##gff-version 3 O43353 UniProtKB Chain 1 540 . . . ID=PRO_0000086608;Note=Receptor-interacting serine/threonine-protein kinase 2 O43353 UniProtKB Domain 18 294 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O43353 UniProtKB Domain 432 524 . . . Note=CARD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00046 O43353 UniProtKB Region 65 73 . . . Note=Helix alphaC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28545134;Dbxref=PMID:28545134 O43353 UniProtKB Region 167 193 . . . Note=Activation segment (AS);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28545134;Dbxref=PMID:28545134 O43353 UniProtKB Region 338 369 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O43353 UniProtKB Compositional bias 338 368 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O43353 UniProtKB Active site 146 146 . . . Note=Proton acceptor;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9705938;Dbxref=PMID:9705938 O43353 UniProtKB Binding site 24 32 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O43353 UniProtKB Binding site 47 47 . . . . O43353 UniProtKB Modified residue 149 149 . . . Note=(Microbial infection) O-acetylthreonine%3B by Yersinia YopJ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22520462;Dbxref=PMID:22520462 O43353 UniProtKB Modified residue 168 168 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19369195;Dbxref=PMID:19369195 O43353 UniProtKB Modified residue 174 174 . . . Note=(Microbial infection) O-acetylserine%3B by Yersinia YopJ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22520462;Dbxref=PMID:22520462 O43353 UniProtKB Modified residue 174 174 . . . Note=Phosphoserine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28545134;Dbxref=PMID:28545134 O43353 UniProtKB Modified residue 176 176 . . . Note=(Microbial infection) O-acetylserine%3B by Yersinia YopJ%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22520462;Dbxref=PMID:22520462 O43353 UniProtKB Modified residue 176 176 . . . Note=Phosphoserine%3B by autocatalysis and LRRK2%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16824733,ECO:0000269|PubMed:27830463,ECO:0000269|PubMed:28545134;Dbxref=PMID:16824733,PMID:27830463,PMID:28545134 O43353 UniProtKB Modified residue 178 178 . . . Note=(Microbial infection) O-acetylserine%3B by Yersinia YopJ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22520462;Dbxref=PMID:22520462 O43353 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28545134;Dbxref=PMID:28545134 O43353 UniProtKB Modified residue 180 180 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28545134;Dbxref=PMID:28545134 O43353 UniProtKB Modified residue 181 181 . . . Note=(Microbial infection) O-acetylserine%3B by Yersinia YopJ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22520462;Dbxref=PMID:22520462 O43353 UniProtKB Modified residue 181 181 . . . Note=Phosphoserine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28545134;Dbxref=PMID:28545134 O43353 UniProtKB Modified residue 183 183 . . . Note=(Microbial infection) O-acetylserine%3B by Yersinia YopJ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22520462;Dbxref=PMID:22520462 O43353 UniProtKB Modified residue 189 189 . . . Note=(Microbial infection) O-acetylthreonine%3B by Yersinia YopJ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22520462;Dbxref=PMID:22520462 O43353 UniProtKB Modified residue 363 363 . . . Note=(Microbial infection) O-acetylserine%3B by Yersinia YopJ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22520462;Dbxref=PMID:22520462 O43353 UniProtKB Modified residue 363 363 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18691976,ECO:0007744|PubMed:19369195,ECO:0007744|PubMed:23186163;Dbxref=PMID:18691976,PMID:19369195,PMID:23186163 O43353 UniProtKB Modified residue 381 381 . . . Note=Phosphotyrosine%3B by CSK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887730;Dbxref=PMID:21887730 O43353 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19369195;Dbxref=PMID:19369195 O43353 UniProtKB Modified residue 397 397 . . . Note=(Microbial infection) O-acetylthreonine%3B by Yersinia YopJ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22520462;Dbxref=PMID:22520462 O43353 UniProtKB Modified residue 423 423 . . . Note=(Microbial infection) O-acetylserine%3B by Yersinia YopJ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22520462;Dbxref=PMID:22520462 O43353 UniProtKB Modified residue 474 474 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21123652;Dbxref=PMID:21123652 O43353 UniProtKB Modified residue 527 527 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18691976,ECO:0007744|PubMed:19369195,ECO:0007744|PubMed:23186163;Dbxref=PMID:18691976,PMID:19369195,PMID:23186163 O43353 UniProtKB Modified residue 529 529 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163 O43353 UniProtKB Modified residue 531 531 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 O43353 UniProtKB Modified residue 539 539 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18691976,ECO:0007744|PubMed:19369195;Dbxref=PMID:18691976,PMID:19369195 O43353 UniProtKB Cross-link 209 209 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18079694;Dbxref=PMID:18079694 O43353 UniProtKB Cross-link 410 410 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29452636;Dbxref=PMID:29452636 O43353 UniProtKB Cross-link 503 503 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28656966;Dbxref=PMID:28656966 