFISFYALLHLVEAQDQKGFISLDCGSLPNEPPYNDPSTGLTYSTDDGFVQSGKTGRIQKAFESIFSKPSLKLRYFPDGFRNCYTLNVTQDTNYLIKAVFVYGNYDGLNNPPSFDLYLGPNLWVTVDMNGRTNGTIQEIIHKTISKSLQVCLVKTGTSSPMINTLELRPLKNNTYNTQSGSLKYFFRYYFSGSGQNIRYPDDVNDRKWYPFFDAKEWTELTTNLNINSSNGYAPPEVVMASASTPISTFGTWNFSWLLPSSTTQFYVYMHFAEIQTLRSLDTREFKVTLNGKLAYERYSPKTLATET... | 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-[p... |
F4I2N7 | MAPSLRNFNFFHRFSTFLVFSLFSVVSSDDLQVLLKLKSSFADSNLAVFDSWKLNSGIGPCSFIGVTCNSRGNVTEIDLSRRGLSGNFPFDSVCEIQSLEKLSLGFNSLSGIIPSDLKNCTSLKYLDLGNNLFSGAFPEFSSLNQLQFLYLNNSAFSGVFPWKSLRNATSLVVLSLGDNPFDATADFPVEVVSLKKLSWLYLSNCSIAGKIPPAIGDLTELRNLEISDSGLTGEIPSEISKLTNLWQLELYNNSLTGKLPTGFGNLKNLTYLDASTNLLQGDLSELRSLTNLVSLQMFENEFSGEIPLEFGEFKDLVNLS... | 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 contro... |
Q9LVI6 | MRLFFTPSMSNLSIFFSILLLSLPLPSIGDLAADKSALLSFRSAVGGRTLLWDVKQTSPCNWTGVLCDGGRVTALRLPGETLSGHIPEGIFGNLTQLRTLSLRLNGLTGSLPLDLGSCSDLRRLYLQGNRFSGEIPEVLFSLSNLVRLNLAENEFSGEISSGFKNLTRLKTLYLENNKLSGSLLDLDLSLDQFNVSNNLLNGSIPKSLQKFDSDSFVGTSLCGKPLVVCSNEGTVPSQPISVGNIPGTVEGSEEKKKRKKLSGGAIAGIVIGCVVGLSLIVMILMVLFRKKGNERTRAIDLATIKHHEVEIPGEKAAVEA... | 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 | MLGPVLRLVVKAGKERKLRNFYPNLYRDEIAAPPEGVGVAEAVDAEGHFLAVGYYDPRSRVPFRAFRFDPGPLNRAFFQGRFARALRRRQGLGESHRLVHGEADGLPGLVVDRFGEVLVLQVRSRGMEALREVWLPALLEVVAPKGVYERSDVEARRQEGLPERVGVVYGEVPEVLEVEEDGLRFPIPLALAQKTGYYLDQRENRRLFEAMVRPGERVLDVYSYVGGFALRAARKGAYALAVDKDLEALGVLDQAALRLGLRVDIRHGEALPTLRGLEGPFHHVLLDPPTLVKRPEELPAMKRHLVDLVREALRLLAEEG... | 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 | MASSSSSASRTWRYRVFTSFHGSDVRTSFLSHFRKQFNNNGITMFDDQRILRGETISPALTQAIRESRISIVLLSKNYASSGWCLDELLEILKCKDDMGQIVMTVFYGVDPSDVRKQTGEFGIAFNETCACRTEEERQKWSQALNYVGNIAGEHLLNWDNEAKMIEKIARDVSEKLNVTPCRDFDGMVGIEAHLRKIQSLLDLDNDEVKMVAISGPAGIGKSTIGRALHSLLSNRFHHTCFVDNLRGSHPIGLDEYGLKLRLQEQLLSKILNQDGSRICHLGAIKERLCDMKVFIILDDVNDVKQLEALANESNWFGPGS... | 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-ass... |
Q9CAK1 | MASPSSFSSQNYKFNVFASFHGPDVRKTLLSHIRLQFNRNGITMFDDQKIVRSATIGPSLVEAIKESRISIVILSKKYASSSWCLDELVEILECKKAMGQIVMTIFYGVDPSDVRKQIGKFGIAFNETCARKTEEERQKWSKALNQVSNIAGEDFLRWDNEAIMIEKIARDVLDKLNATPSRDFDGMVGIEAHLREIKSLLDLDNVEVKIVAIAGPAGIGKTTIARALYGLLSKRFQLSCFVDNLRGSYHSGFDEYGFKLHLQEQFLSKVLNQSGMRICHLGAIKENLSDQRVLIILDDVNKLKQLEALANETTWFGPGS... | 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-as... |
Q12224 | MGRRKIEIQRISDDRNRAVTFIKRKAGLFKKAHELSVLCQVDIAVIILGSNNTFYEFSSVDTNDLIYHYQNDKNLLHEVKDPSDYGDFHKSASVNINQDLLRSSMSNKPSKSNVKGMNQSENDDDENNDEDDDDHGNFERNSNMHSNKKASDKNIPSAHMKLLSPTALISKMDGSEQNKRHPENALPPLQHLKRLKPDPLQISRTPQQQQQQNISRPYHSSMYNLNQPSSSSSSPSTMDFPKLPSFQNSSFNGRPPPISISPNKFSKPFTNASSRTPKQEHKINNSGSNNNDNSNYTQSPSNSLEDSIQQTVKARRKLSA... | 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): ... |
