ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O24926 | MLIHICCSVDNLYFLKKAKEAFAGEKIVGFFYNPNIHPYSEYLLRLEDVKRTCEMLGIELLEGDYELEKFLDKAKGKELLGEKSERCFECFDLRLEASALKAFELGEEKFTTTLLTSPKKDPNQLIAKGQSIAQRHNLEFVVFRNDNFEHFKSELDLNLQALARENELYRQNYCGCQFALKIQKESQNRSPFELYSPLKRQILPASIEERTQVFRTLDMAKKDANKPFLAQKTIATYRLLNGGVWLSKNSNPLNCCILARSKSKAKVRINDLRWVFSQRLSVLVGYSQRDETLFLTLEGLNTLMAKNYDNLKELNLNPLN... | Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 42665
Sequence Length: 368
... |
Q0I1Q0 | MHRTKLEQKQPHFDAQKRRKKECKNSNTPFVRPKLELPHGHNKLLLHSCCAPCSGEVMEAIHASGIDFTIYFYNPNIHPLKEYLIRKEENIRFAEKWGIPFIDADYDRQNWFDRAKGMEDEPERGIRCTMCFDMRFEKAAQYAHENGFPVFTSCLGISRWKDMNQINGCGHRAAEKYDDVVYWDYNWRKGGGSQRMIEISKRERFYQQEYCGCVYSLRDTNKWREANGRQKIEIGKLYYSADK | Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 28874
Sequence Length: 243
... |
A0A0H2VKG8 | MIEANQILAKMKNQKINYDKVLRKIISQWERDGERPKILLHSCCAPCSTYTLEFLTQYADIAIYFANPNIHPKSEYLRRAKVQEQFVNDFNNKTGASVKYIEAEYEPHKFMKMAKDKGLTEEPEGGLRCTACFEMRLEIVAKAALEHGYDYFGSAITLSPKKNAQLINELGMDVQNIYNVKYLPSDFKKNKGYERSIEMCNDYNIFRQCYCGCVFAAMKQGIDFKQINKDAQAFLQQF | Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 27578
Sequence Length: 238
... |
Q9WZJ0 | MGTVLIHVCCAPDLLTTIFHVRDAEFFFYNPNIQPLSEYEKRREAVDKVANHFSLNVRYGEYSTEEIRKWYTAVKDYKDLGEGSKRCERCISFLLERTAQEARKRGHESFSTTLLASPRKNLPMIENIGKTIEEKYGVKFFFKNFRKGGAYQEGVRLSKELGIYRQNYCGCVFSLLERREKHAEISRKRGHM | Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Mass (Da): 22509
Sequence Length: 192
... |
A2RM05 | MKKSKTYDIVTIAIVAALYVILTMTPGLSAISYGPIQFRVSEMLNFTAFFNKKYIIAVTIGCMISNFLSFTWVDVIVGGLSTLVFLSLGVLLFDRFKEDYFWNGQLNKAFFFFAIFFSISMFTIALELKFVAETPFLLTWGTLALGEFASLFIGAFIMDKLGKRVDLSR | Function: Probably a queuosine precursor-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, n... |
Q59086 | MSDPQEKSHIILKVWCFILGLALLITGAFYVIGGGKLISLGGSWYFLIAGLMITTSAFFMFKKKATGVWLYALAFIGTVIWALIDAGFEFWPLHSRLMFPAGLFAAVMLTLPSIRKYQYQTPMSAPAYVIGGLTVLGMLGGLYGMFIPHETVKASGEELPLVPVDPAKKQVNWDHYGNDAGGSRFVALDQINRNNVSKLKEAWRFRTGDFTTGTGNGAEDQMTPLQVGNKVFLCTPHNNIFAIDADSGKQLWKAEVNSTADAWERCRGVAYFDSTQPLVQPTLAGATPVAALAANTECPRRVYTNTVDGRLIAVNADTGA... | Function: Can act either on quinate or on shikimate.
Catalytic Activity: a quinone + L-quinate = 3-dehydroquinate + a quinol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88196
Sequence Length: 809
Pathway: Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3-dehydroquinate from D-qu... |
Q43922 | MKLTSLRVSLLALGLVTSGFAAAETYTVDRYQDDSEKGSLRWAIEQSNANSAQENQILIQAVGKAPYVIKVDKPLPPIKSSVKIIGTEWDKTGEFIAIDGSNYIKGEGEKACPGANPGQYGTNVRTMTLPGLVLQDVNGVTLKGLDVHRFCIGVLVNRSSNNLIQHNRISNNYGGAGVMITGDDGKGNPTSTTTNNNKVLDNVFIDNGDGLELTRGAAFNLIANNLFTSTKANPEPSQGIEILWGNDNAVVGNKFENYSDGLQINWGKRNYIAYNELTNNSLGFNLTGDGNIFDSNKVHGNRIGIAIRSEKDANARITLT... | Function: Converts dehydroshikimate to protocatechuate.
Catalytic Activity: 3-dehydroshikimate = 3,4-dihydroxybenzoate + H2O
Sequence Mass (Da): 52221
Sequence Length: 486
Pathway: Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 2/2.
EC: 4.2.1.118
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Q9I4U2 | MASPAFMRFLPRCGAAAAFGTLLGLAGCQSWLDDRYADSLPPTSGVQPIKGLAQNVSIRRNALGMPLIETGTFHDALFALGYVHASDRLSQMVSLRLLAQGRLAEMVGPGALEIDRFMRTVNLRQAAEIQYRNASPRLQRFFEVYARGVNAYLYRYRDKLPMDLAQSGYRPEYWKPEDSALVFALLNFGLAVNLQEEIASLTLAQKVGSDKLAWLTPTYPDENLPFDEAEKLKGLRLDGQVPGLAGVEGAARQVAALSMLGVAASNNWAIAPQRSRSGKSLMANDTHLPLSMPSVWNYVQIRSPKYQAAGVSIAGLPGVV... | Function: Catalyzes the deacylation of acyl-homoserine lactone (AHL or acyl-HSL), releasing homoserine lactone (HSL) and the corresponding fatty acid. Possesses a specificity for the degradation of long-chain acyl-HSLs (side chains of seven or more carbons in length). Appears to be the acyl-HSL acylase that underlies t... |
Q43923 | MRHFFKLGLVSAAVLGSQMTLANDFWSQDRQWLLGDWGGERQQLEKQGYKFTASIMSQAATNLDGGYNDSNTLENAGQLTLGANFDLSKIAGWEDTTAAIMITKRDGNSLTLERIKDPRSTTLGNTQEIYGRGKIWRLTQAWVKKGFNDNTVQFKIGRMGMSDDFNSSQCEFQNLLLCGGQLGKSIGSIWYNWPVGLWGTNVKYQFAPEWTLGLGVYEVNPDNVKTQSNSDGFNLDMNNVKGATIPVELAWKPKLAMFNGLPGEYKVGALYSTADANDVGTVSKVHDSKHSFWINTQQQLTQHNDNAKRGLFVSFNGVVN... | Function: Could be involved in the transport of quinate or shikimate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49309
Sequence Length: 439
Subcellular Location: Cell outer membrane
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P19892 | MSSDDEGREEYLFKIVVIGDSAVGKSNLLSRYARNEFSANSKATIGVEFQTQSMEIEGKEVKAQIWDTAGQERFRAVTSAYYRGAVGALVVYDITRRTTFESVGRWLDELKIHSDTTVARMLVGNKCDLENIRAVSVEEGKALAEEEGLFFVETSALDSTNVKTAFEMVILDIYNNVSRKQLNSDTYKDELTVNRVSLVKDDNSASKQSSGFSCCSST | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24210
Sequence Length: 218
Subcellular Location: Cell membrane
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Q0WQN4 | MAEESYDEECDYLFKAVLIGDSAVGKSNLLSRFSRDEFRLDSKPTIGVDFAYRNVRVGDKTIKAQIWDTAGQERFRAITSSYYRGALGALLIYDITRRITFKNIEKWLSELRGFSSPETVVVLVGNKSDLGQSREVEEEEGKTLAESEGLYFLETSALENQNVEEAFLSMIGRIHEVLTQKIVLDNRLNGDGNNESNGAVVPPGKEIVNIHEVTATRPLSTSLSNCCYK | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25617
Sequence Length: 229
Subcellular Location: Cell membrane
