ID F9WED8_TRYCI Unreviewed; 446 AA. AC F9WED8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 03-AUG-2022, entry version 28. DE RecName: Full=1-alkyl-2-acetylglycerophosphocholine esterase {ECO:0000256|ARBA:ARBA00013201, ECO:0000256|PIRNR:PIRNR018169}; DE EC=3.1.1.47 {ECO:0000256|ARBA:ARBA00013201, ECO:0000256|PIRNR:PIRNR018169}; GN ORFNames=TCIL3000_0_00740 {ECO:0000313|EMBL:CCD15645.1}; OS Trypanosoma congolense (strain IL3000). OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas. OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCD15645.1, ECO:0000313|Proteomes:UP000000702}; RN [1] {ECO:0000313|Proteomes:UP000000702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IL3000 {ECO:0000313|Proteomes:UP000000702}; RA Jackson A.P., Berry A., Allison H.C., Burton P., Anderson J., Aslett M., RA Brown R., Corton N., Harris D., Hauser H., Gamble J., Gilderthorp R., RA McQuillan J., Quail M.A., Sanders M., Van Tonder A., Ginger M.L., RA Donelson J.E., Field M.C., Barry J.D., Berriman M., Hertz-Fowler C.; RT "Divergent evolution of antigenic variation in African trypanosomes."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCD15645.1, ECO:0000313|Proteomes:UP000000702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IL3000 {ECO:0000313|EMBL:CCD15645.1, RC ECO:0000313|Proteomes:UP000000702}; RX PubMed=22331916; DOI=10.1073/pnas.1117313109; RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P., RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J., RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A., RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D., RA Hertz-Fowler C., Berriman M.; RT "Antigenic diversity is generated by distinct evolutionary mechanisms in RT African trypanosome species."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012). CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O- CC alkyl-sn-glycero-3-phosphocholine + acetate + H(+); CC Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; CC Evidence={ECO:0000256|PIRNR:PIRNR018169}; CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:CCD15645.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CAEQ01001995; CCD15645.1; -; Genomic_DNA. DR SMR; F9WED8; -. DR VEuPathDB; TriTrypDB:TcIL3000_0_00740; -. DR OMA; YSTLLMD; -. DR OrthoDB; 1189747at2759; -. DR Proteomes; UP000000702; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR005065; PAF_acetylhydro-like. DR InterPro; IPR016715; PAF_acetylhydro_eucaryote. DR PANTHER; PTHR10272; PTHR10272; 1. DR Pfam; PF03403; PAF-AH_p_II; 1. DR PIRSF; PIRSF018169; PAF_acetylhydrolase; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR018169}; KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, KW ECO:0000256|PIRNR:PIRNR018169}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, KW ECO:0000256|PIRNR:PIRNR018169}; Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000702}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32..52 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 58..80 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT ACT_SITE 289 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1" FT ACT_SITE 319 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1" FT ACT_SITE 398 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1" SQ SEQUENCE 446 AA; 49450 MW; C52C319D684B473B CRC64; MPFWTQKDVA RLVRWSTESF FLGHSLPLRG RLTSLHFAPV SVALVSSFVM YLNGMSSMWS SLAVCIGVLV SGGMFIVFPL PVLRPIGGRY CVSIAHMDGR ASQQLPPVAV FYPTNMSPDI KGISYVPFDD SRFIRGVAAY AKLPYFFLKD FMLLRVGATM NAVQADILSN GRMPPIVVFS HGLAGYHRLY SCFAMDLAAR GAVVVSVGHC DNSASFMRDS TGEESAVYLK DYGWQVPKRE MQISKRVKEV RRVLERLGET DFWTDLGCSA SDAENFLSRR PQVHLSGHSF GGATALAVAL EESQNATKVV NVRSVFVYDP WMLPIQGEHF FKPLSDGSKA YCIPTVTIHS DDWVNDSESW SFFQKVKSVV LAQPSYASLG SDEREAKFRT LITRNTSHIS MVDIAVLSPV IHGKVNSVVS PRVQIMEWCN ALLQFARANT VVSDLS //