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Database: UniProt
Entry: A0A2N1J7J9_9BASI
LinkDB: A0A2N1J7J9_9BASI
Original site: A0A2N1J7J9_9BASI 
ID   A0A2N1J7J9_9BASI        Unreviewed;       962 AA.
AC   A0A2N1J7J9;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=OBG-type G domain-containing protein {ECO:0000259|PROSITE:PS51710};
GN   ORFNames=MVES_003485 {ECO:0000313|EMBL:PKI82533.1};
OS   Malassezia vespertilionis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=2020962 {ECO:0000313|EMBL:PKI82533.1, ECO:0000313|Proteomes:UP000232875};
RN   [1] {ECO:0000313|EMBL:PKI82533.1, ECO:0000313|Proteomes:UP000232875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NWHC:44797-103 {ECO:0000313|EMBL:PKI82533.1,
RC   ECO:0000313|Proteomes:UP000232875};
RA   Lorch J.M., Palmer J.M., Vanderwolf K.J., Schmidt K.Z., Verant M.L.,
RA   Weller T.J., Blehert D.S.;
RT   "A novel species of cold-tolerant Malassezia isolated from bats.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol +
CC         H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868;
CC         Evidence={ECO:0000256|ARBA:ARBA00043665};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monoacylglycerol + H2O = a fatty acid + glycerol + H(+);
CC         Xref=Rhea:RHEA:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868;
CC         Evidence={ECO:0000256|ARBA:ARBA00043831};
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DR   EMBL; KZ454994; PKI82533.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N1J7J9; -.
DR   STRING; 2020962.A0A2N1J7J9; -.
DR   OrthoDB; 589269at2759; -.
DR   Proteomes; UP000232875; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd01896; DRG; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 6.10.140.1070; -; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR045001; DRG.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR031662; GTP-binding_2.
DR   InterPro; IPR006074; GTP1-OBG_CS.
DR   InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43127; DEVELOPMENTALLY-REGULATED GTP-BINDING PROTEIN 2; 1.
DR   PANTHER; PTHR43127:SF2; DEVELOPMENTALLY-REGULATED GTP-BINDING PROTEIN 2; 1.
DR   Pfam; PF02450; LCAT; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF16897; MMR_HSR1_Xtn; 1.
DR   Pfam; PF02824; TGS; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51710; G_OBG; 1.
DR   PROSITE; PS00905; GTP1_OBG; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232875}.
FT   DOMAIN          63..290
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51710"
SQ   SEQUENCE   962 AA;  108033 MW;  257156EBB017D0F1 CRC64;
     MGVVEKMKEI EQEMARTQKN KATEYHIGLL RAKLAKLRMQ LLEPDKKNSK PGEGFDVMKS
     GNARVVLIGF PSVGKSTLLS TITETESATA AYEYTTLTAI PGVLEYEGAR IQLLDLPGII
     EGAAQGRGRG RQVVSVAKTA DLVLMMLDAT KPAQQRQLLE KELEDVGVRL NQQKPDVILK
     RKNGGGIVVT KAMGLTLTKI DEKMIRSILQ GYKIHNCDIM MRQDITVDQF IDVVLGNRKY
     VPCLYVYNKI DRISMEEMDK LAHQPQSVVI SAELRLNLDY LIERIWEDLD LHRIYTKKRG
     EHPDLSDPIV VRRGATIEHV CHGVHRALVD KFAYALVYGK SSKFPSLWKI VAGVLTLSVA
     VVAWLVSRDP EWQTDALLKA LDYKLSDLGL DTLKYNFVLP KDIRLQLGNI LSSSHNWFET
     LDFKIGRELA EAGAKPEHPV ILLPGIISTG LESWTSKGHS AKYFRERLWA GNSMIKMVLF
     DKDRWVRHLK LDPKTGLDPS GVHVRAAKGL DAASYFAAGY WIWSKIIQNL AAVGYDINKI
     YLASYDWRLS MYNLEIRDHF YSELKSRFEL NLAVTGKKTV FVSHSMGATV ALYFFKWIEE
     EVGSEWIEKH VESLVSISGT WLGVPKAVAA LFTGEMRDTV EVPRIIEYLL EHFFSSHERA
     NLFRSWAGSS SLLIKGGDLV WGNEHGAPDD HANASVTQGN LLEYAARGNV SEDLDVTEAS
     QSVQSRKFTT DATLPLILQH TPIEYQNMIA TNYSFGFEKD AKQIQRNNKD PRKWTNPLEV
     QLPNAPSMKI YCIYGWGKST ERSYWMRAVD AKYSVDTDGM NFTDPLDNAN SANQTVYFPQ
     MEESRIDSRI NFENGEPVVN SGCRMGEGDG TVALLSLGAM CVEGWKRKRY NPAGIEIITH
     EVKHEPDVLD IRGGPSTADH VDILGNAAVN EMILNVATGR GHLVKEHIGS PIREFADNIA
     WD
//
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