FNTB_DICDI
ID FNTB_DICDI Reviewed; 500 AA.
AC Q55D51;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein farnesyltransferase subunit beta;
DE Short=FTase-beta;
DE EC=2.5.1.58;
DE AltName: Full=CAAX farnesyltransferase subunit beta;
DE AltName: Full=Ras proteins prenyltransferase subunit beta;
GN Name=fntB; ORFNames=DDB_G0270948;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the transfer of a farnesyl moiety from farnesyl
CC diphosphate to a cysteine at the fourth position from the C-terminus of
CC several proteins. The beta subunit is responsible for peptide-binding
CC (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P49356};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P49356};
CC -!- SUBUNIT: Heterodimer of fntA and fntB (farnesyltransferase).
CC Heterodimer of an alpha and a beta subunit (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72824.1; -; Genomic_DNA.
DR RefSeq; XP_646280.1; XM_641188.1.
DR AlphaFoldDB; Q55D51; -.
DR SMR; Q55D51; -.
DR STRING; 44689.DDB0237553; -.
DR PaxDb; Q55D51; -.
DR PRIDE; Q55D51; -.
DR EnsemblProtists; EAL72824; EAL72824; DDB_G0270948.
DR GeneID; 8617235; -.
DR KEGG; ddi:DDB_G0270948; -.
DR dictyBase; DDB_G0270948; fntB.
DR eggNOG; KOG0365; Eukaryota.
DR HOGENOM; CLU_028946_0_1_1; -.
DR InParanoid; Q55D51; -.
DR OMA; WCIYWIL; -.
DR PhylomeDB; Q55D51; -.
DR Reactome; R-DDI-9648002; RAS processing.
DR PRO; PR:Q55D51; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR GO; GO:0004660; F:protein farnesyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR CDD; cd02893; FTase; 1.
DR InterPro; IPR026872; FTB.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 1.
DR PANTHER; PTHR11774:SF6; PTHR11774:SF6; 1.
DR Pfam; PF00432; Prenyltrans; 4.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 3: Inferred from homology;
KW Metal-binding; Prenyltransferase; Reference proteome; Repeat; Transferase;
KW Zinc.
FT CHAIN 1..500
FT /note="Protein farnesyltransferase subunit beta"
FT /id="PRO_0000328342"
FT REPEAT 121..162
FT /note="PFTB 1"
FT REPEAT 172..213
FT /note="PFTB 2"
FT REPEAT 220..261
FT /note="PFTB 3"
FT REPEAT 268..309
FT /note="PFTB 4"
FT REPEAT 343..384
FT /note="PFTB 5"
FT REGION 117..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..249
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 288..291
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 297..300
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT SITE 85
FT /note="Important for selectivity against geranylgeranyl
FT diphosphate"
FT /evidence="ECO:0000250|UniProtKB:P49356"
SQ SEQUENCE 500 AA; 56488 MW; 886213CE6714B50C CRC64;
MSSIEEIDTD ETFTSDYVSA RKDEVDDIIT ATTIAQKKME NSILEKLNST ENGNIIEKKK
ILNFLMNGIE KIPMSHQGLD SSKVWISFWI LNGMDMLDSL DSYPNISSRA SKYLSILQND
DNNGNNNNRE NNQNGGGFGG GNSHTSHVVS TFAAVSALYV IGTEESYKTI DREAMYKFLM
RMKTKEGAFT SEDGGEYDSR TTYCAIAVAS MLNILTAELE RGVVDFLLSC QTYEGGFGAY
PFNEAHGGYT FCSVAALSIL NSLHKIDMNS LHRWITYRQS NDGGFEGRTN KLVDTCYSYW
QGAVYIIIQS YFNYYKKQQQ DDGDGKEGDQ QEEGLLFNQA KLQEYVIRFC QQSDKKYSGF
SDHPHRGKDY YHTCYGLSGI SLSQYNEIGK AIQSLNTFTN TFEQPSPPIN KKSTNVFTIS
NNNNNNNNKN NNSDDNNNNS NNNNNNSENQ LVEPVHPIYN IKLSKCEKGF EIDLFLFQKE
FKDASVSLGT LFFYAKFILK
