ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B3DYX1 | METSLSGIRVGMISLGCSKNLVDSEIMLGKLLEAGAVLTASPHQADILLINTCGFILPAKKESIDTILAAIHRRTTTSKKQKIVVSGCLYQRYGKELSALLPEVDLFLGLDDIPKIDLYVKQLIDTPPSSKEMPALNFSPRFIPDFEHPRLKLTPSHFGYLKIAEGCNHPCTFCIIPRIRGRYRSRTIQNVVAEAEAMIRRGTKEIILVSQDTTFYGRDLSNGQSSLLVDLLDSLETLEGDFWIRLLYTHPAHWNASLIEKFSTSKKIAKYIDIPIQHISNPVLERMQRKTEESYIRELLAEMRTKIKNAAIRTTLIVGF... | 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 ... |
Q2RJK1 | MIRVAVITLGCPKNQVESEYMLGILEKNHLEVVSDPRQAEVVIINTCSFITAAREEALDTILELARAANHPRLIVAGCLAQQYASELWQELPEAAAFIGPGATGRLPEIINRVLKGERVLDVPGPEMITGELPRLIEDGKPFAYLKIAEGCNNRCTYCTIPSIKGPYRSRPLEKVVAEAVSLAARGIKELVLVAQDTTAYGLDCYGEYRLPELLRRLARIEGIEWVRLLYAYPTRITPELIEVMATEPGVVPYLDLPLQHASEGVLRRMGRPGTGAAGLRAIESLRRAIPEITIRSTFIVGFPGEEEEDFQILLDFLTDA... | 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 ... |
Q1DC90 | METTTPKSLYMMTLGCPKNRVDSEVMLGTLRHRGYTLVQEASDAQVIVVNTCAFIGPAKQESVDSILEMAELKKSGACKTLVVTGCLSQRYGEELSKEMPEVDHFLGTSAYAQIGDLLAAEASPRQVIPDPDYIHDANTPRINSMPKYTAYLKISEGCDNACAFCIIPTLRGGQRSRPIDDIVAEAKQLADSGVQELNLVAQDLTAYGHDLPGRPKLHDLLKALVQVDVKWIRLHYAYPRIFPDELIEVMASEPKIARYLDMPVQHVSDKLLLSMKRGRNSEFLKGLLTKLRERVPGLVMRTSLIVGLPGETEEDFEMLK... | 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 ... |
B2A3C0 | MKVGIISLGCAKNQVDTEVMQGILENSNYKMTDDYYDADIIIVNTCGFIDDAKEESVDHILEVAQLKETGKLKVLIVAGCLSQRYQESLKEEIPEIDAMIGTDTQDKITEVISSALKGNYISFYDRLNKIDEQLFLRQPYQPGPSAYIKIAEGCHNYCSYCAIPLIRGGYRSRTIEDIKIEANHFIEKGSKELTLIAQDTTNYGSDIYGKFSLDTLLDELATIPGDFWIRVLYAYPTRITDSLIEVINRHEKICSYLDIPLQHIDDDILTSMNRGGNKEQILNLIHNLRKNIPDITLRTSLIVGFPGETDEKYQNLISFM... | 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 ... |
Q315T9 | MISVYSISLGCPKNRVDTEWLLGVLGPEVRPVREMADADLVLINTCGFIAPAVEESVRTVVEAVAELEDLPRRPLLAVAGCLVGRYGRQDLAAELPEVDLWLTNRDMDAWPEMIGRALGVAVHVPPVRLLSTGPSYAYLKVSDGCGHNCSFCTIPSIRGGLVSTPADVLEAEAVNLLSRGVKELIFVAQDVAAYGRDMGLRHGLRSLLDRLLPLDGLERLRLMYLYPAGLDAGLLRYLRDAGKPFVPYFDIPVQHAHPDVLSRMGRPFARNPREVVDRVRDVFPEAALRTSIIVGFPGETQQHYDHLTRFVQDVRFMHLG... | 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 ... |
B1ZW93 | MIKVSLISLGCAKNLVDSEIMVGHLHQAGMAVIPEAEKADVVIVNTCSFIDSSKEESIGHILEVHQHRGLRKRRKEQKLIVAGCMSQRFSKDLSSSLHDEVDAFIGLDQVTKVAPIIQEIYARERTKTDDPVSFVEGRSTFIPDYDTPRFRLTPKHFAYVKIAEGCNHPCTFCIIPQIRGRHRSRTVESVVAEVRQLVREGVKEINLISQDTTFFGMDTWEQRPNPRTPVDSGRGTALTTLLRQLNAIEGDFWIRLLYTHPAHWSDELIRTIAECPKVARYIDIPLQHISDAMLSRMQRETSGGYIRDLIARIRAGIPGI... | 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 ... |
Q06587 | MTTPANAQNASKTWELSLYELHRTPQEAIMDGTEIAVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCSDCIVTALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSREEYEAHQDRVLIRLSRLHNQQALSSSIEEGLRMQAMHRAQRVRRPIPGSDQTTTMSGGEGEPGEGEGDGEDVSSDSAPDSAPGPAPKRPRGGGAGGSSVGTGGGGTGGVGGGAGSEDSGDRGGTLGGGTLGPPSPPGAPSPPEPGGEIELVFRPHPLLVEKGEYCQTRYVKTTGNATVDHLSKYLALRIALERRQQQEAGEPGGPG... | Function: Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inac... |
Q99496 | MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAMAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWK... | Function: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation . H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. M... |
Q9CQJ4 | MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAVAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWK... | Function: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation . H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals . ... |
Q4KLY4 | MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAVAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVSICQ | Function: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Ma... |
Q8LE94 | MGCVSSCFRVEDIDEYMNPNSSVYRNCPCIRCLAHNFLNLYISVFRRGETRSLPSSVQATASITSSSSHDNFLSEAFRSTPRPLPYDADPRYFRSLVSRREKGSSHSHEEVEPLRSDSDADSESFGVGGCKWANNKSTLSDKDSKEEYSSKSSLRILRSRSKSIMADSENMYILSEDEDVCPTCLEEYTSENPKIVTKCSHHFHLSCIYEWMERSENCPVCGKVMEFNETP | Function: Mediates E2-dependent protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 26258
Sequence Length: 231
Domain: The R... |
Q93Z92 | MSSSSSTTTNTTTESDSSSLPTHIGRSNSDGIIDTTPFLPPTVTRTISVDEESNPIHRSARRQGLREAARFLRHAGSRRMMREPSMLVRETAAEQLEERQSDWAYSKPVVFLDILWNLAFVAIGVAVLILSRDEKPNMPLRVWVVGYGIQCWLHMACVCVEYRRRRRRRHPEDGGGSGLTNSSSQQYVSLAQLEDRGETSNPAKHLESANTMFSFIWWIIGFYWVSAGGQTLSSDSPQLYWLCIIFLGFDVFFVVFCVALACVIGLAVCCCLPCIIAILYAVADQEGASKNDIDQMPKFRFTKTGNVEKLSGKARGIMTE... | Function: Mediates E2-dependent protein ubiquitination in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Location Topology: Multi-pass membrane protein
Sequ... |
P13489 | MSLDIQSLDIQCEELSDARWAELLPLLQQCQVVRLDDCGLTEARCKDISSALRVNPALAELNLRSNELGDVGVHCVLQGLQTPSCKIQKLSLQNCCLTGAGCGVLSSTLRTLPTLQELHLSDNLLGDAGLQLLCEGLLDPQCRLEKLQLEYCSLSAASCEPLASVLRAKPDFKELTVSNNDINEAGVRVLCQGLKDSPCQLEALKLESCGVTSDNCRDLCGIVASKASLRELALGSNKLGDVGMAELCPGLLHPSSRLRTLWIWECGITAKGCGDLCRVLRAKESLKELSLAGNELGDEGARLLCETLLEPGCQLESLWV... | Function: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 49973
Sequence Length: 461
Domain: The LRR domain forms a horseshoe-shaped structure that interacts tightly with target RNases via a large protein interaction... |
Q9LSD0 | MPSMPEEPLLTPTPDRFCMFPIHYPQIWEMYKKAEASFWTAEEVDLSQDNRDWENSLNDGERHFIKHVLAFFAASDGIVLENLASRFMSDVQVSEARAFYGFQIAIENIHSEMYSLLLDTYIKDNKERDHLFRAIETIPCVAKKAQWAMKWIDGSQTFAERIIAFACVEGIFFSGSFCSIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYTLLKTKLSEERVKSIVCDAVEIEREFVCDALPCALVGMNRDLMSQYIEFVADRLLGALGYGKVYGVTNPFDWMELISLQGKTNFFEKRVGDYQKASVMSSVNGNGA... | Cofactor: Binds 2 iron ions per subunit.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Involved in DNA damage repair and programmed cell death inhibition.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyr... |
A0QPD3 | MTRTHFDSIRAGGLNWSSLPLKLFAGGNAKFWDPADIDFSRDRADWEALTEREREYATRLCAEFIAGEEAVTKDIQPFMSAMRAEGRLGDEMYLTQFAFEEAKHTQVFRMWLDAVGVTDDLHSLIEEVPAYVQIFCEELPAALEALTSDPSPAAQVRASVVYNHVVEGMLALTGYYAWHRICVDRGILPGMQELVRRIGDDERRHMAWGTFTCRRHVAADDANWAVFETHMNELIPVALRLTQEGFALYGDDIPFGLEEGEFLQYSSDRGMRRFGTISSARGRPLAEIDVDYTPLQLEDTFADEDERALTAVKAAAAAAN | Cofactor: Binds 1 Fe cation per subunit.
