ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A9GCQ1 | MPPDERAPLPLPAPAPLTPPEGFAERLAAIGVTLDAAVIAKLGDYLARLLAMNELMNLTSITDPVEVWEKHVLDSLTLLPLLEELSAGARLADIGSGGGLPGLPLAIARPDLKVTLVEATQKKASFLVAVAAGLGLTNVSVRAERAEQLGKGDLCGAFDAVTARAVGRLVMLIPLTVPFVRPSGLVLLVKGQRAEEELAEASWVLGRQRAAFVKTVATPTGKIVMLRKSGEEPKRHPGR | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25175
Sequence Length: 239
Subcellular Location: Cytoplasm
EC: 2.1.1.... |
Q1GP62 | MIIPHRADGGKNDVSAAELLKDERAARGWLTQAFAPSTEQWAQIERFVTMLIAENAKQNLIAASTIPAIWARHIADSAQLLALDTREGEGLWIDLGSGPGLPGLVVAILSERPMLLVESRRRRCDFLRAVVAELALDHVEVAEAPLERVATRPAATISARAFAPLDRLIDLSARFSTESTRWLLPKGRNAVKELALLPEPWQRMFHVEQSRTDAESGILVGTGRIAPKKRGKA | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25591
Sequence Length: 233
Subcellular Location: Cytoplasm
EC: 2.1.1.... |
C1F466 | MERERHVPVLLQDAIRYLNVRRGGTYADATLGLAGHSSAIARLLGPGGTLIAFDRDPEAMELAKSRLDALRAELGSEMPKVILHSTEFSEAEDLIEPGSLDGLLADFGVSSLQFDEAHRGFSFQADGPLDMRMNPRVGLTAAQVVNQFGEKELADLIYEFGEERRSRRIARAIVRARPVSTTAQLARVVSAAAPAMKSERIHPATRTFQALRIYVNQELGQIEALLKVAPKLLRKGGRLVVISFHSLEDRIAKDALREGGQQGIYEVLTRKPLTAGEEETDRNPRARSAKLRAAEKK | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32714
Sequence Length: 297
Subcellular Location: Cyt... |
B7J3W0 | MRSANEPDATHVAVLLAETIVALRPALHTGAAVRCVDATGGRGGHSAALLAELGAADTLLILDRDPSAIAALRARFAQDSRVYIRQARFSQLAEVLAALEWERVDAILADLGVSSPQLDEAARGFSFLRDGPLDMRMDPGADRSAAEWLATATEADMTRVLREYGEERFARPIARAILRAREQAPITRTLQLAELIAQVLPRHETGQHPATRSFQGIRIFINRELEELEAFLPQAMNALRAGGRLAVISFHSLEDRLVKRFFRADDYRISADVPLRASELPPLPWHPAGKALRAGPRETRDNPRSRSAVLRVAERSERHA... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35344
Sequence Length: 321
Subcellular Location: Cyt... |
A0KPY0 | MTQAAEHITVLLHEAVEGLAIKPDGIYVDGTFGRGGHSRLILQQLGPNGRLIAIDRDPQAIAEAAKIQDPRFEIVHGPFSGIASYLDERGLLGKVDGFLLDLGVSSPQLDDAERGFSFMKDGPLDMRMDPTSGQSAAEWLARADVDDIAWVLKTFGEERFAKKIARAIVHDRVTEPYVRTRQLAEMIARVNPSKEKGKHAATRSFQAIRIYINSELDEIETALNGALQVLAPEGRLSVISFHSLEDRLVKHFIRKHEKGPEVPHGIPLTEAQLAGGRKLKSVGKALKPSEHEVNENSRSRSSVLRVAQRLAE | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34381
Sequence Length: 312
Subcellular Location: Cyt... |
A0Q055 | MNFNHVPVLLEETIDSLNIKEDGIYVDCTLGGAGHSSEILKKLSKKGRLIGIDQDINAIKAAKERLKDYENVTYVHNNFYNLASILDELNVDKVDGILMDLGVSSYQLDTPERGFSYMKDAMLDMRMNTENGISAYDVVNGYSEDDLFRIIKDYGEERFSRKIAKAIVKERNEKPVETTLELVKIIKDVIPMKFQQGGHPAKKTFQAIRIEVNHELEILNKTVEDGVNYLNPNGRISVITFHSLEDRIIKTKFKELENPCTCPKEFPICVCGKKPVVKVVTRKPIEPNEFERENNSRSRSSKLRVAQKI | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35240
Sequence Length: 309
Subcellular Location: Cyt... |
B5Y8C1 | MTNYIEHKPVMAKQVAELLVSNEEGIYVDATAGSGGHLGLLANTYPEASFIGIDIDPEAVKFLTEKFAGVSNVRIIRGNYADLPDILHSMEIGQVDGILLDLGISMHQALSAQRGFSIKNPGPLDMRFSIDQKVTAYELVNSLSEEQLADIIYRYGEERRARKIAKAVVEARKVKPLETTDELADLVARTVGYRGRIHPATRVFQALRIATNRELDNLQVALPRIFQVLKEGGRLAVISYHSLEDRIVKQFFKTWEEEGKGLRLTKKVVKPSLEEINENPSSRSAKLRVFKKGVGGNEN | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33314
Sequence Length: 299
Subcellular Location: Cyt... |
Q8NNM7 | MEDFSLDGNHGHVPVMRDRMAALIAEHVEALGENAVIVDATLGAGGHAEFFLNTFPKARLIGLDRDQNALRDARARLAPFGERFIGVQTRFDGLREVLESVEGDIIDLAREHGIAGALFDLGVSSMQLDQVERGFAYRTDAPLDMRMDATQGITAADILNTYSHGDIARILKTYGDERFAGKIASAVLKEREKEPFTTSARLVELLYDAIPAATRRTGGHPAKRTFQALRVEVNNELDSLKNVLPQITDALNVGGRAVFMSYQSHEDKLVKKFFTDLTTSKTPPGLPVDLPGTAPQFKQVTRGAETASEAEIEENPRAAP... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36809
Sequence Length: 337
Subcellular Location: Cyt... |
C4LI42 | MADRHTGTHGHVPVMLERMVELIAPTVTESSENSAPSVILDGTLGAGGHTESFLERFPSAMVIGVDRDKKELSRTTERLSRFQDRFYPVHARFDNFDEALDDADHPVVDAFDAHGLSAGFFDLGVSSMQLDQVDRGFTYRDDGPLDMRMDTSTGKTAADVLNTYSHGELARILKTYGDERFAGPLARAIVREREKEPWSTSQRLVDLIYATIPASARRHGGHPAKRTFQALRVEVNAELDALRRVIPKVCSYLHLGGRAVFMSYQSLEDKIVKRELAALTESKTPPGLPIDLPNSAPDFHLVTRGSEKADEQENNKNPRA... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 43090
Sequence Length: 390
Subcellular Location: Cyt... |
Q6KHR2 | MESNVHIPILLNEVLSAFNLKETDVVIDLTLGRAGHSQEMLKKIPKGLLIGIDKDKSAITFSKEKLEQIGSNFKLFHSDFSKISDLLKELKISKVNAILIDLGISSPQIDNANRGFSYNKESRLDMRMNLDQKLDAHFIVNSYSEEQLKNLLYRNAEIKNSRQIAKIITSNRPIETTLQLSVILKKYLPAFIVRKKDPSKAVFQALRVEVNDEINSLNFLLKNLVSILEENGKVAIITFNSIEDRIVKKYFGSFIKDDVLAFLPTKKEKEFEVKTYLPSKKELEENPRSKSAKMRVLKKIER | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34582
Sequence Length: 302
Subcellular Location: Cyt... |
B3DVX0 | MSWKTEEVESHIPVMLKEFLKHCSPKRDEQWIDGTFGYGGHTTALLDKGCKVLALDTDEDAQKRAEILKEKGEEFYFFRKNFSEMAEACFQMGWTAVDGILLDLGVSLGQLKDPKRGFSFQFPDAPLDMRMDRTRERTGAALLNTLSKEQLVQLFSVACNMKESQKLANEIVRFRSTGPIKKVGDFLEIVTRARLLKSKINAATRPFLALRIAVNEELEHLEKALREGTKLLKGGGRIAVISFHSAEDRIVKEFMRSHCLPKKGEGVAEEENHREMFFYKVERVLVSLEERKNNPRSRSARLRIAWKIPLEEKSGL | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36149
