ID   A0A0V0TMQ7_9BILA        Unreviewed;       547 AA.
AC   A0A0V0TMQ7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Rab proteins geranylgeranyltransferase component A {ECO:0000256|PIRNR:PIRNR016550};
GN   Name=Rep {ECO:0000313|EMBL:KRX40161.1};
GN   ORFNames=T05_12230 {ECO:0000313|EMBL:KRX40161.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX40161.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX40161.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX40161.1};
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: Substrate-binding subunit (component A) of the Rab
CC       geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab
CC       proteins and presents the substrate peptide to the catalytic component
CC       B. The component A is thought to be regenerated by transferring its
CC       prenylated Rab back to the donor membrane.
CC       {ECO:0000256|PIRNR:PIRNR016550}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR016550}.
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC       {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|PIRNR:PIRNR016550}.
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:KRX40161.1}.
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DR   EMBL; JYDJ01000208; KRX40161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0TMQ7; -.
DR   STRING; 144512.A0A0V0TMQ7; -.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:UniProtKB-UniRule.
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; IPR001738; Rab_escort.
DR   PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR   PANTHER; PTHR11787:SF4; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A; 1.
DR   Pfam; PF00996; GDI; 2.
DR   PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 1.
DR   PRINTS; PR00891; RABGDIREP.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR016550};
KW   GTPase activation {ECO:0000256|PIRNR:PIRNR016550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW   Transferase {ECO:0000313|EMBL:KRX40161.1}.
SQ   SEQUENCE   547 AA;  62465 MW;  DA1E45C169F63EF3 CRC64;
     MQEDELPDRF SVILLGTGFS ESVLSAACST AGFSVLHIDR QVESSDVYGG NLATLDLDHL
     IKWLHNEGIL WNSEEEIQAP DLARFINEDE CLFPIGDRQQ IGKTIFNVKY EWHIPDKEEK
     VVEGVEVKNT DEIAKPIDRD YLKENNHRFS IDTNPRVVYA NGSLVNLLLR SQCAPYLEFK
     CIDRLFTYFQ DELRTVPCSR TEVFASREIE KMDKRLLMQF LSFCFQYEKF PEQWLEFENR
     PALEFMECKK LPPLVQHHLL QALALGTSQT TTKQFLQRLH RFIQGVGRFG TSPYLWTIHG
     SGELPQAFCR CAAVNGAVYC LRRPVRAWIF NKQRKAVVAV VIGNQRISCD FLVTDRSYVP
     EELWPAELED HHVARAILIT DKTLRVSKSQ LKPVENVPIV SMLAFCTEAN ENPILLFDSA
     SGVCASPKGT SVVNIMSPVS CDDSRELFQP TVQRLFSTGS SENSDADNTE KPRLIFSAYF
     TQKVAKADVD LAKRKLFENV IVTSLPSYNV DLDDVVDETE KLFKILWNDM PFFPPKKSDT
     SVEEMEE
//