Function: Probable oxidase that might be involved in lipid metabolism.
Sequence Mass (Da): 35999
Sequence Length: 320
EC: 1.-.-.-
|
Q0S392 | MSTLTPGRPYAPGRQGFSSLRAGGLNWDAFPLRLFTKGNAKFWNPTDLDFSRDAEDWEGLNSEQQRNSTYLVAQFIAGEEAVTEDIQPFMKAMAAEGRFGDEMYLTQFCFEEAKHTQVFRLWMDAVGLTRDLHPFVAENPYYRQLFYEELPGSLKVLETDPSPVNQVRASVTYNHVIEGSLALTGYYAWQKVCTTRGILPGMQELVRRIGDDERRHMAWGTFTCRRHVAADDSNWGVVQERMAELMPLALGMIDWVNKQFEVQPYGLDDQEFIAYAADRAQRRLGAIESARGRPVEEIDLDYSPEALEEKFGEEDAKAMS... | Cofactor: Binds 1 Fe cation per subunit.
Function: Probable oxidase.
Sequence Mass (Da): 36810
Sequence Length: 324
EC: 1.-.-.-
|
Q01993 | MFTGIIESIGNIGAIIRHNEDLSIVVNTNNLDISDVNIGDSIATNGVCLTVSKLLPSGYTADLSLETYKRTAFHSYRIGQEVNLEKAMLPTTRLGGHLVSGHVDGVGEVIEFKRNGRAINIWVAVPVQLKKYLSEKGSVTIDGISLTINAVYQNVIKLTIVPHTLAETNLVNINIDKKVNVEIDMMARYLEKLIKVDRYESEKTSNVSMDLERYGFIS | Function: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
Catalytic Activity: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-ribitylamino)uracil + riboflavin
Sequence Mass (Da): 24095
Sequence Leng... |
P51961 | MFTGIIEAVGNISAITSKGSDFEVSVNCDTLDLADVKIGDSIATNGICLTVVKLTANSYVADLSIETLSRTAFNYYKVGQAVNLEKAMLPTTRFGGHIVSGHVDAVAEVIECRTSGRAIDIWIRVPSQIEKYLSEKGSVTVDGVSLTVNAVTGNEFKLTIVPHTVVETTIADFKVGNKVNIEVDVLARYIERLLLVDKPEDKQSKISMDLLERNGFLL | Function: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
Catalytic Activity: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-ribitylamino)uracil + riboflavin
Sequence Mass (Da): 23639
Sequence Leng... |
A5DB51 | MFTGLVEHIGTVLQVTEKDTTASGGDGVSMVIGDCSKILEDVQLGDSICTNGVCLTVTEFDMARSQFKVGISPETLRRSDLGELKPGSKVNLERAVKADVRMGGHVVQGHVDTIATIVNRRGDGNAINFTFKLRDSQYGKYIVEKGFIAIDGTSLTVTDVDHEQSEFSISMVSYTQEKVIMPLKNSGDSVNIEVDLTGKLIEKQIELSLLSYIKDETSPLSTLIGKLVEKKVDDVLKRN | Function: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
Catalytic Activity: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-ribitylamino)uracil + riboflavin
Sequence Mass (Da): 26044
Sequence Leng... |
Q9Y7P0 | MFTGLVEAIGVVKDVQGTIDNGFAMKIEAPQILDDCHTGDSIAVNGTCLTVTDFDRYHFTVGIAPESLRLTNLGQCKAGDPVNLERAVLSSTRMGGHFVQGHVDTVAEIVEKKQDGEAIDFTFRPRDPFVLKYIVYKGYIALDGTSLTITHVDDSTFSIMMISYTQSKVIMAKKNVGDLVNVEVDQIGKYTEKLVEAHIADWIKKTQA | Function: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
Catalytic Activity: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-ribitylamino)uracil + riboflavin
Sequence Mass (Da): 22861
Sequence Leng... |
P38145 | MFTGIVECMGTVLENNPYDDSESGGQGVSITIGNAGSILTDCHVGDSIAVNGVCLTVTEFNNDSFKVGISPETIKRSNVASWIQGTQVNLERAVSQDVRFGGHYVQGHVDTVANIVSRRPEGNSIIFGFQLRDQEYFKYIVEKGFICIDGTSLTIIKVDPLSQGGAFYISMIKHTQDNVIMPLKKIGDEVNIEVDLTGKIIEKQILLTLENQISKKDSTLNTMISNIIEEKVRNYLNK | Function: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
Catalytic Activity: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-ribitylamino)uracil + riboflavin
Sequence Mass (Da): 26196
Sequence Leng... |
Q89K80 | MADARRAPLKDQTDISGARALIVEARFYDDLQDALLDGAVAELKAAGLTHDVITVPGALEIPAAVAIAVDAAAANGKPYDAVIALGCVIRGDTIHFEIVSQESSRALMDLAVSRKLPLGNGILTVNTEAQAWARARASELNKGGDAARAALAMLRIKRRLARA | 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 = ... |
Q2YNC6 | MEFLMSKHEADAPHLLIVEARFYDDLADALLDGAKAALDEAGATYDVVTVPGALEIPATISFALDGADNGGTEYDGFVALGTVIRGETYHFDIVSNESCRALTDLSVEESIAIGNGILTVENEEQAWVHARREDKDKGGFAARAALTMIGLRKKFGA | 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 = ... |
Q9A9S4 | MTDPVPPRIAIVVSQFNPEVTDGLLKGALDHLAAQGAPVAAPDIIAAPGAYELPLIAQTLARTGRYAGVVCLGCVIKGETAHFEFISLGASLGLMAAGLQTETPVSFGVLTTYTDEQAVARSRDDAENKGREAANACLSTVQTLRRIRENALA | 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 = ... |
Q889Q6 | MTLKTIEGTFIAPQGRYALVVGRFNSFVVESLVSGAVDALVRHGVSESDITIIRAPGAFEIPLVVQKVAQRSEFAAIVALGAVIRGGTPHFEYVAGECVKGLSQVSMEFGVPVAFGVLTVDSIEQAIERSGTKAGNKGAEAALSAIEMVSLLSQLEAK | 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 = ... |
Q92QU0 | MAKIKPVHILIVEARFYDDMADAMLDGAKHALDAAGATYDIVTVPGALEIPAAIAMALDGADEGGAEYDGFVALGMVIRGETYHFDIVANESARALMDLAVSESLALGNGILTVENDEQAWARARRTEGDKGGFAARAALTMIELKQRLGAEK | 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 = ... |
Q89DI7 | MDPPAIEHPRFAKPQRVAFVQACWHRDVVEEARIAFMKEAEARHLTHVDVFEVPGSFEIPLHAQILAKTRRYTAIVAAGLVVDGGIYRHEFVADTVIKALMDVQLRTEVPVFSAVLTPQQFHETEVHYDFFRRHFAIKGVEVAEACANTLLGLERLRGQVAAGIA | 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 = ... |
Q2YKV1 | MNQSCPNKTSFKIAFIQARWHADIVDEARKSFVAELAAKTGGSVEVEIFDVPGAYEIPLHAKTLARTGRYAAIVGAAFVIDGGIYRHDFVATAVINGMMQVQLETEVPVLSVVLTPHHFHESKEHHDFFHAHFKVKGVEAAHAALQIVSERSRIAALV | 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. The isozyme RibH2 but not RibH1 is essential for Brucella intracellular survival and replica... |
A6H143 | MATANKNLSNYDKNTIPNAKNFRFGIVISEWNDHITEGLYSGVIEALTDCGALHKNIIRWNVPGSFELIYGAKKMIETQKPDVVITIGCVIKGETMHFEFVCEGVTQGIKDLNVLSDIPTIFCLLTDNTEQQSIDRSGGTHGNKGTEAAIAAIKMAYLREQANLGFHQSDKLLKTNQLQIEGLPLKIQE | 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 = ... |
Q8RIR4 | MKVFEGKFNGKGTKIAIVAARFNEFITSKLIGGAEDILKRHEVQDDDINLFWVPGAFEIPLIAKKLAQSKKYDAVITLGAVIKGSTPHFDYVCAEVSKGVAHVSLESEVPVIFGVLTTNSIEEAIERAGTKAGNKGADAAMTAIEMINLIKGI | 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 = ... |