Sequence Length: 316
Subcellular Location: Cyt... |
B8IMX2 | MSGMPPHIPVLLKEVRSALRLGEGPGIVVDGTFGAGGYTRAILEADPGQRVIAIDRDPTAIATGRGLAAAMAGRLMLVQGRFGELDRLVRAQGIETVDGVVLDIGVSSMQLDQAQRGFSFRQDGPLDMRMESGGTSAADLVNEASEAELADIIYHYGEERRARAVARAILEARRRGRIATTATLAEIVASVVRPEPGSGIHPATRTFQALRIAVNDELGELQRALHAAERILRPGGRLAVVTFHSLEDRIVKQFFSARSGRAVSASRHLPMAEKPAPRSFTLVTKGPIGPSEAEATANPRARSAKLRAGERTDAPIPEPL... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36071
Sequence Length: 339
Subcellular Location: Cyt... |
B1LYT9 | MSRRRPAPESSPRHDGADAPPEPHVPVLLAEVVEALGTEGGTAVDGTFGAGGYTRALLAADPALQVVAIDRDPTAIAGGQALVAESGGRLRLLPGRFGDLDGLLAEAGIAQVDRVVLDIGVSSMQLDAPERGFSFRSDGPLDMRMACDGPSAADLVNEADETVLADIIYHFGEERRSRAVARTILEARRRGRIETTAQLAELVAGVVRTEPGSHIHPATRTFQGLRIAVNDELGELVRALHAAERVLRPGGRLAVVTFHSLEDRIVKQFFAARSGRSAQGSRHLPGGPVETVRSFRPVTKGPVLPGEAETARNPRARSAK... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37439
Sequence Length: 353
Subcellular Location: Cyt... |
C5CA38 | MDAGQPRPEDRHLPVMRDRVVDLLAPAVQAALEAGRTPVAVDGTLGMGGHTEALLTRFPHLRVIGIDRDAHAQAMAAERLGPLADRVIPFHGTYDRVPEAMAAAGVTKVDAALYDLGVSSYQLDDRERGFAYSYDAPLDMRMDDTAERSAATLVAELDEQELRRIIRRDGEERFAGPIARAIVRARAEAPIETTGRLVEVIRSAVPVAAGATGGHPAKRTFQALRIAVNEELDILDAAVPAILDALHVGGRLVVMSYHSLEDRITKRHLSAWATSTAPPGFPVVLEEHEPVVRVLTRGTEKPTEEEISENRRASSAKVRA... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36012
Sequence Length: 331
Subcellular Location: Cyt... |
Q2S535 | MSDDDSQDDSVPEGDPRRYATDFHAPVLSHDVQARLVTDASGRYVDATLGGGGHARALLDVLDPDGVVLGIDRDPEALETARDRLADEREAGRFWAVHGTFGNLRDVLAAEDLIPIDGLLLDLGVSSHQIDVPERGFSFRDEGPLDMRMDPQRGLTAQQVVNGWGERDLRDVLREYGEESRAGQIARALCDARPLDTTRALAEVVEDCAPPPDTVKTLTRVFQALRIVVNAELDELEQVLEQATEVVRTGGRIAAISYHSLEDRRVKRYLRYGNFEGEPRRDLYGTLVAPWAETPRGPIEAGESEVEANPRARSAHLRVA... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37041
Sequence Length: 336
Subcellular Location: Cyt... |
A4X9S3 | MGELRGAHVPVLLERCLELLSPALDRTGQTGRTVYVDATLGLGGHAEAILTAHPRTMLVGLDRDTEALAHARVRLARFADRVHLEHAVYDELPDVLDRIGHPVVDGILFDLGVSSLQLDAPDRGFAYAQDAPLDMRMDQSRGVTAEEVVNSYSHPELARVLRVYGEEKFASRIASAIVRERDRAPITSSAQLAELVRQAIPAPARRTGGHPAKRTFQALRIEVNRELAALETALPAALDRLAIEGRMVVLSYHSLEDRLTKVALADRVRSKGPIDLPVELPGTGPTFRLLSRGAELPGEAEVAVNPRAASVRLRAAERLD... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40641
Sequence Length: 371
Subcellular Location: Cyt... |
Q08329 | MASIQLARTTRGGDGVARADGTRQADEAGSGTLYLVPTPIGNPGDITLRAIEVLRRVGVVASEDTRHTYRLFQSLEIDARLVSYHDHNEESRSRQLLGLLREGTDVALVSDAGTPLVNDPGYRLVAAAVEADVPVRPLPGATASVTALIGSGMPNHQFHYVGFLPRKEAARRAALTALRSTPATLIFFEAPHRIVAMLADLAAVLGDRPAALARNLTKDDEEFLRGRLNELTARLRVEQVVRGQFTVVVAGSPEAHADEDRALAARLTETLVRHGAEARLIREVVREVTGLPRNWVYEQVRLATERSGPLGNS | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33906
Sequence Length: 313
Subcellular Location: Cytoplasm
... |
P47302 | MKTLKVVATPIGNIQEISERAKKALQDCEVLFCEDSRVTRKMLDLLNIDCKQKKFVINNSFKEKQNLTFAEEFITNFKCCLVSDAGYPSLSDPGNEMINWIISKNKEIRIEVINGPSALMCGLITSGFKTTPLLFLGFLSHKQNQLKNYLSTYQNQKSTIVFFEAVHRLENTLETVKNVFKNNDVFIGRELTKLHESHYWFNTSENTLPDITLKGEFVIVIDNQNINHQTLSSNQYLVYEIKKLMDIGVKLKDACNYLAKKMHLKSSMLYTLFHESI | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 31895
Sequence Length: 277
Subcellular Location: Cytoplasm
... |
Q98RF5 | MAKIYIVGTPIGNLSDITLRALETLKKVDYIACEDTRVSKILLNHYQINKPLFSYHKFNEKSKLNYIFELVESGSDVALISDSGMPVISDPGFLLIREAKKKNIDLEVIPGVSAFSMAFVKSSFPLPFSFLGFLNDKTGKRKNELKKLSAGISYISYVSKYKLIQTLKDLKEVFGLNVEVFLTRELTKKFENDYTGTIDEIIDQLGESIKGEFTLIFFIKQA | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25117
Sequence Length: 222
Subcellular Location: Cytoplasm
... |
P9WGW6 | MSSGRLLLGATPLGQPSDASPRLAAALATADVVAAEDTRRVRKLAKALDIRIGGRVVSLFDRVEALRVTALLDAINNGATVLVVSDAGTPVISDPGYRLVAACIDAGVSVTCLPGPSAVTTALVISGLPAEKFCFEGFAPRKGAARRAWLAELAEERRTCVFFESPRRLAACLNDAVEQLGGARPAAICRELTKVHEEVVRGSLDELAIWAAGGVLGEITVVVAGAAPHAELSSLIAQVEEFVAAGIRVKDACSEVAAAHPGVRTRQLYDAVLQSRRETGGPAQP | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29647
Sequence Length: 285
Subcellular Location: Cytoplasm
... |
Q9JXE3 | MFQKHLQKASDSVVGGTLYVVATPIGNLADITLRALAVLQKADIICAEDTRVTAQLLSAYGIQGKLVSVREHNERQMADKIVGYLSDGMVVAQVSDAGTPAVCDPGAKLARRVREAGFKVVPVVGASAVMAALSVAGVEGSDFYFNGFVPPKSGERRKLFAKWVRAAFPIVMFETPHRIGATLADMAELFPERRLMLAREITKTFETFLSGTVGEIQTALSADGNQSRGEMVLVLYPAQDEKHEGLSESAQNIMKILTAELPTKQAAELAAKITGEGKKALYDLALSWKNK | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 31353
Sequence Length: 291
Subcellular Location: Cytoplasm
... |
Q9HVZ3 | MSAGTLFVVATPIGNLDDISPRALRVLREVALVAAEDTRHSIRLFQHFGIETPLAACHEHNEREEGGRFISRLQGGEDVALISDAGTPLISDPGFHLVRQAQALGIRVVPVPGSCALIAALSAAGLPSDRFIFEGFLPAKAAGRRSRLQAVQEEPRTLIFYEAPHRLLESLADMRDVFGGERRAVLARELSKTFETIRSLPLAELHDWVASDSNQQRGECVVLVAGWQAPEGEESIGAEALRVLDLLLAELPLKKAAALAAEITGVRKNLLYQQALQRQGKS | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30617
