##gff-version 3
P22007	UniProtKB	Chain	1	431	.	.	.	ID=PRO_0000119768;Note=Protein farnesyltransferase subunit beta	
P22007	UniProtKB	Repeat	130	171	.	.	.	Note=PFTB 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22007	UniProtKB	Repeat	182	224	.	.	.	Note=PFTB 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22007	UniProtKB	Repeat	231	273	.	.	.	Note=PFTB 3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22007	UniProtKB	Repeat	280	322	.	.	.	Note=PFTB 4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22007	UniProtKB	Repeat	332	375	.	.	.	Note=PFTB 5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22007	UniProtKB	Binding site	258	261	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49356	
P22007	UniProtKB	Binding site	301	304	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49356	
P22007	UniProtKB	Binding site	307	307	.	.	.	Ontology_term=ECO:0000250,ECO:0000305,ECO:0000305;evidence=ECO:0000250|UniProtKB:P49356,ECO:0000305|PubMed:10529185,ECO:0000305|PubMed:12173942;Dbxref=PMID:10529185,PMID:12173942	
P22007	UniProtKB	Binding site	309	309	.	.	.	Ontology_term=ECO:0000250,ECO:0000305,ECO:0000305;evidence=ECO:0000250|UniProtKB:P49356,ECO:0000305|PubMed:10529185,ECO:0000305|PubMed:12173942;Dbxref=PMID:10529185,PMID:12173942	
P22007	UniProtKB	Binding site	310	313	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49356	
P22007	UniProtKB	Binding site	363	363	.	.	.	Ontology_term=ECO:0000250,ECO:0000305,ECO:0000305;evidence=ECO:0000250|UniProtKB:P49356,ECO:0000305|PubMed:10529185,ECO:0000305|PubMed:12173942;Dbxref=PMID:10529185,PMID:12173942	
P22007	UniProtKB	Site	108	108	.	.	.	Note=Important for selectivity against geranylgeranyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49356	
P22007	UniProtKB	Mutagenesis	57	64	.	.	.	Note=Impairs isoprenyl transferase activity. RYKVLQSV->HYKFFQRH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9545274;Dbxref=PMID:9545274	
P22007	UniProtKB	Mutagenesis	74	74	.	.	.	Note=Farnesylates only Ras-CIIS and not Ras-CII(M%2CL)%2C and it geranylgeranylates all three substrates as well or better than wild type. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9545274;Dbxref=PMID:9545274	
P22007	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Alters protein substrate specificity. Able to farnesylate Ras2 variants with positively charged C-terminal amino acids (CIIR and CIIK). G->D%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9380709;Dbxref=PMID:9380709	
P22007	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Alters protein substrate specificity. Able to farnesylate Ras2 variants with a negatively charged C-terminal aspartate (CIID). G->R%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9380709;Dbxref=PMID:9380709	
P22007	UniProtKB	Mutagenesis	159	159	.	.	.	Note=Can substitute for PGGT-I beta subunit (CDC43) in vivo. Has increased activity to farnesylate a substrate for PGGT-I. On the other hand%2C the ability to farnesylate its own substrate is reduced%2C due to its increased affinity for PGGT-I protein substrates. Increases the kcat/Km value for PGGTase-I substrates about 20-fold. S->D%2CN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7878044,ECO:0000269|PubMed:8995312;Dbxref=PMID:7878044,PMID:8995312	
P22007	UniProtKB	Mutagenesis	206	212	.	.	.	Note=Farnesylates Ras-CII(S%2CM%2CL) at wild type levels but can no longer geranylgeranylate the RasCII(M%2CL) substrates. GEVDTRG->DEDDLRF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9545274;Dbxref=PMID:9545274	
P22007	UniProtKB	Mutagenesis	209	209	.	.	.	Note=In ram1-1%3B causes a defect in a-factor production. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2124698,ECO:0000269|PubMed:8494894;Dbxref=PMID:2124698,PMID:8494894	
P22007	UniProtKB	Mutagenesis	259	259	.	.	.	Note=In ram1-2%3B abolishes farnesyltransferase activity. G->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1860864,ECO:0000269|PubMed:8494894;Dbxref=PMID:1860864,PMID:8494894	
P22007	UniProtKB	Mutagenesis	308	308	.	.	.	Note=Impairs isoprenyl transferase activity. G->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9545274;Dbxref=PMID:9545274	
P22007	UniProtKB	Mutagenesis	310	310	.	.	.	Note=Impairs isoprenyl transferase activity. Y->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10529185;Dbxref=PMID:10529185	
P22007	UniProtKB	Mutagenesis	351	354	.	.	.	Note=Farnesylates Ras-CIIS and Ras-CIIM but not Ras-CIIL%2C and is not capable of geranylgeranylating the Ras-CII(M%2CL) substrates. LRDK->FSKN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9545274;Dbxref=PMID:9545274	
P22007	UniProtKB	Mutagenesis	362	362	.	.	.	Note=Can substitute for PGGT-I beta subunit%2C by modulating the substrate specificity for the peptide substrate. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8995312;Dbxref=PMID:8995312	
P22007	UniProtKB	Mutagenesis	362	362	.	.	.	Note=Can substitute for PGGT-I beta subunit%2C by modulating the substrate specificity for the peptide substrate. Increases the kcat/Km value for PGGTase-I substrates about 20-fold. Y->L%2CM%2CI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8995312;Dbxref=PMID:8995312	
P22007	UniProtKB	Mutagenesis	366	366	.	.	.	Note=Can substitute for PGGT-I beta subunit%2C by modulating the substrate specificity for the peptide substrate. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8995312;Dbxref=PMID:8995312	
P22007	UniProtKB	Sequence conflict	47	47	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305