ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9TXJ8 | MATFIFSRGNIFFYVNKITIPDLMSDVLLSKLSTELADLDGEIGQIDQQISQLRRKKSELTQKRQAIERKIELKTNEDSDVVTDRWDRDGFPWSDEATKILKEQFHLEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPALLANGLALVVSPLISLVEDQILQLRSLGIDSSSLNANTSKEEAKRVEDAITNKDSKFRLLYVTPEKLAKSKKMMNKLEKSLSVGFLKLIAIDEVHCCSQWGHDFRTDYSFLNVLKRQFKGVPILGLTATATSNVLDDVKDMLGIQAALTFRAGFNRSNLKYKVVQKPGSEDECTE... | Function: DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phos... |
P46063 | MASVSALTEELDSITSELHAVEIQIQELTERQQELIQKKKVLTKKIKQCLEDSDAGASNEYDSSPAAWNKEDFPWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSNTEDFIEDIVKLINGRYKGQSGIIY... | Function: DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence M... |
Q5HP94 | MNYPNGKPYSKNKPLDGRKSSPFSSNIEYGGRGMTLEKDIEQSNTFYLKSGIAVIHKKPTPVQIVNVHYPKRSKAVINEAYFRTPSTTDYNGVYNGYYIDFEAKETKNKTSFPLNNIHAHQVEHMKNTYHQKGIVFLMIRFKSLDEVYLLPYSKFEKYWQRYINNIKKSITVEEIRKNGYHIPYQYQPRLNYLKAVDKLILDESEDRV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous ... |
Q49XQ5 | MNYPNGKPFNRNKSQVGRTHKGQTSKIDYGGRGMSLEKDIELSNDYYLNRGIAVIHKKPTPIQIVNVHYPMRSKAVINEAYFRTPSTTDYNGIYHGRYLDFEAKETKNKTSFPLNNMHEHQVRHMEACYQQQGVVFLLIRFKSLDEVYLLPYANFKKFWERHIQEIKKSVTVEEIRKNGYYIPYQYQPRLNYLKTVDKLILDESEDRV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous ... |
Q9H6H4 | MVSWMICRLVVLVFGMLCPAYASYKAVKTKNIREYVRWMMYWIVFALFMAAEIVTDIFISWFPFYYEIKMAFVLWLLSPYTKGASLLYRKFVHPSLSRHEKEIDAYIVQAKERSYETVLSFGKRGLNIAASAAVQAATKSQGALAGRLRSFSMQDLRSISDAPAPAYHDPLYLEDQVSHRRPPIGYRAGGLQDSDTEDECWSDTEAVPRAPARPREKPLIRSQSLRVVKRKPPVREGTSRSLKVRTRKKTVPSDVDS | Function: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes.
Location Topology: Multi-pass membrane pr... |
Q8K072 | MVSWMICRLVVLIFGMLYPAYASYKAVKSKNIREYVRWMMYWIVFAIFMAAETFTDIFISWFPFYYEFKMAFVLWLLSPYTKGASLLYRKFVHPSLSRHEKEIDACIVQAKERSYETMLSFGKRSLNIAASAAVQAATKSQGALAGRLRSFSMQDLRSIPDTPVPTYQDPLYLEDQVPRRRPPIGYRPGGLQGSDTEDECWSDNEIVPQPPVRPREKPLGRSQSLRVVKRKPLTREGTSRSLKVRTRKKAMPSDMDS | Function: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes (By similarity).
Location Topology: Multi-... |
Q6AZM3 | MVSWIISRAVVLVFGLLYPAYASYKAVKTKNVRDYVRWMMYWIVFALFMTVETFTDIFIAWFPFYYEIKMAFVVWLLSPYTRGASLLYRKCIHPTLSLKEKEIDSYIIQAKERSYESFVNIGRKGLNIAASAAVQAATKGQGALVGRLRSFSMQDLRALPDDTPIHYTDALYPDEPQLHRRPMGFPTTSQADSDSMDERWSDSEIAETRTAARTRGGMPSKSLQRSQSLRVSKKKGLSREVSTKTTKPRAKKKPAQSEPEN | Function: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes (By similarity). May play a role in the ma... |
Q6PBX9 | MAAALKQRFDNALHEKNMVTDLLAKIEAKTGVNRSYIAYAVIAFIAIYLVIGYGASLLCNLIGFVYPAYISIKAIESPAKDDDTKWLTYWVVYGVFSVVEFFADIFLSWFPFYFLAKCAFLVWCMAPTPSNGSIMLYTRIIRPFFLKNEAKIDNVMKDLTDKAAGAADKIKDEAKKATANIMFEEKKHY | Function: Plays an essential role in heart function and development by regulating the organization and function of the sarcoplasmic reticulum in cardiomyocytes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21407
Sequence Length: 189
Domain: The short lumenal loops between transmembrane domains 1 a... |
Q00765 | MSAAMRERFDRFLHEKNCMTDLLAKLEAKTGVNRSFIALGVIGLVALYLVFGYGASLLCNLIGFGYPAYISIKAIESPNKEDDTQWLTYWVVYGVFSIAEFFSDIFLSWFPFYYMLKCGFLLWCMAPSPSNGAELLYKRIIRPFFLKHESQMDSVVKDLKDKAKETADAITKEAKKATVNLLGEEKKST | Function: Plays an essential role in heart function and development by regulating the organization and function of the sarcoplasmic reticulum in cardiomyocytes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21493
Sequence Length: 189
Domain: The short lumenal loops between transmembrane domains 1 a... |
Q60870 | MRERFDRFLHEKNCMTDLLAKLEAKTGVNRSFIALGVIGLVALYLVFGYGASLLCNLIGFGYPAYISMKAIESPNKDDDTQWLTYWVVYGVFSIAEFFSDLFLSWLPFYYMLKCGFLLWCMAPSPANGAEMLYRRIIRPIFLRHESQVDSVVKDVKDKAKETADAISKEVKKATVNLLGDVKKST | Function: Plays an essential role in heart function and development by regulating the organization and function of the sarcoplasmic reticulum in cardiomyocytes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21051
Sequence Length: 185
Domain: The short lumenal loops between transmembrane domains 1 a... |
Q66IF1 | MFAIFTKIKDRVEAFLNEKNIVTDCLNKIEEKTGIKKRYLAYGAAGVTGAFLLLGYGASLICNLIGFVYPAYFSIKAIESPGKEDDTQWLTYWVIYGFFSVGEFFSDIFLHWFPFYYVCKCLFLLWCMAPVSWNGSQVLYRHVVRPFFLKHEAAVDGMVSNISVKAMSAAENVTREVLHTLVRNRTVGPAESEPRSLPSSAHTEPTVD | Function: Required correct function and survival of retinal photoreceptors . Required for retinal development (By similarity). In rod photoreceptors, facilitates stability and/or trafficking of guanylate cyclases and is required to maintain endoplasmic reticulum and mitochondrial homeostasis (By similarity). May play a... |
Q96HR9 | MDGLRQRVEHFLEQRNLVTEVLGALEAKTGVEKRYLAAGAVTLLSLYLLFGYGASLLCNLIGFVYPAYASIKAIESPSKDDDTVWLTYWVVYALFGLAEFFSDLLLSWFPFYYVGKCAFLLFCMAPRPWNGALMLYQRVVRPLFLRHHGAVDRIMNDLSGRALDAAAGITRNVLQVLARSRAGITPVAVAGPSTPLEADLKPSQTPQPKDK | Function: Required for correct function and survival of retinal photoreceptors . Required for retinal development (By similarity). In rod photoreceptors, facilitates stability and/or trafficking of guanylate cyclases and is required to maintain endoplasmic reticulum and mitochondrial homeostasis (By similarity). May pl... |
Q7XII4 | MLSEQTAASGSSSSSRGADDREIVISTGREIVVRSSGGEEREEEVVVEEELEEPEFRDIHALSPPPTPTPSQPSSSYHRRRRESWESAAGSRHTSIRSVGSDTAPSELFPTMSREFSAMVAAAANANAAAAAAANGGDSSRAGVDDALGRIGEDELEETNPLAIVPDSNPIPSPRRAHLALPAPGDVSSAGGGHGDEVSVGQVKKEEVESKIAAWQIAEVAKVNNRFKREEVVINGWEGDQVEKANAWLKKYERKLEEKRAKAMEKAQNEVAKARRKAEEKRASAEAKRGTKVARVLELANFMRAVGRAPSKRSFF | Function: Functions in abscisic acid (ABA) signaling downstream of BZIP23. Acts as antagonistic and negative regulator of brassinosteroid (BR) signaling. Binds to BAK1 and inhibits its interaction with the BR receptor BRI1. Inhibits the formation and subsequent activation of the BRI1-BAK1 receptor complex.
