ID A0A067QKS8_ZOONE Unreviewed; 645 AA.
AC A0A067QKS8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Rab proteins geranylgeranyltransferase component A {ECO:0000256|PIRNR:PIRNR016550};
GN ORFNames=L798_00901 {ECO:0000313|EMBL:KDR09526.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR09526.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR09526.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR09526.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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; KK853238; KDR09526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067QKS8; -.
DR STRING; 136037.A0A067QKS8; -.
DR EnsemblMetazoa; KDR09526; KDR09526; L798_00901.
DR eggNOG; KOG4405; Eukaryota.
DR InParanoid; A0A067QKS8; -.
DR OMA; LDQNDYY; -.
DR Proteomes; UP000027135; 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; 2.
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; PR00893; RABESCORT.
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:UP000027135};
KW Transferase {ECO:0000313|EMBL:KDR09526.1}.
FT REGION 489..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 71260 MW; 67467AD88AB413DB CRC64;
MEDDLPSEYD VIVVGTGMTE SIVAAAASRI GKRVLHLDSN EYYGGLWASF NFEGIQKWIE
DCHHPANPQE ENVMSAVAND GEMLIKAGNQ FSTISNIEEK WYIVEELADY QEGLLFSRNT
QTDGGEIKGD VDNTKKEEDY ETEKHEEEES EAGCGKDIVP HAPTQQWSQA KLKKEYRKFN
LDLAPKLLFA RGSLVELLIS SNIARYAEFR SVTRVLTWLD GRLESVPCSR ADVFATRHVT
VVEKRMLMKL LTACMEYENS SKEFEGFEDK PFLEYLKSKK LTPNLLHYVL YAIAMATGTT
PCMEGVARTQ KFLNSLGRYG NTPFLWPMYG SGEIPQCFCR LCAVFGGLYH LKRAAEAVIV
SDGEDSNLTC HAIVSGGRRL NTSHLVLAVG YAPPQFLQTA PNGGVSRGIF ITDRSILPAD
KESLTLLQFP SADGCGEPVT VIEVGPSTNA CPPGMYVVHM TCKQKITARE DLQTVVQKLL
HTEFSDGAMI RTNTDTQSTQ TASPNKTHSE DSEGQEGNET EDKGKSDPGS DLKPQVLWSL
FFNCPETSDC DLTANVPTNV FLCSGPDVDL DFEHAVKQAK EIFSKMYQDS EFLPRAPDPE
EIVLEGEEST PGPVFEGDSS EAKADENKSE LGDEEEKGAD DGGAE
//
