GENTAUR Molecular Products.

 PGTB2_YEAST             Reviewed;         325 AA.
 P20133; D6W4H7; P32433;
 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
 01-FEB-1996, sequence version 3.
 28-MAR-2018, entry version 162.
 RecName: Full=Geranylgeranyl transferase type-2 subunit beta;
          EC=2.5.1.60;
 AltName: Full=Geranylgeranyl transferase type II subunit beta;
          Short=GGTase-II-beta;
 AltName: Full=Type II protein geranyl-geranyltransferase subunit beta;
          Short=PGGT;
 AltName: Full=YPT1/SEC4 proteins geranylgeranyltransferase subunit beta;
 Name=BET2; OrderedLocusNames=YPR176C; ORFNames=P9705.12;
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
 Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
 Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
 NCBI_TaxID=559292;
 [1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 PubMed=2204247; DOI=10.1002/yea.320060407;
 Petersen-Bjoern S., Harrington T.R., Friesen J.D.;
 "An essential gene in Saccharomyces cerevisiae shares an upstream
 regulatory element with PRP4.";
 Yeast 6:345-352(1990).
 [2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 PubMed=1903184; DOI=10.1038/351158a0;
 Rossi G., Jiang Y., Newman A.P., Ferro-Novick S.;
 "Dependence of Ypt1 and Sec4 membrane attachment on Bet2.";
 Nature 351:158-161(1991).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=ATCC 204508 / S288c;
 PubMed=9169875;
 Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
 Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
 Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
 Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
 Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
 Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
 Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
 Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
 Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
 Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
 Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
 Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
 Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
 Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
 Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
 Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
 Zollner A., Vo D.H., Hani J.;
 "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
 Nature 387:103-105(1997).
 [4]
 GENOME REANNOTATION.
 STRAIN=ATCC 204508 / S288c;
 PubMed=24374639; DOI=10.1534/g3.113.008995;
 Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
 Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
 Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
 Cherry J.M.;
 "The reference genome sequence of Saccharomyces cerevisiae: Then and
 now.";
 G3 (Bethesda) 4:389-398(2014).
 [5]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 STRAIN=ATCC 204508 / S288c;
 PubMed=17322287; DOI=10.1101/gr.6037607;
 Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
 Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
 Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
 Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
 Kolodner R.D., LaBaer J.;
 "Approaching a complete repository of sequence-verified protein-
 encoding clones for Saccharomyces cerevisiae.";
 Genome Res. 17:536-543(2007).
 [6]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187.
 PubMed=2528686; DOI=10.1128/MCB.9.9.3698;
 Petersen-Bjoern S., Soltyk A., Beggs J.D., Friesen J.D.;
 "PRP4 (RNA4) from Saccharomyces cerevisiae: its gene product is
 associated with the U4/U6 small nuclear ribonucleoprotein particle.";
 Mol. Cell. Biol. 9:3698-3709(1989).
 [7]
 CHARACTERIZATION.
 PubMed=8232542; DOI=10.1038/366084a0;
 Jiang Y., Rossi G., Ferro-Novick S.;
 "Bet2p and Mad2p are components of a prenyltransferase that adds
 geranylgeranyl onto Ypt1p and Sec4p.";
 Nature 366:84-86(1993).
 [8]
 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
 PubMed=14562106; DOI=10.1038/nature02046;
 Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
 Dephoure N., O'Shea E.K., Weissman J.S.;
 "Global analysis of protein expression in yeast.";
 Nature 425:737-741(2003).
 -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
     geranyl-geranyl pyrophosphate to proteins having the C-terminal
     -XCC or -XCXC, where both cysteines may become modified. Acts on
     YPT1 and SEC4.
 -!- CATALYTIC ACTIVITY: Geranylgeranyl diphosphate + protein-cysteine
     = S-geranylgeranyl-protein + diphosphate.
 -!- COFACTOR:
     Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
     Note=Binds 1 zinc ion per subunit. {ECO:0000250};
 -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
 -!- INTERACTION:
     Q00618:BET4; NbExp=3; IntAct=EBI-3559, EBI-3573;
     Q9UJC3:HOOK1 (xeno); NbExp=3; IntAct=EBI-3559, EBI-746704;
     Q15008:PSMD6 (xeno); NbExp=3; IntAct=EBI-3559, EBI-359701;
 -!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD
     medium. {ECO:0000269|PubMed:14562106}.
 -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
     family. {ECO:0000305}.
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 EMBL; M29585; AAA66939.1; -; Genomic_DNA.
