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Database: UniProt
Entry: U5H9A3_USTV1
LinkDB: U5H9A3_USTV1
Original site: U5H9A3_USTV1 
ID   U5H9A3_USTV1            Unreviewed;      1267 AA.
AC   U5H9A3;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE            EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN   ORFNames=MVLG_03795 {ECO:0000313|EMBL:KDE05852.1};
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:KDE05852.1};
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:KDE05852.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE05852.1};
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:KDE05852.1, ECO:0000313|Proteomes:UP000017200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200}, and P1A1
RC   Lamole {ECO:0000313|EMBL:KDE05852.1};
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_03795T0}
RP   IDENTIFICATION.
RG   EnsemblFungi;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty
CC         acid + H(+); Xref=Rhea:RHEA:33275, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:28868; EC=3.1.1.116;
CC         Evidence={ECO:0000256|ARBA:ARBA00024531};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33276;
CC         Evidence={ECO:0000256|ARBA:ARBA00024531};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AEIJ01000371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GL541680; KDE05852.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5H9A3; -.
DR   EnsemblFungi; MVLG_03795T0; MVLG_03795T0; MVLG_03795.
DR   HOGENOM; CLU_001871_1_0_1; -.
DR   InParanoid; U5H9A3; -.
DR   OMA; SWKVHKG; -.
DR   OrthoDB; 373802at2759; -.
DR   Proteomes; UP000017200; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00519; Lipase_3; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002921; Fungal_lipase-like.
DR   PANTHER; PTHR45792; DIACYLGLYCEROL LIPASE HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR45792:SF7; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G02710)-RELATED; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017200};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          898..1062
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          43..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..738
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1267 AA;  137013 MW;  F118B34ABFB2056E CRC64;
     MFPSSLSSAD PTTGDPAPRS TPRSTPRTRT DSFAMTAANA LGPCPFSSSS SPPNSIMTGS
     RRRSVSAAMD NLPLDAPPSL LIQSEILARL AHGPTLLPSS LAHLISAISV CSRVSIRSAA
     LFIEAILESI RQGTTAGLGL ARRALISAVA SARTLHYVAK GLDWDGRNAQ GQRDLGLYLG
     LLDRYTNLGI YVINHTFTLA ELFSLAGLSL TMSTTSLAFA TAEESVRMLD SLLGSGETSR
     ALSAIIALVR TEMAEDPNFK IIDDGVISTL ALLTRTLTAF VCLQAATSKR TARQMKMRVV
     YDCTVVAEGE EMITGCVPFP TTTQGSADEP SSAPALEDHY VREHRRSRAS SIELVAQEFR
     RDPHGSLLGS TSPKLMRSRT KSIGHEEIDV QRNEREEETE IVEELNELCG LDQDQMAFGS
     DQVDADDALV RLPPEVSAAL EELKHSAAGK TIVTSSMGSH YEVEVTETTT TTTTTVRATA
     STMGGDGYST RTLSKRTAPR TRPLSSIFQI AVPQASDVEE GDVSMDDAGD PSPGNSSDEW
     VDVGEQSPKQ QPDDVFGPEE SVAAGPSGEG SRNAKLQVVF RTMTSKFTQR KRTFRRVDRN
     ETVTTTSTST LSSGESTPRP RRIAVSSEIE EPCSPDSAAS RKSPRRILKA LGKALKRNPS
     VENVSSSSPP VSSRSSRTVS RESTNSAGST EQVSRLPSTP PKMPGKTPLA QINDTRSATA
     SFASSRRPSL SDLATTSRRG SKVPLEPLNL TGAQVPAQIS TSSGPVPKLR RAESMVSIVT
     TCKHSQATPM EEPEPKASNF PRQHLVANLQ RFMRYSSAAY GQAFLRILGL GKSRGLDFSF
     PNTKSHANSH AFAHHVGIPV DDILIDSYTT PGGGIFDNHR ISPIVTYLAV DHEMKAIVLS
     CRGSLGLSDV LVDLVCSYEQ IHVPDGDTMA LYQVHAGMWH AATRLQRGLV HKTIKEALEQ
     YPSYGLVLTG HSLGGGVSSL LSLLWSTPSH VFERNRRPVD IGRHPPIHTP FVTSYASGLP
     AGRPIHCYVF GPPCVASPDL GRYCQGLVTS TTHNNDVVPT LSLGTLRDLK TMAMNLHEDG
     GTGTTREIIG RVCGIYQRKI TLATSERLYR GLPGGSEKEI PSLHDVSDEA RLVALTKAEI
     SAGRGKNRAL DPAYCDPTLL QESEEPEDVV VNDYLWSVMR TLRADNDNDK LYPPGNVFVV
     ENHTVFISSE SRPGQYARRE GRRILLRAVD DVEKRFAEPV FGKTLFMDHS PTGYEENVDL
     LARAVLG
//
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