PGTB2_SCHPO
ID PGTB2_SCHPO Reviewed; 311 AA.
AC P46960;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
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;
GN Name=ptb1; ORFNames=SPAC167.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8740421;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<479::aid-yea926>3.0.co;2-p;
RA Godfrey R., Davey J.;
RT "Sequence of ptb1, a gene for the beta subunit of the type-II
RT geranylgeranyltransferase from the fission yeast Schizosaccharomyces
RT pombe.";
RL Yeast 12:479-482(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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.
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.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; X92183; CAA63094.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA22847.1; -; Genomic_DNA.
DR PIR; S65091; S65091.
DR RefSeq; NP_593383.1; NM_001018815.2.
DR AlphaFoldDB; P46960; -.
DR SMR; P46960; -.
DR STRING; 4896.SPAC167.02.1; -.
DR MaxQB; P46960; -.
DR PaxDb; P46960; -.
DR EnsemblFungi; SPAC167.02.1; SPAC167.02.1:pep; SPAC167.02.
DR GeneID; 2543284; -.
DR KEGG; spo:SPAC167.02; -.
DR PomBase; SPAC167.02; ptb1.
DR VEuPathDB; FungiDB:SPAC167.02; -.
DR eggNOG; KOG0366; Eukaryota.
DR HOGENOM; CLU_028946_3_0_1; -.
DR InParanoid; P46960; -.
DR OMA; VKRCQCP; -.
DR PhylomeDB; P46960; -.
DR Reactome; R-SPO-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR Reactome; R-SPO-8873719; RAB geranylgeranylation.
DR PRO; PR:P46960; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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; ISO:PomBase.
DR GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IC:PomBase.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
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; Reference proteome; Repeat; Transferase;
KW Zinc.
FT CHAIN 1..311
FT /note="Geranylgeranyl transferase type-2 subunit beta"
FT /id="PRO_0000119779"
FT REPEAT 54..95
FT /note="PFTB 1"
FT REPEAT 102..143
FT /note="PFTB 2"
FT REPEAT 150..191
FT /note="PFTB 3"
FT REPEAT 197..239
FT /note="PFTB 4"
FT REPEAT 246..288
FT /note="PFTB 5"
FT BINDING 176..178
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250"
FT BINDING 218..230
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 311 AA; 35092 MW; 2AB617FC769D3B08 CRC64;
MAVLLRDKHI SYLHDIGNRT DELDFWLKEH LHVSAIYWSC MSFWLLKKKD QIDKERIVSF
LLSCLTESGG FACYPGHDDH ITNTVYAVQV LAMLDSLHVV DKDKVASYII GLQNEDGSMK
GDRWGEIDAR FLYSGINCLA ILGKLDYLNK NTAVDWLMKC YNFDGGFGLC PGAESHGAMV
FTCVAALKIL NKLDLIDEEL LGWWISERQV KGGGLNGRPE KLPDSCYGWW DLSPLAIIGK
LDWIDRNQLI DFLLGTQDAD SGGFADRKED ATDVYHTCFS LAGLSLLQFP NIEPVDPRFC
LPLEVTQKMK L
