ID F9F248_FUSOF Unreviewed; 576 AA.
AC F9F248;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=1-alkyl-2-acetylglycerophosphocholine esterase {ECO:0000256|ARBA:ARBA00013201};
DE EC=3.1.1.47 {ECO:0000256|ARBA:ARBA00013201};
DE Flags: Fragment;
GN ORFNames=FOXB_00472 {ECO:0000313|EMBL:EGU88960.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU88960.1};
RN [1] {ECO:0000313|EMBL:EGU88960.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU88960.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU88960.1}.
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DR EMBL; AFQF01000132; EGU88960.1; -; Genomic_DNA.
DR AlphaFoldDB; F9F248; -.
DR STRING; 660025.F9F248; -.
DR PaxDb; 5507-FOXG_01282P0; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016715; PAF_acetylhydro_eukaryote.
DR PANTHER; PTHR10272:SF11; 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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 421
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 485
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGU88960.1"
SQ SEQUENCE 576 AA; 63823 MW; F0159B74984FA8B0 CRC64;
PLASSPPSSL TNKKHSTHHL TSHHFPHHNL LVLILIPQEM PQSQNSIDLE LNRLNSPFSD
SSSDPDLPLT MDPPAPKPRW LDPRPSSIFT RITSSVKPFA QYLRHVLRPR LTWRYVACSV
IGVYVLYCFV TWQPFFSSRL PAYSGPHDVG AIDLEIPLEK PKRLSETLLK STKKPAFEVE
SVLFTVYYPA VKGARSKDAP HPWVPKPLSL TAEGYARAAG VNNFIIRPIF TFALWVLVGS
IKIPAKVDVP LLGSDGEKFP VMVFSHGSVS SRTDYTHYLG ELASRGHVIA ALEHRDGSCP
GSMVQIKNKK DRPVFLLKEG DLISEPPMND TLLKKEQLAF RTEEIMQAIR VLKDVNDGKG
KDIFTSSSRG EGSTLDGWKD RLDFKHLTIS GHSYGATGAL QALKTANTTA ANPAIGGIAL
DPGKSSGQLN TNIPVPLLVV HSNSWSKTHS IFFGRPHFDT VLDLVRGVRD KVGSAWFLTS
VGTAHPSVTD APLLQPLLLN FATGATADVK KALGEYVKVT MDFLEFTKTN KENGVLDEAV
THEKYGEWVS KEREKSFPKE YAKYWEVHVC PLDQDK
//
