ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9QZU4 | MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPIDGIRSSFTSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFPIGQEVAYDLLVNNCEHFVTLLRYGEGVSEQANRAIGTIGLVAAGIDIFTFLGLFPKRQRTKY | Function: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids . Shows O-acyltransferase activity, catalyzing the transfer of... |
D2KX21 | MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPVDGIPSSFSSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFAIGQEVTYDLLVNNCEHFVTLLRYGEGVSEQANRAIGTIGLVAAGIDIFTFLGLFPKRQGAKS | Function: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (By similarity). Shows O-acyltransferase activity, catalyzing ... |
P53816 | MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKHDDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDVIIAASVAGMGLAAMSLIGVMFSRNKRQKQ | Function: Exhibits both phospholipase A1/2 and acyltransferase activities . Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids . For most substrates, PLA1 activity is much higher than PLA2 activity . Show... |
Q8R3U1 | MLAPIPEPKPGDLIEIFRPMYRHWAIYVGDGYVIHLAPPSEIAGAGAASIMSALTDKAIVKKELLCHVAGKDKYQVNNKHDEEYTPLPLSKIIQRAERLVGQEVLYRLTSENCEHFVNELRYGVPRSDQVRDAVKAVGIAGVGLAALGLVGVMLSRNKKQKQ | Function: Exhibits both phospholipase A1/2 and acyltransferase activities . Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids . For most substrates, PLA1 activity is much higher than PLA2 activity (By similarity)... |
Q9UL19 | MASPHQEPKPGDLIEIFRLGYEHWALYIGDGYVIHLAPPSEYPGAGSSSVFSVLSNSAEVKRERLEDVVGGCCYRVNNSLDHEYQPRPVEVIISSAKEMVGQKMKYSIVSRNCEHFVTQLRYGKSRCKQVEKAKVEVGVATALGILVVAGCSFAIRRYQKKATA | Function: Exhibits both phospholipase A1/2 and acyltransferase activities . Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids . For most substrates, PLA1 activity is much higher than PLA2 activity . Shows O-acylt... |
Q96KN8 | MGLSPGAEGEYALRLPRIPPPLPKPASRTASTGPKDQPPALRRSAVPHSGLNSISPLELEESVGFAALVQLPAKQPPPGTLEQGRSIQQGEKAVVSLETTPSQKADWSSIPKPENEGKLIKQAAEGKPRPRPGDLIEIFRIGYEHWAIYVEDDCVVHLAPPSEEFEVGSITSIFSNRAVVKYSRLEDVLHGCSWKVNNKLDGTYLPLPVDKIIQRTKKMVNKIVQYSLIEGNCEHFVNGLRYGVPRSQQVEHALMEGAKAAGAVISAVVDSIKPKPITA | Function: Exhibits both phospholipase A1/2 and acyltransferase activities . Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids . Shows N-acyltransferase activity, catalyzing the calcium-independent transf... |
B0Y665 | MKTTTVACAVAGLLFSCVSGAPDPVHVEIQQRALPNAPDGYTPSTVGCPASRPTIRSAASLSPNETSWLETRRGKTTSAMKDFFNHVKIQDFDAAGYIDRHSSNSSDLPNIGIAVSGGGYRALMNGAGAIKAFDSRTPNSTSAGQLGGLLQSATYLSGLSGGSWLVGSIYINNFTTISALQTHQKGTVWQFQNSIFEGPDGGSIQILDSATYYRDISNAVSGKSDAGYPTSITDYWGRALSYQMINATNGGPSYTWSSIALTDAFQKAEMPMPLVVADGRYPGELLISSNATVYEFNPWEFGTFDPTVFGFAPLEYLGTK... | Function: Catalyzes the release of fatty acids from lysophospholipids.
PTM: The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.
Location Topology: Lipid-anchor
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosph... |
Q500W4 | MAAFTGTTDKCKACDKTVYVMDLMTLEGMPYHKSCFRCSHCNGTLVICNYSSMDGVLYCKTHFEQLFKESGNFSKNFQTAGKTEKSNDATKAPNRLSSFFSGTQDKCAACKKTVYPLEKMTMEGESYHKTCFRCAHSGCPLTHSSYAALDGVLYCKVHFSQLFLEKGNYNHVLQAAANHRRSTAEEDKTEPKEDEANPTEEETSDAAAEEHES | Function: Binds to actin filaments and promotes cross-linking into thick bundles. Has an actin-stabilizing activity. Associates predominantly with long and dynamic actin bundles in the shank of growing pollen tubes. The actin regulatory activities are inhibited by pH > 6.8 and/or high [Ca(2+)].
Sequence Mass (Da): 2376... |
P34331 | MNRLPNIAKPPQKSNQRKEKAPPEVPALIADKDRGTYYEKGRFLGKGGFAHCYELTNRATREVVAGKVVPKSMLVKQYQRDKVDNERILIHRELGHINIVKLFNFFEDNLNVYITLELCARRSLMELHKRRKAVTEPEARYFTHQIVDGVLYLHDLNIIHRDMKLGNLFLNDDLVVKIGDFGLATTVNGDERKKTLCGTPNYIAPEVLNKAGHSFEVDIWAVGCILYILLFGQPPFESKSLEETYSRIRHNNYTIPSIATQPAASLIRKMLDPEPTRRPTAKQVQRDGFFKSGFMPTRLPVSCLTMVPKFGGHETSMMEE... | Function: Required for oocyte nuclear envelope breakdown before entry of oocyte into spermatheca . In meiotic cells, required for spindle dynamics and probably for spindle attachment to the chromosomes . Zygotic role in the development of the germline and nerve cord . In mitotic cells, plays a role in spindle organizat... |
P53350 | MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITCLT... | Function: Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and... |
Q07832 | MNAAAKAGKLARAPADLGKGGVPGDAVPGAPVAAPLAKEIPEVLVDPRSRRQYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQKEKMSMEISIHRSLAHQHVVGFHDFFEDSDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNQVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYEGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIHELLNDEFFTSGYIPARLPITCLT... | Function: Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and... |
P58606 | AEKDCIAPGAPCFGTDKPCCNPRAWCSSYANKCL | Function: Binds reversibly and blocks N-type voltage-gated calcium channels (Cav).
Sequence Mass (Da): 3621
Sequence Length: 34
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
P70032 | MAQVAGKKLTVAPEAAKPPGIPGSSSAVKEIPEILVDPRTRRRYLRGRFLGKGGFAKCYEITDLESREVFAGKIVPKTMLLKPHQKDKMTMEIAIQRSLDHRHVVGFHGFFEDNDFVYVVLELCRRRSLLELHKRRKAVTEPEARYYLKQTISGCQYLHSNRVIHRDLKLGNLFLNDEMEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLGKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYMRIKKNEYSIPKHINPVAAALIQKMLRSDPTSRPTIDDLLNDEFFTSGYIPSRLPTTCLTVPPRFSIAP... | Function: Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and... |
A0A6B9L3U7 | MMKFLLVLFLITITLITMAYSEEHGCIPPFQPCEGVNSRCCGLYVCFNKICLATP | Function: Binds reversibly and blocks P/Q-type voltage-gated calcium channels (Cav).
Sequence Mass (Da): 6175
Sequence Length: 55
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
Q9R012 | MELLRTITYQPAAGTKMCEQALGKACGGDSKKKRPQQPSEDGQSQAQVTPAAPHHHHHHSHSGPEISRIIVDPTTGKRYCRGKVLGKGGFAKCYEMTDLTNNKVYAAKIIPHSRVAKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINEAMELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYTMPSSLLAPAKHLIASMLSKNPEDRP... | Function: Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, R... |
A0A6B9KZ66 | MKAGMKLVLVLVIASIALLALATEVAGDCIPQGASCNRLSTIPRRCCFPMVCGWDSSTCVPATINVKP | Function: Binds reversibly and blocks P/Q-type voltage-gated calcium channels (Cav).
Sequence Mass (Da): 7107
Sequence Length: 68
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
Q20845 | MQHVLRTRGNSAQDKNKKHVPNVPPIIYDDMQVPYEKGAFLGEGGFAHCFEFRKLDCNDRLAVKVVPKVILLKSTAREKLTREVEIHRQLSHRNIVQFHHFFEDSQNVYFTLELCSKNSLMELNKQRGPLTEHEARFYTIQVAEGVKHLHNLQIIHRDLKLGNLFLNEHLQVKIGDFGLATFCEKNEKKMTRGGTPNYIAPEVLNETGHAFEVDIWAIGCILYVLLFGSPPFESRRVQETYVRIKNNDYVVPENASPTANRLIRSLLDPVPDRRPTAEAVLLDQFFKTTIEPTYPPVHQQLHKEQDVKYFAPINPVLPHV... | Function: May be required for cell division and may have a role during G1 or S phase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 70436
Sequence Length: 615
Subcellular Location: Nucleus
EC: 2.7.11.21
|
Q9H4B4 | MEPAAGFLSPRPFQRAAAAPAPPAGPGPPPSALRGPELEMLAGLPTSDPGRLITDPRSGRTYLKGRLLGKGGFARCYEATDTETGSAYAVKVIPQSRVAKPHQREKILNEIELHRDLQHRHIVRFSHHFEDADNIYIFLELCSRKSLAHIWKARHTLLEPEVRYYLRQILSGLKYLHQRGILHRDLKLGNFFITENMELKVGDFGLAARLEPPEQRKKTICGTPNYVAPEVLLRQGHGPEADVWSLGCVMYTLLCGSPPFETADLKETYRCIKQVHYTLPASLSLPARQLLAAILRASPRDRPSIDQILRHDFFTKGYTP... | Function: Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2,... |
P65735 | MTAREVGRIGLRKLLQRIGIVAESMTPLATDPVEVTQLLDARWYDERLRALADELGRDPDSVRAEAAGYLREMAASLDERAVQAWRGFSRWLMRAYDVLVDEDQITQLRKLDRKATLAFAFSHRSYLDGMLLPEAILANRLSPALTFGGANLNFFPMGAWAKRTGAIFIRRQTKDIPVYRFVLRAYAAQLVQNHVNLTWSIEGGRTRTGKLRPPVFGILRYITDAVDEIDGPEVYLVPTSIVYDQLHEVEAMTTEAYGAVKRPEDLRFLVRLARQQGERLGRAYLDFGEPLPLRKRLQEMRADKSGTGSEIERIALDVEH... | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69224
Sequence Length: 621
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Subcellular Location: Cell membrane
|
Q88MQ0 | MTRSPLHRLIFGGLRRLLYLWVRSETINQSSMTLNLDRSRPVFYALPSPALTDLAVLDHECTKAGLPRPVLPVAVGPLQEPAAFFYLTPDPDWLGRQDKSGAPPTLERLVAAVSQHAEEDAQIIPVSVFWGQTPASESSPWKLLFADSWAVTGRLRRLLTVLILGRKTRVQFSAPIHLRELVQHNKGHERTVRMAQRLMRVHFRNLKTAVIGPDISHRRTLVKGLVHAPQVRQAIADEAQRENLPLAKAEAQALRYGNEIASDYTYTAIRFLEVVLSWFWNKIYDGIKVNHIEQVQGIAPGHEVIYVPCHRSHIDYLLLS... | Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 93693
Sequence Length: 828
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety ... |
Q886Q7 | MTRSPFRRLVFGTLRRLLYLWVRSETINQSSFTLNLDRSRPVFYALQSPSISDLAVIDTECRKAGLPRPVLSVAVGNLIEPSAYFYLTPAPDWLGRQDKRGAPPTLERLVAAVSQNPGEDAQIIPVSVFWGQSPDHESSAWKLLFADSWAVTGRLRRLVSILILGRKTRVQFSAPIHMRELVDQNKGHELTLRMSQRLLRTHFRNLKSAVIGPDVSHRRTVVKGLLDEPLVKQAIIEEAERENITQEKARERALSYGNEIASDYTYSVIRFMEVVLSWFWNKIYDGIKVSHIEGVQEIAPGHEVIYVPCHRSHIDYLLLS... | Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 94878
Sequence Length: 833
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety ... |
Q3IF27 | MRIVNYCLNVLSAGVSRLLVRSKVLPEKPTEQYELNSKNPTFYIVRLNSRFDLAALARVCKRHGLPDPREQQVLGTQRLDRFIGIENPPPLIGDIAKPTNALAQGKQIIDHLLSSGQKDVQVIPVTILWGRAPGKEKPGLSTLITHSLTPSWFRKLFVVLFSGRDNFIRFSQPLDLSLLVDEKADVNELPQKLLRVARVHFRRQKLAATGPKMPSREQLFNSLLASPTIKKAIQDEAKAKNISQAQARQNAVKLLNEIAANYSEAMIRVAERFLTWLWNKLYNGIDIKYTEQIHELTNKGHEIIYMPCHRSHMDYLLLTY... | Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 92076
Sequence Length: 812
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety ... |
Q49427 | MAFRFAVDCLGFENKPSEAIEAVLKYWSFHQDLNFILIGDEKAFDGLDILPKNITKKLANSFIEMTDTPLSARRKVNSSMQIAINLVREGNADVVISAGSSAVYASLTNDAFGKINKNTKSAFMSYVPTDNNNWFYFLDVGANKYFTGKELYFLGLMADIFVKKTTTKKTPKIGLLNIGTEENKGFDYHQEAFKLLKADKNLNFLGFVESRFLLDGICDILIADGYSGNLVLKAMEGTFKTIARILKRGYKRNPLAGLFSLGIIKSVAKKFDYKNNAGAVVMGLNKLALKTHGSADKQQFLSTIRLAHLSLKSDLINAIK... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36502
Sequence Length: 328... |
Q98R48 | MKTIAFDVMGNDFGPQAAVQASLEFVQKNPDFQIILVGDKKEIEKFTKETSQIKILESPNIASSKDGLRQVSKMENSMNSALDLVVEKKADAVLSSGDSGAYLTSALLKVKRLKGILRPAFMPIFPTIVKDKKILVLDVGANLETKVEYLIQWTKLASIFSNKILKVKNPKCALVNIGVEDYKGFDFHKQANEELKQSNANYIGFLEPRNILDGKVDVAVVDGYGGNLILKSMEGAVLALKKVIKESITKTFFRKILALFLKKAFKDAAERLDYRNVGAAWVLGLNGIVVKSHGSNDFKAYLGALEQVKQGINAKVIDVF... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 35918
Sequence Length: 325... |
Q1D339 | MRLVLDAMGGDHAPAAPVEGGVLFARAHPGHEVLLVGDEAKVAPLLGKLRPPSNLQVHHASEVVEMDEHASTAFRRKRDSSLRVGFELVRDGRAEALVSAGNSGAVMAGGLLTLGRLPGVERPAIAALFPALKGGGRCLLLDAGANVDCKPTHLAQFAVMGEAYVRARMGVARPRVAVLSNGEESSKGTPLTREASGLLRRSDLDFVGYVEGKDLFSGEVQVVVTDGFTGNVVLKTSEGVGMGVIGMLRQAIERRGGLAEKVGAMLLQPALAGLRRVVDYAEYGGAPLLGIQGVGIVAHGRSTPRALFNALGAALAMAEG... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36631
Sequence Length: 353... |
Q9JXR8 | MITLAVDAMGGDQGLAVTVPGATAFLQAHPDVRLIMTGDETQLRQALTAAGAPMERIDICHTTQVVGMDEAPQSALKNKKDSSMRVAINQVKEGKAQAAVSAGNTGALMATARFVLKTIPGIERPAIAKFLPSDTDHVTLALDLGANVDCTSEQLAQFAVIGSELVHALHPQKGQPRVGLVNVGTEDIKGTDTVKQTYKLLQNSKLNFIGNIESNGILYGEADVVVADGFVGNVMLKTIEGAVKFMSGAIRREFQSNLFNKLAAVAALPALKGLKNKLDPRKFNGAILLGLRGIVIKSHGGTDETGFRYALEEAYHEAKS... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37006
Sequence Length: 351... |
Q2GDD6 | MDQVGRKVVVALDTMGGDRAPDEILLGASVYLRQNPSSVFFRLFGNSSSIERCLSSKANVHLLESCEIIHAGDVVMSDDKLSSAVRKKGSSMYKAVQDVREKASQCVVSAGNTGAFMGISKILLGMLENIYRPAIVTTLPTKKGEVVVLDLGANLDCSSDVLYQFAFMGSAFAKAALGVKNPRVALLNVGVEENKGTDAVKEAFHLLNERTDEDFTFIGYAEPSDVLGGEVDVVVSDGFTGNVMLKTAESIFRLLRDDIVGATRTSLLSRLAGLVLAKSLKKSISRFNPDLRNGAMLIGVNGVAVKAHGGSDSVAFANAI... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36395
Sequence Length: 343... |
Q2YA47 | MTITVAVDCMGGDHGPHVTVPATVSYLQSNPAIDVVLVGLPDVIESELRALGYTQSPRLRIHAASEVVGMDESPATALRGKKNSSMRVALNLVKSGEAQACVSAGNTGALLATSRFVLKTLPGIDRPALAVVLPTMRGHTYVLDLGANVDCTAEHLLQFGVMGATLVSSIENKEKPSIGLLNIGEEEIKGNDVVKRAAELLRDSGLNFYGNIEGNDIYKGTTDVVVCDGFVGNVALKTSEGVAQMLSHYLREEFRRNLLTKLAGLIALPVISAFKRRVDHRRYNGASLLGLRGIVIKSHGSADRRAFGFAIARAVDEVRG... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37879
Sequence Length: 353... |
Q2JJA1 | MRIAVDAMGGDYAPEEIIKGALLAHRQLRVGIALVGRPDSLKPFLPQPLPAGITIVPAEEDVGMAEEPLMVRKKPKASINISMQQVRSNQADAVVAAGNTGAAMAAAYLNLGRLAGIDRPAIGALLPTLKGKPVLLLDVGANVDCRPRFLEQFARMGSLYCQCVLGIEKPRVGLLNIGEEPNKGNDLALATHQRLAQLPGIHFAGNAEGRDVLTGEFDVVVCDGFVGNALLKFAESVGQVITQVLREELPRGWRGKLGCWLLRPNLKQVKRRMDYVEYGGALLLGVNGICVITHGSSKAPMVYHAIRLAKEAAEQKILQR... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 40412
Sequence Length: 374... |
Q0AYW2 | MRIAVDAMGGDYAPLEIVAGAVKWVAEEEERQIFLVGQEELLKQELKSYSYDPSRLIVVNASEVITMEESPATAIRRKKDASIVVASRMVKEKKADAIISCGSTGAQMAAAIFILGRMEGIERPPIVASIPNMTGAYTLLIDVGANVDCKPRQLLQFALLGKTYASIIYGVEQPRVALLNNGEEESKGNTVTMETYALLRQQSGINFTGNVEGRDIFTGKSDVIVCDGFTGNVLLKTMEGMALFIAQGILGAGGPMPAFFQRLDYTQTGGAPLLGINGLSIVCHGSSKREAVYNGLRIAEDCYNKNIIEMQQLELSKISG | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 34553
Sequence Length: 320... |
Q47TA8 | MSSPVTAQRPPAAPPLIAVDAMGGDHAPREIVAGAVRAVREHGLRLALVGRSSELAPLVAAEQAARELPIVHAEEALAMHEGALAAWRRARSSVAVGCKLVRQGTAAALVSAGSTGGVVSTATVRLRTLPGVLRPALALVLPTTPTPTILLDAGANADAKPEMLVQFAHLGAAYARVGHGIAEPRVGILTIGSEPGKGNKLARRAAELLSANATEDRLDFRGNIEGHDLLAGLVDVVVTDGFTGNVALKSVEGAVRFAFDEIRAALTSSPLARFGTLFQRRALRELRTRFDSETYGGAVLLGLNGTVVIAHGASRAEGIA... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37479
Sequence Length: 360... |
Q9WXZ6 | MKIAIDVMGGDRAPDEILKGALLASKEVEGEIVLIGPEEIVKNKGLPFVSASEIVKMDDPPLEVLRKKNSSMHMGLKLLSEGKVDAFVSAGATGPLFLGATSIVGKLEGIERPALGVAVPSLKGATVLIDAGANAKVRPEHLVDFAFMGIAYSKVLGAENPRVGLLNMGSEENKGPDDIKRAYQLLKEFLGDTFFGNVEGHDINLGTVDVVVADGFSGNVALKTMEGTAKLVTSVLKESIKDGGFLSLLGALLMKRSFDKMKEKLDPRSYGGTFILGVKGIVVKAHGSSDAKAIKHAIKVAEKGIRVNIVQEIERGISHV... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 34609
Sequence Length: 327... |
O65984 | MRIAVDAMGGDYAPLEITKGVYKALENFNIEIVLVGNKDQLDKYVKEEKGLTVVHTTETITNNEPPVAAIRKKKDSSMAVGIDMLKKGEVDAFLSAGNTGALMAGSLLKIGRIKGIDRPALAPILPTLNGATILLDAGSNTDCKPINLFQFAIMGNVYAQKMLNIDNPKIGLFNIGAEEEKGNELTKQVYDLIKNSHLNFIGNVEGRDIAYGVADVVTCDGFVGNAILKSMEGTASVISSLLKQELQRNLLTKLGAILIYNGLKNIVKKMDYTEYGGAPLLGIKKPVIKAHGSSKSKAIFNAIRQAKTIVEMDVISHIQR... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 35929
Sequence Length: 333... |
B5YG77 | MLKIAVDAMGGDFAPEVNILGAYEVVQDIEVEIILVGDEKKIKSFLPEKKETKGIISVIPADDVIQMDENISSALRRKNTSMRKAVELVKAGKADAVISAGHSGAMMALSFLLLGKLPNVERPAIATVMPCLKGHFILLDAGANVDCKPEHLVQFAFMGEAYHKALFNSQSPKIALLSIGEEGSKGNELTKEAFKLLKSSRLNFVGNIEGKDIFFGQADVVVCDGFVGNIVLKVGEGLAEALMKMLKREIADIITGKLGYMMIKPAIKSFRKKVDYSEYGGALLLGINGTSIICHGRSSAKAIKNAIKVATEMVKKQIYT... | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37451
Sequence Length: 345... |
B1I461 | MSALAVILVIGLSYLVGSVPTGYLIARHVKGIDIRGHGSGNIGATNVWRTLGPGWGLASLVGDTAKGIVAVLLGRAVGVPGLELLTGAAALTGHGWSVFLRFQGGKIIATSLGVLIMLPPVALATAAAVWIAVLALTRYVSLASIIAASSVPLAFALGGVGWRHVLFGLFLALVAVYKHRANIDRLLKGKESRFSFRK | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
B8J229 | MLEILWIALAYVLGSAPWGLVIARTFCGIDPRESGSRNTGATNVARLCGFGWGVATLLCDVLKGAVPVWLAFRINASPVFVSMVALACVLGHVFSCFMKFRGGKAVATSIGIFLPLAFWQLLASSLLCMLVIWRSGFVSLGSLTLVTALPVALAVSGQWGWLPLSLAVWAVVVWKHRENIVRLRSGTEKSWLKSKNKGAAAGNAAEGDDTQNMNPQDAGRKDG | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
Q6AQV6 | MDFIFPLISYLLGAIPFGLLIGKLAGRDVRLEGSKNIGATNVSRILGKKLGFATLLCDSLKGFLPMVLAATLLPSSENRELIVCLSGVMGVLGHMFPVYLGFKGGKGVATGLGVFLFLSPAAIAISLGVFAASVFFSGFVSVGSLLASGLIPLWLYLLGASQLKIITAGFVALLIWIKHRKNIKRLMTGTEKSWKKK | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
A4J3P2 | MVHITTVMIIIGAYLIGSIPFGFLLAYFWKGIDIRKCGSGNIGATNVWRTLGKVPGMIVLILDMIKGISAVLLAKQLENTDIAVLGVALAVMAGHSWPLWLRFKGGKIIATGAGAILALSPMPLLLAFLVWLTTVVVSRYVSLGSILGAVSLPIWMALLNQNRHYLIFSVLVASFAVWKHSSNIGRLIKGTEFKIGQKKT | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
Q726E5 | MGSLLWLAVAYVMGSIPFGLLFAKMFCGTDPRTGGSRNVGATNVARLCGTKVGVLTLVCDALKGAIPVAVALSISDSTVFHSLTALAALLGHLYSCFLSFKGGKAVATTVGVFLPLAFWPLVLSGIACLAVIWRSGFVSLGSLTLVTAMPAMLLLGGHWKLVPLALVVMVLVYWSHRENIGRLSRGEEKPWQKKHHDAAQGTDAGAAPEAAADAAHAGTVDCGCDCGCDAHKPSTEAAPSQETSDASAHGAEAPVAADEGDKRENEEHDNAPEASAAESKPEDKPAGKTVGKPASRSVAKPASKSAGKTGGKAADKSAGK... | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
Q2RPF8 | MADLSTLMPALVLGVCALAGYLLGSVPFGLVLVRLAGLGDVRGIGSGNIGATNVLRTGRKDLALATLVLDSGKGAIAALVASALASRIAGFEDAVLAGLLAGGMAVVGHNFPIWLGFKGGKGVATTLGTLLATAWPVGLAACATWLVVAALFRYSSLAALVCLALAPAYALVLATPAHAAVFALLALLAWIRHRANIARLLKGEESRIGAKKKAAP | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
A5UZW0 | MMPTIASIALVLLAYLSGSIPFSLLVARAWGVDLRVSGSGNVGAANVWRTCGFSAFALAMGGDMLKGALPTIAAQALGLSPLAVVIVGTAAMLGHTRSIFLGFRGGKAVATGGGVVLTLAPLVALPGLAAWAVTFGITRISAVASLTAAAVCGIAAAVLLALGMLPPAYAIFVWGAVAAIVFLHRSNIHRLRTGTENRFEKLF | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
Q1AU71 | MLEVLLVLLGYVLGSVPTGILVGRAYGVDVRKVGSGNIGTANVMRAAGKGAAALTMLGDMLKGVAPVLLARALGAGPWVLAAVALAAVVGHCWPVFLRFRGGKGVATGAGTSIALAPPVGLGMFALWWVVALASRYTSLAAMVVTVVSPFAFLLSGQPLPYVLYTVVGGAAVLWRHRENARALLRGTERKFGGRSGGGG | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
Q5LX62 | MPAFDTPAMMLILWAVIGYGLGSIPFGLILTRAMGMGDLRQIGSGNIGTTNVLRTGNKGAAALTLLLDGGKGAVAVLLARAFAGEDAAQVAALAAFVGHCYPIWLGFKGGKGVATFLGLWLALAWPVGVACCLSWLAGAAVTRISSMGALVAAASSTFWLVLLDQGAGFVLGIVLTLMVFWRHRANIARLKARTEPKIGQKSA | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
A1AXL0 | MLPELLFIVLLLLSYLIGSISTAIIVCKMFNLPDSRTQGSNNPGATNVLRIGGKKAAAITLIGDGLKGAIPVLIAHYLAFNMLNVTWVILVTFLGHVYPIFFSFKGGKGVATFLGALLALSYLTGLSFIITWVFVAKVLKISSLSALISTVLTPVYFYLITNNLASTYVIILICLWIFYTHQSNIKRLLNSQENKIN | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
Q9LJ42 | MVIFSRSFLALSTTLIILALCINSSTMAQETEDLNSHSSSNSSTANKLPNDDGAWNEHAVKNPEEVAAMVDMKIKNSTERRRLGFFSCATGNPIDDCWRCDRNWHLRRKRLANCAIGFGRNAIGGRDGRYYVVTDPSDHDAVNPRPGTLRHAVIQDRPLWIVFKRDMVITLTQELIMNSFKTIDGRGVNVAIAGGACITIQYVTNIIIHGINVHDCRRTGNAMVRSSPSHYGWRTMADGDAISIFGSSHIWIDHNSLSNCADGLIDAIMGSTAITISNNYMTHHNEVMLMGHSDSYTRDKLMQVTIAYNHFGEGLIQRMP... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 48761
Sequence Length: 440
Pathway: Glycan metabolism; pectin degradat... |
Q9LTZ0 | MVSYSNNHFAYAFLLLLTIGNTLAFSSSLPDHVQDPNLVVDDVNRSVFNASRRSLAYLSCRTGNPIDDCWRCDPNWETNRQRLADCAIGFGKNAIGGRKGRIYVVTDPANDDPVNPRPGTLRYAVTQEEPLWIIFKRDMVIRLKKELIITSFKTIDGRGSSVHITDGPCLKIHYATNIIIHGINIHDCKPGSGGMIKDGPHHTGWWMQSDGDAVAIFGGKHVWIDHCSLSNCDDGLIDAIHGSTAITISNNHMTHHDKVMLLGHSDSYTQDKNMQVTIAFNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSASP... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 45985
Sequence Length: 412
Pathway: Glycan metabolism; pectin degradat... |
Q9SCP2 | MMLQRSCIVLFFSLFLLVPQMVFSMLNRTLLLIPHPDPELVAYQVQWKVNASITRRQALDTTDQAGSTPCITGNPIDDCWKCDPNWPNNRQGLADCGIGFGQYALGGKGGQFYFVTDSSDDDAVNPKPGTLRYGVIQEEPLWIVFPSNMMIKLKQELIFNSYKTLDGRGANVHIVGGGCITLQYVSNIIIHNIHIHHCYQSGNTNVRSSPTHYGFRTKSDGDGISIFGSKDIWIDHCSLSRCKDGLIDAVMGSTGITISNNFFSHHNEVMLLGHSDHYEPDSGMQVTIAFNHFGEKLIQRMPRCRRGYIHVVNNDFTQWE... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 53593
Sequence Length: 483
Pathway: Glycan metabolism; pectin degradat... |
Q93Z04 | MLLQNFSNTIFLLCLFFTLLSATKPLNLTLPHQHPSPDSVALHVIRSVNESLARRQLSSPSSSSSSSSSSSSSSCRTGNPIDDCWRCSDADWSTNRQRLADCSIGFGHGTLGGKNGKIYVVTDSSDNNPTNPTPGTLRYGVIQEEPLWIVFSSNMLIRLKQELIINSYKTLDGRGSAVHITGNGCLTLQYVQHIIIHNLHIYDCKPSAGFEKRGRSDGDGISIFGSQKIWVDHCSMSHCTDGLIDAVMGSTAITISNNYFTHHDEVMLLGHDDNYAPDTGMQVTIAFNHFGQGLVQRMPRCRRGYIHVVNNDFTEWKMYA... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Function: Susceptibility factor required for infection by most powdery mildews, but not by unrelated pathogens. Exact function not known, but clearly affects cell wall composition.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give ol... |
Q9SVQ6 | MVVARTLFSISATLIIFLALFLHVNAVQETREPKHESSRNTSTVDNLSDGEWHEHAVKDPEEIAAMVDMSIRNSTYRRKLGFFSSCSTGNPIDDCWRCDKKWHRRRKRLADCAIGFGRNAVGGRDGRYYIVTDPSDHDPVTPKPGTLRYAVIQDEPLWIVFKRDMVITLSQELIMNSFKTIDGRGVNVHIAGGACLTVQYVTNIIIHGINIHDCKRTGNAMVRSSESHYGWRTMADGDGISIFGSSHIWIDHNSLSSCADGLIDAIMGSTAITISNNYLTHHNEAILLGHTDSYTRDKMMQVTIAYNHFGEGLIQRMPRC... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 48548
Sequence Length: 438
Pathway: Glycan metabolism; pectin degradat... |
Q944R1 | MASSSQKLISVCVAVLVVLALTAMIFRNSEISLSRKLKTEVIQSSNSSTMAAIRKLKTEEFQSLNSSTMAATRLDGEPQQQQHAVADDPDMVADEVAKLVQMSEQNRTARRKLGFFSCGTGNPIDDCWRCDRNWHKNRKRLADCGIGFGRNAIGGRDGRFYIVTDPTDEDVVNPKPGTLRHAVIQEEPLWIVFKRDMVIELKQELIMNSFKTIDARGSNVHIANGACITIQFITNVIIHGLHIHDCKPTGNAMVRSSPSHFGWRTMADGDAVSIFGSSHIWIDHNSLSHCADGLVDAVMGSTAITVSNNHFTHHNEVMLL... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 51936
Sequence Length: 470
Pathway: Glycan metabolism; pectin degradat... |
O65456 | MTLFTVSCLLVVLFLCHSLVHAENNGYYGYTPTVANYLPEKPQNIMNPVDSCWRLKSDWAANRKDLADCVVGFGSSTLGGKKGNLYVVTNPYDNAQNPQPGSLRYGVIQAKPLWITFAKDMVITLENELMVNSYKTIDGRGAKVEIAYGPCITIQDVTNVIVHGISIHDCKPGKYGMVRSSPTHVGHRKGSDGDAIAIFGSSNIWIDHCYLASCTDGLIDVIHASTGITISNNYFTQHDKVMLLGHNDDFVQDVKMKVTVAFNHFGPGLVERMPRVRRGYAHVANNRYDKWIMYAIGGSADPTIFSEGNYFIASDKSNSK... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 43476
Sequence Length: 394
Pathway: Glycan metabolism; pectin degradat... |
Q9C5M8 | MKMQTKKLFITIVSFLLYAPLFLSSPVPDPESVVEEVHKSINASVAGRRKLGYLSCTTGNPIDDCWRCDPHWEQHRQRLADCAIGFGKNAIGGRDGRIYVVTDSGNDNPVSPKPGTLRHAVVQDEPLWIIFQRDMTIQLKEELIMNSFKTIDGRGASVHISGGPCITIQYVTNIIIHGIHIHDCKQGGNAMVRSSPRHFGWRTISDGDGVSIFGGSHVWVDHCSFSNCEDGLIDAIMGSTAITLSNNHMTHHDKVMLLGHSDTYSRDKNMQVTIAFNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINS... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 45014
Sequence Length: 408
Pathway: Glycan metabolism; pectin degradat... |
P24396 | MSTLFFTFSLLLLAPLLVISSIQDPELVVQDVHRSINASLTRRNLGYLSCGSGNPIDRLLAMQPQLGKKSPAFSYCAIGFGKNAIGGKNGRIYVVTDSGNDDPVNPKPGTLRHAVIQDEPLWIIFKRDMVIQLKQELVMNSYKTIDGRGASVHISGGPCITIHHTSNIIIHGINIHDCKQSGNGNIRDSPNHSGWWDVSDGDGISIFGGKNIWVDHCSLSNCHDGLIDAIHGSTAITISNNYFTHHDKVMLLGHSDSFTQDKGMQVTVAFNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSAAPTINSQGNRFL... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Function: May have a role in the development of the transmitting tissue of the style and/or in the events related to pollination such as some aspect in the facilitation of compatible pollen tube growth.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-g... |
P17872 | MVKSILASVLFAATALAASRMTAPSGAIVVAKSGGDYDTISAAVDALSTTSTETQTIFIEEGSYDEQVYIPALSGKLIVYGQTEDTTTYTSNLVNITHAIALADVDNDDETATLRNYAEGSAIYNLNIANTCGQACHQALAVSAYASEQGYYACQFTGYQDTLLAETGYQVYAGTYIEGAVDFIFGQHARAWFHECDIRVLEGPSSASITANGRSSESDDSYYVIHKSTVAAADGNDVSSGTYYLGRPWSQYARVCFQKTSMTDVINHLGWTEWSTSTPNTENVTFVEYGNTGTGAEGPRANFSSELTEPITISWLLGSD... | Function: Involved in maceration and soft-rotting of plant tissue.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 35715
Sequence Length: 331
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-glu... |
P86085 | IDAFQDTLYTHTLRTYLGRPWK | Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 2696
Sequence Length: 22
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.... |
