ID R9PE41_PSEHS Unreviewed; 452 AA.
AC R9PE41;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN ORFNames=PHSY_007124 {ECO:0000313|EMBL:GAC99522.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC99522.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|RuleBase:RU363124}.
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DR EMBL; DF238831; GAC99522.1; -; Genomic_DNA.
DR RefSeq; XP_012193109.1; XM_012337719.1.
DR AlphaFoldDB; R9PE41; -.
DR STRING; 1305764.R9PE41; -.
DR GeneID; 24112388; -.
DR eggNOG; KOG1439; Eukaryota.
DR HOGENOM; CLU_021695_0_1_1; -.
DR OrthoDB; 8704at2759; -.
DR Proteomes; UP000014071; 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; 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:UP000014071}.
SQ SEQUENCE 452 AA; 50722 MW; C1FE154D92964CA4 CRC64;
MDEKYDAVIL GTGVTECVLS ALLSVEGKKV LHIDRGQVYG GEMASLNLTQ LYEKFRPGAE
PPKDWGRDRD WAVDLIPKLI MANGELTQML VHTDVTRYLE FKQIAASYVY RDGRIAKVPA
TEMEAVRSSL MGLFEKRRAK KFFEFIQNWR DSDPATHQTL DLDSDPMVKV FNYFGLEPGT
KDFIGHSMAL HLDDSYLQRP ARETYDRIML YTSSMARYGK SPYIYPLYGL GELPQAFARL
SAIYGGTYML DKSVDEIVVD EETGKFVGVR SGEETVKADM VIGDPSYFRS GVAGKDKVRE
TGKVVRAICI LKHPIPNTDN SDSVQLIIPQ NQVGRKHDIY ISGVSSAQNV AARDFYVAQV
STIVETDKPE LELRPGLDLL GPILDKFVAI SPIEEPIEGG KEDNIFITRS YDATSHFETV
VEDVHDVWRR LTNGEKLVLK KRDDGEGAQV QA
//
