ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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|---|---|---|
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: 2.1.1.170
|
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: 2.1.1.170
|
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: Cytoplasm
EC: 2.1.1.199
|
B7J3W0 | MRSANEPDATHVAVLLAETIVALRPALHTGAAVRCVDATGGRGGHSAALLAELGAADTLLILDRDPSAIAALRARFAQDSRVYIRQARFSQLAEVLAALEWERVDAILADLGVSSPQLDEAARGFSFLRDGPLDMRMDPGADRSAAEWLATATEADMTRVLREYGEERFARPIARAILRAREQAPITRTLQLAELIAQVLPRHETGQHPATRSFQGIRIFINRELEELEAFLPQAMNALRAGGRLAVISFHSLEDRLVKRFFRADDYRISADVPLRASELPPLPWHPAGKALRAGPRETRDNPRSRSAVLRVAERSERHAA | 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: Cytoplasm
EC: 2.1.1.199
|
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: Cytoplasm
EC: 2.1.1.199
|
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: Cytoplasm
EC: 2.1.1.199
|
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: Cytoplasm
EC: 2.1.1.199
|
Q8NNM7 | MEDFSLDGNHGHVPVMRDRMAALIAEHVEALGENAVIVDATLGAGGHAEFFLNTFPKARLIGLDRDQNALRDARARLAPFGERFIGVQTRFDGLREVLESVEGDIIDLAREHGIAGALFDLGVSSMQLDQVERGFAYRTDAPLDMRMDATQGITAADILNTYSHGDIARILKTYGDERFAGKIASAVLKEREKEPFTTSARLVELLYDAIPAATRRTGGHPAKRTFQALRVEVNNELDSLKNVLPQITDALNVGGRAVFMSYQSHEDKLVKKFFTDLTTSKTPPGLPVDLPGTAPQFKQVTRGAETASEAEIEENPRAAPVKVRAIERIGNNSGDLS | 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: Cytoplasm
EC: 2.1.1.199
|
C4LI42 | MADRHTGTHGHVPVMLERMVELIAPTVTESSENSAPSVILDGTLGAGGHTESFLERFPSAMVIGVDRDKKELSRTTERLSRFQDRFYPVHARFDNFDEALDDADHPVVDAFDAHGLSAGFFDLGVSSMQLDQVDRGFTYRDDGPLDMRMDTSTGKTAADVLNTYSHGELARILKTYGDERFAGPLARAIVREREKEPWSTSQRLVDLIYATIPASARRHGGHPAKRTFQALRVEVNAELDALRRVIPKVCSYLHLGGRAVFMSYQSLEDKIVKRELAALTESKTPPGLPIDLPNSAPDFHLVTRGSEKADEQENNKNPRAHSVRVRAVERTGYSHSSPPPGSTPARASGSSTTYSARSGSRHEAHREGREHLVSSAQQSISHREDVEGEQ | 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: Cytoplasm
EC: 2.1.1.199
|
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: Cytoplasm
EC: 2.1.1.199
|
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: Cytoplasm
EC: 2.1.1.199
|
B8IMX2 | MSGMPPHIPVLLKEVRSALRLGEGPGIVVDGTFGAGGYTRAILEADPGQRVIAIDRDPTAIATGRGLAAAMAGRLMLVQGRFGELDRLVRAQGIETVDGVVLDIGVSSMQLDQAQRGFSFRQDGPLDMRMESGGTSAADLVNEASEAELADIIYHYGEERRARAVARAILEARRRGRIATTATLAEIVASVVRPEPGSGIHPATRTFQALRIAVNDELGELQRALHAAERILRPGGRLAVVTFHSLEDRIVKQFFSARSGRAVSASRHLPMAEKPAPRSFTLVTKGPIGPSEAEATANPRARSAKLRAGERTDAPIPEPLTALAALAALPSRERGGGRR | 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: Cytoplasm
EC: 2.1.1.199
|
B1LYT9 | MSRRRPAPESSPRHDGADAPPEPHVPVLLAEVVEALGTEGGTAVDGTFGAGGYTRALLAADPALQVVAIDRDPTAIAGGQALVAESGGRLRLLPGRFGDLDGLLAEAGIAQVDRVVLDIGVSSMQLDAPERGFSFRSDGPLDMRMACDGPSAADLVNEADETVLADIIYHFGEERRSRAVARTILEARRRGRIETTAQLAELVAGVVRTEPGSHIHPATRTFQGLRIAVNDELGELVRALHAAERVLRPGGRLAVVTFHSLEDRIVKQFFAARSGRSAQGSRHLPGGPVETVRSFRPVTKGPVLPGEAETARNPRARSAKLRAAERTESDVPEPLAALTALASLPDAARGHRR | 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: Cytoplasm
EC: 2.1.1.199
|
C5CA38 | MDAGQPRPEDRHLPVMRDRVVDLLAPAVQAALEAGRTPVAVDGTLGMGGHTEALLTRFPHLRVIGIDRDAHAQAMAAERLGPLADRVIPFHGTYDRVPEAMAAAGVTKVDAALYDLGVSSYQLDDRERGFAYSYDAPLDMRMDDTAERSAATLVAELDEQELRRIIRRDGEERFAGPIARAIVRARAEAPIETTGRLVEVIRSAVPVAAGATGGHPAKRTFQALRIAVNEELDILDAAVPAILDALHVGGRLVVMSYHSLEDRITKRHLSAWATSTAPPGFPVVLEEHEPVVRVLTRGTEKPTEEEISENRRASSAKVRAVEKIRTSRTTA | 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: Cytoplasm
EC: 2.1.1.199
|
Q2S535 | MSDDDSQDDSVPEGDPRRYATDFHAPVLSHDVQARLVTDASGRYVDATLGGGGHARALLDVLDPDGVVLGIDRDPEALETARDRLADEREAGRFWAVHGTFGNLRDVLAAEDLIPIDGLLLDLGVSSHQIDVPERGFSFRDEGPLDMRMDPQRGLTAQQVVNGWGERDLRDVLREYGEESRAGQIARALCDARPLDTTRALAEVVEDCAPPPDTVKTLTRVFQALRIVVNAELDELEQVLEQATEVVRTGGRIAAISYHSLEDRRVKRYLRYGNFEGEPRRDLYGTLVAPWAETPRGPIEAGESEVEANPRARSAHLRVAERRDDDEAGAPLPPLS | 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: Cytoplasm