Q9FT77 | MKSSSSQSYDVFPNFRGEDVRHSLVSHLRKELDRKFINTFNDNRIERSRKITPELLLAIENSRISLVVFSKNYASSTWCLDELVKIQECYEKLDQMVIPIFYKVDPSHVRKQTGEFGMVFGETCKGRTENEKRKWMRALAEVAHLAGEDLRNWRSEAEMLENIAKDVSNKLFPPSNNFSDFVGIEAHIEALISMLRFDSKKARMIGICGPSETGKTTIGRALYSRLKSDFHHRAFVAYKRKIRSDYDQKLYWEEQFLSEILCQKDIKIEECGAVEQRLKHTKVLIVLDDVDDIELLKTLVGRIRWFGSESKIVVITQKRE... | 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(... |
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 Len... |
Q4WX78 | MGRRKIEIKAIKDDRNRSVTFLKRKGGLFKKAHELAVLCSVDVAVIIFGHNKKLYEFSSCDMRETLGRYQYYGPPHEHKGPEDFNGKRDDDDDEDETTPAPEEMQPTTQNPPAVVPAHIPSHPGFQHVNHAPSASPPISNGIPFDPRHGTPQPQGASRPSSRNHLRRVSSNLGPQQHHGTPPPPPQNGFAYIPNPSMYHPNANPNIAQQPRPPQFAHYGPQQPLPPHAIPPHPMPQPVPPHHQAPQHLPQHPHPLAQQTPAMGLSQPPHASIPQVAQPFLPEQGRNSIPPAFPTEQSQPPRPVSLPDVSSADQMVGPLKV... | 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, gliotoxi... |
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 | MARSRSRIDRTPFQTEILDLSHDGRGVARREGEGGKVTFVSGALPGEVVMAEQTARSRHFDEARTVEVLKASPQRVTPKCPHFGTCAGCVLQHLDEDQQIVAKQRVLMDNLERIGHVKPGTVLAPLVGESWGYRRKGRFSVRRVEKKDKTLVGFREQDPRFVADLSQCLTVIPEIGTKVEALSTFIESLDGKRDIPQIEFIAGDQAVVLTVRHLQPLSDADRAAWATFGQQHGFVIYLQSGGVDTVQPLDGQGVPLSFRLAPWDVELAFRPLDFIQVNAKLNEKMIAHALDLLEPGEDERVLDLFCGLGNFTLPLARRVR... | 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 | MVQFFQPKPKALPTQAVEITIDNLDHHLTGVGRYQGKACFVEGVLPGEKVSVQITEQKKQYAHARLRQVIEPSADRCEPFCPAFKQCGGCNAQMMPQAMQCQAKQQGVQRLFRQLAKIDLPAPLWIESSAPQAYRRVCRLAVKYDKNKRCVLVGFRQKQSQALVEINSCPVLTAALSALIVPLRTLINELSSARDVGHIELYETESGLAMLLRHNGRPPVKDKELLLAFALQHDCALYLQTTGYPEPLADVKPSFYQLDGLRLYFQPGDFLQVNPQVNQRLVNYVREWLAPTATDNVLDLFCGIGNFTLPLAREAASVTG... | 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
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A5CXB2 | MRRRRKLEHKTYKLNIESFSHEGRGIAHFEDKIIFVSDALPGELVIANRTFSCAKFEEADAKEILKPADNRMKPKCDVFGICGGCSFQNLSSEDQIQIKSRWLKKVFARQAKVEPETWLKSLQFQSWGYRRKARLGIRYVAKKDKVLIGFRERKSSFITNMSRCEVLHPSIGEHLEVLANCIERLSIKSSIPQFEVVISESGIALILRHLESLSVKDEKILADCAQELNITFYTQSGGLDSVKPLDEPTILTYSHSNYNIIMEFLPTDFVQVNFKLNQQMVSLAVELLELNESDKVIDLFCGLGNFTLPIARYAKYVVGI... | 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
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Q7MHP7 | MARFFQPKKKLQPESKHQQVLVEKLDHQGAGIAYLNKKPLFIDGTLPGEEVVTQLTESKSKFARGKLIKLLKPAAERVEPFCSHFNQCGGCDMQHMDYQAQLAYKQRTLLQLMKKFSGSEILLSPPVTGLEKAYRRRARVSLMWDKKSRQLQFGFRRKQSKQIENVTQCPVLVAELECLLPELKAILSHFHHPEHLGHVELVAADNGAVITLRHTGPLLDEDVAKLRQCAEQHQATLYLMPASDQLERISGEAPYYQEIGFKVPFEPNNFIQVNQKVNQQMVVQALEWLDPQSSDRVLDLFCGLGNFSLPIASKAKSVTG... | 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