 EMBL; M26597; AAA79331.1; -; Genomic_DNA.
 EMBL; U25842; AAB68110.1; -; Genomic_DNA.
 EMBL; AY558067; AAS56393.1; -; Genomic_DNA.
 EMBL; BK006949; DAA11593.1; -; Genomic_DNA.
 PIR; S59834; S59834.
 RefSeq; NP_015502.1; NM_001184273.1.
 ProteinModelPortal; P20133; -.
 SMR; P20133; -.
 BioGrid; 36349; 354.
 DIP; DIP-2214N; -.
 IntAct; P20133; 5.
 STRING; 4932.YPR176C; -.
 MaxQB; P20133; -.
 PaxDb; P20133; -.
 PRIDE; P20133; -.
 EnsemblFungi; YPR176C; YPR176C; YPR176C.
 GeneID; 856306; -.
 KEGG; sce:YPR176C; -.
 EuPathDB; FungiDB:YPR176C; -.
 SGD; S000006380; BET2.
 GeneTree; ENSGT00530000063392; -.
 HOGENOM; HOG000180334; -.
 InParanoid; P20133; -.
 KO; K05956; -.
 OMA; WGEEDTR; -.
 OrthoDB; EOG092C3IJW; -.
 BioCyc; YEAST:MONOMER3O-1; -.
 Reactome; R-SCE-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
 Reactome; R-SCE-8873719; RAB geranylgeranylation.
 PRO; PR:P20133; -.
 Proteomes; UP000002311; Chromosome XVI.
 GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:SGD.
 GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IDA:SGD.
 GO; GO:0017137; F:Rab GTPase binding; ISS:UniProtKB.
 GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
 GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:SGD.
 GO; GO:0018344; P:protein geranylgeranylation; IDA:SGD.
 GO; GO:0006612; P:protein targeting to membrane; IMP:SGD.
 CDD; cd02894; GGTase-II; 1.
 InterPro; IPR001330; PFTB_repeat.
 InterPro; IPR026873; Ptb1.
 InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
 Pfam; PF00432; Prenyltrans; 5.
 SUPFAM; SSF48239; SSF48239; 1.
 1: Evidence at protein level;
 Complete proteome; Metal-binding; Prenyltransferase;
 Reference proteome; Repeat; Transferase; Zinc.
 CHAIN         1    325       Geranylgeranyl transferase type-2 subunit
                              beta.
                              /FTId=PRO_0000119777.
 REPEAT        9     50       PFTB 1.
 REPEAT       57     99       PFTB 2.
 REPEAT      109    150       PFTB 3.
 REPEAT      157    198       PFTB 4.
 REPEAT      208    249       PFTB 5.
 REPEAT      256    298       PFTB 6.
 REGION      183    185       Geranylgeranyl diphosphate binding.
                              {ECO:0000250}.
 REGION      228    240       Geranylgeranyl diphosphate binding.
                              {ECO:0000250}.
 METAL       234    234       Zinc. {ECO:0000250}.
 METAL       234    234       Zinc; catalytic. {ECO:0000250}.
 METAL       236    236       Zinc. {ECO:0000250}.
 METAL       236    236       Zinc; catalytic. {ECO:0000250}.
 METAL       286    286       Zinc. {ECO:0000250}.
 METAL       286    286       Zinc; via tele nitrogen; catalytic.
                              {ECO:0000250}.
 CONFLICT     22     22       K -> N (in Ref. 1 and 5). {ECO:0000305}.
 SEQUENCE   325 AA;  36666 MW;  6A9C44DFBE62AAFC CRC64;
 MSGSLTLLKE KHIRYIESLD TKKHNFEYWL TEHLRLNGIY WGLTALCVLD SPETFVKEEV
 ISFVLSCWDD KYGAFAPFPR HDAHLLTTLS AVQILATYDA LDVLGKDRKV RLISFIRGNQ
 LEDGSFQGDR FGEVDTRFVY TALSALSILG ELTSEVVDPA VDFVLKCYNF DGGFGLCPNA
 ESHAAQAFTC LGALAIANKL DMLSDDQLEE IGWWLCERQL PEGGLNGRPS KLPDVCYSWW
 VLSSLAIIGR LDWINYEKLT EFILKCQDEK KGGISDRPEN EVDVFHTVFG VAGLSLMGYD
 NLVPIDPIYC MPKSVTSKFK KYPYK

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