FNTB_RAT
ID FNTB_RAT Reviewed; 437 AA.
AC Q02293;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 181.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1855253; DOI=10.1016/0092-8674(91)90622-6;
RA Chen W.-J., Andres D.A., Goldstein J.L., Russell D.W., Brown M.S.;
RT "cDNA cloning and expression of the peptide-binding beta subunit of rat
RT p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1.";
RL Cell 66:327-334(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH ZINC.
RX PubMed=9065406; DOI=10.1126/science.275.5307.1800;
RA Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.;
RT "Crystal structure of protein farnesyltransferase at 2.25-A resolution.";
RL Science 275:1800-1804(1997).
RN [4]
RP ERRATUM OF PUBMED:9065406.
RA Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.;
RL Science 276:21-21(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL
RP DIPHOSPHATE AND ZINC IONS, SUBUNIT, AND COFACTOR.
RX PubMed=9609683; DOI=10.1021/bi980531o;
RA Dunten P., Kammlott U., Crowther R., Weber D., Palermo R., Birktoft J.;
RT "Protein farnesyltransferase: structure and implications for substrate
RT binding.";
RL Biochemistry 37:7907-7912(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL
RP DIPHOSPHATE AND ZINC IONS, COFACTOR, AND SUBUNIT.
RX PubMed=9657673; DOI=10.1021/bi980708e;
RA Long S.B., Casey P.J., Beese L.S.;
RT "Cocrystal structure of protein farnesyltransferase complexed with a
RT farnesyl diphosphate substrate.";
RL Biochemistry 37:9612-9618(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND
RP FARNESYL DIPHOSPHATE ANALOG, COFACTOR, AND SUBUNIT.
RX PubMed=9843427; DOI=10.1021/bi981197z;
RA Strickland C.L., Windsor W.T., Syto R., Wang L., Bond R., Wu Z.,
RA Schwartz J., Le H.V., Beese L.S., Weber P.C.;
RT "Crystal structure of farnesyl protein transferase complexed with a CaaX
RT peptide and farnesyl diphosphate analogue.";
RL Biochemistry 37:16601-16611(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA AND
RP KRAS, INTERACTION WITH KRAS, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, AND
RP SUBUNIT.
RX PubMed=10673434; DOI=10.1016/s0969-2126(00)00096-4;
RA Long S.B., Casey P.J., Beese L.S.;
RT "The basis for K-Ras4B binding specificity to protein farnesyltransferase
RT revealed by 2 A resolution ternary complex structures.";
RL Structure 8:209-222(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FNTA AND
RP GERANYLGERANYL DIPHOSPHATE, AND SUBUNIT.
RX PubMed=11687658; DOI=10.1073/pnas.241407898;
RA Long S.B., Hancock P.J., Kral A.M., Hellinga H.W., Beese L.S.;
RT "The crystal structure of human protein farnesyltransferase reveals the
RT basis for inhibition by CaaX tetrapeptides and their mimetics.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12948-12953(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL
RP DIPHOSPHATE AND ZINC IONS, SUBUNIT, AND COFACTOR.
RX PubMed=12374986; DOI=10.1038/nature00986;
RA Long S.B., Casey P.J., Beese L.S.;
RT "Reaction path of protein farnesyltransferase at atomic resolution.";
RL Nature 419:645-650(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA;
RP GERANYLGERANYL DIPHOSPHATE AND ZINC IONS, COFACTOR, AND SUBUNIT.
RX PubMed=12667062; DOI=10.1021/bi0266838;
RA Turek-Etienne T.C., Strickland C.L., Distefano M.D.;
RT "Biochemical and structural studies with prenyl diphosphate analogues
RT provide insights into isoprenoid recognition by protein farnesyl
RT transferase.";
RL Biochemistry 42:3716-3724(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH FNTA AND ZINC IONS,
RP COFACTOR, AND SUBUNIT.
RX PubMed=15451670; DOI=10.1016/j.jmb.2004.08.056;
RA Reid T.S., Terry K.L., Casey P.J., Beese L.S.;
RT "Crystallographic analysis of CaaX prenyltransferases complexed with
RT substrates defines rules of protein substrate selectivity.";
RL J. Mol. Biol. 343:417-433(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL
RP DIPHOSPHATE AND ZINC, COFACTOR, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=18844669; DOI=10.1111/j.1747-0285.2008.00698.x;
RA DeGraw A.J., Hast M.A., Xu J., Mullen D., Beese L.S., Barany G.,
RA Distefano M.D.;
RT "Caged protein prenyltransferase substrates: tools for understanding
RT protein prenylation.";
RL Chem. Biol. Drug Des. 72:171-181(2008).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL
RP DIPHOSPHATE AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, AND
RP SUBUNIT.