EC: 2.1.1.199
|
A4X9S3 | MGELRGAHVPVLLERCLELLSPALDRTGQTGRTVYVDATLGLGGHAEAILTAHPRTMLVGLDRDTEALAHARVRLARFADRVHLEHAVYDELPDVLDRIGHPVVDGILFDLGVSSLQLDAPDRGFAYAQDAPLDMRMDQSRGVTAEEVVNSYSHPELARVLRVYGEEKFASRIASAIVRERDRAPITSSAQLAELVRQAIPAPARRTGGHPAKRTFQALRIEVNRELAALETALPAALDRLAIEGRMVVLSYHSLEDRLTKVALADRVRSKGPIDLPVELPGTGPTFRLLSRGAELPGEAEVAVNPRAASVRLRAAERLDPTQQQRQRTDRERYRRQVRAMHQPGTGSAVRRPVSGDDGTGTDEEGEGHDD | 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: Cytoplasm
EC: 2.1.1.199
|
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
EC: 2.1.1.198
|
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
EC: 2.1.1.198
|
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
EC: 2.1.1.198
|
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
EC: 2.1.1.198
|
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
EC: 2.1.1.198
|
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
EC: 2.1.1.198
|
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
EC: 2.1.1.198
|
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
EC: 2.1.1.198
|
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
EC: 2.1.1.198
|
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
EC: 2.1.1.198
|
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
EC: 2.1.1.198
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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 membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA (By similarity). Enables malignant tumor cells to penetrate laminin tissue and vessel barriers. Activates precursor thymic anti-OFA/iLRP specific cytotoxic T-cell. May induce CD8 T-suppressor cells secreting IL-10.
PTM: Acylated. Acylation may be a prerequisite for conversion of the monomeric 37 kDa laminin receptor precursor (37LRP) to the mature dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for membrane association.
Sequence Mass (Da): 32838
Sequence Length: 295
Subcellular Location: Cell membrane
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Q974U1 | MIEIDGSFGEGGGQILRTSLTLSALTKKPFRIYKIRANRPKPGLQRQHLTAVEAVKKLTNAKVKGDFVGSTELVFEPEDIVEKGDFEFDVGTAGSVTLILQTILPLLINRNIKVTIKGGTDVPKSPSIDYIRLTFLSLLEKIGIRVNLILIRRGHYPEGGGEIKITEVKGNPSSFSLMERGELLMIKGISHVSSLPSHIAERQAKSAKEFLLSKIKIPVEIEIDVRENERSKGSGIALTAIFEKTFLGSDSLGEKGKRAEIVGEEAAKSIYEEIISNATVDRHMSDMLMLYASLYYGEYIGSELTSHARTNSEIIKKFLNVNIQISGEKPFIFRAKKEL | 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'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Mass (Da): 37505
Sequence Length: 339
Subcellular Location: Cytoplasm
EC: 6.5.1.4
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C5A2A3 | MEWVEIDGSYGEGGGQILRTAVALSVITGKPVRIHRIRANRPNPGLRPQHLHGILALKELSNARVKGAKVGSTVLEFVPGRAEPKHVKVPIKTAGSITLVLQALLPAMAFIGGSFEITGGTDVPWSPPVDYLRNVTLFALEKMGLRAEIELKRRGHYPKGGGLVTGSVEPWESKKPLVALEWNKVDSFAGISHATNLPAHVAERQAKSAEERLREFFNAPVEIETEVSRSLGPGSGIVVWAETDSLRLAGDALGKRGKPAEVVGREAAEELIEQLTPRKAVDRFLGDQLIPFLAFAGGEIGVAEITNHLVTNVWVVERFLGRTFEVEGEIGEPGVVRVVRKAEV | 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'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Mass (Da): 37245
Sequence Length: 344
Subcellular Location: Cytoplasm
EC: 6.5.1.4
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Q5JIQ0 | MEWVEIDGSYGEGGGQILRTSVALSVITGKPVRIYNIRANRPNPGLRPQHLHGILALKELSNAKIKGASVGSTELEFIPGKAEPKHVRVPIKTAGSITLVLQALLPAMAFIGGSFEITGGTDVPWSPPVDYLKHVTLYALEKMGIKVELEIKRRGHYPRGGGLVVGRIEPWEEKKPLKALKWERIEWFAGISHATNLPAHVAERQAKAARERLSEVYSAPVEIETEVSRSLGPGSGIVVWAETDKLRLGGDALGKRGKPAEVVGREAADELIEALKTGMAADRFLGDQLIPFLAFAGGEVGVSEITNHLVTNVWVVEKFFGNVFEVEGEVGKPGTLRVVKSVL | 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'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity).
