ID   A0A075A334_9TREM        Unreviewed;       323 AA.
AC   A0A075A334;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN   ORFNames=T265_00440 {ECO:0000313|EMBL:KER33761.1};
OS   Opisthorchis viverrini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX   NCBI_TaxID=6198 {ECO:0000313|EMBL:KER33761.1, ECO:0000313|Proteomes:UP000054324};
RN   [1] {ECO:0000313|EMBL:KER33761.1, ECO:0000313|Proteomes:UP000054324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA   Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA   Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA   Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT   "Opisthorchis viverrini - life in the bile duct.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates the GDP/GTP exchange reaction of most RAB proteins
CC       by inhibiting the dissociation of GDP from them, and the subsequent
CC       binding of GTP. {ECO:0000256|RuleBase:RU363124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU363124}.
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC       {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|RuleBase:RU363124}.
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DR   EMBL; KL596622; KER33761.1; -; Genomic_DNA.
DR   RefSeq; XP_009162477.1; XM_009164213.1.
DR   AlphaFoldDB; A0A075A334; -.
DR   STRING; 6198.A0A075A334; -.
DR   GeneID; 20314628; -.
DR   KEGG; ovi:T265_00440; -.
DR   CTD; 20314628; -.
DR   OrthoDB; 8704at2759; -.
DR   Proteomes; UP000054324; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
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; 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   Cytoplasm {ECO:0000256|RuleBase:RU363124};
KW   GTPase activation {ECO:0000256|RuleBase:RU363124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054324}.
SQ   SEQUENCE   323 AA;  36527 MW;  20083790AD7A5F1F CRC64;
     MSLFEKRRFR KFLVWVMNVD ASDPSTWSAV YSEPKDLRKD CIIHAFRAFE LEDDTQNFIG
     HAICLYPDDC YKDTVPASEV TDRIQLYSKS MLRYGKSPYV YPLYGLGELS QAFARLSAVH
     GGTYMLNRPV DEIVFENGKV VGVKSQGEMA QCKAVICDPT YAPDRVKKVG QVVRCICILN
     HPIPGLLDVS SAQIIIPQSV TKRKHDIYIS CLSRQHMVCP DGFFIVLVAT TVETDKPHDE
     LKAGLDLLGE IEEKFVSVDD LYEPVDDGHD SQLFISSSYD ASTHFESTCA DVLDLYHRII
     GEPFDFSKVD ELRAKWNEAQ SDD
//