##gff-version 3 O95363 UniProtKB Domain 358 450 . . . Note=FDX-ACB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00778 O95363 UniProtKB Binding site 157 160 . . . . O95363 UniProtKB Binding site 179 179 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18611382,ECO:0000269|PubMed:19549855;Dbxref=PMID:18611382,PMID:19549855 O95363 UniProtKB Binding site 186 188 . . . . O95363 UniProtKB Binding site 193 195 . . . . O95363 UniProtKB Binding site 287 287 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18611382,ECO:0000269|PubMed:19549855;Dbxref=PMID:18611382,PMID:19549855 O95363 UniProtKB Binding site 312 312 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18611382,ECO:0000269|PubMed:19549855;Dbxref=PMID:18611382,PMID:19549855 O95363 UniProtKB Modified residue 202 202 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 O95363 UniProtKB Natural variant 57 57 . . . ID=VAR_052642;Note=S->C;Dbxref=dbSNP:rs34382405 O95363 UniProtKB Natural variant 142 142 . . . ID=VAR_077044;Note=In SPG77%3B resulted in severely impaired phenylalanine-tRNA ligase activity. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26553276;Dbxref=dbSNP:rs145555213,PMID:26553276 O95363 UniProtKB Natural variant 144 144 . . . ID=VAR_069487;Note=In COXPD14%3B results in decreased affinity for tRNA causing a decrease in the catalytic efficiency for tRNA charging%3B does not affect ATP or Phe binding. Y->C;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22499341,ECO:0000269|PubMed:22833457;Dbxref=dbSNP:rs397514610,PMID:22499341,PMID:22833457 O95363 UniProtKB Natural variant 280 280 . . . ID=VAR_052643;Note=N->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14702039,ECO:0000269|Ref.3,ECO:0000269|Ref.7;Dbxref=dbSNP:rs11243011,PMID:14702039 O95363 UniProtKB Natural variant 329 329 . . . ID=VAR_069488;Note=In COXPD14%3B results in a 4-fold decrease in the catalytic efficiency of amino acid activation mainly due to a decreased affinity for ATP%3B does not affect Phe binding%3B affects the stability of the enzyme%2C leading to a significant decrease in overall charging capacity. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22833457;Dbxref=dbSNP:rs397514611,PMID:22833457 O95363 UniProtKB Natural variant 391 391 . . . ID=VAR_069489;Note=In COXPD14%3B results in a decrease in affinity for Phe causing a decrease in aminoacylation activity%3B affects the stability of the enzyme%2C leading to a significant decrease in overall charging capacity. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22833457;Dbxref=dbSNP:rs397514612,PMID:22833457 O95363 UniProtKB Sequence conflict 158 158 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 O95363 UniProtKB Sequence conflict 361 361 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 O95363 UniProtKB Beta strand 49 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 56 59 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 68 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Turn 72 75 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 78 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 81 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3TUP O95363 UniProtKB Helix 85 99 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 104 106 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGH O95363 UniProtKB Beta strand 111 113 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 118 121 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 122 125 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 127 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 136 138 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Turn 140 142 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 145 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 156 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 160 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 169 178 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 184 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3TUP O95363 UniProtKB Beta strand 189 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 202 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Turn 206 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 212 214 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGH O95363 UniProtKB Helix 233 255 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 256 258 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HFV O95363 UniProtKB Beta strand 261 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 271 281 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 284 294 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 296 301 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 308 315 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 316 324 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 329 333 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 337 340 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 341 343 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 363 370 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 378 389 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 390 392 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 393 403 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Turn 405 407 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 410 418 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 421 423 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Helix 427 445 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MGW O95363 UniProtKB Beta strand 448 451 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3HFV