ID   PGTB2_CANAX             Reviewed;         341 AA.
AC   O93830;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   22-FEB-2023, entry version 85.
DE   RecName: Full=Geranylgeranyl transferase type-2 subunit beta;
DE            EC=2.5.1.60;
DE   AltName: Full=Geranylgeranyl transferase type II subunit beta;
DE            Short=GGTase-II-beta;
DE   AltName: Full=Type II protein geranyl-geranyltransferase subunit beta;
DE            Short=PGGT;
DE   AltName: Full=YPT1/SEC4 proteins geranylgeranyltransferase subunit beta;
GN   Name=BET2;
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 BET2 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC       family. {ECO:0000305}.
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DR   EMBL; AB021171; BAA35193.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93830; -.
DR   SMR; O93830; -.
DR   VEuPathDB; FungiDB:CAWG_02253; -.
DR   VEuPathDB; FungiDB:CR_09890C_A; -.
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:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR   CDD; cd02894; GGTase-II; 1.
DR   Gene3D; 1.50.10.20; -; 1.
DR   InterPro; IPR001330; PFTB_repeat.
DR   InterPro; IPR045089; PGGT1B-like.
DR   InterPro; IPR026873; Ptb1.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11774; GERANYLGERANYL TRANSFERASE TYPE BETA SUBUNIT; 1.
DR   PANTHER; PTHR11774:SF11; GERANYLGERANYL TRANSFERASE TYPE-2 SUBUNIT BETA; 1.
DR   Pfam; PF00432; Prenyltrans; 5.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Prenyltransferase; Repeat; Transferase; Zinc.
FT   CHAIN           1..341
FT                   /note="Geranylgeranyl transferase type-2 subunit beta"
FT                   /id="PRO_0000119776"
FT   REPEAT          15..55
FT                   /note="PFTB 1"
FT   REPEAT          62..104
FT                   /note="PFTB 2"
FT   REPEAT          122..163
FT                   /note="PFTB 3"
FT   REPEAT          170..211
FT                   /note="PFTB 4"
FT   REPEAT          223..264
FT                   /note="PFTB 5"
FT   REPEAT          271..313
FT                   /note="PFTB 6"
FT   BINDING         196..198
FT                   /ligand="geranylgeranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57533"
FT                   /evidence="ECO:0000250"
FT   BINDING         243..255
FT                   /ligand="geranylgeranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57533"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   341 AA;  38460 MW;  24A89E11FF911488 CRC64;
     MSNLPPDEKV ILFDKSKHVQ YIVEQESHRS FEYWLSEHLR MNGLYWGVTA LITMNELSAL
     AQQDVIDYIM LCWDDKTGAF GSFPKHDGHI LSTLSALQVL KIYDQELTVL NDNNESSNGN
     KRERLIKFIT GLQLPDGSFQ GDKYGEVDTR FVYTAVSSLS LLNALTDSIA DTASAFIMQC
     FNFDGGFGLI PGSESHAAQV FTCVGALAIM NKLDLLDVEN KKVKLIDWLT ERQVLPSGGF
     NGRPEKLPDV CYSWWVLSSL SILKRKNWVD LKILENFILT CQDLENGGFS DRPGNQTDVY
     HTCFAIAGLS LIDYKKYGFK EIDPVYCMPV EVTSKFVRRS A
//