ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q6ZIB5 | MIGWGDVYKVVGAMAPLYFALGLGYGSVRWWRFFTAEQCAAINTMVVYFSMPFFTFDFVVRTDPFAMNYRVIAADAVSKAIAIAAMAAWARTRCGCAAAKAGAQSWSITGFSLAALNNTLVVGVPLLDAMYGRWAQDLVVQIAVVQSMVWFPLLLMAFELRKAWVVGGGGGVGPAVMSSSSPPEKQSDVEMNGAVVAAPGGGGGVRLPFWATARTVGLKLARNPNVYASVLGVVWACIAYRWHLSLPGIVTGSLQVMSRTGTGMSMFSMGLFMGQQERVIACGAGLTALGMALRFVAGPLATLVGAAALGLRGDVLHLAIIQAALPQSIASFVFAKEYGLHADVLSTAVIFGTLISLPILIAYYAVLGFV | 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 | MINCGDVYKVIEAMVPLYVALILGYGSVKWWHIFTRDQCDAINRLVCYFTLPLFTIEFTAHVDPFNMNYRFIAADVLSKVIIVTVLALWAKYSNKGSYCWSITSFSLCTLTNSLVVGVPLAKAMYGQQAVDLVVQSSVFQAIVWLTLLLFVLEFRKAGFSSNNISDVQVDNINIESGKRETVVVGEKSFLEVMSLVWLKLATNPNCYSCILGIAWAFISNRWHLELPGILEGSILIMSKAGTGTAMFNMGIFMALQEKLIVCGTSLTVMGMVLKFIAGPAAMAIGSIVLGLHGDVLRVAIIQAALPQSITSFIFAKEYGLHADVLSTAVIFGMLVSLPVLVAYYAALEFIH | 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 . Involved in unfolded protein response (UPR) activation . Involved in the control of vein patterning . Promotes vein formation . PIN5, PIN6, and PIN8 control vein network geometry, but they are expressed in mutually exclusive domains of leaf vascular cells .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38573
Sequence Length: 351
Subcellular Location: Endoplasmic reticulum membrane
|
Q9SQH6 | MITGNEFYTVMCAMAPLYFAMFVAYGSVKWCKIFTPAQCSGINRFVSVFAVPVLSFHFISQNNPYKMDTMFILADTLSKIFVFVLLSLWAVFFKAGGLDWLITLFSIATLPNTLVMGIPLLQAMYGDYTQTLMVQLVVLQCIIWYTLLLFLFELRAARLLIRAEFPGQAAGSIAKIQVDDDVISLDGMDPLRTETETDVNGRIRLRIRRSVSSVPDSVMSSSLCLTPRASNLSNAEIFSVNTPNNRFFHGGGGSGTLQFYNGSNEIMFCNGDLGGFGFTRPGLGASPRRLSGYASSDAYSLQPTPRASNFNELDVNGNGTPVWMKSPAAGRIYRQSSPKMMWESGQRHAAKDINGSVPEKEISFRDALKAAPQATAAGGGASMEEGAAGKDTTPVAAIGKQEMPSAIVMMRLILTVVGRKLSRNPNTYSSLLGLVWSLISFKWNIPMPNIVDFSIKIISDAGLGMAMFSLGLFMALQPKMIPCGAKKATMGMLIRFISGPLFMAGASLLVGLRGSRLHAAIVQAALPQGIVPFVFAREYNLHPDLLSTLVIFGMIVSLPVTILYYVLLGL | 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-formation-promoting functions of PIN5 . PIN5, PIN6, and PIN8 control vein network geometry, but they are expressed in mutually exclusive domains of leaf vascular cells .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62044
Sequence Length: 570
Subcellular Location: Endoplasmic reticulum membrane
|
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-phospho-L-seryl-[protein]
Sequence Mass (Da): 31979
Sequence Length: 272
EC: 2.7.11.1
|
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 | MDTTLQDPLVGQVLDGRYRVDARIAVGGMATVYRAVDTRLDRVLALKVMHPSLAADASFVERFIREAKSVARLAHPNVVQVFDQGTDGAYVYLAMEYIAGCTLRDVLRERGALQPRAALDILEPVLAALGAAHRAGFVHRDMKPENVLIGDDGRVKVADFGLVRAVDSVTNTTGTVLGTVSYLAPEQIEHGTADPRVDVYACGILLYEMLTGEKPHDGDSPAIVLYKHLHDDVPPPSAAVPGMAYELDELVASATARGPEVRPHDAVALLARARDARARLGDEQLDAVPPQALASEHDNADDRTSVIPRALTVRRPLPVNEEDEGADAAHRTSRFRSPPPLPPRGRTALRRGPMAIVIGVLLVLGLGAGVWYINSGQFTKVPPLLAKTEKEARDRLADAGLDAGQVSEAYSDTVERGSVATDPEAGARIRTNDSVSLTLSKGPRTVRVPDLDGYPQDKARSLLEDEGLKPGMSTREFSDSVPAGSVISTEPGKGTEVRAGSAVALTVSKGAPVDVPDVAGDDLEDARAELEEAGLEVKVATERVTSEYDAGRVARQDPGPGGRVAEGDTVTLTLSKGPEMAEVPDVVGDSVGEAREKLEGAGFRVDEDRGLLGLFGDTVKGQSVDGGDSAPKGSTITIEIR | 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 | MSEEPTVSPPSPEQPAAQPAKPARPAARRAPRKPATRRPRVASPAQKAREEIQAISQKPVALQVASAPHGSSEDSTSASLPANYPYHTRMRRNEYEKAKHDLQIELLKVQSWVKETGQRVVVLFEGRDAAGKGGTIKRFMEHLNPRGARIVALEKPSSQEQGQWYFQRYIQHLPTAGEMVFFDRSWYNRAGVERVMGFCSPLQYLEFMRQAPELERMLTNSGILLFKYWFSVSREEQLRRFISRRDDPLKHWKLSPIDIKSLDKWDDYTAAKQAMFFHTDTADAPWTVIKSDDKKRARLNCIRHFLHSLDYPDKDRRIAHEPDPLLVGPASRVIEEDEKVYAEAAAAPGHANLDIPA | 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-fold greater than the rate of polyP synthesis.
Catalytic Activity: [phosphate](n) + GTP = [phosphate](n+1) + GDP
Sequence Mass (Da): 40788
Sequence Length: 357
EC: 2.7.4.34
|
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): 34847
Sequence Length: 300
EC: 2.7.4.-
|
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
Sequence Length: 306
EC: 2.7.4.1
|
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 Length: 301
EC: 2.7.4.-
|
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: Autophosphorylated at His-115 and His-247 using polyP as a phosphate donor.
Catalytic Activity: [phosphate](n) + GTP = [phosphate](n+1) + GDP
Sequence Mass (Da): 34124
Sequence Length: 295
EC: 2.7.4.-
|
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 | MDTETIASAVLNEEQLSLDLIEAQYALMNTRDQSNAKSLVILVSGIELAGKGEAVKQLREWVDPRFLYVKADPPHLFNLKQPFWQPYTRFVPAEGQIMVWFGNWYGDLLATAMHASKPLDDTLFDEYVSNMRAFEQDLKNNNVDVLKVWFDLSWKSLQKRLDDMDPSEVHWHKLHGLDWRNKKQYDTLQKLRTRFTDDWQIIDGEDEDLRNHNFAQAILTALRHCPEHEKKAALKWQQAPIPDILTQFEVPQAEDANYKSELKKLTKQVADAMRCDDRKVVIAFEGMDAAGKGGAIKRIVKKLDPREYEIHTIAAPEKYELRRPYLWRFWSKLQSDDITIFDRTWYGRVLVERVEGFATEVEWQRAYAEINRFEKNLSSSQTVLIKFWLAIDKDEQAARFKARESTPHKRFKITEEDWRNRDKWDDYLKAAADMFAHTDTSYAPWYIISTNDKQQARIEVLRAILKQLKADRDTD | 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 monophosphates, with lower efficiency. Cannot use low-molecular weight polyP as donors. Can also catalyze the synthesis of polyP from ADP or GDP, with lower efficiency.