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P24409 | MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIGIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYRGAMGIMLVYDITNGKSFENISKWLRNIDEHANEDVERMLLGNKCDMDDKRVVPKGKGEQIAREHGIRFFETSAKVNINIEKAFLTLAEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (By similarity). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream e... |
Q5ZIT5 | MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIGIDLKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYRGAMGIMLVYDITNAKSFENISKWLRNIDEHANEDVERMLLGNKCDMEDKRVVPKAKGEQIAREHGIRFFETSAKANINIEKAFLTLAEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
P61026 | MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIGIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYRGAMGIMLVYDITNGKSFENISKWLRNIDEHANEDVERMLLGNKCDMDDKRVVPKGKGEQIAREHGIRFFETSAKANINIEKAFLTLAEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes . Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors direct... |
P35281 | MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIEIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYRGAMGIMLVYDITNGKSFENISKWLRNIDQHANEDVERMLLRNKCDMDHKRVVPKGKGEQIAREHRIRFFETSAKANINIEKAFLTLPEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (By similarity). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream e... |
P51152 | RPADFKLQVIIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYDITKKETFDDLPKWMKMIDKYASEDAELLLVGNKLDCETDREITRQQGEKFAHEITGMRFCEASAKDNFNVDEIFLKLVDDILKKMPLDILRNELSNSILSLQPEPEIPPELPPPRPHVRCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
Q6IQ22 | MDPGAALQRRAGGGGGLGAGSPALSGGQGRRRKQPPRPADFKLQVIIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYDITKKETFDDLPKWMKMIDKYASEDAELLLVGNKLDCETDREITRQQGEKFAQQITGMRFCEASAKDNFNVDEIFLKLVDDILKKMPLDILRNELSNSILSLQPEPEIPPELPPPRPHVRCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
P35283 | MDPSAALHRRPAGGSLGAVSPALSGGQARRRKQPPRPADFKLQVIIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYDITKKETFDDLPKWMKMIDKYASEDAELLLVGNKLDCETDREISRQQGEKFAQQITGMRFCEASAKDNFNVDEIFLKLVDDILKKMPLDVLRNELSNSILSLQPEPEIPPELPPPRPHVRCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
F1PTE3 | MAKAYDHLFKLLLIGDSGVGKTCLIIRFAEDSFNNTYISTIGIDFKIRTVDVEGKKIKLQVWDTAGQERFKTITTAYYRGAMGIILVYDITDEKSFENIQNWMKSIKENASAGVERLLLGNKCDMEAKRKVQKEQAIKLAREHGIRFFETSAKSSTNVDEAFSSLARDILLKSGGRRSGNSHKAPGTDLKPCDKKNTSKCSLG | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors direct... |
O23561 | MSYAYRFKYIIIGDTGVGKSCLLLKFTDKRFQAVHDLTIGVEFGAKTITIDNKPIKLQIWDTAGQESFRSVTRSYYRGRAGTLLVYDITRRETFNHLASWLEEARQHASENMTTMLIGNKCDLEDKRTVSTEEGEQFAREHGLIFMEASAKTAHNVEEAFVETAATIYKRIQDGVVDEANEPGITPGPFGGKDASSSQQRRGCCG | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22945
Sequence Length: 205
Subcellular Location: Cell membrane
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P62820 | MSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGATAGGAEKSNVKIQSTPVKQSGGGCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes . Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors direc... |
Q52NJ2 | MSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQGSFNNVKQWLQEIDRYASENVNKLLVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGATAGGAEKSNVKIQSTPVKQSGGGCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors direct... |
P32960 | MIGILAGMGPKSTSPFIDKVIDYCQKLYGASNDIDYPHMMIYSCPTPFYADRPIDHDEMKKAIIDGAVKLEKTGVDFIALPCNTAHVYYEEIQQALSVPMLHIVEETIKEIPHPAKKAVVLGTEPTIQSAIYQKVLKGNGQEVIHKDHWQQAVNQLIAAIKQPNHMQHTQALWQTLYEEISQHADIIISACTDLNAVLDHIQSEIPIIDSSACLAKSTVSTYLAYQS | Function: Amino-acid racemase able to utilize a broad range of substrates. Preferentially catalyzes the epimerization of LL-diaminopimelate, as well as the racemization of D-lysine, L-arginine, L-ornithine, L-lysine and D-arginine. Has lower activity against D-ornithine, L-histidine, L-alanine, L-tyrosine, L-phenylalan... |
P26659 | MKFYIDDLPILFPYPRIYPEQYQYMCDLKHSLDAGGIALLEMPSGTGKTISLLSLIVSYQQHYPEHRKLIYCSRTMSEIDKALAELKRLMAYRTSQLGYEEPFLGLGLTSRKNLCLHPSVRREKNGNVVDARCRSLTAGFVREQRLAGMDVPTCEFHDNLEDLEPHSLISNGVWTLDDITEYGEKTTRCPYFTVRRMLPFCNVIIYSYHYLLDPKIAERVSRELSKDCIVVFDEAHNIDNVCIESLSIDLTESSLRKASKSILSLEQKVNEVKQSDSKKLQDEYQKLVRGLQDANAANDEDQFMANPVLPEDVLKEAVPG... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription... |
P36617 | METKVHLPLAYQQQVFNELIEEDGLCVIAPGLSLLQIAANVLSYFAVPGSLLLLVGANVDDIELIQHEMESHLEKKLITVNTETMSVDKREKSYLEGGIFAITSRILVMDLLTKIIPTEKITGIVLLHADRVVSTGTVAFIMRLYRETNKTGFIKAFSDDPEQFLMGINALSHCLRCLFLRHVFIYPRFHVVVAESLEKSPANVVELNVNLSDSQKTIQSCLLTCIESTMRELRRLNSAYLDMEDWNIESALHRSFDVIVRRQLDSVWHRVSPKTKQLVGDLSTLKFLLSALVCYDCVSFLKLLDTLVLSVNVSSYPSNA... | Function: Endonuclease that specifically degrades single-stranded DNA and which is involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Required for double strand break-induced interchromosomal gene conversion.
Sequence Mass (Da): 100264
Sequence Length: 877
Subce... |
P31244 | MQEGGFIRRRRTRSTKKSVNYNELSDDDTAVKNSKTLQLKGNSENVNDSQDEEYRDDATLVKSPDDDDKDFIIDLTGSDKERTATDENTHAIKNDNDEIIEIKEERDVSDDDEPLTKKRKTTARKKKKKTSTKKKSPKVTPYERNTLRLYEHHPELRNVFTDLKNAPPYVPQRSKQPDGMTIKLLPFQLEGLHWLISQEESIYAGGVLADEMGMGKTIQTIALLMNDLTKSPSLVVAPTVALMQWKNEIEQHTKGQLKIYIYHGASRTTDIKDLQGYDVVLTTYAVLESVFRKQNYGFRRKNGLFKQPSVLHNIDFYRVI... | Function: Component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. Involved in differential repair of DNA after UV damage. Will repair preferentially the MAT-alpha locus compared with the HML-alpha locus.