C1A8F6 | MAEFSGEPRGEGRRIVVVASRFNEGVTVPLAEGAVSALVGKGVAFDNIDVLWVPGAWELPVAVRRALSSERYDAAVAVGAVIRGDTPHFDIVAGETARGLMEASRDFDVPVTLGLLTTDTLEQAEARAGGVHGNKGADAALAALEVLDLFDRALPANDYDEDGE | 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 = ... |
Q1GNT5 | MAHVLIVEARFYSHLNDMLLDGVRSALDAEGHSHETVTVPGALEVPAAIALAADSGRFDAYVALGVVIRGETYHFEVVSNESARGIMALTLDGLAIGNGILTVENEEQALARADKTRKDKGGEAAKAALAMLALKEQFGIG | 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 = ... |
Q9XH32 | MASFAASQTCFLTTNPTCLKPNSPQKSSTFLPFSAPLSSSSSFPGCGLVHVASNKKNRASFVVTNAVRELEGYVTKAQSFRFAIVVARFNEFVTRRLMEGALDTFKKYSVNEDIDVVWVPGAYELGVTAQALGKSGKYHAIVCLGAVVKGDTSHYDAVVNSASSGVLSAGLNSGVPCVFGVLTCDNMDQAINRAGGKAGNKGAESALTAIEMASLFEHHLKA | 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 = ... |
P0CV46 | MCGAHYVAIALLVVAGSLAAAEFDQNEIQQTSDDDVMASVNSTYELLQSRILRERREPKDNLLSAGDEERTPSSPSSFLKELKVSDSIMDAANVIRTEGGASAIDAALKNLNQLNRKRRQRIAPTSKNVAGHEVGTSSDTDKSLVSVENETPFVLAKRRRTKRSAAMMTNAARSAKQHDYRLAPTESSTIPAKAPDDQLNKQPISQKALQLDKNEHVDESLWREELMTVDEVLHLFEEFDKPAHPTAVNLQEPNAIETTSKKLNHLRRNKRKRKHIASTPKNVGQLVRAPPLSDKSPVLVAKGIPFVLAIRLKKNHPTAI... | Function: Secreted effector that dos not suppress the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 49912
Sequence Length: 447
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular L... |
P0CV48 | MRGAYYVTIALLVVASSQISAEFGHQLQAYDHDVTAADDAVAETLAKRSLRGSRDVSNDVAIEERTKYSNVIEDGIEMLLRAAEALKEMPRAAVAVKDMPRAEEAVEKMAPIAEQDLLKNVIGADEASKRRRAPHGISTQRTLALPFKEWNTELKQMRGGSVLKKYRSKIKSVHQAFVDLCDKDLNPTVTETALLWGMFDWDVKSYSASAHKHNLIRLAKRYVHKDVVQIQSDDLAWNRWNEVSIPLRIGALNILLNLHYQRWVRMYNIFEQYQSALIGTPVSLELSLGGTTGTSSATALDKHLEVPMNKASTSKGKSSV... | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 42338
Sequence Length: 382
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellu... |
P0C0W9 | MSAKAQNPMRDLKIEKLVLNISVGESGDRLTRASKVLEQLSGQTPVQSKARYTVRTFGIRRNEKIAVHVTVRGPKAEEILERGLKVKEYQLRDRNFSATGNFGFGIDEHIDLGIKYDPSIGIFGMDFYVVMNRPGARVTRRKRCKGTVGNSHKTTKEDTVSWFKQKYDADVLDK | 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... |
P62987 | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLRQLAQKYNCDKMICRKCYARLHPRAVNCRKKKCGHTNNLRPKKKVK | Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via ... |
P05318 | MSTESALSYAALILADSEIEISSEKLLTLTNAANVPVENIWADIFAKALDGQNLKDLLVNFSAGAAAPAGVAGGVAGGEAGEAEAEKEEEEAKEESDDDMGFGLFD | 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... |
Q8ZME1 | MAQFYSAKRRVTTRQIITVKVNDLDSFGQGVARHNGKALFIPGLLPEESAEVIITEDKKQFARARVSRRLNDSPERETPRCPHFGVCGGCQQQHVSIALQQRSKSAALARLMKHEVNDIIAGAPWGYRRRARLSLNCPPDKPLQMGFRKAGSSDIVNVEQCPVLAPQLAALLPRIRACLASLHGTRHLGHVELVQAGSGTLMILRHTAPLSAADKEKLERFSHSEGLSLFLAPFSEILETVSGEAPWYDSHGLRLAFSPRDFIQVNEAVNQQMVARALEWLDVRAEDRVLDLFCGMGNFTLPLATRAASVIGVEGVPALV... | 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): 47768
Sequence Length: 431
EC: 2.1.1.190
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Q0HXI0 | MAQFFKAKPNSSKQLSAKQSFSVHQLDHLGAGIAQHQGKVVFIPGALPSETVQAQLTEQKKNYARAKLIKVETPSAERVTPLCPHYQSCGGCDLQHMSLAGQREHKSAALVDIMAKFAGAEGNSVPALTGEGWHYRRRARLATLFDKNTKQLSLGFRASSSNQVVPIDSCLVLAKPLSDLIAPFAKLLNQLAAKSSLGHLELIDADNGHFAVIRITKSLNDKDMAKLAQFAEQHQIHICLQDNNGEFHGVNGTLLLPVYQLLDDKADATPVSLTFTPGNFVQVNAQINKAMVAQALDWLAPQPGERILDLFCGMGNFSLP... | 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): 48920
Sequence Length: 449
EC: 2.1.1.190
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Q5UYP9 | MSGKDDYYNRAKQEGYRARSAYKLQQLDDTAGLLGEGRTVVDLGAAPGGWMQVAAERIGERGTLVGVDRQTIDDLEDPEPTVEYVRGDMTEDSTKDEIREIVGESDGSGGPVDVVISDMAPNMTGQYDLDHARSVHLVRQAFEVATDLLDAGGDFCAKVFDGQDLDDLIADIEPEFEYVREVRPDASRDSSSELYLVAKHRLTGPVREGDIVEATIEDIGEEGDGIAKVENFTVFVSGVEDGETVEVRIDDVKPRYAFAEPVE | 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)... |
Q0C187 | MSDDDRRRWKGPGPERQDSGRRSTERKVIARNARTESSKRWIERQLQDPYVRKAKDEGYRSRAAYKLLEIDAAAKILRKGMRVVDLGCAPGGWIQVSLQQGAAEVVGIDLLPLDPIEGATIIEGDVNNPDDVARMMAGLSGTPDLILSDMAANTTGHKQTDHLRTVALVEMAVAFAIEHLDDGGAFCAKVFQGGATKDVLNLLKQHFRTVKHIKPAASRAGSPEIYVVAKGFRR | 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)... |
Q1MRQ0 | MKPYRDYYFLKAKHEKYPARSIYKLKEIDNRFCLFQKGMSVLDLGASPGSWSLGAAEKVGKTGRVVSCDIQTITIPLPSNVSFFQEDIFHRSDSFNNILIKEGPFHVIMSDMAPQTTGVKITDHSRSLELCLEALAIAKCYLLQQGSFIVKIFMGADTIELVKEMRQHFERVTSFKPCSSRTKSKEIFYVGLGFKRFTTS | 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)... |
A5IHX0 | MSRTKSSKRWLQEHFDDVYVKKAQAEGYRSRAVYKLKEIDDKESLIKPGMTVVDLGAAPGGWTQYASEKMKGSGRLVALDILPMDALPNVEFILGDFREDNVLQELINLIPQRTLDLLLSDMAPNMSGSSAIDIPRAMYLVELAFDFAEKMLKPGGNMLVKIFHGSGFDELVKQARASFEKVVIRKPSASRSRSKETYLLAKGYNL | 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)... |
Q89YP0 | MAERSELHTRNKHNGQYDFSLLTENYPPLRKFVLLNPLGIQTIDFFNPHAVKALNKALLISYYGIRYWDIPRNYLCPPIPGRADYVHYIADLIDPERVSNTANEENGDKPKRQCRCLDIGVGANCIYPIIGHVEYGWMFVGSDIDPVSIENARKIVTCNPVLAHKIDLRLQKDNRRIFDGIIAPDEYFDVTICNPPFHSSKKEAEEGTLRKLSSLKGEKVKKTKLNFGGNANELWCEGGELRFLLNMISESRKYRKNCGWFTSLVSKEKNLDKLYAKLKAVHVSEYKIIRMCQGTKNSRILAWRFLE | Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Catalytic Activity: adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35358
Sequence Length: 307
Subcellular Location: Cytoplasm
EC: 2.1.1.181
