ID A0A139HJK9_9PEZI Unreviewed; 1013 AA.
AC A0A139HJK9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Lysophospholipase {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
GN ORFNames=AC578_10653 {ECO:0000313|EMBL:KXT02593.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT02593.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXT02593.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT02593.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000256|RuleBase:RU362103};
CC -!- SIMILARITY: Belongs to the lysophospholipase family.
CC {ECO:0000256|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
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:KXT02593.1}.
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DR EMBL; LFZN01000040; KXT02593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HJK9; -.
DR STRING; 321146.A0A139HJK9; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR10728:SF33; LYSOPHOSPHOLIPASE 1-RELATED; 1.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51210; PLA2C; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW ProRule:PRU00555};
KW Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 108..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 404..966
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1013 AA; 109578 MW; 20373A8FF504D48B CRC64;
MTSDQSPESL PEPTSSTEKE ETYFDARHTS TPETLVADEN LIVYTSALSP PIQDGLGPRN
ELAEFVPLPT PNVLTPDKED IEPYAGIEGK SSPSPIPALP LNLNNHKIAI ACNWIPIIFS
GGLLPIIFYF SLHYTTSLET RYILTIPLVL TAITTLFSLG SSIYVLAKPG STCRPLGIES
EKWDWTTLDY FTYNYIFGFV VVTILISVGI GLENLRIVSL PLSILMLYIC AEMVIAEIGI
WCGWKAPFRI SSIPRGGALR PAVYVIVEDV VAVEGGMGRD WREVWGRRYD MDEGFKKFLK
GMDFVWGVTD SDSERRRTLT CSGGEGVPWC AVPAERKHAK AQIGFQPTVR GRAADVISSY
SRQQAERQAT PVQLSETEAR AILELAARAA PANQPNGYTP QTVPCPSATP AIRSAAQRSQ
EEIGWTETRR NATIEPMRDL LSRMNISGID TTAYIDNYQN NATALPNIGI AISGGGYRAM
LNGAGVLQAF DSRTPNATAV GQLGGLLQAA TYLSGLSGGS WLVSTLYGNN WTSVADIVSQ
DTSSDRSGGV WQLGHTIFEG PKTGGVQLLD SIGYYSALGD AVHGKEDAGF NTTITDYWGR
ALSYQMINAT DGGPAYTFSS IADQEWFRRG DAPLPLITID SRMPGETIVS TNSTVFTVSP
WEIGSDDPTL YAFAPLEYSG TNFSAGSPRN DDRCVVGFDN IGYVFGTSSS LFNAIITTVN
GTNTTGWTSS VLQAAITSIL SAIGEDEEDI ASWPNPFVNY NNDTNFNNNE LDLHLVDGGE
DGQNIPFHPL IQPNRNVDVI FAVDSSADTN DTFPTSDSAP GWPDGISIIT TYQRSLSDIG
NGTAFPKIPS LNTFMNLGLN SKPTFFGCDA SQLDGPAPLV VYMPNAPYVY TSNTSTFQME
YNDTERNAII LNGHNMATLG NGTVDNEWPQ CVGCAILSRS LNRTNTEVPD ICTQCFNRYC
WNGTEDDSTP GTYNPAFKLS ADDVIKVTSG AGTFSASTSL AISVAILAGF SVL
//