Sequence Length: 282
Subcellular Location: Cytoplasm
... |
Q98DM9 | MVGQTEIPARPLEPALYLVATPIGNLADITLRALETLAAADIVACEDTRVSRVLLDRYGIRRRTTAYHEHNAGEAGPKLIAALQGGQSVALISDAGTPLVSDPGYRLVGEAIDHGIRVVPIPGPSAPLAALTASGLPSDAFLFAGFLPVKVGQRLTRLEALKAVPATLIFFESPRRLAESLGAMVEALGGERKAAIGRELTKTFEEMRTGTLRALADHYAAADTPKGEIVVCVGPAEAKADEPADIDRLLLSLAAEMPASKAASEAAKMTGGQKQALYRRLLELKDTSGEGDGG | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30807
Sequence Length: 294
Subcellular Location: Cytoplasm
... |
Q9ZCJ3 | MILKSGLYIVSTPIGNFEDITLRAISTLKNSDIILCEDTRISQKLLAKHYIHTKLQIYNDHSDYKDREYIISLIKAGNVVSLISDAGTPLISDPGYKLVRDLRNLNYYIEVVPGVSSPITALTLSSLPTDRFLFSGFLPKTIESKKKIFAELVNLKATLIFFDTASRLINTLLLAKEIFGNREICVARELTKIYQETKTGDIDEIIEFYKNNILKGEIVLLISGNVQVQNKQINLEKFIEFCLSKNLSSKTIIELAYDKFKDVYSKKEIYSVVHKKKFTA | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 31844
Sequence Length: 280
Subcellular Location: Cytoplasm
... |
Q9A186 | MQVQKSFKDKKTSGTLYLVPTPIGNLQDMTFRAVATLKEVDFICAEDTRNTGLLLKHFDIATKQISFHEHNAYEKIPDLIDLLISGRSLAQVSDAGMPSISDPGHDLVKAAIDSDIAVVALPGASAGITALIASGLAPQPHVFYGFLPRKAGQQKAFFEDKHHYPETQMFYESPYRIKDTLTNMLACYGDRQVVLVRELTKLFEEYQRGSISEILSYLEETPLKGECLLIVAGAQADSEVELTADVDLVSLVQKEIQAGAKPNQAIKTIAKAYQVNRQELYQQFHDL | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 31818
Sequence Length: 287
Subcellular Location: Cytoplasm
... |
P74038 | MGILYLVATPIGNLGDMTPRAVETLQTVDLIAAEDTRHTGKLLQHFQITTPQISYHDHNRHGRTQELLAKLQAGQNIALVSDAGTPGISDPGQELVAACGEANIEVIPIPGATALIAALISSGLATDRFVFEGFLSTKNRPRQQLLQSLAQEERTIILYEAPHRLLATLTDLQTFLGQERSLTVARELTKYHEQFWRGTLQTAIAYFTENTPKGEFCLVIAGATPEDRPSFSEENLRDELRSLMAKGLTRSQASRQLAEETKLPRRQLYQLSLELEADG | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30830
Sequence Length: 279
Subcellular Location: Cytoplasm
... |
Q9WZG8 | MGKLIIVGTPIGNLEDITIRALKTLREVDLILAEDTRRTMVLLNKYRIKKPLLSFNERNSKKRIKEILPLLKEGKKVAIVSDAGMPVISDPGYNLVEECWREGIEVDIVPGPSALTSAVAVSGFPGSKFIFEGFLPRGKNRRRLLKSLKKENRVIVFFESPERLLSTLRDILEIIGDREVFIAREMTKLHQEFFRGKVSEAISHFEKKKPLGEITVVLSGKE | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25125
Sequence Length: 222
Subcellular Location: Cytoplasm
... |
P14206 | MSGALDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTAAQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGATTEWS | Function: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement mem... |
Q974U1 | MIEIDGSFGEGGGQILRTSLTLSALTKKPFRIYKIRANRPKPGLQRQHLTAVEAVKKLTNAKVKGDFVGSTELVFEPEDIVEKGDFEFDVGTAGSVTLILQTILPLLINRNIKVTIKGGTDVPKSPSIDYIRLTFLSLLEKIGIRVNLILIRRGHYPEGGGEIKITEVKGNPSSFSLMERGELLMIKGISHVSSLPSHIAERQAKSAKEFLLSKIKIPVEIEIDVRENERSKGSGIALTAIFEKTFLGSDSLGEKGKRAEIVGEEAAKSIYEEIISNATVDRHMSDMLMLYASLYYGEYIGSELTSHARTNSEIIKKFLN... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
C5A2A3 | MEWVEIDGSYGEGGGQILRTAVALSVITGKPVRIHRIRANRPNPGLRPQHLHGILALKELSNARVKGAKVGSTVLEFVPGRAEPKHVKVPIKTAGSITLVLQALLPAMAFIGGSFEITGGTDVPWSPPVDYLRNVTLFALEKMGLRAEIELKRRGHYPKGGGLVTGSVEPWESKKPLVALEWNKVDSFAGISHATNLPAHVAERQAKSAEERLREFFNAPVEIETEVSRSLGPGSGIVVWAETDSLRLAGDALGKRGKPAEVVGREAAEELIEQLTPRKAVDRFLGDQLIPFLAFAGGEIGVAEITNHLVTNVWVVERFL... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
Q5JIQ0 | MEWVEIDGSYGEGGGQILRTSVALSVITGKPVRIYNIRANRPNPGLRPQHLHGILALKELSNAKIKGASVGSTELEFIPGKAEPKHVRVPIKTAGSITLVLQALLPAMAFIGGSFEITGGTDVPWSPPVDYLKHVTLYALEKMGIKVELEIKRRGHYPRGGGLVVGRIEPWEEKKPLKALKWERIEWFAGISHATNLPAHVAERQAKAARERLSEVYSAPVEIETEVSRSLGPGSGIVVWAETDKLRLGGDALGKRGKPAEVVGREAADELIEALKTGMAADRFLGDQLIPFLAFAGGEVGVSEITNHLVTNVWVVEKFF... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
C6A4N4 | MRVIDGSYGEGGGQILRTAVALSVITGEPIKIINIRAKRSNPGLRPQHLHGILALKELSDAKVKGAKEGSTELEFYPKSTRVRHVKVLIKTAGSISLVLQALLPAMVFAEEEVTFEITGGTDVAWSPPVDYLKHITLYALEKLGIKVEIEIRRRGHYPRGGGFVIGKVYPWGTKRPLVARTFDKIYSFEGISHAVRLPSHVAIRQAKAAKEALERVYPSIPIKIHEEYYEQGKDPHFGPGSGIVIWANTDVLRLGGDALGERGKPAEIVGREAAKALIEQLGPRHAVDKFLGDQLIPFLTFAGGDIWVSEVTKHLITNVW... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
C4M6T2 | MAKSRYSRKNKGKKLQRAQQNTVSTEEKPEQEVETIDFNGFQIPKVYDGKFERKPMELEIKKGFVEGMNGDAKIFCNDDLLNLLTFEMIKDISNNYPSCVRQTANAATLPGVVGSLAMPDAHSGYGFSIGGVVAMRLDDPEAVICPGGVGFDINCGVRLIRTNLQREDIEQHKARLADELFKQIPSGVGTQAQIAFSPEDFDSIMKEGLEFLVENGYAWEEDLNHCEEHGKIANADPSLVSNSAKSRGYKQVGTLGSGNHYLEVQVVDEIMDVEAAKAMGITEIGQVCIMVHCGSRGLGHQVCQDYINLCMKSGICNPVD... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an R... |
O29399 | MNMEGILKKITDYKWELPKSYKPGMRVPAYFYISRKLMQILEKDAVEQAANVATMPGIQVASLVMPDVHVGYGFPIGGVAGFDVNEGVVSPGGVGFDINCGVRLLRSNLNVEDVKPLIKKLIDELFVAVPSGVGSEGRLRVSDRELDEIFVEGARWAVENGYGYERDLKHCEEEGALEGARPEVVSKKARDRGRPQLGTLGSGNHFLEVQYVDKVFDEKVAAKFGIEEGMVTVMIHCGSRGLGHQVCTDFLEVLDRAVKKYGIKLPDRQLACAPINSKEGQDYFAGMAASANYAWCNRQIIAHWVRETFQKVMGMSEDDL... | Cofactor: Binds 2 manganese ions per subunit.
