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Database: UniProt
Entry: A0A139ICK2_9PEZI
LinkDB: A0A139ICK2_9PEZI
Original site: A0A139ICK2_9PEZI 
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
//
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