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Mass (Da): 37149
Sequence Length: 343
Subcellular Location: Cytoplasm
EC: 6.5.1.4
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C6A4N4 | MRVIDGSYGEGGGQILRTAVALSVITGEPIKIINIRAKRSNPGLRPQHLHGILALKELSDAKVKGAKEGSTELEFYPKSTRVRHVKVLIKTAGSISLVLQALLPAMVFAEEEVTFEITGGTDVAWSPPVDYLKHITLYALEKLGIKVEIEIRRRGHYPRGGGFVIGKVYPWGTKRPLVARTFDKIYSFEGISHAVRLPSHVAIRQAKAAKEALERVYPSIPIKIHEEYYEQGKDPHFGPGSGIVIWANTDVLRLGGDALGERGKPAEIVGREAAKALIEQLGPRHAVDKFLGDQLIPFLTFAGGDIWVSEVTKHLITNVWVVEQFFGRVFEMEGEIGKPGKVRVVKKVEL | 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'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Mass (Da): 38601
Sequence Length: 350
Subcellular Location: Cytoplasm
EC: 6.5.1.4
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C4M6T2 | MAKSRYSRKNKGKKLQRAQQNTVSTEEKPEQEVETIDFNGFQIPKVYDGKFERKPMELEIKKGFVEGMNGDAKIFCNDDLLNLLTFEMIKDISNNYPSCVRQTANAATLPGVVGSLAMPDAHSGYGFSIGGVVAMRLDDPEAVICPGGVGFDINCGVRLIRTNLQREDIEQHKARLADELFKQIPSGVGTQAQIAFSPEDFDSIMKEGLEFLVENGYAWEEDLNHCEEHGKIANADPSLVSNSAKSRGYKQVGTLGSGNHYLEVQVVDEIMDVEAAKAMGITEIGQVCIMVHCGSRGLGHQVCQDYINLCMKSGICNPVDKQLTGVPFNSPIGQQYYSAMNCCANFAFANRGMITYRIRQAFETVLRMKPKKMDMHLVYDVCHNIAKVEEHDVDNKKVQCIVHRKGATRAFPPQHPDISEDYKEIGQPAIIGGSMGTCSYVLVGTQEGMKKSFGSTCHGAGRKMSRTKAMDNLTSKDVINRMKEMGIELRITDPKLAAEEADEAYKDVTEVVETCQAANISKIVLRLKPLIVIKG | 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 RNA ligase with broad substrate specificity, and may function toward other RNAs.
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP
Sequence Mass (Da): 59146
Sequence Length: 535
EC: 6.5.1.8
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O29399 | MNMEGILKKITDYKWELPKSYKPGMRVPAYFYISRKLMQILEKDAVEQAANVATMPGIQVASLVMPDVHVGYGFPIGGVAGFDVNEGVVSPGGVGFDINCGVRLLRSNLNVEDVKPLIKKLIDELFVAVPSGVGSEGRLRVSDRELDEIFVEGARWAVENGYGYERDLKHCEEEGALEGARPEVVSKKARDRGRPQLGTLGSGNHFLEVQYVDKVFDEKVAAKFGIEEGMVTVMIHCGSRGLGHQVCTDFLEVLDRAVKKYGIKLPDRQLACAPINSKEGQDYFAGMAASANYAWCNRQIIAHWVRETFQKVMGMSEDDLGMELVYDVAHNIAKFEEHRVDGKKMKLCVHRKGATRAFGPGLKEVPEDYRDVGQPVLIPGSMGTPSYILVGTEKAMEETFGSTCHGSGRVMSRAAAKRKLRGNVVKQNLERKGIYVRATHGALLAEEAPEAYKLSDDVVDVVHRAGISKLVARLRPLGVAKG | 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'-end dephospho-ribonucleoside-RNA + GTP = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP
Sequence Mass (Da): 53025
Sequence Length: 482
EC: 6.5.1.8
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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(+)
Sequence Mass (Da): 26742
Sequence Length: 246
EC: 3.5.1.110
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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 | MAMFGFPHWQLKSTSTESGVVAPDERLPFAQTAVMGVQHAVAMFGATVLMPILMGLDPNLSILMSGIGTLLFFFITGGRVPSYLGSSAAFVGVVIAATGFNGQGINPNISIALGGIIACGLVYTVIGLVVMKIGTRWIERLMPPVVTGAVVMAIGLNLAPIAVKSVSASAFDSWMAVMTVLCIGLVAVFTRGMIQRLLILVGLIVACLLYGVMTNVLGLGKAVDFTLVSHAAWFGLPHFSTPAFNGQAMMLIAPVAVILVAENLGHLKAVAGMTGRNMDPYMGRAFVGDGLATMLSGSVGGSGVTTYAENIGVMAVTKVYSTLVFVAAAVIAMLLGFSPKFGALIHTIPAAVIGGASIVVFGLIAVAGARIWVQNRVDLSQNGNLIMVAVTLVLGAGDFALTLGGFTLGGIGTATFGAILLNALLSRKLVDVPPPEVVHQEP | 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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22158
Sequence Length: 202
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 20723
Sequence Length: 186
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 21898
Sequence Length: 201
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 23494
Sequence Length: 211
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 21486
Sequence Length: 203
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 21477
Sequence Length: 206
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 21637
Sequence Length: 211
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 21986
Sequence Length: 207
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22363
Sequence Length: 203
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 25916