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A0M4S0 | MHPDNIHKDSYDFEALTESNPQLSEFVFQNKYGTQTINFANPEAVLQLNKALLKFHYQVENWSIPKQYLCPPIPGRADYIHYLNDLLSEENIQGEIRGIDIGVGANAIYPILASRIYDWKMLGTDIEEKSVAIAQANIETNPTIAKNIEIRHQEDRGSIFKGMIKKGEYYHFSICNPPFHASQEEANKATSRKFKNLGLEKGSALNFGGQANELWCNGGEALFIKRMIKESVLFKSQVGYFTSLVSKKENLPKIYKHLNKLKADFKTIEMGQGNKKSRIIAWKFD | Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Catalytic Activity: adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32511
Sequence Length: 285
Subcellular Location: Cytoplasm
EC: 2.1.1.181
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A8AIX5 | MSAQKPGLHPRNRHHHRYDLATLCQVTPELAQFLTRTPAGEQSVDFANPLAVKALNKALLAYFYQVANWDIPEGFLCPPVPGRADYIHHLADLLGETTGAIPADASVLDVGTGANCIYPLIGVHEYGWRFTGSEVHAQALASAQVIISGNPGLTRSIRLRRQKDPAAIFNGIIHKNEQYDATLCNPPFHDSAASARAGSERKRRNLGQDKNDALNFGGQQQELWCEGGEVAFIKTMIAESQAFGRQVMWFTTLVSRGENLPPLYRALTDVGAVKVVKKEMAQGQKQSRFIAWTFMDDDQRRRFMARKR | Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Catalytic Activity: adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34254
Sequence Length: 308
Subcellular Location: Cytoplasm
EC: 2.1.1.181
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Q482M9 | MHKKNRHNQGYNFTALVKAHPGLLQFIIKNQYNNQDTIDFANPQAVKALNLSLLKSEYHVKFWDIPDGYLCPAIPGRVDYIHHLQDLLAATPKTLLPNKTPINVLDIGTGASCIYPILGQREYDWHFVASDVDPISIKVAKHIISSDKSLNRNINCRLQPNSNQIFNGIIAEDEFYHLTICNPPFHSSLAEASKGTARKIKNLNKGNHSSKNQDKTLNFGGQKAELWCPGGELAFIGKMIKESKAYQKQVLWFTCLVSKKDHLSKLKLSLKKSDAKQIKVIDMAQGQKISRFIAWSFYDVN | Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Catalytic Activity: adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34029
Sequence Length: 301
Subcellular Location: Cytoplasm
EC: 2.1.1.181
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Q47C26 | MHPRNKNAEGYDFAALAATSAALAKHIKTTQAGTASIDFANPAAVKMLNRAILMHHYGVKGWDIPAGYLCPPIPGRADYIHSVADLLATCNKKNIPSGPGVRVLDIGVGANMVYPLIGHAEYGWSFLGVDIDEAALANAQSIIGKNPELASDIELRHQPVWDNIFTGLLRSGEVFDLSICNPPFHNSPDDVHAVSQRKWNNLNKPGAKRGAAEPRLNFGGGGSELWCNGGERAFVKRMIEQSCNIPKRVMWFTSLLSQGDNLPHIEAALKKAKVVESRIIPMAQGQKQSRLVAWTFCGNGEREKWRRERWTAAPSYAVPA... | Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Catalytic Activity: adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36947
Sequence Length: 340
Subcellular Location: Cytoplasm
EC: 2.1.1.181
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Q6ANQ6 | MASQHDKKSVQSGLLHPRNPHRGRYDLDALCRTCPELKMHIQIKPTGDKTIDFSDAKAVLCLNRALLAHYYQVSNWQIPEGYLCPPIPGRADYIHYLADLLAEDLPTSAKGKKIRVLDIGTGANCIYPIIGSQSYGWHFVGTDIDPLAIKIAGMIVQANSCLNGKITLKQQLDKKLIFKGIINEDKFDLTMCNPPFHASLAEAEAGNQRKRKNLGHGKENRAQEKLNFGGQNAELWCPGGEIVFLRQMAEESVAFAKQVRWFSSLLSKGKNVAPLKKLLKQLGCKRIKVVEMAQGQKISRFIAWSFSQE | Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Catalytic Activity: adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34541
Sequence Length: 309
Subcellular Location: Cytoplasm
EC: 2.1.1.181
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Q9K3L9 | MTTPWGERVLSRFPEDPRDRLRAWDASDEYLLGHLAEREVPLSGTVVVVGDRWGALVTALAPHRPVQITDSHLAREATRVNLERSGVEPGSVRLLTTQDPPPDRVDVLLVRVPKSLALLEDQLLRLAPALHEGTVVVGTGMVKEIHTSTLRLFERIVGPTRTSLAVKKARLIFAEPDPALKRPANPWPLGYRLPDDVGRLSGRPVVNHAGVFCADRLDIGTRFFLRHLPAPGRFRRVVDLGCGNGVVGTAVSLADPDAELLFTDESFQAVASARATYRANEVAGQAEFRVGDGLAGVPDGSVDLVLNNPPFHSHQATTGA... | 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): 41282
Sequence Length: 377
Subcellular Location: Cytoplasm
EC: 2... |
A5F5X3 | MKTELTLLEQTLTLHRFPKRNNETLQAWDAGDEYLIQHVEQLALPESSHIVIINDHFGTLSCWFSQKHKVSMMSDSYIAHQATQANLQQNQRPPVQLLTTLDPVPNDASVVLLQLPKSNRHLVWILSQLRKALSPNIPIIAVNKAKEIHTSTLNLFEKHLGPTTTSLAWKKHRLVFSSATVNPANEVNPECGWSIEPYAITLTNLPNVYSGESLDLGSRFILEHLPADPTLEDFIDLGCGNGVLSVRLGQLNPQAKITCVDESFMAIASAQKNLHDNLGKRDIHCIANNCLDGFPAHSSSMIVCNPPFHQQQTITDHIAW... | 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): 42051
Sequence Length: 376
Subcellular Location: Cytoplasm
EC: 2... |
P59732 | MKIKLVTVGKLKEKYLIQGINEYLKRLNSYAKMEIIEVPDEKAPEKLSDAEMLQVKEKEGQRILGKINDNEYVFVLAINGKQLSSEEFSKEIEQLGISGKSNLTFVIGGSLGLSDSVLQRSNQQISFGRLTYPHQLMRLVLVEQIYRGFRIMKGEPYHK | 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): 18193
Sequence Length: 159
Subcellular Location:... |
Q7VCH9 | MLNPSRFRILAIGKVRKSWIQNGLEVYRKRLPGLSITEIRDGDIKKESRAIISSIKKDELLIALCEEGEKFTSMDFSHWLQNLGSSRIVFAIGGTNGLSQEVKTSADLCISLSALTFPHEMARLILAEQLYRAISIAKGSPYHRE | 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): 16291
Sequence Length: 145
Subcellular Location:... |
Q46L60 | MLNISHYKIIAIGKIKKKWIQEGIEMYLKRLPGLEVKEIKDSTQLKEEHTIKEIISKNEFLVTLNENGQSFTSKQLATKLLNSHNQNITFVIGGASGLSSSLNNLASWQLSLSPLTFPHEIARLLLIEQLYRAKAITQGGPYHKE | 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): 16399
Sequence Length: 145
Subcellular Location:... |
A8F6Q8 | MKIEIVVIGKLKEYIRPAVKEYIKMLSSFAEIKLTQIKHAKGYKDFDKSLKKEAEGIISQLKESDYVILLDQSGRSCDSISFANHFHQLIQINSSIVFVIGGPFGVDESLKKRANELLSLSDLTFTHQLAVVILLEQLFRAFKIINNQKYHY | 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): 17406
Sequence Length: 152
Subcellular Location:... |
