ID N1P8J7_YEASC Unreviewed; 290 AA.
AC N1P8J7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ORFNames=CENPK1137D_1270 {ECO:0000313|EMBL:EIW09500.1};
OS Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=889517 {ECO:0000313|EMBL:EIW09500.1};
RN [1] {ECO:0000313|EMBL:EIW09500.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CEN.PK113-7D {ECO:0000313|EMBL:EIW09500.1};
RA Nijkamp J.F., van den Broek M.A., Datema E., de Kok S., Bosman L.,
RA Luttink M.A., Daran-Lapujade P., Vongsangnak W., Nielsen J., Heijne W.H.M.,
RA Klaassen P., Platt D., Paddon C.J., Koetter P., van Ham R.C.,
RA Reinders M.J.T., Pronk J.T., de Ridder D., Daran J.-M.;
RT "De novo sequencing, assembly and analysis of the genome of the laboratory
RT strain Saccharomyces cerevisiae CEN.PK113-7D, a model for modern industrial
RT biotechnology.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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; CM001531; EIW09500.1; -; Genomic_DNA.
DR AlphaFoldDB; N1P8J7; -.
DR HOGENOM; CLU_031996_0_1_1; -.
DR Proteomes; UP000013192; Chromosome X.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0097354; P:prenylation; IEA:UniProtKB-UniRule.
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; 4.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU367120}.
SQ SEQUENCE 290 AA; 35046 MW; 89996EC020601052 CRC64;
MRDEKIYSIE ALKKTSELLE KNPEFNAIWN YRRDIIASLA SELEIPFWDK ELVFVMMLLK
DYPKVYWIWN HRLWVLKHYP TSSPKVWQTE LAVVNKLLEQ DARNYHGWHY RRIVVGNIES
ITNKSLDKEE FEYTTIKINN NISNYSAWHQ RVQIISRMFQ KGEVGNQKEY IRTEISYIIN
AMFTDAEDQS VWFYIKWFIK NDIVCKTLDE QEYLKMLKDL RENILLINND EIEFSGKQNI
WCLKILLVLE DILEEKEALT ERSSEQYLVQ LIDADPLRKN RYLHLLEQHK
//