RX PubMed=19246009; DOI=10.1016/j.chembiol.2009.01.014;
RA Hast M.A., Fletcher S., Cummings C.G., Pusateri E.E., Blaskovich M.A.,
RA Rivas K., Gelb M.H., Van Voorhis W.C., Sebti S.M., Hamilton A.D.,
RA Beese L.S.;
RT "Structural basis for binding and selectivity of antimalarial and
RT anticancer ethylenediamine inhibitors to protein farnesyltransferase.";
RL Chem. Biol. 16:181-192(2009).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA AND
RP ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=19219049; DOI=10.1038/nchembio.149;
RA Nguyen U.T., Guo Z., Delon C., Wu Y., Deraeve C., Franzel B., Bon R.S.,
RA Blankenfeldt W., Goody R.S., Waldmann H., Wolters D., Alexandrov K.;
RT "Analysis of the eukaryotic prenylome by isoprenoid affinity tagging.";
RL Nat. Chem. Biol. 5:227-235(2009).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL
RP DIPHOSPHATE AND ZINC, SUBUNIT, AND COFACTOR.
RX PubMed=20056542; DOI=10.1016/j.bmcl.2009.12.013;
RA Zhu H.Y., Cooper A.B., Desai J., Njoroge G., Kirschmeier P., Bishop W.R.,
RA Strickland C., Hruza A., Doll R.J., Girijavallabhan V.M.;
RT "Discovery of C-imidazole azaheptapyridine FPT inhibitors.";
RL Bioorg. Med. Chem. Lett. 20:1134-1136(2010).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA;
RP FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY,
RP AND FUNCTION.
RX PubMed=22963166; DOI=10.1021/jm300624s;
RA Stigter E.A., Guo Z., Bon R.S., Wu Y.W., Choidas A., Wolf A., Menninger S.,
RA Waldmann H., Blankenfeldt W., Goody R.S.;
RT "Development of selective, potent RabGGTase inhibitors.";
RL J. Med. Chem. 55:8330-8340(2012).
CC -!- FUNCTION: Essential subunit of the farnesyltransferase complex.
CC Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate
CC to a cysteine at the fourth position from the C-terminus of several
CC proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.
CC {ECO:0000269|PubMed:10673434, ECO:0000269|PubMed:19219049,
CC ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:22963166}.
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:10673434, ECO:0000269|PubMed:18844669,
CC ECO:0000269|PubMed:19219049, ECO:0000269|PubMed:19246009,
CC ECO:0000269|PubMed:22963166};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10673434, ECO:0000269|PubMed:12374986,
CC ECO:0000269|PubMed:12667062, ECO:0000269|PubMed:15451670,
CC ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:19219049,
CC ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:20056542,
CC ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:9609683,
CC ECO:0000269|PubMed:9657673, ECO:0000269|PubMed:9843427};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10673434,
CC ECO:0000269|PubMed:12374986, ECO:0000269|PubMed:12667062,
CC ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:18844669,
CC ECO:0000269|PubMed:19219049, ECO:0000269|PubMed:19246009,
CC ECO:0000269|PubMed:20056542, ECO:0000269|PubMed:22963166,
CC ECO:0000269|PubMed:9609683, ECO:0000269|PubMed:9657673,
CC ECO:0000269|PubMed:9843427};
CC -!- SUBUNIT: Heterodimer of FNTA and FNTB. {ECO:0000269|PubMed:10673434,
CC ECO:0000269|PubMed:11687658, ECO:0000269|PubMed:12374986,
CC ECO:0000269|PubMed:12667062, ECO:0000269|PubMed:15451670,
CC ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:19219049,
CC ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:20056542,
CC ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:9065406,
CC ECO:0000269|PubMed:9609683, ECO:0000269|PubMed:9657673,
CC ECO:0000269|PubMed:9843427}.
CC -!- INTERACTION:
CC Q02293; Q04631: Fnta; NbExp=16; IntAct=EBI-602454, EBI-602447;
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; M69056; AAA41176.1; -; mRNA.
DR EMBL; BC087675; AAH87675.1; -; mRNA.
DR PIR; A40037; A40037.
DR RefSeq; NP_742031.1; NM_172034.2.
DR PDB; 1D8D; X-ray; 2.00 A; B=1-437.
DR PDB; 1D8E; X-ray; 3.00 A; B=1-437.
DR PDB; 1FPP; X-ray; 2.75 A; B=1-437.
