##gff-version 3 Q7Z434 UniProtKB Chain 1 540 . . . ID=PRO_0000144096;Note=Mitochondrial antiviral-signaling protein Q7Z434 UniProtKB Topological domain 1 513 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q7Z434 UniProtKB Transmembrane 514 534 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z434 UniProtKB Topological domain 535 540 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q7Z434 UniProtKB Domain 10 77 . . . Note=CARD Q7Z434 UniProtKB Region 10 77 . . . Note=Required for interaction with NLRX1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18200010;Dbxref=PMID:18200010 Q7Z434 UniProtKB Region 95 297 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7Z434 UniProtKB Region 143 147 . . . Note=Interaction with TRAF2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16153868;Dbxref=PMID:16153868 Q7Z434 UniProtKB Region 153 158 . . . Note=Interaction with TRAF6 Q7Z434 UniProtKB Region 314 358 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7Z434 UniProtKB Region 373 419 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7Z434 UniProtKB Region 455 460 . . . Note=Interaction with TRAF6 Q7Z434 UniProtKB Region 476 507 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7Z434 UniProtKB Motif 439 442 . . . Note=PLxIS motif;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25636800;Dbxref=PMID:25636800 Q7Z434 UniProtKB Compositional bias 102 124 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7Z434 UniProtKB Compositional bias 145 166 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7Z434 UniProtKB Compositional bias 184 262 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7Z434 UniProtKB Compositional bias 314 350 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7Z434 UniProtKB Compositional bias 373 389 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7Z434 UniProtKB Compositional bias 400 415 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7Z434 UniProtKB Compositional bias 493 507 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7Z434 UniProtKB Site 148 149 . . . Note=(Microbial infection) Cleavage%3B by viral Seneca Valley virus protease 3C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28566380;Dbxref=PMID:28566380 Q7Z434 UniProtKB Site 148 148 . . . Note=(Microbial infection) Cleavage by CV3B;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21436888;Dbxref=PMID:21436888 Q7Z434 UniProtKB Site 208 209 . . . Note=(Microbial infection) Cleavage by protease 2A of enterovirus 71;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28253362;Dbxref=PMID:28253362 Q7Z434 UniProtKB Site 250 251 . . . Note=(Microbial infection) Cleavage by protease 2A of enterovirus 71;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28253362;Dbxref=PMID:28253362 Q7Z434 UniProtKB Site 264 265 . . . Note=(Microbial infection) Cleavage by protease 2A of enterovirus 71;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28253362;Dbxref=PMID:28253362 Q7Z434 UniProtKB Site 427 428 . . . Note=(Microbial infection) Cleavage%3B by HAV protein 3ABC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17438296;Dbxref=PMID:17438296 Q7Z434 UniProtKB Site 429 430 . . . Note=Cleavage%3B by CASP3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30878284;Dbxref=PMID:30878284 Q7Z434 UniProtKB Site 490 491 . . . Note=Cleavage%3B by CASP3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30878284;Dbxref=PMID:30878284 Q7Z434 UniProtKB Site 508 509 . . . Note=(Microbial infection) Cleavage%3B by HCV and hepatitis GB virus B NS3/4A protease complex;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16177806,ECO:0000269|PubMed:16301520;Dbxref=PMID:16177806,PMID:16301520 Q7Z434 UniProtKB Modified residue 152 152 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:24275569;Dbxref=PMID:18669648,PMID:19690332,PMID:24275569 Q7Z434 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q7Z434 UniProtKB Modified residue 165 165 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:24275569;Dbxref=PMID:18669648,PMID:19690332,PMID:24275569 Q7Z434 UniProtKB Modified residue 180 180 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q7Z434 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q7Z434 UniProtKB Modified residue 215 215 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q7Z434 UniProtKB Modified residue 222 222 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:16964243,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:16964243,PMID:18669648,PMID:23186163,PMID:24275569 Q7Z434 UniProtKB Modified residue 233 233 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q7Z434 UniProtKB Modified residue 234 234 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q7Z434 UniProtKB Modified residue 236 236 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8VCF0 Q7Z434 UniProtKB Modified residue 253 253 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 Q7Z434 UniProtKB Modified residue 258 258 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:20068231 Q7Z434 UniProtKB Modified residue 408 408 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8VCF0 Q7Z434 UniProtKB Modified