PTM: Phospho... |
P11334 | MACLRPLQVHNLKKGEKVNFKHYSNGDVARYDMNKNYIVNDSVPCRKCVGCRLDNSAEWGVRASLEIKSNPKHNWFVTLTYSDEHLVYNALGRPNCVPEHITKFIKSLRKYFERRGHIGIKYLASNEYGTKRMRPHYHICFFNLPLDDLEKTIDSQKGYQQWTSKTISRFWDKGFHTIGELTYHSANYTARYTTKKLGVKDYKALQLVPEKLRMSKGIGLKYFMENKERIYKEDSVLISTDKGIKRFKVPKYFDRRMEREWQDEFYLDYIKEKREKVAKRTLFQRQIVSSRSYTDYLGDEQKKLNNIVKRLTRPLKTGKK | Function: Plays an essential role in viral DNA replication. Binds the origin of replication and cleaves the dsDNA replicative form I (RFI) and becomes covalently bound to it via phosphotyrosine bond, generating the dsDNA replicative form II (RFII). In turn, viral DNA replication initiates at the 3'-OH of the cleavage s... |
P03567 | MPSHPKRFQINAKNYFLTYPQCSLSKEESLSQLQALNTPINKKFIKICRELHEDGQPHLHVLIQFEGKYCCQNQRFFDLVSPTRSAHFHPNIQRAKSSSDVKTYIDKDGDTLVWGEFQVDGRSARGGCQTSNDAAAEALNASSKEEALQIIREKIPEKYLFQFHNLNSNLDRIFDKTPEPWLPPFHVSSFTNVPDEMRQWAENYFGKSSAARPERPISIIIEGDSRTGKTMWARSLGPHNYLSGHLDLNSRVYSNKVEYNVIDDVTPQYLKLKHWKELIGAQRDWQTNCKYGKPVQIKGGIPSIVLCNPGEGASYKVFLD... | Cofactor: Divalent metal cations, possibly Mg(2+) or Mn(2+).
Function: Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved se... |
Q67622 | MASSSAPRFRVYSKYLFLTYPECTLEPQYALDSLRTLLNKYEPLYIAAVRELHEDGSPHLHVLVQNKLRASITNPNALNLRMDTSPFSIFHPNIQAAKDCNQVRDYITKEVDSDVNTAEWGTFVAVSTPGRKDRDADMKQIIESSSSREEFLSMVCNRFPFEWSIRLKDFEYTARHLFPDPVATYTPEFPTESLICHETIESWKNEHLYSESPGRHKSIYICGPTRTGKTSWARSLGTHNYYNSLVDFTTYDVNAKYNIIDDIPFKFTPNWKCFVGAQRDFTVNPKYGKRKVIRGGIPCIILVNPDEDWLKDMTPEQSDY... | Cofactor: Divalent metal cations, possibly Mg(2+) or Mn(2+).
Function: Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved se... |
Q6NS82 | MASSGGGNTGAGGTSGLGLGLGLSLGMGEATGDAEEEAAAAEAVGRLATSLWLRLRGWEAVLAAAQRLLVWEKPLHSLVTAATLNGLFWLLSSSSLRPFFLLSISLLTYFLLDLWHPRFLPDVSAPPPEEPHSDSEGAGSGAQPHLLSVPELCRYLAESWLTFQIHLQELLQYKRQNPAQFCARGCAACAVLAVLGHYVPGVMISYIVLLSILLWPLVVYHELIQRMYTRLEPLLMQLDYSMKAEADALHHKHDKRKRQGKSAPPAGDEPLAETESESEAELAGFSPVVDVKKTALALAITDSELSDEEASILESGGFSV... | Function: Endoplasmic reticulum (ER)-anchored autophagy regulator which exists in an inactive state under basal conditions but is activated following cellular stress . When activated, induces ER fragmentation and mediates ER delivery into lysosomes through sequestration into autophagosomes via interaction with ATG8 fam... |
Q86VR2 | MAEAEGVPTTPGPASGSTFRGRRDVSGSWERDQQVEAAQRALVEVLGPYEPLLSRVQAALVWERPARSALWCLGLNAAFWFFALTSLRLVFLLAFGLMIIVCIDQWKNKIWPEIKVPRPDALDNESWGFVHPRLLSVPELCHHVAEVWVSGTIFIRNVLLFKKQNPGKFCLLSCGILTFLAVLGRYVPGLLLSYLMLVTVMMWPLAVYHRLWDRAYVRLKPALQRLDFSVRGYMMSKQRERQLRRRALHPERAMDNHSDSEEELAAFCPQLDDSTVARELAITDSEHSDAEVSCTDNGTFNLSRGQTPLTEGSEDLDGHS... | Function: Endoplasmic reticulum (ER)-anchored autophagy regulator which exists in an inactive state under basal conditions but is activated following cellular stress . When activated, induces ER fragmentation and mediates ER delivery into lysosomes through sequestration into autophagosomes via interaction with ATG8 fam... |
Q0P4Z1 | MAQRVGEEEQGASGLRRRRSGARCVEARERDEQVREVQEMLQRGLSSYEPVLSYVQAVLVWERPRHSALLHLALNAAFWFFALTSLRIIFLVAFGLMIIICADQWKNKLWPELGAARASELENESWGYVHPRLLSVPELCYHAADTWVSVYNFLRNLLLFKTENPGKFCLLACSFLTFLAVLGGYIPGVVLSYLLLLFLLLWPLAIYHQLGRRIYQKLEPALQRLDFSVRGYMMSKYKERQKHNRALPPTDASDSEEELAAFCPSLDDSAVAKELTISDSEHSDAEVSFTENGTFNLSRGQTPLTEGSEDLDRHSDPEES... | Function: Endoplasmic reticulum (ER)-anchored autophagy regulator which exists in an inactive state under basal conditions but is activated following cellular stress. When activated, induces ER fragmentation and mediates ER delivery into lysosomes through sequestration into autophagosomes via interaction with ATG8 fami... |
Q5BLE8 | MWFAVVAIFLALVAFLYRYVVGSGPNPFAIDTREPLKPMVFDRKLKNKVLKQGFLASRVPEDLDAVVVGSGIGGLAIAVLLAKVGKKVLVLEQHDRAGGCCHTFKEQGFEFDVGIHYIGELSNHKPLRCIIDQMTNGQLQWDPLENPFDNVVIGPPENRRIYQIYSGRKRYMDELKKCFPGEEKAIDEYVRLCKEVGQGVWVMVLLKFLPTPIANFLVRTGLANRLTSFSRYASRSLTDVVNELTQNKDLRAVLSYIFGTYGKIPKEASFSMHSLIVNHYMNGAWYPKGGATEIAYHMIPIIEKAGGAVLVRAPVNRILL... | Function: Catalyzes the saturation of all-trans-retinol to all-trans-13,14-dihydroretinol. In addition, saturates the 7-8 double bond of all-trans-retinol to produce all-trans-7,8-dihydroretinol. Can also use vitamin A2 (all-trans-3,4-didehydroretinol) as a substrate, to produce all-trans-13,14-dihydro-3,4-didehydroret... |
Q64FW2 | MWITALLLAVLLLVILHRVYVGLYAASSPNPFAEDVKRPPEPLVTDKEARKKVLKQAFSVSRVPEKLDAVVIGSGIGGLASAAVLAKAGKRVLVLEQHTKAGGCCHTFGENGLEFDTGIHYIGRMREGNIGRFILDQITEGQLDWAPMASPFDLMILEGPNGRKEFPMYSGRKEYIQGLKKKFPKEEAVIDKYMELVKVVARGVSHAVLLKFLPLPLTQLLSKFGLLTRFSPFCRASTQSLAEVLQQLGASRELQAVLSYIFPTYGVTPSHTAFSLHALLVDHYIQGAYYPRGGSSEIAFHTIPLIQRAGGAVLTRATVQ... | Function: Catalyzes the saturation of all-trans-retinol to all-trans-13,14-dihydroretinol . Does not exhibit any activity toward all-trans-retinoic acid, nor 9-cis, 11-cis or 13-cis-retinol isomers . May play a role in the metabolism of vitamin A . Independently of retinol conversion, may regulate liver metabolism upst... |
Q9W0P2 | MTRDEDNGFSEWGGYFEAKKSKLEEQFAAASDPFRKSDLFQGISIFVNGRTDPSADELKRIMMVHGGTFHHYERSHTTYIIASVLPDVKVRNMNLSKFISAKWVVDCLEKKKIVDYKPYLLYTNQKTSQPMLIFGKPKDNGANESKSDVEPPKDKAEVEVDSTKDETQMELGGILKNLQQAVATSPEKEASASESKITNLSTTSNNSTTARTAADPNFLSEFYKNSRLHHIATLGAGFKQYVCRLRQKHGTQGFPKRETLKSLANSHHNCLERYVMHIDMDCFFVSVGLRTRPELRGLPIAVTHSKGGNAATDVPVHPQA... | 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... |
O94623 | MAFNQRKRRRPVGIADFDEANDEAYESVGFHDYADYFSRKQRKLQNQNAALYKSIDEDSKSDLFHGLAIAINGYTKPSYTELRQMIVSNGGTFIQYVDGKTSISYLVCSFLTPSKARQWKHQKVVKPEWIVDCIKQKKILPWINYRTFQASSAQATLSFVASKPSQPEGNLEDIQTSSQEEEHDNEKDKTKESKAKGFLDDLSGLSASSLHNYQLLKNPNVRNSTTQNQDFLENFFSSSRLHHLSTWKADFKNEIQAMTTASEPVRPIMKDKSKKSRFLLHVDFDCFFASVSTRFSHELRLKPVAVAHGIKNSEIASCNY... | 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 ... |
