ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6MS67 | MFSNWDIFLNYKNFTINQEIKNKLDLYYQILIQENQKYNLTRITELNEVFEKHFLDSLLFVEQFQIIDQKIADIGTGAGFPGIVLKIFFPNIKLTLIESNNKKANFLKYLVQKLELNNVEILNKRAEELNEYKEHLI | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 16349
Sequence Length: 137
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
P75220 | MNNSKLKQYVQLVQTANQNFNLTGLKTEGEIYEHLVQEIIELFNEYDSYFDHKKVADLGSGNGCPGVILKLLFPQIKTLDLIDSKHKKVNFLKEVIQTLELNNTQALCARIENHTEQYDTLCSRGLGSIIEVNAFALKLLKPNGIIFHIKQSLDQYLEFEDSEQKDQFKPLFFKFFHGKRQQILIAMKKNV | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 22080
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q98R82 | MNCLEKITNEYGQKTASRLEQFVKLIEEENKKINLTSFEGQRLWQEGIYESIKCLEPFVKSNDSLLDIGAGVGFPSVPFLIVNPEVKLTIIESNKKRVLFLEKVKKDLNLSFEIFNGRVENFNKEIHFDFITARALAPLNILMELTINLGSILPKPTNYIFVKGANYLSELNEAQNAIKILKLKVFDLKKIDVFFDKNIFMIHYIKTANVSKEYPRAWDKIIKKPIR | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 26276
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A0R7J5 | MKHGSVPATPEAASLVFGDRLEAAELYARILAGAGVEWGLLGPREVDRVWERHILNSAALGELMEPGERVADIGSGAGLPGIPLALARPDIHVTLIEPLLRRSEFLRETVTELGLDVTVVRGRAEDREVRDRVGEMDVVTSRAVASLDKLTRWSVPFLRDGGRMLPIKGERAEVEIEEHRRVMESLGAVDARVVRCGANYLSPPVTVVDARRRAAKPGRNKSGRTARSRGRTGRR | Function: Specifically methylates the N7 position of guanine in position 518 of 16S rRNA.
Sequence Mass (Da): 25732
Sequence Length: 235
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q4A6Q0 | MEFKNKVIAYCKERNANFLDFEKYVSLIEEHNKNINLTGFSGESLWEEGILNSLLYMNSSTKDKSEIKILDIGSGVGFPAIPYALLRENNSIDIFEPIQKRVDFLNLVKQKLTLDKVNIYKQRAEEFSQKNIYDVVVARAVGSVKTMLMAAFHLVALKGEMVLIKGPKYKQEILEAQEILSKLKVEVIVDKFILNAKENFLVRIKKLRNCPKEFPYSWKDIKKQS | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 25986
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q30TL7 | MNLKTALLELDTELPDTFFHHIQKFKEHLFKWNKIHNLTGAKDENTIDEFIYDAIYPITFLPKCKNLLDIGTGAGFPGLILAMGLPETEVTLVEPLAKRASFLQFIKADLGLSNVKVVQKRVQDMPSEIFEIVTSRAVIDTNMLLELSKGFRNKDSKLLFFKGERVYDEVNKDLKYKIIKRENRHYLLIGETL | 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): 22245
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 2.1.1.... |
A6QC07 | MQYLNAEGIVLDDGIIGKLEGFAVLLHEWNQVHNLTGARSVVAIYDNIVDSLYPLTFIRIPKTLLDVGTGAGFPGLVLAIALPETEVVLAEPLKKRVSFLKYAAIDLGLKNVTVEAKRVENVVYEAFDMISSRAVTNTKLLLDLTSRISDEHTEYLFYKGSRVFDEIAQVEGQMSYDIIQKNQRNYLYIKNET | 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): 21672
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 2.1.1.... |
Q67J35 | MDATAYRGLLEEGLASLGVEAEPGGVEAVLLHLDLVREWNERMNLTAITDPQEMVIKHALDAASGLAVAGVEPGQRVIDVGTGAGFPGVVWKCLRPGIDLTLLESLQKRCRFLEEVGQAVIGPLAGGEGYQVVWGRAEDVGRNPAHRERYDLVTARAVAELRVLAEYCLPLARVGGRFLAMKGPSVGEEILAAEAAVEKLGGRLEEVRELELPDGGGRRSLVLIRKERPTPKAYPRRAGVPAKSPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 26424
Sequence Length: 246
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q2LY85 | MIRLLNNFNFSEIDNADPAQWCRLFQEAAAEFDVLLSDAQLNRFLMYYRELKFWNSRINLIASAESVTDIVIKHFLDSLTLIPCIPFPDGRLIDIGTGGGFPGIPLKIALNSLKVTLLEASRKKVSFLKSLRRVLNLQDMKILNERVEDLITQAPCPNRFDMVVSRAALKLPEYLRFGKELVSSHGVIIAMKGANYQHELEDVNDILEEYGIFLAEVRSLALPCTGDFRAILIFRKSLSRT | 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): 27379
Sequence Length: 241
Subcellular Location: Cytoplasm
EC: 2.1.1.... |
Q39ZT2 | MQNRLQELLTRIGLSLEKPVCDRLLWYLDEMLRWNRRINLTAIENKEEALEKHLLDSLTVVPLLRGDERLLDMGSGAGLPSIPIKIARPQMCVLSVDSVHKKIVFQQHVARQLKLQGFEARACRIQSLSQGESETSFDVVTARALTHLSDLLSMAEPLLNDKGRLIAMKGPDGEAELAECAQQIRKAGFVAEPLQHLSLPLSGSERTLVVLKRKPGR | 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): 24302
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 2.1.1.... |
Q7VQJ5 | MFIMHHNSVLLHEAINALNINPSGIYIDGTFGLGGHSHYILSKLTSHGRLIAMDRDWSAVNIGEVLTKQDGRFSIIHAPFSKMLRCIYNMNLVGLINGILLDLGVCESQLTDSSRGFSFMRDGPLDMRMDNSVGQSAYEWIAKASQKDIEWVLRTFGEEKLSKKIARSIVLKREVYPIDRTSALSEIISDTVLYYNNRYNRRKHPATRSFLAIRIYINEELVEIMKILQDVFKLLAPGGRLVVISFNSLEDRIVKKFINQYSRVFAYPPKIPLTHTQLLHKYSGTMKFKNLGKIKPTVLEIKKNIRARSAILRYAEKLIY... | 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): 36798
Sequence Length: 321
Subcellular Location: Cyt... |
Q2KVE4 | MKFEHRPVLLEPTVDALLQADFGGRGASRARPRDEAAALTRQATGIFVDGTFGRGGHSRELLGRLGPQARLVVFDKDPEAIAVAQALAAEDARVTVVHGGFATMTEELAARGIERIDGVMLDLGVSSPQIDDADRGFSFMREGPLDMRMDTSRGPTVADWLAQASVEEMREVIADYGEERFAFQVAKAIAARRATRPLHTTLELAECVASAVRTREKGQHPATRTFQALRIYINRELEELARALASAIELLVPGGRLAVISFHSLEDRMVKQCIAAAARPAAAHPRLPLRESELPQPILQTLGKVVADDAEVAGNARSRS... | 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): 38344
Sequence Length: 355
Subcellular Location: Cyt... |
O51286 | MNNNAFHFPVLLDAICKLIEDLPVKSDLIYIDSTLGEGVHAKAILEKYDFLSLVGIERDPQILERARQFLSIFEERITYFNDWFDNFFVNYPLNVKANFILVDLGISMFHYKGSKKGFSFLEDEPLDMRLCSSSCKISAAEIVNTYSKYDLEALIYDLSNEHYSRRISKAIVEYRKIKKIETTKELQSIISKVYPFSKVKINPATKTFQALRIYVNDELARLKRSLPFWVENLAKDGILAIITFHSIEDRIVKDFFRSLSCDLYAKISKKPIMPSFDEIKKNKPSRSAKLRVVKKL | 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): 34382
Sequence Length: 296
Subcellular Location: Cyt... |