Q42920 | MEICNEVLDYAVDGIHKSVGTLDQFDFHKLSEYAFDLKVWLTGTLSHQQTCLDGFANTTTKAGETMTKVLKTSMELSSNAIDMMDAVSRILKGFDTSQYSVSRRLLSDDGIPSWVNDGHRRLLAGGNVQPNAVVAQDGSGQFKTLTDALKTVPPKNAVPFVIHVKAGVYKETVNVAKEMNYVTVIGDGPTKTKFTGSLNYADGINTYNTATFGVNGANFMAKDIGFENTAGTGKHQAVALRVTADQAIFYNCQMDGFQDTLYVQSQRQFYRDCSISGTIDFVFGERFGVFQNCKLVCRLPAKGQQCLVTAGGREKQNSAS... | Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 49133
Sequence Length: 447
Pathway: Glycan metabolism; pectin degrad... |
Q43043 | MVKLLNSTRELSINALSMLNSFGDMVAQATGLNRKLLTTDSSDATARRLLQISNAKPNATVALDGSGQYKTIKEALDAVPKKNTEPFIIFIKAGVYKEYIDIPKSMTNVVLIGEGPTKTKITGNKSVKDGPSTFHTTTVGVNGANFVAKNIGFENTAGPEKEQAVALRVSADKAIIYNCQIDGYQDTLYVHTYRQFYRDCTITGTVDFIFGNGEAVLQNCKVIVRKPAQNQSCMVTAQGRTEPIQKGAIVLQNCEIKPDTDYFSLSPPSKTYLGRPWKEYSRTIIMQSYIDKFIEPEGWAPWNITNFGRDTSYYAEYQNR... | Function: May play a role in pollen germination and/or tube growth.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 41467
Sequence Length: 374
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gl... |
Q43062 | MPYLLMASHNPLPAGKQLLLLVLLCAFFSSSFIPFASCSITDDLQTQCLKVSATEFAGSLKDTIDAVQQVASILSQFANAFGDFRLANAISDCLDLLDFSADELNWSLSASQNQKGKNNSTGKLSSDLRTWLSAALVNQDTCSNGFEGTNSIVQGLISAGLGQVTSLVQELLTQVHPNSNQQGPNGQIPSWVKTKDRKLLQADGVSVDAIVAQDGTGNFTNVTDAVLAAPDYSMRRYVIYIKRGTYKENVEIKKKKWNLMMIGDGMDATIISGNRSFVDGWTTFRSATFAVSGRGFIARDITFENTAGPEKHQAVALRSD... | Function: May have roles in the deposition of pectin in developing tissues and in the wall loosening and cell separation that occurs in cell expansion, fruit ripening and abscission.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Se... |
P24791 | MQSTTLYLKTAAFLGGCSLFAATALAATSTATRPQLSNADARAYTIASYMASFGTIGSLTTDNWDPTGGVGAVSGFRANYAVAADGSAQYKTVQAAIDAAVADGGVARKYISVKAGTYNELVCVPESAPPITLYSLDANANNTVIVYNNANPTPASGAKTNPCMGTSSNATVGTVRSATAMVRASNFNARNLTFKNSYVEGTFADNNQSAVALAVRGDKAILENVSVIGNQDTLYLGATNNTMVIRAYFKNSFIQGDTDFIFGAGTAVFHGCTIQYTAARLGARATSYVFAPSTAPDNPHGFLAINSTFNATGNASNNST... | Function: Involved in maceration and soft-rotting of plant tissue.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 41016
Sequence Length: 396
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-glu... |
E7CIP7 | MKIIVLLLLAVVLASADQTAPGTASRPILTASESNYFTTATYLQGWSPPSISTSKADYTVGNGYNTIQAAVNAAINTGGTTRKYIKINAGTYQEVVYIPNTKVPLTIYGGGSSPSDTLITLNMPAQTTPSAYKSLVGSLFNSADPAYSMYNSCASKSGTIGTSCSTVFWVKAPAVQIVNLSIENSAKNTGDQQAVALQTNSDQIQIHNARLLGHQDTLYAGSGSSSVERSYYTNTYIEGDIDFVFGGGSAIFESCTFYVKADRRSDTAVVFAPDTDPHKMYGYFVYKSTITGDSAWSSSKKAYLGRAWDSGVSSSSAYVP... | Function: Pectinesterase which probably plays an important role in the digestion of plant cell walls.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 40697
Sequence Length: 382
Pathway: Glycan metabolism; pectin d... |
P53514 | MLIPYSPHTIWKTICATLLLSLAFFSQAEQDDSVEFNIHMLDAEDRDNVDLSRFSTSNYIIPGMYYLDIRLNGRDFPRQNINYIEVADNHSVACIDPTLLKKLTINQENQKYIKQISPDCFDISQLPGISIKNDGGVLDITLPRSLMKYEESDWTPPELWDSGVSGLIFDYTLTGTSTRPNKGNNNNTLTGYGQAGLNLGEWRLRAEYQGNYSSEYSSNNRFDWNQIYAYKPLPDLAAKLTVGETYLNSQIFDSFRFTGANLQSDERMLPPSLQGYAPEIHGIANTNAKVTVTQNGRLIYETTVPAGPFVINHLQNTVQG... | Function: Involved in the export and assembly of PMF fimbrial subunits across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93108
Sequence Length: 828
Subcellular Location: Cell outer membrane
|
O74837 | MSNVTLSDFLLIVLSFFVPFIVVGIRRGFCTADFLINICLCALGIPGIIHAIYIVIKYPRTVRLDIENSPNDPLVRYTPNPEHAVSPHSGPAPPSYSSLASNDNKHQSP | Function: Has a role in meiosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11962
Sequence Length: 109
Subcellular Location: Vacuole membrane
|
Q9P824 | MNSEKIIEVIIAIFLPPVAVFMKCGATTPLWINLVLCIFIWFPAILHALYVVLKD | Function: Plays a role in the regulation of membrane potential.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6230
Sequence Length: 55
Subcellular Location: Membrane
|
Q2HAR0 | MPFTASDICKIIFAVILPPLGVFLERGCNSDLLINILLTILGVGSILASMNPA | Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5587
Sequence Length: 53
Subcellular Location: Cell membrane
|
P0CS19 | MAFTCSDIFKIILAIILPPLGVFLERGCGADLLINILLTILGYIPGIIHALYIILKY | Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6275
Sequence Length: 57
Subcellular Location: Cell membrane
|
Q6BVN0 | MAFTCSDIFKIIIAIILPPLGVFLERGCASSFWINIVLTILGYIPGIIHALYVILKY | Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6356
Sequence Length: 57
Subcellular Location: Cell membrane
|
Q9C1W4 | MALTGSDIFKVIFAIILPPLGVFLERGCGADVIINILLCCLGYVPGIIHALYIILKY | Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak. Regulated by the spc1-atf1 pathway and so expression is stress-induced.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6179
Sequence Length: 57
Subcellular Location: Cell membrane
|
P87284 | MDSAKIINIILSLFLPPVAVFLARGWGTDCIVDIILTILAWFPGMLYALYIVLQD | Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6138
Sequence Length: 55
Subcellular Location: Cell membrane
|
Q89SS3 | MTVTDIASRTYNHSWRLDPIIRSLLDTDFYKLLMLQMIREDYSNQQVTFSVINRSRHVRLAEIIDEGELRAQLDHARTIRFTKKELIWLAGNTFYGKTHMFSADFIRWLAEFRLPEYELRKVEGQYELHFHGPWTHTTMWEIPALAILNELRSRAAIKGRGRFELDVLYARAKAKLWTKVERLRKLENLRLSDFGTRRRHGFLWQRWCVEAVKEGLGPSFIGTSNVLLAMDNDLEAIGTNAHELPMVAAGLAKDDEELRWAPYRILDQWRQTYGGNLLIALPDAFGTKAFLRDAPEWVADWTGFRPDSAPPIQAGEEIIA... | Function: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate ... |
Q55G10 | MSQSNTPLKRKKTENGYSENGSTTGATSNQIRELKRATTVDYVYRDQESKDKIKPLNGFVTPLLTDLYQITMAYSLWKNNRHEIPAVFDLYFRKSPFGGEFTVFAGLEEVIRFVSDFHYTKEEVGFIKEMIPDCEQEFLDYLSKLDSSSVTLYAMKEGSVVFPRVPLLRVEGPMILCQLFETTLLCLVNFASLVATNAARHRLAVGKEKVMLEFGLRRAQGPDGAMSASRYSYLGGADGTSNVLAHCFFGIPIRGTHAHSFITNYSGPDELLDASIKDTNGNVHNLLEMSQKYRDELGYTATNLSELVAFVAYARTFPNG... | Cofactor: Activity is highest with Mn(2+).
Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis.
PTM:... |
Q9VQX4 | MNDRELGCAGGQFMDRGRMNQNGVVQPLLTDLYQITMAYAYWKSDKTDDTAVFDLFFRNNPFHGEFTIFAGLEECLKFLDSFHYSQSDIEYLKQTLPEGIEHEFFEYLGNLTARDVTLYAIDEGTVAFPRVPIIKIEGPLIIVQLLETTLLTLVNYASLMATNAARYRMVAGKHVKLLEFGLRRAQGPDGGLSASKYSYTGGFDGTSNVLAGKLFNIPVKGTHAHAYITSFSSIGELKTRLIKHKQTGILEDLLEHAVRHRALLSHLLDVSTEESSEGELAAMVSYAIAFPDGFMALVDTYDVKRSGLLNFSAVALALND... | Cofactor: Activity is highest with Mn(2+).
Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis.
PTM:... |
P10938 | MSGTDRSQAAGAVPDSDPGLAAVSSAYQRFEPRAYLRNNYAPPRGDLSCPDGVGPWKLRCLAQTFATGEVSGRTLIDIGSGPTIYQLLSACAHFEDITMTDFLEVNRQELRLWLREEPGAFDWSVYSQHVCLIEGKGESWQEKECQLRARVKRILPIDVHRPQPLGAGGLAPLPADALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLAVVPVREEEVREALVRTATRCGICARTPMPAHLQTGVDDVKGIFFTRAQKKVGV | Function: Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-methionine as the methyl donor . Other substrates include phenylethanolamine and octopamine (By similarity). Also methylates normetanephrine .
PTM: The N-terminus is blocked.
Catalytic Activit... |
P10937 | MDRGSDPKHTAGMDSDSDPGQAEVALAYQRFEPRAYLRNNYAPPRGDLSNPDGVGPWKLRCMAQVFATGEVSGQVLIDIGSGPTIYQLLSACAHFEDITMTDFLEVNRQELGLWLREEPGAFDWSVYSQHVCLIEDKGESWQEKERQLRARVKRVLPIDVHKPQPLGASGLAPLPADALVSAFCLEAVSPDLPSFRQALYHITTLLRPGGNLLFIGALEESWYLAGEARLSVVPVSEEEVREALVCSGYEVRDLRTYIMPAHLRTGVDDVKGIFFAWAQKIEVQV | Function: Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-methionine as the methyl donor (By similarity). Other substrates include phenylethanolamine, octopamine and normetanephrine .
Catalytic Activity: phenylethanolamine + S-adenosyl-L-methionine =... |
A1R0N0 | MRKILKLKVGREDLILETGLLAKQANGAVLATYGGSTVLATVCCSDSARENLDFVPLSVEYNEKYYAAGKIPGGFIKREGKPKDKEVLVSRLIDRPMRPLFDKRFGREIQVVPTTLSTDQMNPPDIVGMNAAFAAVFLSDIPFNGPIAAVRIAYLNSEFIVNPSFDEIQDSILDIVVAGSLDGITMVEGGANEVSEEVLLAAIDQAYEYIKQICNLQKEFILIVGEREKLPLAYEERVFEFKAELKDFIYSELKDACFVKGKLNRDKAIKLVKQKAYEHFSSVSQVDEENETLFYKALDDFEQEIVRRSILENNLRTDGR... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 80046
Sequence Length: 717
Subcellular Location: Cytoplasm
EC: 2.7.... |
C0R0E0 | MVTVKSVFCGEELILETGLLAKQAHGSVTLRLGNTTILATVVAAKEPNLESDFFPLTVNYNEKYYAGGKIPGGFFKREAKPRDKEILISRIIDRPLRPLFPEGFRNEVQIIPTVLSVDTDMPTDALALIASSAALTISWIPFGGPVAAVRIGYKNGEYIINPKNSELSTSELDIIVAGSKDAILMIEGEAKEVSEEVFIGAIELAHKEMQKYIDMQNEMASLCGTQKIEQELFEFDADLVKMVTEYGRDKIESANYNPDKTKRNESMDNAFNEIEEYIKTKVEDEKLISQVKGICHSIEEEIVREAIVEKCMRPDGRALD... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 78604
Sequence Length: 712
Subcellular Location: Cytoplasm
EC: 2.7.... |
C4L6J6 | MLGTKQVFSTEWGGRPLSVEVGQLAKQANGSALVRYGDTVVLATVTASKAPKDLDFFPLTVNYEEKLYSVGKIPGGFLRREGRPGENAILTSRLIDRPIRPLFPDGFRHDIQVMIYVMSNDPDCSAEMAGMLGTSIALSISDVPFDGPIAGVTVGRVDGEFVINPTTAQLEKTDLELQVAGTSTAINMVEAGANEVPEDVMLESILFGHEEIKRLIAFQQEIVEAVGKPKFEYTVSKYDEALTAELEAARPEIVEAVQVEEKHARDEAINEVIAKYVAMYEARLADEPSKLGEVSGILNKFVKDEVRRLITVEKVRPDGR... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 80709
Sequence Length: 738
Subcellular Location: Cytoplasm
EC: 2.7.... |
B0S1D9 | MIKKYEYDLCGKKIEVTIGKVAEQANGACLIQSGETVLLVTAVGSKEPREGVDFFPLTCDFEEKLYSVGKIPGGFIKREGRPSEKATLTARLIDRPLRPLFPEGYHNDVQVIATALSVDQDNTPDILAMIGSSIALSISDIPFLGPTGSVAVGMIDGEFIINPTKEQREKSDLELTVAGTKDAIMMVEAGCNNITEQQVLKAILRAHEEIKKICEFIESIQKECGKPKQEFIQPEKNIELDEEVKSFCIEDLKKITVNEDKLDREDHINTLKRSVVDYFVEKYDESIASKVSTIYDDLEKSEVRRLILEDYIRPDNRKLD... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 79341
Sequence Length: 714
Subcellular Location: Cytoplasm
EC: 2.7.... |
A6H185 | MIPQLFVESIDLGDGRNITIETGRLAKQADGSVVVRIGKTVILGTVVSSRKATPGIDFLPLTVDYREKFAAAGRFPGGFFKREARPSDSEVLTMRLVDRVLRPLFPSDYHAEVQVMIQLMSHDEEVMPDALAGLAASAALALSDIPFETLISEARVGRIDGKFIINPSRAQLELSDIDMMIGASTDSIAMVEGEMKEISEAEMLEAIKFAHEHIKVQIAAQERLAAAFGKKEVRTYEKEKSDDAIYAKVKEAAYDKIYNIAKVGSAKQERTAAFDAVKEEVKALFTEEELAENGDLVSKYFYKTNKEAVRNVTLDLGTRL... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 77852
Sequence Length: 711
Subcellular Location: Cytoplasm
EC: 2.7.... |
Q8RIA1 | MKELMFDEKIMELELAGRTLKVSTGKISRQSSGAIVIQYGDTVLLSTANRSKEARKGADFFPLTVDYIEKFYSSGKFPGGFNKREGRPSTNATLVARLIDRPIRPMFPDGFNYDVHIVNTVLSYDEINIPDYLGVIGSSLALMISDIPFLGPVASVIVGYKNGEFILNPSPKELEESELDLIVAGTKEAVNMVEAGAKELDEETMLKAIMFAHENIKKICEFQEEFSKLYGKENIEFEKPEVLTLVKDFIDTNGYERLQQAVLTTGKKNREDAVDSLEEELMEKFIQENYPDVPEEELPEDIILEFKTYYHDLMKKLVRE... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 78262
Sequence Length: 703
Subcellular Location: Cytoplasm