Catalytic Activity: [phosphate](n) + ADP = [phosphate](n+1) + AMP
Sequence Mass (Da): 55838
Sequence Length: 475
EC: 2.7.4.33
|
Q504Y2 | MRRRRAAVAAGFCASFLLGSVLNVLFAPGSEPPRPGQSPEPSPAPGPGRRGGRGELARQIRARYEEVQRYSRGGPGPGAGRPERRRLMDLAPGGPGLPRPRPPWARPLSDGAPGWPPAPGPGSPGPGPRLGCAALRNVSGAQYMGSGYTKAVYRVRLPGGAAVALKAVDFSGHDLGSCVREFGVRRGCYRLAAHKLLKEMVLLERLRHPNVLQLYGYCYQDSEDIPDTLTTITELGAPVEMIQLLQTSWEDRFRICLSLGRLLHHLAHSPLGSVTLLDFRPRQFVLVDGELKVTDLDDARVEETPCAGSTDCILEFPARNFTLPCSAQGWCEGMNEKRNLYNAYRFFFTYLLPHSAPPSLRPLLDSIVNATGELAWGVDETLAQLEKVLHLYRSGQYLQNSTASSSTEYQCIPDSTIPQEDYRCWPSYHHGSCLLSVFNLAEAVDVCESHAQCRAFVVTNQTTWTGRQLVFFKTGWSQVVPDPNKTTYVKASG | 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 and quantitatively secreted from platelets in response to stimulation of platelet degranulation . May also have serine/threonine protein kinase activity. Required for longitudinal bone growth through regulation of chondrocyte differentiation. May be indirectly involved in protein transport from the Golgi apparatus to the plasma membrane (By similarity).
PTM: N-glycosylated.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 54132
Sequence Length: 493
Subcellular Location: Secreted
EC: 2.7.10.2
|
Q5RJI4 | MRRRRAAVAAGFCASFLLGSVLNVLFAPGSEPPRPGQSPGSSAAPGPGRRGGRGELARQIRERYEEVQRYSRGGPGPGAGRPERRRLMDLAPGGPGLQRPRPPRVRSPPDGAPGWPPAPGPGSPGPGPRLGCAALRNVSGAQYVGSGYTKAVYRVRLPGGAAVALKAVDFSGHDLGSCVREFGARRGCYRLAAHKLLKEMVLLERLRHPNVLQLYGYCYQDSEGIPDTLTTITELGAPVEMIQLLQTSWEDRFRICLSLGRLLHHLAHSPLGSVTLLDFRPRQFVLVNGELKVTDLDDARVEETPCTSSADCTLEFPARNFSLPCSAQGWCEGMNEKRNLYNAYRFFFTYLLPHSAPPSLRPLLDSIVNATGELAWGVDETLAQLETALHLFRSGQYLQNSTSSRAEYQRIPDSAITQEDYRCWPSYHHGGCLLSVFNLAEAIDVCESHAQCRAFVVTNQTTWTGRKLVFFKTGWNQVVPDAGKTTYVKAPG | 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 activity . Required for longitudinal bone growth through regulation of chondrocyte differentiation . May be indirectly involved in protein transport from the Golgi apparatus to the plasma membrane . Probably plays a role in platelets: rapidly and quantitatively secreted from platelets in response to stimulation of platelet degranulation .
PTM: Phosphorylated on tyrosines; probably via autophosphorylation.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 53841
Sequence Length: 492
Subcellular Location: Secreted
EC: 2.7.10.2
|
C8VI81 | MDHPHPSTFSLGLSQILVCLALLYAAIHILSVYRRLCHISGPFWARISNLPRVWWVNTSRAHEIHQQLHEKYGDVVRFGPNMVSLRNPTWIPTVYPTRMGVKKSDFYRTLAPYTPSGALPAVFSSRDEEVHRGLRGPIASLYSMSKVLPLEVFVDRTIDVLVRQLDGRFAGAGETFDLASWLQFFAFDVMGTLTFSKRYGFLEKGMDVHGMLDTIWRFLKGAAPFTQIPWVDEIWNKNVLATKLKGATGVSILGIVGKFVSQRQEESKAGKIDGTADRDMLSLFMEIQKNNQLPPWYVTAWTFSNITAGSDSAAVVMRTVFYNLLSHPSTLQKLRSELLSAGPLTQPYPSWKDVCNLPYLDACILEALRLHPPFCLPFERIVPQGGMVLGDTYFPEGTVVGMSPWVVNRHKPTFGEDSDVWNPERWMVSKELKSKREAAVLTFGAGRRVCLGRHIAILELKKIVPALVLRYDFELIDPERFTTENFWFFRQRGMDVRVKKRMQAEAGI | 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 the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E . The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57688
Sequence Length: 508
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
|
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 one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E . The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Sequence Mass (Da): 34218
Sequence Length: 312
Pathway: Secondary metabolite biosynthesis.
EC: 1.1.1.-
|
Q5B8A3 | MGSLWSSPSLLPSQQDNETEPFSHLPKEIGTDPTLREDSNVSNRNSEAASTSTDSSTNTNENHASTSQSSLEGAPDSGPIKIAIIGGGIIGIITALGLIHRGINVTVYERAPKYTETSAGFSFSKGARKAMEIVSPRVLEALLRVAAPNKHPFIRYFDGFTPGADEAQWQIPAERPDYYGCLRAAFLESLGQEVPEGIVKFGKVLESYEDNEEGKVLLRFRDGSTAEVDAVIGCDGIKSRTRRIMLGDTHPAAAPGYTEIVAYRAVLPLEGVVAALGEDRGHSHCLAVGPDAYTVSYPIANKPLANMILFRKQRGSWANSDKLLETCHRSTAQDAVKDWKPEIQRLVDLLPENPNKWAIFDTSDNPVPSYVSASGRVCIAGDAAHASTPFLASGAAMGVEDAAVLATVLNTALKEQSYNKTTVVKRKAITAAFQAYSGIRMQRSQRVVKDSRTVGEVCMWQDAETARDPEKCFQAIWQRYTQIWEFDVEEMVERARSECVRLFS | 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 the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E . The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Sequence Mass (Da): 55079
Sequence Length: 504
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
|
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 groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E . The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33432
Sequence Length: 309
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 2.5.1.-
|
Q5B8A1 | MRHTALLPLVSSFIVPALAQIPGQTTVNATVNQGRFGNATYDYVIVGGGTSGLAIAARLAEDPSLSVAVIEAGGYYELDGTVASIIPGLAAGANVGTDATEYSTVDWNFQAQPLTSANDRSLRYNRGKTLGGSSARHYMVYQRGTRGSYDQWAELTGDESWGWDSVFPYFQRSVNVTPANMTGRFPNTTVTYDPSGFNKAGGPLHVTWPNYGSPWSTWIEQGLEAIGILPDTDFNTGTLNGSSWAPITINPLSQKRDSSETSFLQQSLKTTNLTVYLHTMALKIGFDGTTASSVDVRSPVGRFTLSARREIIVSAGALQSPQLLMVSGIGPRETLERHGIPVVKELAGVGQKMWEHPFFGITHQVNLVTATELAINQQALLQALNQYKSQQGPLTSAGFGVLGWEKLPNSTLSDSTNEALATFPSDWPTIEYLSIDGYLNGWHSAADQATGNGQQWGTIAVALVAPLSRGNVTISSSDMDDPPVFDLGFLTHPADREIAVAAMRRIRQAFAAISEITIGDEVVPGADVSTDEELLDFIRESIVPVYHVAGTCAMGREDDPEAVVDPQARVIGVNNLRVVDASIFPTLPPGHPQSTCYMVAEKIADLIKKGN | 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 groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E . The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Sequence Mass (Da): 65610
Sequence Length: 611
Pathway: Secondary metabolite biosynthesis.
EC: 1.1.-.-
|
A7MBL8 | MAADSVQNDARGPMVSGRLDFDQNLDFSDTMVQKNLDEIKDQIKREIRKELKIKEGAENLRKVTTDKKSLAYVDNMLKKSNKKVEELHQELQELNAHIVVKDPEEVEEYPLTPDTPKSETRMSTNSNRLAALKKQADIELKVKQGAEDMIQMYSNGSSKDRKLLAAAQQMLQDSKTKIEFIRMQILKASQTSEINYENNDVTTSKPIISPLDLRIEELRHHYRIESAVADGAKNVMKLLGTGKVTEKKAHSEAQARLNESSQKLDLLKFSLEQRLSELPKNHPKGTLIMEELAMVASPPNSPRQSIMSTSNQYSTVAKPAALTGTLDVRLMGCQDLLENVPGRSKTASVSLPGWSPSEARSSFMSRGNKNKSGSSRTLSKSDDLSNEISAVLKLDNTVVGQTHWKPVSNQSWDQKFTLELDRSRELEIAVYWRDWRSLCAVKFLRLEDFLDNQRHGMCLYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPSVNTSFSPQAADLGSAMSHETAPMGHPDAHSLPSDPTVTKLDFDKAVTPPSKRNSIEVEIEETAPPDKISDGKEVQDALATFDFLNNTVAKPDYDSLVEHEQPGLELTEIQRKTEIREEEEVQFSLSDFKCVAVLGRGHFGKVLLADYKTTGEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHADVFSETRSVFYAACVVLGLQFLHDHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFKDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIFEMLVGESPFPGDDEEEVFDSIVNDEVRYPKYLSTEAISIMRRLLRRNPERRLGAGERDAEEVKRHPFFRDMDWPGLLAKKIRPPFVPTITSREDVSNFDDEFTSEAPILTPPREPRILTLGEQDLFADFDYIADWC | 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 processes (By similarity).