Q89FT9 | MSSAPHIPVLGREAIDHLAPREGGIYVDATFGAGGYSRAILDVPGTRLIAIDRDRTAIAGGAELVERSAGRLTLVEDRFSHLADVCAAQGVDAVDGVVMDVGVSSMQLDQAGRGFSFRLDGPLDMRMGQAGPTAADVVARASEADLADIIYLLGEERHSRRVARAIVADRQETPFTTTRALADLVGRVVRSKPGDIHPATRTFQALRIFVNEELEELQTALTAAERVLKPGGRLVVVSFHSLEDRIVKNFLAERSKTGGGSRHLPEVAQTAPSFQLLTRRPVVAGEDEVAHNPRARSAKLRAAERTSAPAHKDDQSSSWP... | 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): 35347
Sequence Length: 329
Subcellular Location: Cyt... |
C5B9E8 | MSENFQHKTVLLDEAVAGLNLRSDGIYIDGTFGRGGHSRLILSQLGAEGRLIAIDRDPQAIAAAAQIDDPRFSIIHGPFSALADYVQEMGLSSRIDGILLDLGVSSPQLDDPERGFSFMRDGPLDMRMDPSRGLSAAQWLMQAEEDDIAWVLKTFGEERFAKRIARAIVERNRTEPLSRTRELAALISDASPFKEKHKHPATRSFQAIRIYINSELDEIERALEGALVALAPQGRLSVISFHSLEDRLVKRFIRQYSRGPQVPKGLPLTEAQLQAQGGPQLKALGKRMPGEREVVDNPRARSSVLRVAERIAR | 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): 34753
Sequence Length: 313
Subcellular Location: Cyt... |
Q8YRT9 | MTKTPLTIEEPIFSHLPVLPQEVITGLVVRPGGRYLDVTVGGGGHSRLILEAAPDVKLTAVDQDGDALTAAKQELAEFGEQVKFVRSNFAAYDFPSTSFDGVLADLGVSSYHLDTPERGFSFRHQASLDMRMDQRQSLSAADVINDWDEVELANIFFKYGEERLSRRIARRIVEKRPFHTTTELAEAIASSVPPKYRYGRIHPATRVFQALRIVVNDELKSLETFIEKAPKALVPGGRIAIISFHSLEDRLVKHGLRNSPLLKVLTKKPIIATDDEIANNPRSRSAKLRIAEKQAETGDEDN | 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): 33612
Sequence Length: 302
Subcellular Location: Cyt... |
Q2G9A3 | MSAETGSRAPHIPVLLEEVVAALDPKPGDLIVDATFGAGGYTRRLLDAGATVHAFDRDPDAIAAGKLWGETCGKEPRLVLHPRRFSEIAEGLAEAGIAGVQGVVFDIGVSSMQLDQAARGFAFSSDGPLDMRMSQEGPSAADFLNEADEGEIADVLYRYGEERQSRRIARAIVAARPLTTTAQFAAVVRKALGYRPDIKGPKAPKDPATRSFQAVRIHVNGELDELVQGLAAAEKVLVPGGRIAVVSFHSLEDRIVKQFLREGAGAVPAGSRHLPQLESKVQAVFEKPSGAIRPTPEEEARNPRARSATLRCAVRTAAPA... | 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): 34987
Sequence Length: 329
Subcellular Location: Cyt... |
Q313R1 | MTADNGHDNNRHQYTAHVPVLLDEVLHYLSPVRGGRYLDGTLGLGGHSEAIMNRCGGDAWLLGLDRDREALAAASGRLAPFGDRVTTRYACYSQFAAIMDEIGWTGLDGALIDIGVSSMQIDTPSRGFSFYADGPLDMRMDPSGDMPSAGVLVNTGSVERLKEIISTYGEDPMAGRIARAIVDARARNPIETTARLAEVVESAYPAKWRAKSRNHPATRTFQALRMAVNGELEELETFLAAIVDRMNPGGRIVVITFHSLEDRLVKNAFRDEAKGCLCPRHIPVCVCGKKPRVNVLTRKPVTAGQAELQANSRASSAKLR... | 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): 35388
Sequence Length: 325
Subcellular Location: Cyt... |
P60397 | MNKTHFNHISVLKQEAIDFLKIKPEGIYVDATLGQCGHTIEIANLLQQGFLYSFDQDVEACTNAKKILPPHLPIEIIHSNFSHLKTQLAQRNVFQLDGILFDLGLSSCQIDNPQRGFSYLHNTPLDMRMNVNQTITAQYILNNYSFAQLKNIFKVYGEVKNAALVASEIIKQRPLCTSYDLVAITDRFCNRQKGHSAKKIFQALRIEVNQELESLKQALEQSLDLLKPNAMIVVISFHSLEDRIVKHFFKKNSTFVLPKKMPITIMPQTPLSIITKKAFLPSEEEMQNNSRSISAKLRVAVKNG | 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): 34555
Sequence Length: 304
Subcellular Location: Cyt... |
B1ZU25 | MTPGHQPVLLREVLGFLAPRARGRYLDCTFGGGGHTRALLEAAAEVRVVALDRDPAAQPRAAALRETFGERFEFIDRDFGRLAELPHEGFDGVLFDFGVSSFQLDETERGFSFRHDAPADMRMDPRSGVPASQWLETATEEMLVRAIRDFGEEQHWRRIVRAIRDARGTGALARTASLAELIAAAIPACDRHAAKIHPATRAFQGVRIAVNDEIGAIERALPAAFAKLAPGGVLCVISFHSLEDRPAKQFFRRMCGQPESAADATPQDLRVKLADPLTRRPVTPADDELAANPRSRSAKLRALRRL | 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): 33675
Sequence Length: 306
Subcellular Location: Cyt... |
A5CD85 | MNNIHTPVMATEMLSYLAPVDNETYLDCTFGTGGYSKLILSNCNCKIIAFDRDPAVISIASQFYQQYSNRFTFFNDNFVEANKYLSKSAKLNGIVMDLGVSSMQLDAANRGFSFRYDAELDMRMSQKGYKASELVNEASEHQLADIIYKFGEENKANKIAKHIVLAREKKPITTTLQLANIIREAVGYNNYYKKNKIDSATKTFQAIRIFINDELSAIQNFLNQSLELLAVNGRLIVVSFHALEDAIVKKFMHQNAVKKVAQSKYSTNKQLPLQNGVLHLLTKKIAVPTRTEIINNPRSRSARLRAALKINE | 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): 35267
Sequence Length: 312
Subcellular Location: Cyt... |
Q01Q40 | MHVPVMPAEAIELLAIRPEGVYLDATAGLGGHSGLIARQLTTGTVIANDRDTRSLEMARANTAEWSDRMCFHYGSFGSLSDAVSQAGFEKVDGLLADLGVSRYQLTAPDRGFSFMADGPLDMRMDASIQTTAADLVNHTDEKTLADLIYQMGEERRARRIARAIVRARPLRSTLHLADVVERAVPRTGRLHPATKTFMALRMAVNDEPGELRRLLEIAPGLLKSGGRMVVISFMSSDDRMVKEKFKELGQSKQATILTKHPLQPSDEESFNNPASRSAKLRALEMR | 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): 31505
Sequence Length: 286
Subcellular Location: Cyt... |
A9FI25 | MNVVNVVPMHLPPPPPRPRGEQHVSVLGREVLAALSPVSEGVYVDATLGAGGHTATILETPGARVIGIDRDERALAIARARLARAGDRVTYVHGEFSEIERHLAALGVPQVDGLLADIGVSSMQLDDPGRGMSFRAEGPLDMRMDSSRGETALELIERLSDEELADLIYRYGEERRSRRVARCIKQAADSGELVTTLDLRRAVVRAVGPARIGGVDPATRTFQALRIAVNGELDQLEALLEAAPRIIAPGGVLAVISFHSLEDRIVKRALREPEVWEPLTKKPVTAGDDEVEGNPRARSAKLRAARRVGGAEALA | 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): 33913
Sequence Length: 315
Subcellular Location: Cyt... |
Q0A6F5 | MINRNHRPLRGVLSDPDEPAAAAALAHRLDLPLLTEPPETPALFLHHSRNGLALRSSGSNAPGPIRVSLDEGRQGQRLRQASLKRETLARACGLRGGRSLRIVDATAGLGRDAMVLAALGARVTLIERHPVIAALLADGLRRARRSHPELAARLHLVEADSLQWLAELTPAERPEVICLDPMYPAGSTRGAVRKDLQALRELPDWPGLAPVDEVALLALARASATARVVVKRPGRAAPLAGKAPDWQLPGRSTRFDVYRGLAGD | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28378
Sequence Length: 264
Subcellular Location: Cytoplasm
EC: 2.1.1.242... |
B4S2X7 | MLNSVPLVIAQHSTQDDTSLLNSIGNKWGFPVVSHSEKPAEGFYLQIQNGVLGLADASEKKVLPVEVDFASPASLYRKQHGGGRKEPIVKAIGLKGNEGWHVVDATPGLGRDAFVLVSVGCKVTMIERSPIVAALLEDGIRRLALSFPELAAKMSLQHGNSAEVMQYFTGENVNAIYLDPMFPHKKKSALVKKEMRLFQQLLGHDPDADALLPPALKLATHRVVVKRPNSADVLAGEKPSMAIESKKHRFDVYLCQKP | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28163
Sequence Length: 258
Subcellular Location: Cytoplasm