Sequ... |
Q6TEN1 | MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNSCAFLESSAKSKINVNEIFYDLVRQINRKTPVTGKPRKKSTCQLL | Function: Probable GTP-binding protein that possesses GTPase activity. May play a role in endothelial cell polarity and endothelial barrier function (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 20828
Sequence Length: 184
Subcellular Location: Cell membrane
EC: 3.6.5.2
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P61224 | MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL | Function: GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Play... |
Q62636 | MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWSNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL | Function: GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Play... |
Q18246 | MREYKIVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVYSITAQSTFNDLMDLRDQILRVKDTDEVPMILVGNKCDLEDERVVGKDQGQNLARQFGSAFLETSAKAKINVSEVFYDLVRQINRRYPESGRRQGQSNKQCCSCVIM | Function: Required in the hypodermis for proper formation of the cuticle.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 21248
Sequence Length: 188
EC: 3.6.5.2
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Q59XU5 | MLREYKLVVVGGGGVGKSALTIQLIQSHFVDEYDPTIEDSYRKQCTIDDQQVLLDVLDTAGQEEYSAMREQYMRTGEGFLLVYSINSLNSFQELNSFYDQILRVKDSDNVPVLVVGNKCDLEMERQVSYEDGLALANSFNCPFLETSAKQRINVEEAFYGLVRNINQYNAKIAEAEKQQQQQQQQQNANQQGQDQYGQQKDNQQSQFNNQINNNNNTSAVNGGVSSDGIIDQNGNGGVSSGQANLPNQSQSQSQRQQQQQQQEPQQQSENQFSGQKQSSSKSKNGCCVIV | Function: Required for the regulation of both a MAP kinase signaling pathway and a cAMP signaling pathway. The activation of these pathways contributes to the pathogenicity of the cells through the induction of the morphological transition from the yeast to the polarized filamentous form (By similarity).
Location Topol... |
P08646 | MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLASWNVNNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRRGRKMNKPNRRFKCKML | Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (By similarity). Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells . During larval development, mediates Ptth/tor signaling leading to the production of ... |
G4N1S3 | MTGRLQLHKLVVLGDGGVGKTALTIQLCLQHFVETYDPTIEDSYRKQVVIDNQACMLEVLDTAGQEEYTALRDQWIRDGEGFVLVYSISSRSSFSRIKRFHHQIQRVKESCASSPSYPGSPIATVTTQAPVPIMLVGNKSDRVTEREVSTQEGHALARELGCEFVEASAKNCINVEKAFYDVVRILRRQRQQASRPSLPGNSRTKTGGMGKSESFYQSDGKRGSRKDGEKHRSKPIKCVIL | Function: Modulates the activity of the adenylate cyclase catalytic subunit and therefore affects the biosynthesis of cyclic-AMP (By similarity). Plays a role in both surface attachment and surface recognition of appressoria, a highly specialized infection structure for plant penetration. Regulates appressorium formati... |
P22126 | MANKFTREYKLVVVGGGGVGKSCLTIQLIQGHFLDEYDPTIEDSYRKQCTIDNEVALLDILDTAGQEEYSAMREQYMRTGEGFLLVFAINSRESFEEIRIYQQQILRVKDRDSFPMIIVGNKYDLRGERVVSEQEGQALAAEFGTKYIETSAKTQHNVENAFYDLVREIRKEDKKLGEKVGGTSFANNNGAVKQMDVGDEDVQAGCCAKCIMM | Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 24026
Sequence Length: 213
Subcellular Location: Cell membrane
EC: 3.6.5.2
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Q6DB93 | MRQTAALAERISRLSHALEHGLYERQHTIRLCLLAALSGESVFLLGPPGIAKSMIARRLKFAFRHANAFEYLMTRFSTPEEVFGPLSIQALKDEGRYQRLTAGYLPEAEIVFLDEIWKAGPAILNTLLTAINERRFRNGNSEDTIPMRLLVAASNELPEADGGLEALYDRMLIRLWLDRVQEKQNFHALLVNNSSDRDNPVPPALSVSDEEYQQWQKDIEHVALPEVGFELIYMLRQQLDALEQAPYISDRRWKKALRLLQASAFFCGRDAITPVDIILLKDCLWHDQSTLTLIERQLELLITEHAYQQKSLLFRLQQVN... | Function: Functions as an ATPase. May play a role in metal insertion (metal-chelatase) or as a chaperone.
Sequence Mass (Da): 57514
Sequence Length: 499
Subcellular Location: Cytoplasm
EC: 3.6.3.-
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P37624 | MTHLELVPVPPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRIAWMPQGLGKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQSATLEEAFINLLPQAQRQAHQAVVIPPYQPENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMK... | Function: Exhibits an intrinsic ATPase activity that is stimulated by both 70S ribosomes and 30S ribosomal subunits. Could be involved in protein-chain elongation and in release of deacyl-tRNA from ribosomes after peptide bond synthesis. Stimulates the synthesis of polyphenylalanine in vitro.
Location Topology: Multi-p... |
Q9LIS2 | MAFCNKLSGILRQGVSQSSNGPVTSMLGSLRYMSSKLFVGGLSWGTDDSSLKQAFTSFGEVTEATVIADRETGRSRGFGFVSFSCEDSANNAIKEMDGKELNGRQIRVNLATERSSAPRSSFGGGGGYGGGGGGGY | Function: Possibly has a role in RNA transcription or processing during stress . Binds sequence non-specifically to RNAs and DNAs . Mediates cell-to-cell trafficking of RNA interference (RNAi) signals (small RNAs (sRNA), e.g. small interfering RNA (siRNA) and microRNA (miRNA)) which regulate growth and development, as ... |
Q03250 | MASGDVEYRCFVGGLAWATDDRALETAFAQYGDVIDSKIINDRETGRSRGFGFVTFKDEKAMKDAIEGMNGQDLDGRSITVNEAQSRGSGGGGGHRGGGGGGYRSGGGGGYSGGGGSYGGGGGRREGGGGYSGGGGGYSSRGGGGGSYGGGRREGGGGYGGGEGGGYGGSGGGGGW | Function: Plays a role in RNA transcription or processing during stress. Binds RNAs and DNAs sequence with a preference to single-stranded nucleic acids. Displays strong affinity to poly(U) and poly(G) sequence. Involved in mRNA alternative splicing of numerous targets by modulating splice site selection. Negatively re... |
Q03251 | MSEVEYRCFVGGLAWATNDEDLQRTFSQFGDVIDSKIINDRESGRSRGFGFVTFKDEKAMRDAIEEMNGKELDGRVITVNEAQSRGSGGGGGGRGGSGGGYRSGGGGGYSGGGGGGYSGGGGGGYERRSGGYGSGGGGGGRGYGGGGRREGGGYGGGDGGSYGGGGGGW | Function: Plays a role in RNA transcription or processing during stress. Binds RNAs and DNAs sequence with a preference to single-stranded nucleic acids. Involved in mRNA alternative splicing of numerous targets by modulating splice site selection. Negatively regulates the circadian oscillations of its own transcript a... |
P30828 | PVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in... |
P31193 | MSPKTETKASVGFKAGVKEYKLTYYTPEYETKDTDTLAALRVTPQPGVPPEEAG | Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By s... |
A0T0N6 | MSQSVSERTRIKSDRYESGVIPYAKMGYWDAAYTVKDTDVLALFRITPQPGVDPVEAAAAVAGESSTATWTVVWTDLLTACERYRAKAYRVDPVPSATDQYFAFIAYECDLFEEASLSNLTASIIGNVFGFKAISALRLEDMRIPHSYLKTFQGPATGIVVERERLNKYGTPLLGATVKPKLGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRERFLNCLEGINRASAATGEVKGSYLNITAATMEEVYKRAEYAKMIGSVIVMIDLVMGYTAIQSIAYWARENDMLLHLHRAGNSTYARQKNHGINFRVICKW... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in... |
O93627 | MVEKFDTIYDYYVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESSTGTWTTLYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAYPFHAFEEANLPGLLASIAGNIFGMKRVKGLRLEDLYFPEKLIREFDGPAFGIEGVRKMLEIKDRPIYGVVPKPKVGYSPEEFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERAEIMAKIIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKHAMVDVVITGWGALRYIRDLAADYGLAIHGHRAMHAAFTRNPYHGISMFVLAKLYRLIGIDQLHVGTAGA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA) . Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase .
Catalytic Activity:... |
Q8DIS5 | MAYTQSKSQKVGYQAGVKDYRLTYYTPDYTPKDTDILAAFRVTPQPGVPFEEAAAAVAAESSTGTWTTVWTDLLTDLDRYKGCCYDIEPLPGEDNQFIAYIAYPLDLFEEGSVTNMLTSIVGNVFGFKALKALRLEDLRIPVAYLKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFQRWRDRFLFVADAIHKAQAETGEIKGHYLNVTAPTCEEMLKRAEFAKELEMPIIMHDFLTAGFTANTTLSKWCRDNGMLLHIHRAMHAVMDRQKNHGIHFRVLAKCLRM... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in... |
Q6NZZ9 | MATSLGSNTYNRQNWEDSDFPILCQTCLGENPYIRMTKEKFGKECKICARPFTVFRWCPGVRMRFKKTEVCQTCSKMKNVCQTCLLDLEYGLPIQVRDTGLSVKDEVPRSDVNKEYYTQNMEREIANSDGTRPVGLLGKAPSSSDMLLKLARTTPYYKRNRPHICSFWVKGECKRGEECPYRHEKPTDPDDPLADQNIKDRYYGINDPVANKLLMRASTMPRLDVPDDKSITTLYIGGLGENVTDSELRNHFYQFGEIRTITIVQRQQCAFIQFATRQAAETAAEKSFNKLIINGRRLNVKWGRSQAARGKGEKDGVTES... | Function: Required for pre-mRNA splicing as component of the activated spliceosome. Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycl... |
Q9NW64 | MATSLGSNTYNRQNWEDADFPILCQTCLGENPYIRMTKEKYGKECKICARPFTVFRWCPGVRMRFKKTEVCQTCSKLKNVCQTCLLDLEYGLPIQVRDAGLSFKDDMPKSDVNKEYYTQNMEREISNSDGTRPVGMLGKATSTSDMLLKLARTTPYYKRNRPHICSFWVKGECKRGEECPYRHEKPTDPDDPLADQNIKDRYYGINDPVADKLLKRASTMPRLDPPEDKTITTLYVGGLGDTITETDLRNHFYQFGEIRTITVVQRQQCAFIQFATRQAAEVAAEKSFNKLIVNGRRLNVKWGRSQAARGKEKEKDGTTD... | Function: Required for pre-mRNA splicing as component of the activated spliceosome . Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cyc... |
Q8I4V2 | MDRYGHNVRSDIKKQGYEDSNLPILCETCLGENPYVRIIREENGKECKICKNVFTHFRWKPGENSRYKQTVICMKCAKVKNVCQTCLFDLQYNLPVQVRDKFLENSIVLPENETNRNFFLEQMENDMSSTYDKMNRINMDLSKLKRRDPYFKRNMARVCSFWRKNSCNRGDECPYLHKEIHLDKSLSNQNIKNRYTGENDILAEKILLKHNEKNNDDKNMSNKICIQGISESVSQANIKECFKKFGDIKSIKVIPKDSKMFISYSNSQAAKKASDKYKDGLLLNGCNLTVHLQDNPTYNNKNQQPVINYMNNNMYQNNMS... | Function: Involved in pre-mRNA splicing (By similarity). Binds RNA (By similarity).
Sequence Mass (Da): 41968
Sequence Length: 357
Domain: The C-terminal RRM domain and the zinc finger motif are necessary for RNA-binding.
Subcellular Location: Nucleus
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Q4V7D7 | MATSLGSNTYNRQNWEDADFPILCQTCLGENPYIRMTKEKYGKECKICARPFTVFRWCPGVRMRFKKTEVCQTCSKLKNVCQTCLLDLEYGLPIQVRDAGLSFKDDMPKSDVNKEYYTQNMEREISNSDGTRPVGMLGKATSTSDMLLKLARTTPYYKRNRPHICSFWVKGECKRGEECPYRHEKPTDPDDPLADQNIKDRYYGINDPVADKLLKRASTMPRLDPPEDKTITTLYVGGLGDTITETDLRNHFYQFGEIRTVTVVQRQQCAFIQFATRQAAEVAAEKSFNKLIVNGRRLNVKWGRSQAARGKEKEKDGTTD... | Function: Required for pre-mRNA splicing as component of the activated spliceosome. Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycl... |
Q86U06 | MASDDFDIVIEAMLEAPYKKEEDEQQRKEVKKDYPSNTTSSTSNSGNETSGSSTIGETSKKKRSRSHNKSRDRKRSRSRDRDRYRRRNSRSRSPGRQCRHRSRSWDRRHGSESRSRDHRREDRVHYRSPPLATGYRYGHSKSPHFREKSPVREPVDNLSPEERDARTVFCMQLAARIRPRDLEDFFSAVGKVRDVRIISDRNSRRSKGIAYVEFCEIQSVPLAIGLTGQRLLGVPIIVQASQAEKNRLAAMANNLQKGNGGPMRLYVGSLHFNITEDMLRGIFEPFGKIDNIVLMKDSDTGRSKGYGFITFSDSECARRA... | Function: RNA-binding protein that acts both as a transcription coactivator and pre-mRNA splicing factor . Regulates steroid hormone receptor-mediated transcription, independently of the pre-mRNA splicing factor activity .
PTM: Aryl sulfonamide anticancer drugs, such as indisulam (E7070) or E7820, promote ubiquitinatio... |
Q76LC6 | MHTTQKDTTYTKIFVGGLPYHTTDSSLRKYFEVFGEIEEAVVITDRQTGKSRGYGFVTMADRSAADRACKDPNPIIDGRKANVNLAYLGAKPRVMQPGFTFGVPQIHPAFIQRPYGIPTHYVYPQAFMQPSVVIPHIQPTATSATASSPYIDYTGAAYAQYASAATAAAAAAYEQYPYAASPAATGYVAAAGYGYAMQQPLATAAPGSAAAAAAAFGQYQPQQLQAERMQ | Function: Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation. Plays a major role in pre-mRNA alternative splicing regulation. Mediates preferentially muscle-specific exon inclusion in numerous mRNA... |
Q9BX46 | MHTTQKDTTYTKIFVGGLPYHTTDASLRKYFEVFGEIEEAVVITDRQTGKSRGYGFVTMADRAAAERACKDPNPIIDGRKANVNLAYLGAKPRIMQPGFAFGVQQLHPALIQRPFGIPAHYVYPQAFVQPGVVIPHVQPTAAAASTTPYIDYTGAAYAQYSAAAAAAAAAAAYDQYPYAASPAAAGYVTAGGYGYAVQQPITAAAPGTAAAAAAAAAAAAAFGQYQPQQLQTDRMQ | Function: Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation . Plays a major role in pre-mRNA alternative splicing regulation . Mediates preferentially muscle-specific exon inclusion in numerous mR... |
D3Z4I3 | MHTTQKDTTYTKIFVGGLPYHTTDASLRKYFEVFGDIEEAVVITDRQTGKSRGYGFVTMADRAAAERACKDPNPIIDGRKANVNLAYLGAKPRIMQPGFAFGVQQLHPALIQRPFGIPAHYVYPQAFVQPGVVIPHVQPTAAAASTTPYIDYTGAAYAQYSAAAAAAAAAAAYDQYPYAASPAAAGYVTTGGYSYAVQQPITAAAPGTAAAAAAAAAAAAAFGQYQPQQLQTDRMQ | Function: Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation . Plays a major role in pre-mRNA alternative splicing regulation . Mediates preferentially muscle-specific exon inclusion in numerous mR... |
M0R7T6 | MHTTQKDTTYTKIFVGGLPYHTTDASLRKYFEVFGDIEEAVVITDRQTGKSRGYGFVTMADRAAAERACKDPNPIIDGRKANVNLAYLGAKPRIMQPGFAFGVQQLHPALIQRPFGIPAHYVYPQAFVQPGVVIPHVQPTAAAASTTPYIDYTGAAYAQYSAAAAAAAAAAAYDQYPYAASPAATGYVTTGGYSYAVQQPITAAAPGTAAAAAAAAAAAAAFGQYQPQQLQTDRMQ | Function: Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation . Plays a major role in pre-mRNA alternative splicing regulation (By similarity). Mediates preferentially muscle-specific exon inclusion... |
Q8VY15 | MADESSSPATGDPNSQKPESTTPISIPNPNPNPSLTPPPPQQHSQPPVAPLVPPGPPYAPPAQIPSSLLPTNLPPPPPFRPGMQFTPVANFQNPSSGVPPPGSMPQYQPQPGMRPFQPMANGYPGIHGVAPPGAMPPHGLLRYPSPYPTMVRPGFIMRPPGTIGAVQLAPRPLIPGMPGLRPVMPPMVRPASLPFVTPAEKPQTTIYIGKIATVENDFMMSILEFCGHVKSCLRAEDPTTKKPKGFGFYEFESAEGILRAIRLLTQRTIDGQELLVNVNQATKEYLLKYVEKKIETAKKAKESQGTKENQAEGPESEQDK... | Function: RNA-binding protein that acts as a regulator of alternative pre-mRNA splicing . Negative regulator of responses to abscisic acid (ABA), including in early development .
