FNTB_MAGO7
ID FNTB_MAGO7 Reviewed; 514 AA.
AC G4MY67;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Protein farnesyltransferase subunit beta;
DE Short=FTase-beta;
DE Short=PFTase beta;
DE EC=2.5.1.58 {ECO:0000250|UniProtKB:P22007};
DE AltName: Full=CAAX farnesyltransferase subunit beta;
DE AltName: Full=Ras proteins prenyltransferase subunit beta;
GN Name=RAM1; ORFNames=MGG_01287;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP RAS1 AND RAS2.
RX PubMed=31250536; DOI=10.1111/mpp.12838;
RA Aboelfotoh Hendy A., Xing J., Chen X., Chen X.L.;
RT "The farnesyltransferase beta-subunit RAM1 regulates localization of RAS
RT proteins and appressorium-mediated infection in Magnaporthe oryzae.";
RL Mol. Plant Pathol. 20:1264-1278(2019).
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 having the C-terminal sequence Cys-aliphatic-
CC aliphatic-X. The beta subunit is responsible for peptide-binding.
CC {ECO:0000269|PubMed:31250536}.
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:0000250|UniProtKB:P22007};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13346;
CC Evidence={ECO:0000250|UniProtKB:P22007};
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 an alpha and a beta subunit (By similarity).
CC Interacts with RAS1 and RAS2 (PubMed:31250536).
CC {ECO:0000250|UniProtKB:P49356, ECO:0000269|PubMed:31250536}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31250536}.
CC -!- TISSUE SPECIFICITY: Highly expressed in mycelium, conidium, conidial
CC germination, early formed appressorium and the late infection hypha.
CC {ECO:0000269|PubMed:31250536}.
CC -!- DISRUPTION PHENOTYPE: Shows a significantly reduced endogenous cAMP
CC level. Results in the reduction of hyphal growth and sporulation, and
CC an increase in the sensitivity to various stresses. Attenuates
CC virulence on the plant host by impairing appressorium-mediated
CC penetration and invasive growth. {ECO:0000269|PubMed:31250536}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001232; EHA54398.1; -; Genomic_DNA.
DR RefSeq; XP_003714205.1; XM_003714157.1.
DR AlphaFoldDB; G4MY67; -.
DR SMR; G4MY67; -.
DR STRING; 318829.MGG_01287T0; -.
DR EnsemblFungi; MGG_01287T0; MGG_01287T0; MGG_01287.
DR GeneID; 2679721; -.
DR KEGG; mgr:MGG_01287; -.
DR VEuPathDB; FungiDB:MGG_01287; -.
DR eggNOG; KOG0365; Eukaryota.
DR HOGENOM; CLU_028946_1_0_1; -.
DR InParanoid; G4MY67; -.
DR OMA; WCIYWIL; -.
DR OrthoDB; 1042804at2759; -.
DR BRENDA; 2.5.1.58; 5238.
DR Proteomes; UP000009058; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IDA:PHI-base.
DR GO; GO:0005965; C:protein farnesyltransferase complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004660; F:protein farnesyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; IMP:PHI-base.
DR GO; GO:0018343; P:protein farnesylation; IMP:PHI-base.
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 Cytoplasm; Metal-binding; Prenyltransferase; Reference proteome; Repeat;
KW Transferase; Zinc.
FT CHAIN 1..514
FT /note="Protein farnesyltransferase subunit beta"
FT /id="PRO_0000449943"
FT REPEAT 180..221
FT /note="PFTB 1"
FT /evidence="ECO:0000255"
FT REPEAT 231..272
FT /note="PFTB 2"
FT /evidence="ECO:0000255"
FT REPEAT 293..334
FT /note="PFTB 3"
FT /evidence="ECO:0000255"
FT REPEAT 346..388
FT /note="PFTB 4"
FT /evidence="ECO:0000255"
FT REPEAT 410..454
FT /note="PFTB 5"
FT /evidence="ECO:0000255"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 319..322
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 367..370
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 376..379
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 442
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT SITE 159
FT /note="Important for selectivity against geranylgeranyl
FT diphosphate"
FT /evidence="ECO:0000250|UniProtKB:P49356"
SQ SEQUENCE 514 AA; 56099 MW; 88352690C3B2758F CRC64;
MRHHTKNLRR RAIFLRTTPR GNMDSSSSVA TSTSSSSNHR LVRSSEGSPS AGGDDIEEVI
MTPGIATGRV QPAVSVAIPD LFTQLPPVKD DLATSTSKTQ DETVAICLPY LAGSDANADV
EHNAHGVPHI DRKKHVRFLR NMLRQLPAPF IAADASRPWF LYWSLNAMAI LGENVKEDYA
ESLADTARSM QNESGGFSGG HGQTSHLATT YAVVLALAVV GDEEGLSLID RRALWKWLCD
LKEADGGFRM SLGGEEDVRG AYCAAVIISL LNLPLDLCKD SEAYIRDPTA NLFTGLGDYV
RKCQTFEGGI SGQPDAEAHG AYAFCALGCL SLLGTPSETI PKYLNIERLI SWLSSRQYAP
EGGFSGRTNK LVDGCYSHWV GGCWPLIEAC LNGPVKVSSL DVEPQPLFSR EGLMRYILCC
CQEQGKRGGL RDKPGKPSDA YHSCYVLSGL SSAQNRWQLV VGDDDMPAWM VSPFPNEEEI
FDEKDRVGTV HPVYVIPEDK VAKVQTFFAS RDGF