A6Q162 | MLKEKLHPFIQRYNEINELLSSPEITQDIKKMTALSKEQSEIEPIVEKAKEYMNILEAIEENRSLIEDEELGELAKEELKELEPKKEQLEEEIKVLLISKDPNDEKDIYLEIRAGTGGEEAALFASDLFKAYARYAEKKGWRVEIVSSSESDSGGYKEIIAKIKGQGVYSRLKYEAGTHRVQRVPETESQGRIHTSAVTVAIMPEVDDVDVEINPNDLKIDVYRSSGHGGQSVNTTDSAVRITHIPTGIVVAMQDEKSQHKNKEKALKILKARIFEKRMREQQEALAKDRKEQVGSGDRSERIRTYNFPQNRVTDHRIGL... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 40360
Sequence Length: 354
Subcellular Location: Cytoplasm
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B2ITM5 | MAESYLLDKLKSVEQTFNELTRRLGDPDTASNPDEYQEIAKSRSSLEEVVNTYEIWKTAQEDLIGAREVYKESASDPELQEMASLEVKELEEKIEHLESRLKVLLLPRDPNDEKNIMLEIRAGTGGDEASIWAGDLMQMYTRYAQTQGWKVSLVSESRGEMGGWKEVILEIKGNDVYSQLKFEAGVHRVQRVPATESGGRVHTSTATVAIMPEVDDVEIHIDPKDIEMTTARSGGAGGQNVNKVETAVDLMHKPTGIRIFCTEERSQLQNKERAMQILRAKLYDIKLGEQQAAVTSMRRSQVGTGSRSEKIRTYNYKDNR... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 40969
Sequence Length: 365
Subcellular Location: Cytoplasm
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Q9K4E4 | MFEAVEELVAEHADLEKKLADPSVHSDQANARKLNKRYAELTPIVATFRSWKQTGDDMETAREFAADDPDFAAEVKELDKQRDELTEKLRLLLVPRDPSDDKDVILEIKAGAGGDESALFAGDLLRMYLRYAERIGWKTEIIDSTESELGGYKDVQVAVKTKGGQGATEPGQGVWARLKYEGGVHRVQRVPATESQGRIHTSAAGVLVTPEAEEIDVEINPNDLRIDVYRSSGPGGQSVNTTDSAVRITHIPTGVVASCQNEKSQLQNKEQAMRILRSRLLAAAQEEAEKEAADARRSQVRTVDRSEKIRTYNFPENRIS... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 39460
Sequence Length: 358
Subcellular Location: Cytoplasm
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Q2GDG2 | MDFETQVVLHNLKKSVEVIRRQLDIEKKHSRLEEIQALVDSPTLWEDQSRAQLLLKEKSQIETSLKEFKELSIQLDDLIEMIELASKDHEEETMKDLERELLLLKEKIQKKEIECLFSGEADGNDCLLEIQSGAGGTESNDWAMMLLRMYTRWAEIYHKFQVQIVDKVEGEETGIKSCTLKVMGKNAYGWARTETGVHRLVRISPFDANAKRHTSFAKIFVSPCIEGEINISIDEKDLKIDTYRASGAGGQHVNKTESAIRITHLPSKIVVQSQSSRSQHQNKAEAMQMLKSRLYEIELRKKEEKLNAARNVEDSIGWGY... | Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Sequence Mass (Da): 41764
Sequence Length: 365
Subcellular Location: Cytoplasm
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Q04GC3 | MELAQARNSISDMQEQIDGFRSTLDLDALDASIAENEDKMSQPGFWDDQQSAQKIIDETNTLKNRRDSFLSLQKSVEDLTAMAELLSEEDDADMHAELDTDIEKTEKDLEKYNLNQLLTEKYDSNNAILEIHPGEGGTESTDWASNLYRMYTRWAQAHDFKVEVTDYQTGDVAGIDSATLRIIGHNAYGFLRSEKGVHRFVRISPFDSAGRRHTSFVSIDVMPELDDDEIEIEIKPQDVKMDVYRSGGAGGQNVNKVSTAVRLTHIPTGIVVASQVERTQYGNRDIAMKMLKAKLYEQEEQKREEEHAKLSGTKLDVAWG... | Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Sequence Mass (Da): 42213
Sequence Length: 372
Subcellular Location: Cytoplasm
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Q7U3W6 | MDLTDFKRDLSELTDRLGHAQDCLDVPALKARQQDLEQLAAQPDFWDDQQAAQKQMRRLDEVKAQLQQLADWGGAVDDAKATLELYELEPDEEMLTEAQEGLNQLRQGLDRWELERLLSGDYDKEGAVLTINAGAGGTDAQDWAQMLLRMYTRWAEDHGMKVTVDELSEGEEAGIKSCTIEVEGRYAYGYLRNEKGTHRLVRISPFNANDKRQTSFAGIEVMPKIDEEVDIDIPEKDLEVTTSRSGGAGGQNVNKVETAVRILHIPTGLAVRCTQERSQLQNKEKAMALLKAKLLVIAQEQRAAEIADIRGDIVEAAWGN... | Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Sequence Mass (Da): 41776
Sequence Length: 374
Subcellular Location: Cytoplasm
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Q9ZQ19 | MFSSSQFEPNSGFSGGGFMSSQPSQAYESSSSTAKNRDFQGLVPVTVKQITECFQSSGEKSGLVINGISLTNVSLVGLVCDKDESKVTEVRFTLDDGTGRIDCKRWVSETFDAREMESVRDGTYVRLSGHLKTFQGKTQLLVFSVRPIMDFNEVTFHYIECIHFYSQNSESQRQQVGDVTQSVNTTFQGGSNTNQATLLNPVVSSQNNDGNGRKNLDDMILDYLKQPACTARQQGIHIDEIAQQLKIPKNKLEGVVQSLEGDGLIYSTIDEYHFKHVEL | Function: Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions. Required fo cell division in meristems. Involved in the maintenance of transcriptional epigenetic gene silencing... |
Q6K9U2 | MMSFSQPDAFSPSQFTSSQNAAADSTTPSKSRGASSTMPLTVKQISEAQQSGITGEKGAPFVVDGVETANVRLVGLVSGKTERNTDVSFTIDDGTGRLDFIRWVNDGADSAETAAVQNGMYVSVIGSLKGLQERKRATAFAIRPVTDYNEVTLHFIQCVRMHLENTKSQIGSPAKTYSAMGSSSSNGFSEMTTPTSVKSNPAPVLSVTNGSKTDLNTEVLNVFREPANVESEHGVHIDEIVKRFRLPEAKIKVAIDYLADIGHIYSTIDESHYKSAFNE | Function: Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions (By similarity).
PTM: Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). In respon... |
Q8LFJ8 | MYGGDFDGNAAFAGGGFMPSQATTQAHESSSSLKNRDVRTLLPLTLKQLSSASTTGESNFSIDGVDIKTVVIVGRISRMENRITQVDFVVDDGTGWVDCVRWCHARQETEEMEAVKLGMYVRLHGHLKIFQGKRSVNVFSVRPVTDFNEIVHHFTECMYVHMYNTKLRGGSITQDTATPRPQMPYSTMPTPAKPYQTGPSNQFPNQFNDSMHGVKQTVLNYLNQPMHIVSEAGVHCDIIARELRIPLLQVKEALEQLSNDGCIYSTLDETCFKSTANA | Function: Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions. Required fo cell division in meristems. Involved in the maintenance of transcriptional epigenetic gene silencing... |
Q6H7J5 | MYGVGVGGGGGGNYDGGGGNASSLFGGGGFMPSQATNAAEGTSGGGGGFPKSRNAQALLPLTVKQIMDASQTNDDKSNFAVNGMEVSTVRLVGRMLNKLDRVTDVSFTLDDGTGRVPVNRWENDSTDTKEMADIQNGDYVIVNGGLKGFQGKRQVVAYSVRRITNFNDVTHHFLHCVHVHLELTRPKSQVNANTATGTPNQTMPRDSMAYNQSPLTNQASTFSAPQNTGTGTNMIDLVLNVFHDPAVMNDDHGVGVDYVSRRLNLPEETVGKIIIDQVDLGHLYATIDDHHYKSTMNG | Function: Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions (By similarity).
PTM: Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). In respon... |
Q5Z8L1 | MAAAASYFSGTALMPSQRSGAPAPEYSAAGTGAAAAPSPSKPRDPRFSGCVPATVLHISRSFAAALAADGGGDPVFSIDGVETTNVRVLGRVVSVVSRDTDVCFTLDDSTGKIPLVRWITDQSDTRDTSYIQEGVYVKVQVNLMGFQAKKQGLARSIRPINNFNEVVLHFIECMHVHLESVQSKMQRQLPPSVQTNEYTHVPSSGGVRDYQVHFTPQVNQGLPPAVQTNTSTYVPLLGGVRDHQAHFAQVNQGQFSPAVQANTSTHLPFSGGVGEHQIHFTPKVNQGQFPPSVQTNTSAHVPYSGGFREHQVHFTPPVNQ... | Function: Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions (By similarity).