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Q8PMU6 | MARTRNRLDRTPFQTAVTDLSHDGRGVARRDGEGGKVTFISGALPGELVRAEPTARSRHFDEAKTVGVLEASPQRVTPRCPHFGVCAGCVLQHLEESQQIVAKQRVLMDNLERIGHVTPQAVLPALTGDNWGYRRKGRFSVRRVEKKDKTLVGFRELDPRFVADLSVCYTVIPQIGEKIPLLAALIEGMDGKRDIPQIEFIAGDDAVALTIRHMQPLSERDRQAWITFAQEHGFAIFLQPGGVDSVQPLWPQEVPLSFRLPQWDVELAFRPLDFIQVNASLNQKMIAHAVALLEAKPDDRVLDLFCGLGNFTLPLARVVR... | 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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
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)... |
B2VDD5 | MSQLELSNRMLTLHRFPQMREESPLQAWDAADEYLLNHLDNLPVNGPTLIFNDTFGALACALAGEGVWSISDSWLNQQATRQNLALNQLDEGDVRLLDSLAPLPGAPARVLIKVPKTLALLEKQLRALRAVVTPETQIVAAGKAKEIHTSTLQLFEKILGPTTTSLAWKKARLIYATFTQPELAESEVISRWPLDGTPWQIHNHANVFARGGLDIGARFFMQHLPDDIDGEIVDLGCGNGVIGLMALRQNPLAQVHFLDESYMAVASSRMNVELNCPDDLARCEFRVNNALAGYPSDRLHAVLCNPPFHQQNAVTDHIAW... | 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... |
A0L9S5 | MQHLNIHGHTLTLRRFPHKPGCPLQAWDAADALALTNHALPDGEILILNDHFGALACGLAYPERTLEWVNDSYMAHQALAQNLQLNRIETPLHRTPALAASPTNPVGILIKLPRMLQLLSSQLDWLNLHLPKGTPVVIAARQKDMPSTLPDLTRRLLDDVHPSRAEKKARLIFGQLSGRQSGQAEITAWHCAELDCLLSHYPNVFGRQKLDLGARVLLQNLGTIPDQVVDLGCGNGVLSIAALQRNPNSHVLAVDESWQATRSCQINLERVRTPEHFKVVWGHSLSFIEGMQADLVLCNPPFHQHQTLTDDIAWCMFKDA... | 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... |
Q48DT7 | MPLLISPFAELDLIRQPEQQDEPLQAFDAADEYLLNHVAETGLSLQSRVLVLNDSFGALAASLASHATVVSSTDSFLAAQGLEKNLARNGMSYDAVPHIPASEPLSGPFDWVLIRVPKTLALLEEQLIRLQGQLAPGARVVAAAMVKHLPRSAGDLLEEYVGPVQASLAVKKARLLFATPQPMEVRTSPYPTRYRLDEPAIELLNHANVFCRDGLDIGTRAFLPYLPKNLGTARVADLGCGNGVLAIASALDNPQAHYTLVDESFMAVQSAAENWRATLGERVVEVRAADGLDTQEPDSLDVVLCNPPFHQQQVVGDFLA... | 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... |
Q15YR1 | MKTELTLLDHSYELLRYPAENQHVSWQAWDSADEYLMEYVAQNITDLNGLNIHIYNDDFGALGVWFATNNAPLWISDSFVAHKALALNLERNHLPIENVNVQNSLYKANQKADLVLIKVPKTLALLEQQLIDLQSSVTPETRIIAAGKANAIQKSTLALFEKHLGLTTTSLAKKKSRLIFCQYDGVKQSVSPYPTKWKTDNTQFIMSNLANVFSRQQLDIGARVLLAHLPDANHKCIVDLGCGNGVLGLHVLHKSPGAHVIFVDESFMAIASAKMNIEQNMPDKLDQCKFIVSNCLDECLSSGENEATVDIVLCNPPFHQ... | 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... |
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:... |
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:... |
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:... |
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:... |
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:... |
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:... |
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:... |
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:... |
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:... |
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:... |
