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Database: UniProt
Entry: G8BRR1_TETPH
LinkDB: G8BRR1_TETPH
Original site: G8BRR1_TETPH 
ID   G8BRR1_TETPH            Unreviewed;       448 AA.
AC   G8BRR1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN   Name=TPHA0C02840 {ECO:0000313|EMBL:CCE62437.1};
GN   OrderedLocusNames=TPHA_0C02840 {ECO:0000313|EMBL:CCE62437.1};
OS   Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS   Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE62437.1, ECO:0000313|Proteomes:UP000005666};
RN   [1] {ECO:0000313|EMBL:CCE62437.1, ECO:0000313|Proteomes:UP000005666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC   {ECO:0000313|Proteomes:UP000005666};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC       {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|RuleBase:RU363124}.
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DR   EMBL; HE612858; CCE62437.1; -; Genomic_DNA.
DR   RefSeq; XP_003684871.1; XM_003684823.1.
DR   AlphaFoldDB; G8BRR1; -.
DR   STRING; 1071381.G8BRR1; -.
DR   GeneID; 11533604; -.
DR   KEGG; tpf:TPHA_0C02840; -.
DR   eggNOG; KOG1439; Eukaryota.
DR   HOGENOM; CLU_021695_0_1_1; -.
DR   OMA; FETKAKM; -.
DR   OrthoDB; 8704at2759; -.
DR   Proteomes; UP000005666; Chromosome 3.
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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005666}.
SQ   SEQUENCE   448 AA;  50513 MW;  F23E2846449ABEAA CRC64;
     MSQSDLDTDY DVIILGTGLT ECILSGLLSV DGKKILHIDR QDHYGGEAAS ASLSQLFNKF
     KQKPMSDADR EAKFGKDRDW NVDLIPKFLM ANGELTNILV HTNVTSYLDF KQVSGSYVFK
     NGKIYKVPSN EMEAITSPLM GIFEKRRMKK FLEWISNYND DDNSTHQGLD LDKNTMDEVF
     YKFGLGNATK EFIGHAMALW TNDDYIQEPA RPTFERILLY CKSVAKYGKS PYLYPMYGLG
     ELPQGFARLS AIYGGTYMLD TPIEEIMYTA DDKFKSIKTK LGEFRAPVVI ADPTYFPEKC
     KSTGKRVIRA ICILEHSVPG TGDADSLQII IPQSQVGRSN DIYIAVVSDS HNVCSKGRYI
     AIISTIVETD KPHIELEPAL KLLGPIAEKF MGIAELFEPK EDGFKDNIFL SKSYDASSHF
     ETTTDDVKDI YFRVTGHPLM LKTRELQE
//
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