PTM: Autophosphorylated. Phosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 110657
Sequence Length: 977
Subcellular Location: Cytoplasm
EC: 2.7.11.13
|
Q16513 | MASNPERGEILLTELQGDSRSLPFSENVSAVQKLDFSDTMVQQKLDDIKDRIKREIRKELKIKEGAENLRKVTTDKKSLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDITDCPRTPDTPNNDPRCSTSNNRLKALQKQLDIELKVKQGAENMIQMYSNGSSKDRKLHGTAQQLLQDSKTKIEVIRMQILQAVQTNELAFDNAKPVISPLELRMEELRHHFRIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNEVPKNHPKSRIIIEELSLVAASPTLSPRQSMISTQNQYSTLSKPAALTGTLEVRLMGCQDILENVPGRSKATSVALPGWSPSETRSSFMSRTSKSKSGSSRNLLKTDDLSNDVCAVLKLDNTVVGQTSWKPISNQSWDQKFTLELDRSRELEISVYWRDWRSLCAVKFLRLEDFLDNQRHGMCLYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPTVNHSGTFSPQAPVPTTVPVVDVRIPQLAPPASDSTVTKLDFDLEPEPPPAPPRASSLGEIDESSELRVLDIPGQDSETVFDIQNDRNSILPKSQSEYKPDTPQSGLEYSGIQELEDRRSQQRFQFNLQDFRCCAVLGRGHFGKVLLAEYKNTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHTDVFSEPRAVFYAACVVLGLQYLHEHKIVYRDLKLDNLLLDTEGFVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNPERRLGASEKDAEDVKKHPFFRLIDWSALMDKKVKPPFIPTIRGREDVSNFDDEFTSEAPILTPPREPRILSEEEQEMFRDFDYIADWC | 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 activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis .
PTM: Autophosphorylated. Phosphorylated during mitosis. Phosphorylated by CDK10 .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 112035
Sequence Length: 984
Domain: The N-terminal regioninterferes with the interaction between AKT1 and the C-terminal regionof PKN2.
Subcellular Location: Cytoplasm
EC: 2.7.11.13
|
P54736 | MLAPDSLVLDGRFRVLRPLGSGGMGEVYLGEQVSLGRKVAIKVLHHDLHAQAGMAERFKREARLLSAVEHPAVVRIVDFGESGDHACLVMEFVEGESLYDVLTPGPMPPGRALPLLQQLAEGLAAIHDKGIIHRDLKPENVFISKSARGEQARLLDFGIARLVEPDAASSVSQIGVVLGTPEYLSPEQAVGAKVDTRSDLYSFGVLTYRVLSGRLPFDGPLPRNFLSQHASAAPLPLDRAAPTLSRYVGLLSLVMRLLEKDASKRPQSAHELADALAAAHSALSAFTPGLGTPAYVPQPGSGATPSSGTSVFGTGSASGSSSGPTGTAAFAGVAPAPQASSGTAAFGVASSSGSASGALPAASPHTGTASFGLKSSGGVAAVTGGNASVVKPQNLTVMLTDIQGFTERTSRQTHEENARMLETHDKLLMPLVKEHDGRLVQKRGDALLVVFRSPTAGVLCGMAMQDRLWRHNQTVPEVDRLNVRVCLHAGEVLATPDSVLGEPMEVIEAVEHVASAGEVTFTEAVNLARNRAEATAEPCGAITLPGRNEQLQLYRCQRAAEGPPFGDRFASQGSRGNALAPLLAKLQAVKLPTGLGELLRQRRREAALVAGAVVLLGAGAAWLSQRNDAGTRAFALLEDGKLNEALALMDAATDEEKELPSLRRARVAANHAKGHHISERTALSHLKEEELEDVEPLILDGLAEDYGKEPLTVLGNALARFPKDRLRAHYEDLAEEAYSLRQWGALRYLEFVKAADGVNLVRAYSEALNSPDCDIRTQAANRLAGLGDADAIPAMERVTSLPKAKGLLGSKDCGHEAAATAIKSLKQKSD | 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
Sequence Mass (Da): 87680
Sequence Length: 830
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q6P5Z2 | MEEGAPRQPGPSQWPPEDEKEVIRRAIQKELKIKEGVENLRRVATDRRHLGHVQQLLRSSNRRLEQLHGELRELHARILLPGPGPGPAEPVASGPRPWAEQLRARHLEALRRQLHVELKVKQGAENMTHTCASGTPKERKLLAAAQQMLRDSQLKVALLRMKISSLEASGSPEPGPELLAEELQHRLHVEAAVAEGAKNVVKLLSSRRTQDRKALAEAQAQLQESSQKLDLLRLALEQLLEQLPPAHPLRSRVTRELRAAVPGYPQPSGTPVKPTALTGTLQVRLLGCEQLLTAVPGRSPAAALASSPSEGWLRTKAKHQRGRGELASEVLAVLKVDNRVVGQTGWGQVAEQSWDQTFVIPLERARELEIGVHWRDWRQLCGVAFLRLEDFLDNACHQLSLSLVPQGLLFAQVTFCDPVIERRPRLQRQERIFSKRRGQDFLRASQMNLGMAAWGRLVMNLLPPCSSPSTISPPKGCPRTPTTLREASDPATPSNFLPKKTPLGEEMTPPPKPPRLYLPQEPTSEETPRTKRPHMEPRTRRGPSPPASPTRKPPRLQDFRCLAVLGRGHFGKVLLVQFKGTGKYYAIKALKKQEVLSRDEIESLYCEKRILEAVGCTGHPFLLSLLACFQTSSHACFVTEFVPGGDLMMQIHEDVFPEPQARFYVACVVLGLQFLHEKKIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEEEVFDCIVNMDAPYPGFLSVQGLEFIQKLLQKCPEKRLGAGEQDAEEIKVQPFFRTTNWQALLARTIQPPFVPTLCGPADLRYFEGEFTGLPPALTPPAPHSLLTARQQAAFRDFDFVSERFLEP | 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
EC: 2.7.11.13
|
Q8K045 | MEHRKPGTGQRAPKDEKEMVRRAIQKELKIKEGMENMRRVATDRRHLGHVQQLLRASNRRLEQLHGELRELHAQVLLPASAEPVTSEPQPRAEQSRARLSEALHRQLQVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLRMKISSLESSGSPEPGPDLLAEELQHRLRVEAAVAAGAKNVVKLLGGQRMQDRKALAEAQAQLQESSQKLDLLRLALELLLERLPPTHSLRSRVTQELWMAMLGNPQPLGTLVKPIALTGTLQVRLLGCKDLLVAVPGRSPMAVLAGSPSESWLRTRSRQQRGGGELASEVLAVLKVDNRVVGQTGWGLVAEKSWDQSFIISLDRARELEIGVHWRDWRQLCGVAFLKLEDFLDNACHQLSLSLVPQGRLFAQVTFCEPVIERRPRLQRQRCIFSKRRGRDFMRASQMNLSMAAWGRLVMSLLPPCSSPNTASPPKGRPSTAVCGTPSAASPSNFLPMKTLSKEDTKPPPKPPRLYLQEPAPGTPCTKRPHMDPRPAVVPALAALSTRKPPRLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTGHPFLLSLLACLQTSSHACFVTEFLPGGDLMAQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEEEVFECIVSADVPCPHFLSVQGLELIQKLLQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSLPPTLTPPVSQSSLTARQQAAFRDFDFVSEQFLES | 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
EC: 2.7.11.13
|
P54737 | MPLKVIGPYRVLETLGSGGAGTVYRALDRRTTDEVALKLLSAGPARDARAARRLAREFDTLVDLSHPNVVKVFESGVHQGVPYLAMELIEGLTLRHYLDLSSGDRQTPPGSHTPRSPLSVLRTADDDFGPLSRSFSDSMDDSEDSPFDGTFGLEAFAEEAPSEDLESFASSASPHVGIGSDDSLEGFDLPPPMPRPAEPEEEPGRVVREEDLNRPERMGRLKDAMLQICEALAYIHGHGLVHRDLKPSNIMVDDDRQVRLMDFGLAKFLADDAAITEAGKLVGTYRYMAPEQILGEPLDGRADLYSLGVILYELLSGRPPFDAKTPHELWRQVLETEPPPVLALNLHGDPQLARVAHRLIRKEPDDRFQTAEEVYEALSE | 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
Subcellular Location: Cytoplasm
EC: 2.7.11.1
|
P54738 | MQIGKYQLVRKLASGGMAEVFLAKAAGPRGFEKTLVLKRILPHLAEDAAFVEMFLGEARLAAQLEHPNIVQIFDFGEAEGSFFLAMEFIDGPNLRKLVKRAAEEALPPAFCAKVVAAAAEGLAYAHEFRDVETGEPLGLIHRDVSPDNILVSRQGAVKVVDFGIAKVAGQGHRTLTGVVKGKVAYMPPEQLQAKAMDRRVDVYALGVVLYELLTGKRPFDATTDVSVMQAILFESFIPVSARRPDVPVALQQVLDKALAKDRERRYADCRALQDDLERFVLSTGEPVGAYQIAQRIAQWVPEVAAAPAMTPSQGGSKGAVASQAKADARSASMVSPPVDSTSPTTPMPRSLVAPVEVPADSTSPTTPMPVAIGGVVQALEPRSSPQQDTLQSYPVVVKTPALRADASARGASRPRAQSRASGVKVQAPQARDEDVVAMAAASSPPSGGASPAPTTPEDADDAVHTRSTEYAATVPSGRPGGRIAGIVGAVVALLVGGAVTVMRGDDSEVSPVRVNPPPLTHLPREPAVPSQGGRNVPQEKPAANVNAGARDSNDGAQAKPQVSTDVSVVPQEPHVARDATTPEAGLPTVKDAPPENGGAASKEGSAVVAKREPAKASGDPEPNPSRVRERAPTQKVAAVAKGRLEFRIRPYAVVSLDGKVLGQTPFAAVEVPEGRHTVRLVNKELGKDVTRTVDVKAGQATVFKLNLEAE | 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-phospho-L-seryl-[protein]