residue 442 442 . . . Note=Phosphoserine%3B by TBK1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25636800,ECO:0000269|PubMed:27302953;Dbxref=PMID:25636800,PMID:27302953 Q7Z434 UniProtKB Cross-link 10 10 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27992402;Dbxref=PMID:27992402 Q7Z434 UniProtKB Cross-link 311 311 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27992402;Dbxref=PMID:27992402 Q7Z434 UniProtKB Cross-link 325 325 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29743353;Dbxref=PMID:29743353 Q7Z434 UniProtKB Cross-link 461 461 . . . Note=(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37311461;Dbxref=PMID:37311461 Q7Z434 UniProtKB Cross-link 461 461 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27992402;Dbxref=PMID:27992402 Q7Z434 UniProtKB Alternative sequence 1 141 . . . ID=VSP_045872;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q7Z434 UniProtKB Alternative sequence 40 131 . . . ID=VSP_047816;Note=In isoform 6. DRLRATCTLSGNRDTLWHLFNTLQRRPGWVEYFIAALRGCELVDLADEVASVYQSYQPRTSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYN->GPRTVPQTHWSHRHFLLRGQGPPHLLRPTASPTTAAERRSQVTPCLSRRPRRQSPQERIQSKPCRRSAPEPSQGIQMVAPWSPPLTWQPSAL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:18207245;Dbxref=PMID:18207245 Q7Z434 UniProtKB Alternative sequence 64 148 . . . ID=VSP_010261;Note=In isoform 3. RRPGWVEYFIAALRGCELVDLADEVASVYQSYQPRTSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYNSCREKEPSYPMPVQETQ->LPTWAGEETPGGQSSGRGLDFSSLTSGAVWLWQMSDFWSCFSTWTVSIWLILHWVLLRLNLQVFAKCLAQSKWPLLLPSLSCPTW;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q7Z434 UniProtKB Alternative sequence 98 124 . . . ID=VSP_047817;Note=In isoform 5. RTSDRPPDPLEPPSLPAERPGPPTPAA->QFRASPADAQPQSHPKESRWWPPGVLL;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:18207245;Dbxref=PMID:14702039,PMID:18207245 Q7Z434 UniProtKB Alternative sequence 99 131 . . . ID=VSP_010262;Note=In isoform 2. TSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYN->ERPALALLDPQPAPWPPLSFSLSLYFLPFSVILFLVTVKR;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q7Z434 UniProtKB Alternative sequence 125 540 . . . ID=VSP_047818;Note=In isoform 5. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:18207245;Dbxref=PMID:14702039,PMID:18207245 Q7Z434 UniProtKB Alternative sequence 132 540 . . . ID=VSP_010263;Note=In isoform 2 and isoform 6. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:18207245;Dbxref=PMID:14702039,PMID:18207245 Q7Z434 UniProtKB Alternative sequence 149 540 . . . ID=VSP_010264;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q7Z434 UniProtKB Natural variant 79 79 . . . ID=VAR_048609;Note=C->F;Dbxref=dbSNP:rs11905552 Q7Z434 UniProtKB Natural variant 79 79 . . . ID=VAR_059197;Note=C->S;Dbxref=dbSNP:rs11908032 Q7Z434 UniProtKB Natural variant 93 93 . . . ID=VAR_048610;Note=Q->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:16127453,ECO:0000269|PubMed:16153868;Dbxref=dbSNP:rs17857295,PMID:14702039,PMID:15489334,PMID:16127453,PMID:16153868 Q7Z434 UniProtKB Natural variant 198 198 . . . ID=VAR_048611;Note=Q->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:16125763,ECO:0000269|PubMed:16177806;Dbxref=dbSNP:rs7262903,PMID:15489334,PMID:16125763,PMID:16177806 Q7Z434 UniProtKB Natural variant 409 409 . . . ID=VAR_018448;Note=S->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:16125763,ECO:0000269|PubMed:16177806;Dbxref=dbSNP:rs7269320,PMID:15489334,PMID:16125763,PMID:16177806 Q7Z434 UniProtKB Mutagenesis 10 10 . . . Note=Abolished ubiquitination by TRIM31%3B when associated with R-311 and R-461. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23582325;Dbxref=PMID:23582325 Q7Z434 UniProtKB Mutagenesis 26 26 . . . Note=Impairs filament formation and abolishes antiviral signaling activity. E->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24569476;Dbxref=PMID:24569476 Q7Z434 UniProtKB Mutagenesis 54 54 . . . Note=Impairs ability to induce IFN-beta. Loss of interaction with the ATG5-ATG12 conjugate. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16125763,ECO:0000269|PubMed:17709747;Dbxref=PMID:16125763,PMID:17709747 Q7Z434 UniProtKB Mutagenesis 56 56 . . . Note=Impairs filament formation and abolishes antiviral signaling activity. W->A%2CE%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24569476;Dbxref=PMID:24569476 Q7Z434 UniProtKB Mutagenesis 67 69 . . . Note=Impairs ability to induce IFN-beta. GWV->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16125763;Dbxref=PMID:16125763 Q7Z434 UniProtKB Mutagenesis 145 145 . . . Note=No interaction with TRAF2. Q->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16153868;Dbxref=PMID:16153868 Q7Z434 UniProtKB Mutagenesis 148 148 . . . Note=Complete loss of cleavage by Seneca Valley virus protease 3C. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28566380;Dbxref=PMID:28566380 Q7Z434 UniProtKB Mutagenesis 155 155 . . . Note=No interaction with TRAF6%3B when associated with D-457. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16153868;Dbxref=PMID:16153868 Q7Z434 UniProtKB Mutagenesis 159 159 . . . Note=No effect on cleavage by Seneca Valley virus protease 3C. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28566380;Dbxref=PMID:28566380 Q7Z434 UniProtKB Mutagenesis 162 162 . . . Note=No effect on cleavage by Seneca Valley virus protease 3C. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28566380;Dbxref=PMID:28566380 Q7Z434 UniProtKB Mutagenesis 196 196 . . . Note=No effect on cleavage by Seneca Valley virus protease 3C. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28566380;Dbxref=PMID:28566380 Q7Z434 UniProtKB Mutagenesis 198 198 . . . Note=No effect on cleavage by Seneca Valley virus protease 3C. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28566380;Dbxref=PMID:28566380 Q7Z434 UniProtKB Mutagenesis 209 209 . . . Note=Complete loss of cleavage by protease 2A of enterovirus 71. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28253362;Dbxref=PMID:28253362 Q7Z434 UniProtKB Mutagenesis 251 251 . . . Note=Complete loss of cleavage by protease 2A of enterovirus 71. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28253362;Dbxref=PMID:28253362 Q7Z434 UniProtKB Mutagenesis 265 265 . . . Note=Complete loss of cleavage by enterovirus 71. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28253362;Dbxref=PMID:28253362 Q7Z434 UniProtKB Mutagenesis 311 311 . . . Note=Abolished ubiquitination by TRIM31%3B when associated with R-10 and R-461. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23582325;Dbxref=PMID:23582325 Q7Z434 UniProtKB Mutagenesis 325 325 . . . Note=Abolished ubiquitination by TRIM21. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29743353;Dbxref=PMID:29743353 Q7Z434 UniProtKB Mutagenesis 427 427 . . . Note=No cleavage by HHAV 3ABC. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17438296;Dbxref=PMID:17438296 Q7Z434 UniProtKB Mutagenesis 429 429 . . . Note=Decreased cleavage by CASP3. Abolished cleavage by CASP3%3B when associated with A-490. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30878284;Dbxref=PMID:30878284 Q7Z434 UniProtKB Mutagenesis 435 435 . . . Note=No effect on cleavage by NS3/4A protease complex. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16301520;Dbxref=PMID:16301520 Q7Z434 UniProtKB Mutagenesis 442 442 . . . Note=Abolished ability to bind and activate IRF3. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25636800,ECO:0000269|PubMed:27302953;Dbxref=PMID:25636800,PMID:27302953 Q7Z434 UniProtKB Mutagenesis 452 452 . . . Note=No effect on cleavage by NS3/4A protease complex. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16301520;Dbxref=PMID:16301520 Q7Z434 UniProtKB Mutagenesis 457 457 . . . Note=No interaction with TRAF6%3B when associated with D-155. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16153868;Dbxref=PMID:16153868 Q7Z434 UniProtKB Mutagenesis 461 461 . . . Note=Abolished ubiquitination by TRIM31%3B when associated with R-10 and R-311. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23582325;Dbxref=PMID:23582325 Q7Z434 UniProtKB Mutagenesis 461 461 . . . Note=Abolished UFMylation by UFM1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37311461;Dbxref=PMID:37311461 Q7Z434 UniProtKB Mutagenesis 463 463 . . . Note=No effect on cleavage by HHAV 3ABC. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17438296;Dbxref=PMID:17438296 Q7Z434 UniProtKB Mutagenesis 490 490 . . . Note=Decreased cleavage by CASP3. Abolished cleavage by CASP3%3B when associated with A-429. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30878284;Dbxref=PMID:30878284 Q7Z434 UniProtKB Mutagenesis 508 508 . . . Note=No cleavage by HCV and hepatitis GB virus BNS3/4A protease complex. C->A%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16177806,ECO:0000269|PubMed:16301520,ECO:0000269|PubMed:17093192;Dbxref=PMID:16177806,PMID:16301520,PMID:17093192 Q7Z434 UniProtKB Sequence conflict 42 42 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q7Z434 UniProtKB Sequence conflict 191 191 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q7Z434 UniProtKB Sequence conflict 356 356 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q7Z434 UniProtKB Sequence conflict 373 373 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q7Z434 UniProtKB Helix 3 14 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VGQ Q7Z434 UniProtKB Helix 16 19 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VGQ Q7Z434 UniProtKB Helix 24 27 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VGQ Q7Z434 UniProtKB Helix 28 30 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VGQ Q7Z434 UniProtKB Helix 36 49 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VGQ Q7Z434 UniProtKB Helix 51 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VGQ Q7Z434 UniProtKB Helix 68 78 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VGQ Q7Z434 UniProtKB Helix 82 92 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VGQ Q7Z434 UniProtKB Beta strand 95 97 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2MS8 Q7Z434 UniProtKB Beta strand 456 459 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4Z8M Q7Z434 UniProtKB Beta strand 504 507 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3RC5