FNTA_SCHPO
ID FNTA_SCHPO Reviewed; 294 AA.
AC O60052;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha;
DE EC=2.5.1.58 {ECO:0000269|PubMed:10617635};
DE EC=2.5.1.59 {ECO:0000269|PubMed:9781874};
DE AltName: Full=CAAX farnesyltransferase subunit alpha;
DE AltName: Full=FTase-alpha;
DE AltName: Full=Ras proteins prenyltransferase subunit alpha;
DE AltName: Full=Type I protein geranyl-geranyltransferase subunit alpha;
DE Short=GGTase-I-alpha;
GN Name=cwp1; ORFNames=SPAPB1A10.04c;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9781874; DOI=10.1046/j.1365-2958.1998.01009.x;
RA Arellano M., Coll P.M., Yang W., Duran A., Tamanoi F., Perez P.;
RT "Characterization of the geranylgeranyl transferase type I from
RT Schizosaccharomyces pombe.";
RL Mol. Microbiol. 29:1357-1367(1998).
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=10617635; DOI=10.1074/jbc.275.1.429;
RA Yang W., Urano J., Tamanoi F.;
RT "Protein farnesylation is critical for maintaining normal cell morphology
RT and canavanine resistance in Schizosaccharomyces pombe.";
RL J. Biol. Chem. 275:429-438(2000).
CC -!- FUNCTION: Catalyzes the transfer of a farnesyl or geranyl-geranyl
CC moiety from farnesyl or geranyl-geranyl diphosphate to a cysteine at
CC the fourth position from the C-terminus of several proteins having the
CC C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha(cwp1) subunit
CC is thought to participate in a stable complex with the substrate. The
CC beta(cpp1 or cwg2) subunits bind the peptide substrate.
CC {ECO:0000269|PubMed:10617635, ECO:0000269|PubMed:9781874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019,
CC ChEBI:CHEBI:175763; EC=2.5.1.58;
CC Evidence={ECO:0000269|PubMed:10617635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13346;
CC Evidence={ECO:0000269|PubMed:10617635};
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=2.5.1.59;
CC Evidence={ECO:0000269|PubMed:9781874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21241;
CC Evidence={ECO:0000269|PubMed:9781874};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P29703};
CC -!- SUBUNIT: Heterodimer of an alpha(cwp1) and a beta(cpp1 or cwg2)
CC subunit. {ECO:0000269|PubMed:10617635, ECO:0000269|PubMed:9781874}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000305}.
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DR EMBL; AJ223304; CAA11246.1; -; Genomic_DNA.
DR EMBL; CU329670; CAC21477.1; -; Genomic_DNA.
DR RefSeq; NP_593518.1; NM_001018952.2.
DR AlphaFoldDB; O60052; -.
DR SMR; O60052; -.
DR BioGRID; 279575; 4.
DR STRING; 4896.SPAPB1A10.04c.1; -.
DR MaxQB; O60052; -.
DR PaxDb; O60052; -.
DR EnsemblFungi; SPAPB1A10.04c.1; SPAPB1A10.04c.1:pep; SPAPB1A10.04c.
DR GeneID; 2543143; -.
DR KEGG; spo:SPAPB1A10.04c; -.
DR PomBase; SPAPB1A10.04c; cwp1.
DR VEuPathDB; FungiDB:SPAPB1A10.04c; -.
DR eggNOG; KOG0530; Eukaryota.
DR HOGENOM; CLU_026582_1_1_1; -.
DR InParanoid; O60052; -.
DR OMA; RRKYWQY; -.
DR PhylomeDB; O60052; -.
DR Reactome; R-SPO-9648002; RAS processing.
DR PRO; PR:O60052; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004660; F:protein farnesyltransferase activity; IDA:PomBase.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; ISM:PomBase.
DR GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; IDA:PomBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IC:PomBase.
DR InterPro; IPR002088; Prenyl_trans_a.
DR Pfam; PF01239; PPTA; 5.
DR PROSITE; PS51147; PFTA; 5.
PE 1: Evidence at protein level;
KW Magnesium; Prenyltransferase; Reference proteome; Repeat; Transferase.
FT CHAIN 1..294
FT /note="Protein
FT farnesyltransferase/geranylgeranyltransferase type-1
FT subunit alpha"
FT /id="PRO_0000119753"
FT REPEAT 57..91
FT /note="PFTA 1"
FT REPEAT 92..125
FT /note="PFTA 2"
FT REPEAT 126..160
FT /note="PFTA 3"
FT REPEAT 161..194
FT /note="PFTA 4"
FT REPEAT 199..233
FT /note="PFTA 5"
SQ SEQUENCE 294 AA; 34876 MW; 840889770F11451E CRC64;
MDPIDPELNE ILDFTEYGPL TPIPQDDGEN PLAKICYTTG YEQGMAYFRA IMAKKEYSLR
ALNLTGFLIM NNPAHYTVWA YRFQILNHTP SYIDNELEWL DEIAEDFQKN YQVWHHRQKI
LSLTKNYERE LEFTKKMFEI DSKNYHVWSY RVWILQNFND YSQELKLTNE LLEKDIYNNS
AWNHRFYVLF ETSKVVSWSL EEELNYLKDK ILFAPDNQSA WNYLCGVLDK SGPSKLDNLI
ANLRKNLPAL HKPLLEFLAM YEPSSSEEIY QKLANEVDVP HAALWTWMSQ RSNP
