ID U5HAZ3_USTV1 Unreviewed; 618 AA.
AC U5HAZ3;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=MVLG_04357 {ECO:0000313|EMBL:KDE05220.1};
OS Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther
OS smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=683840 {ECO:0000313|EMBL:KDE05220.1};
RN [1] {ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200};
RA Cuomo C., Perlin M., Young S.K., Zeng Q., Gargeya S., Alvarado L.,
RA Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Mehta T.,
RA Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Microbotryum violaceum strain p1A1 Lamole.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KDE05220.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE05220.1};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Yandava C., Wortman J., Nusbaum C., Birren B.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KDE05220.1, ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE05220.1}, and p1A1 Lamole
RC {ECO:0000313|Proteomes:UP000017200};
RX PubMed=26076695; DOI=10.1186/s12864-015-1660-8;
RA Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J.,
RA Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E.,
RA Badouin H., Andrews J., Razeeq D., Gabaldon T., Quesneville H., Giraud T.,
RA Hood M.E., Schultz D.J., Cuomo C.A.;
RT "Sex and parasites: genomic and transcriptomic analysis of Microbotryum
RT lychnidis-dioicae, the biotrophic and plant-castrating anther smut
RT fungus.";
RL BMC Genomics 16:461-461(2015).
RN [4] {ECO:0000313|EnsemblFungi:MVLG_04357T1}
RP IDENTIFICATION.
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR EMBL; AEIJ01000427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL541690; KDE05220.1; -; Genomic_DNA.
DR AlphaFoldDB; U5HAZ3; -.
DR EnsemblFungi; MVLG_04357T1; MVLG_04357T1; MVLG_04357.
DR HOGENOM; CLU_013227_1_0_1; -.
DR OrthoDB; 1997175at2759; -.
DR Proteomes; UP000017200; 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:UP000017200}.
FT DOMAIN 1..618
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 187..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 69188 MW; 29CA197C794559B0 CRC64;
MKVHFARLMD LHEEEIDVRD LPVIAMAGSG GGYRAMVNTL GSVKAAQESG VWDVVSYVSA
ISGSCWAIST YYSIGEGNID RTLDHIKKRM QQHFLDPTTL EWLIQPKTNQ YVLSGAILKG
ASKAGTLSLV DAYGTAVASR LYVPDDPEAE LSLENLKISH QRVHIDSGEH PLPIYCTIRH
EIPRAAEVDK ADSESKDENR TDAERKGAKE KKEELLLEGR WMWFETTPHE VGCDELGAWI
PTWSLGRAFE NGKSVERVPE LSLTIMSGVF ASAFCATLYS YFKEIRPVLG TLPFFDTINS
FVMDRQPQLD SIHPLPPAEF PNFLKGLAGK LRPGAPQDIT QLTSLGFMDA GANLNIPYVP
LFRRDVDIAI ALDASADSQD LWFETAHQYA EARELKSWPR VDWKGLFKDL KEEASSGSKE
KNEKDKKASS DQAASKVDAA KLQEKEAKLA NGGIEHKEQE INPQRPPVGS APHSMKLNNE
GEEVRKEGEE ETVDKLPTSQ EGEPPLGKCN IWIGSTQDED APCRNDNPTV QQVMERDGIS
LVYYPLTSGP ELENVSEVWS TWRFEYPEDE TERLIRLARA NFHSGDEQLK MLIRGVYERK
KKQRLANEAS DKKTRAKL
//