PTM: Phosphorylated; the phosphorylation level is repressed by abscisic acid (ABA).
Sequence Mass (Da): 101497
Sequence Length: 899
Domain: T... |
P49756 | MSFPPHLNRPPMGIPALPPGIPPPQFPGFPPPVPPGTPMIPVPMSIMAPAPTVLVPTVSMVGKHLGARKDHPGLKAKENDENCGPTTTVFVGNISEKASDMLIRQLLAKCGLVLSWKRVQGASGKLQAFGFCEYKEPESTLRALRLLHDLQIGEKKLLVKVDAKTKAQLDEWKAKKKASNGNARPETVTNDDEEALDEETKRRDQMIKGAIEVLIREYSSELNAPSQESDSHPRKKKKEKKEDIFRRFPVAPLIPYPLITKEDINAIEMEEDKRDLISREISKFRDTHKKLEEEKGKKEKERQEIEKERRERERERERER... | Function: RNA-binding protein that acts as a regulator of alternative pre-mRNA splicing. Involved in apoptotic cell death through the regulation of the apoptotic factor BCL2L1 isoform expression. Modulates the ratio of proapoptotic BCL2L1 isoform S to antiapoptotic BCL2L1 isoform L mRNA expression. When overexpressed, ... |
Q5A6M2 | MRFAFTTVSLSLLLSSLVASDAASSDVQFLTALVGDYQDHKTDYIKFFATAKDVPGDLSTLATKVLTYTDDSYTTLLNDDSLNVSNLEAYATSLPWYSRIQADAGGKGSASGSASGSGSAKSTASAEKSSGSSASASSTAGGSSSKGGVSELVAPVGAVVGALAVALM | Function: Probable cell wall protein which may have esterase activity, with a preference for esters of fatty acids from 4 to 16 carbon atoms.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moi... |
Q6T486 | MTDDEMYEDYDVDDDSAEESGNESLDDTEYDDAATQEFDFDENQPQRSLGKLTRQKSFEVLNKDDLFSESHKIIKEVKDVLSIPSEAAVSTLLRHMKWNKEKLIERYMENPEKLCIDAGVPNVMKLNATIVEKSGNVSCLICLEDYPPTQTFALICNHRYCLPCYKNYLEIKVSEGPECIYTPCPAPKCKVIVHQDAFKQIVSPEVFERFNNFILKSYVDDNPQVKWCPAPGCIYSIRCDRKERKEAVNCKCGFQYCFNCNDYEIGDHMPCPCSQVDKWLQKASDESENVTWMLANTKKCPECRSPIEKNGGCMHMTCRK... | Function: Might act as an E3 ubiquitin-protein ligase. Appears to be required for normal cell-type proportioning and cell sorting during multicellular development. In addition to being necessary for a normal percentage of prestalk cells and the organization of the slug, rbrA is also necessary for spore cell viability.
... |
Q1ARR5 | MEPVVRLRGVSKEFPGVVAVDGVDLDILPGEVHVVAGENGAGKSTLMKLLSQVERPTSGEIYISGERVEFHGPGHARRLGVAMVYQEFALAPHLSVAENLFLGREPGRGGFVNRRAEKEEARGLLRRVGLEVDPDRLVSSLTVAEQQRVEIAKALAIDARVVIMDEPTATLAEKEIEELFEVIRDLTSHGRAVLYISHRLDEIFRIADRVTVMRDGKVVATLPVEELDEAKLVRLMVGREIGNLYPKPEAEIGEVLLRVRGLSRGERLKDCSFEVRAGEILGFAGLVGAGRTELARAVFGADPVDSGEIELEGRPLRIRK... | Function: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54368
Sequence Length: 495
Sub... |
Q81V36 | MRIEMKNISKAFNGNPVLKNAQFMIETGEVHALMGENGAGKSTLMKILTGVYKRDGGTITIDGQERTFKNAKEAEEYGIAFIHQELNILPNLTVAENMFLGKELMYGKTGILRTRQMNAIAQQQLAELGLHVKGAMLAGELSVGQQQIIEIAKALMTNASVIIMDEPTAALTDREIETLFTVINKLRKEGVSFVYISHRMEEIFSICDAITILRDGEYVGKRSIPETSFDEVVSMMVGRSIGERYPERNSQIGDVIFEMRNGTKKGKFENVSFQVRKGEILGVAGLMGAGRTDIMKAIFGYEPLDSGQIFINGQEVKIDS... | Function: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54267
Sequence Length: 494
Sub... |
Q8RD43 | MEPILQMKGISKKFGNVKVLDNVDLTLYRGRVLALLGENGAGKSTLMKILCGIYEKDEGSIYLKGKKVNIRNVRDAEKYGIAMIHQELNLVPSLSVAENIFLGREYVRTFNSIDWKKIKQESAKILHELGMDLNVDRLVKHLSVGEQQMVEIARSLLMNAEILVMDEPTAALTEGETRRLFEVIKRLRKEGKSIIYISHRMNEIFEICDDYIVLRDGCLISQGEISEVTRDDLVKMMVGRELKEHFPYECSSPGEEILRVENLTVKGMFEKVSFVVKKGEVVGFAGLIGAGRTEVAKTIFGFYKKTSGKIYLGGEEVKIN... | Function: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55826
Sequence Length: 496
Sub... |
Q3J3V9 | MSGLAIDMTGISKAFGPVKALVDADLRVARGTIHGLVGQNGAGKSTIIKVLAGILKPDSGRITINGTRVESLTPASVERLGVHFIHQERLLVPTATVAEAVFLNYELRFGPFLRPGAMKRRAEELIRTHFGLELPGDTLVRDLTTAQQKIVQITRALAQEAQVLVLDEPTAALVKREVDSLFAVLRNLRAQGIAVIFISHYMQEIEDLCDEVTVMRNGTDVGVVRPGETSIDEIVSMMIARDVGEMFPCRSHALGAPVLRVEGLSQAGHFRNVSFEVRAGEVLGITGLLGSGVKELVECLFGLEQPDAGSVTIDGEVRRF... | Function: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54306
Sequence Length: 502
Sub... |
Q7NTN6 | MQVTMRGISKAFGPVKVLENVEFTLRGGEIHALMGENGAGKSTLMKILSGVHRADAGEILLDGRKAELRSTEAAEAAGIAIIHQELNLIPQLSVMENLFLGREPSRFGIIDYAAMRREARAQLEALGAGGIDPDAEAGSLSIGQQQMVEIAKALALNARVLIMDEPTAALTEREIDRLFELMAQLRENGAAIVYVSHRMEEIFRVCDRISVLRDGCFVGEREIARTDFDEVVRMMVGREIGDRYPKREAAPGEVRLKVENLADENMIAGIGFEVRAGEVLGIAGLMGSGRSDILKTLFGAKRRTAGRVELDGKELKVAAP... | Function: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53950
Sequence Length: 502
Sub... |
Q9M2B0 | MASLNSDVIMGESSSISVPSSSSKNSKRFELKKWSAVALWAWDIVVDNCAICRNHIMDLCIECLANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDVCEWEFQKYGH | Function: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The SCF complex plays a crucial role in regulating response to auxin and is essential for growth and development. Through the RING-type zinc ... |
Q9NHX0 | MAEEIEVEETEDFHDMDFNDEEPSCSGGAVQARTERFVVKKWVAHAMWGWDVAVDNCAICRNHIMNLCIECQADPNANQDECTVAWGECNHAFHYHCIARWLKTRLVCPLDNKEWVYQKYGR | Function: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the sub... |
Q23457 | MAQASDSTAMEVEEATNQTVKKRFEVKKWSAVALWAWDIQVDNCAICRNHIMDLCIECQANQAAGLKDECTVAWGNCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH | Function: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the sub... |
Q54K33 | MADVEASSSASKTPKKKFEVKRWNAVALWIWDIVVDNCAICRNHIMDLCIECQANQASNTSEECTVAWGICNHAFHFHCISRWLKSRQVCPLDNRDWEFQKYGR | Function: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the sub... |
P62877 | MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH | Function: E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupl... |
