ID B0WTT3_CULQU Unreviewed; 596 AA.
AC B0WTT3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Rab proteins geranylgeranyltransferase component A {ECO:0000256|PIRNR:PIRNR016550};
GN Name=6043097 {ECO:0000313|EnsemblMetazoa:CPIJ010669-PA};
GN ORFNames=CpipJ_CPIJ010669 {ECO:0000313|EMBL:EDS34624.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS34624.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS34624.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ010669-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ010669-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR EMBL; DS232092; EDS34624.1; -; Genomic_DNA.
DR RefSeq; XP_001855828.1; XM_001855782.1.
DR AlphaFoldDB; B0WTT3; -.
DR STRING; 7176.B0WTT3; -.
DR EnsemblMetazoa; CPIJ010669-RA; CPIJ010669-PA; CPIJ010669.
DR KEGG; cqu:CpipJ_CPIJ010669; -.
DR VEuPathDB; VectorBase:CPIJ010669; -.
DR VEuPathDB; VectorBase:CQUJHB009564; -.
DR eggNOG; KOG4405; Eukaryota.
DR HOGENOM; CLU_021695_4_1_1; -.
DR InParanoid; B0WTT3; -.
DR OMA; LMKFLTA; -.
DR OrthoDB; 197300at2759; -.
DR Proteomes; UP000002320; 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; 2.
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:UP000002320};
KW Transferase {ECO:0000313|EMBL:EDS34624.1}.
FT REGION 526..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 65989 MW; 6A3B72A722F1DC3F CRC64;
MDEDLPTEFD LIVVGTGLPE SIVAAAASRI GKTVLHLDSN EYYGGFWSSF NLEALRKYAE
ECRDRTQLGC EKVEEGFLPL GRATFVENVA EEWFPFEEGV EVDGWNREKI LKEFRRFNVD
LAPKLLYSRG SMVELLISSN ICRYAEFRAV DRVATIWNGR IMTVPCSRSD VFTSRDVNVV
EKRLLMKFLQ SCASFETDGS GTDEHRLEDI EGKTFLEYLK SHKLTPNLIH YLLYTIAMGN
DRTSCREGLE GVKKFLLSLG RYGNSPFLFP MYGCGEIPQC FCRLCAVFGG IYCLSKSIEG
ITLKHSEGER SFQSLRCGKQ TIEAKSIVIG QGYDANHKGC GKMARGVFLV NVPLGGASQN
TGGGGVSLMK LPPVEGHEDG ATIIQLAHFS GTCPKEIYLI HITARAISDD PQADLAPYVT
QILSRETPKI APSPPEGEIF ENTQENTDST ILYQLYFTIP TCVSCSHGRP STLPRGLHLA
CGPLLELDYD ESIARAQAIF KDIYPEEEFL PRAPDPEQII IGDEEDQQPE QAQEVPSSEK
ATTGDKVESG RECRESESSS SVPVTPSSVG VPQAEDDAQE AKEDAVEKAE ECVEQK
//