Q5GWE6 | MSGLLCYCRQGFEPELAAELSARAAFVGIAGYARTQRNDGYVLFVCDEAAQLAAKLQWRELIFARQKLVVIAELKGIDPKDRITPILAALEGQQRFGDLWVEHPDSDAGKPLAGLARSFGNALRPALRKAGLLTDKPQPRQPRLHICFLDGDHALLAVADSADSAPWPLGIPRLKLLPEAPSRSALKLDEALLTLLTPEEREALVKPGMRAADLGAAPGGWTWVLTRQHVHVTSVDNGPLRAHVLETGLVEHLRADGFHWKPAQPLDWMVCDMVEQPRRVAERMATWVREGWCRNTIFNLKLPMKKRWDETRLCLELFEQ... | 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): 38900
Sequence Length: 347
Subcellular Location: Cytoplasm
EC: 2.1.1.186
|
B2I9N9 | MSGLIAYCRQGFEPELAAELRDRAVLLGIASDIHAQRNHGFVLLRCDPLHVDTLLQQLHWRRLIFARQTLRLHAELKTLNSRDRIAPILAALPKTPCFGDLWIEYPDSDMGKPLAGLARSFGNALRPVLRSAGRLSAQLHPQWPRLHVCFLSGDHVLLGSTRSVDSAPWQLGIPRLKLLPEAPSRSALKLEEALITLLTPNEREAKLRPGMCATDLGAAPGGWTWVLICQHLRVTSIDNAALRPPLLNHPLVQHVRADGFRWIPPRPMDWMVCDMVEQPRRVAERMAVWLREGWCRHMIFNLKLPMKKRWDETRLCLERF... | 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): 40041
Sequence Length: 351
Subcellular Location: Cytoplasm
EC: 2.1.1.186
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A9WFY6 | MHYAMEQRCLYDYNLSELTELLQSWGEPAFRARQLYRHLYVNLARQVDQMTDLPLALRSRLAEIPFSTLRCEQVQIGDNGMTRKALFRLPDGAVVETVLMVYPDRSTVCVSTQAGCGMGCVFCATGQLGLLRNLSSGEIVAQAIWASQELRAMGMAGPTGRVSNLVFMGMGEPFANYDRWWQAVERLHDPQGFNLGARSMTVSTVGLVKGIERLANERLPINLAISLHAPDDALRSELMPVNRRYPIADLMAATRNYIAKTRRRVSFEYVLLQGKNDHPHQAIALARLLRHSAPRGPLLFHVNLIPWNPVPGTPLGRSEW... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
Q3B4B8 | MKRERSNILNLRMDELKEALAAINEPQWRAAQLHQWLFSHRAGSFDDMTTLSLPLRRKLAESFYIQQPVTEKHDETMEGSPAGATEKLLIQLPDGERVETVLIPGPNRMTACVSAQAGCLLGCSFCATGQMGFRRNLSSGEITGQVWALSDMLQERNREASISNIVFMGMGEPLLNTANVIEAVLNLSTRKYRFSTSQRKITISTVGITPEIDRLADTGLKTKLAVSLHSAIQEKREALMPQAARQYPLDRLRESLIGYASKTGEPVTLAYMLLKGINDSEMDAKRLIRYASGFFCKINLIDYNPIVNIKFEPVCDGTRE... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
B3QS43 | MNEVKHDIKALSLEALMALINSYGQPAFRAKQIFHWIYAHGVTDFAQMKNLSASFQTLLSQHFTVSSIQPHADTVSHEITPEQTVKFLFRLSDEQSIESVFIPSDSTSRNTLCISSQVGCAFACKFCATGYMGFIRNLTIGEILDQVLWVNRWLGDQRGGKITNVVFMGMGEPLANFDNCLAAIRILTNPDYAFQISTRKITVSTVGFIPGIQRLIDTGINCKLAISLHSAHQAIREELIPIAKEYSLATLKAILTRYNQAYKQPITFEYSLIHKINDSEQDAILLSKFCKGINCKINLIDYNSVDNIDYLPSPEGHKQA... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
Q8KD71 | MEKNEISEERRTQEKEKQHGHRLNIRRLGRKELTELLTRLGEPAYRANQLHRWLYSNQALRFEEMSTLSKQLRQKLASEWIIHPASLVGTERETTDASLVTGNPTAKFLIKLEDNELVESVLIPSEERITACISSQIGCPLRCTFCATGHMGFRRNLTASEITDQVFLLEKEAQKRHWRGLTNIVFMGMGEPLLNLDNVLESIGTLTEKDYQFSISERKITISTVGLPVEMDRIARSGLKTKLAISLHSADQLIRERMMPIAADITLDKLAKAINSYNSVTSQPVTLVYMLLEGINDSPEDARKLVRFAKRVLCKINLID... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
Q1QTL1 | MTLDTVTPRTNLLGLTREEMESFFVSLGEKKFRAAQVMKWIHHEGCADFASMTNLSKALRTRLEELAEIRGPRVVYEGTSQDGTRKWVLEVEDGSYVETVLIPAEGGKRRTLCVSSQVGCSLDCSFCSTGKQGFQRNLTSAEIIGQVWVASNSFGARRDTTNRPVTNVVMMGMGEPLLNYDNVVPAMKLMLDDNGYGLSKRRVTLSTSGVVPKLDQLGDELDVSLAVSLHAANDELRNELVPLNRKYNIATLLDACRRYLAKCDDTRMLTIEYTLIKDVNDQQHHAEELAALLADLPSKINLIPFNPFPHSGYEKPSRNQ... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurrin... |
A6LSK1 | MNNLLDFTLEELKAWMKENGESAFRGQQILSWIYKGVKEFDNMKNIPKPLVQKLKENFFVGLPKIIEVYKSNIDGTEKFLLGFKDGNLIESVLMRYKHGNSICISTQVGCAMGCKFCASTIEGKVRNLTTGEILSQIMVVQDYINERISNVVLMGSGEPLDNYNNVIKFLEIVSAEYALNIGQRHITLSTCGIVPKIYELADKELSITLALSLHAFSNDKRKEIMPIANRYSIEEILEACRYYINKTNRRITFEYALVKDVNDGREDAKALGKLLKGMLCHVNLIPVNEIKENTYKRSSKKAIEDFSEILKNHGIEVTTR... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
A1SLQ4 | MSDSERTSLPLVFDEPRGRKKPPRHLADLAPDERTAYAKELGLPGFRAKQLSTHYFSRLVDDPDQMTDLPAGQRAELVAGLLPGLMTPLRTMEADRGTTRKTLWRLFDGALVESVLMRYPDRATMCVSSQAGCGMACPFCATGQGGLQRNMSTAEIVEQVVAGARSLARGEVPGGPGRVSNVVFMGMGEPLANYKAVLGAVRRLTDPAPDGLGMSARGVTVSTVGLVPRMRQLADEGIPVTLALSLHAPDDELRNELVPINTRFSVAETVEAAWNYAKVTKRRVSIEYAMMRGINDQAWRADLLGDVLRGYGDWGWVHVN... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
Q8YZV0 | MSATPVTQLTPSSQPQQPCSPLLGASVTELTSWVQQQGQPAYRGKQLHDWIYHKGVRSLTDISVFSKQWRAAVADVPIGRSTIHHRSVASDGTVKYLLQLSDGEIVEAVGIPTDKRLTVCVSTQVGCPMACDFCATGKGGYKRNLERHEIVDQVLTVQEDFQQRVSHVVFMGMGEPLLNTENVLAGLRSLNQDVGIGQRSLTLSTVGIRDRISELAEHHLQVTLAVSLHAPNQALREQLIPSARSYHIEDLLAECREYVAITGRRISFEYILLAGVNDLPEHALELSKHLRGFQNHVNLIPYNSIDEVDYKRPSGDRIQA... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
Q8ELW7 | MSKSSIYGLTYEKLKDWLIEHGEKRFRAEQVWNWLYKKRINSFDEMNNVNQSAIQLLKDNFVLHTMGEEIRQESQDGTIKFLFKLEDGNLIETVLMRFHYGLSVCVTTQVGCNIGCTFCASGLLRKSRDLSSGEVVEQIMNVQKHLDERGEKDRVSHIVVMGIGEPFDNYNNLMDFLYTVNDDRGLNIGARHITVSTSGLAHKIYEFADDPIQVNLAISLHAPNDELRTKIMKINRAFPIDKLMKSVDYYLQKKNRRITYEYIMLDDVNDHKKEAIELANLIKNHRHLAYVNLIPYNTVDEHIDYRRSKSENIQAFYETL... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
A4VNX4 | MIATTGKVNLLGLTQPQLESFFESIGEKRFRAGQVMKWIHHFGVDDFDAMSNLGKALREKLKACAEIRGPEIVSEDISSDGTRKWVVRVASGSCVETVYIPQGGRGTLCVSSQAGCALDCSFCSTGKQGFNSNLTAAEVIGQVWIANKSFGTVPAKIDRAITNVVMMGMGEPLLNFDNVVAAMQIMMDDLGYGISKRKVTLSTSGVVPMIDELAKVIDVSLALSLHAPNEALRDQLVPINKKYPLDVLLAACKRYVSRLGEKRVLTIEYTLLKGVNDQPEHAEQMIALLADIPCKINLIPFNPFPHSGYERPSNNAIRRF... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurrin... |
Q67PQ7 | MQESGYVPLKIADPALLFAELGRQPLPGMSLEEMADLMADLGEPRFRAKQLFQWVYQKGVKDFDAMTNLPARLRQHLAGTTMLRLLEKETEQHDRRTGTTKYLFRLADGSQVESVLMRQSWGNSVCVTTQVGCRMGCTFCASTVGGLVRNLTAGEIVDQIVMMQRELPQGERISTVVLMGSGEPLENYDHVLKAVRLVHDPEGLNIGYRHITISTSGIVPGMRRLAEEGLPITLALSLHAPTDELRRQLMPVARIWPLAEVLAAAREYGEKTGRRVTYEYILIEGVNDGPEEARQLARLLKGALAHVNLIPMNPVAERPQ... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] +... |