Sequence Mass (Da): 74622
Sequence Length: 710
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
P54743 | MSPRIGVMLSGRYRLHRLIATGGMGQVWEAVDSRLGRRVAVKVLKGEFSSDPEFIERFRAEARTTAMLNHPGIASVHDYGESHMDGEGRTAYLVMELVNGEPLNSVLKRTGRLSLRHALDMLEQTGRALQIAHAAGLVHRDVKPGNILITPTGQVKITDFGIAKAVDAAPVTQTGMVMGTAQYIAPEQALGHDATPASDVYSLGVIGYEVVSGKRPFTGDGALTVAMKHIKEPPPPLPADLPPNVRELIEITLVKNPGMRYPSGGLFAEAVAAVRAGHRPPRPNQTPSSGRASPTTIPSSTQARAAVACGTKTPAPRRSRPSTSGNRPPPARNTFSSGQRALLWAAGMLGALAIIIAVLIVINSYAGNEQHQPPTPTVTDTGTPPATKTLSGFPAAYCEYRVNWTNHKEISNSGLPKQAARAQLAGATDISPVAGQT | 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 Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 46312
Sequence Length: 437
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
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 a role in virulence (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 16470
Sequence Length: 148
Subcellular Location: Secreted
EC: 3.1.1.4
|
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, including more efficient penetration of the insect cuticle and evasion of host immune response by repressing the expression of host immunity genes .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 21498
Sequence Length: 190
Subcellular Location: Lipid droplet
EC: 3.1.1.4
|
Q0JKT4 | MFSCDMASRWRELHGSGHWDGLLDPLDVDLRRCLITYGEMIMATYEAFIGEHRSPNAGMCRYRHADLFRRVDVSHPGWYAATRYIYATANADVHGKVLLRPLCREGRATECNWMGYVAVATDEGAAALGRRDIVVAWRGTQRALEWVADLKLAPASAAGILGPEGADGTDPSVHRGYLSLYTSEDQCSELNKQSARMQVLTEIARLMDKYKDEETSITVIGHSLGATLATLNAADIAANSYNTSSLSPSGETRAPVTAVVFGSPRTGDRGFRDAFHRLRDLRMLRVRNRPDRIPHYPPVGYADVGVELLIDTRLSPFLRRHGSESQSHDLECHLHGVAGWHGDHRGFELVVDRDVALVNKFDDCLADEYPVPVRWKVHHNKSMVKGPDGRWVLQDHEPDDDDDDDDDD | 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 Gram-negative and Gram-positive bacteria: B.cereus (MIC>9 ug/ml), B.subtilis (MIC>12 ug/ml), E.faecalis (MIC>7 ug/ml), S.epidermidis (MIC>12 ug/ml), S.aureux (MIC>5 ug/ml), E.coli (MIC>7 ug/ml), K.pneumonia (MIC>8 ug/ml), P.aeruginosa (MIC>10 ug/ml), and S.enteric (MIC>9 ug/ml). It also shows antifungal activities: A.niger (MIC>15 ug/ml), B.cinerea (MIC>12 ug/ml), F.solani (MIC>15 ug/ml), and P.digitatum (MIC>10 ug/ml).
PTM: Glycosylated.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 3351
Sequence Length: 30
Subcellular Location: Secreted
|
Q8RZ40 | MCCFLLVSVLLATTLTDVASAQRWRQTSGGGKDRWDGLLDPLDADLRRDIIRYGELAQATSDALIGDPASPFAGASRYAPDAFLRKVRASDPDAYRVTRFVYATSSVRLPDAFMPRPAPSAGAAWSGESNWMGYVAVAADGVAAKAGRRDIVVAWRGTKRAVEWANDLDITLVPADGVVGPGPGWTQPSVHRGFLSVYTSKSFSSPFNKLSAREQVLAEITRLLRAYKNENCSITITGHSLGAALSTLNAIDIVANGYNVRGSSRVPVPVTAIALASPRVGDDQFKRAFDSTSNLSLLRVRNAPDIVPTILPSAFFKDVGAELLVDTRRSPYLKNPAGPAQWHNLECYLHAVAGTQGAGDGAGFSLVVDRDLALVNKEVDALRDEYQVPAAWWVEKNKGMVQNASGRWVLQDHEEGNLAM | 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 | MSTTAPRAVAERWRELHGEDHWKGLLDPLDADLRRSVIGYGELAQATNDAFIREAWSPHAGACRYSRDRFLEKAQASTQLAGLYEVTAFFYATAGAGGVPAPFMVRNRESNWMGYVAVATDAGVAALGRRDVVVAWRGTVRPMEWLNDLDFTLVSAAGVLGAGGRSPAPRVHRGWLSIYTASDPASKYSKLSAREQISDEIKRLMDKYKDEETSITVVGHSLGAAVATLNAADIVSNGLNQHGACPVTAVAFACPRVGDSGFRKLFDELPGLRLLRVCNSPDVVPKYPPMGYADVGVELPVDTRRSPYLKSPGNQAVWHSLECYMHGVAGAQGKRGGFKLEVDRDVALVNKNVDALKEEYHVPPSWSVQRDKGMVRGADGHWKLMDYEGEESSQDK | 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 | MDKSQGVLLSSNVGAGSRPWPELLGSAHWDGLLDPLDLTLRRLILLCGDLCQVTYDSFNSDSHSKYCGTCRFSRSTLLDRTQFPAAGDLSVAAYLYATSDATAFPGSMVYSMSREAWSKESNWIGYVAVSNDAAAAASGQRVIYVAWRGTIRSLEWVDVLKPDLVDHDDILPEGHPGRGRSRVMKGWYLIYSSTDERSPFSKYSARDQMLAAVRELVARYRNESLGVVCTGHSLGASLATLCAFDIVVNGVSKVGDGAHIPVTAVVFGSPQIGNPEFKKQFEEQPNLRALHVRNMPDLIPLYPSGLLGYANVGKTLQVDSKKSPYVKRDTSPGDYHNLQGILHTVAGWNGKDGEFKLQVKRSVALVNKSSGFLKDSNLVPESWWVERNKGMVLGQNGEWQLEGPAEENLPVPPVVTGKIIDDDVAAVATSSSAKEDKKTGKGSKLLSGLIDQLLCVPDTCKAGAA | 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 | MSSSPMLGGIADRWRELHGQDSWNGLLDPLDLDLRSSILSYGELVQATYDSFNRERRSPHAGACVYGHGDLLAAAGASAAGSYAVTKFVYATSGLPVPEAFLLLPLPSLLPPAWSRESNWMGYVAVATDEGVAALGRRDIVVAWRGTVESLEWVNDFDFTPVPAAPVLGAAAAANPRAIVHRGFLSVYTSSNKDSKYNKASARDQVLEEVRRLMELYKDEVTSITVVGHSLGASLATLNAVDIVANGANCPPASSSSSQPPCPVTAIVFASPRVGDGFFKAAFASFPDLRALHVKNAGDVVPMYPPLGYVDVAVKLRISTSRSPYLRSPGTIETLHNLECYLHGVAGEQGSAGGFKLEVDRDVALANKGVDALKDKYPVPPRWWVSKNRCMVKDADGHWALHDFEQI | 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-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31717
Sequence Length: 283
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.51
|
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-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30914
Sequence Length: 278
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.51
|
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-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31011
Sequence Length: 278
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.51
|
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
Sequence Length: 166
Subcellular Location: Secreted
|
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 glycosylation has no role in the association of this PLI and PA2 enzyme.