EC: 2.1.1.242... |
Q6MQB7 | MVSASLDGGLRICVRASAPEVHDKAVAWASFLKAPLNPENPEQYFFHFFVEPEGVYVRDQEKRLLEIDFDKNHLDYERKGHRGKNELIAKALGVAKGARRILDLSVGMGIDSVFLTQLGFSVIGVERSPVLYALLKEAFARTKKDSLKSYELHFADSLQFLKQNKGLLEVDAIYFDPMYPHKKKSALPKQEMVVFRDLVGHDDDASLVLQEALTWPVKRVVVKRPMQAEELLPGVRHSYEGKVVRYDTYVVG | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28576
Sequence Length: 252
Subcellular Location: Cytoplasm
EC: 2.1.1.242... |
P57646 | MKIYLKFKSYNKRICKLLQLFKLEHDQNCSMGLLINHNSLELYNRDNVNQKPIKVDFTSKKNHYRCHHFRRKNEVLYRVSGIKNSYFPTILDATAGLGNDAFIFSFLGCKVIMIERHPIVAALLKDGLQRGYQDKKIGHWLQTRLHLIVNDSLKMLEIPILQPDVIYLDPMYPFHHKKSLPKKDMQFFRQLIGHNYDSKKLLEVSRKLAKNRIIVKRPYYAKPLSEDKVNHIVTTRNHRFDIYQPF | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29240
Sequence Length: 246
Subcellular Location: Cytoplasm
EC: 2.1.1.242... |
B3PLF9 | MLSIPLVCSSDFAPAAQVLAQEFNLPIRVGEVPETIGDCEFVLVLDETGLALQQTGRKAPGAVRAEFTEGAVDHRRKFGGGKGQMIAKAVGVKAGFSPRVLDATAGLGRDAFVLATLGCRLQMIERSPLVFALLRDGLARAHAFAHAQDRELLQVVERMELAAQDSKTYLQGLAPEQFPDVIYLDPMFPERQKSADVKKEMRAFHSIVGTDEDADVLLPLALEHVRFRVVVKRPRKAPFLNNQIPSYQLEGKSSRYDIYTRKKLPD | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29370
Sequence Length: 266
Subcellular Location: Cytoplasm
EC: 2.1.1.242... |
Q7P0V2 | MTATPLYCAEPARLDTARRLCERFSLPLIKQRPADGYWLELGSERLELLTTGKHGAVYAEFVEGAARHRREQGGGRGQPVAKAVGLKGAKDLPHVADATAGLGRDSFVLATLGCRVTMVERSPVAAALLADALERAQRDETTRDIAARMTLVHANSRNWLAGLTEAQRPDVVFVDPMFPDTDKKSAAAKKDMQAFQQVIGDDMDSAELLAAAIAAARVRVVVKRPRLGAAIAGVKPSAVLDGKSTRFDLYVIKALASG | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27673
Sequence Length: 258
Subcellular Location: Cytoplasm
EC: 2.1.1.242... |
A9KB94 | MNDTLAITYSTPARLSEAEKLARQMKLPLVSLNSTDYSFLLVFTPAHLELRSTGTKAPGPLYVDFLKGATAHRRLFGGGRSQLIVRAVGLKSHPHPTILDLTAGLGRDAFVLANFGCDVLMIERNPVIALLLRDGLERAQSVEWFKSLKLELIEIDAQIYLSTLKKQFDVIYMDPMYPIRKKSALVKKEMRILRRLVGADDDAPQLLALALKKAKHRVVIKRPLLSNPLPGPAPDVVYEGKSSRFDVYLLKPSS | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28302
Sequence Length: 254
Subcellular Location: Cytoplasm
EC: 2.1.1.242... |
Q03516 | MNSTNSTNSTTTATSTNTSTQQVVTSLVSNGTIFGVFVIAFLILRIKLKRIYEPKSSFNLINEEKKPEPLPQGVWQWLKPLLKKSDNFVIQQAGLDGYFFLRYLFIIAIYCAVSMSYIFPILLSINASNGNHESGLNQLAYQNVKHRGRYFAHVFCGWIFFWGFLYIIYRELYFYTSMKQAVLASPRYAKKLSSRTVLFQTVPKQYLSEEEFSKLFDGVKRVWIARGSGSIEAMVKARDNMAIQLEGAETKYLKAALKKIKKLNKKSPQLSVSDNIAEYVPDKKRPHHKINKVAKFFFGKKVDTISYIKEELPKLNQKVK... | Function: Acts as an osmosensitive calcium-permeable cation channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 107673
Sequence Length: 953
Subcellular Location: Membrane
|
Q23121 | MAARIYIGRLTSRVSEKDIEHFFRGYGQIRDVLLKNGFGFVEFDDKRDAEDAVHDLNGKELGGERVILDYSKPRGGGGDRGGFGGGGRGGARVSSYSGGGGGGRDRFDRYDRGPPRRESRYGRPYSTRHRVVVENLSSRISWQDLKDQVRRQGVEPTYAEAHKRPNEALLCFATPSDLKRCIEKCDGMDLNGRKIKMIDDSQAGRSRSRSNSRSRSRSRSRDRRRSRSRSSSRSKSRSRSPPKRSRRESKSKSRSRSRSRSADNRKSRSPSRSPKKVDRSPSPPRGSRSPSEKGSPRRSRSASPMDNGDGDN | Function: Plays a functionally redundant role in spermatogenesis and growth rate control.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 35042
Sequence Length: 312
Subcellular Location: Nucleus
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Q27YU0 | MALGPFVLPFRGDQYSFGINFKSSPEEKLNFDLSCVAFDVKGQLHDTLHARKPTALDGALVKGFEKQALPEETVQVEGDDVIYMFPKKFERQVEVLLFVASAPSIPGKKHDLDSSSKLEFAVSYSDVGGQAFNQSFDLKPLAAQGGVSSIIVAVMYLQAEGGWTLRSVGDCHPFDSPGLIVPELKQTILNLRDHHGVQLDAADAIQAIDPAERVPVTRQFQDQSLDEASAGRAAEPAPVKKLRIDLSWTFWPPPPPTEEGEEPPEEPALEYNLVMYNKDGEEVQSISTGNREATGARAGRPEPEEDEEEEKEEEKEEPEE... | Function: Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to the a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the project... |
Q23120 | MVRVYIGRLPNRASDRDVEHFFRGYGKLSDVIMKNGFGFVDFQDQRDADDAVHDLNGKELCGERVILEFPRRKVGYNEERSGSGFRGREPTFRKGGERQFSNRYSRPCSTRFRLVIDNLSTRYSWQDIKDHIRKLGIEPTYSEAHKRNVNQAIVCFTSHDDLRDAMNKLQGEDLNGRKLKCTDETRDRSRSRSPRRRSRSRSPTRSRSPPARRRSPGSDRSDRKSRSASPKKRSDKRARSESKSRSRSGGRRSRSNSPPNRSPSPKKRRDNSSPRSGSASP | Function: Plays a functionally redundant role in spermatogenesis and growth rate control. Required for the development of somatic gonad structures and for progression from larval stage to adulthood.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 32421
Sequence Length: 281
Subce... |
Q6UBQ3 | MAPTQAGHDTAYLKETVGEALARGCAAAISAQPNDPVEYLGLWLLKYVKNAEVEGNFYRERQQDLQKKKDRLVKEAQSEQAAKSVALTRKEAADALALVTAEPRELLEAAVKLVKQHTAAGAAYAAVVAEPEEPDWVAPEDDEAAAVETEDEAAGGAALAEGEEPPPEPEPEPEAAPEDGEGDAPAPKIPRPVDYSKKYFAYVAASAGQEHVLEADLYRPAPPPEDADEDFKPEPLPYSFRVLDEKLPMLYVPNVAAEERVKFFRKFPKIGSYQACGVALPASGEFKALLAADTLFPEGSGQPLSADDRDFVWEVSQSLS... | Function: Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to the a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the project... |
Q9NEW6 | MPRGGSEDQKVYVGNLPGDVREKEVEDIFHKYGRIKYVDIKSGRGPAFAFVEFEDHRDAEDAVRARDGYEFDGRRIRVEFTRGVGPRGPGGRPLQDGGDHRGGDFRGGRGGGRGGGPQRRTGYRVIVEGLPPTGSWQDLKDHMRDAGDVCYADVARDGTGVVEFTRYEDVKYAVRKLDDTKFRSHEGETAYIRVREDNSSGGGSGGGGRDRSRSRSPRAERRASPKYSPRRSRSRSRSRSRSRSRSASRSPSRSPSPQ | Function: Plays an essential role in embryogenesis.
PTM: Directly phosphorylated by spk-1 in vitro on serine residues of the RS domain.