Sequence Length: 221
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 23245
Sequence Length: 203
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 21401
Sequence Length: 201
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 23003
Sequence Length: 209
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22529
Sequence Length: 214
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 21230
Sequence Length: 202
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22459
Sequence Length: 198
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22126
Sequence Length: 202
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 20365
Sequence Length: 200
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22293
Sequence Length: 203
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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Q8U9K6 | MSDADRLITPEKRGEDIDTTLRPQSLDDFTGQAEARANLKVFIEAAKNRGEALDHVLFVGPPGLGKTTLAQIMAKELGVNFKSTSGPVIAKAGDLAALLTNLEERDVLFIDEIHRLNPAVEEILYPAMEDFQLDLIIGEGPAARSVKIDLSKFTLVAATTRLGLLTTPLRDRFGIPVRLAFYTVDELELIVRRGARLMGLNMTDGGAREIARRARGTPRIAGRLLRRVRDFAEVARAEAVTREIADEALTRLLVDNMGLDQLDMRYLTMIAVNFGGGPVGIETIAAGLSEPRDAIEDIIEPYMIQQGFIQRTPRGRILTATAWKHLGLQPPKDLEAAQFRLTLEDD | 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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 38119
Sequence Length: 346
Domain: Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
Subcellular Location: Cytoplasm
EC: 3.6.4.12
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Q9X719 | MTAPENLDAALRPKTLTEYVGQEKLKDKLGVYLQAARGRREALDHTLLFGPPGLGKTTLAHIIAYELGVNIRVTSGPAIEKPGDLAAILTNSLEEGDVLFIDEIHRLGRVAEEHLYPAMEDFKLDIVLGQGPAARTIELPLPRFTLVGATTRPGLITAPMRSRFGIIEHLEYYTAEEIATNLLRDARLLGFGLDEEAGLEIGARSRGTMRIAKRLLRRVRDYADVAGETTIGLERAQSALDKLGLDSAGLDDRDKKYLETLIHRFAGGPVGVDTLATAISEDALTLEDVYEPYLIQLGFIKRTPRGRVATAHAYDHLGLPPGGIDDGNGIFLN | 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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 36325
Sequence Length: 333
Domain: Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
Subcellular Location: Cytoplasm
EC: 3.6.4.12
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C0QKP4 | MSDGILSFSSKNDKRGETSGKELITPSSQPVDDSSEVVSLRPDRFESYVGQTDTVETLKIAIQAAKMRGDCLDHVLLHGPPGLGKTTISHIIANEMGGTLTVTSGPALEKGGDLIGMLTNLARGDILFIDEIHRLPKTVEEFLYPAMEDFAVDFVFDKGLHARSHRYRLKQFVLVGATTRVGLISSPLRDRFGIFRSLDFYTDEELVTIIRRSAGLLNVVLDDGAALELARRSRGTPRIANRLLKRVRDFSMVRSSGEVTQKSVAAALSLEGIDSKGLTVLDRNYLRTIIEFYRGGPVGIEAVAATLQEETDTLVDVVEPYLLKIGMVMRTSAGRRASVGAYEHLGIKHQMELF | 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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 38910
Sequence Length: 354
Domain: Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
Subcellular Location: Cytoplasm
EC: 3.6.4.12
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B7USN7 | MIEADRLISAGTTLPEDVADRAIRPKLLEEYVGQPQVRSQMEIFIKAAKLRGDALDHLLIFGPPGLGKTTLANIVANEMGVNLRTTSGPVLEKAGDLAAMLTNLEPHDVLFIDEIHRLSPVVEEVLYPAMEDYQLDIMIGEGPAARSIKIDLPPFTLIGATTRAGSLTSPLRDRFGIVQRLEFYQVPDLQYIVSRSARFMGLEMSDDGALEVARRARGTPRIANRLLRRVRDFAEVKHDGTISADIAAQALDMLNVDAEGFDYMDRKLLLAVIDKFFGGPVGLDNLAAAIGEERETIEDVLEPYLIQQGFLQRTPRGRMATVRAWNHFGITPPEMP | 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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 37172
Sequence Length: 336
Domain: Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
Subcellular Location: Cytoplasm
EC: 3.6.4.12
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Q97SR6 | MSRILDNEMMGDEELVERTLRPQYLREYIGQDKVKDQLQIFIEAAKMRDEALDHVLLFGPPGLGKTTMAFVIANELGVNLKQTSGPVIEKAGDLVAILNDLEPGDVLFIDEIHRLPMSVEEVLYSAMEDFYIDIMIGAGEGSRSVHLELPPFTLIGATTRAGMLSNPLRARFGITGHMEYYAHADLTEIVERTADIFEMEITHEAASELALRSRGTPRIANRLLKRVRDFAQIMGNGVIDDVITDKALTMLDVDHEGLDYVDQKILRTMIEMYSGGPVGLGTLSVNIAEERETVEDMYEPYLIQKGFIMRTRSGRVATAKAYEHLGYEYSEK | 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 open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 37279