Sequence Mass (Da): 18230
Sequence Length: 166
Subcellular Location: Secreted
|
P46925 | MDITVREHDFKHGFIKSNSTFDGLNIDNSKNKKKIQKGFQILYVLLFCSVMCGLFYYVYENVWLQRDNEMNEILKNSEHLTIGFKVENAHDRILKTIKTHKLKNYIKESVNFLNSGLTKTNYLGSSNDNIELVDFQNIMFYGDAEVGDNQQPFTFILDTGSANLWVPSVKCTTAGCLTKHLYDSSKSRTYEKDGTKVEMNYVSGTVSGFFSKDLVTVGNLSLPYKFIEVIDTNGFEPTYTASTFDGILGLGWKDLSIGSVDPIVVELKNQNKIENALFTFYLPVHDKHTGFLTIGGIEERFYEGPLTYEKLNHDLYWQITLDAHVGNIMLEKANCIVDSGTSAITVPTDFLNKMLQNLDVIKVPFLPFYVTLCNNSKLPTFEFTSENGKYTLEPEYYLQHIEDVGPGLCMLNIIGLDFPVPTFILGDPFMRKYFTVFDYDNHSVGIALAKKNL | 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 synthesis, and regulates osmolarity (Probable).
PTM: Not N-glycosylated.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves small molecules substrates such as Ala-Leu-Glu-Arg-Thr-Phe-|-Phe(NO2)-Ser-Phe-Pro-Thr.
Sequence Mass (Da): 51490
Sequence Length: 453
Subcellular Location: Membrane
EC: 3.4.23.39
|
Q04383 | MSHLFPPSSPVAGKPLESPQKEPGKLANTSVLTLGRKRYNYELEEYPTPDPSSSIGRQSSPVKDITSRLNETKSALSSPSKQEKVLAGPIEIELDASDPSRLAIGRKKSVCNIILPCRKNISRQHAFISYAADRNEIKLECNGTNGLSVHLPYSMQLHLVKPFPTRNFYKLVAEEPLTSQNTKQSHGKTLQKNQNFISFVLAKGETVTFPYIQGSFINFTGVTVCLSLKKVAPYPGDGNNNFDEENSTETEDELCLLTTTSDDFSWQKETPSMKFVPVEHSPRTEQISKPLLIASPALVKNSPISYRTTPQTSFVINQPSTPKKLKRKSISLKNNTIQETPLPKDKIIGTLSASTRSGGINEEESFAAVAKKTKELSSTTAIVSPAQKRLKTSLNIIPEISRSLSERGIRFDDLVHVLCNHLAFSNLQQTPLSQLQNINSNTSQLSKDELKKVLETISCIGIIVREGKDASGKPLEDEYYYDVENDDSDERKILYNSLKGRSRLRSCRKKHKQYFWKRPTK | 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 | MNLTIKEEDFTNTFMKNEESFNTFRVTKVKRWNAKRLFKILFVTVFIVLAGGFSYYIFENFVFQKNRKINHIIKTSKYSTVGFNIENSYDRLMKTIKEHKLKNYIKESVKLFNKGLTKKSYLGSEFDNVELKDLANVLSFGEAKLGDNGQKFNFLFHTASSNVWVPSIKCTSESCESKNHYDSSKSKTYEKDDTPVKLTSKAGTISGIFSKDLVTIGKLSVPYKFIEMTEIVGFEPFYSESDVDGVFGLGWKDLSIGSIDPYIVELKTQNKIEQAVYSIYLPPENKNKGYLTIGGIEERFFDGPLNYEKLNHDLMWQVDLDVHFGNVSSKKANVILDSATSVITVPTEFFNQFVESASVFKVPFLSLYVTTCGNTKLPTLEYRSPNKVYTLEPKQYLEPLENIFSALCMLNIVPIDLEKNTFVLGDPFMRKYFTVYDYDNHTVGFALAKNL | 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 form by cysteine proteases in the digestive vacuole of trophozoites (By similarity). Proteolysis requires an acidic environment (By similarity). Transprocessing may serve as an alternate activation system .
Location Topology: Single-pass type II membrane protein
Catalytic Activity: Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves small molecules substrates such as Ala-Leu-Glu-Arg-Thr-Phe-|-Phe(NO2)-Ser-Phe-Pro-Thr.
Sequence Mass (Da): 51693
Sequence Length: 451
Subcellular Location: Membrane
EC: 3.4.23.39
|
Q8I6Z5 | MNNYFLRKENFFILFCFVFVSIFFVSNVTIIKCNNVENKIDNVGKKIENVGKKIGDMENKNDNVENKNDNVGNKNDNVKNASSDLYKYKLYGDIDEYAYYFLDIDIGKPSQRISLILDTGSSSLSFPCNGCKDCGIHMEKPYNLNYSKTSSILYCNKSNCPYGLKCVGNKCEYLQSYCEGSQIYGFYFSDIVTLPSYNNKNKISFEKLMGCHMHEESLFLHQQATGVLGFSLTKPNGVPTFVDLLFKHTPSLKPIYSICVSEHGGELIIGGYEPDYFLSNQKEKQKMDKSDNNSSNKGNVSIKLKNNDKNDDEENNSKDVIVSNNVEDIVWQAITRKYYYYIKIYGLDLYGTNIMDKKELDMLVDSGSTFTHIPENIYNQINYYLDILCIHDMTNIYEINKRLKLTNESLNKPLVYFEDFKTALKNIIQNENLCIKIVDGVQCWKSLENLPNLYITLSNNYKMIWKPSSYLYKKESFWCKGLEKQVNNKPILGLTFFKNKQVIFDLQQNQIAFIESKCPSNLTSSRPRTFNEYREKENIFLKVSYINLYCLWLLLALTILLSLILYVRKMFYMDYFPLSDQNKSPIQEST | 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 the leucine residue in the RxLxE/Q/D (or RxLxxE) motif of exported proteins including RESA, EMP2, EMP3, KAHRP, RIF/Rifin and STEVOR . Also, by regulating protein export, plays an essential role in gametocyte development and thus, parasite transmission to the mosquito vector (By similarity).
PTM: It is not clear if the zymogen has a cleavable propeptide . In vitro, appears to be cleaved between Asn-80 and Ala-81 . Cleavage of the putative propeptide is dispensable for catalytic activity .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 68480
Sequence Length: 590
Domain: The transmembrane domain is essential for localization to the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.4.23.-
|
A5K302 | MVGASLGPPGRGSLSRLIRLVICVLTLCALSVQGRSESTEGHSKDLLYKYKLYGDIDEYAYYFLDIDIGTPEQRISLILDTGSSSLSFPCAGCKNCGVHMENPFNLNNSKTSSILYCENEECPFKLNCVKGKCEYMQSYCEGSQISGFYFSDVVSVVSYNNERVTFRKLMGCHMHEESLFLYQQATGVLGMSLSKPQGIPTFVNLLFDNAPQLKQVFTICISENGGELIAGGYDPAYIVRRGGSKSVSGQGSGPVSESLSESGEDPQVALREAEKVVWENVTRKYYYYIKVRGLDMFGTNMMSSSKGLEMLVDSGSTFTHIPEDLYNKLNYFFDILCIQDMNNAYDVNKRLKMTNESFNNPLVQFDDFRKSLKSIIAKENMCVKIVDGVQCWKYLEGLPDLFVTLSNNYKMKWQPHSYLYKKESFWCKGIEKQVNNKPILGLTFFKNRQVIFDIQKNRIGFVDANCPSHPTHTRPRTYNEYKRKDNIFLKIPFFYLYSLFVVFALSVLLSLVFYVRRLYHMEYSPLPSEGKAPADA | 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 the leucine residue in the RxLxE/Q/D (or RxLxxE) motif of exported proteins including EMP1 (By similarity). Also, by regulating protein export, plays an essential role in gametocyte development and thus parasite transmission to the mosquito vector (By similarity).