Sequence Mass (Da): 28680
Sequence Length: 258
Subcellular Location: Nucleus
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P12759 | MVQAKAQQQLYTHAAEPKAVQQRRAKYREDETTQTLPTANIMFDRRVVRGNTYAARILPADATQTQTKGPSPASTKKRTTRTLPPRTPEAVDGRRHIDIQTDVYLEELTDTVPEADTSTQTDAFLDRPPTPLFVPQKTGTDAITQIENGDLFDFDFEVEPILEVLVGKVLEQGLMEVLEEEELAAMRAHQEHFEQIRNAELVATQRMEAAERRKLEEKERRMQQERERVERERVVRQKVAASAFARGYLSGIVNTVFDRLVSSGYIYDPVMREVETAFMPWLKEQAIGYLARGVVARRVVDKLVEDAAAALAANRSTLAD... | Function: Protein 3 may attach the radial spoke to the outer doublet microtubule or is required to form a stable spoke structure.
PTM: Protein 3 is one of the 5 radial spoke proteins that are phosphorylated.
Sequence Mass (Da): 56785
Sequence Length: 516
Subcellular Location: Cytoplasm
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Q09511 | MSRGGGGDRRAAPDINGLTSLKIDNLSYQTTPNDLRRTFERYGDIGDVHIPRDKYSRQSKGFGFVRFYERRDAEHALDRTDGKLVDGRELRVTLAKYDRPSDERGGRGGGGGRRRSRSPRRRSRSPRYSRSRSPRRSRSRTRSPPSRDRRDSPDRRDNSRSRSRSPPPREDGSPKERRSRSRSASRSPSRSRSNSR | Function: May play a functionally redundant role in embryogenesis.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 22588
Sequence Length: 196
Subcellular Location: Nucleus
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P52108 | MNTIVFVEDDAEVGSLIAAYLAKHDMQVTVEPRGDQAEETILRENPDLVLLDIMLPGKDGMTICRDLRAKWSGPIVLLTSLDSDMNHILALEMGACDYILKTTPPAVLLARLRLHLRQNEQATLTKGLQETSLTPYKALHFGTLTIDPINRVVTLANTEISLSTADFELLWELATHAGQIMDRDALLKNLRGVSYDGLDRSVDVAISRLRKKLLDNAAEPYRIKTVRNKGYLFAPHAWE | Function: Member of the two-component regulatory system RstB/RstA.
PTM: Phosphorylated by RstB.
Sequence Mass (Da): 26704
Sequence Length: 239
Subcellular Location: Cytoplasm
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P18392 | MKKLFIQFYLLLFVCFLVMSLLVGLVYKFTAERAGKQSLDDLMNSSLYLMRSELREIPPHDWGKTLKEMDLNLSFDLRVEPLSKYHLDDISMHRLRGGEIVALDDQYTFLQRIPRSHYVLAVGPVPYLYYLHQMRLLDIALIAFIAISLAFPVFIWMRPHWQDMLKLEAAAQRFGDGHLNERIHFDEGSSFERLGVAFNQMADNINALIASKKQLIDGIAHELRTPLVRLRYRLEMSDNLSAAESQALNRDISQLEALIEELLTYARLDRPQNELHLSEPDLPLWLSTHLADIQAVTPDKTVRIKTLVQGHYAALDMRLM... | Function: Member of the two-component regulatory system RstB/RstA. RstB functions as a membrane-associated protein kinase that phosphorylates RstA (Probable).
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequ... |
P0AA45 | MRLDKFIAQQLGVSRAIAGREIRGNRVTVDGEIVRNAAFKLLPEHDVAYDGNPLAQQHGPRYFMLNKPQGYVCSTDDPDHPTVLYFLDEPVAWKLHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPVADDTAEQFAKGVQLHNEKDLTKPAVLEVITPTQVRLTISEGRYHQVKRMFAAVGNHVVELHRERIGGITLDADLAPGEYRPLTEEEIASVV | Function: Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA.
Catalytic Activity: uridine(516) in 16S rRNA = pseudouridine(516) in 16S rRNA
Sequence Mass (Da): 25865
Sequence Length: 231
EC: 5.4.99.19
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Q9CPN4 | MRLDKFLAENTGLTRSQANKVLKQSAVTVNGHVEKNGAQKVSQTDEICLEGEHLPWVSAGQYLMLYKPQGYVCSHEDGDYPTIYQFFDYPLAGKLHSAGRLDVDTTGLVLLTDDGKWSHRITSPKHHCEKTYLVTLADPVESHYQQACAEGMLLRGEKTPTKPATLEILDDYNVNLTISEGRYHQVKRMFAALGNKVVGLHRWKIGQIELDDRLAEGEYRSLSAEEIATFNK | Function: Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA.
Catalytic Activity: uridine(516) in 16S rRNA = pseudouridine(516) in 16S rRNA
Sequence Mass (Da): 26096
Sequence Length: 232
EC: 5.4.99.19
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P77285 | MLKTIRKHGITLALFAAGSTGLTAAINQMTKTTIAEQASLQQKALFDQVLPAERYNNALAQSCYLVTAPELGKGEHRVYIAKQDDKPVAAVLEATAPDGYSGAIQLLVGADFNGTVLGTRVTEHHETPGLGDKIELRLSDWITHFAGKKISGADDAHWAVKKDGGDFDQFTGATITPRAVVNAVKRAGLYAQTLPAQLSQLPACGE | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21912
Sequence ... |
O81127 | MTRVYVGNLDPRVTERELEDEFKAFGVLRNVWVARRPPGYAFLEFDDERDALDAISALDRKNGWRVELSHKDKGGRGGGGGRRGGIEDSKCYECGELGHFARECRRGRGSVRRRSPSPRRRRSPDYGYARRSISPRGRRSPPRRRSVTPPRRGRSYSRSPPYRGSRRDSPRRRDSPYGRRSPYANGV | Function: Probably involved in intron recognition and spliceosome assembly.
PTM: Extensively phosphorylated on serine residues in the RS domain (By similarity). Phosphorylated by AFC2.
Sequence Mass (Da): 21537
Sequence Length: 187
Subcellular Location: Nucleus speckle
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Q6K4N0 | MARLYVGNLDPRVTSGELEDEFRVFGVLRSVWVARKPPGFAFIDFDDKRDAEDALRDLDGKNGWRVELSRNSSSRGGRDRHGGSEMKCYECGETGHFARECRLRIGPGGLGSGKRRSRSRSRSRSPQYRKSPTYGRRSYSPRDRSPRRRSVSPVRGRSYSRSPRGRGGSPYADGRDGGRYRRSRS | Function: Involved in pre-mRNA splicing.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 21023
Sequence Length: 185
Subcellular Location: Nucleus
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O81126 | MSRVYVGNLDPRVTERELEDEFRAFGVVRSVWVARRPPGYAFLDFEDPRDARDAIRALDGKNGWRVEQSHNRGERGGGGRGGDRGGGGGGRGGRGGSDLKCYECGETGHFARECRNRGGTGRRRSKSRSRTPPRYRRSPSYGRRSYSPRARSPPPPRRRSPSPPPARGRSYSRSPPPYRAREEVPYANGNGLKERRRSRS | Function: Sequence-specific RNA-binding protein probably involved in pre-mRNA splicing. In vitro, can complement efficiently splicing-deficient mammalian SRSF7-depleted HeLa cell extract.
PTM: Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by AFC2.
Sequence Mass (Da): 22458
Sequence Leng... |
Q9FYB7 | MPRYDDRYGNTRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFVEFSDPRDADDARYYLDGRDFDGSRITVEASRGAPRGSRDNGSRGPPPGSGRCFNCGVDGHWARDCTAGDWKNKCYRCGERGHIERNCKNSPSPKKARQGGSYSRSPVKSRSPRRRRSPSRSRSYSRGRSYSRSRSPVRREKSVEDRSRSPKAMERSVSPKGRDQSLSPDRKVIDASPKRGSDYDGSPKENGNGRNSASPIVGGGESPVGLNGQDRSPIDDEAELSRPSPKGSESP | Function: Probably involved in intron recognition and spliceosome assembly.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 31823
Sequence Length: 284
Subcellular Location: Nucleus
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Q8VYA5 | MPRYDDRYGNTRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFVEFGDPRDADDARHYLDGRDFDGSRITVEFSRGAPRGSRDFDSRGPPPGAGRCFNCGVDGHWARDCTAGDWKNKCYRCGERGHIERNCKNSPKKLRRSGSYSRSPVRSRSPRRRRSPSRSLSRSRSYSRSRSPVRRRERSVEERSRSPKRMDDSLSPRARDRSPVLDDEGSPKIIDGSPPPSPKLQKEVGSDRDGGSPQDNGRNSVVSPVVGAGGDSSKEDRSPVDDDYEPNRTSPRGSESP | Function: Splicing factor involved in constitutive and/or alternative splicing. Regulates the splicing of its own pre-mRNA and the alternative splicing of RS30, RS31 and RS34. Associates the cyclin-dependent kinase G1 (CDKG1) with the spliceosome and recruits it to U1 snRNP to facilitate splicing.