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:... |
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:... |
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:... |
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:... |
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:... |
Q0VP88 | MHSDLLNSQSETLLALCRPGFEADLAAELNFHAADQMVAGYPRATANSGYVLWHSQQGSLASLQESGLIFARTLSVCEGEFSDIGDDRISALWPLLEAAGPFSELYLEHPDTNEGRELQRFLRGFRKALEPRLKKVGLLRRQAKQRLHLFFSDSHNGWVGTSPSAVPLVEGGVLRLRLPAEAPSRSALKVEEALIRFFGSADALNAKTAVDLGAAPGGWSWQLARRGIRVQAVDHGKMAPRLLDEYPVQHVYGDAFTWRPRSKVDLVVCDVVDKPARTLQHMEKWLTQGWATAALFNLKLPMKRRFQETWQLLEKLTAAM... | 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 | MTERDPIPTRHATRWLLQCRPGFGADLAAELAAWSSDAGVAGWPRVENDQGRVDFHSADGRPLPTPPALTFARQAWPVVADCPQLPERDRVGALLEALAPHLPEALAGVWLEHPDTNDGKALGRFCRKFRPHLERALRERGVALERAGAPRLHLWFADSRQVVAGLAPAGSGRPWPMGIPRLRLPRAAPSRSALKLEEAVGWLLTPVEREAALRPGMSAVDLGAAPGGWTWVLRQAGLHVTAVDNGPLAESLRADRAVRHLREDGFRYRPPHRVDWLVCDMVEQPHRVARLVRHWLVSGWCGRALFNLKLPMRRRWQCVA... | 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 | MSDTSILAYCRPGYENDTANELTSRYGEAGFYGYPVSKKNSGFAHYHLYDAAQLEQTVTQFAVHDSIFPRQLVAVFAAINDVEKEDRVGQVLDALKEVEKPFSIFGAVDVEYPDTEEGKTLAKFCRKFTVPLRQALRKAGWLTAKENLGKPKLHIFFASFEICYIGFTLPSHASRDHLGICRLKFPSDSPSRSTLKLEDALVNMLSNKQQSKVLRSGGRAVDLGACPGGWTYQLVKRGMYVEAIDNGLIADSLMSTGLVEHHAADGFTYRPQFGRVDLLVCDMIEQPDRVAKLMGDWLVKHWATHAIFNIKLPMKRRYET... | 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 | MNQLFLHCRPGFEKECAAEITELAAAQGIYGYSKTKDNAAFVVFITQDERGAETLIRQLPFQSLIFVRQWFAGFGNLSDLPVTDRVSPLLEAARALPKTSDLTGETVDTNEGKALSALVKKFLLPFGKALDAHKCLDRKSPWRLHLVFLSGTEAYLGVAPVNNSSAWPMGIPRLRLPKSAPSRATLKLEEAWHHFIPAADWDRRLAPGMRAVDLGAAPGGWTWQLVQRSIYVEAIDNGPMDKDLLDSGLVTHVLADGFLFEPKKPVDWLVCDIVDKPARVSSMVIKWFSKGHCRQAIFNLKLPMKQRYMEVQKCRTRILG... | 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 | MAVCPHEWLLYCRPGFEKDLSAELADKTAHAGQGGYPIAARDSGHVRFVLDPETPANEVHRALPLEALVFARQSLVAFPPLEALPRDDRLSAIVDLVVASGWSFESIWQETPDTNEEKALAGLMKALRKPLESTLKKRGALRRKAGGRRLHLFWTAGDRVQLAMSFPGNRAEHLGGIPRLKFPREAPSRSTLKLEEAWHVFVPREAWPTRLSDSMQAADLGAAPGGWTYQLVRKGMYVYAIDNGPMDDALMASGQVEHLCEDGFVWQPPMRLDWLVCDIVDKPMRVIDMVERWLVAPWCHEAIFNLKLPMKKRWDEVSRC... | 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
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Q47YA5 | MTSIVLFCRPGFEKECGAEIQEKAAWNEMYGYLELKINQGLVFFHLHESAHGEALMNKLPLKRLIFARQWFVTVTDKIDLPDYNRVEAITEALGNDWQYSDLRMEMADDNDGKSLSKFCRKLSVPLRQALRKNKVLTQKGNNSADDPEGAILHALFLSGQEVILGFSLARNSSPHVMGIPRLKFPSASPSRSTLKLDEAFLHFIPRDEWDERLTSGMNAVDLGSAPGGWTYQLVRRGMMVTAIDNGLMAESLMETGQVKHKMMDGFKYVPLKQNVYWLVCDMIEKPQRVAKLMSEWLLHGHCKEAMFNLKLPMKGRYQQV... | 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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