PTM: It is not clear if the zymogen has a cleavable propeptide (By similarity). Cleavage of the putative propeptide is dispensable for catalytic activity (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 60916
Sequence Length: 536
Domain: The transmembrane domain is essential for localization to the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.4.23.-
|
A0A509AI82 | MTNFCIKSYLFLYLSFLLFFDIITIFHVSSIRISTVLKNDKKKKNFNTSLVEENKKYLFNEIKLNNRFKNDIKGYIQNINNFHSIIESKIPNSLLYVHEDLINFHNSQFIGDIEIGNPPQSFKVVFDTGSSNFAIPSTKCVKGGCTLHNKFDAKKSRTFMSNLKNKKESIYTYVQYGTGKSILEHGYDDVYMKGLKINKQCIGLIIEESMHPFSDLPFDGIVGLGFSDPDNSFQTKYSKSLIETIKEQNLLQQNIFSFYVPKELEKSGAITFGRANSKYAIEGEKIEWFPVISMYFWEINLLGILLPDKNFEICSNKKCRAAVDTGSSLITGPSSLMQPLIENINLEKDCSNISSLPIISFVLKNVEGKTVILDFTPDDYILQENSEEDNSSQCVIGLMSLDIPPPRGPIFIFGNVFIRKYYTIFDNDHKLVGVVKSNHNF | 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 | MFFINFKKIKKKQFPIYLTQHRIITVFLIFIYFINLKDCFHINNSRILSDVDKHRGLYYNIPKCNVCHKCSICTHENGEAQNVIPMVAIPSKRKHIQDINKEREENKYPLHIFEEKDIYNNKDNVVKKEDIYKLRKKKKQKKNCLNFLEKDTMFLSPSHDKETFHINHMNKIKDEKYKQEYEEEKEIYDNTNTSQEKNETNNEQNLNINLINNDKVTLPLQQLEDSQYVGYIQIGTPPQTIRPIFDTGSTNIWIVSTKCKDETCLKVHRYNHKLSSSFKYYEPHTNLDIMFGTGIIQGVIGVETFKIGPFEIKNQSFGLVKREKASDNKSNVFERINFEGIVGLAFPEMLSTGKSTLYENLMSSYKLQHNEFSIYIGKDSKYSALIFGGVDKNFFEGDIYMFPVVKEYYWEIHFDGLYIDHQKFCCGVNSIVYDLKKKDQENNKLFFTRKYFRKNKFKTHLRKYLLKKIKHQKKQKHSNHKKKKLNKKKNYLIFDSGTSFNSVPKDEIEYFFRVVPSKKCDDSNIDQVVSSYPNLTYVINKMPFTLTPSQYLVRKNDMCKPAFMEIEVSSEYGHAYILGNATFMRYYYTVYRRGNNNNSSYVGIAKAVHTEENEKYLSSLHNKINNL | 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 maturation . Also cleaves rhoptry protein RON3 .
PTM: Autocleaved into a p55 mature form.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 74183
Sequence Length: 627
Subcellular Location: Membrane
EC: 3.4.23.-
|
Q8TBJ4 | MAVGNNTQRSYSIIPCFIFVELVIMAGTVLLAYYFECTDTFQVHIQGFFCQDGDLMKPYPGTEEESFITPLVLYCVLAATPTAIIFIGEISMYFIKSTRESLIAQEKTILTGECCYLNPLLRRIIRFTGVFAFGLFATDIFVNAGQVVTGHLTPYFLTVCKPNYTSADCQAHHQFINNGNICTGDLEVIEKARRSFPSKHAALSIYSALYATMYITSTIKTKSSRLAKPVLCLGTLCTAFLTGLNRVSEYRNHCSDVIAGFILGTAVALFLGMCVVHNFKGTQGSPSKPKPEDPRGVPLMAFPRIESPLETLSAQNHSASMTEVT | 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 | MAVENNTQRSYSIIPCFIFVELVIMAGTVLLAYYFECTDTFQVHIQGFFCQDGDLMKPYPGTEEESFISPLVLYCVLAATPTAIIFIGEISMYFIKSTRESLIAEEKMILTGDCCYLSPLLRRIVRFIGVFAFGLFATDIFVNAGQVVTGHLTPYFLTVCQPNYTSTDCRAHHQFINNGNICTGDLEVIEKARRSFPSKHAALSIYSALYATMYITSTIKTKSSRLAKPVLCLGDLCTAFLTGLNRVSEYRNHCSDVIAGFILGTAVALFLGMCVVHNFKGTQGSASKPKPEDPRGVPLMAFPRIESPLETLSAQNHSASMTEVT | 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 | MQRAGSSGARGECDISGAGRLRLEQAARLGGRTVHTSPGGGLGARQAAGMSAKERPKGKVIKDSVTLLPCFYFVELPILASSVVSLYFLELTDVFKPVHSGFSCYDRSLSMPYIEPTQEAIPFLMLLSLAFAGPAITIMVGEGILYCCLSKRRNGAGLEPNINAGGCNFNSFLRRAVRFVGVHVFGLCSTALITDIIQLSTGYQAPYFLTVCKPNYTSLNVSCKENSYIVEDICSGSDLTVINSGRKSFPSQHATLAAFAAVYVSMYFNSTLTDSSKLLKPLLVFTFIICGIICGLTRITQYKNHPVDVYCGFLIGGGIALYLGLYAVGNFLPSEDSMLQHRDALRSLTDLNQDPSRVLSAKNGSSGDGIAHTEGILNRNHRDASSLTNLKRANADVEIITPRSPMGKESMVTFSNTLPRANTPSVEDPVRRNASIHASMDSARSKQLLTQWKSKNESRKMSLQVMDTEPEGQSPPRSIEMRSSSEPSRVGVNGDHHVPGNQYLKIQPGTVPGCNNSMPGGPRVSIQSRPGSSQLVHIPEETQENISTSPKSSSARAKWLKAAEKTVACNRSNNQPRIMQVIAMSKQQGVLQSSPKNAEGSTVTCTGSIRYKTLTDHEPSGIVRVEAHPENNRPIIQIPSSTEGEGSGSWKWKAPEKSSLRQTYELNDLNRDSESCESLKDSFGSGDRKRSNIDSNEHHHHGITTIRVTPVEGSEIGSETLSVSSSRDSTLRRKGNIILIPERSNSPENTRNIFYKGTSPTRAYKD | 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-synaptic membrane . Modulates lysophosphatidic acid (LPA) activity in neuron axonal outgrowth during development by attenuating phospholipid-induced axon collapse (By similarity).