PTM: Extensively phos... |
P23070 | MKSAEYLNTFRLRNLGLPVMNNLHDMSKATRISVETLRLLIYTADFRYRIYTVEKKGPEKRMRTIYQPSRELKALQGWVLRNILDKLSSSPFSIGFEKHQSILNNATPHIGANFILNIDLEDFFPSLTANKVFGVFHSLGYNRLISSVLTKICCYKNLLPQGAPSSPKLANLICSKLDYRIQGYAGSRGLIYTRYADDLTLSAQSMKKVVKARDFLFSIIPSEGLVINSKKTCISGPRSQRKVTGLVISQEKVGIGREKYKEIRAKIHHIFCGKSSEIEHVRGWLSFILSVDSKSHRRLITYISKLEKKYGKNPLNKAKT | Function: Reverse transcriptase (RT) component of antiviral defense system retron Ec86, composed of a non-coding RNA (ncRNA), a ribosyltransferase/DNA-binding protein and this RT. Expression of the 3-gene retron confers protection against bacteriophage T5. At multiplicity of infection (MOI) of 0.02 cultures grow normal... |
P0DV59 | MKTKKMILVDKVFYEKILSVESFKENIITQSAIPKISNKEVRLISSGSKIFYAINNTSPHSHVQLRLNRFFLSHIPLNSAAKAFVRGGSYLKYLEPHIYGSSYCRLDISSFFNNISFDDVKQSLSPYIKDEYLIGTEQKLIDAILNSVGYESPIRKDKGMIIPMGFRTSPAISNIVFRKMDLLIQDFCAKKGVIYSRYADDMLFSNPRESKLLMSDYFIDEISSLLSIMGFNINQSKYISREKEISINGYVIENKGGNGSIGTIRLSKSKLNTVLKVTHALAQNIPYKNICNKYIKVRLKEKNIKYESKKDEFEKKYYRD... | Function: Reverse transcriptase (RT) component of antiviral defense system retron Eco8, composed of this RT, the following endonuclease and a non-coding RNA (ncRNA) encoded between them. Expression of retron Eco8 confers protection against bacteriophages T4, T6, T7 and SECphi4, SECphi6 and SECphi18. At multiplicity of ... |
P0DV94 | MNILTTLREQLLTNNVIMPQEFERLEVRGSHAYKVYSIPKRKAGRRTIAHPSSKLKICQRHLNAILNPLLKVHDSSYAYVKGRSIKDNALVHSHSAYVLKMDFQNFFNSITPTILRQCLIQNDILLSVNELEKLEQLIFWNPSKKRNGKLILSVGSPISPLISNAIMYPFDKIINDICTKHGINYTRYADDITFSTNIKNTLNKLPEIVEQLIIQTYAGRIIINKRKTVFSSKKHNRHVTGITLTNDSKISIGRSRKRYISSLVFKYINKNLDIDEINHMKGMLAFAYNIEPIYIHRLSHKYKVNIVEKILRGSN | Function: Reverse transcriptase (RT) component of antiviral defense system retron Vc95, composed of a non-coding RNA (ncRNA), this reverse transcriptase (RT), a probable ATPase and a putative HNH endonuclease. Expression of retron Vc95 confers protection against bacteriophages T2, T4 and T6. At multiplicity of infectio... |
B2KWI0 | MSPESKKITAHGSTSMPLSRTSKPQKFTIPLTVGAIFSVIGFLQRFFLASGKGDVQSLYTLSTMFILGAGPTYAGADYFICGRLFSFVPSAAPMSPIRVVRTFITFDVLAEVCVWTGAGLLAGAHTDTAARYKIGLNLIRAAMITQAFLFTSFVAILASFHVRVCALRAEWSVTSNGGTGRRFMMVVHSLYASSIFIIIRSAYHIAGHSFRTNEQPFLICEASLMLLNTAMFNVFHPGHILPIDSRVYVGIDGQERANETIEGAFTDSRPLLQKILDPLDVKGLFSRDKKRWHDPTAELEMDINSTLYAALT | Function: Lipid-translocating exporter-like protein; part of the gene cluster that mediates the biosynthesis of hydroxamate-containing siderophores that play a critical role in virulence via intracellular iron acquisition during macrophage infection .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 3... |
E5AE43 | MNAYAYTACLGIYGSTPNNEQLVLGSPDQLQRNKPRFRLIVLPHAPAASPFYPPWRSFAPDWEGQGARPMDHFKVGNLRFQLETHRIDEHSTFGKLFGHAPSPSQSCVSFQKKSDRAEPLLLARCSAASWSCIHPPTVLYFVAYQLEYPFAARFSATKISPIQDKMVATSDVPIVGSLYVYAPNKGAPIFFTIAFAISTILHSWQCHRYKAWKLIWLQPACAALFTLGYALREYGAYNYLYDGTEKAPLALFILSQICIYLGPPLLELANYHILGRVFHYVPYAAPFNPGRVTAFFGGLMAIVEGLSGSGVSLTANAKAK... | Function: Lipid-translocating exporter-like protein; part of the gene cluster that mediates the biosynthesis of phomenoic acid, a long chain aliphatic carboxylic acid that does not appear to be essential for pathogenicity but may play a role in allowing to outcompete other fungi in the environmental niche via its antif... |
P53047 | MAKDGFELYRYTPELGASILFTVLFAVSGVAFVILLFHYSVKSKRRVGSLMKSQPVLRYYGTVNLAGAYIPFIFGCFVECVGFAFRCKSSKDTTLLNPYIIQTVFLLVSPTLYAASIYMIFGRMATLLFAENLMIMPARFNTTIFVIGDVGSLLLQAIGGAMMSKVTSASSGSHLVTAGLFIQIAFFGLFIINEVLFIFKMSKKPTNVSVRYGSWKYLNIALLVNSFLILIRSIVRAVEFIQGYDGEIASHEWYLYIFDGLPMFLLVLIFIVAFPLINIFRIHEESIQAQQSARFDGTDYPDVEVTSIEEDLASKSE | Function: Involved in 7-aminocholesterol resistance.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35486
Sequence Length: 317
Subcellular Location: Membrane
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Q9BSG5 | MDCRVHMRPIGLTWVLQLTLAWILLEACGGSRPLQARSQQHHGLAADLGKGKLHLAGPCCPSEMDTTETSGPGNHPERCGVPSPECESFLEHLQRALRSRFRLRLLGVRQAQPLCEELCQAWFANCEDDITCGPTWLPLSEKRGCEPSCLTYGQTFADGTDLCRSALGHALPVAAPGARHCFNISISAVPRPRPGRRGREAPSRRSRSPRTSILDAAGSGSGSGSGSGP | Function: Riboflavin-binding protein which might have a role in retinal flavin transport.
PTM: Not N-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24615
Sequence Length: 229
Subcellular Location: Secreted
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Q5DRQ5 | MACRSHIQPSDLACTMQLALAWIILGACGGSHQFQARSQGHLGLASNLGTNQVQLAGDLQASGPQPYMMIQDPDSQAFPLPEPCCPSEMDTPETSGPGIFPPRCRTPSSGCESFLGHLQRALRNRFHLLLLGVRQAPPLCEELCQNWFATCEADITCGRTWLWPSGKRSCEGRCRTYGQTFADGVDLCRSVLGHILPVAAPGSRHCLNISISLLPRPRPGRWARETISQRSRRRGTGILDAGGSGSGSGSGSGP | Function: Riboflavin-binding protein which might have a role in retinal flavin transport.
PTM: Not N-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27236
Sequence Length: 254
Subcellular Location: Secreted
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Q8QZY4 | MAHEGHSQHSGLVWALRPILAWIFLVACGWSHPLQTRSWGHPGLAAKVRTGQLQPAGHPQSSVLPSYPRIQVPGSQTPPVPVPCCTAEIDRPESLLESCGAPSPECEFFLGQLQGALRDRFHPQLFGARPVQPLCPELCQIWFTTCQADFICGPTWLQSSGERGCEPSCRTYGQTFANATDLCHSVLGHVLRVAAPGSSHCLNVSISSPGARRRPRAWISNVVGSGSGSGSGDSPEPMFGFQYVSLP | Function: Riboflavin-binding protein which might have a role in retinal flavin transport.
