ID   A0A194RDE3_PAPMA        Unreviewed;       616 AA.
AC   A0A194RDE3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Rab proteins geranylgeranyltransferase component A {ECO:0000256|PIRNR:PIRNR016550};
GN   ORFNames=RR48_09327 {ECO:0000313|EMBL:KPJ15300.1};
OS   Papilio machaon (Old World swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ15300.1, ECO:0000313|Proteomes:UP000053240};
RN   [1] {ECO:0000313|EMBL:KPJ15300.1, ECO:0000313|Proteomes:UP000053240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ15300.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPJ15300.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
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; KQ460397; KPJ15300.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194RDE3; -.
DR   STRING; 76193.A0A194RDE3; -.
DR   InParanoid; A0A194RDE3; -.
DR   Proteomes; UP000053240; 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; 3.
DR   Gene3D; 3.30.519.10; Guanine Nucleotide Dissociation Inhibitor, domain 2; 2.
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; 3.
DR   PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 3.
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; 2.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR016550};
KW   GTPase activation {ECO:0000256|PIRNR:PIRNR016550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW   Transferase {ECO:0000313|EMBL:KPJ15300.1}.
FT   REGION          83..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  68761 MW;  45B037DD250A5542 CRC64;
     MDDDLPTDFQ VIVVGTGMVE SIVAAACSRI HKNVLHLDSS DHYGGLWASY NFDGLQKFIK
     EVNSDPEKQV QVYNLREQWY IEKESPPEEE KGEGEAKEDG KTEPPKKIWS QASFAAEYRK
     FNIDMTPKLL FSRGPLVELL ISSNIARYAE FRCVTRVLTW LDDHLVPVPC SRADVFATEA
     VGIVEKRMLM KMLTSIVAYN EEEMNNEFKD WNDKTFKEYL THKGLTPNLI HYVLFAIAGG
     TDAMPCLEGV RECKKFLMSL GRYGNTPFLW PMYGSGELPQ CFCSYHKNSG FNSGRDWNDK
     TFKEYLTHKG LTPNLIHYVL FAIAGGTDAM PCLEGVRECK KFLMSLGRYG NTPFLWPMYG
     SGELPQCFCR LCAVFGGVYC LNRPIDSVET KTVEEGKTKV VIESKSKTLN CEHLVIGINE
     CPKDLVSPEP AETCDISKAV FITNGTIMKS EKEPLTLLRF PPLVEGGGAV TVLEVGPATG
     SCPKGLFVVY FITKKVTDAE TDLRPYADKI FDLSGGDQTE ETDKPKCLWS LFYNVKDTSG
     AASSAAAGVH VCSGPDAGLD FDRAVEQAEQ IFKKICPGEE FLPRAPDPEE IVFEDDVTHG
     PEFQREDEDA EGDAKE
//