ID   PGTA_CANAX              Reviewed;         371 AA.
AC   O93829;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Geranylgeranyl transferase type-2 subunit alpha;
DE            EC=2.5.1.60;
DE   AltName: Full=GGTase-II-alpha;
DE   AltName: Full=Geranylgeranyl transferase type II subunit alpha;
DE   AltName: Full=PGGT;
DE   AltName: Full=Type II protein geranyl-geranyltransferase subunit alpha;
DE   AltName: Full=YPT1/SEC4 proteins geranylgeranyltransferase subunit alpha;
GN   Name=BET4;
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 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RA   Ishii N., Aoki Y., Arisawa M.;
RT   "Molecular cloning of BET4 gene from Candida albicans.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC       geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or
CC       -XCXC, where both cysteines may become modified. Acts on YPT1 and SEC4
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC         diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC         ChEBI:CHEBI:86021; EC=2.5.1.60;
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB021170; BAA35192.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93829; -.
DR   SMR; O93829; -.
DR   VEuPathDB; FungiDB:C1_04070C_A; -.
DR   VEuPathDB; FungiDB:CAWG_00986; -.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0004663; F:Rab geranylgeranyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR   GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR   InterPro; IPR002088; Prenyl_trans_a.
DR   InterPro; IPR032955; RabGGTase_alpha.
DR   PANTHER; PTHR11129:SF2; PTHR11129:SF2; 1.
DR   Pfam; PF01239; PPTA; 4.
DR   PROSITE; PS51147; PFTA; 5.
PE   3: Inferred from homology;
KW   Prenyltransferase; Repeat; Transferase.
FT   CHAIN           1..371
FT                   /note="Geranylgeranyl transferase type-2 subunit alpha"
FT                   /id="PRO_0000119755"
FT   REPEAT          45..79
FT                   /note="PFTA 1"
FT   REPEAT          92..126
FT                   /note="PFTA 2"
FT   REPEAT          131..165
FT                   /note="PFTA 3"
FT   REPEAT          177..211
FT                   /note="PFTA 4"
FT   REPEAT          242..276
FT                   /note="PFTA 5"
SQ   SEQUENCE   371 AA;  44462 MW;  69DC54570B3E9FF0 CRC64;
     MQHGIKRVKL SEEAKRLKLE KDQIKIKNYR QLTDEIFELR ANENYSDEAL IKTNELLIIN
     PEFYTIWNYR REILINNYSS SNDKDDQIYE DILNQDLNFV LVQLKKFPKC YWIWNHRRWL
     LFELVKLGKV NWKYEFGVVS KLLDLDQRNF HGWHYRRFVV KNMELECKND TTLILKINLD
     EFNYTTLKIQ KDFSNFSAWH NRTKLIPKIY NLIQQQQQQQ QKDGKIFGDL PGIELFQNPI
     LLLKNDLEMI KTGVYMSPED TSVWLYLYWL LTDDLFTNAF KSHQQDYMNI LHEQLQLINE
     VNEMEKEDTG QDNVGCLKSM IFINALIQNE NNKPVLTEQV KSCLKQLAKI DPLRKNKYLD
     QLAGNAPIFH H