PTM: Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). In respon... |
Q23697 | MLASQAGSNFSAAASSNGGQQQQQRRQHPIRPLTIKQMLEAQSVGGGVMVVDGREVTQATVVGRVVGYENANMASGGGAITAKHFGYRITDNTGMIVVRQWIDADRAQEPIPLNTHVRASGTVNVWQQSPIVTGTVVSMADSNEMNYHMLDAILTHLRLTQGNKRAAGNIGSGASVQNSAAAVGVQNMLPGGDNKVLLTDLLVSFIKQNGHGDAGMSMDELTMAAQRYSFTPGDVRTAMRTLAAEGKVYQTHDNRFNI | Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism... |
P15927 | MWNSGFESYGSSSYGGAGGYTQSPGGFGSPAPSQAEKKSRARAQHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAGRAPISNPGMSEAGNFGGNSFMPANGLTVAQNQVLNLIKACPRPEGLNFQDLKNQLKHMSVSSIKQAVDFLSNEGHIYSTVDDDHFKSTDAE | Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism... |
Q62193 | MWNSGFESFTSSTYGGRGGYTQSPGGFGSPTPSQAEKKSRVRAQHIVPCTISQLLSATLTDEVFRIGDVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAPPMDVRQWVDTDDASGENAVVPPETYVKVAGHLRSFQNKKSLVAFKIIPLEDMNEFTAHILEVVNSHMMLSKPNSQASAGRPSMSNPGMSESFNFSGNNFMPANRLTVVQNQVLNLIKACPRPEGLNFQDLRSQLQHMPVPSIKQAVDFLCNEGHIYSTVDDDHFKSTDAE | Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism... |
Q92373 | MAYDAFGKPGYGPDFNSAFSPGMGGGAGFNEYDQSSQPSVDRQQGAGNKLRPVTIKQILNASQVHADAEFKIDGVEVGQVTFVGVLRNIHAQTTNTTYQIEDGTGMIEVRHWEHIDALSELATDTYVRVYGNIKIFSGKIYIASQYIRTIKDHNEVHFHFLEAIAVHLHFTQKANAVNGANAPGYGTSNALGYNNISSNGAANSLEQKLAEYSLTPAQMTVMQAIHSAPETNEGVHVRQLAQSVGPGIDLTAVTDFLQQEGIIYTTIDENHFKSVLQDQ | Function: Binds to single-stranded sequences.
PTM: Phosphorylated in a cell cycle-dependent manner. Hypophosphorylated in G1, becomes phosphorylated at the G1/S boundary, it is maintained in this state through the M phase.
Sequence Mass (Da): 30391
Sequence Length: 279
Subcellular Location: Nucleus
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P26754 | MATYQPYNEYSSVTGGGFENSESRPGSGESETNTRVNTLTPVTIKQILESKQDIQDGPFVSHNQELHHVCFVGVVRNITDHTANIFLTIEDGTGQIEVRKWSEDANDLAAGNDDSSGKGYGSQVAQQFEIGGYVKVFGALKEFGGKKNIQYAVIKPIDSFNEVLTHHLEVIKCHSIASGMMKQPLESASNNNGQSLFVKDDNDTSSGSSPLQRILEFCKKQCEGKDANSFAVPIPLISQSLNLDETTVRNCCTTLTDQGFIYPTFDDNNFFAL | Function: Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the... |
P35244 | MVDMMDLPRSRINAGMLAQFIDKPVCFVGRLEKIHPTGKMFILSDGEGKNGTIELMEPLDEEISGIVEVVGRVTAKATILCTSYVQFKEDSHPFDLGLYNEAVKIIHDFPQFYPLGIVQHD | Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism.... |
Q9CQ71 | MEDIMQLPKARVNASMLPQYIDRPVCFVGKLEKIHPTGKMFILSDGEGKNGTIELMEPLDEEISGIVEVVGKVTAKATVLCASYTLFKEDTNRFDLELYNEAVKIINELPQFFPVGLPQHE | Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism... |
A4IIE8 | MERGSCSAPGDPGHLGLFLQRLRQVFDACDGDADGFIKVEHFVALGLQFAQGDEVKKLAKRLDPNAQGRIGFKDFCHGVLAMKGCDKFVKGILGVTGTAPQHYEAPYTPYYYQSPETIEGPFLDTESSYSDSEFFAYEDGLTLSHRDAQHESDLDSAMYSTPSSEASDEGRNEDKAGGLGSLYLPGEQNLLKPSAGSGFSTHSTASLISNEEQFEDYGEGEDIDYSPGSPCPDDESRTNALSDLGSSVPSSAGQTPRKARLMYNTDLLDIYCTQCSKKITLLNDLEARLKNLKANSPNRKISSTAFGRQLLHNSNLSSSN... | Function: Acts as a regulator of endocytic traffic by participating in membrane delivery. Required for the abcission step in cytokinesis, possibly by acting as an 'address tag' delivering recycling endosome membranes to the cleavage furrow during late cytokinesis (By similarity).
Location Topology: Peripheral membrane ... |
Q9BXF6 | MALVRGAEPAAGPSRWLPTHVQVTVLRARGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTHGCPEWREECSFELPPGALDGLLRAQEADAGPAPWAASSAAACELVLTTMHRSLIGVDKFLGQATVALDEVFGAGRAQHTQWYKLHSKPGKKEKERGEIEVTIQFTRNNLSASMFDLSMKDKPRSPFSKIRDKMKGKKKYDLESASAILPSSAIEDPDLGSLGKMGKAKGFFLRNKLRKSSLTQSNTSLGSDSTLSSASGSLAYQGPGAELLTRSPSRSSWLSTEGGRDSAQSPKLFTHKRTYSDEANQMRVAPPRA... | Function: Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis.
PTM: Phosphorylated on serine and threonine residues. Phosphorylation at Ser-... |
Q9Y644 | MSRARGALCRACLALAAALAALLLLPLPLPRAPAPARTPAPAPRAPPSRPAAPSLRPDDVFIAVKTTRKNHGPRLRLLLRTWISRARQQTFIFTDGDDPELELQGGDRVINTNCSAVRTRQALCCKMSVEYDKFIESGRKWFCHVDDDNYVNARSLLHLLSSFSPSQDVYLGRPSLDHPIEATERVQGGRTVTTVKFWFATGGAGFCLSRGLALKMSPWASLGSFMSTAEQVRLPDDCTVGYIVEGLLGARLLHSPLFHSHLENLQRLPPDTLLQQVTLSHGGPENPHNVVNVAGGFSLHQDPTRFKSIHCLLYPDTDWC... | Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in enhancement of NOTCH1 activation by DLL1 and JAG1. May b... |
O09009 | MSRARRVLCRACLALAAVLAVLLLLPLPLPLPLPRAPAPDPDRVPTRSLTLEGDRLQPDDVFIAVKTTRKNHGPRLRLLLRTWISRAPRQTFIFTDGDDPELQMLAGGRMINTNCSAVRTRQALCCKMSVEYDKFLESGRKWFCHVDDDNYVNPKSLLHLLSTFSSNQDIYLGRPSLDHPIEATERVQGGGTSNTVKFWFATGGAGFCLSRGLALKMSPWASLGSFMSTAERVRLPDDCTVGYIVEGLLGARLLHSPLFHSHLENLQRLPSGAILQQVTLSYGGPENPHNVVNVAGSFNIQQDPTRFQSVHCLLYPDTHW... | Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in enhancement of NOTCH1 activation by DLL1 and JAG1 . May ... |
Q9YHB3 | MNFSCLGLSKICFLVSVIFCTFLLLFIPKTKTPWRPRTYPQPRPPPLFNATCGKQFALPGIEHAQQKLPTHTTDITHFEDPGNVEDWRAYILGRENPDEKHEGPTDNPGEHKSVLASSINSSKDALEFEDLFIAVKTTRKYHKTRLDLLLQTWISRAKQQTFIFTDGEDQDLRQRAGIQVINTNCSAMHTRQALCCKMAVEYDKFIESERKWFCHVDDDNYVNLFSLRHLLASFSHSQDVYLGRPSLDHPIEAIERVKSDGSASVRFWFATGGAGFCISRGLALKMSPWASMGNFITTAELVRLPDDCTIGYIIEGLLGV... | Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (By similarity). Involved in forelimb development and in adult forelimb regeneration.
