ID A8PVF5_MALGO Unreviewed; 377 AA.
AC A8PVF5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN ORFNames=MGL_0848 {ECO:0000313|EMBL:EDP44366.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP44366.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP44366.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|RuleBase:RU363124}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP44366.1}.
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DR EMBL; AAYY01000003; EDP44366.1; -; Genomic_DNA.
DR RefSeq; XP_001731580.1; XM_001731528.1.
DR AlphaFoldDB; A8PVF5; -.
DR STRING; 425265.A8PVF5; -.
DR GeneID; 5855886; -.
DR KEGG; mgl:MGL_0848; -.
DR VEuPathDB; FungiDB:MGL_0848; -.
DR InParanoid; A8PVF5; -.
DR OMA; FETKAKM; -.
DR OrthoDB; 8704at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR Gene3D; 3.30.519.10; Guanine Nucleotide Dissociation Inhibitor, domain 2; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR000806; RabGDI.
DR PANTHER; PTHR11787:SF8; RAB GDP DISSOCIATION INHIBITOR; 1.
DR PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR Pfam; PF00996; GDI; 1.
DR PRINTS; PR00892; RABGDI.
DR PRINTS; PR00891; RABGDIREP.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008837}.
SQ SEQUENCE 377 AA; 42907 MW; 09D2F5735DA05C87 CRC64;
MVPKFMMANG EIVNMLVHTD VTRYLEFKQI SASYVYRDKR IAKVPSTEIE AVRSPLMGLF
EKRRAKRFFE FLQKWRDEDP STHQGIDLDE WPMEKVFAHF GLEPGTRDFI GHAMALHLED
SYMKRPARET YERILLYMSS MARYGKSPYI YPLYGLGELP QGFARLSAIH GGTYMLDKPV
DEIVVDNKGH FVGVRSGDET VKANLVVGDP SYFRQVGGKS LVRETVKVVR AICILKHPIP
NTDNSDSVQL IIPQNQVGRK NDIYIAEVSS AHNICAKGIY VAQVSTIVET DKPELELRPG
LDLLGEILDK FVTVASLEEP LDSGRDSNIY ITRSYDPTSH FETVVEDIHD VWRRMTGHPL
VLKKRQEQEE DGAQVQS
//