Q8QG64 | MAAAMDVDTPSATNSGASKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH | Function: E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupl... |
O13959 | MEDEMQIDKKEVEIEQKPPRFEIKKWNAVALWQWDIVVDNCAICRNHIMDLCIECQANTDSAAAQECTVAWGTCNHAFHFHCISRWLNTRNVCPLDNREWEFQRYGH | Function: Component of E3 ubiquitin ligase SCF complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recruit the E2 ubiquitination enzyme, like UBC3/CDC34, to the complex and brings it into close proximity to the substrate. Component of the rik1-associated E3 ub... |
Q08273 | MSNEVDRMDVDEDESQNIAQSSNQSAPVETKKKRFEIKKWTAVAFWSWDIAVDNCAICRNHIMEPCIECQPKAMTDTDNECVAAWGVCNHAFHLHCINKWIKTRDACPLDNQPWQLARCGR | Function: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs), which mediate the ubiquitination of target proteins. Recruits the E2 ubiquitin-conjugating enzyme CDC34/UBC3 to the complex and brings it into close proximity to the substrate. Also stimulates CDC34/UBC3 autoubiquitinat... |
Q9UBF6 | MADVEDGEETCALASHSGSSGSKSGGDKMFSLKKWNAVAMWSWDVECDTCAICRVQVMDACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVVQRIGK | Function: Probable component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription . CRLs complexes and ARIH1 collaborate in tandem to mediate ... |
B3FWT8 | MAPSQDLGERDQQQPPAPYPADLENGRYGRIPNGHGSTTGTEGSGTLQLNEKDDATLRPNGSHDVKEEGQETSTNVVDWDGPDDPANPQNWTLSKKWLNISVVGLITFNVPLASSMFAPAVPQLLQDFHTDNASLSTFVVSVYILGLAAGPLILAPMSELYGRLNVYHVGNVLFIIFTVACGLATNINMLVAFRFLAGLVGAAPIAIGAGTIADVTNLQQRGTAMSIWSLGPLLGPSIGPVIGGFLAQAAGWRWIFWLLAIIAGAVAIISFFVLQETHAPTLLKRKTNRLRKETGNMALRSKLDTQLPPKEMFLRAIVRP... | Function: Efflux pump that might be required for efficient secretion of radicicol or other secondary metabolies produced by the radicicol gene cluster .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58675
Sequence Length: 539
Subcellular Location: Cell membrane
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Q9H7X2 | MTVGARLRSKAESSLLRRGPRGRGRTEGDEEAAAILEHLEYADEAEAAAESGTSAADERGPGTRGARRVHFALLPERYEPLEEPAPSEQPRKRYRRKLKKYGKNVGKVIIKGCRYVVIGLQGFAAAYSAPFAVATSVVSFVR | Function: Regulates drug efflux through modulation of ABCB1 localization and activity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15517
Sequence Length: 142
Subcellular Location: Membrane
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Q3ZCQ0 | MTVGARLRSKASSLVGRGPLGRLRRAGDEETDAIVEHLEGEDEDPESQDCEREEDGRRAGTPSARRVHLAALPERYDSLEEPAPGDKPKKRYRRKLKKYGKNVGKAISKGCRYIVIGLQGFAAAYSAPFGVATSVVSFVR | Function: Regulates drug efflux through modulation of ABCB1 localization and activity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15343
Sequence Length: 140
Subcellular Location: Membrane
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P90897 | MSSFGNNAGGGGREYHDDRSNRDHRHGNGGSDAGQRRREDHNSSYQSYRRPDGRQDSYGGGHQGNHGNSYGRREDDRSHSRDNHGGSRYGERDDRGNNGRSADNRYSQSNYNYDSNRGGQHYQRDNHGSKDDRGPMNQYNDHGSNHNSNSRNDQYRQGSYQGDGHSGYRRDDDRRRNDNDQARPYQSNRDSDRNSPRDHHNYNSQSSPRSHQGGQDRYSAPKEDNQRRYDNHQGGHDSYRGQNSGGYSGNNSGEYRNDYRSQQDSRDHRSGGNNSSSGFKNDGGFGGNDNRGFGNNGGGSFGNPNNSYRGNSNNIGGFHR... | Function: Probable ATP-dependent RNA helicase involved in RNAi-mediated gene silencing . Specifically required in the endogenous siRNA pathway for biogenesis of secondary endogenous small interfering RNA (siRNA) intermediates called 22G-RNAs . May associate with and recruit rde-10 to primary siRNA-targeted mRNA for sec... |
Q54RR8 | MISDYEGPTPTKKFDQDILFDYSEGEKEFTFELLDSYISSVEEHLPELLNSFEAKDLKGAVLHSHDIKGSSSYIGCEAVRYVSGKIEAYCKNDELEKAESFYPELKKEVEEVFKILSDFKKNWDKNHGEGGSDDGGDDNESEPTENNNNDGSSVNNNDSSSGGGGKDIENKNTDENTGKNLNERSKSPVPLQTTLKPVTIETPKTASDKIATETPTSLANNTNSSSNNNSKNENGLNSKQPQTSSNSPTKIQTK | Function: Phosphorelay protein that supplies phosphate to regA or accepts phosphate from regA; depending on the relative concentration of the phosphodonor proteins. In vitro, acts as a substrate for cheA (bacterial kinase). Plays a role in the development. ypd1 (yeast) can complement rdeA defect.
PTM: The phosphorelay ... |
Q8IZV5 | MNIVVEFFVVTFKVLWAFVLAAARWLVRPKEKSVAGQVCLITGAGSGLGRLFALEFARRRALLVLWDINTQSNEETAGMVRHIYRDLEAADAAALQAGNGEEEILPHCNLQVFTYTCDVGKRENVYLTAERVRKEVGEVSVLVNNAGVVSGHHLLECPDELIERTMMVNCHAHFWTTKAFLPTMLEINHGHIVTVASSLGLFSTAGVEDYCASKFGVVGFHESLSHELKAAEKDGIKTTLVCPYLVDTGMFRGCRIRKEIEPFLPPLKPDYCVKQAMKAILTDQPMICTPRLMYIVTFMKSILPFEAVVCMYRFLGADKC... | Function: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinol to all-trans-retinal. Has no detectable activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol.
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Location Topology: Single-pass membra... |
Q8VCH7 | MNIVVEFFVVTFKVLWAFVLAAARWLVRPKEKSVAGQVCLITGAGSGLGRLFALEFARRRALLVLWDINTQSNEETAGMVRHIYRDLEAADAAALQAGKGEEEILPPCNLQVFTYTCDVGKRENVYLTAERVRKEVGEVSVLVNNAGVVSGHHLLECPDELIERTMMVNCHAHFWTTKAFLPTMLEINHGHIVTVASSLGLFSTAGVEDYCASKFGVVGFHESLSHELKAAEKDGIKTTLVCPYLVDTGMFRGCRIRKEIEPFLPPLKPDYCVKQAMRAILTDQPMVCTPRLMYIVTFMKSILPFEAVVCMYRFLGADKC... | Function: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinol to all-trans-retinal. Has no detectable activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol (By similarity). Required for normal embryonic development.