O43353 UniProtKB Cross-link 538 538 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29452636;Dbxref=PMID:29452636 O43353 UniProtKB Alternative sequence 1 137 . . . ID=VSP_013266;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:12975309,ECO:0000303|PubMed:14702039;Dbxref=PMID:12975309,PMID:14702039 O43353 UniProtKB Natural variant 259 259 . . . ID=VAR_041045;Note=I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs2230801,PMID:17344846 O43353 UniProtKB Natural variant 268 268 . . . ID=VAR_041046;Note=L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs35004667,PMID:17344846 O43353 UniProtKB Natural variant 313 313 . . . ID=VAR_041047;Note=K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs35395048,PMID:17344846 O43353 UniProtKB Mutagenesis 47 47 . . . Note=Abolishes protein-kinase activity without preventing ability to activate NF-kappa-B downstream of NOD2. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28545134,ECO:0000269|PubMed:29452636,ECO:0000269|PubMed:30026309,ECO:0000269|PubMed:9575181,ECO:0000269|PubMed:9642260;Dbxref=PMID:28545134,PMID:29452636,PMID:30026309,PMID:9575181,PMID:9642260 O43353 UniProtKB Mutagenesis 47 47 . . . Note=Abolishes protein-kinase activity. Reduces FAS-mediated apoptosis. K->M;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27830463,ECO:0000269|PubMed:9575181,ECO:0000269|PubMed:9642260;Dbxref=PMID:27830463,PMID:9575181,PMID:9642260 O43353 UniProtKB Mutagenesis 95 95 . . . Note=Abolished ability to activate NF-kappa-B downstream of NOD2. T->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30026309;Dbxref=PMID:30026309 O43353 UniProtKB Mutagenesis 146 146 . . . Note=Abolishes protein-kinase activity without preventing ability to activate NF-kappa-B downstream of NOD2. D->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28545134,ECO:0000269|PubMed:29452636,ECO:0000269|PubMed:30026309,ECO:0000269|PubMed:9705938;Dbxref=PMID:28545134,PMID:29452636,PMID:30026309,PMID:9705938 O43353 UniProtKB Mutagenesis 176 176 . . . Note=Decreased phosphorylation and activation. Abolished phosphorylation by LRRK2. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27830463;Dbxref=PMID:27830463 O43353 UniProtKB Mutagenesis 209 209 . . . Note=Decreased polyubiquitination. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18079694;Dbxref=PMID:18079694 O43353 UniProtKB Mutagenesis 381 381 . . . Note=Prevents phosphorylation. Reduces serine and threonine phosphorylation of ARHGEF2. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887730;Dbxref=PMID:21887730 O43353 UniProtKB Mutagenesis 410 410 . . . Note=Reduced ubiquitination by XIAP and activation of NF-kappa-B%3B when associated with R-538. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29452636;Dbxref=PMID:29452636 O43353 UniProtKB Mutagenesis 437 437 . . . Note=Decreased interaction with NGFR. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26646181;Dbxref=PMID:26646181 O43353 UniProtKB Mutagenesis 444 444 . . . Note=Abolishes interaction with NOD1. Abolished activation of NF-kappa-B. R->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17054981,ECO:0000269|PubMed:30478312;Dbxref=PMID:17054981,PMID:30478312 O43353 UniProtKB Mutagenesis 445 445 . . . Note=Strongly decreased activation of NF-kappa-B. Does not affect activation of NF-kappa-B%3B when associated with E-458. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Mutagenesis 449 449 . . . Note=Strongly decreased activation of NF-kappa-B. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Mutagenesis 450 450 . . . Note=Increased activation of NF-kappa-B. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30279485;Dbxref=PMID:30279485 O43353 UniProtKB Mutagenesis 452 452 . . . Note=Impaired interaction with NOD2 and decreased homooligomerization and ability to transmit NOD2 signaling. T->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30279485;Dbxref=PMID:30279485 O43353 UniProtKB Mutagenesis 453 453 . . . Note=Decreased homooligomerization and ability to transmit NOD2 signaling. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30279485;Dbxref=PMID:30279485 O43353 UniProtKB Mutagenesis 455 455 . . . Note=Decreased homooligomerization and ability to transmit NOD2 signaling. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30279485;Dbxref=PMID:30279485 O43353 UniProtKB Mutagenesis 458 458 . . . Note=Strongly decreased activation of NF-kappa-B. Does not affect activation of NF-kappa-B%3B when associated with R-445. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Mutagenesis 461 461 . . . Note=Abolished activation of NF-kappa-B. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Mutagenesis 467 467 . . . Note=Decreased interaction with NGFR. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26646181;Dbxref=PMID:26646181 O43353 UniProtKB Mutagenesis 470 470 . . . Note=Decreased homooligomerization and ability to transmit NOD2 signaling. M->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30279485;Dbxref=PMID:30279485 O43353 UniProtKB Mutagenesis 471 471 . . . Note=Abolished activation of NF-kappa-B. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Mutagenesis 471 471 . . . Note=Decreased interaction with NGFR. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26646181;Dbxref=PMID:26646181 O43353 UniProtKB Mutagenesis 472 472 . . . Note=Abolished activation of NF-kappa-B. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Mutagenesis 474 474 . . . Note=Decreases interaction with NOD2. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21123652;Dbxref=PMID:21123652 O43353 UniProtKB Mutagenesis 474 474 . . . Note=Abolished activation of NF-kappa-B. Y->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Mutagenesis 475 475 . . . Note=Abolished activation of NF-kappa-B. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Mutagenesis 483 483 . . . Note=Abolished activation of NF-kappa-B. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Mutagenesis 483 483 . . . Note=Abolishes interaction with NOD1. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17054981;Dbxref=PMID:17054981 O43353 UniProtKB Mutagenesis 488 488 . . . Note=Abolishes interaction with NOD1. Abolished activation of NF-kappa-B. R->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17054981,ECO:0000269|PubMed:30478312;Dbxref=PMID:17054981,PMID:30478312 O43353 UniProtKB Mutagenesis 492 492 . . . Note=Abolished activation of NF-kappa-B. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Mutagenesis 496 496 . . . Note=Decreased interaction with NGFR. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26646181;Dbxref=PMID:26646181 O43353 UniProtKB Mutagenesis 497 497 . . . Note=Increased activation of NF-kappa-B. Q->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30279485;Dbxref=PMID:30279485 O43353 UniProtKB Mutagenesis 497 497 . . . Note=Strongly decreased activation of NF-kappa-B. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Mutagenesis 500 500 . . . Note=Decreased interaction with NGFR. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26646181;Dbxref=PMID:26646181 O43353 UniProtKB Mutagenesis 503 503 . . . Note=Abolished ubiquitination by ZNRF4. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28656966;Dbxref=PMID:28656966 O43353 UniProtKB Mutagenesis 513 513 . . . Note=Reduced formation of filaments and activation of NF-kappa-B. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Mutagenesis 528 528 . . . Note=Decreased interaction with NGFR. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26646181;Dbxref=PMID:26646181 O43353 UniProtKB Mutagenesis 538 538 . . . Note=Reduced ubiquitination by XIAP and activation of NF-kappa-B%3B when associated with R-410. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30478312;Dbxref=PMID:30478312 O43353 UniProtKB Sequence conflict 271 271 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 O43353 UniProtKB Sequence conflict 514 514 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 O43353 UniProtKB Beta strand 7 9 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Beta strand 18 26 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Beta strand 31 37 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Turn 38 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Beta strand 43 48 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Helix 57 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Beta strand 81 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Beta strand 90 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Helix 103 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Turn 110 112 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Helix 118 136 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Beta strand 138 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Helix 149 151 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Beta strand 152 154 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Beta strand 160 162 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Helix 168 176 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG3 O43353 UniProtKB Turn 189 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ES0 O43353 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Helix 202 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ES0 O43353 UniProtKB Helix 210 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Turn 228 231 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Helix 235 243 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Turn 252 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Helix 262 272 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Helix 277 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Helix 283 295 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NG0 O43353 UniProtKB Helix 300 312 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ES0 O43353 UniProtKB Turn 313 315 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ES0 O43353 UniProtKB Helix 435 442 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GFJ O43353 UniProtKB Helix 444 450 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GFJ O43353 UniProtKB Helix 453 465 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GFJ O43353 UniProtKB Helix 471 478 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GFJ O43353 UniProtKB Beta strand 480 482 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GFJ O43353 UniProtKB Helix 483 497 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GFJ O43353 UniProtKB Helix 499 511 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GFJ O43353 UniProtKB Beta strand 526 528 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2N7Z O43353 UniProtKB Turn 530 532 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2N83