Function: Essential for tRNA splicing and maturation. Acts by directly joining spliced tRNA halves to mature-sized tRNAs. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends.
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + a 5... |
B9JLT8 | MSAVTAAGYQAPQERSQSVTLPARPEPITLKPSETAVVVVDMQNAYSTEGGYVDLAGFDIAGAKGTIANIKKTLDAARAAGVQVIYFQNGWDKDYVEAGGPGSPNYHKSNALKTMRQRPELQGQLLAKGTWDYAIVDELQPQPGDILVPKTRYSGFFNTNMDSVLRARGIRNLVFVGIATNVCVESSLRDAFHLEYFGVMLEDATHHLGPDFIQQATVYNVEKFFGWVATVNDFCATVSQAAPTEA | Function: Hydrolyzes ureidoacrylate to form aminoacrylate and carbamate. The carbamate hydrolyzes spontaneously, thereby releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2.
Catalytic Activity: (Z)-3-ureidoacrylate + H(+) + H2O = (Z)-3-aminoacrylate + CO2 + NH4(+)
Se... |
A6T799 | MRLNIAPAPWPGAPVVVLSAGLGGGGGYWLAQRAALEEQYQLVSYDHNGTGENAGPLPAGYSLATMAGELFSALQAAGIARFALVGHALGALIGLQLALDRPEAVSALALVNGWLSLSPHTRRCFQVRERLLHAGGAQAWVEAQPLFLYPAEWMAARLPRLEAEDALAISHFQGKENLLKRLQALKQADFSRRASAIACPTLIISAADDLLVPASCSRVLQTAIPGSQLVEMPWGGHACNVTDADTFNTILRDGLSAMLPVARETR | Function: Involved in pyrimidine catabolism. May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously.
Catalytic Activity: carbamate + 2 H(+) = CO2 + NH4(+)
Sequence Mass (Da): 28248
Sequence Length: 266
EC: 3.5.1.-
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C5B0U6 | MAAPVHHEVHGPEGGRKVLLSPGLGGSAHYFAPQVPVLAERFRVVTYDHRGTGRSPGPLEPGHDIAAMARDVLDLLDHLDIGTADIVGHALGGLIALQLALTHPERVGRIVVINGWAAMDPATRRCFAARKALLRHAGPEAFVRAQAIFLYPAPWLSENAARLADDEAQALAHFAGTRTVLTRIAALETFDATAALGRIPHETLLMAARDDVLVPFTASDILAAGLPNARLDLAPEGGHAHSATRPEAFNRTLLDFLTSP | Function: Involved in pyrimidine catabolism. May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously.
Catalytic Activity: carbamate + 2 H(+) = CO2 + NH4(+)
Sequence Mass (Da): 27673
Sequence Length: 260
EC: 3.5.1.-
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D4GEU7 | MYYKVLGQQNADAETVVLSSGLGGSGGFWQPQLAMLSAHFRVVVYDQYGTGASQGSVPAGYRMEDMADELAGLLNALNISRCHLVGHALGGIMGLHLALRYPALLQSLVVINGWTVLNSQTRRCFDVRRNLLLNSGVDAYVQAQPLFLYPGDWLSEHEAFLQEERQHQVANFQGMENLLHRLQALMDSDLTTSLKGVIAPTLALSAKDDLLVPWSCSADLASRLPHGEHLQMGYGGHAMSVTDPDTFNPILLDWLQRQASHPSGTPSDFIPVEMP | Function: Involved in pyrimidine catabolism. May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously.
Catalytic Activity: carbamate + 2 H(+) = CO2 + NH4(+)
Sequence Mass (Da): 30097
Sequence Length: 275
EC: 3.5.1.-
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P75892 | MAMFGFPHWQLKSTSTESGVVAPDERLPFAQTAVMGVQHAVAMFGATVLMPILMGLDPNLSILMSGIGTLLFFFITGGRVPSYLGSSAAFVGVVIAATGFNGQGINPNISIALGGIIACGLVYTVIGLVVMKIGTRWIERLMPPVVTGAVVMAIGLNLAPIAVKSVSASAFDSWMAVMTVLCIGLVAVFTRGMIQRLLILVGLIVACLLYGVMTNVLGLGKAVDFTLVSHAAWFGLPHFSTPAFNGQAMMLIAPVAVILVAENLGHLKAVAGMTGRNMDPYMGRAFVGDGLATMLSGSVGGSGVTTYAENIGVMAVTKVY... | Function: May function as a proton-driven pyrimidine uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45557
Sequence Length: 442
Subcellular Location: Cell inner membrane
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A3DBU3 | MFAYIRGRLEYKNNDFLIVESNGVGYRIFTSLSTISGIGEIGQEVKVYTYLYVREDVISLYGFLTQEELNVFELLISVSGVGPKAAVSVLSAISPSRFSLAVITDDVKTLTKAQGIGKKIAQRIILELKDKIKKEQLTEYAQSEEGGKVLDTDSSKMAEAVSALMVLGYSPAEANKAVSAVYREDMDIETIIKNALKGLARP | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A9NF61 | MYRYIKGIVTQINPQHIVVENNGVGYLVLSPVPYQYKIGEETTVVTYLHVREDIFQLYGFKDEETLNLFLKLISVSGIGPKSAMSIVAFDDTNKIIAAIETSDAKYLTKFPGIGMKSAQQIILDLKGKLVNDELDMQLLSDNSKDVAAALEALGYNKKEIAKSLKHVNFDQDLNKALKEALAILLK | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q6F992 | MIGCLIGEVFALEAPTVLLNVNGVGYEIDTPLSTFCQLQKGQHVTLWTHLVVREDAQQLYGFIDAQEKLIFRTLLKVNGVGPKMALGILSTLSIELFIHTIEHDDINTLIKVPGVGRKTAERLMIELRDRFKALSVQATTGSTVTSAQIQFSSNSPIAEAEAALQSLGYKPIEAQKAIAAVKADYTEAADLIRAALKSMMK | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q483C5 | MIGRLRGMLVEKNSPEILIECAGVGYEVTMPMTSIYALPELEQQATIYTHFVVREDAQLLYGFANKVERKLFRLLIKVNGVGPKLALAILSNMSADQFVSCVRHDDISAIVKIPGVGKKTAERLLIEMRDRLKDWQAQQIHLVSDDGVIPEQLSAELSQETTFVNDNKGDAINALLSLGYKQVQADKAVKSVYNRGMSSENIIRDALKSMI | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q6NGX4 | MIVSLRGTVESIGLGSAVIECNGVGYEVLAAPTTLGRLTRGEQARVLTTMVVREESQTLYGFTDDASRRMFVLLQSVSGLGPKLALAAQSVFTTEDIARHIAGGDAKALQKIPGVGKRMAERMIVDLKDKVVGFNDGIPAAAQPQLSIAVDQAVQEQVLEALVGLGFSEKIALPVLSRVLRDSPELSKSQALRAALSELGTKN | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q9AE10 | MIASLRGTVINIGLSSAVIECNGVGYEVVTTPNTLSQLVRGEEALVLTTMVVREDAMKLYGFIDNESREMFSVLQTVSGLGPRLALACESVLSPLEISQAITNADAKTLQRVPGVGKRMADRLIVELKGKVAAFAAGVVDEGGEQISLPNANIASEVVVEQVSQALVGLGFSEKQSDDAVSFVLAADPSLDTSGALRAALAKLSGK | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q4JVD8 | MIASLRGTVIDKGLDYVTIECAGVGYQCSGTATTIAELPRGEEVFVTTALVVREDSQTLYVFKDADEKRAFATLQSVSGVGARLALAILSVITPQELARAVSNGDHKTLQRAPGVGKRLAERMAVDLKGKVADLGEIADTGAVGAAGAVGDGGDGQAVAPDVREQVLEALVGLGFTESKAGTTIEAVLSQWSAPQAPDASGLLRASLAAIK | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