DR PDB; 1FT1; X-ray; 2.25 A; B=1-437.
DR PDB; 1FT2; X-ray; 3.40 A; B=22-422.
DR PDB; 1JCR; X-ray; 2.00 A; B=1-437.
DR PDB; 1JCS; X-ray; 2.20 A; B=1-437.
DR PDB; 1KZO; X-ray; 2.20 A; B=1-437.
DR PDB; 1KZP; X-ray; 2.10 A; B=1-437.
DR PDB; 1N94; X-ray; 3.50 A; B=22-418.
DR PDB; 1N95; X-ray; 2.30 A; B=22-423.
DR PDB; 1N9A; X-ray; 3.20 A; B=22-423.
DR PDB; 1NI1; X-ray; 2.30 A; B=22-423.
DR PDB; 1NL4; X-ray; 2.70 A; B=23-423.
DR PDB; 1O1R; X-ray; 2.30 A; B=1-427.
DR PDB; 1O1S; X-ray; 2.30 A; B=1-427.
DR PDB; 1O1T; X-ray; 2.10 A; B=1-427.
DR PDB; 1O5M; X-ray; 2.30 A; B=1-437.
DR PDB; 1QBQ; X-ray; 2.40 A; B=1-437.
DR PDB; 1SA5; X-ray; 2.60 A; B=1-437.
DR PDB; 1TN7; X-ray; 2.30 A; B=1-437.
DR PDB; 1TN8; X-ray; 2.25 A; B=1-437.
DR PDB; 1X81; X-ray; 3.50 A; B=22-418.
DR PDB; 2BED; X-ray; 2.70 A; B=23-423.
DR PDB; 2R2L; X-ray; 2.23 A; B=23-423.
DR PDB; 2ZIR; X-ray; 2.40 A; B=1-437.
DR PDB; 2ZIS; X-ray; 2.60 A; B=1-437.
DR PDB; 3DPY; X-ray; 2.70 A; B=1-437.
DR PDB; 3E30; X-ray; 2.45 A; B=1-437.
DR PDB; 3E32; X-ray; 2.45 A; B=1-437.
DR PDB; 3E33; X-ray; 1.90 A; B=1-437.
DR PDB; 3E34; X-ray; 2.05 A; B=1-437.
DR PDB; 3EU5; X-ray; 2.80 A; B=1-427.
DR PDB; 3EUV; X-ray; 2.75 A; B=1-427.
DR PDB; 3KSL; X-ray; 2.05 A; B=1-437.
DR PDB; 3KSQ; X-ray; 2.10 A; B=1-437.
DR PDB; 4GTM; X-ray; 2.20 A; B=1-427.
DR PDB; 4GTO; X-ray; 2.15 A; B=1-427.
DR PDB; 4GTP; X-ray; 2.75 A; B=1-427.
DR PDB; 4GTQ; X-ray; 2.60 A; B=1-427.
DR PDB; 4GTR; X-ray; 2.20 A; B=1-427.
DR PDB; 7RN5; X-ray; 2.28 A; B=1-437.
DR PDB; 7RNI; X-ray; 1.98 A; B=1-437.
DR PDBsum; 1D8D; -.
DR PDBsum; 1D8E; -.
DR PDBsum; 1FPP; -.
DR PDBsum; 1FT1; -.
DR PDBsum; 1FT2; -.
DR PDBsum; 1JCR; -.
DR PDBsum; 1JCS; -.
DR PDBsum; 1KZO; -.
DR PDBsum; 1KZP; -.
DR PDBsum; 1N94; -.
DR PDBsum; 1N95; -.
DR PDBsum; 1N9A; -.
DR PDBsum; 1NI1; -.
DR PDBsum; 1NL4; -.
DR PDBsum; 1O1R; -.
DR PDBsum; 1O1S; -.
DR PDBsum; 1O1T; -.
DR PDBsum; 1O5M; -.
DR PDBsum; 1QBQ; -.
DR PDBsum; 1SA5; -.
DR PDBsum; 1TN7; -.
DR PDBsum; 1TN8; -.
DR PDBsum; 1X81; -.
DR PDBsum; 2BED; -.
DR PDBsum; 2R2L; -.
DR PDBsum; 2ZIR; -.
DR PDBsum; 2ZIS; -.
DR PDBsum; 3DPY; -.
DR PDBsum; 3E30; -.
DR PDBsum; 3E32; -.
DR PDBsum; 3E33; -.
DR PDBsum; 3E34; -.
DR PDBsum; 3EU5; -.
DR PDBsum; 3EUV; -.
DR PDBsum; 3KSL; -.
DR PDBsum; 3KSQ; -.
