ID   A0A0V1CZI7_TRIBR        Unreviewed;       443 AA.
AC   A0A0V1CZI7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN   Name=Gdi1 {ECO:0000313|EMBL:KRY54650.1};
GN   ORFNames=T03_12458 {ECO:0000313|EMBL:KRY54650.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY54650.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY54650.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY54650.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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}.
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:KRY54650.1}.
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DR   EMBL; JYDI01000066; KRY54650.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1CZI7; -.
DR   STRING; 45882.A0A0V1CZI7; -.
DR   Proteomes; UP000054653; 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; 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:UP000054653}.
SQ   SEQUENCE   443 AA;  49843 MW;  38595462BFBDF916 CRC64;
     MDEIYDCVIL GTGLTECIVS GMLSVSGKKI LHMDRNNYYG GESASITPLE DLFDKFMPGT
     KPLESMGRGR DWNVDLIPKF LMANGELVKL LLSTGVTRYL EFKSIEGSFV YKGGKVYKVP
     ADEAEALTTS LMGIFEKRRF KKFLVWAQNF DFDNKATWEG LDPYTNTMND VYRKFDLDEN
     TADFTGHALA LYINDKYKNE PFGETVKRVK LYSASLERYG KSPYLYPLYG LGELPQGFAR
     LSAIYGGTYM LDTPVDEIVM ENGCVIGVRC GNQTVRCRQV YCDPSYAPNL VRHVGKVIRA
     ICLLNHPIPN TNDSKSCQII IPQRQVGRQH DIYISMVSYT NMVAAKDWYV AIVSTTVETN
     SPESELLPGL QLLGSITQKF VSISDLMEPI NDGRTSQVFI SKSYDATSHF KTTCDDVIDI
     FQRGTGEPFD FSKISHLTLE DTQ
//