ID   PGTA_SCHPO              Reviewed;         344 AA.
AC   O94412;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 121.
DE   RecName: Full=Geranylgeranyl transferase type-2 subunit alpha;
DE            EC=2.5.1.60;
DE   AltName: Full=GGTase-II-alpha;
DE   AltName: Full=Geranylgeranyl transferase type II subunit alpha;
DE   AltName: Full=PGGT;
DE   AltName: Full=Type II protein geranyl-geranyltransferase subunit alpha;
GN   Name=bet4; ORFNames=SPCC1620.05;
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 [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. {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   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC       family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA22489.1; -; Genomic_DNA.
DR   PIR; T41035; T41035.
DR   RefSeq; NP_588463.1; NM_001023454.2.
DR   AlphaFoldDB; O94412; -.
DR   SMR; O94412; -.
DR   BioGRID; 275909; 1.
DR   STRING; 284812.O94412; -.
DR   MaxQB; O94412; -.
DR   PaxDb; 4896-SPCC1620-05-1; -.
DR   EnsemblFungi; SPCC1620.05.1; SPCC1620.05.1:pep; SPCC1620.05.
DR   GeneID; 2539343; -.
DR   KEGG; spo:SPCC1620.05; -.
DR   PomBase; SPCC1620.05; bet4.
DR   VEuPathDB; FungiDB:SPCC1620.05; -.
DR   eggNOG; KOG0529; Eukaryota.
DR   HOGENOM; CLU_031996_0_0_1; -.
DR   InParanoid; O94412; -.
DR   OMA; RKFPKCY; -.
DR   PhylomeDB; O94412; -.
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:O94412; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; 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: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   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; 6.
PE   3: Inferred from homology;
KW   Prenyltransferase; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..344
FT                   /note="Geranylgeranyl transferase type-2 subunit alpha"
FT                   /id="PRO_0000314652"
FT   REPEAT          44..78
FT                   /note="PFTA 1"
FT   REPEAT          89..123
FT                   /note="PFTA 2"
FT   REPEAT          125..159
FT                   /note="PFTA 3"
FT   REPEAT          165..199
FT                   /note="PFTA 4"
FT   REPEAT          214..248
FT                   /note="PFTA 5"
FT   REPEAT          266..293
FT                   /note="PFTA 6"
SQ   SEQUENCE   344 AA;  41194 MW;  6801D2872013427F CRC64;
     MHGILRVKLS EEQRKLKAEK ERAKIEEYRG LVSRFQEARK RKDYSEGNLK LTTELLDWNP
     ETYSVWNYRR EILLNDVFPK ISLNEKQDLL DNELKYVLSK MKVFPKVYWI FNHRRWCLEN
     APYPNWNYEM MITEKLLSAD ARNFHGWHYR RYVVSQIERA GNCSLAKKEM EYTTSAIATN
     FSNFSALHNR TKLIETILNL EADPNSQKAL AKQILEQELD MIHQAVFTDP DDSSVWIYHR
     WLMGHCNPNS MTPLISMITI EERIQYLQKE IELIQELHEM EPENRWCCES LVNYEALCKT
     LEKQKPTEAD IKRWTLLVDK MIKVDPQRRG RYRTLQEKIN NLNK
//