ID W9XA14_9EURO Unreviewed; 809 AA.
AC W9XA14;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=A1O3_10216 {ECO:0000313|EMBL:EXJ77058.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ77058.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ77058.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ77058.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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|ARBA:ARBA00000960,
CC 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:EXJ77058.1}.
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DR EMBL; AMGY01000011; EXJ77058.1; -; Genomic_DNA.
DR RefSeq; XP_007738496.1; XM_007740306.1.
DR AlphaFoldDB; W9XA14; -.
DR STRING; 1182542.W9XA14; -.
DR GeneID; 19174296; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_013227_1_0_1; -.
DR OrthoDB; 1997175at2759; -.
DR Proteomes; UP000019478; 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 CDD; cd00147; cPLA2_like; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019478}.
FT DOMAIN 172..800
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 33..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 89426 MW; EFA39E8CE0C2E054 CRC64;
MGAARLLNSS RLRQTALLAA ACAGVHSATR RSPLVRLDSP SGTHIPQDAS LVSYTRRKQN
DRAQAEDAKH AATPGDVQPI GKANDLEHYT PAFEPDDENS WAVFSRNFQN FREGIASIEW
SSIPDKITDF VLPSWAKLLP EGIQKLQLEL SMQPGSLADE IWQEAHDPEI NPEILWNATV
RVGDTLGPDE LEFRRKRKER VVKALAKYLD INETEIHPDD VPTIAMCGSG GGLRAMVAGT
SSYLSAQDAG LFDCVTYMAG VSGSCWLQSL FFSSLGKQDF RSLLKHLKAR LGTHIAFPPA
ALKLVTSAPT NKFILSGFIE KIKGDPGASF GLVDVYSLLL AARLLVPHGD LDVHDQDLKL
SNQRMYLANG EYPLPIYTAV RHEIPVDEEE IEEAKDNLAL KEEIKDKAQK EAWFQWFEMH
PWEVWCEEFG AGIPTWSLGR PFNKGQNQLL DTGVALPEIR QSLLLGVWGS AFCATLSHYY
KEIKPALVGI VGFGGLDGLL EEKNDDLMKI HPIDPATFPN FVYGMKDQLP STCPDSVFKN
GHLQLMDAGM SNNLPIYPLL RPGRDVEILI AFDASADIQR ENWLSVVDGY AKQRGVKGWP
VGAGWPQASS KPQENALALE EAQATSAQEA ATKVAEAREG SREAKASGSI GSNAPESPTT
GQRPDAETTL GACNVWVGTK AERSIDREPP PSKRLAWDDL DDSTFHLMHP EAGLAVVYFP
LIPNPKVKGV DPDKTDYMST WNFVYTPEQI DDVVALAKAN FEEGADVTKQ TVRAVYERKK
RVRMEREARE RRKAWKVTLR EHGDHFGGA
//