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-r... |
P03430 | MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSERGRWTTNTETGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGIFETSCLETMEVVQQTRVDKLTQGRQTYDWTLNRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVMESMNKEEMEITTHFQRKRRVRDNMTKKMVTQRTIGKRKQRLNKRSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVYFVETLARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTEISFTITGDNTKWNENQNPRMFLA... | Function: RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are us... |
P22958 | MELPNQHKQTAAEGFVSFLNWLCNPWRRQRTVNAAVAFQKDLLAIEDSEHLDDINECFEESAGAQSQRTKVVADGAYAPAKSNRTRRVRKQKKHKFVKYLVNEARAEFGLPKPTEANRLMVQHFLLRVCKDWGVVTAHVHGNVALALPLVFIPTEDDLLSRALMNTHATRAAVRGMDNVQGEGWWNNRLGIGGQVGLAFRSKXGCLERRPGFSTSVSRGEHPDLVVIPSGRPEKQRQLLRYSGIGGHLLIGIHNNSLSNLRRGLMERVFYVEGPNGLQDAPKPVKGAFRTLDKFRDLYTKNSWRHTPVTSEQFLMNYTGR... | Function: RNA-dependent RNA polymerase that plays an essential role in the virus replication.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 82279
Sequence Length: 724
EC: 2.7.7.48
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P27209 | MESLPIVLLSLISKAVVLICSLLTLIIQNSTAVTWGLACVWLAYVSFRFLFQVKITVHPAARETFESMVRKFQAESMFSEEATPCIVSVGDKDADLTPDPQREDIKIVKSSRRVSYAVRVAHVAKAQVGLLANSRANELVYSRLCREEMVKHGVRPSHIAHMVPLAVAACFIPLDSDFLAASIRQGEGMRERRALLGPSWEKXGGLLVTSGFTTPTWRGDPRGMLVTKGPPLAKPRKLYRFTGMGTHIRYGVHDHSLGNVRRGLVERLYMVEVKGELQPTPKPTPGAFNQMSRFSDRLSIHLPKTTRLTPREFLGFYTGR... | Function: RNA-dependent RNA polymerase that plays an essential role in the virus replication.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 82357
Sequence Length: 725
EC: 2.7.7.48
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P89678 | MDLVIKNLIVYHLRRRIDIGTSFGIEPADYIDWVKVFLLKFIIEHTARFADFATIHTTMLLVLGEDDPNYVEKDTPIMEIDPFYLPYDDLDVDYTSLRVCGDEDQSCSDRDELSDFISNISHIPEGTSWGSESDTSFVEHLETIQDIPTKCEIADKPVEEIPFDDDGKVVNDVWVDAELSNAPEISCDADIRACGFVSLRLLESSRGYPKWTPERVSSGLNPDLPVNSKPAVDEIFPHHHSVDDRFFQEWVETHDIDLEVTSCDLDMSTFNDWTKGVDTRLVPNMSVGGLSHRVPTQREALLAIKKRNMNVPELQSNFDH... | Function: RNA-dependent RNA polymerase which replicates the viral genome composed of 3 RNA segments, RNA1, RNA2 and RNA3.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 91545
Sequence Length: 800
EC: 2.7.7.48
|
P05079 | GAHLVPTKSGDADTYNANSDRTLCALLSELPLEKAVMVTYGGDDSLIAFPRGTQFVDPCPKLATKWNFECKIFKYDVPMFCGKFLLKTSSCYEFVPDPVKVLTKLGKKSIKDVQHLAEIYISLNDSNRALGNYMVVSKLSESVSDRYLYKGDSVHALCALWKHIKSFTALCTLLPRRKG | Function: Replicase large subunit: is an RNA-dependent RNA polymerase active in viral RNA replication.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 19950
Sequence Length: 179
EC: 2.1.1.-
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Q64FP0 | MDYLITAFNRITHWFLTPTNLEYIGSYSLPPGLLRVNDVAVANHKATLDRSFDKYLYEHEINLITKEYRRSPIDEDSILEDFFSGDLPYFEIPFDEHVERGLECMAAAFRPPRPCRPAHILDVKHGYPYKWNVNAEPPFSTDEYFLSQRKTFGEFIRMHEYEHIDKEDFFRRHPNIESHDFLRTVVPPKFGFLKSMIFSWTRRWHHIIKSGFQDSTDLEQTGYFFNRFIFPMLLHTKTAIVKKNDPNKMRTIWGASKPWIIAETMFYWEYLAWIKHNPGATPMLWGYETFTGGWFRLNHELFCGLIQRSFLTLDWSRFDK... | Function: RNA-dependent RNA polymerase which replicates the viral genome.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 72865
Sequence Length: 616
EC: 2.7.7.48
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P0A5U5 | MTQTPDREKALELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNKCLAEGTRIFDPVTGTTHRIEDVVDGRKPIHVVAAAKDGTLHARPVVSWFDQGTRDVIGLRIAGGAIVWA... | Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage (By similari... |
P35901 | MAQVPDREKALELAMAQIEKNYGKGSVMRLGDEMCQPISVIPTGSIALDVALGIGGLPRGRIVEIYGPESSGKTTVALHAVANAQAVGGVAAFIDAEHALEPEYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSYVGLQARLMSQALRKMTGALSNSGTTAIFINQLREKIGVMFGCMNYSTRVTLADGSTEKIGKIVNNKMDVRVLSYDPVTDRIVPRKVVNWFNNGPAEQFLQFTVEKSGSNGKSQFAATPNHLIRTPGGWTEAGNLIAGDRVLAVEPHMLSDQQFQVV... | Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage (By similari... |
O50224 | MSTSTNFSQSGHVARPCRARNSMAGAKAGLYLQSSVSALRGVGPALVPRLQHMDLWRVQDVLFHLPSRYQDRRHIASMATLQAGQECAILGEIVRVDHQRGGREQWLVTVSDGSGRLQIRLFHMTVALRAQWQVGRRLWCFGELRGGFHGLEMIHPEWQMADVPQFQAPRHLTPFYPSSEGITQAQWRRWMAQALTLLDQLPDYLENRLPPQWPGLREGLRLLHESADEIPSPQHPAWQRLALEELLANHLAVRRMRQSGMMQNAPCLRSKGQLWHRFLAHLPFSPTMAQERVIAEINADLVRHRPMRRLLQGDVGSGKT... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA) (By similarity).
Catalytic Activity: ATP... |
O67837 | MDTAFVKDFIDNLLENDGLKLKRAIGVGIFLFNKLKEDAPDYILESLKEVDKLPFEKKKAVLREVRKFLSEYEKRKKEGNFLEKTKRKPIDVFFNPIEKVKILTKTQISTLKALGIETVYDALFYFPEKYEDKRLNTSIKTAKVGEKVALKVKVKEVKIKENERYTLEVVCTDGTGYITLKYRYKNPHFALKAFRKGMEIVVYGKLKSFKGEKYMVHPEVKSPSSEELGKIIPVYYVRKRGELQEISSKTKQKRVRTALTALSESLYRYFPEYMPDYLIEKYNFPDIALCIKELHNPKDISVNALNSFTDLYHKRVIYDE... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA) (By similarity).