Catalytic Activity: 3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain ... |
A6X7E7 | MTDATAARRNIVILTIAQALGASSPPIVISLGGLVGQKLSSDPALVTLPVSLFNLGLALGTLPAAFFMRQFGRRNAYMLGALVGAAAGVIAAAGIFAASFLIFCLGTLTAGFYASYVQSYRFAATDAATGDMKARAISWVMVGGLVAAIVGPQLVIWTRDTIPDAMFAGSFLSQAVLGLLALPVLFMLRAPKVRKDPNAIHDTGRPLGEILRSPRFILSVAAGVCSYALMTFVMTAAPIAMVGHGHSVDHAALGIQWHVLAMFAPSFFTGKLITRFGKEKITALGLVLIAFSAIIALGGFDVGHFWGALIFLGIGWNFGF... | Function: Transports riboflavin into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41659
Sequence Length: 398
Subcellular Location: Cell membrane
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Q08DC7 | MPTPPEAEKQQTGPEEADQPPSMSSHDAAPPAPPRRNPCCLCWCCCCSCSWNEERRRAWRASRESRLQPLPSCEVCATPTPTPTPTPEEVRSWAQSFDKLMHSPAGRSVFREFLRTEYSEENMLFWLACEELKAEANQHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINKKMQEPSAHTFDDAQLQIYTLMHRDSYPRFLSSPAYRALLLQGASQSSSEA | Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoyl... |
P49795 | MPTPHEAEKQITGPEEADRPPSMSSHDTASPAAPSRNPCCLCWCCCCSCSWNQERRRAWQASRESKLQPLPSCEVCATPSPEEVQSWAQSFDKLMHSPAGRSVFRAFLRTEYSEENMLFWLACEELKAEANQHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINKKMQEPSAHTFDDAQLQIYTLMHRDSYPRFLSSPTYRALLLQGPSQSSSEA | Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoyl... |
Q8H1F2 | MASGCALHGGCPSDYVAVAISVICFFVLLSRSVLPCLIHKAPRTNSSSFWIPVIQVISSFNLLFSIMMSVNLLRFRTKHWWRYCYLWAVWIEGPLGFGLLMSCRITQAFQLYFIFVKKRLPPVKSYIFLPLVLLPWIFGAAIIHATKPLNDKCHMGLQWTFPVAGLHALYVLALIAFTRAVRHVEFRFDELRDLWKGILVSATSIVIWVTAFVLNEIHEEISWLQVASRFVLLVTGGILVVVFFSISSNQPLLSQISLKKRQNFEFQRMGQALGIPDSGLLFRKEEFRPVDPNEPLDKLLLNKRFRHSFMEFADSCYAGE... | Function: Glucose-regulated GTPase-accelerating protein (GAP) for the GTP-bound self-activating heterotrimeric G alpha protein GPA1. Cooperates with G beta-gamma dimers to maintain an unactivated but fully functional pool of GPA1. Phosphorylation-dependent endocytosis of RGS1 physically uncouples the two proteins, resu... |
Q6RG78 | MPGMFFSANPKDLKGTDQSLLDDKTQKRRPKTFGMDVKAYLRSMIPHLESGMKSSKSKDILSADEVMQWSQSLEKLLANQTGQDVFGNFLKSEFSEENIEFWLACEDYKKTESDLLRCKAEKIYKAFVHSDAAKQINIDFHTRESTAKKIKAPTLTCFDEAQKVIYTLMEKDSYPRFLKSNIYLNLLNDLQANSLK | Function: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the N-formylpeptide chemoattractant receptors and leukotriene receptors. Inhibits B cell chemotaxis toward CXCL12 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subuni... |
Q08116 | MRAAAISTPKLDKMPGMFFSANPKELKGTTHSLLDDKMQKRRPKTFGMDMKAYLRSMIPHLESGMKSSKSKDVLSAAEVMQWSQSLEKLLANQTGQNVFGSFLKSEFSEENIEFWLACEDYKKTESDLLPCKAEEIYKAFVHSDAAKQINIDFRTRESTAKKIKAPTPTCFDEAQKVIYTLMEKDSYPRFLKSDIYLNLLNDLQANSLK | Function: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the N-formylpeptide chemoattractant receptors and leukotriene receptors . Inhibits B cell chemotaxis toward CXCL12 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subun... |
Q09777 | MPALHNPSSPPPSYEAVTSYRNGNSIDSGDKRQQCSRLMKITSNGRPYSKDFLELFSTMVISTNFSRNRYRFSYVENSCTLLQLLSTLENLQLSQVNRIKSRCGSKVLKSTTKFTIPKTAAKCLCNTFLNARLLQIVNNPSARKFSNEKCLLQLTRKGYSVVSEFLQHNGHNSQAELYASKWNHSAPVIVSISRFSSTDQILKDSSFCEMLLVRMLGSVHEIGKSKNPLLVPVYSVSSPSPKDSLSKVTKYQMFGIDIAEWLMCNTMLLDWSEMETVASDLLIHSYIAYENNSETPLKFSYAKGVSYFLTGKGIATLGWT... | Function: Negatively regulates pheromone signaling during mating. Acts in a negative feedback loop that is essential for the mating process. This loop acts to down-regulate cellular sensitivity to pheromone. Activated by ste11.
Sequence Mass (Da): 54362
Sequence Length: 481
Domain: The fungal-differentiation regulator ... |
A1A643 | MPGIFFSHPNALKEVTNKPDEVMAQKKKNFAVPWKNYLKSMLPHLETIKSSSSSSSSDTEKNKLTPNEIIQWTMSLEKLLVSEEGQAVFRAFLKSEFSEENIEFWLACEDYKATNDSEELRCKANVIYQEFIQPNANKQINIDFSTRNSVTKDLLEPTKATFNGAQKMIFILMERDSYPRFLKSEIFFRLAERHHGNNMRG | Function: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the N-formylpeptide chemoattractant receptors and leukotriene receptors. Inhibits B cell chemotaxis (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby dr... |
P79348 | MPRLSQDNQQGHQKHFSRPSRRIQFLPPPWTEAYNVNVHQTVENEGCATAMHNVKLLGSPAAPTLLSLLSGTLSGFARFFALLLRRPPPEAPLRRRDFSALIPALPAAVLSPGHEERPGRLSLLLRAALALPGRPPGGRLPREVDASAGQSSSIPPMGSEWMEMRKRPVCAAQEPTACAPGQPGVENQGSNACCFCWCCCCSCSCLTVRNQEEQRLRRTSYEARTEDLPTCEESPGPTLEEASAWAQSFDKLMLTPAGRNAFREFLRTEFSEENMLFWMACEELKKEANKATIEEKARIIYEDYISILSPKEVSLDSRVR... | Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is i... |
Q9PWA1 | MGSERTEMRKRQMAATQETPGTAQAQHSVGNRGPNACCFCWCCCCSCSCLTVRNQEEERARRTSHELQAEGIPNCEESPAPTLEEVNAWAQSFDKLMLTPAGRNAFREFLRTEFSEENMLFWMACEELKQESNKSVIEEKARLIYEDYISILSPKEVSLDSRVREVINRNMLEPSQHTFDDAQLQIYTLMHRDSYPRFMNSAIYKDLLRSLSEKSIEA | Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is i... |
O76081 | MPQLSQDNQECLQKHFSRPSIWTQFLPLFRAQRYNTDIHQITENEGDLRAVPDIKSFPPAQLPDSPAAPKLFGLLSSPLSSLARFFSHLLRRPPPEAPRRRLDFSPLLPALPAARLSRGHEELPGRLSLLLGAALALPGRPSGGRPLRPPHPVAKPREEDATAGQSSPMPQMGSERMEMRKRQMPAAQDTPGAAPGQPGAGSRGSNACCFCWCCCCSCSCLTVRNQEDQRPTIASHELRADLPTWEESPAPTLEEVNAWAQSFDKLMVTPAGRNAFREFLRTEFSEENMLFWMACEELKKEANKNIIEEKARIIYEDYIS... | Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is i... |
Q93ZG7 | MADTVEKVPTVVESSSSSTVEASNSAEKTEPTTEKKKWGDVEDDDDEEEAVSELNSLSIKEEEKPDSILEEPEDSNIKAVTSGDTPYTSASRFEDLNLSPELMKGLYVEMKFEKPSKIQAISLPMIMTPPHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTRELANQNMEVLQKMGKFTGITAELAVPDSTRGAPAATRGAPVSAHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATDGFRDDSLKIMKDIGRVNPNFQVLLFSATFNETVKDFVARTVKDPNQLFVKREDLALDSVKQYKVVC... | Function: ATP-dependent RNA helicase essential for mRNA export from the nucleus. Plays an important role in the positive regulation of CBF/DREB transcription factors.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 55384
Sequence Length: 496
Domain: The Q motif is unique to and characteristic... |
Q10RI7 | MADGGKPPTPEKKSWADVEEEEEAKAKAAAAAEAASSSSSNEPAVDAQAKQIEALSLSVPEEHGGSGGGGDDQGPPLLDDSDESQIQAVTSGGTVYESAAAFEDLKLTPELLKGLHDEMGFSRPSKIQAVTLPMILTPPYKDLIAQAHNGSGKTTCFVLGMLSRVDPNRKVTQAICICPTRELAQQNKSVLMRMGKFTGITCACAIPPAQKDYVPIAKMPKITDQVVIGTSGTLMKWINHKKILTNDIKILVFDEADHMLAEDGFRSDSERIMRDIQRSAGGCQVLLFSATFNERVKDFVTRVIKDGNQIFVKKEELTLE... | Function: ATP-dependent RNA helicase essential for mRNA export from the nucleus. Plays an important role in the positive regulation of CBF/DREB transcription factors (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 55855
Sequence Length: 505
Domain: The Q motif is unique to an... |