Q2LUM5 | MHMNRINIRDMSLEEIESFISSLGKEKYRARQIMKWLYSQGAKSFDEMTTLSRAVRDQLNEMACITLPEIARVQQSSDGTRKILFRLQDNSFIESVLIPGKHNWTACISTQVGCHMGCRFCFTARQGFRRNLKPSEITGQLTMLQFYLPEGPEIKNIVMMGMGEPLANYRNTLKAIRIITSDYGLGFSTRKITLSTSGITPMIEQLGRDLCINLAISLNAPTDSIRSELMPVNRKYPLDRLLQACRNYPMPGRRMLTFEYILIDGVNSSPAHAEMLCRLLKGIRCKLNLIRFNEFPDCPFKTPSEETVLAFQQILVKHHY... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurrin... |
Q3A2Z4 | MDVSMDQDTRIDLKNFTLEELTEFLAGMGKERFRAGQVMRWMYHRLVDDFDAMSDLSKVLRAELHQRARISRLTPEATEDSRDGTRKYLFRLEDGETIESVRIPMDDNRATLCISTQVGCAMGCVFCHTGSFGLVRNLTPGEIVNQVCAALADGPVNNIVLMGMGEPLHNLDNVVKALQILYMPQGLDYSPRKVTLSTAGLVPQMQELGKRVRVNLAVSLNATTDEVRNRLMPVNQRYPLQQLMAACRQYPLHAKKRITFEYILIRDVNDSDQDARRLVKLLHGIKAKVNIIPFNEHSASEFRAPTEERISRFQGYLLDH... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurrin... |
A0LQM1 | MEPVCVKDFTLPELEEWVQGIGERSFRARQLFRHVYGRGVRSWSECSDLSRMFRVQLEHGVELDALSVLKKEQADDGTSKYLFGLRDGHSIEAVLIPDLPRSTLCVSSQVGCALGCKFCLTGSLGFKRNLSAAEIVDQVCQVQRDLGSRSRITNIVFMGMGEPLANLDSVLRAIRVIAEPNGMAFSHRRITLSTAGLVPQLRRLGRESPVNLAVSLHAAENELRAELMPVNRTYPLEVLMAACREYPLPPRKRITFEYILLDGINDDPKQAKQLVKLLHGIRAKVNLMPFNPHPGSVFRKPSEQRVLAFQEALQNARITT... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurrin... |
A0A0P1AK67 | MRSLVWAVIATLIVLTPFSEATSSIASNNEEFKQNVRVASSSLEQKGTIEDSVITRKLQSDSVKKGDSTGLEERGGLHVPTIHDNKIVQGFYKVMRYLRQKLGIDFLLTRLRYGKNGSHQPNMGYSRVDHYH | Function: Secreted effector that does not suppress pattern-triggered immunity (PTI) in plant host.
Sequence Mass (Da): 14894
Sequence Length: 132
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: Sec... |
A0A0P1B8W9 | MRFFYKLALMTTVASLACSDTALASTDLMPFNVAETQVSTHDIVSAGRSLRAEDTSTSIDNLRDPTMKEKIQFKLWYTRGKTPGQVHRDFFEGLDESIIVNNPNYEVWKMYEAYYNNKKGND | Function: Secreted effector that does not suppress pattern-triggered immunity (PTI) in plant host.
Sequence Mass (Da): 13973
Sequence Length: 122
Domain: Has the canonical translocation RxLR motif, but lacks the canonical EER motif, which characterizes most oomycete effectors identified so far.
Subcellular Location: Se... |
A0A172M470 | MRSWLLLLVGLSSYFALSTSVNRAKNSGSDFDLESRASTTNVNSILSKRKLRAPGGDTNTLKDSGKARREKKVWKLFCRVFLQLDDEKKCMFETNQVSSHQPEPRPALSFMPGPKPAHSLVPESKPVRSLMTGNAPVRSIATKLKLVLPRITETVKNPSKSQVVMLWLHKVAEFSRSEHGVNTMSYRTLYEWLSPSFSDAKLAKFFVGLREDEALRETAEKMLAYMLIKSTSTEAVGRAWLKSGEHPSRLFESMNFKEADFKDTVFLGWLKYASLYEKHYFSQSELTDYRRQLFFYRMYDYIKPMYSYEKTQGFLEYKFE... | Function: Effector that partially suppresses the tobacco programmed cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 48494
Sequence Length: 416
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subc... |
A0A0P1AL95 | MTGILCFPPFARFFMLLSGCAWLAGVSSGTSLVASAFSDENQLSEFVHVAEIAQIHRNLRGHINSAIIEANDTSEERMQPNNVVGEGKAPSGAQETVAQILVKGMNKVADFLKDLTRSQK | Function: Secreted effector that does not suppress pattern-triggered immunity (PTI) in plant host.
Sequence Mass (Da): 12965
Sequence Length: 120
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: Sec... |
A0A172M468 | MTNLFTRHTRRSLTALALLSGGVYAADEVNAKILSRSLRVFVTGGQVLWDYRIHFKGIERDHPDYHSKLQSLNQRIAHRLLYLCFENGGIYTKFGQQLATFNHGLPREYTMTLAQLQDQAKPVSFDKVKQTIEAEMGRPWNECYKEFDQTPIASASLAQVHHAVDALGREMAVKVQYPHLELQMKADIRVIKWAFQFTEYCFPDVQLQWLFPEFQKALLAEVHFDAQCTALLIIF | Function: Effector that acts as a broad suppressor of cell death to interrupt plant immunity. Inhibits cell death induced by cell death-inducing proteins, including the PAMP elicitor INF1 from P.infestans.
Sequence Mass (Da): 27137
Sequence Length: 235
Domain: The RxLR-dEER motif acts to carry the protein into the host... |
A0A0N7L4N2 | MKAVKLTAAVVVLFMAPYVPITSSRSLAETPNDSIDRHLRHESAQIDSKLKEVEGKHDSNTPLQRRDQTLVAAHRVYDPVSGLACSLVGECMSCPITEKDESFCRETGYRQELACPHSKDEALLQTLEEKQTPRYRPCSPADTVRPGVTFVKFEAIMSLLLAISVTLLRREREKHMSSFDLRKDSRQRVGLLNSSASGVKDSD | Function: Secreted effector that does not suppress pattern-triggered immunity (PTI) in plant host.
Sequence Mass (Da): 22674
Sequence Length: 203
Domain: Has the canonical translocation RxLR motif, but lacks the canonical EER motif, which characterizes most oomycete effectors identified so far.
Subcellular Location: Se... |
A0A172M4N0 | MHVSRIIAHIALATAITATTVSPTDAAWGWTVKSTDEVKADKRDLVASRGLRGLIGQASPNEVSPANVPVSGIPLLGDKQPSGYPMLPADSPSTGSSLLNDDLLQENPVPPANGLVHGVPLLSSNQPLQTPMLSGNGPITGYRFFSGNESPMLPANSPITGLPLLSGNIPSTFEGEQISNGDEYQQNVDEDKGQNFGHSVSGPPTTTLTGPHTKSGIPPFENLVAPAKGSMPNTRRNGYQFFE | Function: Effector that significantly enhances susceptibilities of grapevine and tobacco to pathogens . Acts as a broad suppressor of cell death to interrupt plant immunity. Completely inhibits cell death induced by cell death-inducing proteins, including the PAMP elicitor INF1 from P.infestans . Reduces the transcript... |
A0A172M473 | MRRTAFIVLSLVALIAPCVTSVAVEDLAQANNIETNVNPNVKVGSRRHLRSEANGRLAVVDEEKVFRDFCGLGPCFDWLKPQNLGGFIYKFVEWASRDRVNFKLKMLKREHQIPIRKRNQ | Function: Effector that acts as a broad suppressor of cell death to interrupt plant immunity. Inhibits cell death induced by cell death-inducing proteins, including the PAMP elicitor INF1 from P.infestans.
Sequence Mass (Da): 13767
Sequence Length: 120
Domain: The RxLR-dEER motif acts to carry the protein into the host... |
A0A172M418 | MICRSPLIVVMLFVIAAHTVLALEIATRIDASETESPVSAQMTRVSYRPITSVDNKRFLRQETTFEKKLGVNDVHAVHAEERSALGKAKILGRDLLWFMSILGRFLIPRIGRRGP | Function: Effector that acts as a broad suppressor of cell death to interrupt plant immunity. Inhibits cell death induced by cell death-inducing proteins, including the PAMP elicitor INF1 from P.infestans.
Sequence Mass (Da): 12930
Sequence Length: 115
Domain: The RxLR-dEER motif acts to carry the protein into the host... |
A0A0P1A8A0 | MRLYALSVSLLAAITLLACVIASADSNMVSQMKRRLSQDVSETEITELSESKKPTAQDIDNEERAQLTLLSDSQAIVAVAEKAAHSSPKVLGGTSALATTKFALQSQKTSRLRQLLDKVMKISGLLKKFLNFFKNKKTNTVPKLENKPHNAFDTV | Function: Secreted effector that does not suppress pattern-triggered immunity (PTI) in plant host.
Sequence Mass (Da): 16978
Sequence Length: 155
Domain: Has the canonical translocation RxLR motif, but lacks the canonical EER motif, which characterizes most oomycete effectors identified so far.
Subcellular Location: Se... |
A0A172M466 | MRSSTILIVLGIAILAVNGVATALTRDGIEMGTQEKSRLLRSTSTEHETDEERKFRFKLPSFRFKRRVKVPKVAKPKKKNPVMANRARKYHDVLHSDRGYDVYDMMRSDKLTLQELIEFLTTYGQIDKNGIKILTDGLRSYNIPKAYPVAK | Function: Effector that acts as a broad suppressor of cell death to interrupt plant immunity. Inhibits cell death induced by cell death-inducing proteins, including the PAMP elicitor INF1 from P.infestans.
Sequence Mass (Da): 17343
Sequence Length: 151
Domain: The RxLR-dEER motif acts to carry the protein into the host... |
P0CV02 | MRHCACLFHLFLIGFLCNVYFSACTHTSSLKESDDESPRAEHWGSDGKRILRANDSEFLLTEERILLILLWSPLGR | Function: Secreted effector that dos not suppress the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 8768
Sequence Length: 76
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellular Loc... |
P0CV03 | MRGAYYVAFALLVAASTRTAAEPDQAEPHIAPNNDYMTSGGAFNKMLPRRILRESPDPKDRLPVYASDEERMVNRLSNGNSIAKGLERTIMKAANVLRTNGEDVIANAAKPIKNYNRLRPKLEIKKSKRQRIEPTLSKSSEHKLHTTSNSKKSLVSSASAKGQGRDEPRATVNTAKKMQHNHRSAPSRSSPTSADVSDGRLEKQLNAQKAINLDKNKRPDEAKIRNKKQHVIDPTPKNENGQALRAPPTPESLGIGGKQCTVRIGREK | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 29584
Sequence Length: 268
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellu... |
P0CV04 | MRGAYYIIIALCVVASSQVAAGSDRQLQIYEHGVMPADNAVVKTLAKRFLRGSRVVHDDLANEERSFHPFLVDMIEEGIKEMSHAAEIVEEMPLAGKVVEEVPHATEGGQQKMDKGAEEAFEKHVEPSGHTATIQDTSRDISTQEVIQLSPHEWESDLSKLKPFVVLNKHRGRIEPVKDAFAAFCDEGLKPTTEETSIIWSMLGWNLARKPKGKHRQHLIAQARRGVLLDLRIVRMDESLWNKWMQLPKPLRMLKLNNLLNMHYQRWVHLFNIFQRRLSEIIGPPPKLKVAHGDTTDTSKALALHTHSNMQSSTPSEPLN... | Function: Secreted effector that acts as an elicitor that induces cell death in host plant cells.
Sequence Mass (Da): 48858
Sequence Length: 435
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... |
P0CV05 | MRGTIYVAIAILVAASSRSSAESDQVEPQQAPNSDFVTSDDTIYEVLPTRILRESRGSNDKLAVGAGDEERMMNNLSNGNSLSESLEQTTIKLTTDDVIAKAEEAIKNFKQLEPVLNMIRRKRQRIDPTPSNLGGQALHAPPNPDKSLVSVTENAPNVIANRLEKSGPTVIMKNAVRSITQHDYRPAPSGSSTTSAAATDIRLHEQPIARKGSELFKNIYPNKMVSNSVEHPLHMLEGNENSAHTVTVNGITYLMAQGPALGRKDTVNEEAKKIHEAFLKAFSLPFHQYPEETTHMLRLLRWSYNSSPNNINTATSLKDL... | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 44095
Sequence Length: 399
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellu... |
P0CV06 | MTYRLPFVAVILFVTAKHVVLALENANWIEASKTVPSDSTQTTRVAYRRITGGFNERFLRQLEKKPGVNDKRDEERANFFEAVFKNTLFNAFGYRSDAKAKLQDPNSNIFVNLLRRIFVWWAKNKPEFNKNADMHKEAMV | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 16317
Sequence Length: 140
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellu... |
P0CV07 | MHLIYIVMAATATTLHASSSAILDPSDVKIMTKNVESRIGNDAAFAAGRFLRGAYEDVHREEERMFGLKQNQHSFIKPSQAQDAAAIDALNIAKEALESTRNTKDHPHATATAGDQSLNPLIAAYPLRASPNAGVPQQHLGVALGSVHPHTSRST | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 16618
Sequence Length: 155
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellu... |
P0CV08 | MRGAYYVAIALLIVASCSAAEVDQTEPEKVPNNGFVTSGGTVNKMLPKRVLRGSRDLKNKWAVHAGGEDRMLNRFSNENNLLEGIDQTITKAANVMGTNRDDVIVKAAEAMTNYKQLDPTLNILNSKHQLIKPRPINVYRQALLHATPNPKKSVVAVPNDVPFVLANRLEREKSTNTVNYAGRPITQHDYLPASLSFPSTSAVAPDGQFNKQLITQKALEFDLIKRPDEVKARSSKRQRTNPMLNNMDGRELHAQPNLEEPLAPVANNMPFVWATKLGEK | Function: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
Sequence Mass (Da): 31074
Sequence Length: 280
Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate.
Subcellu... |
Q5A2V2 | MFRLIASGAQQGLRPSLISKVKPPTTTTTTSTTSKFTSTTQHFPFENNNLLGYQVRNNSSQAGVASEPKISLPETDVYQQKLLKYNIKKHEPYHLKFNPKTKNQRNNDSASSFSIDEFSQLLQDETFRNQLNEKHLFVYASNLYSGTINSRRARLNKSKNRDKDQRSAFREDMTLQSAVLNLTEIISTGELNSVLSARTLFKVFGTLLQFKLNDEIVNLWETGVNSDVGKLYLAHEVLSIVIQVGHETRRFNYDEIKQIYEMSVKEDKTVHPYLSDRMGQVAVMEGDYVTALDALESLMNLYEQNPNEKSVLGALAQIHL... | Function: Binds the 3'-UTR of mitochondrial mRNAs (By similarity). Involved in the processing or stability of mitochondrial mRNAs (By similarity).
PTM: Phosphorylated. Phosphorylation promotes binding to RNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 70286
Sequence Length: 613
Subcellular Locat... |
Q6FU02 | MFRYLSRTSTIYKGVIATSKTASTANVVAAQESRRNYANKRNNNRNGPADALDEKLNSILSGKTSSKRKPYGGRKSPVDETSPWYAQLCALDDCLTTTLKQSATPMRKLLSDRVNHPDMRSNPTFWHSVSRAMTLYNELKQCPEMTDQRVTSLVHLLHNGLRTDRQLVSSLNKKPDYDSQSFHKEMVNFIYTSLNEISDDILNNNVPINANGLMHLFTSYQEMGFTDLVVQIWKKIETIAEQNPQSNIGKISKHPNVVGIVLPILYEKEIVNFSEAEKLFKECEQYHNRMFPNLYVGMILTSLKANENMKALELFETLCT... | Function: Binds the 3'-UTR of mitochondrial mRNAs. Involved in the processing or stability of mitochondrial mRNAs.