Catalytic Activity: ATP... |
F4INA9 | MAAVTLSPCSMCCGSRRLRSVIVIQAQRGNWNRIRLSNFFFSKVWNISYRSKHKYSDNLLEQVEKYASARLENQSKLITKVAALMECDNVDDFIDKKSDEQVKKDLVLACKRFPSIILGDSRPVELYSNSKSYGESSSILKTPTDNSFLPTPMHGGWFDPDNLSRTLSSFCPELLQNDDSSDPREDILDDGSSFTSKTATSEVEATSDDVFAAQRFLATSIDSMPGLSKRHSNQLDSCGFHTMKKLLHHFPRTYADLQNAQVDIEDGQYLIFVGKVLSSKGVRASSSFSFLEVIVSCEVSGRDRTPEDLSHNAEDKAGKS... | Function: Critical role in recombination and DNA repair.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 108376
Sequence Length: 973
Subcellular Location: Plastid
EC: 3.6.4.12
|
O34942 | MKQHQQTSIANIKGIGPETEKTLNELGIYDISDLLNYFPYRYDDYELRDLEEVKHDERVTVEGKVHSEPSLTYYGKKRNRLTFRLLVGHYLITAVCFNRPYLKKKLSLGSVVTVSGKWDKHRQTISVQELKNGPHQEDKSIEPVYSVKENVTVKMMRRFIQQALTQYADSLPDPLPEKLRKSYKLPDYYQALKAMHQPETREALKLARRRFVYEEFLLFQLKMQAFRKAEREQTQGIRQRFSNEELMRFIKSLPFPLTNAQSRVLREITADMSSPYRMNRLLQGDVGSGKTAVAAIALYAAILSGYQGALMVPTEILAEQ... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA) (By similarity).
Catalytic Activity: ATP... |
O51528 | MFLHEFEYELKGIGGLGEKGVERLNNLQIFNVKDLIEFFPVKYEDRQNIQTFPDFSKVKSCDMMTVFTVLGHKKFGDSSKKNLKLTVKSINEEPFEILLFNRAFLENVFKIDKKFYIYSKFTYNDYSGLWSCSNFDSEVYSDKPERFKKILPVYSLTEGLTSKKISLYVKEALEYFFKFGQTDIPRFLIEKYSLLSLSDALKEIHFPSSLEMLEKAKKTLIYREIFLLQFFSRYRSSKILFREKKDLSKDLLEKVVSSLPFELTEDQKISIDEIFFDLNSSKPMNRLLQGDVGSGKTLVALLSGLPLIEAGYQVAFMAPT... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA) (By similarity).
Catalytic Activity: ATP... |
P0C5C9 | MPGLTIGDTVPNLELDSTHGKIRIHDFVGDTYVILFSHPGDFTPVCTTELAAMAGYAKEFDKRGVKLLGISCDDVQSHKDWIKDIEAYKPGNRVTYPIMADPSREAIKQLNMVDPDEKDSNGGHLPSRALHIVGPDKKVKLSFLYPACVGRNMDEVVRAVDALQTAAKHAVATPVNWKPGERVVIPPGVSDDEAKEKFPQGFDTADLPSGKGYLRFTKVG | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Seems to contribute to the inhibition of germination during stress .
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide... |
O04005 | MPGITLGDTVPNLEVETTHDKFKLHDYFANSWTVLFSHPGDFTPVCTTELGAMAKYAHEFDKRGVKLLGLSCDDVQSHKDWIKDIEAFNHGSKVNYPIIADPNKEIIPQLNMIDPIENGPSRALHIVGPDSKIKLSFLYPSTTGRNMDEVLRALDSLLMASKHNNKIATPVNWKPDQPVVISPAVSDEEAKKMFPQGFKTADLPSKKGYLRHTEVS | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Seems to contribute to the inhibition of germination during stress .
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide... |
P52572 | MPGLTIGDTVPNLELDSTHGKIRIHDYVGNGYVILFSHPGDFTPVCTTELAAMANYAKEFEKRGVKLLGISCDDVQSHKEWTKDIEAYKPGSKVTYPIMADPDRSAIKQLNMVDPDEKDAQGQLPSRTLHIVGPDKVVKLSFLYPSCTGRNMDEVVRAVDSLLTAAKHKVATPANWKPGECVVIAPGVSDEEAKKMFPQGFETADLPSKKGYLRFTKV | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Seems to contribute to the inhibition of germination during stress (By similarity).
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thiored... |
A2SZW8 | MPGLTIGDTVPNLELDSTHGKIRIHDYVGDGYAIIFSHPADFTPVCTTEMAAMAGYAKEFEKRGVKLLGISCDDVESHRQWTKDVEAYGGKQQQQQATTTKVTFPILADPARDAIRQLNMVDPDEKDAAGRSMPSRALHVVGPDKAVKLSFLYPATTGRNMDEVLRAVDSLLTAAKHGGKVATPANWKPGECAVIAPGVSDEEARKMFPQGFETADLPSKKGYLRFTKV | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Seems to contribute to the inhibition of germination during stress (By similarity).
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thiored... |
Q09820 | MSLGLQPNNDISSLVSSKNMTSENGLEHQFEELLVEKQYSEEHCAYCHIKNPNSILKCLHCNKWFCNVRGKSGASHIISHLVRARHKQVALHSHSSLSDTVLECYNCGTRNVFLLGFIPAKAKTVVVLLCRQPCARASIAKDMNWDLTQWQPIISDRQFLPWLITPPSEEEQKLAIPITSQQMVRLEELWRKDPNANLEDLDKPIEDDSLPSVELRYKDAHAYQAVLSPLIQAEADYDKRLKESQTQKDVVVRWDQAINKRYTAWFLLPKLESGEIRLAIGDEMKLTYEGELRAPWSSTGYVIKIPNNVSDEVGLELKRS... | Function: RNA-dependent helicase required for nonsense-mediated decay (NMD) of aberrant mRNAs containing premature stop codons and modulates the expression level of normal mRNAs (By similarity). Also capable of unwinding double-stranded DNA and translocating on single-stranded DNA (By similarity).
Catalytic Activity: A... |
P30771 | MVGSGSHTPYDISNSPSDVNVQPATQLNSTLVEDDDVDNQLFEEAQVTETGFRSPSASDNSCAYCGIDSAKCVIKCNSCKKWFCNTKNGTSSSHIVNHLVLSHHNVVSLHPDSDLGDTVLECYNCGRKNVFLLGFVSAKSEAVVVLLCRIPCAQTKNANWDTDQWQPLIEDRQLLSWVAEQPTEEEKLKARLITPSQISKLEAKWRSNKDATINDIDAPEEQEAIPPLLLRYQDAYEYQRSYGPLIKLEADYDKQLKESQALEHISVSWSLALNNRHLASFTLSTFESNELKVAIGDEMILWYSGMQHPDWEGRGYIVRL... | Function: RNA-dependent helicase required for nonsense-mediated decay (NMD) of aberrant mRNAs containing premature stop codons and modulates the expression level of normal mRNAs . Also capable of unwinding double-stranded DNA and translocating on single-stranded DNA .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosph... |
P12689 | MGEHGGLVDLLDSDLEYSINRETPDKNNCLSQQSVNDSHLTAKTGGLNARSFLSTLSDDSLIEYVNQLSQTNKNNSNPTAGTLRFTTKNISCDELHADLGGGEDSPIARSVIEIQESDSNGDDVKKNTVYTREAYFHEKAHGQTLQDQILKDQYKDQISSQSSKIFKNCVIYINGYTKPGRLQLHEMIVLHGGKFLHYLSSKKTVTHIVASNLPLKKRIEFANYKVVSPDWIVDSVKEARLLPWQNYSLTSKLDEQQKKLDNCKTVNSIPLPSETSLHKGSKCVGSALLPVEQQSPVNLNNLEAKRIVACDDPDFLTSYF... | Cofactor: Binds 2 magnesium ions.
Function: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for ... |
P24097 | MDQDLDRAERGERGGGSEELLQEEINEGRLTAREALQTWINNDSPRYVKKLRQGQPELPTSPGGGGGRGHRARKLPGERRPGFWKSLRELVEQNRRKQERRLSGLDRRIQQLEDLVRHMSLGSPDPSTPSASVLSVNPPAQTPLGHLPPRSYFKLKRVDCGAGWDLRTTAAPGLPICELDWIQGTK | Function: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is es... |
P33460 | MDAGARYMRLTGKENWVEVTMDGEKERKREGFTAGQQDIQNSKYPDIPTGHSHHGNKSRRRRRKSGFWRWLRGIRQQRNKRKSDSTESLEPCLGALAELTLEGAMEKGPAEAARPSADDGNLDKWMAWRTPQK | Function: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is es... |
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