DR PDBsum; 4GTM; -.
DR PDBsum; 4GTO; -.
DR PDBsum; 4GTP; -.
DR PDBsum; 4GTQ; -.
DR PDBsum; 4GTR; -.
DR PDBsum; 7RN5; -.
DR PDBsum; 7RNI; -.
DR AlphaFoldDB; Q02293; -.
DR SMR; Q02293; -.
DR BioGRID; 249096; 1.
DR ComplexPortal; CPX-2181; Protein farnesyltransferase complex.
DR DIP; DIP-6132N; -.
DR IntAct; Q02293; 1.
DR STRING; 10116.ENSRNOP00000010588; -.
DR BindingDB; Q02293; -.
DR ChEMBL; CHEMBL2095197; -.
DR iPTMnet; Q02293; -.
DR PhosphoSitePlus; Q02293; -.
DR jPOST; Q02293; -.
DR PaxDb; Q02293; -.
DR Ensembl; ENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660.
DR GeneID; 64511; -.
DR KEGG; rno:64511; -.
DR UCSC; RGD:620119; rat.
DR CTD; 2342; -.
DR RGD; 620119; Fntb.
DR eggNOG; KOG0365; Eukaryota.
DR GeneTree; ENSGT00950000183128; -.
DR HOGENOM; CLU_028946_0_1_1; -.
DR InParanoid; Q02293; -.
DR OMA; WCIYWIL; -.
DR OrthoDB; 1042804at2759; -.
DR PhylomeDB; Q02293; -.
DR TreeFam; TF353162; -.
DR BRENDA; 2.5.1.58; 5301.
DR BRENDA; 2.5.1.59; 5301.
DR Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-RNO-9648002; RAS processing.
DR SABIO-RK; Q02293; -.
DR EvolutionaryTrace; Q02293; -.
DR PRO; PR:Q02293; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000007660; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q02293; RN.
DR GO; GO:0005875; C:microtubule associated complex; ISO:RGD.
DR GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR GO; GO:0004311; F:farnesyltranstransferase activity; ISO:RGD.
DR GO; GO:0004660; F:protein farnesyltransferase activity; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
DR GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR GO; GO:0048145; P:regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; IMP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IMP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IMP:RGD.
DR GO; GO:0042060; P:wound healing; ISO:RGD.
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; 5.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lipid metabolism; Metal-binding;
KW Phosphoprotein; Prenyltransferase; Reference proteome; Repeat; Transferase;
KW Zinc.
FT CHAIN 1..437
FT /note="Protein farnesyltransferase subunit beta"
FT /id="PRO_0000119763"
FT REPEAT 123..164
FT /note="PFTB 1"
FT REPEAT 174..215
FT /note="PFTB 2"
FT REPEAT 222..263
FT /note="PFTB 3"
FT REPEAT 270..312
FT /note="PFTB 4"
FT REPEAT 332..374
FT /note="PFTB 5"
FT BINDING 248..251
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT BINDING 291..294
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18844669,
FT ECO:0000269|PubMed:20056542, ECO:0000269|PubMed:9065406"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18844669,
FT ECO:0000269|PubMed:20056542, ECO:0000269|PubMed:9065406"
FT BINDING 300..303
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18844669,
FT ECO:0000269|PubMed:20056542, ECO:0000269|PubMed:9065406"
FT SITE 102
FT /note="Important for selectivity against geranylgeranyl
FT diphosphate"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2I1"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2I1"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 43..65
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:3E33"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:3E33"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:3E33"
FT TURN 219..224
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 225..232
FT /evidence="ECO:0007829|PDB:3E33"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:3E33"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:3E33"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:3E33"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:3E33"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1NI1"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1NI1"
FT HELIX 332..342
FT /evidence="ECO:0007829|PDB:3E33"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1FT1"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:1N94"
FT HELIX 360..374
FT /evidence="ECO:0007829|PDB:3E33"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:3E33"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:3E33"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 405..415
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:1FT1"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:1FT1"
SQ SEQUENCE 437 AA; 48673 MW; 41A9D6D79CD319A8 CRC64;
MASSSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK VEEKIQEVFS
SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR PWLCYWILHS LELLDEPIPQ
IVATDVCQFL ELCQSPDGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYN VINREKLLQY
LYSLKQPDGS FLMHVGGEVD VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG
GVPGMEAHGG YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY
SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL LDKPGKSRDF
YHTCYCLSGL SIAQHFGSGA MLHDVVMGVP ENVLQPTHPV YNIGPDKVIQ ATTHFLQKPV
PGFEECEDAV TSDPATD
