ID A0A066XF11_COLSU Unreviewed; 579 AA.
AC A0A066XF11;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 03-MAY-2023, entry version 33.
DE RecName: Full=Putative phospholipase {ECO:0000256|PIRNR:PIRNR018169};
DE EC=3.1.1.47 {ECO:0000256|PIRNR:PIRNR018169};
GN ORFNames=CSUB01_06112 {ECO:0000313|EMBL:KDN66199.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN66199.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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 -!- SIMILARITY: Belongs to the serine esterase family.
CC {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:KDN66199.1}.
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DR EMBL; JMSE01000958; KDN66199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XF11; -.
DR STRING; 1173701.A0A066XF11; -.
DR eggNOG; KOG3847; Eukaryota.
DR HOGENOM; CLU_024458_0_0_1; -.
DR OMA; FCPEHRD; -.
DR OrthoDB; 2787776at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016715; PAF_acetylhydro_eukaryote.
DR PANTHER; PTHR10272:SF7; PHOSPHOLIPASE-RELATED; 1.
DR PANTHER; PTHR10272; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR Pfam; PF03403; PAF-AH_p_II; 1.
DR PIRSF; PIRSF018169; PAF_acetylhydrolase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR018169};
KW Lipid degradation {ECO:0000256|PIRNR:PIRNR018169};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR018169};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238}.
FT ACT_SITE 278
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 329
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 419
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
SQ SEQUENCE 579 AA; 63469 MW; E6DCBCC41F4A7482 CRC64;
MSPAAKAPPT AAEKVASFFS RLSPVPAFPD YTGPYKVGTV DIEVPVAELE SPSPTPYSAS
EILTVQCRVF YPATPDSNGK RINWLPSPQR HHVSAYTQFI GIRPMLAEIV SFLPRHLHYT
TIPVHKNAEI LDPDTPNRRW PTMIFSHGLG GNRNTYSHLA GSLASHGVVV ICPEHRDGSA
VASFVRIPGK QDQYFLRDTR RTIPYVRLDH EPRPEIYEAR EDQLRIRLWE LGLIHVVALN
MDLGLAMSNL NKSTPSLTQF KNKLHVHEPG SIIFGGHSFG AASIVQFLKT TYYADSSALA
HVPKPLFTPR RDSALCQQIT EKNVTMLLDM WCFPLLAPGS AELFDLPLPA YANSPSAPGG
TALLAVESDA FVKWTDHLHV TARVLSPQPS ASVITPQLFS RSGVRLAEPN FFYVRNSAHL
SQSDFGILFP WLTKKIFNSE EPERALRLNL RAQLQLLRSN GVPVARTWIG DLVDGTGSGK
MGIAGDEDAD NGPDDGLMDD KAIFDRSEGK VRFWKWIDVI GMGEPGDAVP AARTTTNGVG
GSTVDAQVAG VERTNQDMED ELEPLQAVAS AAQAATVRS
//