ID A0A139ICK2_9PEZI Unreviewed; 673 AA.
AC A0A139ICK2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AC579_7358 {ECO:0000313|EMBL:KXT12458.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT12458.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT12458.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT12458.1,
RC ECO:0000313|Proteomes:UP000073492};
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:KXT12458.1}.
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DR EMBL; LFZO01000150; KXT12458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139ICK2; -.
DR STRING; 113226.A0A139ICK2; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
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:SF40; LYSOPHOSPHOLIPASE; 1.
DR Pfam; PF01735; PLA2_B; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492}.
FT DOMAIN 99..673
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 75669 MW; 960B8D7E40F52863 CRC64;
MHDHSNIRRS ETAEQRQYEQ EVHEKQDFSS TPGDIDSEMD EKMHISNDAT KREGPMERFY
HNVVKPAFPE AIADIKIMGG MTALETRVKH DIQNPKLFPE IERIAHVRRG IDLCPEELAF
LAKRKARCRD AFAKYIGVDP VDVNAEDVPT VSFGGSGGGF RAMIGTLGYC EEMKQTGLWD
CLTYVAGVSG SCWSLAAYYT FGRGSMQAVL DHCKKRFSPY HPLSGDAIRT LLSVPGGAKI
TLGPLIQKSK SGLQTVAMDL YSVFATGWIF FQDDPASHPG GHANREVAGM QKSWYRWSTA
RQYTDEGTDP LPIITAIRHE RPWRDWEDKE HPFKDADHSS GDHTDATEAW FQWFEMTPYE
VGCDEIEAWV PTWGFGRPFE QGKSTMQLPE QSLALLLGLA TSAPAGPLTS YISTISRNLP
GGFLGNTVHK MAHAVTEFWG KDGTEEFRNH HPLHACNEHN FMYHYSHVEP AQGRPPGLEN
SPRIHLIDSG MDNNCPTYVL LHPKRDADVI INMDASSDVQ KDTFQERVDQ IGSRRGLKFT
KRHDIKPGND EKDPNRFNGL YAQIYDGKPA PRPDTVVDSY GRTVVNPPAP LFTKECTMIY
MPLLPNEKAV PGFDPSTAKF SGSYNLVWTA DQVETLVKVC KANFDEAQGT IKEALHEAWQ
RKKAARDEQH CEF
//