ID Q6FPT6_CANGA Unreviewed; 317 AA.
AC Q6FPT6;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 2.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Geranylgeranyl transferase type-2 subunit alpha {ECO:0000256|RuleBase:RU367120};
DE EC=2.5.1.60 {ECO:0000256|RuleBase:RU367120};
DE AltName: Full=Geranylgeranyl transferase type II subunit alpha {ECO:0000256|RuleBase:RU367120};
GN OrderedLocusNames=CAGL0J01067g {ECO:0000313|CGD:CAL0132854,
GN ECO:0000313|EMBL:CAG60705.2};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG60705.2, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG60705.2, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC geranyl-geranyl pyrophosphate to cysteines occuring in specific C-
CC terminal amino acid sequences. {ECO:0000256|RuleBase:RU367120}.
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 Evidence={ECO:0000256|ARBA:ARBA00001577,
CC ECO:0000256|RuleBase:RU367120};
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000256|ARBA:ARBA00006734, ECO:0000256|RuleBase:RU367120}.
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DR EMBL; CR380956; CAG60705.2; -; Genomic_DNA.
DR RefSeq; XP_447758.2; XM_447758.2.
DR AlphaFoldDB; Q6FPT6; -.
DR STRING; 284593.Q6FPT6; -.
DR EnsemblFungi; CAGL0J01067g-T; CAGL0J01067g-T-p1; CAGL0J01067g.
DR GeneID; 2889850; -.
DR KEGG; cgr:CAGL0J01067g; -.
DR CGD; CAL0132854; CAGL0J01067g.
DR VEuPathDB; FungiDB:CAGL0J01067g; -.
DR eggNOG; KOG0529; Eukaryota.
DR HOGENOM; CLU_031996_0_0_1; -.
DR InParanoid; Q6FPT6; -.
DR OMA; TNAMFTD; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0005777; C:peroxisome; IEA:EnsemblFungi.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IEA:EnsemblFungi.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR GO; GO:0097354; P:prenylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006612; P:protein targeting to membrane; IEA:EnsemblFungi.
DR Gene3D; 1.25.40.120; Protein prenylyltransferase; 1.
DR InterPro; IPR002088; Prenyl_trans_a.
DR PANTHER; PTHR11129:SF2; GERANYLGERANYL TRANSFERASE TYPE-2 SUBUNIT ALPHA; 1.
DR PANTHER; PTHR11129; PROTEIN FARNESYLTRANSFERASE ALPHA SUBUNIT/RAB GERANYLGERANYL TRANSFERASE ALPHA SUBUNIT; 1.
DR Pfam; PF01239; PPTA; 5.
DR SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR PROSITE; PS51147; PFTA; 5.
PE 3: Inferred from homology;
KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602,
KW ECO:0000256|RuleBase:RU367120};
KW Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU367120}.
SQ SEQUENCE 317 AA; 38376 MW; 0F25361DF35B3812 CRC64;
MELLKQKRVQ DQLKIEKYRQ LTDTVLGLKD KREFTIESLK LTTNLLELNP EFNAVWNYRR
DIIVDLGEKL EPKFWEDELM FVMAQLKRFP KVYWIWNHRL WTLQNYPGAS VKIWGRELVI
VNKLLDADAR NYHGWHYRRI VVSHMQKMTG NDMNKEELEY ATTMIKSNIS NFSAWHQRVQ
LIQKMLEKNE IEDKTLFIEK EIDFVTNAMF TDAEDQAVWF YIKWFIRSDL VLKVLTKERY
LEMLKTFWEN ITMINEDELE FSGKENTWCL KLLLVIQQIQ KSEGIDIEDH TKIYLEKLLT
VDPLRKNRYK HLLKLEC
//