PTM: Phosphorylated. Phosphorylation promotes binding to RNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71001
Sequence Length: 616
Subcellular Location: Mitochondrion inner membran... |
Q6CKI3 | MFRLVQQQTLKSRVPNQFVSASRNSLNSQFRFNSAVALERNPQQDPTTAAPAKSSSDKRNSKKKYENNEIIERNVKKVRNLRRNIKFDNFKNSPNSPAFSKLNALDDCLARGLEASSSRAPDGKFLDQSSLFWDSVSSSMNIYRELVITGDLNNHRASRVIQLMHVALKVNRTQLTSMNKKPDYDSQSFHKEMTNYLCESLREISGDILANRVSVSEHGAAHLLSSFKELLLYEETLNIWKAAVNSENKDIVKSFMFPNVVGVVLPLLYENGTTFEEIKKLYEKSASNTTRSHGSPSLVLGMIKTSLAANENEHALSLFQ... | Function: Binds the 3'-UTR of mitochondrial mRNAs. Involved in the processing or stability of mitochondrial mRNAs.
PTM: Phosphorylated. Phosphorylation promotes binding to RNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 75244
Sequence Length: 664
Subcellular Location: Mitochondrion inner membran... |
A5DDF2 | MFRLLASSGQVSLRPVLLQHVRNNKHGLGFPNASGVPQSPSSMTSSSIVSPSQFTRSNSSAAGLSESPASSVDSKIENFLSKSAKDPLVREALDAETKNKLNYFKEQIDLAHRYRSIHDHDSERAFASTLDNLSRALEDESLRDTFVSRDLFSYAQVLNSGVYNNRTNRLSGAKNRDSDQYQNQNLHDEVLLKQAVLHLGELITNGEFKAILNAPTLSFLFYSMKQFQLYPEMIHLWENGVNDQQTGQVYLDEKILAVILPVTFEQNRFTYEEILHIYELNTEKLDKVGHELLTSMGKIAIAAGDYSRGLDSLESILQLY... | Function: Binds the 3'-UTR of mitochondrial mRNAs. Involved in the processing or stability of mitochondrial mRNAs.
PTM: Phosphorylated. Phosphorylation promotes binding to RNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 73046
Sequence Length: 632
Subcellular Location: Mitochondrion inner membran... |
A3LQ52 | MFRLVSSNAQGSFRSSLLTKVRIPISVPASSPLNTSTSNNTTTNNNNFGVNNSTNNTQFTRHQSSAAVDLSARKVYQDEFLRSHSSFTAPDHETKVKLNHFKELLVTGNQKLRALNRQEARAFYSVLQSLSHMLEDAKLRRSLNVDLLHQYSLLLHSAIFSSRTNRLAEKRNRDKDEYNATSYTDEVVLRGSVLNFAQLVEAGEFKYCFTDKVLQYLLYSMFQFKFNTEALNLWENGVNDAETGSVYLRPLVLATVLPRAFELKRFTYEEILHIYELNTKKEQFPHHTLVTAMGKIAIHAGDYSRALDFLERLLEKYDQK... | Function: Binds the 3'-UTR of mitochondrial mRNAs. Involved in the processing or stability of mitochondrial mRNAs.
PTM: Phosphorylated. Phosphorylation promotes binding to RNA.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 73036
Sequence Length: 629
Subcellular Location: Mitochondrion inner membran... |
P53140 | MMLRRNAVRSLKTMEISVSNVVNSGSIAMLRGKLANVVLSDRTYHSSPIFHKNVPKGVLDKKNGREQRKTEQNVFNVDPASPWRHELLSFDECVSSALKYSTTPLQNTYKRIGNNQLNKNPSFAMFWDSMGRAMELYYSLRESPDFNAYRVSRLIHLLHNGLRSTRDQLVKLSRKPDYDSQSFHKEMMNFLCNSLKDISDDILIGKVSVSGYGATHLLTSFKELSFDDDCIRIWEASKNLSDETTSQAFQEPKVVGFMLPLLYAKTRSLTEPNELYNQIIQSKEFIHPNLYSGLIKVFIKAEDYEKALSLFGQLCEKAEV... | Function: Binds the RNA motif 5'-AAUAA[U/C]AUUCUU-3' in the 3'-UTR of mitochondrial mRNAs . Involved in the processing or stability of mitochondrial mRNAs .
PTM: Phosphorylated . Phosphorylation promotes binding to RNA .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74596
Sequence Length: 646
Subce... |
Q6T1X6 | MRALITGVAGFVGKYLANHLTEQNVEVFGTSRNNEAKLPNVEMISLDIMDSQRVKKVISDIKPDYIFHLAAKSSVKDSWLNKKGTFSTNVFGTLHVLDAVRDSNLDCRILTIGSSEEYGMILPEESPVSEENQLRPMSPYGVSKASVGMLARQYVKAYGMDIIHTRTFNHIGPGQSLGFVTQDFAKQIVDIEMEKQEPIIKVGNLEAVRDFTDVRDIVQAYWLLSQYGKTGDVYNVCSGIGTRIQDVLDLLLAMANVKIDTELNPLQLRPSEVPTLIGSNKRLKDSTGWKPRIPLEKSLFEILQSYRQA | Function: Reductase that catalyzes the conversion of GDP-6-deoxy-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose (GDP-D-rhamnose).
Catalytic Activity: GDP-alpha-D-rhamnose + NAD(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADH
Sequence Mass (Da): 34556
Sequence Length: 309
EC: 1.1.1.281
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Q9HTB6 | MTQRLFVTGLSGFVGKHLQAYLAAAHTPWALLPVPHRYDLLEPDSLGDLWPELPDAVIHLAGQTYVPEAFRDPARTLQINLLGTLNLLQALKARGFSGTFLYISSGDVYGQVAEAALPIHEELIPHPRNPYAVSKLAAESLCLQWGITEGWRVLVARPFNHIGPGQKDSFVIASAARQIARMKQGLQANRLEVGDIDVSRDFLDVQDVLSAYLRLLSHGEAGAVYNVCSGQEQKIRELIELLADIAQVELEIVQDPARMRRAEQRRVRGSHARLHDTTGWKPEITIKQSLRAILSDWESRVREE | Function: Reductase that catalyzes the conversion of GDP-6-deoxy-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose (GDP-D-rhamnose).
Catalytic Activity: GDP-alpha-D-rhamnose + NAD(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADH
Sequence Mass (Da): 33929
Sequence Length: 304
EC: 1.1.1.281
|
Q9FFL1 | MTELSSPNLDSASQKPRISTENPPPPPPHISIGVTTGDPATSPARTVNQIKKITVLPLVFLIFYEVSGGPFGIEDSVKAAGPLLAIVGFIVFPFIWSIPEALITAEMGTMFPENGGYVVWVTLAMGPYWGFQQGWVKWLSGVIDNALYPILFLDYLKSGIPILGSGIPRVAAILVLTVALTYLNYRGLSIVGVAAVLLGVFSILPFVVMSFMSIPKLKPSRWLVVSKKMKGVNWSLYLNTLFWNLNYWDSVSTLTGEVENPSKTLPRALFYALLLVVFSYIFPVLTGTGAIALDQKLWTDGYFADIGKVIGGVWLGWWIQ... | Function: Cell membrane polyamine/proton symporter involved in the polyamine uptake in cells. Possesses high affinity for spermine and spermidine and lower affinity for putrescine. Transports paraquat, a polyamine analog, and thus confers sensitivity to this chemical which is used as a herbicide.
Location Topology: Mul... |
Q3T0Y9 | MACLEIPQQPQLVCQKATPSDPAGCDGGPGGPTEGDLECLVCREPYSGVRPPKLLGCQHAFCAVCLKLLLCVQDDAWSIPCPLCRKVTAVPGGLVCTLRDQEKVLERLARPGLEVPLRPQGLANPATLTAGQPREAGEEEQDAVTTNRAAARRLAAHLLLLVLLIILILPFIYPGVIRWVLSFLETLALLLALLFCSHPGQQDGCMPTPRTLFCRERKPSEIASIS | Function: E3 ubiquitin protein ligase that is part of an apoptotic signaling pathway activated by endoplasmic reticulum stress. Stimulates the expression of proteins specific of the unfolded protein response (UPR), ubiquitinates BNIP1 and regulates its localization to the mitochondrion and induces calcium release from ... |
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