PTM: O-glycosylated. Probably at Ser-347.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83290
Sequence Length: 766
Subcellular Location: Postsynaptic density membrane
|
Q32ZL2 | MPLLPAALTSSMLYFQMVIMAGTVMLAYYFEYTDTFTVNVQGFFCHDSAYRKPYPGPEDSSAVPPVLLYSLAAGVPVLVIIVGETAVFCLQLATRDFENQEKTILTGDCCYINPLVRRTVRFLGIYTFGLFATDIFVNAGQVVTGNLAPHFLALCKPNYTALGCQQYTQFISGEEACTGNPDLIMRARKTFPSKEAALSVYAAMYLTMYITNTIKAKGTRLAKPVLCLGLMCLAFLTGLNRVAEYRNHWSDVIAGFLVGISIAVFLVVCVVNNFKGRQAENEHIHMDNLAQMPMISIPRVESPLEKVTSVQNHITAFAEVT | 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 | MPLLPVALISSMLYFQMVIMAGTVMLAYYFEYTDTFTVNVQGFFCHDSAYRKPYPGPEDSSAVPPVLLYSLAAGVPVLVIIVGETAVFCLQLATRDFENQEKTILTGDCCYINPLVRRTVRFLGIYAFGLFATDIFVNAGQVVTGNLAPHFLALCKPNYTALGCQQYTQFISGEEACTGNPDLIMRARKTFPSKEAALSVYAATYLTMYITSTIKAKGTRLAKPVLCLGLMCLAFLTGLNRVAEYRNHWSDVIAGFLVGISIAVFLVVCVVNNFKGRQPENGHIHRDNVARMPMTNIPRVESPLEKVTSLQNHVTAFAEVT | 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 | MTKPVADTSAVLTSEDTLVLASMGSPVEMQLIMDWLGEQRARTPGAKFDVLKLPPRNAPTAALTALVEQLESGSEAGADRSIVPVQVFWQPPADRSRLAKVAGLLPGRDPYHPNPRQQRRILRSDPQRARVMAGESATVSELRKQWRDNTVGEDQHDFAHFVARRAILALARAEYRILGPQYKSPRLVKPEMLASARFRAGLEKIPGATVEEAGKMLDELATGWSQASVDVFSVLGRLISRGFDPEFDYDEYQVAAMRTALEAHPAVLLFSHRSYIDGAVVPVAMQDNRLPPVHMFGGVNLSFGVMGPLMRRAGMIFIRRNIAGDPLYKYVLKEYVGYVVEKRFNLSWSIEGTRSRTGKMLPPKLGLMSYVADAYLDGRSDDILLQGVSICFDQLHEIAEYAAYARGAEKTPEGFSWLYNFIKAQGERNYGKIYVRFPEAVSMRQYLGVPHGPITHDLAAKRLALQKMSFEVAWRILRATPMTATGLVCALLLTARGTALTLGQLHHTLQDSLDYLERKQTPMSTSALRLRSREGVRAAVDALSNAHPVTRVDSGREPVWYIAPEDELAAAFYRNSVIHAFLETSIVELALAHARHAEGDRMAAFWDQVMRLRDLLKFDFYFADSAAFRANIAEEMAWHRDWESQVAAGGDQIDAILYAKRPLISDAMLRVFFEAYAIVADVLRDAPANIKQKDLTDLALGLGRQYVAQARVRSSEPVSTLLFATARQVVDDQHLIEPAPDLTERRSAFLAELRNILRDFDYVGKIARNRFVARELKARQERLEQQAQ | 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 of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
Subcellular Location: Cell membrane
EC: 2.3.1.15
|
Q2GH18 | MSIISIAVDAMGGDFAPEAVVSGLDFALTNLLDDQNVSFNIYGQGSQVLPILDKYKDLKEHSVFIDTPEVVLANDKPSFALRKRRSSSMWCAIDSIKSGVTSGVVSSGNTGALMAISRFLLGTLPNIDRPAICTALPSRGEEYFVLLDLGANIESSSNALFQFAIMGSAFAKAVLNIASPKVALLNVGQEEVKGTDVIREAFLLLKQAEGRINFCGYIEPIDILGDKVDVVVTDGFCGNIVLKVAESIAYTFKSVFEKSVTSSIISKFAGLLLKSQMKKDFMRFNPKMYNGAMLLGLNGVVVKSHGNADKVAFAHAIKVTVNAVRNDINAKIIHELS | 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
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
|
B2KC86 | MRIALDASGGDFGYQPNILGAARAVKELKCEVILVGDEKVLKEQLASLGLSDLKGLSVEHAPDVIDMDADPAKEVRSKKNASVVVAADLVKQGRAKAFVSAGNSGATMVAALMKMGRIEGVLRPAIGAPLPTVKGLMLLLDAGANAECKPQHLMQFAVMGSIYTQKVFGIRKPKVGLLSIGEEEGKGNDLVKETYPYLSNLGINFCGNVEGRDLPFGTTDVVVTDGFTGNVCLKLEEGLAKAMFHMIKGEIKKNPIAMLGAMLAKPAFASVKKITDPDTAGGAPLLGVDGVAIVSHGKSSETAVFNAVRTAKRLVDSGFVSDIKQHIAEYKEIFEKLEAKK | 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
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
|
B1H0Q6 | MIIALDAMGGDFAPASTVEGAIFAAKESKHKILLVGIEKILVGELLKYRGRYDLKSLNIEIINATEFITMDEHPAKAVRQKKDSSLSVCARLVADGKADAFVSMGNSGAAMSAALFYLKRIEGVLRPAISTVFPNFGGHCIIADMGANVDCTPEYLLQFGIMASLFCEKVASVENPRVGLVSIGEESTKGNELTLAAFELLKKADINFIGNVEGRDIPGGKVDVAICDGFVGNVILKLGEGLTEMMLKLIRKEFKQHPMTWASLPFLWLAIKDLRKRVDYSEFGGAPLLGVEGVCIIGHGSSNGKAVKNAIFAGAETAKHNIAAGIKEAILRYNNKVV | 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
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
|
Q82ZE8 | MKIAVDAMGGDNAPQAIVEGVMLAKQDFPDIEFQLYGKEAEIKKYITDEKNITIIHTDEKIASDDEPVKAIRRKKTASMVLAAQAVKNGEADAIFSAGNTGALLAAGLFIVGRIKNVERPGLMSTLPVMGEPDKGFDMLDLGANADNKPEHLVQYAVLGSFYAEKVRNVQNPRVGLLNNGTEETKGSELTKKAFELLAADETINFVGNVEARELLNGVADVVVTDGFTGNAVLKSIEGTAMNMMSLLKTAILSEGVKGKMGALLLKNALHGMKDEMDYSKHGGAVLFGLKAPVIKTHGATGPDAVRYTIRQIHTMLETQVVPQLVEYYEGKAE | 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
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
|
Q2RTS9 | MSNSLVISVDAMGGDDAPDMVVDGVKLARKRFPDVRFLLFGDEARIGPLVAGDSALSAVCTIRHTASAVSGDAKPSQAVRSGRQSSLWLSIEAVKKGEAAGVVSAGNTGAFMAMAKLILRTLPGIDRPAIATLLPTLRGESVVLDLGANAECNANNLVEFAIMGEVFARTVLSLDRPTVGIMNIGSESGKGTDTVRDASARLQDSALPIRFMGFVEGDDLGKGTVDVIVTDGFTGNVMLKTAEGTAKLYSQFLRNAFLSSLLARLGYLLSRSALQKVKARTDPRRYNGAMFLGLDGVAVKSHGGTDALGFSNALAVAIDLVRQGFNESIKDEIAKVQVLPSTVSVSHAV | 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
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
|
Q1AW88 | MRIAVDALGGDNAPQEIVAGALAAARRLPGVEILLVGEPGAVEPLLERAPGNVSLRPSGGAVRMDEEPAAALRSRPDASVAVAARLVRSGEADALFSAGNTGAAVAASLLYIGRIGGCRRPAIATVLPFSHPTLLLDVGATVSCRAQDLLNFAILGSVFARRYLETEGAPRVGLLNVGEEPGKGHDLAREAHRLLAASPQVEFAGNVEGRDLGSGRADVVVTDGFTGNAVLKTAEGVARECLRLVREALLGSLAGRVAALAARPRLLAVRDRVDPENYGGSFLLGVRGAVVIGHGNSTARGVENALAGIARAGGGLVAELEATLARQRAASGREGA | 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
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
|
Q21K90 | MSEEIHLSVDAMGGDFGPRLCVEAAASFIAKHSNVRITLVGDKAAVSSCIPPQADLSRLHVLHADQVVDMADKPSHALRHKKNSSMWRALQLVADGEAQACVSGGNTGALMAIGCHLLKTIAGIDRPAIAKQIPTARGSSVLLDLGANLECSPQQLFQFGLMGQGLARVYGKSEPTVALLNVGSELTKGNDIIQDTAQLMGDCADMHFRGFVEGDSLYSGEVDVVVCDGFIGNVALKVSEGVAKFVFGDLRSRIGRGVRSRLLAWLAKPVLKPWAEQFRPAKYNGAALLGLKGVVIKSHGGADAEGFEQALYVALEQASAGIPLKIQASLAAMLGAGLETK | 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
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20891
Sequence Length: 194
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22948
Sequence Length: 219
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21343
Sequence Length: 196
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21193
Sequence Length: 198
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22483
Sequence Length: 216
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19613
Sequence Length: 185
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25388
Sequence Length: 233
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25409
Sequence Length: 233
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21531
Sequence Length: 196
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23964
Sequence Length: 220
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21678
Sequence Length: 205
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24237
Sequence Length: 224
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22816
Sequence Length: 215
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22890
Sequence Length: 207
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23362
Sequence Length: 213
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23016
Sequence Length: 208
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30467
Sequence Length: 277
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22235
Sequence Length: 200
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21024
Sequence Length: 198
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21249
Sequence Length: 203
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28494
Sequence Length: 252
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
|
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-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21203
Sequence Length: 198
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
|
Q51915 | MTKPSTFTACKLASAVFGALLFSSVPAHAADIWLDVATTGWATQNGGTKGGSRAAANDIYTVKNAAELKKALSASAGSNGRIIKITGIIDVSEGKVYTKTADMKVRGRLDIPGKTTIVGIGSNAEIREGFFYAKENDVIIRNITVENPWDPEPIFDKDDGADGNWNSEYDGLTVEGANNVWVDHVTFTDGRRTDDQNGTEHERPKQHHDGALDVKNGANFVTISYSVFKSHEKNNLIGSSDSRTTDDGKLKVTIHNTLFENISARAPRVRYGQVHLYNNYHVGSTSHKVYPFSYAHGVGKNSKIFSERNAFEIAGISGCDKIAGDYGGSVYRDTGSTLNGSALSCSWSSSIGWTPPYSYTPLAADKVAADVKAKAGAGKL | 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
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
Subcellular Location: Secreted
EC: 4.2.2.2
|
P40972 | MDVYRIRISVFFLLVLLTFAALTTATNIPRRQLSNKKYKGPCRAENAIDKCWRCDPNWAENRQKMADCALGFGSNAIGGKLGRIYVVTDNSDDDVVDPKPGTLRYGVIQKEPLWIIFGKNMKIKLSRELIVTSNKTIDGRGFNVHIQNGAGIKIQSASNIIISNLRIHNIVPTPGGLLRESEDHVGLRGSDEGDGISIFSSHDIWIDHISMSRATDGLIDAVAASTNITISNCHFTDHEKVMLFGANDHYVLDKDMKITLAYNHFGKRLDQRMPRCRFGFFHLVNNDYTHWERYAIGGSSGATIISQGNRFIAEDELLVKEVTYREKLTASVAEWMKWTWISDGDDMENGATFTPSGDQNLLDKIDHLNLIKPEPSSKVGILTKFSGALSCVKGRPC | 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 degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
EC: 4.2.2.2
|
O24554 | MATTILPLILFISSLAIASSSPSRTPHAIVNEVHKSINASRRNLGYLSCGTGNPIDDCWRCDPNWANNRQRLADCAIGFGKNAMGGRNGRIYVVTDPGNDDPVNPVPGTLRYAVIQDEPLWIIFKRDMVIQLRQELVMNSHKTIDGRGVNVHIGNGPCITIHYASNIIIHGIHIHDCKQAGNGNIRNSPHHSGWWTQSDGDGISIFASKDIWIDHNSLSNCHDGLIDAIHGSTAITISNNYMTHHDKVMLLGHSDSYTQDKNMQVTIAFNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSASPTIYSQGNRFLAPNTRFDKEVTKHENAPESEWKNWNWRSEGDLMLNGAYFRESGGRAASSFARASSLSGRPSTLVASMTRSAGALVCRKGSRC | 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 extensible.
