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Database: UniProt
Entry: V9DBW2_9EURO
LinkDB: V9DBW2_9EURO
Original site: V9DBW2_9EURO 
ID   V9DBW2_9EURO            Unreviewed;       676 AA.
AC   V9DBW2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=G647_05254 {ECO:0000313|EMBL:ETI23452.1};
OS   Cladophialophora carrionii CBS 160.54.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1279043 {ECO:0000313|EMBL:ETI23452.1, ECO:0000313|Proteomes:UP000030678};
RN   [1] {ECO:0000313|EMBL:ETI23452.1, ECO:0000313|Proteomes:UP000030678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 160.54 {ECO:0000313|EMBL:ETI23452.1,
RC   ECO:0000313|Proteomes:UP000030678};
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 Cladophialophora carrionii CBS 160.54.";
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}.
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DR   EMBL; KB822705; ETI23452.1; -; Genomic_DNA.
DR   RefSeq; XP_008727807.1; XM_008729585.1.
DR   AlphaFoldDB; V9DBW2; -.
DR   GeneID; 19983747; -.
DR   VEuPathDB; FungiDB:G647_05254; -.
DR   HOGENOM; CLU_013227_0_0_1; -.
DR   OrthoDB; 1997175at2759; -.
DR   Proteomes; UP000030678; 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}.
FT   DOMAIN          83..676
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   676 AA;  74747 MW;  100C312F80F644E9 CRC64;
     MPDRGGEDGR DGKDEDGHER PSSSPSAGSS GARAKVKGKL KSFWNKTVVP AFPEAIADIS
     IIKAALKVEA TITKDLRDTS RHPEVAQSAT VRRGFELAPE EMRFRDVRKV KVRDAFCRYL
     GLDPAEVHVD DVPIVAFGGS GGGYRAMIGM LGYGDEMKRT GLWDVLTYVS GVSGSCWSLA
     AYYTWAGTSM DAVIRHCKQR LHPHHPLSPE AIREVLHAPG GPSKTLGPLV QKHRTGLSTV
     AMDLYSVFTT GHLFLVHDPA LEPPGSHGRS GVKKEVAGQH EQWFKWSSAN AHLVDGQEPL
     PILTAIRHER PWKDWVDQEH PFKDADPGAK EHEEAQDAWF NWFEISPIEV GCDELEAWCP
     TWAFGRPFEK GRDTMQIPEQ SLALLLGLCT SAPAGPLTSY LATIKRSLPS GFIGNSINDM
     AKGVARMWGE KGTEEFQAHH PLHAVNEHNF MFHLSKGENK DTPSPPIENS PRIHLIDSGM
     DNNCPTYVML HPRRNVDVIL NMDASSDVLK GTFQDRVDQI ASRRCLKFSK RYPELQAGTD
     PKNPDQFQGL YAQIYDGSIL VDRPEEVVDS YGHTVTNPPA PPCLHESTMI YLPLLPNQGA
     VPDFDPSTAK FSGSYNLVWT PDQVEMLVRI CCANFKAGEE TIKMVLREQW LKKRAKRETA
     AASVLPLADS PGEACA
//
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