PTM: Not N-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26559
Sequence Length: 247
Subcellular Location: Secreted
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Q60335 | MDFIVIDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLSPKDFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGGGEVIFEVKPSKIKKFDLIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNKEKLLPNIKIECSKGISTGAGIVLWNDTLGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAFGKGIVGVSEITNHTKTNMWVVKHFLDVDF... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
O27937 | MIVIDGSEGEGGGAVVRVSTALAAVTSRSVRVYNIRARRSRSGLSHQHLTAVRAVARISNGTLRGDELGSMELEFSPGRVTGGTFNFDVKTAGSTGLVLQAIMVAAAASEGEIDVTVSGGTDVLWAPTCDYLREVTIPVLEMMGYSARIEIIRRGYYPEGGGRVHAIIEPSELRPITLEESEIHAVRGISHSRNLPVHVAERQAESAMKILRGAGLDVDIMVEDASGPVGRGSGITLWAEGNTRLGAVSLGKPGKRAEKVGSEAARELLGFIESGSPLDRYMGDQIIPYMALTGDSRVRTCELTLHAETNIILSEKITGR... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
A0B532 | MIEIDGSYGEGGGQIVRTSVALSTLTGIPVRIKNIRRNRPRPGLAAQHVRAIEALAQISRAETRGVHLGSEEIEFIPGRISAGSYDVDIGTAGSVTLLIQCLLPALTAAEGPVTVTVRGGTDVRWSPTVDYLEHVALPAMHLFGVTATFRCERRGYYPRGGGVVVLSTRPSRLRPARLELIEEGICGISHCGSLPEHVARRQADAALELLKEKGYDARIDIQTMSSSSPGSGITLWSGFRGSSALGERGVRAEDVGREAAKALIDELKSKASVDVHLADQLIPYIALAGGEYTTREISSHTRTNIWTAQRILRCRIDIDE... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
Q9D7H3 | MEGQRVEVDGGIMEGGGQILRVSTALSCLLGLPLRVQKIRAGRSTPGLRPQHLSGLEMVRDLCGGHLEGAEIGSTEITFTPEKIRGGVHTADTKTAGSVCLLMQVSMPCVLFAASPSELRLKGGTNAEMAPQIDYTMMVFKPIAEKFGFTFNCDIKTRGYYPKGGGEVIVRVSPVKRLDPINLTDRGSVTKIYGRAFVAGVLPLKVAKDMAAAAVRCIRKEIRDLYVSIQPVQEARDQAFGNGSGIIIVAETSTGCLFAGSSLGKRGVNADKVGIEAAEMLLANLRHGGTVDEYLQDQLIIFMALANGISRIKTGSVTLH... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
Q2Y720 | MQEIDGSYGEGGGQLLRTSVALAAITGQSVRVYNIRAKRSNPGLAPQHLTAVKAVAALCRARTEGMEVKSQEIIFRPGPLRGGEYDFPIGTAGSVTLVLQAALPVALACGEKVRMNISGGTDVRAAPPLDYFRYVLLPLVYSMGARAKIEVLLRGYYPRGGGKVVVDVEPCLPLRPVLLNASEGLEGITGFVHISNLPKHIIHRMANGALAELSTFPTPAVGLEVFGKDDAIGEGGAVLLTAHKEHSRLGASAVAERGVPAERLGAEAGRCLREEILSGATLDIHAADQVLIYLALASGVSCFLTRELSSHAATTIWLLE... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
B2IWJ8 | MIEIDGSYGEGGGQVLRTSLSLAAITGEPIRIAGIRAGRKKPGLAAQHLTAVRAAGRICNAQLRGDALGSMLLEFIPGSAVQAGIYTFDVSKAQEGGSAGAIALVLQTILLPLALATGNSQVTLKGGTHVNFSPTVTYIEQVYLPILQRMGVEAQVKLGAWGWFPQGGGEIELQVIGGTQLGGINLLERGELQQVRGIAAVTELPSHIPQRMANRAENLLREAHLKVRVQTLREKGVAPGAGIFLTAEYQNSLTGFGGFGRLRLSAETVAEIACQQLLEFHYTGAAVDEHLADQLLLPATLASQESQYQVAEVSRHLITN... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
Q4KEB8 | MKQDVVELDGAIGGGQVLRSALSLSMLTGKTLRIHNIRARRSRPGLLRQHLTAVLAAAQVCGARSTGAELGSQVLSFEPGPIRGGDYRFAIGTAGSCTLVLQTLLPALLRAPQPSRVSISGGTHNPLAPPVDFLQQAWLPQLRRMGGRVELQLLRHGFVPAGGGELEAFIQPSELQPLHLQERGALLGSRAWALSAGLPEHVAERELRRVHDRLQLPREQLTPVLLDEEYGPGNVLLLEFAFEHLTELFCGFGQNSLRAEKVADGAIDQARDWLDSGAAVAEHLADQLLLPMALAGGGSFTTPCMTEHLQSNIRVIEAFL... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
Q9V0Z6 | MITIDGSYGEGGGQILRTSIALSAITGEPVRIINIRANRPNPGLRPQHLHGILALKHLANADVKGAHVGSRELVFIPKRLEAKKVEVNIGTAGSITLVLQALLPAMAFAKNRVEFKITGGTDVPWSPPVDYLANVTLFALEKLGIMAGIKIVRRGHYPKGGGIIEGYVEPWKERRELVATKYSSIAKVEGISHATNLPAHVAERQAKAAKEELSKLEVPVKIKTEVSKSLGPGSGIVVWAETDCLRLGGDALGKRGKPAEVVGKEAAQELLEQLKPGYCVDKFLGDQLIPFLAFSGGEIWVSEVTNHLKTNIWVVENFLG... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
P24931 | MKSLKGSRTEKNILTAFAGESQARNRYNYFGGQAKKDGFVQISDIFAETADQEREHAKRLFKFLEGGDLEIVAAFPAGIIADTHANLIASAAGEHHEYTEMYPSFARIAREEGYEEIARVFASIAVAEEFHEKRFLDFARNIKEGRVFLREQATKWRCRNCGYVHEGTGAPELCPACAHPKAHFELLGINW | Cofactor: Binds 3 Fe(3+) ions per subunit.
Function: May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide.
Sequence Mass (Da): 21544
Sequence Length: 191
Subcellular Location: Cytoplasm
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Q58144 | MINNFFVINMKETLKNLTKAYIGESLARNRYTCYAKIAKQEGYEQIAEIFLLTAENEREHAKWLYYLITELKKKYNIDDKAIKVDGVEVPIVLGNTAENLKASIEGEHFEHTEMYPKFADIAEKEGLKEIADRLRAIGIAEKHHEERFKKLLKEVEEGTVFKKDKPVEWVCRKCGFVHLGKEPPEKCPSCSHPRKYFEVKCEKY | Cofactor: Binds 3 Fe(3+) ions per subunit.
Function: May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide.
Sequence Mass (Da): 23835
Sequence Length: 204
Subcellular Location: Cytoplasm
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Q9AGG3 | MSIKKKTEMNKSIKGSKTEKHLLMAFAGESQARSRYTFFASVAKKEGYEQIAGVFMETAEQEKEHAKRFFSFLEGGMLEITASFPAGIIGSTAENLRAAAAGENEEWTDLYPAFAETAEEEGFKEIAAVFRQIAKVEAEHERRYLALLAHVEDGSVFERTEEIAWQCRNCGYVITSKKAPKLCPACAHPQAYFEPMKTNY | Cofactor: Binds 3 Fe(3+) ions per subunit.
Function: May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide.
Sequence Mass (Da): 22456
Sequence Length: 200
Subcellular Location: Cytoplasm
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Q12234 | MGKNKKKTGKKAKSHPHVEDVDETVNKPEEIINSVNVTVPPKMSTDPEADGIVASPDDEGKDLSEGVDKQKVNDGLTVDTINPLEDKKAGDEMKELREEIERLKLELSHKKDQETPNEDFKNELANVIKERDEFKTQYDTLLSKISSMKSIFNKMKEAQKQLEEVQEQLTEYESQNLKLKKKLEATKTENSELQSTIVTLNTELENLEKEQESTEEVFLEYESRIEALEDEKHDIIEKHSKELNTYRKEKDQLNLQVQELMIILENNKQDISDLRTERDELRQALESHEKEKAVLKNSLNDLELKIEEVDNKREEEARER... | Function: Involved in the structural organization of the cis-Golgi and in vesicle targeting/fusion stages of ER to Golgi transport.
Sequence Mass (Da): 56069
Sequence Length: 484
Domain: The GRIP domain binds to ARF1, which leads to the Golgi localization of RUD3.