Q56X76 | MVGASRTILSLSLSSSLFTFSKIPHVFPFLRLHKPRFHHAFRPLYSAAATTSSPTTETNVTDPDQLKHTILLERLRLRHLKESAKPPQQRPSSVVGVEEESSIRKKSKKLVENFQELGLSEEVMGALQELNIEVPTEIQCIGIPAVMERKSVVLGSHTGSGKTLAYLLPIVQLMREDEANLGKKTKPRRPRTVVLCPTRELSEQVYRVAKSISHHARFRSILVSGGSRIRPQEDSLNNAIDMVVGTPGRILQHIEEGNMVYGDIAYLVLDEADTMFDRGFGPEIRKFLAPLNQRALKTNDQGFQTVLVTATMTMAVQKLV... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 68924
Sequence Length: 621
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
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A0A1D6LAB7 | MASLTLPALALALSNPGAVRLRAAAFRCWALRRRGWAAAGALASPNSVLSEHAFKRLQLGSDDEDGEGPYGSDADEGFEAGEGDNEELAIARLGLPDELVATLEKRGITHLFPIQRAVLIPALEGRDLIARAKTGTGKTLAFGIPMIKQLIEQDDGRITRRGRTPRVLVLAPTRELAKQVEKEIKESAPKLGTVCVYGGVSYNVQQNALSRGVDVVVGTPGRIIDLINGGSLQLGEVQYLVLDEADQMLAVGFEEDVETILQQLPAGRQSMLFSATMPSWVKKLSRRYLNNPLTIDLVGDQDEKLAEGIKLYAIPLTTTS... | Function: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts. Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit. Required for normal development of... |
Q8L7S8 | MASTVGVPSLYQVPHLEISKPNSKKRSNCLSLSLDKPFFTPLSLVRRTRRIHSSSLLVPSAVATPNSVLSEEAFKSLGLSDHDEYDLDGDNNNVEADDGEELAISKLSLPQRLEESLEKRGITHLFPIQRAVLVPALQGRDIIARAKTGTGKTLAFGIPIIKRLTEEAGDYTAFRRSGRLPKFLVLAPTRELAKQVEKEIKESAPYLSTVCVYGGVSYTIQQSALTRGVDVVVGTPGRIIDLIEGRSLKLGEVEYLVLDEADQMLAVGFEEAVESILENLPTKRQSMLFSATMPTWVKKLARKYLDNPLNIDLVGDQDEK... | Function: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts . Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit . Required for normal development ... |
Q0DM51 | MASLLTLPSLSLSNPSASAAAAGAGAAPSLRLRAAFRCWALRRAGGGRWAAAGAIASPNSVLSEHAFKRLQLSDEEEEEEEGAYGSDEEGVEAVGGGEGDEDELAIARLGLPEQLVSTLEKRGITHLFPIQRAVLIPALDGRDLIARAKTGTGKTLAFGIPMIKQLMEEDDGRSVRRGRIPRVLVLAPTRELAKQVEKEIKESAPKLSTVCVYGGVSYNVQQNALSRGVDVVVGTPGRIIDLINGGSLQLGEVKYLVLDEADQMLAVGFEEDVETILQQLPAERQSMLFSATMPGWVKKLSRRYLNNPLTIDLVGDQDEK... | Function: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts. Binds specific group II introns in chloroplasts and facilitates their splicing. Required for normal development of chloroplasts.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 81615
Sequence Length: 758
... |
Q5JKF2 | MSAGTAPAAPRYAPDDPSLPKPWRGLVDGTTGYLYYWNPETNITQYEKPLPPEDQLPPPPPLPPPPPRSGRGDRDRDRRDRSRSRTPPRRDHRDRDRDRDRRHDDHRSAPSHHHPLPAAAAIAADDPSTEAYRHRHEITVVGDNVPAPITSFETGGFPPEILKEIQRAGFSSPTPIQAQSWPIALQCQDVVAIAKTGSGKTLGYLLPGFMHIKRLQNNPRSGPTVLVLAPTRELATQILEEAVKFGRSSRISSTCLYGGAPKGPQLRDLDRGVDVVVATPGRLNDILEMRRISLKQVSYLVLDEADRMLDMGFEPQIRKI... | Function: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 87980
Sequence Length: 792
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases an... |
Q3EBD3 | MNEEGCVPHNSDVVKQKSIDQRAPLSGEPKCVICSRYGEYICDETNDDVCSLECKQALLRRVDSARVFPATDECFYVRDPGSSSHDAQLLRRKLDIHVQGQGSAVPPPVLTFTSCGLPPKLLLNLETAGYDFPTPIQMQAIPAALTGKSLLASADTGSGKTASFLVPIISRCTTYHSEHPSDQRRNPLAMVLAPTRELCVQVEDQAKMLGKGLPFKTALVVGGDPMSGQLYRIQQGVELIIGTPGRVVDLLSKHTIELDNIMTFVLDEVDCMLQRGFRDQVMQIFQALSQPQVLLFSATISREVEKVGGSLAKEIILVSI... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 55218
Sequence Length: 505
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
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Q0E2Z7 | MEQEENHSADHLSAQPGNGNELEESSVKERCFEQREALVGEPRCVICGRYGEYICDQTDDDICSVECKTILLSKLSAETRPVVKAAKRVNLPVGDESFCIRDENFPKIPSMHDGQIASLRSKLDICVKGEDVPDPIMCFSSSGLPEKLVLNLEAAGYVMPTPVQMQVIPSSICNRSLLVSADTGSGKTASFLVPIIAHCSHVRSERCTDKQGPLAIVLAPTRELCLQVEEQAKVLGKGLPFKTALVVGGDPLAQQIYRIENGIELIVGTPGRLIDLLMKHNVDLNKVDVFVLDEVDCLLERGFRDQVMQIFQALSHPQVM... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 59046
Sequence Length: 536
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
|
Q9SZB4 | MEVDDGYVEYVPVEERLAQMKRKVVEEPGKGMMEHLSDKKKLMSVGELARGITYTEPLSTWWKPPLHVRKMSTKQMDLIRKQWHITVNGEDIPPPIKNFMDMKFPSPLLRMLKDKGIMHPTPIQVQGLPVVLSGRDMIGIAFTGSGKTLVFVLPMIILALQEEIMMPIAAGEGPIALVICPSRELAKQTYDVVEQFVASLVEDGYPRLRSLLCIGGVDMRSQLDVVKKGVHIVVATPGRLKDILAKKKMSLDACRLLTLDEADRLVDLGFEDDIRHVFDHFKSQRQTLLFSATMPAKIQIFATSALVKPVTVNVGRAGAA... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 60258
Sequence Length: 542
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
|
Q9SF41 | MLEKSKSRKENDRKDRDRSKKENGRRDTTEMRSRVKRCDSEEEERIRIRRDRKSSDFEEEEYERDSKRRGEDKGRGRRERDRDRGKYLKRDRERREREKEKGRKKQKKERSREDCNEESDDVKCGLKRKRTERSRHGDDDVEKKTRDEQVEDEQKQLAEEVEKRRRRVQEWQELKRQNEEAQIESKGPETGKAWTLDGESDDEVKSDSEMDVDRDTKLENGGDAKMVASENETAVTVSENGGDRAADEDEIDPLDAFMNTMVLPEVEKLSNIVIDGILDFKMNGKETGDQAKKGFNKAALGRIIQGEDSDSDYSEPKSDD... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 111625
Sequence Length: 989
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
|
Q0J7Y8 | MEEEEVVVVVDEEESERRRQKMIEEEKKRLDEEMELRRRRVKEWQEQKRLEEEEAKRREQEAAAGAGTPAAAAGADGDSNAGKKWTLDGEESDEEGYKEDSQNAEDDGGITADLPSEVNDANVAAPMEEDEIDPLDAFMSSMVLPEVAKLETAVASMESMPASNMGDKNGKSAKDAVSNGDKKGQKKAMGRIMQGDDSDSDYDDDDDDEGGSKDEDDEEFMKRVKKTKVEKLAIVDHSKIEYQPFRKNLYIEVKDITMMTGEEVATYRKNLELKVHGKDVPKPIKTWVQSGLTSKLLDTIKKLGFEKPMPIQAQALPIIM... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 104832
Sequence Length: 947
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
|
O05263 | MKRKASIMFVHQDKYEEYKQRHDDIWPEMAEALKAHGAHHYSIFLDEETGRLFAYLEIEDEEKWRKMADTEVCQRWWKSMAPLMKTNSDFSPVAIDLKEVFYLD | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12575
Sequence Length: 104
Pathway: Carbohydrate metabolism; L-rhamnose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
|
Q8A044 | MKREAFKMYLKPGYEAEYEKRHAAIWPELKALLSKNGVSDYSIYWDKETNILFAFQKTEGEGGSQDLGNTEIVQKWWDYMADIMEVNPDNSPVSIPLPEVFHMD | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12123
Sequence Length: 104
Pathway: Carbohydrate metabolism; L-rhamnose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
|
Q0BA68 | METIAFRMRLHPGKRDEYRRRHDAIWPELADALRAAGISDYWIFLDEDTHHLFAVLKRPIGHRIAQLAETDVMRRWWAYMADLMATGPDGRPVEKSLEPMFHLE | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12314
Sequence Length: 104
Pathway: Carbohydrate metabolism; L-rhamnose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
|
A6LQL0 | MIQKAFKMKLFEGKEEEYKKRHNEIWPDLVKELKSHGTSKYLIFYDKDTNILFSYIEMENEELWDEIAETDACKKWWAFMKDIMETNPDNSPISVELSNVFNLK | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12547
Sequence Length: 104
Pathway: Carbohydrate metabolism; L-rhamnose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
|
A7ML65 | MIRKAFVMQVNPDAHEEYQRRHSPIWPELEAVLKQHGAHHYAIWLDAQRHLLFATVEIESEARWNAVAQTEVCQRWWKHMREIMPSNPDNSPVSQELKNVFYLE | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12446
