ID A0A183PRL3_9TREM Unreviewed; 446 AA.
AC A0A183PRL3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN ORFNames=SMTD_LOCUS16999 {ECO:0000313|EMBL:VDP72908.1};
OS Schistosoma mattheei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=31246 {ECO:0000313|WBParaSite:SMTD_0001699801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMTD_0001699801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP72908.1, ECO:0000313|Proteomes:UP000269396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Denwood {ECO:0000313|EMBL:VDP72908.1}, and Denwood, Zambia
RC {ECO:0000313|Proteomes:UP000269396};
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; UZAL01038034; VDP72908.1; -; Genomic_DNA.
DR STRING; 31246.A0A183PRL3; -.
DR WBParaSite; SMTD_0001699801-mRNA-1; SMTD_0001699801-mRNA-1; SMTD_0001699801.
DR WBParaSite; SMTH1_59070.1; SMTH1_59070.1; SMTH1_59070.
DR Proteomes; UP000050791; Unassembled WGS sequence.
DR Proteomes; UP000269396; 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:UP000269396}.
SQ SEQUENCE 446 AA; 50635 MW; 87BF1A8058CDC8AD CRC64;
MDDEYDVVVL GTGLKECILS SLMSMEGKKV LHIDKNSYYG GDITSVNIDS LFQYFDVETD
ISKYHRAKDW NVDLVSKFLM ANGKLVQILV HTGVTRYLEF RSVEGSYVYH SGCVYKVPCN
ESEALSTKLM DLFEKRRFRK LLVWSMNVDV DNPSTWNYVY PPPMDIKKDT ISHAFSSFNI
NKETQNFIGH AICLFQDDSY KENVPAIEVI SRMQLYSQSV CRFGKSPYLY PLYGLGELPQ
AFARLCAVYG GTYMLNKPID ELVMEKGRVV GVKSDNKIAK CGMVICDPSY VPTMVRKVDQ
VVRAICILTH PIAEVQNSLS TQIIIPQSEV NRKHDIYISC VSHQHNACPE NFFVAHVATI
VETSSPEKEL EPGLALLGTI EQVFYSVQDL FVPTDDGRES RVFISSSYDA STHFESTCAD
VLDLYERIVG KPFELSKLKR YEEVNE
//