Sequence Length: 332
Domain: Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
Subcellular Location: Cytoplasm
EC: 3.6.4.12
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 17010
Sequence Length: 158
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 17960
Sequence Length: 169
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 17464
Sequence Length: 164
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 20788
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 18705
Sequence Length: 178
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 18019
Sequence Length: 166
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 19370
Sequence Length: 181
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 17941
Sequence Length: 170
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 18451
Sequence Length: 174
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 20056
Sequence Length: 189
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 17875
Sequence Length: 163
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 17741
Sequence Length: 163
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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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 arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 17459
Sequence Length: 159
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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Q0WW17 | MASSSPVTPGLMSVVFGIVPVIVAWLYSEYLHYAKYSVSAKTRHSDVNLVEIAKDFVKEDDKALLIEDGGGLQSASPRAKGPTTHSPLIRFVLLDESFLVENRLTLRAIIEFAVLMVYFYICDRTDVFNSSKKSYNRDLFLFLYFLLIIVSAITSFTIHTDKSPFSGKAIMYLNRHQTEEWKGWMQVLFLMYHYFAAAEYYNAIRVFIACYVWMTGFGNFSYYYIRKDFSLARFAQMMWRLNFLVIFSCIVLNNSYMLYYICPMHTLFTLMVYGALGIMSKYNEMGSVIAAKFFACFVVVIIVWEIPGVFEWIWSPFTLLMGYNDPAKPQLPLLHEWHFRSGLDRYIWIIGMLYAYYHPTVESWMDKLEEAEMKFRVAIKTSVALIALTVGYFWYEYIYKMDKLTYNKYHPYTSWIPITVYICLRNITQSFRGYSLTLLAWLGKITLETYISQFHIWLRSGVPDGQPKLLLSLVPDYPLLNFMLTTSIYVAISYRLFELTNTLKTAFIPTKDDKRLVYNTISALIICTCLYFFSFILITIPQKLV | 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
Subcellular Location: Golgi apparatus membrane
EC: 2.3.1.-
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Q66GQ5 | MADSQPITPGQVSFLLGVIPVFIAWIYSEFLEYKRSSLHSKVHSDNNLVELGEVKNKEDEGVVLLEGGLPRSVSTKFYNSPIKTNLIRFLTLEDSFLIENRATLRAMAEFGAILFYFYISDRTSLLGESKKNYNRDLFLFLYCLLIIVSAMTSLKKHNDKSPITGKSILYLNRHQTEEWKGWMQVLFLMYHYFAAAEIYNAIRVFIAAYVWMTGFGNFSYYYIRKDFSLARFTQMMWRLNLFVAFSCIILNNDYMLYYICPMHTLFTLMVYGALGIFSRYNEIPSVMALKIASCFLVVIVMWEIPGVFEIFWSPLTFLLGYTDPAKPELPLLHEWHFRSGLDRYIWIIGMIYAYFHPTVERWMEKLEECDAKRKMSIKTSIIAISSFVGYLWYEYIYKLDKVTYNKYHPYTSWIPITVYICLRNSTQQLRNFSMTLFAWLGKITLETYISQFHIWLRSNVPNGQPKWLLCIIPEYPMLNFMLVTAIYVLVSHRLFELTNTLKSVFIPTKDDKRLLHNVLAGAAISFCLYLTSLILLQIPH | 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 | MVVSQPITPGQVSFLLGVIPLMIAWLYSEFLEYRRSSFHAKVHSDKNLVELEMVTNKEDEGTVLMEGGLPRSASSKFYSSPIKTNLIRFLTLEDSFLLENRATLRAMAEFGAILLYFYICDRTSLIGQSQKNYSRDLFLFLFCLLIIVSAMTSLKKHTDKSPITGKSILYLNRHQTEEWKGWMQVLFLMYHYFAAVEFYNAIRVFIAGYVWMTGFGNFSYYYIRKDFSLARFTQMMWRLNFFVAFCCIILNNDYMLYYICPMHTLFTLMVYGALGIYSQYNEIASVMALKIASCFLVVILMWEIPGVFEIFWSPLAFLLGYTDPAKPDLPRLHEWHFRSGLDRYIWIIGMIYAYFHPTVERWMEKLEECDAKRRMSIKTSIIGISSFAGYLWYEYIYKLDKVTYNKYHPYTSWIPITVYICLRNCTQQLRRFSLTLFAWLGKITLETYISQFHIWLRSSVPNGQPKLLLSIIPEYPMLNFMLTTAIYVLVSVRLFELTNTLKSVFIPTKDDKRLLHNVIAMAAISFCLYIIGLILLLIPH | 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 regulates the NF-kappa-B signaling pathway by enhancing the sumoylation of NF-kappa-B inhibitor alpha (NFKBIA), promoting its stabilization which consequently leads to an increased inhibition of NF-kappa-B transcriptional activity. Negatively regulates the hypoxia-inducible factor-1 alpha (HIF1A) signaling pathway by increasing the sumoylation of HIF1A, promoting its stabilization, transcriptional activity and the expression of its target gene VEGFA during hypoxia. Has no effect on ubiquitination (By similarity).