Sequence Length: 104
Pathway: Carbohydrate metabolism; L-rhamnose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
|
A8LS71 | MEKIAFKMMLNPGCREEYIKRHDAIWPELVDLLRKAGVSDYSIHLDPETDTLFAVLWRKEGHGMDDLPSHPVMQKWWAHMADIMQTQPDNAPVVTPLDTVFHMP | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12083
Sequence Length: 104
Pathway: Carbohydrate metabolism; L-rhamnose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
|
Q53QZ3 | MQKSTNSDTSVETLNSTRQGTGAVQMRIKNANSHHDRLSQSKSMILTDVGKVTEPISRHRRNHSQHILKDVIPPLEQLMVEKEGYLQKAKIADGGKKLRKNWSTSWIVLSSRRIEFYKESKQQALSNMKTGHKPESVDLCGAHIEWAKEKSSRKNVFQITTVSGNEFLLQSDIDFIILDWFHAIKNAIDRLPKDSSCPSRNLELFKIQRSSSTELLSHYDSDIKEQKPEHRKSLMFRLHHSASDTSDKNRVKSRLKKFITRRPSLKTLQEKGLIKDQIFGSHLHKVCERENSTVPWFVKQCIEAVEKRGLDVDGIYRVSG... | Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has activity toward RAC1. Overexpression results in an increase in actin stress fibers and cell contraction.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54544
Sequence Length: 475
Domain: The PH... |
Q811M1 | MEKRTSCSVQTSTNCDNSLEILNSAHQATGAVQMRIKNANSHQDRQSQTKSMILTDAGKVTEPISRHRRNHSQHVLKDVIPPLEHPMVEKEGYLQKAKIADGGKKLRKNWSTSWIVLSGRKIEFYKDSKQQALPNMKTRHNVESVDLCGAHIEWAKEKSSRKSVFQITTVSGNEFLLQSDIDFLILDWFQAIKNAIDRLPKNPSCGSLELFNLQRSSSSELPSHCHIDRKEQKPEHRKSFMFRLHHSASDTSDKNRVKSRLKKFISRRPSLKTLQEKGLIKDQIFGSHLHTVCEREHSTVPWFVKQCIEAVEKRGLDVDG... | Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has activity toward RAC1. Overexpression results in an increase in actin stress fibers and cell contraction (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55339
Sequence Length: 48... |
Q68EM7 | MKKQFNRMKQLANQTVGRAEKTEVLSEDLLQIERRLDTVRSICHHSHKRLVACFQGQHGTDAERRHKKLPLTALAQNMQEASTQLEDSLLGKMLETCGDAENQLALELSQHEVFVEKEIVDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSGTNFQGLPSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKTLPEMRAHQDKWAEKPAFGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAV... | Function: Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex form... |
Q9FMM4 | MQGERASLGYLSEALNFEHGSSSSNGVIDHWENIHSLGDNDLQDYMIANSESNTSLANSVYHEQQGLRRFSLGEASSSGTKDEASSHNEQRMETRCFDGRGNEIIDLDPVFAQPSGTNQPVQNVNLNAEYIEIHEDINPYRGRSGFIEANGPGTRVSQPGRSFEENGVGTGSSVEGRRASCKRKALEGSISQSSSGGYHDFQRGESSSWTPGSTVFRPGNGLNISGSLDNGPRGMVSGTVPNFPVSAPNFPVSAIAESSSRNICVRSNPSDHQETVNPSTFAAGTVVRRPVPPSQLNLSRHLPADQHSLDLRPGQSFVVS... | Function: Probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass... |
P25888 | MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASDQVTQHVHFVDKKRKRELLSHMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY... | Function: DEAD-box RNA helicase involved in ribosome assembly. Has RNA-dependent ATPase activity and unwinds double-stranded RNA. May play a role in the interconversion of ribosomal RNA-folding intermediates that are further processed by DeaD or SrmB during ribosome maturation.
Catalytic Activity: ATP + H2O = ADP + H(+... |
Q9RPT1 | MHPYFSLAGRIALVTGGSRGIGQMIAQGLLEAGARVFICARDAEACADTATRLSAYGDCQAIPADLSSEAGARRLAQALGELSARLDILVNNAGTSWGAALESYPVSGWEKVMQLNVTSVFSCIQQLLPLLRRSASAENPARVINIGSVAGISAMGEQAYAYGPSKAALHQLSRMLAKELVGEHINVNVIAPGRFPSRMTRHIANDPQALEADSASIPMGRWGRPEEMAALAISLAGTAGAYMTGNVIPIDGGFHL | Function: Required for the synthesis of the beta-hydroxy acid moiety of rhamnolipids.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Mass (Da): 26831
Sequence Length: 256
Pathway: Lipid metabolism; rhamnolipid biosynthesis.
EC: 1.1.1.100
|
P54291 | MIELLSESLEGLSAAMIAELGRYRHQVFIEKLGWDVVSTSRVRDQEFDQFDHPQTRYIVAMSRQGICGCARLLPTTDAYLLKDVFAYLCSETPPSDPSVWELSRYAASAADDPQLAMKIFWSSLQCAWYLGASSVVAVTTTAMERYFVRNGVILQRLGPPQKVKGETLVAISFPAYQERGLEMLLRYHPEWLQGVPLSMAV | Function: Required for the synthesis of BHL (N-butanoyl-L-homoserine lactone), and HHL (N-hexanoyl-L-homoserine lactone) autoinducer molecules which bind to RhlR and thus acts in elastase biosynthesis regulation.
Catalytic Activity: a fatty acyl-[ACP] + S-adenosyl-L-methionine = an N-acyl-L-homoserine lactone + H(+) + ... |
Q9LPG6 | MDDTTYKPKNILITGAAGFIASHVANRLIRNYPDYKIVVLDKLDYCSDLKNLDPSFSSPNFKFVKGDIASDDLVNYLLITENIDTIMHFAAQTHVDNSFGNSFEFTKNNIYGTHVLLEACKVTGQIRRFIHVSTDEVYGETDEDAAVGNHEASQLLPTNPYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGPNQFPEKMIPKFILLAMSGKPLPIHGDGSNVRSYLYCEDVAEAFEVVLHKGEIGHVYNVGTKRERRVIDVARDICKLFGKDPESSIQFVENRPFNDQRYFLDDQKLKKLGWQERTNWEDGLKKTMDW... | Function: Trifunctional enzyme involved in UDP-beta-L-rhamnose biosynthesis, a precursor of the primary cell wall components rhamnogalacturonan I (RG-I) and rhamnogalacturonan II (RG-II). Catalyzes the dehydration of UDP-glucose to form UDP-4-dehydro-6-deoxy-D-glucose followed by the epimerization of the C3' and C5' po... |
Q9LH76 | MATYKPKNILITGAAGFIASHVANRLVRSYPDYKIVVLDKLDYCSNLKNLNPSKSSPNFKFVKGDIASADLVNYLLITEEIDTIMHFAAQTHVDNSFGNSFEFTKNNIYGTHVLLEACKVTGQIRRFIHVSTDEVYGETDEDASVGNHEASQLLPTNPYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGPNQFPEKLIPKFILLAMNGKPLPIHGDGSNVRSYLYCEDVAEAFEVVLHKGEVNHVYNIGTTRERRVIDVANDISKLFGIDPDSTIQYVENRPFNDQRYFLDDQKLKKLGWCERTNWEEGLRKTMEWYT... | Function: Trifunctional enzyme involved in UDP-beta-L-rhamnose biosynthesis, a precursor of the primary cell wall components rhamnogalacturonan I (RG-I) and rhamnogalacturonan II (RG-II) . Catalyzes the dehydration of UDP-glucose to form UDP-4-dehydro-6-deoxy-D-glucose followed by the epimerization of the C3' and C5' p... |
B7MG11 | MNALLTNPFKERLRKGEVQIGLWLSSTTAYMAEIAATSGYDWLLIDGEHAPNTIQDLYHQLQAVAPYASHPVIRPVEGSKPLIKQVLDIGAQTLLIPMVDTADQARQVVSATRYPPYGERGVGASVARAARWGRIENYMAQVNDSLCLLVQVESKTALDNLDEILDVEGIDGVFIGPADLSASLGYPDNAGHPEVQRIIETSIRRIRAAGKAAGFLAVAPDMAQQCLAWGANFVAVGVDTMLYSDALDQRLAMFKSGKNGPRVKGSY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible retro-aldol cleavage of 2-keto-3-deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde.
Catalytic Activity: 2-dehydro-3-deoxy-L-rhamnonate = (S)-lactaldehyde + pyruvate
Sequence Mass (Da): 28911
Sequence Length: 267
EC: 4.1.2.53
|
Q8XE09 | MNALLTNPFKERLRKGEVQIGLWLSSTTAYMAEIAATSGYDWLLIDGEHAPNTIQDLYHQLQAVAPYASQPVIRPVEGSKPLIKQVLDIGAQTLLIPMVDTADQARQVVSATRYPPYGERGVGASVARAARWGRIENYMAQVNDSLCLLVQVESKTALDNLDEILDVEGIDGVFIGPADLSASLGYPDNAGHPEVQRIIETSIRRIRAAGKAAGFLAVAPDMAQQCLAWGANFVAVGVDTMLYSDALDQRLAMFKSGKNGPRIKGSY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible retro-aldol cleavage of 2-keto-3-deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde.
