ID M4BRE2_HYAAE Unreviewed; 981 AA.
AC M4BRE2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP808982, ECO:0000313|Proteomes:UP000011713};
RN [1] {ECO:0000313|Proteomes:UP000011713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [2] {ECO:0000313|EnsemblProtists:HpaP808982}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP808982};
RG EnsemblProtists;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH598638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M4BRE2; -.
DR EnsemblProtists; HpaT808982; HpaP808982; HpaG808982.
DR VEuPathDB; FungiDB:HpaG808982; -.
DR eggNOG; KOG1818; Eukaryota.
DR eggNOG; KOG2088; Eukaryota.
DR HOGENOM; CLU_300269_0_0_1; -.
DR InParanoid; M4BRE2; -.
DR OMA; RNEFMQS; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45792; DIACYLGLYCEROL LIPASE HOMOLOG-RELATED; 1.
DR PANTHER; PTHR45792:SF11; LIPASE_3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS50178; ZF_FYVE; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011713};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 297..357
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 912..981
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 93..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 981 AA; 109198 MW; DCF8B0CA5F1BA8B0 CRC64;
MPEVVENQRW YPFVGWTARL HAEDPPAWCN AQKDACPSKD EQKEFVWQVY KGRDYDEEGW
LYGENFQGTL GPMTRSSVVR TRVWMGNKLE VQEETADAAE IPVSEEDEEP LGTSGSKSKC
HTLVSSNDEP HKKDKNEGAT KTEEASVIEQ SEDDKTGEDV VLDASVEQNE TSEISSSWNF
FGRISSAALS LPSSAINLAG SSSKQAVYGT VQSIKEASLC GLEMAQAATA AAISSEPVIL
PHVKQKRRDD TDVLDEENNV EVLSMLSKRF PDLSPFHRSL VTCCKDGIVN FVSPPELTES
KVCKECNIEF GMTKFRYQCG YCSESFCRDD LPEVAIIRAY GHTCPSKLCK NCHYILMEKV
DQQLVQWRVE RVNDFLGGKI ILYYNTATDT AVDKIMRAAE GTLVAAKSAP IGAAAKMAVV
SADFLRKYGR AGLLGFILRN EFMQSFSTLK GLLGDLDNLG FQDAAIGTYY FMAMNRGDRG
AEPEGEKVNH NGCQPISDTL LQRMLKYAPL ALHGIYEHNV LDIQRISRLQ GLSLIYVHVQ
DQDVRHPSFA LLGNKENKTA LLVIRGSKSV QDALTDIQAF PEEIGLSSAG APQSEASGGF
VDAFAHNGML KAVMWIKDRI VKSLRVLHHE GYHIVFTGHS LGAGCAALLS IILQKEFEDL
ECFAYAVPAC VNLTVAESCD NFVHSIVLRD DIVPRAKASN VVKLVDELKN FKGCWRDTAH
EDLEAFKERA KTFWAPRNRE WAKEVADQRK GRLANQEEVG EGAKDSHSCE KVVSDDKAER
TTGIEEGVSS WTLTRTNLID QLDKVGGQDS EGEAIEPSAK ERQEEEKVIA DLATALVEDP
KELYIPGKVT HVYFYKGIFE AVHVDRKCGE LSHIPVQQNM LSDHLGRNYL SALRIVRDAR
RAKPSLPEWV PFSTKTRCMC CDSPFTWNST SSSEAQQNRD QHNCRRCGAL VCEGCSEKFK
SIPEFGINVP VRVCDRCYYE V
//