Sequence Mass (Da): 30406
Sequence Length: 267
Domain: The RWD domain is required for the sumoylation enhancement activity.
Subcellular Location: Nucleus
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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).
Sequence Mass (Da): 29655
Sequence Length: 257
Domain: The RWD domain is required for the sumoylation enhancement activity.
Subcellular Location: Nucleus
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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 and isoform 2 positively regulate the NF-kappa-B signaling pathway by enhancing the sumoylation of NF-kappa-B inhibitor alpha (NFKBIA), promoting its stabilization which consequently leads to an increased inhibition of NF-kappa-B transcriptional activity. Isoform 1 and isoform 2 negatively regulate the hypoxia-inducible factor-1 alpha (HIF1A) signaling pathway by increasing the sumoylation of HIF1A, promoting its stabilization, transcriptional activity and the expression of its target gene VEGFA during hypoxia. Isoform 2 promotes the sumoylation and transcriptional activity of the glucocorticoid receptor NR3C1 and enhances the interaction of SUMO1 and NR3C1 with UBE2I/UBC9. Has no effect on ubiquitination.
Sequence Mass (Da): 30543
Sequence Length: 267
Domain: The RWD domain is required for the sumoylation enhancement activity.
Subcellular Location: Nucleus
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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).
Sequence Mass (Da): 30038
Sequence Length: 265
Domain: The RWD domain is required for the sumoylation enhancement activity.
Subcellular Location: Nucleus
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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 intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread. The iNOS-S100A8/A9 transnitrosylase complex directs selective inflammatory stimulus-dependent S-nitrosylation of GAPDH and probably multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute to S-nitrosylation site selectivity.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10835
Sequence Length: 93
Subcellular Location: Secreted
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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 intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. The iNOS-S100A8/A9 transnitrosylase complex is proposed to direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as GAPDH, ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute to S-nitrosylation site selectivity (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10295
Sequence Length: 89
Subcellular Location: Secreted
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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 intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. The iNOS-S100A8/A9 transnitrosylase complex is proposed to direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as GAPDH, ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute to S-nitrosylation site selectivity (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10239
Sequence Length: 89
Subcellular Location: Secreted
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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 and can induce degranulation of neutrophils by a MAPK-dependent mechanism. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. The iNOS-S100A8/A9 transnitrosylase complex is proposed to direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as GAPDH, NXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif.
PTM: Phosphorylated. Phosphorylation inhibits activation of tubulin polymerization.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17114
Sequence Length: 156
Subcellular Location: Secreted
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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 ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism . Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions . The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase . Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX . The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities . Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration . Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER) . Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade . Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth . Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3 . Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK . Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants . Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread . Has transnitrosylase activity; in oxidatively-modified low-densitity lipoprotein (LDL(ox))-induced S-nitrosylation of GAPDH on 'Cys-247' proposed to transfer the NO moiety from NOS2/iNOS to GAPDH via its own S-nitrosylated Cys-3 . The iNOS-S100A8/A9 transnitrosylase complex is proposed to also direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif .
PTM: Phosphorylated. Phosphorylation inhibits activation of tubulin polymerization.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13242
Sequence Length: 114
Subcellular Location: Secreted
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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 ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism (By similarity). Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions (By similarity). The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase . Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX (By similarity). The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities . Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration (By similarity). Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER) . Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade . Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth (By similarity). Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3 (By similarity). Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK (By similarity). Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants (By similarity). The iNOS-S100A8/A9 transnitrosylase complex is proposed to direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as GAPDH, NXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif (By similarity).
PTM: Phosphorylated. Phosphorylation inhibits activation of tubulin polymerization.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13049
Sequence Length: 113
Subcellular Location: Secreted
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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 ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism (By similarity). Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions (By similarity). The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase (By similarity). Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX (By similarity). The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities . Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration (By similarity). Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER) (By similarity). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade (By similarity). Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth (By similarity). Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3 (By similarity). Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK (By similarity). Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants (By similarity). The iNOS-S100A8/A9 transnitrosylase complex is proposed to direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as GAPDH, NXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif (By similarity).
PTM: Phosphorylated. Phosphorylation inhibits activation of tubulin polymerization.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13145
Sequence Length: 113
Subcellular Location: Secreted
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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: Cytoplasm
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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 | MVPTGQVAEKQACEEPRQDRELKSWRWLVFYLCFFGFMAQLRPGESFITPYLLERNFTKEQVTNEIIPMLPYSHLAVLVPIFLLTDYLRYKPVLVLQCLSFVCVWLLLLLGTSVVHMQLMEVFYSITMAARIAYSSYIFSLVQPSRYQRMASYSRAAVLLGVFISSVLGQVLVTLGGISTYMLNCISLGFILFSLSLSLFLKRPKRSLFFNRSALVQGALPCELDQMHPGPGRPEPRKLERMLGTCRDSFLVRMLSELVKNVRQPQLRLWCLWWVFNSAGYYLITYYVHVLWKITDSRLNYNGAVDAASTLLSAITAFTAGFVNIRWALWSKLVIASVIAIQAGLVFCMFQIPDIWVCYVTFVLFRGAYQFLVPIATFQIASSLSKELCALVFGINTFLATALKTSITLVVSDKRGLGLQVHQQFRIYFMYFLTLSIICLAWAGLDGLRYYRRGRHQPLAQAQALSPLEDSVQAISLQDGDLRRPQPSAPQLLPEDGSVEDGRADLRVEAKA | 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 predominant circulating form of folate (By similarity). Also able to mediate the import of antifolate drug methotrexate . 5-amino-4-imidazolecarboxamide riboside (AICAR), when phosphorylated to AICAR monophosphate, can serve as an organic anion for antiporter activity (By similarity).