EC: 2.7.... |
B3CTX1 | MFNEILKKVDWHGNMLSLSTGKIARNADGAVLASMGNTSVLCTVVFDKNTKKDIDFFPLGVYYREMAYAAGKIPGGFIKKEGKFSEYEVLVSRLIDRSIRPLFDSNFRNDTQVICTVMSYDPRYSPDILAIIGSSAALAISGIPIVKPIGAARVGIVNDEFILNPVIHDNTGVNELDLVVAATFDSVTMIEAQACEIDEEKMLAAIEFGYKSLKPVINAIEEIKSSIRKDIFEVTARPHLRYNDEILKHFSSDIKSALLLQTKNERNQQLQLIQQKVVDYFSSEANDDDAILNIEKALDDVKSKIFRDLVLQDKTRIGNR... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 81456
Sequence Length: 736
Subcellular Location: Cytoplasm
EC: 2.7.... |
A6LFK9 | MLNPINKTIELGDGRTITIETGKLAKQADGAVTVRMNNTVLLATVCAAKDANPGVDFMPLQVEYKEKYSAFGRFPGGFTKREGKASDYEILTSRLVDRALRPLFPDNYHAEVYVNIILFSADGEDLPDALAGLAASAALAVSDIPFNGPISEVRVARTDGKYIVNPTSAELEKADIDIMVAATIDNIMMVEGEMNEVQESEMLEAIKVAHEAIKVQCKAQLELSEACGKLVKREYCHEVNDDELRKDVHDKCYAKAYAVATSGSGKHERSEAFEKIVEEYKAQFSEEELTDEKLEMIGRYYHDVEKEAMRRAILDEGKRL... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 82019
Sequence Length: 746
Subcellular Location: Cytoplasm
EC: 2.7.... |
Q6MDI2 | MQRETISVPVGAQEIIFETGKIARQAGGAVVVRCGETVVFTTACAAPNADSTTDFLPLRVDYQEKFSSAGKTLGGFIKREGRPTEKEVLVSRLIDRPIRPMFEEGYYNEVQLLSFVWSYDGINSPEPLAICGASAALVISDIPLIKPVGAVRIGFIDAQFIVNPTIEQQKQSKLDLLIAGTEEAVLMIEGFCDFLTEDQVLEAIEIGHRSIKTICQTLEQWRAKVGKPKNRETLRQLPKELYADVESIANPLLEKALRICEKQKREEALAEVTKAVNDRLMPENEEPKYPAKHIAYVIKDVSSKMMRQMILNENVRSDGR... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 76628
Sequence Length: 697
Subcellular Location: Cytoplasm
EC: 2.7.... |
B4SDX4 | MIINKEIDLGQGKIISIETGKMAKQADGAVVVRQGDTMVIATVVSSKKTPPPNQDYFPLQVEYREKYSAAGKFPGGFFKRESRPSEKEILSARLIDRALRPLFPDGYLYETQIIVTVISSDQINDADVLGGLAASCAIMVSDIPFQNPMSEVRVGRINGLFVVNPDINELVNSDLDICIGGTENTICMLEGEMKEISEAEMLDAIKFGHAAIRKLCALQSEIAAEVAKPIRPFTPTVIPAELTETVRVLCETRLKELAYTPLKKEERADQTAAIYHEIIESTIEHFKATCSSEEFSTDPAKALCINPHIIDEQIHMVEKR... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 79422
Sequence Length: 728
Subcellular Location: Cytoplasm
EC: 2.7.... |
A5D2S6 | MADRSILTREIIVGGRPMILETGRLANQASGAVFVRYGDTAVLVTATVAPTVRAGIDFFPLTVDYEERFYAVGKIPGGFIKRESRPSEKAILSGRLIDRPIRPLFPKEMRNEVQVIATILSVDQDNAPEIAAMVGASAALHISEIPLKFPIGGVIVGRVDGRFVINPVLAQAEKSDMHLVVAGTKDAVMMVEAGAKEVPEEVILEAISFGHETVKEIVAFIERYREEALEMGLAKEKMVIEVAEPDPVLVEAVTGPATEKLDGVLRRCVNERLSKQERDSLLNNIKDELMQKFLADYPEQESLIKDLLDSIEKKLVRRMI... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 80315
Sequence Length: 734
Subcellular Location: Cytoplasm
EC: 2.7.... |
Q67P77 | MPPGAPDGPGHRRRTNVTASFSMELGGRTMTLETGRLAKQASGSVLVNYGDSVVLCTAVGSATPREGVDFFPLTVDYEERMYSVGRIPGNWFRREGRPTSKAILWARLTDRPIRPLFPEGFRNDVQVVCTVLSVDPDHPVEIMGMIGASAALTISDIPFEGPIGGVIVGLVDGQFVINPTAEQQERSEMHLVVAGTEHAVLMVEAGAKEVPEQTMLDAILFGHEVIKNTIIPTIKQMQAEVGKPKREVVLFNPPPELEQAVREAATVRLREAVRNPDKLAREEAVAAVGEAVQAELAEQFPESEKHIAYLLKKVLKEEVR... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 82820
Sequence Length: 762
Subcellular Location: Cytoplasm
EC: 2.7.... |
Q2LWT4 | MSTIFSAEFAGRNISIKTGYVAGQADGAVMVIYGDTVVMVTAVSLKTAREGVDFLPLTVDYQEMTYAAGKIPGGFFKREGRPNEREILTSRVIDRSIRPLFPKGYCYETQLVATVLSVDSENDSDVAALLAASAALEISDIPFKGPIVGVRVGRVDGQFICNPSKLEQEKGDLNLYLVGRKVVPGTEGRPYDVNLVMLEGEAQQVEEEHVIAGIDFGLECMRPVIELQDQLRSALGKPKREFEAVEIDDALLAEVSEKAAVRMREAYRMSRKLDRHAALDEIRNSVLKAVTADEAGLRLRTAAALEALEKRIVRDVILKE... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 76711
Sequence Length: 705
Subcellular Location: Cytoplasm
EC: 2.7.... |
A0LHM4 | MKHSVQVEVGGRPMVFEAGEIARQAGGSVLMRYGDTVVLIAATKEDRIREGIDFVPLMVDYQEMSYAAGRIPGGFFRREIGRPSEKETLTSRLIDRPIRPLFPKKYCYETQVVATVLSVDMENEPDVVALTGASTALHISPVPFQGPVAAVRVGRINGSFAINPSAKELLESDLNVVVAGSRDAVVMVEGGADFVSEDDLVDAIDFGHKAILPILDAQDELQRRIAPVKEAPPEVVRNESLVQAVRDAAAAEMRAVMTTPEKHPRRDRKKALKERIQAELVSDDPDRPKQIDNILEDLEKEVVRRMMVEEGRRIDGRRFD... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 76332
Sequence Length: 699
Subcellular Location: Cytoplasm
EC: 2.7.... |
P27954 | RNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSSGLYHVTNDCPNSSIVYEAADAILHTPGCVPCVHEGNVSRCWVAMTPTVATRDGKLPTTQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRRHWTTQGCNCSI | Function: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements ta... |
Q5EG65 | MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPKGRNWAQPGYPWPLYGNEGCGWAGWLPSPRGSRPSWGPNDPRRRSRNLGKVIDTLTCGFVDLMGYIPLVGAPLRGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSTGLYHVTNDCPNSSIVYEAVDAILHTPGCVPCVREGNASRCWVAMTPTVATRDGRLPTTQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRRHWTTQGCNCSIYPGHITGHRMAW... | Cofactor: Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3).