C4LIX8 | MIDSLHGEVLHVGLNYVVIECSGVGYRATASPSLLGTLRKGEDARILVTMNVRDDGIDLYAFESDEARQMFAMLRKVSGVGPTSAMAICSIFKPDEFARIITDEDDAELRNVKGIGKRTAERIIVDLKSKVAVFDSGDSASEPQSGVGGNSEAEVDSGVVGTVTQALVELGFPEKQAEKTATSAAAEGGSVSEILKRALRSMSSERN | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
C6C065 | MIAYIHGKLLEATDKSCIILTPGGVGYELFLTLSAISTLPESGSDVTFYVHSVIREDAFDLYGFPCFDDREVFRTLISVDRLGPKKALAILSQFGPKDLQDLVFREDVKTLSIVPGIGPKSARQILWSLKDKMETLKSATVRSGACPVEGDRSEFLDALSGLRNLGYGDDEVRDFLKDIFDEEPDLDAGGAIRVALKKISQNK | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q4A9R7 | MQIYQFGKIVSKNKNYLILENHGSGYLIYVPRIDRFSRDENRKIYIYEHENDYTKITYGFASFRERILFEDLISIQGVGPKTAISALNSGMQNLINLIAANDWKTLAKIPYLSEKNAKQIVFEFQKKYERFNENHKNQTEETNQDSQEKELEKKDDLADITIQKSNLEDKTAANLEDTLKMLGFKPRQIDYALTKVEPNENFENLIENAIKIISNAREFRN | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
B3PMK3 | MIIYKYGKIMHVNTNYLILDHNGEGDLIYAPNISRFKKDELRKIFISQIENEYTKVTYGFDNFKELVIFEDLIEIQGLGPKTAISILNIGWENVINYVATANKGALGKIPYVSSKIANAIIFSYQDKYAKFMKKLTSDEAAKIKVPASSENENKFLDTMKMLGFKQQQIKFALDKIELNDDIETCVENAIKLISQQQHETSRV | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q609L1 | MIGFIRGLLVAKRAPSLLIDVQGLGYELDAPMSTFYNLPEIGAEVRLYTHLQIREDAHSLFGFGTEAERGLFRSLIRVSGIGAKLALAILSGISVDDFRACVERQDSARLVRLPGIGKKTAERLIIELRDRLDIGVPSLAPASFAGGAAPLPAADPADEAVSALIALGFKPQEANTLVARQAAEGRSAEDLIRAALQSAVR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
B0JRV0 | MINYLRGQAIEVIKTPNNRLILILDVNQIGYEIQIPSRLALDIGNNNNDSCQIFTHLLLREEQPLLYGFGTAPERELFRQLLSVNGVGAQLALALIDTLGIEELVVAIVTGNTKILSKTPGVGLKTAERIALELKTKLAAWRQLREATTTITAILPAAAILEDVQMTLLALGYSQEEIDRAMAVLSQDALFSKNTQPEDWIKGAINWLG | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
C5CCI2 | MIASLSGTVEHVALDRAVIAVGGLGVQFSATPQTLSTLHEGRPGAVQTHLVVKEDALTLYGFADRDEREVFEVLITANGVGPRLALAILSVHHPETVRRAVTEEDEKTLTRVPGIGPKMARKIIVELSGRLAPTGEPVPGAEAEASDEPAVETVWHADVVQAMAGLGWSEKEALKAVEATVAARPELDEGRDVAALLRATLRDVGMAGAVRGGR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q2RHT6 | MIGYLRGRLHLVTPEGILLETGGIGWLVRTVTNRSWPAPGTEIAVYTQLVVREDAMELYGFTRPEELHLFTLLRGVNGIGPRGALQILGAAKPEQLSRAIAAGDSAFLTALPGIGAKKAQRLLLELKDAVLKSGLVDGTETEAIPAGGGDNDEALAALLALGYSREEIGPILARVRQELGNAAPTTAVLQAVLKTFGRGGGD | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A5IY12 | MILYRIGEIIHKHNSNIIFESQGIGYSLILPDPERVEIKQKCKLYLFEIKNEYQYATYAFKDFKERLLFVDLISLNGIGPRAAFNILNFGFEKVVALIAEGNAEALIEIPYLNPRMARLIVAELQAKWSKMISPKDAAKINETTNTLSEVKETLKMVGFKTKQIDGALSKISSTDDVEKMIEEAIKLMSTQNYESATA | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q2S5C8 | MIDYVSGTLVDKTTDSALVDVNGLGYRVHVPTSTYKRLPDTDEEVTLHTYHYLREDDESLYGFATKAERTVFETMTGVSRVGPKLALSALSAMTPTELRDHVMEGDKSRLTQISGVGTKTADRLIVELRDRLADLDVLEDTSPLSGGSDARAEARADALEALTELGLSKADAERSIRQVLRDNAGIQSADELVRRALKADQE | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A4X5X2 | MIASVRGVVTATGPDHAVLEVGGVGLAVQCAPGTIADLRVGQPARLATSLVVREDSLTLYGFADDDAKALFELLQTASGVGPRLAQAVLAVHPPEAVRAAIANADTAALTRVPGIGKKGAERLVLELRDRIGPVPVGADSAAGVTTGAWPEQVRQALVGLGWTAAQADQAVTAVAETVDGAVPPVPVLLRQAIRLLGRTR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q12N09 | MIGRLNGILVEKHAPEIVLDVGGVGYELQVPMTSFYELPELEQSATLYTHFVVREDAQLLYGFITKQERALFRLLIKTNGVGPKLALTILSGMTAGEFVSCVERDDIVTLVKLPGVGKKTAERLVVEMRDKLKSLLEASVGNEREFMLQTNYTAPAANAEEDAISALVSLGYKPPQASRAVSKAYKEGMDTETLIKLALKSML | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q8U9K6 | MSDADRLITPEKRGEDIDTTLRPQSLDDFTGQAEARANLKVFIEAAKNRGEALDHVLFVGPPGLGKTTLAQIMAKELGVNFKSTSGPVIAKAGDLAALLTNLEERDVLFIDEIHRLNPAVEEILYPAMEDFQLDLIIGEGPAARSVKIDLSKFTLVAATTRLGLLTTPLRDRFGIPVRLAFYTVDELELIVRRGARLMGLNMTDGGAREIARRARGTPRIAGRLLRRVRDFAEVARAEAVTREIADEALTRLLVDNMGLDQLDMRYLTMIAVNFGGGPVGIETIAAGLSEPRDAIEDIIEPYMIQQGFIQRTPRGRILTA... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q9X719 | MTAPENLDAALRPKTLTEYVGQEKLKDKLGVYLQAARGRREALDHTLLFGPPGLGKTTLAHIIAYELGVNIRVTSGPAIEKPGDLAAILTNSLEEGDVLFIDEIHRLGRVAEEHLYPAMEDFKLDIVLGQGPAARTIELPLPRFTLVGATTRPGLITAPMRSRFGIIEHLEYYTAEEIATNLLRDARLLGFGLDEEAGLEIGARSRGTMRIAKRLLRRVRDYADVAGETTIGLERAQSALDKLGLDSAGLDDRDKKYLETLIHRFAGGPVGVDTLATAISEDALTLEDVYEPYLIQLGFIKRTPRGRVATAHAYDHLGLP... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
C0QKP4 | MSDGILSFSSKNDKRGETSGKELITPSSQPVDDSSEVVSLRPDRFESYVGQTDTVETLKIAIQAAKMRGDCLDHVLLHGPPGLGKTTISHIIANEMGGTLTVTSGPALEKGGDLIGMLTNLARGDILFIDEIHRLPKTVEEFLYPAMEDFAVDFVFDKGLHARSHRYRLKQFVLVGATTRVGLISSPLRDRFGIFRSLDFYTDEELVTIIRRSAGLLNVVLDDGAALELARRSRGTPRIANRLLKRVRDFSMVRSSGEVTQKSVAAALSLEGIDSKGLTVLDRNYLRTIIEFYRGGPVGIEAVAATLQEETDTLVDVVEP... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