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate(out) + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide(in) = (6S)-5-methyl-5,6,7,8-tetrahydrofolate(in) + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58108
Sequence Length: 512
Subcellular Location: Cell membrane
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O60779 | MDVPGPVSRRAAAAAATVLLRTARVRRECWFLPTALLCAYGFFASLRPSEPFLTPYLLGPDKNLTEREVFNEIYPVWTYSYLVLLFPVFLATDYLRYKPVVLLQGLSLIVTWFMLLYAQGLLAIQFLEFFYGIATATEIAYYSYIYSVVDLGMYQKVTSYCRSATLVGFTVGSVLGQILVSVAGWSLFSLNVISLTCVSVAFAVAWFLPMPQKSLFFHHIPSTCQRVNGIKVQNGGIVTDTPASNHLPGWEDIESKIPLNMEEPPVEEPEPKPDRLLVLKVLWNDFLMCYSSRPLLCWSVWWALSTCGYFQVVNYTQGLWEKVMPSRYAAIYNGGVEAVSTLLGAVAVFAVGYIKISWSTWGEMTLSLFSLLIAAAVYIMDTVGNIWVCYASYVVFRIIYMLLITIATFQIAANLSMERYALVFGVNTFIALALQTLLTLIVVDASGLGLEITTQFLIYASYFALIAVVFLASGAVSVMKKCRKLEDPQSSSQVTTS | 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 | MDVPARVSRRAAAAAARMLLRTARVPRECWFLPTALLCAYGFFANLRPSEPFLTPYLLGPDKNLTERQVYNEIYPVWTYSYLLLLFPVFLATDYLRYKPVILLQGLSLIVTWFMLLYAQGLLAIQFLEFFYGIATATEIAYYSYIYTVVDLGMYQKVTSYCRSATLVGFTVGSVLGQILVSVVGWSLFSLNVISLTCVSVAFAVAWFLPMPQKSLFFHHIPSSCHGVNGLKVQNGGIVTDTPAANHLPGWEDIESKIPLNLDEPPVEEPEEPKPDRLRVFRVLWNDFLMCYSSRPLLCWSVWWALSTCGYFQVVNYAQGLWEKVMPSQNADIYNGGVEAVSTLLGASAVFAVGYIKLSWSTWGEMTLFLCSLLIAAAVYVMDTVQSIWVCYASYVVFRIIYMVLITIATFQIAANLSMERYALVFGVNTFIALALQTLLTLIVVDARGLGLCITTQFLIYASYFAAISVVFLANGIVSIIKKCRKQEDPSSSPQASTS | 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
Subcellular Location: Cell membrane
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Q9BZV2 | MDCYRTSLSSSWIYPTVILCLFGFFSMMRPSEPFLIPYLSGPDKNLTSAEITNEIFPVWTYSYLVLLLPVFVLTDYVRYKPVIILQGISFIITWLLLLFGQGVKTMQVVEFFYGMVTAAEVAYYAYIYSVVSPEHYQRVSGYCRSVTLAAYTAGSVLAQLLVSLANMSYFYLNVISLASVSVAFLFSLFLPMPKKSMFFHAKPSREIKKSSSVNPVLEETHEGEAPGCEEQKPTSEILSTSGKLNKGQLNSLKPSNVTVDVFVQWFQDLKECYSSKRLFYWSLWWAFATAGFNQVLNYVQILWDYKAPSQDSSIYNGAVEAIATFGGAVAAFAVGYVKVNWDLLGELALVVFSVVNAGSLFLMHYTANIWACYAGYLIFKSSYMLLITIAVFQIAVNLNVERYALVFGINTFIALVIQTIMTVIVVDQRGLNLPVSIQFLVYGSYFAVIAGIFLMRSMYITYSTKSQKDVQSPAPSENPDVSHPEEESNIIMSTKL | 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
Sequence Length: 496
Subcellular Location: Membrane
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Q99PL8 | MDSSCRTPPSNSWVYPTVILCLFGFFSMFRPSEAFLIPFLSEPSKNLTSPEMTNEILPVWTYSYLATLPPVFVLTDYLRYKPVIMLHVVAFATSYLFLLFGQGVMLMQTAEFFFGVVSATEIAYFAYIYSMVSPEHYQKVSSYCRSITLVAYTAGSVLAQLLVSLTNLPYSSLFYISLACVSVAFFFSLFLPMPKKSMFFHAKSDRDDCPKPLEQCTVPKEAQSNRTHSELFANSKNLEDREMSNPDPENSALRHFAHWFQDLKECYSSKHLVYWSLWWAFATAGYNQILNYVQVLWEHKAPSQDSSIYNGAVEAIATFGGALASFSVGYLKVNWDLLGELGLAVFSAVIAGSLFLMNYSRSIWVCYAGYLLVKSSYSFLITIAVFQIAVNLSLERYALVFGIDTFIALVIQTIMTMIVVDQRGLQLPVTTQFLVYGSYFAVIAGVFLMRSIYILCSAKCRKEVQNLATTRSPNEPHPQEPSNVSTKF | 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: Multi-pass membrane protein
Sequence Mass (Da): 55073
Sequence Length: 488
Subcellular Location: Membrane