Catalytic Activity: 2-dehydro-3-deoxy-L-rhamnonate = (S)-lactaldehyde + pyruvate
Sequence Mass (Da): 28916
Sequence Length: 267
EC: 4.1.2.53
|
Q9Z3Q5 | MGNNENGGISFCVFVVVIGFGTGAVAQEPANQSEAVTSLEEIVVTGGRSAQQISEIARTIYVVDSDQIQAEARSGKTLQQILGETIPSFDPASDGARTSFGQNLRGRPPLILVDGVSMNSARSLSRQFDAIDPFNIERVEVLSGATAIYGGNATGGIINIITKKGKDAEPGLHAEVTGGMGSGFAGSQDFDRNAAGAVTYNSENWDARLSIAGNRTGAFYDGSGTLLIPDITQTSTAFNERIDLMGSIGYQIDDDRRVEFSGQYFDSKQDSDYGLYYGPFFAALADPSLFETRSGYESDFNPQTRRSMLNVTYTDNDVFG... | Function: Receptor for the siderophore rhizobactin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80634
Sequence Length: 746
Subcellular Location: Cell outer membrane
|
E1W9W8 | MPGSTRKLPVWLPILVLLIAMSSIQSGASLAKSLFPLVGAPGVTALRLALGTLILIAFFKPWRLRFAKEQRLPLLFYGLSLGGMNYLFYLSIQTVPLGIAVALEFTGPLAVALFSSRRPVDFIWVVLAVLGLWFLLPLGQDMSHVDLTGAALALGAGACWAVYILTGQRAGAEHGPATVAVGSLIAAIIFVPIGAVQAGDALWHWSILPLGLAVAVLSTALPYSLEMIALTRLPTRTFGTLMSMEPALAAVSGMIFLGETLTGIQILALCAIIAASMGSTLTIRREPQIKQVDVK | Function: Involved in the efflux of threonine and homoserine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31228
Sequence Length: 295
Subcellular Location: Cell inner membrane
|
P0AG36 | MTLEWWFAYLLTSIILSLSPGSGAINTMTTSLNHGYRGAVASIAGLQTGLAIHIVLVGVGLGTLFSRSVIAFEVLKWAGAAYLIWLGIQQWRAAGAIDLKSLASTQSRRHLFQRAVFVNLTNPKSIVFLAALFPQFIMPQQPQLMQYIVLGVTTIVVDIIVMIGYATLAQRIALWIKGPKQMKALNKIFGSLFMLVGALLASARHA | Function: Conducts the efflux of homoserine and homoserine lactone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22427
Sequence Length: 206
Subcellular Location: Cell membrane
|
Q9L6N6 | MTFEWWFAYLLTSTLLSLSPGSGAINTMTTSINHGYRGAVASIAGLQTGLGIHIVLVGVGLGTLFSRSLLAFEILKWAGAAYLIWLGIQQWRAAGAIDLHTLAQTQSRGRLFKRAIFVNLTNPKSIVFLAALFPQFIMPQQPQLAQYLILGVTTIVVDMVVMTGYATLAQRIAAWIKGPKQMKALNKAFGSLFMLVGALLASARHA | Function: Conducts the efflux of homoserine and homoserine lactone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22322
Sequence Length: 206
Subcellular Location: Cell membrane
|
P0AG39 | MLMLFLTVAMVHIVALMSPGPDFFFVSQTAVSRSRKEAMMGVLGITCGVMVWAGIALLGLHLIIEKMAWLHTLIMVGGGLYLCWMGYQMLRGALKKEAVSAPAPQVELAKSGRSFLKGLLTNLANPKAIIYFGSVFSLFVGDNVGTTARWGIFALIIVETLAWFTVVASLFALPQMRRGYQRLAKWIDGFAGALFAGFGIHLIISR | Function: Conducts the efflux of threonine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22474
Sequence Length: 206
Subcellular Location: Cell inner membrane
|
H2DF87 | MDTSTSAYAPLPGEDPLFSGHPPASLRRSWKGFAVIFASVLFLLSLVGLIIHQGPQQPPDVMPDKQDEHHHPQSTTPASETTASWEPRGKALGVSAKSNPPVSDELSYNWTNAMFSWQRTAFHFQPERNWMNDPNGPLFYKGWYHLFYQYNPDSAIWGNITWGHAVSTDLIHWLYLPIAMVADQWYDANGVWSGSATLLPDGQIVMLYTGDTVDAVQVVCLAHPANLSDPLLLDWVKYSGNPVLTPPPGILTTDFRDPTTAWTGPDGKWRITIGSKVNTTGISFVYHTEDFKTYNMSKGVLHAVPGTGMWECIDFYPVAI... | Function: Acidic vacuolar invertase involved in light-induced bud burst .
PTM: Glycosylated.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Mass (Da): 65375
Sequence Length: 588
Subcel... |
H2DF88 | MDTNTTSYTPLPGDPFLSGPPETPRRPLKGFAVIFASVIFLMSLVALIIHQGPQQPPDVMPDKQDEHHHPQSTTNTMLSWQRTAFHFQPEKNWMNDPNGPMYYKGWYHFFYQYNPRGAVWGNIVWGHAVSRDLIHWLHLPLAMVADQWYDINGVWTGSATILPNDQIVMLYTGSTNESVQVQCLAYPADHKDPLLTKWVKYSGNPVLVPPPGIGVKDFRDPTTAWYITEGKWRITIGSKVNKTGISLVYDTKDFIKYEQLDGVLHAVPGTGMWECIDFYPVSKTSDKGLDTSQNGADVKHVMKASLDDDRNDYYALGSYN... | Function: Vacuolar invertase.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71647
Sequence Length: 640
Subcellular Location: Membrane
EC: 3.2.1.26
|
Q8NHV9 | MARSLVHDTVFYCLSVYQVKISPTPQLGAASSAEGHVGQGAPGLMGNMNPEGGVNHENGMNRDGGMIPEGGGGNQEPRQQPQPPPEEPAQAAMEGPQPENMQPRTRRTKFTLLQVEELESVFRHTQYPDVPTRRELAENLGVTEDKVRVWFKNKRARCRRHQRELMLANELRADPDDCVYIVVD | Function: Transcription factor maybe involved in reproductive processes. Modulates expression of target genes encoding proteins involved in processes relevant to spermatogenesis.
Sequence Mass (Da): 20542
Sequence Length: 184
Domain: Mutagenesis of amino acids 147 to 164 and 155 to 164 lead to a major cytoplasmic local... |
Q852U6 | MTSASELFSTRRSRPGRSDPALESDTSSYRHHSHHHHRRHGVHHHNQRHDSDGCDPLRRPTPRLRRFFHHPIQERSRPIRDVQGTSQYLNTDSTDTETQSSSFVNLNGSERLPGAVLLARDRLFERLRGVSLSSNSRSNRVSLDDQRESSFHSIDGDPIFQLAGLQVTYECNKKPQGLTQDAINCLHRQTFSSAEVKSEMRDCSICLESFTKGDMLISLPCTHSFHSSCLNPWLRACGDCPCCRRAIAKE | Function: Probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass... |
Q9XVW1 | MSSSPHTHTLIIMERLSEVRLYSSPMTSVLNSNLSSCLTNAFIPDTVRMASSPLLAWMTLVVIGTLAPVSVFSCLSLKRSVKELLTERSSKLDVLDIFRFVAILWVMLNHTGSEGRIDILDRLPSADAFKSAMHDHPIFGALMGNSALGVEIFLVLSGLLAARSWLRKADEPFFQHWKSFIARRLLRLAPSMFIFVYIAAGPIMNALLPRYSSSMVSACGFWGILSHVTFTSNWQSTPTCMGYLWYLGLDMQLYMVAPIFLNLLHKFPKRGMALTITTIIASMVIRAGYCTAYGTCNQSDVDIPFISYPGQDAETLKSIY... | Function: Involved in the response to variation in environmental oxygen levels by inhibiting hif-1-mediated gene transcription in a vhl-1-independent manner . Plays a role in susceptibility to killing mediated by P.aeruginosa and by pore-forming toxins produced by B.thuringiensis . Probably by preventing hif-1 transcri... |
O88011 | MTEKIGVLGKKTTQRTDVERIVVTPLPTVYGKFRAFGYFDHERGDEQVALVHGDLGAEDVLTRLHSECLTGDAFGSQHCECGAQLASALRQVADAGSGIVVYLRGHEGRGIGLLAKLRAMALQAEGLDTVEANLALGLPVDARDYGVAARILDDLGVRSVRLMSNNPRKREALVRHGIRVAEQVPLLIPPCESNITYLRTKRERLDHHLPHLDAAMAHVSS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (... |
O68248 | HSECLTGDALGSLKCDCGEQLEFALQNISLLGGMIIYLRQEGRNIGLFNKVNAYALQDQGFDTIEANHQLGFKSDERSYEVVETILEHFKIDKIRLLTNNPKKMSCLKNIMIIERWPIIIPSNNHNVDYLKTKKEMMGHLL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (... |
Q97B83 | MIELYSNAKLPTEFGLFRIYTFVNDENKDHAVIVRGDPRGKENVPLRIHSECLTGDVLGSLRCDCRDQLIQSLRYLGRQEYGMLIYLRQEGRGIGLLNKIKAYSLQDMGADTVEANLKLGLPVDSRNYSFAAEVLRYFEIKSIYIMTNNPEKIKSLIESGINVKGRIPIFSDPTPYDKFYLETKKTKLGHEIENI | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (... |
Q9KSJ3 | MAEVRARVDFKVGAKSNIDAEILSFHGLQSDKEHVAVIFKSADTTQEAPLVRMHSECLTGDVFHSSRCDCGEQLEETITRMGQSGGIILYLRQEGRGIGLYNKIDAYRLQSQGMNTYEANNHLGFGDDLRDFTEAAQMLQALGVKKIRLVTNNPKKIRELQEHGIEIVEVVHTSAHIKDGNENYLKAKVSHGKHQLKL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (... |
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