Subcellular Location: Golgi apparatus lumen
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Q96T51 | MADREGGCAAGRGRELEPELEPGPGPGSALEPGEEFEIVDRSQLPGPGDLRSATRPRAAEGWSAPILTLARRATGNLSASCGSALRAAAGLGGGDSGDGTARAASKCQMMEERANLMHMMKLSIKVLLQSALSLGRSLDADHAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKHLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLCLKGEDLDSQVGVIDFSLYLKDVQDLDGGKEHERITDVLDQKNYVEELNRHLSC... | Function: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in early endosomal trafficking.
PTM: Phosphorylation on Tyr-389 and/or Tyr-400 is required for interaction with BMX and endosomal targeting.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 79818
Sequenc... |
Q9D394 | MSALTPPTDMPTPTTDKITQAAMETIYLCKFRVSMDGEWLCLRELDDISLTPDPEPTHEDPNYLMANERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANFCMKGEDLDSQVGVIDFSMYLKDGNSSKGSEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEES... | Function: Plays a role in the generation of neuronal polarity formation and axon growth . Implicated in the formation of a single axon by developing neurons . May inhibit the formation of additional axons by inhibition of PI3K in minor neuronal processes (By similarity). Plays a role in the formation of F-actin-enriche... |
Q6ZNE9 | MAEEGAILKVTKDLRAAVSAILQGYGDGQGPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFELDLQQPDLDGAWPMFSESRCSSSTQTQGRRPRKNKDAPKKIPAAYGGPENVQIEDSHTSQAICLQDAPSGQQLAGLPRSQQQRHLPFFLEKKGESSRKHRYPQSMWEPEGKELQLDQEERAPWIEIFLGNSTPSTQGQGKGAMGTQKEVIGMEAEVTGVL... | Function: Positively regulates macroautophagy in primary dendritic cells. Increases autophagic flux, probably by stimulating both autophagosome formation and facilitating tethering with lysosomes. Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through its FYVE-type zinc finger.
Sequence Mass (Da): 64350
Sequence ... |
Q6FFZ9 | MNYQLFKHSDENASYVVFSSGLGGHGSFWQAQLDVFRQYFHVLIYDQEGCHASSELLADGYSFEHLALQVKQLLQQLNIVRFHFIGHALGGFIGIELAHRYASETCQLLSLTLINAWQQLDPHTLRCFTTRIALLQHAGTAAYLHAQALFLYPPLWISEHTALLEQQEAKMQSDFPPHANVLKRLNALMQYQVNTARIDTLKQLPVCLIANQDDMLVPYVQSLNLWKKLPDAQLKLLPYGGHASTVTEARQVNQLMLDFLKTSAPT | 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): 30161
Sequence Length: 266
EC: 3.5.1.-
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Q7CWX3 | MHFEVHGRTDAEAPTILLSSGLGGSSAYWLPQIEALSDHFRIVTYDHRGTGRTGGEVPTEGGISAMADDVLEIVSALNLEKFHFMGHALGGLIGLDIALRQPRLIDRLVLINAWSKADPHSGRCFDVRIELLEKSGVDAFVKAQPLFLYPAAWMSEHQERLARDDAHGVAHFQGKTNVLRRIAALRAFDIDARLGEIGNPVLVVATKDDLLVPYTRSLRLAEGLPQSELCLLDFGAHAVNITEPDLFNTRLLQFLLPADQT | 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): 28691
Sequence Length: 261
EC: 3.5.1.-
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A8IAD8 | MPYAHGGDADLYYEIHGAGTPILLSAGMGGGAGFWRPQIEALAARHQVILYDHAGTGRSGRDIGPRSITEMARDMARVLDAAGVEDAHVAGHAIGGIIGMELALAAPERVRSLTIVNGWARADGFLRRCFEVRKRILLASGPEAYVRAQPLFLYPPRWIAENIAVLEEEEAQMVAHFPGTQTMLNRIETFLAFDGRERLADIRVPTLLAAAKDDALVPSYLSTLLAEGIPDARIAEVDWGAHAFSAVTPDVFNEMLLGFCGEIDQ | 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): 28703
Sequence Length: 265
EC: 3.5.1.-
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Q9A4N3 | MRRMTIGTVDGLHYELHGGPIAGREVVLLSSGLGGSGAFWAPQMQALTQRWPVVTYDHRGTGRSVRELPPRYTLAHMADDMVKVMDALGLAKAHVVGHAAGGNAGLQLALDHPDRLAKLVVVNGWSRPDPHIRRCFDTRLHLLNDTGPEAYVHAQPIFLYPADWISRNHTRLMAEEAHHVAAFPPREVMLARINALLAFDIDARLEDITHRVLISASADDMLVPMSCSQRLAGRLPNADFQQVAWGGHGFTVTDPETFNEALVSFLEGA | 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): 29553
Sequence Length: 269
EC: 3.5.1.-
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C8U5H1 | MKLSLSPPPYADAPVVVLISGLGGSGSYWLQQLAVLEQEYQVVCYDQRGTGNNPDTLAEDYSIAQMAAELHQALVAAGIEHYAVVGHALGALVGMQLALDYPASVTVLISVNGWLRINAHTRRCFQVRERLLYSGGAQAWVEAQPLFLYPADWMAARAPRLEAEDALALAHFQGKNNLLRRLNALKRADFSHHADRIRCPVQIICASDDLLVPTACSSELHAALPDSQKMVMPYGGHACNVTDPETFNALLLNGLASLLHHREAAL | 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): 28929
Sequence Length: 266
EC: 3.5.1.-
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C1F8Z2 | MIAHLRGTLLSKQPGQAIVECAGVGYDVAISVPTFTALPAEGAEVRLHIHTQVSEDAIALFGFLDREEKRLFERLITVSGVGPKLAIKMLSGLSPERTVAALRAQDHASLTRIPGVGKKLAERLVVELKDKLDDLIAAAPAAGPVAAGPAAEDVLSALLNLGYQRPAALKAIETAVEKDAAAGEDFDLLFRAALKLIR | 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 ... |
A5G2L3 | MIGRLCGTAEQIEDGRCLIDVSGVGYVVFCSARSLAALPAPPARATLLVETQVREDAITLFGFIDAAERDWFRLLTTIQGVGAKVALNLLSALPPDQLASAIAASDRGAITRAPGVGPKLAARLISELRERIAAMPTGSAFIPTGTAPPVAPPQGKLADALSALVNLGYRRAEAEAALSAVQAEAGEDAALDELIRGGLRRLAR | 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 ... |
B7J3G2 | MITSLTGTILQRRPPWLWLDVQGVGYELEMPLSGFYQMPAEGAALTVHTHLTIREDAHLLYGFMTVAERDMFRLLIRVNGIGGKVALACLSGLPAERLSQAVAEGNTAQLTAIPGIGPKTAERLVVELRDKMGGIAPGPMGRGGAGDPRQEAIAALLTLGYKPAQASQAIAGLADGLGLEDLIRQSLQNLSRH | 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 ... |
A0KPA3 | MIGRLRGVVIEKQPPEVLLEVGGVGYEVQMPMSCFYDLPEIGKEATIHTHFVVREDAQLLYGFNHKQERALFRELIKTNGVGPKLALAILSGMTATQFVLSVEREEISSLVKLPGVGKKTAERLVVEMKDRLKGWVSHDLFSPAEITLPARESALRAPDSSEEAASALVALGYKPQQASQIVSKVAADGMSVEDIIREALRSLV | 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 ... |
Q8U9K5 | MIGKLKGSIEEIGADYVLVDVHGVCYVAYCSARTLSKIGSVGEAVVLFIETYVREDQLKLFGFVSALEREWFNLLQSVQGVGSKVALAVLSTLSPSELANAIALQDKTMISRAPGIGPKVAVRLVTELRNKAPAFAGDASASIGLKQELGEGVASAPVADAVSALTNLGYSRDQAANAVAAALKNGGEGGDSAKLIRLGLKELSR | 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 ... |
