ID   RAEP_CANAX              Reviewed;         640 AA.
AC   O93831;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Rab proteins geranylgeranyltransferase component A;
DE   AltName: Full=Rab escort protein;
DE            Short=REP;
GN   Name=MRS6;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060 / 2024;
RA   Ishii N., Aoki Y., Arisawa M.;
RT   "Molecular cloning of Rab geranylgeranyl transferase escort protein (REP)
RT   homologue from Candida albicans.";
RL   Submitted (DEC-1998) 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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
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DR   EMBL; AB021317; BAA36167.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93831; -.
DR   SMR; O93831; -.
DR   VEuPathDB; FungiDB:C3_07170C_A; -.
DR   VEuPathDB; FungiDB:CAWG_03025; -.
DR   GO; GO:0016020; C:membrane; IEA:EnsemblFungi.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0031267; F:small GTPase binding; IEA:EnsemblFungi.
DR   GO; GO:0090630; P:activation of GTPase activity; IEA:EnsemblFungi.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR   GO; GO:0018344; P:protein geranylgeranylation; IEA:EnsemblFungi.
DR   GO; GO:0006612; P:protein targeting to membrane; IEA:EnsemblFungi.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   InterPro; IPR017230; Mrs6.
DR   PANTHER; PTHR11787; PTHR11787; 1.
DR   Pfam; PF00996; GDI; 1.
DR   PIRSF; PIRSF037514; Rab_ger_ger_transf_A_fun; 1.
DR   PRINTS; PR00891; RABGDIREP.
DR   PRINTS; PR00894; YEASTMRS6P.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   GTPase activation.
FT   CHAIN           1..640
FT                   /note="Rab proteins geranylgeranyltransferase component A"
FT                   /id="PRO_0000056692"
FT   REGION          414..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..620
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   640 AA;  72291 MW;  772BB6C1FF005388 CRC64;
     MDNCDVLIIG TGLQESILAA ALSWQGTQVL HIDSNTYYGD SCSTLTIEQL KKWCGDVNSG
     KIHQFQDAQI YIPGGKQSNQ YTSKDYGIDL TPKIMFCQSD LLSLLIKSRV YRYLEFQSLS
     NFHVFENDDF QQKVNATTKQ DIFTDKSLSL MTKRYLMKFL KFLLLDPDYK QRVKPYADTP
     IQVFLQQEFK LEEPQINELV YSIGLSYKEQ TSTKQALIRM KRFLSSFDVY GKFPCMVSKF
     GGPGELSQGF CRSAAVAGTT YKLNTNLTDF DPISKIAHFN DGSHIKINEK IIISPTQLPK
     FLQSSYNKVV ENLQPYYVTR LVTVVRRDCK EWMSGNESSA IVVFPPHSLP TDNQHSVQVI
     IQNGNSGVCP DGQAIWFSST VEQDLSRAKV DLESAFEKME TSLLRESSEE IVNDILGDNN
     NNNNNNNNNN NNNNNNNNND FVMNAQGTTT PVLVNSFKLG SSLINFVPKD KLEIVCKLGY
     VEKTFINPDL SNIFKPTKTN NIVYKDVEDA NNEIIFTNMP SSELSYDGII TDVKSIYQRI
     TGTTDDFFDV DFEDEEDEYD RNNQPVVQPK RSSVVGGIVG GGSITSLTAL REQHNENNHS
     DNAIDSDEDE DEDINDMNDN EEEDDHGRGP EPFGADEMEL