B7USN7 | MIEADRLISAGTTLPEDVADRAIRPKLLEEYVGQPQVRSQMEIFIKAAKLRGDALDHLLIFGPPGLGKTTLANIVANEMGVNLRTTSGPVLEKAGDLAAMLTNLEPHDVLFIDEIHRLSPVVEEVLYPAMEDYQLDIMIGEGPAARSIKIDLPPFTLIGATTRAGSLTSPLRDRFGIVQRLEFYQVPDLQYIVSRSARFMGLEMSDDGALEVARRARGTPRIANRLLRRVRDFAEVKHDGTISADIAAQALDMLNVDAEGFDYMDRKLLLAVIDKFFGGPVGLDNLAAAIGEERETIEDVLEPYLIQQGFLQRTPRGRMA... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q97SR6 | MSRILDNEMMGDEELVERTLRPQYLREYIGQDKVKDQLQIFIEAAKMRDEALDHVLLFGPPGLGKTTMAFVIANELGVNLKQTSGPVIEKAGDLVAILNDLEPGDVLFIDEIHRLPMSVEEVLYSAMEDFYIDIMIGAGEGSRSVHLELPPFTLIGATTRAGMLSNPLRARFGITGHMEYYAHADLTEIVERTADIFEMEITHEAASELALRSRGTPRIANRLLKRVRDFAQIMGNGVIDDVITDKALTMLDVDHEGLDYVDQKILRTMIEMYSGGPVGLGTLSVNIAEERETVEDMYEPYLIQKGFIMRTRSGRVATAK... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q3ABX8 | MKIIGIDPGTAIVGVGVLEKKNGKLIVKNFQAITTPPIAKEKRLKIIFQKLNEILIQEKPEIVVVEELFFSKNVKTAISVGEARGVVLLASALNDIPVLELKPVEVKTIVTGYGHAPKSQVEYMIAKLLGLKTPPKPDDVADALAIAYAGFLKMGGLL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q9A3G6 | MMNANRLPTRILGLDPGLRRTGWGVLAVEGSRMTHIAHGVITPDEKAEFADRLLHLFEGITAVIEQHRPDEAAVEEVFLNTNAQSTLKLGHARAAALIAPARAGLLVAEYSTRLVKKAVVGTGAADKAQIGFMIARLLPTAGKTTADCADALAVAITHANLRVANRRVA | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
A9WIH6 | MRALGIDPGTATMGWGIVEFNNGHLRLIDVGALTTPAGMPHPERLLQLYNGLRAIIERLRPDTAAVEELFFGKNVNTALTVGQARGVALLALAQAGIPVHEYKPLAVKQAVAGYGGADKRQMQEMVRLTLGLATIPRPDDAADALAIAICHAYTAPTLQRFGLS | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q3AU83 | MIVLGVDPGSLKTGYGVVQHHNGSFSVLAAGVIRLQAAWSHPERIGIICRELEQVIAEFQPERVALETAFLSHNVQAALKLGQVRGAVIGLVVRYALPIYEYAPREVKSAITGKGAATKEQVAFMVSRMLSLHTVPKPHDVTDALGIALCDILRGESRQSGVPPRTNSRRKSGTGGSWEQFVRQSPNVVVRS | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q9JTU3 | MSATVRILGIDPGSRVTGFGVIDVRGRDHFYVASGCIKTPADAPLADRIAVIVRHIGEVVTVYKPQQAAVEQVFVNVNPASTLMLGQARGAALAALVSHKLPVSEYTALQVKQAVVGKGKAAKEQVQHMVVQMLGLSGTPQPDAADGLAVALTHALRNHGLAAKLNPSGMQVKRGRFQ | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q2GCH7 | MSYVALGVDPGLLRTGWAVVEYDGLCNVRYIDSGIVKTASQGSLSARLEKIHRGISDVIEKVNPSVAVLEKVFVNNNPYSSLNLAYCRGALILTLALKGLFIVEFAPSVLKKRITGNGRATKAQVKYMVEQLLGLDPCLSKYSDLYDALALAASVTRYDIMEAKGT | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q82XP5 | MTSLVYAAKGIRILGIDPGLRITGFGIVEKIGNRLVYIGSGCVVTGESGLPDRLKTILDGLNEIILQHKPEQVAVEQVFVNINPKSTLLLGQARGAAISAAVLHELSVYEYTALQVKQAVVGNGHARKEQVQEMVMRLLGLGERPRPDAADALACAICHAHGGTGLLTLSARNRSKRSKRL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q1QHP5 | MTSSPIRILGIDPGLRRTGWGVLDIEGNRLMFVGCGSVETREQMALASRLLAIHEGLGRVLDEFRPAEAAIEQTFVNKDGVATLKLGQARGVAMLAPAMFGIVVAEYAPNQVKKTVVGAGHADKTQIQAMLKILLPKADPKSADAADALAIAITHAHHRGAAALRMKVAG | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q3JES5 | MARILGIDPGSRITGYGLIETNNKKTVYIAAGCIRAGEGGLAERLGQIFQGITGIIQAYHPDEVAVEQVFMHQNPGSALKLGQARGAAICAAVNAVLPIFEYTPSQVKQAVVGRGDAAKSQVQYMIRLLLKLPAEPATDAADALACALCHEHAGPLLAGLAGQVRGRRRGRYYR | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q5YTE6 | MRVMGVDPGLTRCGLSMVEGGHGRTVTALDVDVVRTPADMDLAHRLMLVADAAEYWMDTHRPGAVAIERVFAQHNVRTAMGTAQAGGVIALAAARRDIPVVFHTPSEVKAAVTGNGNADKAQVTAMVTRILGLQTAPKPADAADALALAICHCWRAPLLARMAAAEAKAAEAKRRYTERLAEQRKAVRG | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
B2J4H5 | MEKRILGLDPGLATLGFGVITCTQIANKVPETTVNMLDFGVIKTSADVEMGLRLCTLFDDLHTVMEEFQPDLVAIEKLFFYRMSSTILVAQARGVLILVLGQRRLPYVEFTPAQIKQALTGYGNADKLDVQEAVARELDLDEIPKPDDAADALAVALTASYQL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
O52751 | MEKRILGLDPGLAILGFGAITCTPGLTQLQSTKVNVLDFGVIKTSADIEIGQRLCTLFDDLHTVIDQLQPDVVAIEKLFFYRMSSTIVVAQARGVVMLALAQHHLPYVEFTPAQIKLALTGYGNADKSEVQEAVARELDLAEIPRPDDAADALAVALTAWYQM | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
A5CES8 | MIILGIDPSLVSTGWGVISISDSMVNYIDSGVIKTVSKDSLVLKLGNISLMIEKLITRFNPFHVAMEEVFINKNYSSSVTLIQARGAIMSVIGRYNIDFSEYAPNKIKKAIVGAGKAEKHQVQQMVKLLMHIKKAISKDESDALATAYTASVNQQIKII | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q0WW17 | MASSSPVTPGLMSVVFGIVPVIVAWLYSEYLHYAKYSVSAKTRHSDVNLVEIAKDFVKEDDKALLIEDGGGLQSASPRAKGPTTHSPLIRFVLLDESFLVENRLTLRAIIEFAVLMVYFYICDRTDVFNSSKKSYNRDLFLFLYFLLIIVSAITSFTIHTDKSPFSGKAIMYLNRHQTEEWKGWMQVLFLMYHYFAAAEYYNAIRVFIACYVWMTGFGNFSYYYIRKDFSLARFAQMMWRLNFLVIFSCIVLNNSYMLYYICPMHTLFTLMVYGALGIMSKYNEMGSVIAAKFFACFVVVIIVWEIPGVFEWIWSPFTLL... | Function: Probable O-acetyltransferase involved in the acetylation of cell wall polymers (both pectic and nonpectic polysaccharides) and of xylan during secondary wall biosynthesis. Catalyzes the O-acetylation of xyloglucan.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63612
Sequence Length: 545
S... |
Q66GQ5 | MADSQPITPGQVSFLLGVIPVFIAWIYSEFLEYKRSSLHSKVHSDNNLVELGEVKNKEDEGVVLLEGGLPRSVSTKFYNSPIKTNLIRFLTLEDSFLIENRATLRAMAEFGAILFYFYISDRTSLLGESKKNYNRDLFLFLYCLLIIVSAMTSLKKHNDKSPITGKSILYLNRHQTEEWKGWMQVLFLMYHYFAAAEIYNAIRVFIAAYVWMTGFGNFSYYYIRKDFSLARFTQMMWRLNLFVAFSCIILNNDYMLYYICPMHTLFTLMVYGALGIFSRYNEIPSVMALKIASCFLVVIVMWEIPGVFEIFWSPLTFLLG... | Function: Probable O-acetyltransferase involved in the acetylation of xylan during secondary wall biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63331
Sequence Length: 540
Subcellular Location: Golgi apparatus membrane
EC: 2.3.1.-
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Q9FXG3 | MVVSQPITPGQVSFLLGVIPLMIAWLYSEFLEYRRSSFHAKVHSDKNLVELEMVTNKEDEGTVLMEGGLPRSASSKFYSSPIKTNLIRFLTLEDSFLLENRATLRAMAEFGAILLYFYICDRTSLIGQSQKNYSRDLFLFLFCLLIIVSAMTSLKKHTDKSPITGKSILYLNRHQTEEWKGWMQVLFLMYHYFAAVEFYNAIRVFIAGYVWMTGFGNFSYYYIRKDFSLARFTQMMWRLNFFVAFCCIILNNDYMLYYICPMHTLFTLMVYGALGIYSQYNEIASVMALKIASCFLVVILMWEIPGVFEIFWSPLAFLLG... | Function: Probable O-acetyltransferase involved in the acetylation of xylan during secondary wall biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63313
Sequence Length: 540
Subcellular Location: Golgi apparatus membrane
EC: 2.3.1.-
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A3KN24 | MAEPVRQELSALAAIFCGPDEWEVLSLSETDGAVFRILTKAEGFMDTDIPLQLVFHLPLSYPYCLPGIVVNSKHLTRAQCEIVKEKLLEQAETLLLEPMVHELVLWIQENLRHILKCPEAGGGSEKCSSAASMTVDDGLWMTLLHLDHMRAKAKYVKTVEKWASDLRLTGRLMFMGKIILILLQGDRNDIKEYLILQKTCKVDVDSSGKKCKEKMISVLFETKVQTEHKRFLAFEVKEYSSLDELQKEFETTGLKKLFSECVLRLVK | Function: Enhancer of SUMO conjugation. Via its interaction with UBE2I/UBC9, increases SUMO conjugation to proteins by promoting the: binding of E1 and E2 enzymes, thioester linkage between SUMO and UBE2I/UBC9 and transfer of SUMO to specific target proteins which include HIF1A, PIAS, NFKBIA, NR3C1 and TOP1. Positively... |
Q6PBV4 | MSKEAFDELSVLSAIYCEQGEFEVLEESPEKGVVFRVHTLIDNNEKTPLDIIFHISPEYPNTPPDISISSNHLSRRQCHDLRRSLLDTAQSLPAEPMVHGLMLWLQENFSDLIKTSSCHSAEVRPETTEETWTALLHLDHMRSKAKYIKLIEKWTLELRLTGRLFTGKLILILLQGTKENIKQYIHLLKSVKVDVDSSGKRCKEKMMSVLCEIPKPEDKIMMTTFEVKDILSLDDLRREFDLIGLNELYHQFVSSLT | Function: Enhancer of SUMO conjugation. Increases SUMO conjugation to proteins by promoting the: binding of E1 and E2 enzymes, thioester linkage between SUMO and ube2i/ubc9 and transfer of SUMO to specific target proteins which include hif1a, pias, nfkbia, nr3c1 and top1. Has no effect on ubiquitination (By similarity)... |
Q9Y3V2 | MAEPVQEELSVLAAIFCRPHEWEVLSRSETDGTVFRIHTKAEGFMDVDIPLELVFHLPVNYPSCLPGISINSEQLTRAQCVTVKENLLEQAESLLSEPMVHELVLWIQQNLRHILSQPETGSGSEKCTFSTSTTMDDGLWITLLHLDHMRAKTKYVKIVEKWASDLRLTGRLMFMGKIILILLQGDRNNLKEYLILQKTSKVDVDSSGKKCKEKMISVLFETKVQTEHKRFLAFEVKEYSALDELQKEFETAGLKKLFSEFVLALVK | Function: Enhancer of SUMO conjugation. Via its interaction with UBE2I/UBC9, increases SUMO conjugation to proteins by promoting the binding of E1 and E2 enzymes, thioester linkage between SUMO and UBE2I/UBC9 and transfer of SUMO to specific target proteins which include HIF1A, PIAS, NFKBIA, NR3C1 and TOP1. Isoform 1 a... |
A9ULH0 | MSESALEEVAALSAIYCRDGECEVLSSSVNGITVMIQTGVQGITGSEIHLKLIFDLPVEYPSSLPNISVSSEELTRAQRKDLRDKLVEQAKQHILEPMIHDLVVWTQQNLNNLIVQPEPSILEGHFPLSLDTITEETTWTILLRLDHMRAKSKYVKTVEKWTNDLKLCGRLMFLGKLILILLQGDRKSTRDYLVLQKTCKVDVDSSGKKCKEKMISVLCETILPLKQKRFTTFEVKEYSSVSDLQKEFEAAGLQTIFSEFVQALF | Function: Enhancer of SUMO conjugation. Increases SUMO conjugation to proteins by promoting the: binding of E1 and E2 enzymes, thioester linkage between SUMO and ube2i/ubc9 and transfer of SUMO to specific target proteins which include hif1a, pias, nfkbia, nr3c1 and top1. Has no effect on ubiquitination (By similarity)... |
P05109 | MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETECPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE | Function: S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The int... |
P27005 | MPSELEKALSNLIDVYHNYSNIQGNHHALYKNDFKKMVTTECPQFVQNINIENLFRELDINSDNAINFEEFLAMVIKVGVASHKDSHKE | Function: S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The int... |
P50115 | MATELEKALSNVIEVYHNYSGIKGNHHALYRDDFRKMVTTECPQFVQNKNTESLFKELDVNSDNAINFEEFLVLVIRVGVAAHKDSHKE | Function: S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The int... |
P28783 | MEDKMSQMESSIETIINIFHQYSVRLGHYDTLIQKEFKQLVQKELPNFLKKQKKNEAAINEIMEDLDTNVDKQLSFEEFIMLVARLTVASHEEMHNTAPPGQGHRHGPGYGKGGSGSCSGQGSPDQGSHDLGSHGHGHGHSHGGHGHSHGGHGHSH | Function: S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/2... |
P06702 | MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP | Function: S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response . It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/... |
P31725 | MANKAPSQMERSITTIIDTFHQYSRKEGHPDTLSKKEFRQMVEAQLATFMKKEKRNEALINDIMEDLDTNQDNQLSFEECMMLMAKLIFACHEKLHENNPRGHGHSHGKGCGK | Function: S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response . It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/... |
P50116 | MAAKTGSQLERSISTIINVFHQYSRKYGHPDTLNKAEFKEMVNKDLPNFLKREKRNENLLRDIMEDLDTNQDNQLSFEECMMLMGKLIFACHEKLHENNPRGHDHSHGKGCGK | Function: S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response . It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/... |
P31949 | MAKISSPTETERCIESLIAVFQKYAGKDGYNYTLSKTEFLSFMNTELAAFTKNQKDPGVLDRMMKKLDTNSDGQLDFSEFLNLIGGLAMACHDSFLKAVPSQKRT | Function: Facilitates the differentiation and the cornification of keratinocytes.
PTM: Phosphorylation at Thr-10 by PRKCA significantly suppresses homodimerization and promotes association with NCL/nucleolin which induces nuclear translocation.
Sequence Mass (Da): 11740
Sequence Length: 105
Subcellular Location: Cytopl... |
P50543 | MPTETERCIESLIAVFQKYSGKDGNNTQLSKTEFLSFMNTELAAFTKNQKDPGVLDRMMKKLDLNCDGQLDFQEFLNLIGGLAIACHDSFIQTSQKRI | Function: Facilitates the differentiation and the cornification of keratinocytes.
PTM: Phosphorylation at Thr-5 significantly suppresses homodimerization and promotes association with NCL/nucleolin which induces nuclear translocation.
Sequence Mass (Da): 11083
Sequence Length: 98
Subcellular Location: Cytoplasm
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Q62866 | MVPTGQVAEKQACEEPRQDRELKSWRWLVFYLCFFGFMAQLRPGESFITPYLLERNFTKEQVTNEIIPMLPYSHLAVLVPIFLLTDYLRYKPVLVLQCLSFVCVWLLLLLGTSVVHMQLMEVFYSITMAARIAYSSYIFSLVQPSRYQRMASYSRAAVLLGVFISSVLGQVLVTLGGISTYMLNCISLGFILFSLSLSLFLKRPKRSLFFNRSALVQGALPCELDQMHPGPGRPEPRKLERMLGTCRDSFLVRMLSELVKNVRQPQLRLWCLWWVFNSAGYYLITYYVHVLWKITDSRLNYNGAVDAASTLLSAITAFTA... | Function: Antiporter that mediates the import of reduced folates . Mechanistically, acts as a secondary active transporter, which exports intracellular organic anions down their concentration gradients to facilitate the uptake of its substrates (By similarity). Has high affinity for N5-methyltetrahydrofolate, the predo... |
O60779 | MDVPGPVSRRAAAAAATVLLRTARVRRECWFLPTALLCAYGFFASLRPSEPFLTPYLLGPDKNLTEREVFNEIYPVWTYSYLVLLFPVFLATDYLRYKPVVLLQGLSLIVTWFMLLYAQGLLAIQFLEFFYGIATATEIAYYSYIYSVVDLGMYQKVTSYCRSATLVGFTVGSVLGQILVSVAGWSLFSLNVISLTCVSVAFAVAWFLPMPQKSLFFHHIPSTCQRVNGIKVQNGGIVTDTPASNHLPGWEDIESKIPLNMEEPPVEEPEPKPDRLLVLKVLWNDFLMCYSSRPLLCWSVWWALSTCGYFQVVNYTQGLW... | Function: High-affinity transporter for the intake of thiamine . Mediates H(+)-dependent pyridoxine transport .
Catalytic Activity: H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55400
Sequence Length: 497
Subcellular Location: Cell membrane
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Q9EQN9 | MDVPARVSRRAAAAAARMLLRTARVPRECWFLPTALLCAYGFFANLRPSEPFLTPYLLGPDKNLTERQVYNEIYPVWTYSYLLLLFPVFLATDYLRYKPVILLQGLSLIVTWFMLLYAQGLLAIQFLEFFYGIATATEIAYYSYIYTVVDLGMYQKVTSYCRSATLVGFTVGSVLGQILVSVVGWSLFSLNVISLTCVSVAFAVAWFLPMPQKSLFFHHIPSSCHGVNGLKVQNGGIVTDTPAANHLPGWEDIESKIPLNLDEPPVEEPEEPKPDRLRVFRVLWNDFLMCYSSRPLLCWSVWWALSTCGYFQVVNYAQGL... | Function: High-affinity transporter for the intake of thiamine . Essential for spermatogenesis . Mediates H(+)-dependent pyridoxine transport .
Catalytic Activity: H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55676
Sequence Length: 498
Subcellula... |
Q9BZV2 | MDCYRTSLSSSWIYPTVILCLFGFFSMMRPSEPFLIPYLSGPDKNLTSAEITNEIFPVWTYSYLVLLLPVFVLTDYVRYKPVIILQGISFIITWLLLLFGQGVKTMQVVEFFYGMVTAAEVAYYAYIYSVVSPEHYQRVSGYCRSVTLAAYTAGSVLAQLLVSLANMSYFYLNVISLASVSVAFLFSLFLPMPKKSMFFHAKPSREIKKSSSVNPVLEETHEGEAPGCEEQKPTSEILSTSGKLNKGQLNSLKPSNVTVDVFVQWFQDLKECYSSKRLFYWSLWWAFATAGFNQVLNYVQILWDYKAPSQDSSIYNGAVE... | Function: Mediates high affinity thiamine uptake, probably via a proton anti-port mechanism . Has no folate transport activity . Mediates H(+)-dependent pyridoxine transport .
Catalytic Activity: H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55665... |
Q99PL8 | MDSSCRTPPSNSWVYPTVILCLFGFFSMFRPSEAFLIPFLSEPSKNLTSPEMTNEILPVWTYSYLATLPPVFVLTDYLRYKPVIMLHVVAFATSYLFLLFGQGVMLMQTAEFFFGVVSATEIAYFAYIYSMVSPEHYQKVSSYCRSITLVAYTAGSVLAQLLVSLTNLPYSSLFYISLACVSVAFFFSLFLPMPKKSMFFHAKSDRDDCPKPLEQCTVPKEAQSNRTHSELFANSKNLEDREMSNPDPENSALRHFAHWFQDLKECYSSKHLVYWSLWWAFATAGYNQILNYVQVLWEHKAPSQDSSIYNGAVEAIATFG... | Function: High-affinity transporter for the intake of thiamine . Unlike the human ortholog, lacks H(+)-dependent pyridoxine transport activity due to an absence of seven critical amino-acids required for pyridoxine transport .
Catalytic Activity: H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in)
Location Topology: Mu... |
Q8N4F4 | MGFDVLLDQVGGMGRFQICLIAFFCITNILLFPNIVLENFTAFTPSHRCWVPLLDNDTVSDNDTGTLSKDDLLRISIPLDSNLRPQKCQRFIHPQWQLLHLNGTFPNTNEPDTEPCVDGWVYDRSSFLSTIVTEWDLVCESQSLKSMVQSLFMAGSLLGGLIYGHLSDRVGRKIICKLCFLQLAISNTCAAFAPTFLVYCILRFLAGFSTMTILGNTFILSLEWTLPRSRSMTIMVLLCSYSVGQMLLGGLAFAIQDWHILQLTVSTPIIVLFLSSWKMVESARWLIINNQLDEGLKELRRVAHINGKKNTEETLTTELV... | Function: Renal transmembrane organic anion/dicarboxylate exchanger that participates in the reabsorption of conjugated steroids including estradiol-17beta-D-glucuronide (or 17beta-estradiol 17-O-(beta-D-glucuronate)), androstanediol glucuronide (or 5alpha-androstane-3alpha,17beta-diol 3-O-(beta-D-glucuronate)), and es... |
A0A8B7HA97 | MAFAVLLDQVGSLGRFQILQLAFLCIANILLFPHILLENFTAAVPGHRCWVHILDNDTVSHNDTGTLGQDALLRISIPLDSNLKPEKCRRFVHPQWQLLHLNRTFSNTSEPDTEPCVDGWVYEQSSFFSTVVTEWDLVCEWESQKSVVQSLFMAGSLLGSVIFGYLSDRFGRKMICSWCLLQLAISDTCAAFAPTFSVYCSLRFLAGSCVMTIMGHSFLLVIEWTNPQSRSMVTTLLLCASSVGQMLLGGLAFVIQDWRTLQLTVSIPIFVIFLSSRWLVESARWLITYNQLDKGLKELRRAARINGKKNAGEILTIEFL... | Function: Renal transmembrane organic anion/dicarboxylate exchanger that participates in the reabsorption of conjugated steroids, as well as bile acids, driven by an outward gradient of dicarboxylates such as glutarate or succinate (By similarity). Transports androstanediol glucuronide (5alpha-androstane-3alpha,17beta-... |
G1SZD9 | MGFDVLLDQAGSLGRFQILQIAFFFVTSMITYTHILLENFTAAIPGHRCWVPLLDNHTTSGNDSDILSQDALLRVSIPLDSNLRPEKCRRFIHPQWQLLYLNGTSPSTNEPDTEPCVDGWVYDQSSFSSTIVTKWDLVCEFQSLKSVVQTLFMSGSLLGGLMFGRLSDRYGRKAIYTWCLLQTAIADTCAIFAPTFVVFCIFRFLAGLTTINIMTNAFILATEWTVPKLQYIGITLILCSYSIGQMLLGGLAFAIRDWYTLHLTVSIPLFVLSLLSRRLVESARWLVTTNQLDEGTKALRRVARINGKKSAGEILTIEFV... | Function: Renal transmembrane organic anion/dicarboxylate exchanger that participates in the reabsorption of conjugated steroids, as well as bile acids, driven by an outward gradient of dicarboxylates such as glutarate or succinate (By similarity). Transports androstanediol glucuronide (5alpha-androstane-3alpha,17beta-... |
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