##gff-version 3 P41250 UniProtKB Transit peptide 1 36 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 P41250 UniProtKB Chain 37 739 . . . ID=PRO_0000072998;Note=Glycine--tRNA ligase;Ontology_term=ECO:0000255;evidence=ECO:0000255 P41250 UniProtKB Domain 63 119 . . . Note=WHEP-TRS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00531 P41250 UniProtKB Binding site 299 299 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:19710017,ECO:0000269|PubMed:24898252,ECO:0000305|PubMed:27261259,ECO:0007744|PDB:2ZT7,ECO:0007744|PDB:4KR3;Dbxref=PMID:19710017,PMID:24898252,PMID:27261259 P41250 UniProtKB Binding site 331 333 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0000305,ECO:0007744;evidence=ECO:0000269|PubMed:19710017,ECO:0000305|PubMed:24898252,ECO:0000305|PubMed:27261259,ECO:0007744|PDB:2ZT7;Dbxref=PMID:19710017,PMID:24898252,PMID:27261259 P41250 UniProtKB Binding site 342 343 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:19710017,ECO:0007744|PDB:2ZT7;Dbxref=PMID:19710017 P41250 UniProtKB Binding site 350 350 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:19710017,ECO:0000269|PubMed:24898252,ECO:0000305|PubMed:27261259,ECO:0007744|PDB:2ZT7,ECO:0007744|PDB:4KR3;Dbxref=PMID:19710017,PMID:24898252,PMID:27261259 P41250 UniProtKB Binding site 457 458 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0000305,ECO:0007744;evidence=ECO:0000269|PubMed:19710017,ECO:0000305|PubMed:24898252,ECO:0000305|PubMed:27261259,ECO:0007744|PDB:2ZT7;Dbxref=PMID:19710017,PMID:24898252,PMID:27261259 P41250 UniProtKB Binding site 576 578 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:19710017,ECO:0000269|PubMed:24898252,ECO:0007744|PDB:2ZT7,ECO:0007744|PDB:4KR3;Dbxref=PMID:19710017,PMID:24898252 P41250 UniProtKB Binding site 583 583 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:19710017,ECO:0007744|PDB:2ZT7;Dbxref=PMID:19710017 P41250 UniProtKB Modified residue 35 35 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P41250 UniProtKB Modified residue 204 204 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P41250 UniProtKB Modified residue 453 453 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9CZD3 P41250 UniProtKB Modified residue 501 501 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P41250 UniProtKB Modified residue 700 700 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9CZD3 P41250 UniProtKB Modified residue 736 736 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P41250 UniProtKB Alternative sequence 1 54 . . . ID=VSP_060970;Note=In isoform 2. Missing;Ontology_term=ECO:0000312;evidence=ECO:0000312|EMBL:EAL24449.1 P41250 UniProtKB Natural variant 42 42 . . . ID=VAR_054865;Note=P->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:7753621,ECO:0000269|PubMed:7961834,ECO:0000269|PubMed:7962006,ECO:0007744|PubMed:23186163;Dbxref=dbSNP:rs1049402,PMID:14702039,PMID:15489334,PMID:23186163,PMID:7753621,PMID:7961834,PMID:7962006 P41250 UniProtKB Natural variant 111 111 . . . ID=VAR_073187;Note=In CMT2D%3B shows a reduction in aminoacylation activity. A->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17663003,ECO:0000269|PubMed:25168514;Dbxref=dbSNP:rs370531212,PMID:17663003,PMID:25168514 P41250 UniProtKB Natural variant 125 125 . . . ID=VAR_018718;Note=In CMT2D%3B phenotype overlapping with HMND5%3B complements the defect of the wild-type gene in yeast%3B contrary to the wild-type protein%2C strongly binds to NRP1 and competes with VEGFA for NRP1-binding%3B displays slightly elevated aminoacylation activity over wild-type. E->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12690580,ECO:0000269|PubMed:17035524,ECO:0000269|PubMed:24898252,ECO:0000269|PubMed:25168514,ECO:0000269|PubMed:26503042;Dbxref=dbSNP:rs137852645,PMID:12690580,PMID:17035524,PMID:24898252,PMID:25168514,PMID:26503042 P41250 UniProtKB Natural variant 183 183 . . . ID=VAR_018719;Note=In HMND5%3B does not complement the defect of the wild-type gene in yeast%3B contrary to the wild-type protein%2C strongly interacts with NRP1. L->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12690580,ECO:0000269|PubMed:17035524,ECO:0000269|PubMed:25168514,ECO:0000269|PubMed:26503042;Dbxref=dbSNP:rs137852644,PMID:12690580,PMID:17035524,PMID:25168514,PMID:26503042 P41250 UniProtKB Natural variant 200 200 . . . ID=VAR_073188;Note=In CMT2D and HMND5%3B shows a large reduction in aminoacylation activity. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23279345,ECO:0000269|PubMed:25168514;Dbxref=dbSNP:rs1554337369,PMID:23279345,PMID:25168514 P41250 UniProtKB Natural variant 200 200 . . . ID=VAR_074016;Note=In CMT2D. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26244500;Dbxref=PMID:26244500 P41250 UniProtKB Natural variant 265 265 . . . ID=VAR_073189;Note=In CMT2D and HMND5%3B shows a large reduction in aminoacylation activity%3B demonstrates a change in the subcellular location pattern%3B does not associate with granules. S->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23279345,ECO:0000269|PubMed:25168514;Dbxref=dbSNP:rs1554337974,PMID:23279345,PMID:25168514 P41250 UniProtKB Natural variant 265 265 . . . ID=VAR_085141;Note=In CMT2D%3B uncertain significance. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31173493;Dbxref=PMID:31173493 P41250 UniProtKB Natural variant 268 268 . . . ID=VAR_054866;Note=Found in a patient with mild left ventricular posterior wall hypertrophy%2C exercise intolerance and lactic acidosis%3B uncertain significance. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28594869;Dbxref=dbSNP:rs2230310,PMID:28594869 P41250 UniProtKB Natural variant 292 292 . . . ID=VAR_074017;Note=In CMT2D. M->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26244500;Dbxref=dbSNP:rs1064795123,PMID:26244500 P41250 UniProtKB Natural variant 294 294 . . . ID=VAR_018720;Note=In CMT2D%3B shows a large reduction in aminoacylation activity%3B does not impair transcription or translation or protein stability%3B contrary to the wild-type protein%2C strongly interacts with NRP1. G->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12690580,ECO:0000269|PubMed:17035524,ECO:0000269|PubMed:25168514,ECO:0000269|PubMed:26503042;Dbxref=dbSNP:rs137852643,PMID:12690580,PMID:17035524,PMID:25168514,PMID:26503042 P41250 UniProtKB Natural variant 298 298 . . . ID=VAR_073190;Note=In CMT2D%3B shows a large reduction in aminoacylation activity%3B demonstrates a change in subcellular location pattern%3B does not associate with granules. P->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20169446,ECO:0000269|PubMed:25168514;Dbxref=dbSNP:rs137852648,PMID:20169446,PMID:25168514 P41250 UniProtKB Natural variant 310 310 . . . ID=VAR_079827;Note=Found in a patient with growth retardation%2C microcephaly%2C thinning of the corpus callosum%2C decreased white matter and brain stem involvement%2C as well as large calvaria%2C cerebellar vermis atrophy%2C dysmorphic features%2C prominent epicanthal folds%2C hypotelorism%2C high-arched palate%2C delayed motor milestones%2C apnea and sparse thin scalp hair%3B likely pathogenic%3B reduces to less than 1%25 aminoacylation activity. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28675565;Dbxref=dbSNP:rs1135401748,PMID:28675565 P41250 UniProtKB Natural variant 334 334 . . . ID=VAR_073191;Note=In CMT2D%3B uncertain significance%3B shows a large reduction in aminoacylation activity%3B demonstrates a change in subcellular location pattern%3B does not associate with granules. I->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17101916,ECO:0000269|PubMed:24604904,ECO:0000269|PubMed:25168514;Dbxref=dbSNP:rs1554338260,PMID:17101916,PMID:24604904,PMID:25168514 P41250 UniProtKB Natural variant 334 334 . . . ID=VAR_085142;Note=In SMAJI%3B loss of function%3B based on yeast complementation assay. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32181591;Dbxref=dbSNP:rs1554338262,PMID:32181591 P41250 UniProtKB Natural variant 388 388 . . . ID=VAR_054867;Note=R->Q;Dbxref=dbSNP:rs17159287 P41250 UniProtKB Natural variant 412 412 . . . ID=VAR_079828;Note=Found in a patient with mild left ventricular posterior wall hypertrophy%2C exercise intolerance and lactic acidosis%3B uncertain significance. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28594869;Dbxref=dbSNP:rs770924455,PMID:28594869 P41250 UniProtKB Natural variant 472 472 . . . ID=VAR_073192;Note=In HMND5%3B shows a large reduction in aminoacylation activity%3B does not complement the defect of the wild-type gene in yeast. H->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17035524,ECO:0000269|PubMed:24627108,ECO:0000269|PubMed:25168514;Dbxref=dbSNP:rs1060502838,PMID:17035524,PMID:24627108,PMID:25168514 P41250 UniProtKB Natural variant 554 554 . . . ID=VAR_073193;Note=In CMT2D%3B demonstrates no change in subcellular location pattern. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25168514;Dbxref=dbSNP:rs137852647,PMID:25168514 P41250 UniProtKB Natural variant 580 580 . . . ID=VAR_018721;Note=In HMND5%3B higher dimerization stability%3B loss of activity%3B shows a large reduction in aminoacylation activity. G->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12690580,ECO:0000269|PubMed:17035524,ECO:0000269|PubMed:17545306,ECO:0000269|PubMed:25168514;Dbxref=dbSNP:rs137852646,PMID:12690580,PMID:17035524,PMID:17545306,PMID:25168514 P41250 UniProtKB Natural variant 598 598 . . . ID=VAR_079829;Note=In HMND5%3B uncertain significance. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17101916;Dbxref=dbSNP:rs766280100,PMID:17101916 P41250 UniProtKB Natural variant 635 635 . . . ID=VAR_073194;Note=Has no effect on subcellular localization%3B results in decreased affinity for glycine. S->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17101916,ECO:0000269|PubMed:17544401,ECO:0000269|PubMed:25168514;Dbxref=dbSNP:rs201358272,PMID:17101916,PMID:17544401,PMID:25168514 P41250 UniProtKB Natural variant 652 652 . . . ID=VAR_073195;Note=In CMT2D%3B shows a large reduction in aminoacylation activity%3B demonstrates a change in subcellular location pattern%3B does not associate with granules. G->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17101916,ECO:0000269|PubMed:25168514;Dbxref=dbSNP:rs747080824,PMID:17101916,PMID:25168514 P41250 UniProtKB Natural variant 652 652 . . . ID=VAR_085143;Note=In SMAJI. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32181591;Dbxref=dbSNP:rs1783251037,PMID:32181591 P41250 UniProtKB Mutagenesis 121 121 . . . Note=Decrease in catalytic activity by about 10-fold. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24898252;Dbxref=PMID:24898252 P41250 UniProtKB Mutagenesis 211 211 . . . Note=Displays 62%25 of wild-type catalytic activity. Displays 20%25 of wild-type catalytic activity%3B when associated with G-125. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26797133;Dbxref=PMID:26797133 P41250 UniProtKB Mutagenesis 337 337 . . . Note=Decrease in catalytic activity by more than 10-fold. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24898252;Dbxref=PMID:24898252 P41250 UniProtKB Mutagenesis 486 490 . . . Note=Loss of catalytic activity. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26797133;Dbxref=PMID:26797133 P41250 UniProtKB Mutagenesis 602 602 . . . Note=Decrease in catalytic activity by more than 10-fold. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24898252;Dbxref=PMID:24898252 P41250 UniProtKB Mutagenesis 658 658 . . . Note=Decrease in catalytic activity by more than 10-fold. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24898252;Dbxref=PMID:24898252 P41250 UniProtKB Mutagenesis 729 729 . . . Note=Decrease in catalytic activity by about 10-fold. Q->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24898252;Dbxref=PMID:24898252 P41250 UniProtKB Sequence conflict 9 18 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P41250 UniProtKB Sequence conflict 205 205 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P41250 UniProtKB Sequence conflict 530 530 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 P41250 UniProtKB Sequence conflict 634 634 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P41250 UniProtKB Turn 62 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E6M P41250 UniProtKB Helix 65 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E6M P41250 UniProtKB Turn 81 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E6M P41250 UniProtKB Helix 95 112 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E6M P41250 UniProtKB Helix 121 130 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 133 136 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 139 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 148 150 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 152 168 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 170 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 182 185 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 186 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 194 197 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 199 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 211 213 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 214 227 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 229 231 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2Q5I P41250 UniProtKB Helix 233 243 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Turn 244 248 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 251 260 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 266 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 276 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 283 285 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 287 296 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 298 300 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZXF P41250 UniProtKB Helix 301 305 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 308 314 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Turn 315 317 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 321 330 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 339 341 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 344 355 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 357 359 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KQE P41250 UniProtKB Helix 365 367 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Turn 368 370 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 372 376 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 378 382 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 388 391 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 392 397 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 400 402 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2PME P41250 UniProtKB Helix 404 420 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 424 426 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 427 431 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 434 436 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 442 451 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 454 462 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 467 476 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 482 484 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 501 507 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KQE P41250 UniProtKB Helix 512 519 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KQE P41250 UniProtKB Helix 524 535 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KQE P41250 UniProtKB Beta strand 541 544 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KQE P41250 UniProtKB Beta strand 547 550 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KQE P41250 UniProtKB Beta strand 552 554 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KQE P41250 UniProtKB Beta strand 562 564 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2PMF P41250 UniProtKB Turn 565 567 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2PMF P41250 UniProtKB Beta strand 568 570 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 573 580 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 581 592 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 593 595 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 597 600 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KQE P41250 UniProtKB Beta strand 603 605 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Turn 609 611 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 615 621 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Turn 625 627 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 628 640 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 645 647 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 650 652 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E6M P41250 UniProtKB Helix 654 663 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 668 672 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 674 677 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 679 681 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 683 688 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Turn 689 691 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 694 698 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Turn 699 701 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Helix 702 710 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5 P41250 UniProtKB Beta strand 712 714 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KR3 P41250 UniProtKB Helix 716 722 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZT5