ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6ZIB5 | MIGWGDVYKVVGAMAPLYFALGLGYGSVRWWRFFTAEQCAAINTMVVYFSMPFFTFDFVVRTDPFAMNYRVIAADAVSKAIAIAAMAAWARTRCGCAAAKAGAQSWSITGFSLAALNNTLVVGVPLLDAMYGRWAQDLVVQIAVVQSMVWFPLLLMAFELRKAWVVGGGGGVGPAVMSSSSPPEKQSDVEMNGAVVAAPGGGGGVRLPFWATARTVGLKLARNPNVYASVLGVVWACIAYRWHLSLPGIVTGSLQVMSRTGTGMSMFSMGLFMGQQERVIACGAGLTALGMALRFVAGPLATLVGAAALGLRGDVLHLAI... | Function: May act as a component of the auxin efflux carrier.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39032
Sequence Length: 370
Subcellular Location: Membrane
|
Q9FFD0 | MINCGDVYKVIEAMVPLYVALILGYGSVKWWHIFTRDQCDAINRLVCYFTLPLFTIEFTAHVDPFNMNYRFIAADVLSKVIIVTVLALWAKYSNKGSYCWSITSFSLCTLTNSLVVGVPLAKAMYGQQAVDLVVQSSVFQAIVWLTLLLFVLEFRKAGFSSNNISDVQVDNINIESGKRETVVVGEKSFLEVMSLVWLKLATNPNCYSCILGIAWAFISNRWHLELPGILEGSILIMSKAGTGTAMFNMGIFMALQEKLIVCGTSLTVMGMVLKFIAGPAAMAIGSIVLGLHGDVLRVAIIQAALPQSITSFIFAKEYGL... | Function: Auxin transporter regulating intracellular auxin homeostasis and metabolism . Mediates the auxin transport from the cytosol into the lumen of the endoplasmic reticulum . May also act as an auxin efflux carrier when located to the cell membrane . PIN5 and PIN8 may have an antagonistic/compensatory activity . I... |
Q9SQH6 | MITGNEFYTVMCAMAPLYFAMFVAYGSVKWCKIFTPAQCSGINRFVSVFAVPVLSFHFISQNNPYKMDTMFILADTLSKIFVFVLLSLWAVFFKAGGLDWLITLFSIATLPNTLVMGIPLLQAMYGDYTQTLMVQLVVLQCIIWYTLLLFLFELRAARLLIRAEFPGQAAGSIAKIQVDDDVISLDGMDPLRTETETDVNGRIRLRIRRSVSSVPDSVMSSSLCLTPRASNLSNAEIFSVNTPNNRFFHGGGGSGTLQFYNGSNEIMFCNGDLGGFGFTRPGLGASPRRLSGYASSDAYSLQPTPRASNFNELDVNGNGT... | Function: Component of the intracellular auxin-transport pathway . Regulates auxin transport and auxin homeostasis . Directly involved in the regulation of nectar production . Involved in unfolded protein response (UPR) activation . Involved in the control of vein patterning . Redundantly with PIN8, inhibits the vein-f... |
P41415 | MATTNATLQTLVQFYENCKNVKTRYKIINGRFGKISILSHKPTSKLYLQKTISAHNFNADEIKVHQLMSDHPNFIKIYFNHGSINNQVIVMDYIDCPDLFETLQIKGELSYQLVSNIIRQLCEALNDLHKHNFIHNDIKLENVLYFEALDRVYVCDYGLCKHENSLSVHDGTLEYFSPEKIRHTTMHVSFDWYAVGVLTYKLLTGGRHPFEKSEDEMLDLNSMKRRQQYNDIGVLKHVRNVNARDFVYCLTRYNIDCRLTNYKQIIKHEFLS | Function: Serine/threonine protein kinase that plays a role in viral propagation by phosphorylating various viral and cellular substrates including the viral p6.9 protein or host histone H1. Participates in nucleocapsid assembly and polyhedra formation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phosp... |
P41720 | MDALIGDFADFHKECSARTALHLVNGKFGKVSVWKHGPTQKSFFYKRIEHKHFNAIEPFVHHLMKFNKYFLRLFYSLHSLREHLLVMDYIPDGDLFDLMQTEPRLREPEISLIAYQLIDALQALHKHNVVHNDVKLENVLYRRFEQIYVCDYGLCKIAGSPSTFEGTVDYFSPEKINKHAAAVHFDWWAVGVLLYEISTGKHPFKLDQDESLDVETLHKRQIQLDVTFPADFDNPFLEEFICFLLGYCYDYRAHSYEVIQKNTYWKSIVHWKQR | Function: In vitro, can phosphorylate histone H1.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 32438
Sequence Length: 274
EC: 2.7.11.1
|
Q9KIG4 | MDTTLQDPLVGQVLDGRYRVDARIAVGGMATVYRAVDTRLDRVLALKVMHPSLAADASFVERFIREAKSVARLAHPNVVQVFDQGTDGAYVYLAMEYIAGCTLRDVLRERGALQPRAALDILEPVLAALGAAHRAGFVHRDMKPENVLIGDDGRVKVADFGLVRAVDSVTNTTGTVLGTVSYLAPEQIEHGTADPRVDVYACGILLYEMLTGEKPHDGDSPAIVLYKHLHDDVPPPSAAVPGMAYELDELVASATARGPEVRPHDAVALLARARDARARLGDEQLDAVPPQALASEHDNADDRTSVIPRALTVRRPLPVN... | PTM: Autophosphorylated on threonine residue(s).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 67973
Sequence Length: 641
EC: 2.7.11.1
|
Q9I6Z1 | MSEEPTVSPPSPEQPAAQPAKPARPAARRAPRKPATRRPRVASPAQKAREEIQAISQKPVALQVASAPHGSSEDSTSASLPANYPYHTRMRRNEYEKAKHDLQIELLKVQSWVKETGQRVVVLFEGRDAAGKGGTIKRFMEHLNPRGARIVALEKPSSQEQGQWYFQRYIQHLPTAGEMVFFDRSWYNRAGVERVMGFCSPLQYLEFMRQAPELERMLTNSGILLFKYWFSVSREEQLRRFISRRDDPLKHWKLSPIDIKSLDKWDDYTAAKQAMFFHTDTADAPWTVIKSDDKKRARLNCIRHFLHSLDYPDKDRRIAH... | Cofactor: Mg(2+) is preferred for polyP utilization and Mn(2+) is preferred for polyP synthesis.
Function: Uses inorganic polyphosphate (polyP) as a donor to convert GDP to GTP and ADP to ATP. Shows a preference for GDP. Can also catalyze the synthesis of polyP from GTP or ATP, but the rate of polyP utilization is 75-f... |
Q92SA6 | MALDEAPAEARPGSRAVELEIDGRSRIFDIDDPDLPKWIDEEAFRSDDYPYKKKLDREEYEETLTKLQIELVKVQFWMQATGKRVMAVFEGRDAAGKGGAIHATTANMNPRSARVVALTKPTETERGQWYFQRYVATFPTAGEFVLFDRSWYNRAGVEPVMGFCTPDQYEQFLKEAPRFEEMIANEGIHLFKFWINIGREMQLKRFHDRRHDPLKIWKLSPMDIAALSKWDDYTGKRDRMLKETHTEHGPWAVIRGNDKRRSRINVIRHMLTKLDYDGKDEAAIGEVDEKILGSGPGFLR | Cofactor: Has low activity with Co(2+) or Ni(2+).
Function: Uses inorganic polyphosphate (polyP) as a donor to convert ADP to ATP. Can also convert GDP to GTP, with lower efficiency. Cannot dephosphorylate ATP in the presence of polyP.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da)... |
Q5LX16 | MTHESDDPSLDWLEAELEDSLDEDFEIEFSEPMLSMEIRRIYKDQRPDLLDRQVYFRNLLRLQAELIKLQDWVQHTNSKVLIIMEGRDAAGKGGVIKRITQRLNPRIARVVALPAPSRREQSQWYFQRYVPYLPSGGEMVLFDRSWYNRAGVERVMGFATEDQVEQFFQDVPEFERMLVRSGIILLKYWFSITDEEQQLRFLMRVHDPMKQWKLSPMDLESRIRWEQYTKAKEQMFSRTNIPEAPWYIVEGNDKKRERLNCIEHLLSKIPYEDIPHEKVTLPDRRYNPDYERQVLPDELYVPKVY | Function: Uses inorganic polyphosphate (polyP) as a donor to convert NDP to NTP. PolyP hydrolysis is slightly faster with GDP, but it can also use ADP, CDP and UDP.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 36711
Sequence Length: 305
EC: 2.7.4.-
|
Q8NM65 | MVGKLPIMAETNENDLPVIDLAQIEGYVVDDSDEDDPVLLRPDGTPIETWREDFPYEERVTREDYEKVKRSLQIELLKWQNWTKETGQRHIILFEGRDAAGKGGTIKRFNEHLNPRGARTVALEKPSPRESTSWYFQRYIQHFPAAGEIVFFDRSWYNRSGVERVMGFCTESQHAEFLREVPMLENMILGSGISLTKFWFSVTRKEQRTRFAIRQVDPVRQWKLSPMDLASLDRWDDYTRAKEEQFRYTDTDESPWITIKSNDKKRARINAMRYVLSKFDYTDKDYELVGEPDPKVVLRGRDQIGD | Function: Catalyzes the synthesis of polyP from ATP or GTP. Can also use inorganic polyphosphate (polyP) as a donor to convert ADP to ATP, but the activity is 10-fold higher in vitro for polyP synthesis than for ATP formation.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 36044
S... |
Q9I154 | MDSYGDTSGRIGRDWLDRHDEELEQELLDDELNLDELFGPEQEDAPGELSRRRYFRELFRLQRELVKLQNWVVHTGHKVVILFEGRDAAGKGGVIKRITQRLNPRVCRVAALPAPNDREQTQWYFQRYVSHLPAGGEIVLFDRSWYNRAGVERVMGFCNDEQYEEFFRSVPEFEKMLARSGIQLLKYWFSISDAEQHLRFLSRIHDPLKQWKLSPMDLESRRRWEAYTKAKETMLERTHIPEAPWWVVQADDKKRARLNCIHHLLQQMPYREVPQPPVHLPERLRHADYVRHPTPGEIIVPEVY | Function: Uses inorganic polyphosphate (polyP) as a donor to convert ADP to ATP.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 36196
Sequence Length: 304
EC: 2.7.4.-
|
Q92ZU4 | MDKHTDDRKKNNHWKAEDRKSAATEASETRSGGNYAKELARLQEEIAHLQAWVKKTGARIVIVFEGRDAAGKGGVIKRITERVSPRVFRVVALPAPTDREKTQIYMQRYIQQFPAAGEVVIFDRSWYNRPGVERVMGFCSEKKAKRFLEIAPRFEAAMIESGIVLLKYFLDVSEEEQDRRFRQRINDPLRQWKLSPMDVESYRRWWDYTRAYDEMIRMTDTDDAPWWIVPSDNKKQARVNCIAHILSSIPYERVKFEDPDLGKRQKRPADFEGDTRRRTVPNLF | Function: Uses inorganic polyphosphate (polyP) as a donor to convert ADP to ATP. Can also convert GDP to GTP, with lower efficiency.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 33401
Sequence Length: 284
EC: 2.7.4.-
|
Q5LSN8 | MNRNGSTKDPRRMTGAATGEISRYFNDKAPKDIRRAIEKADKDDILSTTYPYDAEMTAKDYRAQMEALQIELVKLQAWIKQSGARVALLFEGRDAAGKGGTIKRFRENLNPRGARVVALSKPTEAERSQWYFQRYIQHLPSAGELVFYDRSWYNRGVVEHVFGWCDEEQRERFFRQVMPFEHDLVDDGIHLFKFWLNVGRAEQLRRFHDRERDPLKQWKLSPVDIAGLDKWEAYTTAISQTLTRSHSDRAPWTVIRSDDKKRARLAAIRTVLSGIDYDNKDRAAVGQPDAAICGGPDIWDA | Cofactor: Also accepts various divalent metal ions.
Function: Uses inorganic polyphosphate (polyP) as a donor to convert NDP to NTP. PolyP hydrolysis is slightly faster with UDP, but it can also use ADP, GDP and CDP.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 34740
Sequence Le... |
A0QQV6 | MLDSTGYAVRDDDDDDPELLLPGGEVVDTWREGYPYDERMHRADYEEQKRLLQIELLKLQKWSQAHGHRHVIVFEGRDAAGKGGTIKRFMEHLNPRGARVVALEKPTERERTQWYFQRYVEHLPAAGELVLFDRSWYNRAGVERVMGYCTPKQHAEFIRQAPLFEQMLVNDGISLTKLWFSVTRSEQLTRFTIRQVDPVRQWKLSPTDLASLDKWDDYTAAKEEMFAWTDTEIAPWTVVKSNDKKRARINAMRYVLGKFDYDNKDHEVVGQADPLIVGRALSD | Function: Uses inorganic polyphosphate (polyP) as a donor to convert GDP to GTP.
Catalytic Activity: [phosphate](n) + GTP = [phosphate](n+1) + GDP
Sequence Mass (Da): 33047
Sequence Length: 283
EC: 2.7.4.-
|
O05877 | MDIPSVDVSTATNDGASSRAKGHRSAAPGRRKISDAVYQAELFRLQTEFVKLQEWARHSGARLVVIFEGRDGAGKGGAIKRITEYLNPRVARIAALPAPTDRERGQWYYQRYIAHLPAKGEIVLFDRSWYNRAGVEKVMGFCTPQEYVLFLRQTPIFEQMLIDDGILLRKYWFSVSDAEQLRRFKARRNDPVRQWKLSPMDLESVYRWEDYSRAKDEMMVHTDTPVSPWYVVESDIKKHARLNMMAHLLSTIDYADVEKPKVKLPPRPLVSGNYRRPPRELSTYVDDYVATLIAR | Function: Uses inorganic polyphosphate (polyP) as a donor to convert GDP to GTP. In addition, modulates nucleotide triphosphate synthesis catalyzed by the nucleoside diphosphate kinase (Ndk) in favor of GTP production over CTP or UTP. Plays an important role in survival of M.tuberculosis in macrophages.
PTM: Autophosph... |
Q6N140 | MKIKTKQFRVGEGEKVDLGKWPTKVDPFYESKEHYHELLRTQVERLSDLQQLLYASNRHAVLLIFQAMDAAGKDGVIRHVLSGINPQGCQVFSFKHPSATELQHDFLWRTTRDLPERGRIGVFNRSYYEEVLIVRVHPDILQSEAVPNGENFGKSFWHKRYRSIRNLEQHLHANGTRIVKFFLHLSKDEQRKRFLARIDEPEKNWKFSAADLEERQYWDDYMDAYEKCLSETSSEDSPWYAVPADDKENARLIVSQVIAETMESLKMSYPETTPARRKELLQMRQQLLK | Function: Uses inorganic polyphosphate (polyP) as a donor to convert ADP to ATP.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 34057
Sequence Length: 289
EC: 2.7.4.-
|
Q83XD3 | MDTETIASAVLNEEQLSLDLIEAQYALMNTRDQSNAKSLVILVSGIELAGKGEAVKQLREWVDPRFLYVKADPPHLFNLKQPFWQPYTRFVPAEGQIMVWFGNWYGDLLATAMHASKPLDDTLFDEYVSNMRAFEQDLKNNNVDVLKVWFDLSWKSLQKRLDDMDPSEVHWHKLHGLDWRNKKQYDTLQKLRTRFTDDWQIIDGEDEDLRNHNFAQAILTALRHCPEHEKKAALKWQQAPIPDILTQFEVPQAEDANYKSELKKLTKQVADAMRCDDRKVVIAFEGMDAAGKGGAIKRIVKKLDPREYEIHTIAAPEKYE... | Cofactor: Lower concentrations of MgCl(2) are required to obtain optimum polyP synthetic activity, whereas higher concentrations of MgCl(2) are necessary for optimum PAP activity.
Function: Uses inorganic polyphosphate (polyP) as a donor to convert AMP to ADP. Can also use GMP, UMP, CMP, TMP or deoxyribonucleoside mono... |
Q504Y2 | MRRRRAAVAAGFCASFLLGSVLNVLFAPGSEPPRPGQSPEPSPAPGPGRRGGRGELARQIRARYEEVQRYSRGGPGPGAGRPERRRLMDLAPGGPGLPRPRPPWARPLSDGAPGWPPAPGPGSPGPGPRLGCAALRNVSGAQYMGSGYTKAVYRVRLPGGAAVALKAVDFSGHDLGSCVREFGVRRGCYRLAAHKLLKEMVLLERLRHPNVLQLYGYCYQDSEDIPDTLTTITELGAPVEMIQLLQTSWEDRFRICLSLGRLLHHLAHSPLGSVTLLDFRPRQFVLVDGELKVTDLDDARVEETPCAGSTDCILEFPARN... | Function: Secreted tyrosine-protein kinase that mediates phosphorylation of extracellular proteins and endogenous proteins in the secretory pathway, which is essential for patterning at organogenesis stages. Mediates phosphorylation of MMP1, MMP13, MMP14, MMP19 and ERP29 . Probably plays a role in platelets: rapidly an... |
Q5RJI4 | MRRRRAAVAAGFCASFLLGSVLNVLFAPGSEPPRPGQSPGSSAAPGPGRRGGRGELARQIRERYEEVQRYSRGGPGPGAGRPERRRLMDLAPGGPGLQRPRPPRVRSPPDGAPGWPPAPGPGSPGPGPRLGCAALRNVSGAQYVGSGYTKAVYRVRLPGGAAVALKAVDFSGHDLGSCVREFGARRGCYRLAAHKLLKEMVLLERLRHPNVLQLYGYCYQDSEGIPDTLTTITELGAPVEMIQLLQTSWEDRFRICLSLGRLLHHLAHSPLGSVTLLDFRPRQFVLVNGELKVTDLDDARVEETPCTSSADCTLEFPARN... | Function: Secreted tyrosine-protein kinase that mediates phosphorylation of extracellular proteins and endogenous proteins in the secretory pathway, which is essential for patterning at organogenesis stages. Mediates phosphorylation of MMP1, MMP13, MMP14, MMP19 and ERP29 . May also have serine/threonine protein kinase ... |
C8VI81 | MDHPHPSTFSLGLSQILVCLALLYAAIHILSVYRRLCHISGPFWARISNLPRVWWVNTSRAHEIHQQLHEKYGDVVRFGPNMVSLRNPTWIPTVYPTRMGVKKSDFYRTLAPYTPSGALPAVFSSRDEEVHRGLRGPIASLYSMSKVLPLEVFVDRTIDVLVRQLDGRFAGAGETFDLASWLQFFAFDVMGTLTFSKRYGFLEKGMDVHGMLDTIWRFLKGAAPFTQIPWVDEIWNKNVLATKLKGATGVSILGIVGKFVSQRQEESKAGKIDGTADRDMLSLFMEIQKNNQLPPWYVTAWTFSNITAGSDSAAVVMRTV... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone . The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA . Hydroxylation, methylation of one of... |
C8VI80 | MVFGSRPPALTEANIGDQSGKVFIVTGATSGYGLLLSTYLYQNNGTVYLAARNAKKTAEVIADLKQRFPASRGRLDSISLNLSDLSTIKKSAEEFLAKETRLHVLWNNAGVMFPPAGSTTSQGYELQLGTNNVGPHLFTKLLYPTLAATAKEAPKNTVRVVWVSSDAASWAPKPAIDFNNLDYRRNESDRSKYGRSKAGTVMQAVELARRARKDGSGIVSIALDPGIANTGLQRDMGRLMSTMVKLIANKPEIGAYTQLFAGLSPEITAEVAEKEWVVPPGKIGCPRRDLFTDTETSRKWWEWNEEQVKAYL | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone . The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA . Hydroxylation, methylation of ... |
Q5B8A3 | MGSLWSSPSLLPSQQDNETEPFSHLPKEIGTDPTLREDSNVSNRNSEAASTSTDSSTNTNENHASTSQSSLEGAPDSGPIKIAIIGGGIIGIITALGLIHRGINVTVYERAPKYTETSAGFSFSKGARKAMEIVSPRVLEALLRVAAPNKHPFIRYFDGFTPGADEAQWQIPAERPDYYGCLRAAFLESLGQEVPEGIVKFGKVLESYEDNEEGKVLLRFRDGSTAEVDAVIGCDGIKSRTRRIMLGDTHPAAAPGYTEIVAYRAVLPLEGVVAALGEDRGHSHCLAVGPDAYTVSYPIANKPLANMILFRKQRGSWANS... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone . The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA . Hydroxylation, methylation of one of t... |
Q5B8A2 | MYSKSWILNALPAPLVPYCELTRVGYLPIGVLVSYLPVLVAILHVAAVARLPYDNILDSCLQWLPLCYVYSAYGCVVDDIADQDLDRKVERCQHRPLVRGAVSTTSACLFAASLASLAVFLTKTFFPDQPAVHIPVALAGSIIYPFLKRFTNFALLYLAFLYVATGLNASRTIGYDILSAPDHLLTSNLLLAAAVFIANVSVETIYMHADLEDDIKSGIGSLAVKIQGYSKPVLFLAAVAYGSLVLASGLAAEFGKWYFTGAITSALTLFTLVARVDLKNGKMCEQFFFMGNAVLMSLLAAGLYGECIA | Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone . The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA . Hydroxylation, methylation of one of the phenol ... |
Q5B8A1 | MRHTALLPLVSSFIVPALAQIPGQTTVNATVNQGRFGNATYDYVIVGGGTSGLAIAARLAEDPSLSVAVIEAGGYYELDGTVASIIPGLAAGANVGTDATEYSTVDWNFQAQPLTSANDRSLRYNRGKTLGGSSARHYMVYQRGTRGSYDQWAELTGDESWGWDSVFPYFQRSVNVTPANMTGRFPNTTVTYDPSGFNKAGGPLHVTWPNYGSPWSTWIEQGLEAIGILPDTDFNTGTLNGSSWAPITINPLSQKRDSSETSFLQQSLKTTNLTVYLHTMALKIGFDGTTASSVDVRSPVGRFTLSARREIIVSAGALQS... | Function: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone . The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA . Hydroxylation, methylation of one of the phenol grou... |
A7MBL8 | MAADSVQNDARGPMVSGRLDFDQNLDFSDTMVQKNLDEIKDQIKREIRKELKIKEGAENLRKVTTDKKSLAYVDNMLKKSNKKVEELHQELQELNAHIVVKDPEEVEEYPLTPDTPKSETRMSTNSNRLAALKKQADIELKVKQGAEDMIQMYSNGSSKDRKLLAAAQQMLQDSKTKIEFIRMQILKASQTSEINYENNDVTTSKPIISPLDLRIEELRHHYRIESAVADGAKNVMKLLGTGKVTEKKAHSEAQARLNESSQKLDLLKFSLEQRLSELPKNHPKGTLIMEELAMVASPPNSPRQSIMSTSNQYSTVAKPA... | Function: Pkc-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. May play a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion and transcription activation signaling proce... |
Q16513 | MASNPERGEILLTELQGDSRSLPFSENVSAVQKLDFSDTMVQQKLDDIKDRIKREIRKELKIKEGAENLRKVTTDKKSLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDITDCPRTPDTPNNDPRCSTSNNRLKALQKQLDIELKVKQGAENMIQMYSNGSSKDRKLHGTAQQLLQDSKTKIEVIRMQILQAVQTNELAFDNAKPVISPLELRMEELRHHFRIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNEVPKNHPKSRIIIEELSLVAASPTLSPRQSMISTQNQYST... | Function: PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activati... |
P54736 | MLAPDSLVLDGRFRVLRPLGSGGMGEVYLGEQVSLGRKVAIKVLHHDLHAQAGMAERFKREARLLSAVEHPAVVRIVDFGESGDHACLVMEFVEGESLYDVLTPGPMPPGRALPLLQQLAEGLAAIHDKGIIHRDLKPENVFISKSARGEQARLLDFGIARLVEPDAASSVSQIGVVLGTPEYLSPEQAVGAKVDTRSDLYSFGVLTYRVLSGRLPFDGPLPRNFLSQHASAAPLPLDRAAPTLSRYVGLLSLVMRLLEKDASKRPQSAHELADALAAAHSALSAFTPGLGTPAYVPQPGSGATPSSGTSVFGTGSASGS... | Function: Regulates the activity of endogenous beta-lactamase or related enzymes, by blocking their secretion by phosphorylation, in response to an external signal yet to be identified.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein... |
Q6P5Z2 | MEEGAPRQPGPSQWPPEDEKEVIRRAIQKELKIKEGVENLRRVATDRRHLGHVQQLLRSSNRRLEQLHGELRELHARILLPGPGPGPAEPVASGPRPWAEQLRARHLEALRRQLHVELKVKQGAENMTHTCASGTPKERKLLAAAQQMLRDSQLKVALLRMKISSLEASGSPEPGPELLAEELQHRLHVEAAVAEGAKNVVKLLSSRRTQDRKALAEAQAQLQESSQKLDLLRLALEQLLEQLPPAHPLRSRVTRELRAAVPGYPQPSGTPVKPTALTGTLQVRLLGCEQLLTAVPGRSPAAALASSPSEGWLRTKAKHQ... | Function: Contributes to invasiveness in malignant prostate cancer.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 99421
Sequence Length: 889
Domain: The C1 domain does not bind the diacylglycerol (DAG).
Subcellular Location: Nucleus
E... |
Q8K045 | MEHRKPGTGQRAPKDEKEMVRRAIQKELKIKEGMENMRRVATDRRHLGHVQQLLRASNRRLEQLHGELRELHAQVLLPASAEPVTSEPQPRAEQSRARLSEALHRQLQVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLRMKISSLESSGSPEPGPDLLAEELQHRLRVEAAVAAGAKNVVKLLGGQRMQDRKALAEAQAQLQESSQKLDLLRLALELLLERLPPTHSLRSRVTQELWMAMLGNPQPLGTLVKPIALTGTLQVRLLGCKDLLVAVPGRSPMAVLAGSPSESWLRTRSRQQRGGGELA... | Function: Contributes to invasiveness in malignant prostate cancer.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 97881
Sequence Length: 878
Domain: The C1 domain does not bind the diacylglycerol (DAG).
Subcellular Location: Nucleus
E... |
P54737 | MPLKVIGPYRVLETLGSGGAGTVYRALDRRTTDEVALKLLSAGPARDARAARRLAREFDTLVDLSHPNVVKVFESGVHQGVPYLAMELIEGLTLRHYLDLSSGDRQTPPGSHTPRSPLSVLRTADDDFGPLSRSFSDSMDDSEDSPFDGTFGLEAFAEEAPSEDLESFASSASPHVGIGSDDSLEGFDLPPPMPRPAEPEEEPGRVVREEDLNRPERMGRLKDAMLQICEALAYIHGHGLVHRDLKPSNIMVDDDRQVRLMDFGLAKFLADDAAITEAGKLVGTYRYMAPEQILGEPLDGRADLYSLGVILYELLSGRPP... | Function: Pkn5 and pkn6 may have reciprocal roles in growth and development. Pkn5 may be a kinase that negatively regulates development.
PTM: Autophosphorylated on serine residues.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 41924
Sequence Length: 380
Subce... |
P54738 | MQIGKYQLVRKLASGGMAEVFLAKAAGPRGFEKTLVLKRILPHLAEDAAFVEMFLGEARLAAQLEHPNIVQIFDFGEAEGSFFLAMEFIDGPNLRKLVKRAAEEALPPAFCAKVVAAAAEGLAYAHEFRDVETGEPLGLIHRDVSPDNILVSRQGAVKVVDFGIAKVAGQGHRTLTGVVKGKVAYMPPEQLQAKAMDRRVDVYALGVVLYELLTGKRPFDATTDVSVMQAILFESFIPVSARRPDVPVALQQVLDKALAKDRERRYADCRALQDDLERFVLSTGEPVGAYQIAQRIAQWVPEVAAAPAMTPSQGGSKGAV... | Function: Pkn5 and pkn6 may have reciprocal roles in growth and development. Pkn6 may be a transmembrane sensor of external signals for development.
PTM: Autophosphorylated on serine and threonine residues.
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phos... |
P54743 | MSPRIGVMLSGRYRLHRLIATGGMGQVWEAVDSRLGRRVAVKVLKGEFSSDPEFIERFRAEARTTAMLNHPGIASVHDYGESHMDGEGRTAYLVMELVNGEPLNSVLKRTGRLSLRHALDMLEQTGRALQIAHAAGLVHRDVKPGNILITPTGQVKITDFGIAKAVDAAPVTQTGMVMGTAQYIAPEQALGHDATPASDVYSLGVIGYEVVSGKRPFTGDGALTVAMKHIKEPPPPLPADLPPNVRELIEITLVKNPGMRYPSGGLFAEAVAAVRAGHRPPRPNQTPSSGRASPTTIPSSTQARAAVACGTKTPAPRRSR... | Function: Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins.
PTM: Autophosphorylated.
Location Topology: Single-pass membrane protein
Catalytic Activi... |
D4B0M5 | MKLSVLLALGASSLAAAAPAATACDCGAAVTDRLLFSSSISTFQAARNALNPPCCDWSSDNCSSSPDKPRGYDFIPSCQRHDYGYRNGKRLNRFTEDYRKKVDDNFKADLYNYCSQFSGLESWKGVECRRYADIYYFFVRECGDGDCP | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secretory phospholipase that catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity). Increases the ability to utilize host-derived nutrients and lipids, and promotes lipid dropplets accumulation (By similarity). Plays... |
J4KMY5 | MKLAYFSSLLPLALAAPASVVDPREPKEDITDRYLFSTPLPTFLEYREKENPDSLDWTSDGCTHASNNPFGFPFEPACQRHDFGYRNYQAQTRFESDSRYRIDLNFYNDMIFQCTDVSALRSCHGLADVYYAGVRMFGGFAKRDEMGAVVASATDPKESAEDLIAVYYTALQEYHQAVKADQADGLLPRL | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Secretory phospholipase that catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides . Increases the ability to utilize insect-derived nutrients and lipids, and promotes lipid dropplets accumulation . Plays a role in virulence, includ... |
Q0JKT4 | MFSCDMASRWRELHGSGHWDGLLDPLDVDLRRCLITYGEMIMATYEAFIGEHRSPNAGMCRYRHADLFRRVDVSHPGWYAATRYIYATANADVHGKVLLRPLCREGRATECNWMGYVAVATDEGAAALGRRDIVVAWRGTQRALEWVADLKLAPASAAGILGPEGADGTDPSVHRGYLSLYTSEDQCSELNKQSARMQVLTEIARLMDKYKDEETSITVIGHSLGATLATLNAADIAANSYNTSSLSPSGETRAPVTAVVFGSPRTGDRGFRDAFHRLRDLRMLRVRNRPDRIPHYPPVGYADVGVELLIDTRLSPFLRR... | Function: Acylhydrolase that catalyzes the hydrolysis of phospholipids at the sn-1 position.
Sequence Mass (Da): 45619
Sequence Length: 408
Subcellular Location: Cytoplasm
EC: 3.1.1.-
|
P0DQD1 | NLYQFKNMVQCVGTQLCVAYVKYGCYCGPG | Function: Relatively highly potent phospholipase A2 that displays potent antimicrobial and hemolytic activities. It does not show cytotoxic effects on the three human cell lines tested. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. It shows similar potencies on both Gra... |
Q8RZ40 | MCCFLLVSVLLATTLTDVASAQRWRQTSGGGKDRWDGLLDPLDADLRRDIIRYGELAQATSDALIGDPASPFAGASRYAPDAFLRKVRASDPDAYRVTRFVYATSSVRLPDAFMPRPAPSAGAAWSGESNWMGYVAVAADGVAAKAGRRDIVVAWRGTKRAVEWANDLDITLVPADGVVGPGPGWTQPSVHRGFLSVYTSKSFSSPFNKLSAREQVLAEITRLLRAYKNENCSITITGHSLGAALSTLNAIDIVANGYNVRGSSRVPVPVTAIALASPRVGDDQFKRAFDSTSNLSLLRVRNAPDIVPTILPSAFFKDVG... | Function: Acylhydrolase that catalyzes the hydrolysis of phospholipids at the sn-1 position.
Sequence Mass (Da): 45328
Sequence Length: 420
Subcellular Location: Secreted
EC: 3.1.1.-
|
B9EYD3 | MSTTAPRAVAERWRELHGEDHWKGLLDPLDADLRRSVIGYGELAQATNDAFIREAWSPHAGACRYSRDRFLEKAQASTQLAGLYEVTAFFYATAGAGGVPAPFMVRNRESNWMGYVAVATDAGVAALGRRDVVVAWRGTVRPMEWLNDLDFTLVSAAGVLGAGGRSPAPRVHRGWLSIYTASDPASKYSKLSAREQISDEIKRLMDKYKDEETSITVVGHSLGAAVATLNAADIVSNGLNQHGACPVTAVAFACPRVGDSGFRKLFDELPGLRLLRVCNSPDVVPKYPPMGYADVGVELPVDTRRSPYLKSPGNQAVWHS... | Function: Acylhydrolase that catalyzes the hydrolysis of phospholipids at the sn-1 position.
Sequence Mass (Da): 43278
Sequence Length: 396
Subcellular Location: Cytoplasm
EC: 3.1.1.-
|
Q5NAI4 | MDKSQGVLLSSNVGAGSRPWPELLGSAHWDGLLDPLDLTLRRLILLCGDLCQVTYDSFNSDSHSKYCGTCRFSRSTLLDRTQFPAAGDLSVAAYLYATSDATAFPGSMVYSMSREAWSKESNWIGYVAVSNDAAAAASGQRVIYVAWRGTIRSLEWVDVLKPDLVDHDDILPEGHPGRGRSRVMKGWYLIYSSTDERSPFSKYSARDQMLAAVRELVARYRNESLGVVCTGHSLGASLATLCAFDIVVNGVSKVGDGAHIPVTAVVFGSPQIGNPEFKKQFEEQPNLRALHVRNMPDLIPLYPSGLLGYANVGKTLQVDS... | Function: Acylhydrolase that catalyzes the hydrolysis of phospholipids at the sn-1 position.
Sequence Mass (Da): 50453
Sequence Length: 465
Subcellular Location: Cytoplasm
EC: 3.1.1.-
|
A2Y7R2 | MSSSPMLGGIADRWRELHGQDSWNGLLDPLDLDLRSSILSYGELVQATYDSFNRERRSPHAGACVYGHGDLLAAAGASAAGSYAVTKFVYATSGLPVPEAFLLLPLPSLLPPAWSRESNWMGYVAVATDEGVAALGRRDIVVAWRGTVESLEWVNDFDFTPVPAAPVLGAAAAANPRAIVHRGFLSVYTSSNKDSKYNKASARDQVLEEVRRLMELYKDEVTSITVVGHSLGASLATLNAVDIVANGANCPPASSSSSQPPCPVTAIVFASPRVGDGFFKAAFASFPDLRALHVKNAGDVVPMYPPLGYVDVAVKLRIST... | Function: Acylhydrolase that catalyzes the hydrolysis of phospholipids at the sn-1 position.
Sequence Mass (Da): 43767
Sequence Length: 407
Subcellular Location: Cytoplasm
EC: 3.1.1.-
|
Q99943 | MDLWPGAWMLLLLLFLLLLFLLPTLWFCSPSAKYFFKMAFYNGWILFLAVLAIPVCAVRGRNVENMKILRLMLLHIKYLYGIRVEVRGAHHFPPSQPYVVVSNHQSSLDLLGMMEVLPGRCVPIAKRELLWAGSAGLACWLAGVIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGTRNHNGSMLPFKRGAFHLAVQAQVPIVPIVMSSYQDFYCKKERRFTSGQCQVRVLPPVPTEGLTPDDVPALADRVRHSMLTVFREISTDGRGGGDYLKKPGGGG | Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-... |
O15120 | MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENMSIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAKRELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGDLLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAADVPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ | Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-... |
Q8K3K7 | MDPWPWLTAALLLLLLLVQLSRTARFYAKVGLYCVLCLSFSAAASIVCLLRHGGRTVDNMSIISWFVRSFKYVYGLRFEVSGQKKLEVDGPCVIISNHQSILDMMGLMEILPKRCVQIAKRELMFTGPVGLIMYLGGVYFINRQQARTAMSVMADLGDLMVKENLKVWIYPEGTRNDNGDLLPFKKGAFYLAIQAQVPIIPVVYSSFSSFYNVKTKLFTSGTIKVQVLDAVPTNGLTDADVTKLVDTCYQSMRATFLQISQIPQENSAIKEPGVLPAQ | Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-... |
A1XRN2 | MRLILLSGLLLLGTFLANGDEKDSDVQMLNSMIEAVMILQRDFANLRHALMTVHNARSFGRGSERLYVTNKEVSKFEGLEEICSQAGGHIPSPQLENQNKAFEDVLERHNKAAYLVVGDSANFTNWAAGQPNEADGTCVKADTHGSWHSASCDDNLLVVCEFYFIL | Function: This phospholipase A2 inhibitor neutralizes the activity of basic PLA2 myotoxins of its own and related venoms. The inhibitory profile shows specificity towards group II PLA2, either belonging to the catalytically-active (D49) or -inactive (K49) subtypes.
PTM: N-glycosylated.
Sequence Mass (Da): 18376
Sequenc... |
P81077 | DEVDPDGKVLNSLIDTLMHLQKEFANLKYAFLTVHKARSFGSGSERLYVTNKEIKNFEPLGDI | Function: Binds to and neutralizes the activities of basic phospholipase A2 (PLA2) myotoxin isoforms.
PTM: Contains 2 disulfide bonds.
Sequence Mass (Da): 7154
Sequence Length: 63
Subcellular Location: Secreted
|
Q8AYA2 | MRLILLSGLLLLGTFLANGDETDPDGQVLNSLIETLMHLQREFANLKYAFLTVHKARSFGSGSERLYVSNKEIKNFEPLGDICSQAGGHIPSPQLENQNKAFANVLERHNKAAYLVVGDSANFTNWAAGQPNEADGTCVKADTHGSWHSASCDDNLLVVCEFYFIL | Function: This phospholipase A2 inhibitor binds directly phospholipase A2 in the presence or absence of calcium. Has anti-enzymatic, anti-myotoxic, anti-edema inducing, anti-cytotoxic, anti-bactericidal, and anti-lethal properties against basic and acidic phospholipases A2 from Bothrops venoms.
PTM: Glycosylated. The g... |
P46925 | MDITVREHDFKHGFIKSNSTFDGLNIDNSKNKKKIQKGFQILYVLLFCSVMCGLFYYVYENVWLQRDNEMNEILKNSEHLTIGFKVENAHDRILKTIKTHKLKNYIKESVNFLNSGLTKTNYLGSSNDNIELVDFQNIMFYGDAEVGDNQQPFTFILDTGSANLWVPSVKCTTAGCLTKHLYDSSKSRTYEKDGTKVEMNYVSGTVSGFFSKDLVTVGNLSLPYKFIEVIDTNGFEPTYTASTFDGILGLGWKDLSIGSVDPIVVELKNQNKIENALFTFYLPVHDKHTGFLTIGGIEERFYEGPLTYEKLNHDLYWQIT... | Function: During the asexual blood stage, participates in initial cleavage of native host hemoglobin (Hb) resulting in Hb denaturation . May cleave preferentially denatured hemoglobin that has been cleaved by PMI . Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthe... |
Q04383 | MSHLFPPSSPVAGKPLESPQKEPGKLANTSVLTLGRKRYNYELEEYPTPDPSSSIGRQSSPVKDITSRLNETKSALSSPSKQEKVLAGPIEIELDASDPSRLAIGRKKSVCNIILPCRKNISRQHAFISYAADRNEIKLECNGTNGLSVHLPYSMQLHLVKPFPTRNFYKLVAEEPLTSQNTKQSHGKTLQKNQNFISFVLAKGETVTFPYIQGSFINFTGVTVCLSLKKVAPYPGDGNNNFDEENSTETEDELCLLTTTSDDFSWQKETPSMKFVPVEHSPRTEQISKPLLIASPALVKNSPISYRTTPQTSFVINQPS... | Function: Binds to the promoters of genes with functions important for the G1/S (start) transition; primarily genes involved in DNA synthesis and repair, chromosome segregation, nuclear division and transcription.
PTM: Phosphorylated by CDC28.
Sequence Mass (Da): 58202
Sequence Length: 521
Subcellular Location: Nucleus... |
Q8IM15 | MNLTIKEEDFTNTFMKNEESFNTFRVTKVKRWNAKRLFKILFVTVFIVLAGGFSYYIFENFVFQKNRKINHIIKTSKYSTVGFNIENSYDRLMKTIKEHKLKNYIKESVKLFNKGLTKKSYLGSEFDNVELKDLANVLSFGEAKLGDNGQKFNFLFHTASSNVWVPSIKCTSESCESKNHYDSSKSKTYEKDDTPVKLTSKAGTISGIFSKDLVTIGKLSVPYKFIEMTEIVGFEPFYSESDVDGVFGLGWKDLSIGSIDPYIVELKTQNKIEQAVYSIYLPPENKNKGYLTIGGIEERFFDGPLNYEKLNHDLMWQVDL... | Function: During the asexual blood stage, catalyzes the cleavage of denatured host hemoglobin (Hb) or globins . Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable).
PTM: Proteolytically cleaved into the soluble active mature f... |
Q8I6Z5 | MNNYFLRKENFFILFCFVFVSIFFVSNVTIIKCNNVENKIDNVGKKIENVGKKIGDMENKNDNVENKNDNVGNKNDNVKNASSDLYKYKLYGDIDEYAYYFLDIDIGKPSQRISLILDTGSSSLSFPCNGCKDCGIHMEKPYNLNYSKTSSILYCNKSNCPYGLKCVGNKCEYLQSYCEGSQIYGFYFSDIVTLPSYNNKNKISFEKLMGCHMHEESLFLHQQATGVLGFSLTKPNGVPTFVDLLFKHTPSLKPIYSICVSEHGGELIIGGYEPDYFLSNQKEKQKMDKSDNNSSNKGNVSIKLKNNDKNDDEENNSKDV... | Function: During the asexual blood stage, plays an essential role in the export of several proteins into the host erythrocytes by cleaving the pentameric localization motif RxLxE/Q/D (termed Plasmodium export element (PEXEL)) located downstream of the N-terminal secretory signal sequence . Specifically, cleaves after t... |
A5K302 | MVGASLGPPGRGSLSRLIRLVICVLTLCALSVQGRSESTEGHSKDLLYKYKLYGDIDEYAYYFLDIDIGTPEQRISLILDTGSSSLSFPCAGCKNCGVHMENPFNLNNSKTSSILYCENEECPFKLNCVKGKCEYMQSYCEGSQISGFYFSDVVSVVSYNNERVTFRKLMGCHMHEESLFLYQQATGVLGMSLSKPQGIPTFVNLLFDNAPQLKQVFTICISENGGELIAGGYDPAYIVRRGGSKSVSGQGSGPVSESLSESGEDPQVALREAEKVVWENVTRKYYYYIKVRGLDMFGTNMMSSSKGLEMLVDSGSTFTH... | Function: During the asexual blood stage, plays an essential role in the export of several proteins into the host erythrocytes by cleaving the pentameric localization motif RxLxE/Q/D (termed Plasmodium export element (PEXEL)) located downstream of the N-terminal secretory signal sequence . Specifically, cleaves after t... |
A0A509AI82 | MTNFCIKSYLFLYLSFLLFFDIITIFHVSSIRISTVLKNDKKKKNFNTSLVEENKKYLFNEIKLNNRFKNDIKGYIQNINNFHSIIESKIPNSLLYVHEDLINFHNSQFIGDIEIGNPPQSFKVVFDTGSSNFAIPSTKCVKGGCTLHNKFDAKKSRTFMSNLKNKKESIYTYVQYGTGKSILEHGYDDVYMKGLKINKQCIGLIIEESMHPFSDLPFDGIVGLGFSDPDNSFQTKYSKSLIETIKEQNLLQQNIFSFYVPKELEKSGAITFGRANSKYAIEGEKIEWFPVISMYFWEINLLGILLPDKNFEICSNKKCR... | Function: During the development in the mosquito midgut, plays a role in sporozoite egress from oocysts.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 50319
Sequence Length: 441
Subcellular Location: Membrane
EC: 3.4.23.-
|
Q8ILG2 | MFFINFKKIKKKQFPIYLTQHRIITVFLIFIYFINLKDCFHINNSRILSDVDKHRGLYYNIPKCNVCHKCSICTHENGEAQNVIPMVAIPSKRKHIQDINKEREENKYPLHIFEEKDIYNNKDNVVKKEDIYKLRKKKKQKKNCLNFLEKDTMFLSPSHDKETFHINHMNKIKDEKYKQEYEEEKEIYDNTNTSQEKNETNNEQNLNINLINNDKVTLPLQQLEDSQYVGYIQIGTPPQTIRPIFDTGSTNIWIVSTKCKDETCLKVHRYNHKLSSSFKYYEPHTNLDIMFGTGIIQGVIGVETFKIGPFEIKNQSFGLV... | Function: During the asexual blood stage, initiates the proteolytic maturation of several rhoptry proteins and thus, is required for merozoite invasion of host erythrocytes and probably the subsequent development of the ring-stage . Cleaves rhoptry associated protein 1 RAP1 and apical sushi protein ASP during schizont ... |
Q8TBJ4 | MAVGNNTQRSYSIIPCFIFVELVIMAGTVLLAYYFECTDTFQVHIQGFFCQDGDLMKPYPGTEEESFITPLVLYCVLAATPTAIIFIGEISMYFIKSTRESLIAQEKTILTGECCYLNPLLRRIIRFTGVFAFGLFATDIFVNAGQVVTGHLTPYFLTVCKPNYTSADCQAHHQFINNGNICTGDLEVIEKARRSFPSKHAALSIYSALYATMYITSTIKTKSSRLAKPVLCLGTLCTAFLTGLNRVSEYRNHCSDVIAGFILGTAVALFLGMCVVHNFKGTQGSPSKPKPEDPRGVPLMAFPRIESPLETLSAQNHSAS... | Function: May play a role in neurite outgrowth and neurogenesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35795
Sequence Length: 325
Subcellular Location: Cell membrane
|
Q6WAY2 | MAVENNTQRSYSIIPCFIFVELVIMAGTVLLAYYFECTDTFQVHIQGFFCQDGDLMKPYPGTEEESFISPLVLYCVLAATPTAIIFIGEISMYFIKSTRESLIAEEKMILTGDCCYLSPLLRRIVRFIGVFAFGLFATDIFVNAGQVVTGHLTPYFLTVCQPNYTSTDCRAHHQFINNGNICTGDLEVIEKARRSFPSKHAALSIYSALYATMYITSTIKTKSSRLAKPVLCLGDLCTAFLTGLNRVSEYRNHCSDVIAGFILGTAVALFLGMCVVHNFKGTQGSASKPKPEDPRGVPLMAFPRIESPLETLSAQNHSAS... | Function: May play a role in neurite outgrowth and neurogenesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35887
Sequence Length: 325
Subcellular Location: Cell membrane
|
Q7TME0 | MQRAGSSGARGECDISGAGRLRLEQAARLGGRTVHTSPGGGLGARQAAGMSAKERPKGKVIKDSVTLLPCFYFVELPILASSVVSLYFLELTDVFKPVHSGFSCYDRSLSMPYIEPTQEAIPFLMLLSLAFAGPAITIMVGEGILYCCLSKRRNGAGLEPNINAGGCNFNSFLRRAVRFVGVHVFGLCSTALITDIIQLSTGYQAPYFLTVCKPNYTSLNVSCKENSYIVEDICSGSDLTVINSGRKSFPSQHATLAAFAAVYVSMYFNSTLTDSSKLLKPLLVFTFIICGIICGLTRITQYKNHPVDVYCGFLIGGGIA... | Function: Postsynaptic density membrane protein that indirectly regulates glutamatergic synaptic transmission through lysophosphatidic acid (LPA)-mediated signaling pathways . Binds lysophosphatidic acid (LPA) and mediates its internalization into cells . Could act as receptor or a transporter of this lipid at the post... |
Q32ZL2 | MPLLPAALTSSMLYFQMVIMAGTVMLAYYFEYTDTFTVNVQGFFCHDSAYRKPYPGPEDSSAVPPVLLYSLAAGVPVLVIIVGETAVFCLQLATRDFENQEKTILTGDCCYINPLVRRTVRFLGIYTFGLFATDIFVNAGQVVTGNLAPHFLALCKPNYTALGCQQYTQFISGEEACTGNPDLIMRARKTFPSKEAALSVYAAMYLTMYITNTIKAKGTRLAKPVLCLGLMCLAFLTGLNRVAEYRNHWSDVIAGFLVGISIAVFLVVCVVNNFKGRQAENEHIHMDNLAQMPMISIPRVESPLEKVTSVQNHITAFAEV... | Function: Induces filopodia formation and promotes neurite growth in a CDC42-independent manner; impedes neurite growth inhibitory-mediated axonal retraction.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35427
Sequence Length: 321
Subcellular Location: Cell membrane
|
Q8BJ52 | MPLLPVALISSMLYFQMVIMAGTVMLAYYFEYTDTFTVNVQGFFCHDSAYRKPYPGPEDSSAVPPVLLYSLAAGVPVLVIIVGETAVFCLQLATRDFENQEKTILTGDCCYINPLVRRTVRFLGIYAFGLFATDIFVNAGQVVTGNLAPHFLALCKPNYTALGCQQYTQFISGEEACTGNPDLIMRARKTFPSKEAALSVYAATYLTMYITSTIKAKGTRLAKPVLCLGLMCLAFLTGLNRVAEYRNHWSDVIAGFLVGISIAVFLVVCVVNNFKGRQPENGHIHRDNVARMPMTNIPRVESPLEKVTSLQNHVTAFAEV... | Function: Induces filopodia formation and promotes neurite growth in a CDC42-independent manner; impedes neurite growth inhibitory-mediated axonal retraction.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35388
Sequence Length: 321
Subcellular Location: Cell membrane
|
B2HNJ0 | MTKPVADTSAVLTSEDTLVLASMGSPVEMQLIMDWLGEQRARTPGAKFDVLKLPPRNAPTAALTALVEQLESGSEAGADRSIVPVQVFWQPPADRSRLAKVAGLLPGRDPYHPNPRQQRRILRSDPQRARVMAGESATVSELRKQWRDNTVGEDQHDFAHFVARRAILALARAEYRILGPQYKSPRLVKPEMLASARFRAGLEKIPGATVEEAGKMLDELATGWSQASVDVFSVLGRLISRGFDPEFDYDEYQVAAMRTALEAHPAVLLFSHRSYIDGAVVPVAMQDNRLPPVHMFGGVNLSFGVMGPLMRRAGMIFIRR... | 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): 88236
Sequence Length: 788
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety ... |
Q2GH18 | MSIISIAVDAMGGDFAPEAVVSGLDFALTNLLDDQNVSFNIYGQGSQVLPILDKYKDLKEHSVFIDTPEVVLANDKPSFALRKRRSSSMWCAIDSIKSGVTSGVVSSGNTGALMAISRFLLGTLPNIDRPAICTALPSRGEEYFVLLDLGANIESSSNALFQFAIMGSAFAKAVLNIASPKVALLNVGQEEVKGTDVIREAFLLLKQAEGRINFCGYIEPIDILGDKVDVVVTDGFCGNIVLKVAESIAYTFKSVFEKSVTSSIISKFAGLLLKSQMKKDFMRFNPKMYNGAMLLGLNGVVVKSHGNADKVAFAHAIKVT... | 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): 36251
Sequence Length: 337... |
B2KC86 | MRIALDASGGDFGYQPNILGAARAVKELKCEVILVGDEKVLKEQLASLGLSDLKGLSVEHAPDVIDMDADPAKEVRSKKNASVVVAADLVKQGRAKAFVSAGNSGATMVAALMKMGRIEGVLRPAIGAPLPTVKGLMLLLDAGANAECKPQHLMQFAVMGSIYTQKVFGIRKPKVGLLSIGEEEGKGNDLVKETYPYLSNLGINFCGNVEGRDLPFGTTDVVVTDGFTGNVCLKLEEGLAKAMFHMIKGEIKKNPIAMLGAMLAKPAFASVKKITDPDTAGGAPLLGVDGVAIVSHGKSSETAVFNAVRTAKRLVDSGFV... | 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): 36050
Sequence Length: 341... |
B1H0Q6 | MIIALDAMGGDFAPASTVEGAIFAAKESKHKILLVGIEKILVGELLKYRGRYDLKSLNIEIINATEFITMDEHPAKAVRQKKDSSLSVCARLVADGKADAFVSMGNSGAAMSAALFYLKRIEGVLRPAISTVFPNFGGHCIIADMGANVDCTPEYLLQFGIMASLFCEKVASVENPRVGLVSIGEESTKGNELTLAAFELLKKADINFIGNVEGRDIPGGKVDVAICDGFVGNVILKLGEGLTEMMLKLIRKEFKQHPMTWASLPFLWLAIKDLRKRVDYSEFGGAPLLGVEGVCIIGHGSSNGKAVKNAIFAGAETAKH... | 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): 36289
Sequence Length: 338... |
Q82ZE8 | MKIAVDAMGGDNAPQAIVEGVMLAKQDFPDIEFQLYGKEAEIKKYITDEKNITIIHTDEKIASDDEPVKAIRRKKTASMVLAAQAVKNGEADAIFSAGNTGALLAAGLFIVGRIKNVERPGLMSTLPVMGEPDKGFDMLDLGANADNKPEHLVQYAVLGSFYAEKVRNVQNPRVGLLNNGTEETKGSELTKKAFELLAADETINFVGNVEARELLNGVADVVVTDGFTGNAVLKSIEGTAMNMMSLLKTAILSEGVKGKMGALLLKNALHGMKDEMDYSKHGGAVLFGLKAPVIKTHGATGPDAVRYTIRQIHTMLETQV... | 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): 35835
Sequence Length: 333... |
Q2RTS9 | MSNSLVISVDAMGGDDAPDMVVDGVKLARKRFPDVRFLLFGDEARIGPLVAGDSALSAVCTIRHTASAVSGDAKPSQAVRSGRQSSLWLSIEAVKKGEAAGVVSAGNTGAFMAMAKLILRTLPGIDRPAIATLLPTLRGESVVLDLGANAECNANNLVEFAIMGEVFARTVLSLDRPTVGIMNIGSESGKGTDTVRDASARLQDSALPIRFMGFVEGDDLGKGTVDVIVTDGFTGNVMLKTAEGTAKLYSQFLRNAFLSSLLARLGYLLSRSALQKVKARTDPRRYNGAMFLGLDGVAVKSHGGTDALGFSNALAVAIDL... | 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): 36570
Sequence Length: 349... |
Q1AW88 | MRIAVDALGGDNAPQEIVAGALAAARRLPGVEILLVGEPGAVEPLLERAPGNVSLRPSGGAVRMDEEPAAALRSRPDASVAVAARLVRSGEADALFSAGNTGAAVAASLLYIGRIGGCRRPAIATVLPFSHPTLLLDVGATVSCRAQDLLNFAILGSVFARRYLETEGAPRVGLLNVGEEPGKGHDLAREAHRLLAASPQVEFAGNVEGRDLGSGRADVVVTDGFTGNAVLKTAEGVARECLRLVREALLGSLAGRVAALAARPRLLAVRDRVDPENYGGSFLLGVRGAVVIGHGNSTARGVENALAGIARAGGGLVAEL... | 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): 34276
Sequence Length: 336... |
Q21K90 | MSEEIHLSVDAMGGDFGPRLCVEAAASFIAKHSNVRITLVGDKAAVSSCIPPQADLSRLHVLHADQVVDMADKPSHALRHKKNSSMWRALQLVADGEAQACVSGGNTGALMAIGCHLLKTIAGIDRPAIAKQIPTARGSSVLLDLGANLECSPQQLFQFGLMGQGLARVYGKSEPTVALLNVGSELTKGNDIIQDTAQLMGDCADMHFRGFVEGDSLYSGEVDVVVCDGFIGNVALKVSEGVAKFVFGDLRSRIGRGVRSRLLAWLAKPVLKPWAEQFRPAKYNGAALLGLKGVVIKSHGGADAEGFEQALYVALEQASA... | 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): 35895
Sequence Length: 341... |
Q2RIV5 | MWLLALVVAYLIGSIPTAYVVGRYLYGFDIRRRGSGNVGATNTLRTMGTIPGLVVLGVDALKGVLAVLLGQALGGPVLVILAALMAIVGHNWSIFLEFQGGRGVATTAGALLAMAPLALFWAFLIWLAVVIFSRYISLGSIVAAAVAPFLVIYFHRPWPYVLFTFVAAALVIYRHRPNIKRLLAGTEHKLGERS | 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... |
Q1MGK1 | MVFWIAGAVGLAIAYLLGSTPSGYLAGKLIRGIDIREHGSKSTGATNVLRTLGKWPALVVLLVDVLKGVGAVVFARWFYSWFSTLSSGMPPTALDLQSLEPWAVCLTGLAVLLGHGRSVWLNFTGGKSVAAGLGVLLAMSWPVGLGAAMVFGVALAISRIVSLSSMLAALTAIALVCGLEQPLPYRLLVIAGGIYVIARHRTNIRRLLAGTEPRLGKVA | 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... |
Q9X1F9 | MGWWLFPILGYFIGSIPFSYLIPKWLKGIDVRKVGSGNVGATNAIRTTGPAVGGICLLLDALKGFFPVFITITFSGDSKIVSLTAIATVLGHDFPIFMKFKGGKGVASTLGIIFCLSWPTGLVFTLTWLVIVMLTKYASLGSLVALYVSALLGYLLKGYDTGMLFLILAVLSTLRHSENIQRLLNGTERKVNLFKR | 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... |