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Q8N4F4 | MGFDVLLDQVGGMGRFQICLIAFFCITNILLFPNIVLENFTAFTPSHRCWVPLLDNDTVSDNDTGTLSKDDLLRISIPLDSNLRPQKCQRFIHPQWQLLHLNGTFPNTNEPDTEPCVDGWVYDRSSFLSTIVTEWDLVCESQSLKSMVQSLFMAGSLLGGLIYGHLSDRVGRKIICKLCFLQLAISNTCAAFAPTFLVYCILRFLAGFSTMTILGNTFILSLEWTLPRSRSMTIMVLLCSYSVGQMLLGGLAFAIQDWHILQLTVSTPIIVLFLSSWKMVESARWLIINNQLDEGLKELRRVAHINGKKNTEETLTTELVRSTMKKELDAVRIKTSIFSLFRAPKLRMRVFGLCFVRFAITVPFYGLILNLQHLGSNVSLFQILCGAVTFTARCVSLLTLNHMGRRISQILFTFPVGLFILVNTFLPQEMQILRVVLATLGIGSVSAASNSASVHHNELVPTILRSTVAGINAVSGRTGAALAPLLMTLMAYSPHLPWISYGVFPILAVPVILLLPETRDLPLPNTIQDVENDRKDSRNIKQEDTCMKVTQF | 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 estrone 3-sulfate, as well as bile acids taurocholate and glycocholate, driven by an outward gradient of dicarboxylates such as glutarate or succinate.
Catalytic Activity: estrone 3-sulfate(out) + glutarate(in) = estrone 3-sulfate(in) + glutarate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61701
Sequence Length: 552
Subcellular Location: Cell membrane
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A0A8B7HA97 | MAFAVLLDQVGSLGRFQILQLAFLCIANILLFPHILLENFTAAVPGHRCWVHILDNDTVSHNDTGTLGQDALLRISIPLDSNLKPEKCRRFVHPQWQLLHLNRTFSNTSEPDTEPCVDGWVYEQSSFFSTVVTEWDLVCEWESQKSVVQSLFMAGSLLGSVIFGYLSDRFGRKMICSWCLLQLAISDTCAAFAPTFSVYCSLRFLAGSCVMTIMGHSFLLVIEWTNPQSRSMVTTLLLCASSVGQMLLGGLAFVIQDWRTLQLTVSIPIFVIFLSSRWLVESARWLITYNQLDKGLKELRRAARINGKKNAGEILTIEFLRSAMQEELDAARSQASIFCLFHAPRLRMIVLYLGFVRLAVSVPLYGLIFNLQYLGRNIYLFQVLFGAITATARFVALLVMNYMGRRISQVLFLLPVGLFILVNTFLDQEMQTLRTILATLGAGVLCIATTSGSVHFSELIPTVLRGTGGGINILFSRIGAALAPLLMIFVGFSPYLPWITYGVFPILAGLVVLLLPETKNLPLPNTIQDVENDRKETRKVKQEDNCMKVTQF | 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-diol 3-O-(beta-D-glucuronate)), estrone 3-sulfate, and estradiol-17-glucuronide (17beta-estradiol 17-O-(beta-D-glucuronate)), but not taurocholate .
Catalytic Activity: estrone 3-sulfate(out) + glutarate(in) = estrone 3-sulfate(in) + glutarate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61792
Sequence Length: 552
Subcellular Location: Cell membrane
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G1SZD9 | MGFDVLLDQAGSLGRFQILQIAFFFVTSMITYTHILLENFTAAIPGHRCWVPLLDNHTTSGNDSDILSQDALLRVSIPLDSNLRPEKCRRFIHPQWQLLYLNGTSPSTNEPDTEPCVDGWVYDQSSFSSTIVTKWDLVCEFQSLKSVVQTLFMSGSLLGGLMFGRLSDRYGRKAIYTWCLLQTAIADTCAIFAPTFVVFCIFRFLAGLTTINIMTNAFILATEWTVPKLQYIGITLILCSYSIGQMLLGGLAFAIRDWYTLHLTVSIPLFVLSLLSRRLVESARWLVTTNQLDEGTKALRRVARINGKKSAGEILTIEFVRSAMQEELNKAQTKTSVIHLLRAPKLRMIICFLSFIRLGASVPFMGLILNLQDLGSSIFLFQVLFGAITFISRCSAHLIMKHMDRRINQSLFFFLVGLCILVNTFLSQEMQTLRVVLATLGIGTVSAANATFFVHALELTPTTFRSTTAGINNVFSRMGSVLAPLLMTLVVYSPHLPWVMYGVFPILAGLIVFCLPETRNRPLPNTIQDVENDTKESRKVKEEDTFIKVTQF | 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-diol 3-O-(beta-D-glucuronate)), estrone 3-sulfate, and estradiol-17-glucuronide (17beta-estradiol 17-O-(beta-D-glucuronate)), and taurocholate .
Catalytic Activity: estrone 3-sulfate(out) + glutarate(in) = estrone 3-sulfate(in) + glutarate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61944
Sequence Length: 552
Subcellular Location: Cell membrane
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