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Database: UniProt
Entry: G1QR06_NOMLE
LinkDB: G1QR06_NOMLE
Original site: G1QR06_NOMLE 
ID   G1QR06_NOMLE            Unreviewed;       653 AA.
AC   G1QR06;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Rab proteins geranylgeranyltransferase component A {ECO:0000256|PIRNR:PIRNR016550};
GN   Name=CHM {ECO:0000313|Ensembl:ENSNLEP00000003374.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000003374.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000003374.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000003374.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) 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; ADFV01047669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01047670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01047671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01047672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01047673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01047674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01047675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01047676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01047677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01047678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003269065.1; XM_003269017.2.
DR   AlphaFoldDB; G1QR06; -.
DR   Ensembl; ENSNLET00000003540.3; ENSNLEP00000003374.1; ENSNLEG00000002762.3.
DR   GeneID; 100596659; -.
DR   KEGG; nle:100596659; -.
DR   CTD; 1121; -.
DR   eggNOG; KOG4405; Eukaryota.
DR   GeneTree; ENSGT00950000182994; -.
DR   HOGENOM; CLU_021695_4_1_1; -.
DR   OrthoDB; 197300at2759; -.
DR   TreeFam; TF320813; -.
DR   Proteomes; UP000001073; Chromosome X.
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: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:SF12; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A 1; 1.
DR   Pfam; PF00996; GDI; 2.
DR   PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 1.
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:UP000001073}.
FT   REGION          606..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   653 AA;  73429 MW;  95CCA1A3342B4599 CRC64;
     MADTLPSEFD VIVIGTGLPE SIVAAACSRS GRRVLHVDSR SYYGGNWASF SFSGLLSWLK
     EYQENSDIVN DSPVWQDQIL ENEEAIALSR KDKTIQHVEV FCYASQDLHE DVEEAGALQK
     NHALVTSANS TEAADSAFLP TEHEPLSTMS CEMLTEQTPS SGPENALEVN GAEVTGEKEN
     HCDDKTCVPS TSAEDMSENV PIAEDTTEQP KKNRITYSQI IKEGRRFNID LVSKLLYSRG
     LLIDLLIKSN VSRYAEFKNI TRILAFREGQ VEQVPCSRAD VFNSKQLTMV EKRMLMKFLT
     FCMEYEKYPD EYKGYEEITF YEYLKTQKLT PNLQYIVLHS IAMTSETASS TIDGLKATKN
     FLHCLGRYGN TPFLFPLYGQ GELPQCFCRM CAVFGGIYCL RHSVQCLVVD KESRKCKAII
     DQFGQRIISE HFLVEDSYFS ENMYSRVQYR QISRAVLITD RSVLKTDSDQ QISILTVPAE
     EPGTFAVRVI ELCSSTMTCM KGTYLVHLTC TSSKTAREDL EPVVQKLFIP YTEMEIENEQ
     VEKPRILWAL YFNMRDSSDI SRSCYNDLPS NVYVCSGPDC GLGNDNAVKQ AETLFQEICP
     NEDFCPPPPN PEDIVLDGDS LQPEASESSA IPEANSETVK ESTNLGNLEE SSE
//
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