ID   A0A183DTP6_9BILA        Unreviewed;       396 AA.
AC   A0A183DTP6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN   ORFNames=GPUH_LOCUS12087 {ECO:0000313|EMBL:VDN19825.1};
OS   Gongylonema pulchrum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX   NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0001210101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:GPUH_0001210101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN19825.1, ECO:0000313|Proteomes:UP000271098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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; UYRT01079028; VDN19825.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183DTP6; -.
DR   WBParaSite; GPUH_0001210101-mRNA-1; GPUH_0001210101-mRNA-1; GPUH_0001210101.
DR   Proteomes; UP000050760; Unplaced.
DR   Proteomes; UP000271098; 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; 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; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU363124};
KW   GTPase activation {ECO:0000256|RuleBase:RU363124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271098}.
SQ   SEQUENCE   396 AA;  44326 MW;  59BE37BF35078D3D CRC64;
     MDEEYDAVVL GTGLKECILS GMLSVSGKKI LHIDRNDYYG GESASITPLE QLYEKFLGRN
     SKPSSDMGRG RDWNVDLIPK FLMANGSLVK LLIHTGVTRY LEFKSIEGSY VYKGGKVFKV
     PADEMEALAT NLMGMFEKRR FKKFLVWVQN FDIKNPATYD GLDPDVHTMQ QVYEKFGLDE
     NTADFTGHAL ALYRDDNYKN ELFVPTAERI RLYSDSLARY GKSPYLYPLY GLGELPQGFA
     RLSAIYGGTY MLDKPVDSIV YENGRVVGVK SGNDIAKCKQ ANLKIISYKA SKWVLQVYCD
     PSYVPDKVRK VGQVVRAICL LNHTIPNTND AQSCQIIIPQ KQVGRHSDIY ISLVSNVNMV
     APKGWYIAMV STTVETASPE AEIIPGLNLL GPISEK
//