PGTB2_CANAX
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 03-AUG-2022, entry version 83.
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}.
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; 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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IEA:EnsemblFungi.
DR CDD; cd02894; GGTase-II; 1.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR026873; Ptb1.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 1.
DR Pfam; PF00432; Prenyltrans; 5.
DR SUPFAM; SSF48239; SSF48239; 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