Q81Y92 | MVTTYLLFIVAYLLGSIPFALVVGKIGYGIDIREHGSGNLGGTNTFRTLGKKAGFTVTIADILKGTLATSLPMVFGLDIHPLWFGLAAVLGHVYPIFAKFRGGKAVATSAGVLLCYSPVVFAILAVVFFTLLFTTRYVSLSSMVTAVVAVIASIVTGDKIFIIAMCLLAGMVIYKHRANIGRIINKTEPKANFSKKQK | 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... |
Q3Z6P4 | MLIAKLLLVVIVSYLLGSIPFGYLVSHRGSKIDIRSYGSGRTGATNVLRTMGRKAALLVAALDVVKGVSAVAFAGLVIGTEALTFGTNGMAILFAQVLAGLAAVAGHIWPVFLKFRGGRGVATFFGGMIALCPVAAIFGGEVLIIGAGLSGFASLGSITGVVGAYALLIPLTFISGFPTEYIVYAVLGSLLITIMHRDNIKRLLAGKERKLNEKSR | 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... |
Q3Z6K1 | MPLLFVLLSYLLGTFPSAYLAGYLSTDRDIRLMGDHNMGAQNAYRCLGRGWGLAVFVFDLAKGSLAITLALAAGLSPGWVMFCGLAAVLGHNWPVWLGFRGGRGEATAIGVMLLIATQPMLIMGGLGLLVLLFTSSVIAASAVMFGLLWLAVILYGLPGGVVAYSIGLPVVVGLTHFIRSRKNRL | 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... |
Q3Z643 | MSLVFIIMAIAGYLVGAIPMAYLLSRWRRGIDIRRYGSGNVGASNVVKTAGKRLGLAVFIFDVSKGAVMILLSGALGLALWQQIVVGLFTIAGHNWPVFLRFNGGRGIATSLGVALVMAPVPALIALGTAIAFGLFKKMAPGVFLGVAALPFMSGYFHGFFGIREYQTISWGFIGIFLIMVTRRLMAPDNEYAHTVSKAELIFNRMFLDRDIRSRSVWINRNSAPAEESPNIL | 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... |
Q8L3A1 | MNMQILWIIIAIICSYLIGAIPFGYIIPKLFKGIDIREHGSKNVGSTNVLRVLGAKYGIPTFLLDCFKGALPIIIIRYMLGMPELFLISDTYDISIVFGAAAAIGHIKSIYIGFKGGKAVATGVGAVIAINPIIGLSGIGLFFIVAFSTKYVSIGSVVASFSVAVMMWIGVLIKEIWIPVPNLTISYESQIINLVAISLIVLLIIYMHKKNFIRLMNGTENKIGQKKIQNITK | 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... |
A3N1Y9 | MSITVYLLIVFAYLLGSVSSAIIFCRLAGLPDPRENGSHNPGATNVLRIGGKFSALGVLLFDILKGGLPVLLAFNFKLEPSEIGLIALAACLGHIFPLFFRFRGGKGVATAFGALLSISFAASAAGLCTWLIVFLLFGYSSLSAVITALIMPFYIWWFLPEFTFPVALVCCLLVYRHHDNIQRLWRGQEQPMWARK | 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... |
A4SI95 | MTALTILMIILAYLGGSLSSAVLVSRITGLPDPRDHGSHNPGATNVLRLGGRVAALVVLLLDVLKGTAPVYLAWYLQIKPVYLGFIGVAACLGHMYPIFFHFRGGKGVATALGTMMPIGFTMGGAVIGTWLVVLLVSGYSSLASIITVLLSPLFTYLIKPEYTLPVSLLSCLILIRHHENIARLLKGEEPRVWGRQAQRRQEEVGEMDDVAQKRDERDKK | 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... |
Q8UFU1 | MSALTDWQTAPALLALAALIGYLLGSIPFGLILTRMAGLGDVRKIGSGNIGATNVLRTGNKKLAAATLLLDALKGTAAVLVANALWGYEASLVAGFFAFLGHLFPVWLGFKGGKGVAVYIGVLLGAAPLMMLAFALIWLATAFITRYSSLSALLAMLIIPVALWVLGPEKTAMLVTLLSVISWWKHRENIRRLMAGTESRIGQKG | 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... |
Q21UZ2 | MRQQENFLESMQSFFPLAATLLGYLIGSLSFAVIVSRVMGLNDPRTFGSKNPGATNVLRSGSKTAAIVTLLLDAAKGWLPVMLVRWYGKPYGMEEGTMALVGLAAFIGHLYPVFFNFAGGKGVATALGVLLGLSPILALATGATWLIMAYFFRYVSLASLTAAVFVPVYYVFGDGMAWYLSKGVLAALCAMSLLLIYRHAENISRLIKGTESRLGKKARTERKS | 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... |
Q1IPR1 | MKTFVPIALLAYLCGSIPFGFILVKLFLKADVRQTGSGNIGATNVARTGAKGLAVLTLLLDAVKGWVAVFAATIFIARVSNPANVDVRLIPAFAGLCAILGHLYPVWLKFKGGKGVATALGVFLALAPTPIGIVLGLFALVVLLTHYISLGSILAAAAFPFVVYFLYRNQYPAATYAIMGASSLLIIWRHRSNIQRLIAGTENRFPASKPTEGKA | 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... |
C5CIV2 | MRFIWLAIIGYLFGSIPWGYIIPKLRGIDIRKVGSGNVGGTNVLRNLGGFWGAITMVLDGFKPFIPIMIAKHTFGVSVSDAMMIGFFAGVGHCYPIWLKFKGGKSVAVSVGTISGTKASLVPVFFAVWLPIVLITQYVSLGSILSLAVITILYFLTDSWQTGIWMLALFLLTTYRHRGNIVRLIRGEERKTDLIAAFTKRNKNKKEG | 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... |
Q9CGW4 | MLTIILLLIASYLLGAIPFGLWIGKIFFKKNLHDYGSGNTGTTNTFRILGVKAGISVFAFDLLKGTLATLLPLFFHINGVSPLIFGLLAVIGHTFSIFDRFKGGKAVATSAGVILGFSPLFLIYLLVVFIIVLWLFSMISLSSVIGAVFALLGILIFPSIGFILTSYDLLFSIIIFVLAIIIILRHRTNLKRIKNHCESLVPFGLNLSKQKEK | 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... |
Q88W28 | MKIIIMLIIAYLIGAIPSGVIIGKFFFHTDIRQAGSGNIGTTNTYRVLGPTAGTIVMVMDILKGTIAALQPTLLFHMNNRYTLLIGLAAILGHTFSIYIGFKGGKAVATSAGILLAYNWEFFLIASAIMLLLVYTTSMVSVASMTAFPIVTLIAIFYYQDWLLSLVAFALTLFIFYRHRSNIARIKNGTESLVHFGLGWRRQQRANRK | 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... |
Q5ZT09 | MALFIFLILVGYLMGSINSAIIVCRTFGLPDPREEGSKNPGATNVLRLGGKQYGIMVMVFDALKGILPVILAKFLSAEPVTVAFTALAAVVGHMYPVFFHFRGGKGVATTIGALLAFHFIIGVMVAATWLLVANFWRYSSLASIASISLAPFYSLILVGNLNIFPPLFMITILVLYKHRDNFNRLIDGKEPKIKFKHSVIEEIMEASPATSAEQEFPGKEVIDTNIDETEKTEQAEAVKKPKVKKATTKAKKTTSKEETTKKPKSTKPKTKTVKEKE | 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... |
A6LL73 | MEYIYSIFIGYFFGAIPFSFFIAKLKGIDIRKTGSGNVGGTNVLRNAGAFYGALAFFFDIFKAYIAVFLVKGFGIKFMLIAGTMAVLGHCYSIFLKFKGGKGVASTFGVFLAVYPWSGLVFFGVWLFIVAVTKYVSLASMIGLIFASIFVFFAGKDFWVIFLALSLFSILRHKDNIQRLINGNERKTDVIGYFFGKGKKN | 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... |
B0K8N4 | MYAVLTAIIAYLIGCINNAYILTKYTRKIDIRNYGSGNAGATNVLRVLGYKAAAPVFALDVLKGVIAVLIGKYLMGNTGAMIAGIAVVCGHNWPVFLKFRGGKGIATSVGVVMTVSPLLGLIALAIGVTVIVLTKYVSLGSITGSVTFVLLNAIFWNSTQIFIFSLILASLAIFQHRSNIKRLLAGTESKLGQKTEIK | 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... |
B8GPT8 | MLLASALVLGAYLLGSVSTAILVCRLAGLPDPRSQGSGNPGATNVLRTGRKGAAIITLLGDLLKGLVPVLVAHALGLEPVWIAAVALAAFLGHLFPVYHGFRGGKGVATALGVILGIQAWVGLAALATWLIVAAISRISSLSALTAATLTPVYMYLLTGERWYVAAGVLLAALIYWRHRANIRRLLRGEEPKIGNKTKNKSEV | 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... |
B5ZBQ1 | MDQVYSVAMAYILTLIISPLYSYLIGSLNASIILSLLLKKQDIRHFASKNAGMTNMTRVYGKKLGILTLFLDIVKPIITISLTYIIYKYALNAPFVLSNGFNQAILVYFGGIFTIIGHCYPIFFKFQGGKGVASYGGFLITIDPIVAVIGIITLLIILLITKYMSLSAMITATITCFLVLIPGINYIPYYNEHFVEYLFDLNHVIKGTWYVWLFLLISASILIYRHKTNILSIATKQERKTFLFQPKPKNNI | 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... |
B7VIV7 | MTPLALIMIIAAYLLGSISSAVLICRLLRLPDPRTVGSNNPGATNVLRVGGKGAAAAVLLCDMLKGTIPVWLGYYLKIDPIILGVVAIAACLGHMYPIFFHFKGGKGVATALGAIAPIGFDLTGMIMATWLVVAFLFRYSSLAALVTVLLAPFYAWLVKPQYTLPVAMLCCLIVLRHHQNIRRLLDGSEPKLGQKKSA | 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... |
Q51915 | MTKPSTFTACKLASAVFGALLFSSVPAHAADIWLDVATTGWATQNGGTKGGSRAAANDIYTVKNAAELKKALSASAGSNGRIIKITGIIDVSEGKVYTKTADMKVRGRLDIPGKTTIVGIGSNAEIREGFFYAKENDVIIRNITVENPWDPEPIFDKDDGADGNWNSEYDGLTVEGANNVWVDHVTFTDGRRTDDQNGTEHERPKQHHDGALDVKNGANFVTISYSVFKSHEKNNLIGSSDSRTTDDGKLKVTIHNTLFENISARAPRVRYGQVHLYNNYHVGSTSHKVYPFSYAHGVGKNSKIFSERNAFEIAGISGCD... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Plays a role in bacterial invasion of plants.
