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Database: UniProt
Entry: A0A0C4DYW3_MAGP6
LinkDB: A0A0C4DYW3_MAGP6
Original site: A0A0C4DYW3_MAGP6 
ID   A0A0C4DYW3_MAGP6        Unreviewed;       814 AA.
AC   A0A0C4DYW3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=MAPG_05244 {ECO:0000313|EMBL:KLU86227.1};
OS   Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS   fungus) (Magnaporthe poae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX   NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_05244T0, ECO:0000313|Proteomes:UP000011715};
RN   [1] {ECO:0000313|Proteomes:UP000011715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA   Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KLU86227.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU86227.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KLU86227.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU86227.1};
RA   Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of Magnaporthe poae ATCC 64411.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EnsemblFungi:MAPG_05244T0}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_05244T0};
RX   PubMed=26416668; DOI=10.1534/g3.115.020057;
RA   Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA   Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA   Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA   Ma L.-J., Dean R.A.;
RT   "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT   family of fungi.";
RL   G3 (Bethesda) 5:2539-2545(2015).
RN   [5] {ECO:0000313|EnsemblFungi:MAPG_05244T0}
RP   IDENTIFICATION.
RC   STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_05244T0};
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; ADBL01001241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADBL01001242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GL876969; KLU86227.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C4DYW3; -.
DR   STRING; 644358.A0A0C4DYW3; -.
DR   EnsemblFungi; MAPG_05244T0; MAPG_05244T0; MAPG_05244.
DR   VEuPathDB; FungiDB:MAPG_05244; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   OMA; WALGRRF; -.
DR   OrthoDB; 1997175at2759; -.
DR   Proteomes; UP000011715; 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; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF40; WW DOMAIN-CONTAINING PROTEIN; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000011715}.
FT   DOMAIN          179..803
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          611..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          683..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          763..790
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        624..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   814 AA;  89294 MW;  77F229EE972EB0E0 CRC64;
     MARLVRAAVR PGGPAHLVAS RAISLRPGLG PLGNIRLRPV FSLAKRPSTP RHRTPLAPLL
     VGGGLLVYSL YPSDDYQRVQ RHRTKAAATW FPMTETGGGD VQGCGAQQSA RSAFAGGFES
     ISKMTEGDWG ASKVVDFILP EWTKLLPGYL RKLQRELSLA PGSLADEVWA EAHDPSVHPE
     IQYAASVRVS SDLCEDEKSF LERRRKVARV ALAKYLGLAE EDIHPDDMPT IGICGSGGGL
     RALVAGAGSM CAASEDGLFD CVTYIAGVSG SCWLQSMYFS TITNCNMHHL IDHLKARLSV
     HIAFPPAAFS ALVSAPTNKP LLSGLIEKLK GDPNADFGLV DVYGILLAAR LLVPRGELDV
     DERNFKLSNQ RQYIRAGANP LPIYTAVRHE IPDVDVDTPP EVPSASEESK EKAKKEAWFQ
     WFEITPYEFF CEEFAAGIPT WAMGRRFYDG KDVLQPGGLH MPEIRMPLLL GMFGSAFCAT
     LSHYYREIQP LVQSISGFAA IDEAISGRNE DLSKVHPIDP TSLPNPVYGM DEGKLPKTTP
     TNLPRSEYIQ LMDAGMSNNL PIYPLLRPGR NVEIIIAFDA SADIKTDNWL SVADGYARQR
     GIKGWPVGIG WPKEEAPPQE TAEQLEEASA SSTAEAESKL QGAQAHQAVE QLGDSGGSGP
     GNKNKYEQAA KTLGYCTVWV GTTQERSTEP PPPIKSDGDG DSWRLMEPDA GIAVVYMPFL
     PNDKVADVDP ATSDYMSTWN FTYTPDQVDK VVALAKVNYG EGREQIKATV RAVYERKKKL
     REQREEAARR ERYRRLIRRG DVGKLGEWEG DHFS
//
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