ID A0A0K0E5A8_STRER Unreviewed; 444 AA.
AC A0A0K0E5A8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000469200.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000469200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
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 AlphaFoldDB; A0A0K0E5A8; -.
DR STRING; 6248.A0A0K0E5A8; -.
DR WBParaSite; SSTP_0000469200.1; SSTP_0000469200.1; SSTP_0000469200.
DR Proteomes; UP000035681; 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:UP000035681}.
SQ SEQUENCE 444 AA; 50101 MW; A0FA58792BE9D6BD CRC64;
MNDEYDAIVL GTGLKECILS GMLSVSGKKV LHIDRNNYYG GESASLSPLN QLFEMFHGKD
AQTPEYMGRG RDWNVDLIPK FLMANGQLVK LLIHTGVTRY LEFKSIEGSY VYKGGKVYKV
PADEVEALAT SLMGMFEKRR FKKFLIWVQG FDINDPNTFD GMDPTKDTMQ KVYEKFGLDE
NTADFTGHAL ALYRDDAYKD ELFVKTVQKI RLYSDSLARY GKSPYLYPLY GLGELPQGFA
RLSAIYGGTY MLDKQVDEVV LENGKIVGVR SGNEIAKCKQ LYCDPSYVLD RCKKNSQVVR
AICILDHPIP DTKDAASCQI IIPQKQVNRG SDIYISCVSN ANQTAPKGWY IAMVSTTVET
GNPELEIQPG LQLLGQIKEK FIRVYDIYEP TDLGHESQIF ISRGYDATTH FETVCNDVLD
IFARGTGEQF DFSKITHLNM EEQD
//