Q5E6A0 | MIGRLRGNLLEKQPPELLIEVSGIGYEVQMPMSCFYELPEVGSEAIIYTHYVVREDAQLLYGFNTKNERALFREVIKANGVGPKLGLAILSGMTAAQFVQSVEREDISTLVKLPGVGKKTAERLVVEMKDRLKGWGAGDLFTPATDAAPMDDGSEFITSPQSAVDEAVSALIALGYKPQQASKTVSQIAKPDMTSEVLIRESLKSMI | 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 ... |
P44632 | MIGRLQGILLEKQPPEILLNVQGVGYELLLPMTSFYDLPEIGQETTLFTHLVVREDAHLLFGFAQKTDRTLFRELIKTNGVGPKLALAILSAMSVEQFAYAIEREELSKLTKIPGVGKKTAERLLVELKGKFKGVKQSDFFVESTHIPLSPSIESHSESSSDEAISALIALGYKPVEAEKMVKRVAKPELTSEQVIREALKVAL | 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 ... |
A1WZ64 | MIARLRGTLLEKRPPTLVVEANGLGYEVEAPLSTIEALPETGREVILHTHLSVREDGQTLFGFRTRAERDLFRRLIRVSGVGPKLGLALLSGVDGEELVRCVRDDDPKRLTQVPGIGRKTAERLIVELRDRLDGVGGGSTAAPAAGADHPTGENDPVSEAIEGLVALGYKPPEAARMARNAAEPELGCEAIIRRALQRAVPRGG | 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 ... |
B8CXG3 | MIGYLKGNVIWKAENKVILETGGVGYRVLVPSTVRLKPVGEKLELFVYTYVREDSLDLYGFKTMEERELFETLLSVSGIGPRAAINILSSLSYKKFIEAILTEKVSILKQVSGIGPKTAKRLILELKGKLKDMSGDFEEPLPDNRNTELSDALASLGYSELEIEEALSNADIKNNGSLEENIKKALGYLGSKGS | 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 ... |
C4K7I5 | MISRMKGIILEKQPPWILLDIQGMGYDIQLPMTCFYQLPELGQEAIIFTHFVVREDAQLLYGFHHPKERAMFSELIKVNGVGPKLGLAILSGMSSEEFICALEKEDISNLIKLPGVGKKTAERLLVEMKDRIKNLNKNLFKSTADHMLSSVSTDLSAKSAEAEAISALISLGYKPQEAAQLIKNIAQPDLDSQALIKHALRSTL | 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 ... |
O25549 | MIVGLIGVVEKISALEVHIEVQGVVYGVQVSMRTAALLEAGQKARLKILQVIKEDAHLLYGFLEEGEKILFERLLKINGVGGRIALAILSSFSPNEFESIIATKEVKRLQQVPGIGKKLADKIMVDLIGFFIQDENRPARNEVFLALESLGFKSAEINQVLKTLKPNLSIEAAIKEALQQLRS | 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 ... |
Q5YTE7 | MIASVRGEVLEIALDHVVVEAAGVGYRLNATPSTLATLTRGAEARLYTAMIVREDSMTLYGFADTEARDLFGLLQTVSGVGPRLAMAVLAVLEPEALRKALAESNVAALTRVPGIGKRGAERMVVELRDKVNLVPVQAGPPGSTPAVAATPVREQVVEALTGLGFPLKQAEQALDTVLAEQPAADTSTALRAALSLLGKNR | 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 ... |
Q8EPQ5 | MIAYIKGTLNSLGDESLIVDVGGIGYEIVCPNPFVFQDLLNQQIHIQTYHHVREDAQILFGFQNRDEKYLFTKLISVSGIGPKGALAILAGVDISGFIAAVENEDDKFLTSFPGVGKKTARQIILDLKGKLTSVFSITDEQQKSSVSNVNNNEVYSEAMEALKALGYTDKEVKQVLPHLKKDNDALSVDEAIRKALALLAK | 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 ... |
B1ZN17 | MITSIQGTLVSATPLQAIVEVAGFGYEVHIPVTTAERLPAAGAAVKLHTLVIYREDSQTLYGFASPAERDFFRLMIEHVTGVGPKMALSIMSRLALPSLESAIRMGDVASLAKCPGIGKKTAERLVVELRTKVGATGAAPGLATQPAAAASPGASAHRDAVAALVALGYRSADADEAVRRASLALGEAATTESLIKKALS | 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 ... |
A1AZW3 | MIGRIAGVILHRAQDHVLIDVRGVGYIVHVSERTAANLPPAGQATALYTELLVREDLLQLFGFPTLLEKEWHRLLTSVQGVGAKVALAILGTLGPDGLSRALALGDWSALRKAPGVGPKLAQRVVMELKDKAPAVMALGGALTVDPGPLPEVELVEAAVPAPVPAKAAPSSAQATADALSALGNLGYAPSEAASAVAEAAAREPAAPTAALIRAALRLLAPKE | 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 ... |
Q7U7F0 | MIGWLKGDVQHRDQKGSRNLVLIACGGVGYDVQLIERDWQAVSTDQRHEFWIHQVVSADNLQLFGFLQLAERDLFRELIQVSGVGPQAGLALLNACAYKELVTALVHSDLKTLCRAKGVGKRTAERLALELRTRLTDSVASTGPERNQLDPVAPDLIATLETLGFETHEIRDALQRLNGMGGPQDGDDDDAWLRACIKLMSSTDP | 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 ... |
Q6MFA5 | MFAYIKGVLAFFNPSQAIVDVHGVGYLLFIPCRLLGQLPQIGEPVQFYTTYVVREFSHTLYGFLSYQERDIFEILMNVTGIGPKMALSLIGHLSMSELQIAVMRQDLSTLCRVPGVGKKTAERLIVELKDKLAAIGHLDTSDHIEPLTQDPKSKSVQDAMLALINLGYNQTTAQKAIKQGMKELPEEIDLAQLITVALKHV | 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 ... |
Q83GK0 | MIASLSGLLEAVRPGSVVVNMHGIGFLVRVPQSFNPEVDAEVKLYTSLQVREDSVSLYGFASVLECTVFEQLITISGVGPRVALAILSVLTPAEVAAAVLEGDDKPLQRVSGVGKKLAGTIVLQLAGKLTSVPLENRKQEQAVDRSAEIVQALIGLGWQRQESAAAVESVLEKDQSLTMPEILRNALRYLAKQE | 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 ... |
B5ZBT6 | MNYLVFKVIYANANVVIGEHNFIGYQIRVPKDYELEVNKFCKLYLYEYASIMPNKNLIIKDLYGFRTYNERLLFIDLISINSIGPKTAINILKYDINLIIDAIATKDVDFLATIKGVNQRSANLICDQLNYKYINKVSEKNPWAKELSIGLENLGYDKKDIEYAITKVKVDTQQNIDISEIIGCAIKEISLRHEN | 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 ... |
Q87QU8 | MIGRLRGILLEKQPPEVLIEVNGIGYEVQMPMSCFYELPNIGEEAIIYTHFVVREDAQLLYGFNTVKERALFREVIKANGVGPKLGLGILSGMTASQFVSCVEREDVSTLVKLPGVGKKTAERLVVEMKDRLKGWGAGDLFTPFTDAAPTDSAAASSNSAEEEAVSALLALGYKPTQASKVVSQIAKPDMSSEQLIREALKSMV | 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 ... |
Q9PMT7 | MDRIVEIEKYSFDETYETSLRPSNFDGYIGQESIKKNLNVFIAAAKKRNECLDHILFSGPAGLGKTTLANIISYEMSANIKTTAAPMIEKSGDLAAILTNLSEGDILFIDEIHRLSPAIEEVLYPAMEDYRLDIIIGSGPAAQTIKIDLPKFTLIGATTRAGMLSNPLRDRFGMQFRLEFYKDSELALILQKAALKLNKTCEEKAALEIAKRSRSTPRIALRLLKRVRDFADVNDEEIITEKRANEALNSLGVNELGFDAMDLRYLELLTAAKQKPIGLASIAAALSEDENTIEDVIEPYLLANGYIERTAKGRIASAKS... | 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 ... |
Q9A3G8 | MTRVISGEPQHGDLAPADRALRPQTLAEFVGQEQAKGNLRVFIEAAKGRGEALDHVLLFGPPGLGKTTLAQIVARELGVNFRATSGPVLNKPGDLAAILTNLEANDVLFIDEIHRLSSNVEEILYPAMEDHVLDLVIGEGPSARSIRIDLAPFTLVAATTRAGMLATPLRDRFGIPIRLEFYTPAELRHVLQHAARKMGAPLTDDGADEIAKRARGTPRVAGRLLRRVRDFATADGADRIDRKAAAMALARLEVDESGLDSLDRRYLRAMIENYGGGPVGVETIAYAIAEARDAVEDVIEPYLMQQGFIQRTPRGRMACG... | 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 ... |
Q600N3 | MPENLEIRPSSFENFIGQKKLVETLQILISSSQKRKQSLDHILFYGPPGTGKTTLANIVANVLEAKIKYVQGPLLEKKSDVLAVLANISPDTIIFIDEIHGINKNIEELLYSAMEEFVIDLQIGVDGERKIMRMKLPQFTLIGASTKLAQISTPLQNRFGYVAKIVDYTLEDMIQIIRNSSAVLKLKMNTEIIKYIASFSNNTPRIANNLLKRIRDFALVLNAKRIDKDIVNKTFDSIGIYNQGLSQINIEYLNLLVKIFKGKSVALDVIANVLKEHRQTIINIIEPPLIEKELIEKTSRGRRITKKGRDYLLELKTN | 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 ... |
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