Function: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable).... |
Q01403 | MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLTRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRAWAQPGYPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGASRALAHGVRVLEDGVNYATGNLPGCSFSIFLSALMSCLTTPASAYEVRNVSGIYHVTNDCSNSSIAYEAAGMIMHTPGCVPCVRENNSSRCWVALTPTLAARNASVPTTTIRRHVDLLVGAATLCSAMYVGDLCGSVFLVSQLFTFSPRRYETVQDCNCSIYPGHVSGHRMAW... | Function: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements ta... |
P27960 | MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKDRRSTGKSWGKPGYPWPLYGNEGLGWAGWLLSPRGSRPSWGPNDPRHRSRNVGKVIDTLTCGFADLMGYIPVVGAPLGGVARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCITVPVSAVQVKNTSNSYMVTNDCSNDSITWQLQGAVLHVPGCVPCEKVGNMSRCWIPVSPNVAVRQPGALTQGLRTHIDMVVVSATLCSALYVGDLCGGVMLAAQMFIVSPQHHWFVQECNCSIYPGAITGHRMAW... | Function: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements ta... |
P03318 | DADLAAVYRAVASLADETVRTMAIPLLSTGTFAGGKDRVLQSLNHLFTALDTTDVDVTIYCRDKSWEKKIQEAIDMRTATELLDDDTTVMKELTRVHPDSCLVGRSGFSTVDGRLHSYLEGTRFHQTAVDVAERPTLWPRREEANEQITHYVLGESMEAIRTKCPVDDTDSSAPPCTVPCLCRYAMTPERVHRLRAAQVKQFTVCSSFPLPKYKIPGVQRVACSAVMLFNHDVPALVSPRKYREPSISSESSSSGLSVFDLDIGSDSEYEPMEPVQPEPLIDLAVVEETAPVRLERVAPVAAPRRARATPFTLEQRVVAP... | Cofactor: For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis at 60% of the levels observed with Mg(2+).
Function: Polyprotein P1234: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA... |
P09523 | MTSSSLFREGELGHFCLNKQEMLHLNVTNPNSIYIEGKLSFEGYKSFNIHCYVDTGASLCIASRYIIPEELWENSPKDIQVKIANQELIKITKVCKNLKVKFAGKSFEIPTVYQQETGIDFLIGNNFCRLYNPFIQWEDRIAFHLKNEMVLIKKVTKAFSVSNPSFLENMKKDSKTEQIPGTNISKNIINPEERYFLITEKYQKIEQLLDKVCSENPIDPIKSKQWMKASIKLIDPLKVIRVKPMSYSPQDREGFAKQIKELLDLGLIIPSKSQHMSPAFLVENEAERRRGKKRMVVNYKAINQATIGDSHNLPNMQELL... | Function: Encodes for at least two polypeptides: protease (PR) and reverse transcriptase (RT). The protease processes the polyprotein in cis. Reverse transcriptase is multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that ca... |
Q9CGD4 | MSKTIIEFKNVSKTYADTDTTVLKDISFELEEGKFYTLLGASGSGKSTILNIIAGLLDATDGDVILDNKRINDLPANKRNVHTIFQSYALFPNMNVFDNVAFALKIKGVDKKEIAKRVSESLKLVRLDGFEKRSITKLSGGQKQRVAIARAIIDRPKVLLLDESLSALDMKLRKDMQYELRELQQSLGITFIFVTHDQEEALAMSDWVFIMNEGEIVQSGTPTDIYDEPINHFVADFIGESNILNGRMIEDYLVEFNGQKFEAVDGGMRKNEPIEVVIRPEDIWFTLPDEGKFNVKVDTQLFRGVHYEIVAYDEFNNEWL... | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology:... |
Q5ZWE4 | MTTPLIEIRQIYKSYGNTPILNNVSLNVNHGEFLTLLGPSGCGKTTLLRLISGFEQPTQGEIFINGQCVNQLPPQKRDVHTVFQSYALFPHLSVFENVAFALRCKKTPNQEIRKRVFDALKLVQLESLAERNVKQLSGGQQQRVAIARAIINRPQVLLLDEPLSSLDYRLRKAMQSELKQLQKTLNMTFIFVTHDQEEALSMSDRIVVFNHGHIEQIGTPKAVYETPANLHVAMFIGEANIFDIQVHTVKDQDIITNIEGIQLSCKNTGNYQVNDRLHLIVRPEDIRVWSLSEVEKTEGMLPGRIVDIIYKGSTVDLKVE... | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology:... |
Q8Y8T6 | MIVTETIIRFENVTKQFDNDPPVLDNVSFEIEKGKFYTLLGPSGCGKTTILRLIAGFLEASKGQIYLGDKVINQIPANKRPVNTVFQDYALFPHLNVYENVAFGLRIKKLKKEAIDEKVKEALRFVNLKGYEKREISEMSGGQRQRVAIARAIVNEPEVILLDEPLSALDLKLRTEMQYELRDLQKRLGITFIFVTHDQEEALAMSDEIFVLNKGEIQQSGTPIDIYDEPINKFVADFIGESNIVNGKMIQDFEVEFVERRFECVDQGFRPNEVVEVVIRPEDLEITSAEKGQLQVTVDWMLFRGVHYEVGCIDIDGNEW... | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology:... |
P44768 | MSAKSNKIGVVQLTILTMVNMMGSGIIMLPTKLAEIGTISIVSWLVTAVGSTALAYAFAQCGMFSKKSGGMGGYAEYSFGKAGNFMANYTYGVSLVIANTAIAISAVGYGSELFGTILSPLSIALWTIFTLWLATVLNFGGARITGNISSFTIWGVIIPVVGISIIGWKWFDGSMYVNSWNPHNVPTFEAIGVSISMTLWAFLGLESACANADAVENPEKNVPIAVLGGTLGAAVIYIVSTNVIAGIVPNLELANSTAPFGLAFAHMFDETVGKVIMGLMVMSCFGSLLGWQFTIAQVFKSSAEEGYFPAFFKKITSKDA... | Function: Catalyzes both the uptake and excretion of putrescine. The uptake of putrescine is dependent on the membrane potential and the excretion involves putrescine-ornithine antiporter activity.
Catalytic Activity: H(+)(in) + putrescine(in) = H(+)(out) + putrescine(out)
Location Topology: Multi-pass membrane protein... |
P31134 | MNDAIPRPQAKTRKALTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLKERQEDGLVLDSPGLVHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPANGCNFAVGEV... | Function: Part of the ABC transporter complex PotFGHI involved in putrescine uptake . Responsible for energy coupling to the transport system . Imports putrescine for maintenance of the optimal concentration of polyamines necessary for cell growth in the presence of glucose .
Catalytic Activity: ATP + H2O + putrescine(... |
P31135 | MSTLEPAAQSKPPGGFKLWLSQLQMKHGRKLVIALPYIWLILLFLLPFLIVFKISLAEMARAIPPYTELMEWADGQLSITLNLGNFLQLTDDPLYFDAYLQSLQVAAISTFCCLLIGYPLAWAVAHSKPSTRNILLLLVILPSWTSFLIRVYAWMGILKNNGVLNNFLLWLGVIDQPLTILHTNLAVYIGIVYAYVPFMVLPIYTALIRIDYSLVEAALDLGARPLKTFFTVIVPLTKGGIIAGSMLVFIPAVGEFVIPELLGGPDSIMIGRVLWQEFFNNRDWPVASAVAIIMLLLLIVPIMWFHKHQQKSVGEHG | Function: Part of the ABC transporter complex PotFGHI involved in putrescine uptake . Responsible for the translocation of the substrate across the membrane (Probable). Imports putrescine for maintenance of the optimal concentration of polyamines necessary for cell growth in the presence of glucose .
Location Topology:... |
P0AFL2 | MNNLPVVRSPWRIVILLLGFTFLYAPMLMLVIYSFNSSKLVTVWAGWSTRWYGELLRDDAMMSAVGLSLTIAACAATAAAILGTIAAVVLVRFGRFRGSNGFAFMITAPLVMPDVITGLSLLLLFVALAHAIGWPADRGMLTIWLAHVTFCTAYVAVVISSRLRELDRSIEEAAMDLGATPLKVFFVITLPMIMPAIISGWLLAFTLSLDDLVIASFVSGPGATTLPMLVFSSVRMGVNPEINALATLILGAVGIVGFIAWYLMARAEKQRIRDIQRARRG | Function: Part of the ABC transporter complex PotFGHI involved in putrescine uptake. Responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30541
Sequence Length: 281
Subcellular Location: Cell inner membrane
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.