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): 44407
Sequence Length: 401
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
EC: 4.2.2.2
|
B2FHL8 | MSLPLRLALLPTLLASASAFAACPAPPPGQPDIRAIGYYTDKAGSVIDPALQQQNKDATAPLDRYAADVARMSDDYLRNGDPAAAQCTLSWLGAWADDGAMLGQMIRVNNDQSFYMRQWMLDAVAMAYLKVHDQANPQQRARIDPWLQKLARANLAYWDNPKRRRNNHYYWGGLGVLATGLATDDDALWQAGHAAFQKGIDDIQDDGSLPLEMARGQRALHYHDYALAPLVMMAELARLRGQDWYASRNHAIDRLARRVIEGSRDPAWFNQHTGAAQLPLQASGWVEFYRLRSPDGGVFDAAHARGPFHSPRLGGDLTLMATHGIVRTPLR | 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 hyaluronate (HA) as well. The oligosaccharide products formed by enzymatic cleavage are comprised mainly of disaccharides, with a lower abundance of trimers and pentamers. Is not active on poly-D-galacturonate, heparin and heparin sulfate.
Catalytic Activity: Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36696
Sequence Length: 331
Subcellular Location: Cell outer membrane
EC: 4.2.2.-
|
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 | MSEKIHITQNSGNVDHTVEALGHAISGGVAGMAAIALTYPFSTVSTRLQVQQKKQQQGQQSEITTVPYKNSIDAFKRIIKEENWRTLYSGLKSALIGIGASSFVYYYWYTLLKSISLKLKNKQELGTIENLAIAALAGCANVLTTLPIWVVNTRLQINSDKGIVGQFKYIIKNEGFGGLYKGLIPALILVSNPSVQFVSYEKLRALWRRQSGRTKLGGLEVFILGAIAKLIAGIVTYPYLLVKSRLQSQSGNASNPESQQQQYKGTLDAIGKIFKSDGFLGFFKGMPSKMVQTVIGAAFMFLVKDKVVIHAVAILFYLKRLLNKNNKRV | 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 (PAP). May catalyze the transport of free CoA, FAD and NAD(+) from the cytosol into the peroxisomal matrix by a counter-exchange mechanism.
Catalytic Activity: AMP(out) + CoA(in) = AMP(in) + CoA(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34567
Sequence Length: 307
Domain: The N- and C-terminal portions are exposed to the cytoplasm. Lacks a typical peroxisomal sorting signal. A region between helical transmembrane domains (TM) 4 and 5 and TM1-TM3 or TM4-TM6 are necessary for the peroxisome-targeting activity.
Subcellular Location: Cytoplasm
|
Q9FM79 | MKVEAFIPAVLLLCFGVMLCLKSSCALQIGNNNELKNYISWEDLRVVEDGRIERSFSIKENSNWVTTNANANANATNVRRVIVVDKNGGGDSVTVQGAVDMVPDSNSQRVKIFILPGIYREKVIVPKSKPYISFIGNESYAGDTVISWSDKASDLGCDGKELGTYRTASVSIESDFFCATAITFENTVVAEAGEQGRQAVALRIIGDKAVFYRVRVLGSQDTLFDDNGSHYFYQCYIQGNVDFIFGNAKSLYQDCDIHSTAKRYGAIAAHHRDSETEDTGFSFVNCDISGTGQIYLGRAWGNYSRTVYSNCFIADIITPVGWSDWKHPERQRKVMFGEYNCRGRGAERGGRVPWSKTLTRDEVKPFLGREFIYGDQWLRL | 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 degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
|
Q8L7Q7 | MDSPTLPHSISASSSTPFASAAVKPHRNKLLSRNGILIIIAASCILLLLISLLIYATVSKSSRNHHNPSHQTPTSDDHPPPETPPSPPPIAQIRLACNATRFPDHCVASLSKPGQVPPDPKPVQIIHSAISVSYENLKSGQSKIQSILDSSAGNRNRTNIATICLEILSYSQHRTESTDIAVTSGDIKDARAWMSAALAYQFDCWSGLKTVNDTKQVVDTITFFEGLVNLTGNALSMMLSFDSFGDDVVSWIRPATERDGFWEKAGPSLGSGTGTEASLGFPSGLTEDVTVCKNGGKDCKYKTVQEAVDSAPDTNRTVKFVIRIREGVYEETVRVPFEKKNVVFIGDGMGKTVITGSLNVGQPGMTTFESATVGVLGDGFMARDLTIENTAGADAHQAVAFRSDSDFSVLENCEFLGNQDTLYAHSLRQFYKQCRIQGNVDFIFGNSAAVFQDCDILIASKHSKLEQGGANNAITAHGRIDASQSTGFVFLNCSINGTEEYMKEFQANPEGHKNFLGRPWKEFSRTVFVNCNLESLISPDGWMPWNGDFALKTLYYGEYKNTGPGSVRSSRVPWSSEIPEKHVDVYSVANFIQADEWASTTA | 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 Length: 602
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Membrane
|
Q4PSQ5 | MKRVASYNYKIVCMVVMTLFVYGYSAAAEQIAYTITVDLNGGGNFTTVQSAIDSISPPNHNWIRVFTQNGIYREKVTIPKEKGFIYLQGKGIEQTVIEYDDHQATDISATFTAFADDIVISGITFKNTYNIVPNNKREIVPAVAARMLGDRYVVTDSSFVGLQDTLFDGKGRHYYKRCIISGGIDFIFGYGQSLFKECTLNMTLGIYAPDNPYGTITAHQRPSPSDEGGFVFSDCTVTGVGKTLLGRAWGSNARVIFDRSRLSDVVLPIGWDAWRAKGNERDLTFVEAGCTGAGADTSQRVPWLKKLSLSEVDGFASVSFIDQDGWISRFPIEGGP | 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 degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
|
Q9LSP1 | MGHRTRMILVLTLVVMSIWGSDASAMQKTKFDAPLLTEKIATNRSIIVDIEGKGDYTSVQKAIDAVPVGNSNWIIVHVRKGIYKERVHIPENKPFIFMRGNGKGKTVIESSQSSVDNVASATFKVEANHFVAFGISIRNDAPVGMAFTSENQSVAAFVAADKVAFYHCAFYSLHNTLFDNKGRHYYHECYIQGSIDFIFGRATSIFNNCEIFVISDKRVKPYGSITAHHRESAEEKTGYVFIRGKVYGIDEVYLGRAKGPYSRVIFAKTYLSKTVVPDGWTNWSYHGSTQNLYHGEYKCHGPGAERQKRSDWAKDLTKQEVESFLSIDFIDGTSWLPVWLQEKF | 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 degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.