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): 40812
Sequence Length: 380
Pa... |
P40972 | MDVYRIRISVFFLLVLLTFAALTTATNIPRRQLSNKKYKGPCRAENAIDKCWRCDPNWAENRQKMADCALGFGSNAIGGKLGRIYVVTDNSDDDVVDPKPGTLRYGVIQKEPLWIIFGKNMKIKLSRELIVTSNKTIDGRGFNVHIQNGAGIKIQSASNIIISNLRIHNIVPTPGGLLRESEDHVGLRGSDEGDGISIFSSHDIWIDHISMSRATDGLIDAVAASTNITISNCHFTDHEKVMLFGANDHYVLDKDMKITLAYNHFGKRLDQRMPRCRFGFFHLVNNDYTHWERYAIGGSSGATIISQGNRFIAEDELLVK... | 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): 44352
Sequence Length: 397
Pathway: Glycan metabolism; pectin degradat... |
O24554 | MATTILPLILFISSLAIASSSPSRTPHAIVNEVHKSINASRRNLGYLSCGTGNPIDDCWRCDPNWANNRQRLADCAIGFGKNAMGGRNGRIYVVTDPGNDDPVNPVPGTLRYAVIQDEPLWIIFKRDMVIQLRQELVMNSHKTIDGRGVNVHIGNGPCITIHYASNIIIHGIHIHDCKQAGNGNIRNSPHHSGWWTQSDGDGISIFASKDIWIDHNSLSNCHDGLIDAIHGSTAITISNNYMTHHDKVMLLGHSDSYTQDKNMQVTIAFNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSASPTIYSQGNRFLA... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Function: Involved in the degradation of pectin. May assist in the removal and modification of an existing pectin matrix in order to allow the deposition of newly synthesized walls polymers for a specialized function or to create an architecture that is extensibl... |
B2FHL8 | MSLPLRLALLPTLLASASAFAACPAPPPGQPDIRAIGYYTDKAGSVIDPALQQQNKDATAPLDRYAADVARMSDDYLRNGDPAAAQCTLSWLGAWADDGAMLGQMIRVNNDQSFYMRQWMLDAVAMAYLKVHDQANPQQRARIDPWLQKLARANLAYWDNPKRRRNNHYYWGGLGVLATGLATDDDALWQAGHAAFQKGIDDIQDDGSLPLEMARGQRALHYHDYALAPLVMMAELARLRGQDWYASRNHAIDRLARRVIEGSRDPAWFNQHTGAAQLPLQASGWVEFYRLRSPDGGVFDAAHARGPFHSPRLGGDLTLM... | Function: Polysaccharide lyase that catalyzes the depolymerization of several anionic polysaccharides via a beta-elimination mechanism. Exhibits broad substrate specificity, catalyzing the degradation of not only alginate and poly-beta-D-mannuronate (poly-ManA), but poly-beta-D-glucuronate (poly-GlcA or poly-GlcUA) and... |
Q6L4D2 | MAGVGRTMIAPLLVLNLIMYLIVIGFASWNLNHYINGETNHPGVAGNGATFYFLVFAILAGVVGAASKLAGVHHVRSWGAHSLAAGAASALIAWAITALAFGLACKEIHIGGYRGWRLRVLEAFVIILAFTQLLYVAMLHGGLFSGNHAAGAGGYGGDYPADHHHKPAAAARV | Function: May be involved in abiotic stress response through abscisic acid-dependent signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18055
Sequence Length: 173
Subcellular Location: Membrane
|
Q26616 | MKLLAILLVLPALCFGQRHEGPGMGPGMGPGMGPGMGPGMGPGMGPGMGPGMGPGQGQGQGQGQGQVGGSKCKGGWFLIGQQCFKMMSRALKWNDAELMCEQNAPCGTPVLGGVMTIPDIQTSNAVINHLKSLSSTAMAIDIPFWTGLHNKWNALLERYEGWKWPAGWSTTQQPLRFVNWAPREPNNQLLDQQHSYCARMNRMGQWYVVRCDEPMYFACSMPVSPPLVGGANTNPGMGMLVENPAPIINGYTEFESGLLMRNGVGGP | Function: May play a role in the regulation or execution of skeletal growth.
Sequence Mass (Da): 28580
Sequence Length: 267
Domain: The repetitive domain may provide a calcite binding matrix.
Subcellular Location: Secreted
|
Q76P23 | MSEKIHITQNSGNVDHTVEALGHAISGGVAGMAAIALTYPFSTVSTRLQVQQKKQQQGQQSEITTVPYKNSIDAFKRIIKEENWRTLYSGLKSALIGIGASSFVYYYWYTLLKSISLKLKNKQELGTIENLAIAALAGCANVLTTLPIWVVNTRLQINSDKGIVGQFKYIIKNEGFGGLYKGLIPALILVSNPSVQFVSYEKLRALWRRQSGRTKLGGLEVFILGAIAKLIAGIVTYPYLLVKSRLQSQSGNASNPESQQQQYKGTLDAIGKIFKSDGFLGFFKGMPSKMVQTVIGAAFMFLVKDKVVIHAVAILFYLKR... | Function: May have transport activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36316
Sequence Length: 329
Subcellular Location: Peroxisome membrane
|
O43808 | MASVLSYESLVHAVAGAVGSVTAMTVFFPLDTARLRLQVDEKRKSKTTHMVLLEIIKEEGLLAPYRGWFPVISSLCCSNFVYFYTFNSLKALWVKGQHSTTGKDLVVGFVAGVVNVLLTTPLWVVNTRLKLQGAKFRNEDIVPTNYKGIIDAFHQIIRDEGISALWNGTFPSLLLVFNPAIQFMFYEGLKRQLLKKRMKLSSLDVFIIGAVAKAIATTVTYPLQTVQSILRFGRHRLNPENRTLGSLRNILYLLHQRVRRFGIMGLYKGLEAKLLQTVLTAALMFLVYEKLTAATFTVMGLKRAHQH | Function: Peroxisomal transporter for multiple cofactors like coenzyme A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN) and nucleotide adenosine monophosphate (AMP), and to a lesser extent for nicotinamide adenine dinucleotide (NAD(+)), adenosine diphosphate (ADP) and adenosine 3',5'-diphosphate ... |
Q9FM79 | MKVEAFIPAVLLLCFGVMLCLKSSCALQIGNNNELKNYISWEDLRVVEDGRIERSFSIKENSNWVTTNANANANATNVRRVIVVDKNGGGDSVTVQGAVDMVPDSNSQRVKIFILPGIYREKVIVPKSKPYISFIGNESYAGDTVISWSDKASDLGCDGKELGTYRTASVSIESDFFCATAITFENTVVAEAGEQGRQAVALRIIGDKAVFYRVRVLGSQDTLFDDNGSHYFYQCYIQGNVDFIFGNAKSLYQDCDIHSTAKRYGAIAAHHRDSETEDTGFSFVNCDISGTGQIYLGRAWGNYSRTVYSNCFIADIITPV... | Function: Pectinesterase required for cell type-specific pectin degradation to separate microspores.
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): 42475
Sequence Length: 380
Pathway: Glycan metabolism; pectin de... |
Q8L7Q7 | MDSPTLPHSISASSSTPFASAAVKPHRNKLLSRNGILIIIAASCILLLLISLLIYATVSKSSRNHHNPSHQTPTSDDHPPPETPPSPPPIAQIRLACNATRFPDHCVASLSKPGQVPPDPKPVQIIHSAISVSYENLKSGQSKIQSILDSSAGNRNRTNIATICLEILSYSQHRTESTDIAVTSGDIKDARAWMSAALAYQFDCWSGLKTVNDTKQVVDTITFFEGLVNLTGNALSMMLSFDSFGDDVVSWIRPATERDGFWEKAGPSLGSGTGTEASLGFPSGLTEDVTVCKNGGKDCKYKTVQEAVDSAPDTNRTVKF... | 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
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65478
Sequence Lengt... |
Q4PSQ5 | MKRVASYNYKIVCMVVMTLFVYGYSAAAEQIAYTITVDLNGGGNFTTVQSAIDSISPPNHNWIRVFTQNGIYREKVTIPKEKGFIYLQGKGIEQTVIEYDDHQATDISATFTAFADDIVISGITFKNTYNIVPNNKREIVPAVAARMLGDRYVVTDSSFVGLQDTLFDGKGRHYYKRCIISGGIDFIFGYGQSLFKECTLNMTLGIYAPDNPYGTITAHQRPSPSDEGGFVFSDCTVTGVGKTLLGRAWGSNARVIFDRSRLSDVVLPIGWDAWRAKGNERDLTFVEAGCTGAGADTSQRVPWLKKLSLSEVDGFASVSF... | 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): 37017
Sequence Length: 336
Pathway: Glycan metabolism; pectin degrad... |
Q9LSP1 | MGHRTRMILVLTLVVMSIWGSDASAMQKTKFDAPLLTEKIATNRSIIVDIEGKGDYTSVQKAIDAVPVGNSNWIIVHVRKGIYKERVHIPENKPFIFMRGNGKGKTVIESSQSSVDNVASATFKVEANHFVAFGISIRNDAPVGMAFTSENQSVAAFVAADKVAFYHCAFYSLHNTLFDNKGRHYYHECYIQGSIDFIFGRATSIFNNCEIFVISDKRVKPYGSITAHHRESAEEKTGYVFIRGKVYGIDEVYLGRAKGPYSRVIFAKTYLSKTVVPDGWTNWSYHGSTQNLYHGEYKCHGPGAERQKRSDWAKDLTKQE... | 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): 38812
Sequence Length: 344
Pathway: Glycan metabolism; pectin degrad... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.