##gff-version 3 Q66478 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Chain 2 2193 . . . ID=PRO_0000426136;Note=Genome polyprotein Q66478 UniProtKB Chain 2 862 . . . ID=PRO_0000426137;Note=P1 Q66478 UniProtKB Chain 2 323 . . . ID=PRO_0000426138;Note=Capsid protein VP0 Q66478 UniProtKB Chain 2 69 . . . ID=PRO_0000426139;Note=Capsid protein VP4 Q66478 UniProtKB Chain 70 323 . . . ID=PRO_0000426140;Note=Capsid protein VP2 Q66478 UniProtKB Chain 324 565 . . . ID=PRO_0000426141;Note=Capsid protein VP3 Q66478 UniProtKB Chain 566 862 . . . ID=PRO_0000426142;Note=Capsid protein VP1 Q66478 UniProtKB Chain 863 1440 . . . ID=PRO_0000426143;Note=P2 Q66478 UniProtKB Chain 863 1012 . . . ID=PRO_0000039485;Note=Protease 2A Q66478 UniProtKB Chain 1013 1111 . . . ID=PRO_0000039486;Note=Protein 2B Q66478 UniProtKB Chain 1112 1440 . . . ID=PRO_0000039487;Note=Protein 2C Q66478 UniProtKB Chain 1441 2193 . . . ID=PRO_0000426144;Note=P3 Q66478 UniProtKB Chain 1441 1548 . . . ID=PRO_0000426145;Note=Protein 3AB Q66478 UniProtKB Chain 1441 1526 . . . ID=PRO_0000039488;Note=Protein 3A Q66478 UniProtKB Chain 1527 1548 . . . ID=PRO_0000426146;Note=Viral protein genome-linked Q66478 UniProtKB Chain 1549 2193 . . . ID=PRO_0000426147;Note=Protein 3CD Q66478 UniProtKB Chain 1549 1731 . . . ID=PRO_0000426148;Note=Protease 3C Q66478 UniProtKB Chain 1732 2193 . . . ID=PRO_0000426149;Note=RNA-directed RNA polymerase Q66478 UniProtKB Topological domain 2 1503 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q66478 UniProtKB Intramembrane 1504 1519 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q66478 UniProtKB Topological domain 1520 2193 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q66478 UniProtKB Domain 1216 1374 . . . Note=SF3 helicase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00551 Q66478 UniProtKB Domain 1549 1727 . . . Note=Peptidase C3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01222 Q66478 UniProtKB Domain 1958 2073 . . . Note=RdRp catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00539 Q66478 UniProtKB Zinc finger 1381 1397 . . . Note=C4-type%3B degenerate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B9VUU3 Q66478 UniProtKB Region 1 22 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q66478 UniProtKB Region 566 588 . . . Note=Amphipathic alpha-helix;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q66478 UniProtKB Region 568 588 . . . Note=Amphipathic alpha-helix;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q66478 UniProtKB Region 1112 1250 . . . Note=Oligomerization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Region 1112 1184 . . . Note=Membrane-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Region 1133 1137 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Region 1424 1431 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Region 1435 1440 . . . Note=Oligomerization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Active site 883 883 . . . Note=For protease 2A activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Active site 901 901 . . . Note=For protease 2A activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Active site 972 972 . . . Note=For protease 2A activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Active site 1588 1588 . . . Note=For protease 3C activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01222 Q66478 UniProtKB Active site 1619 1619 . . . Note=For protease 3C activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01222 Q66478 UniProtKB Active site 1695 1695 . . . Note=For protease 3C activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01222 Q66478 UniProtKB Binding site 918 918 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9QF31 Q66478 UniProtKB Binding site 920 920 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9QF31 Q66478 UniProtKB Binding site 978 978 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9QF31 Q66478 UniProtKB Binding site 980 980 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9QF31 Q66478 UniProtKB Binding site 1240 1247 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00551 Q66478 UniProtKB Binding site 1381 1381 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B9VUU3 Q66478 UniProtKB Binding site 1392 1392 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B9VUU3 Q66478 UniProtKB Binding site 1397 1397 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B9VUU3 Q66478 UniProtKB Binding site 1964 1964 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Binding site 1964 1964 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Binding site 2060 2060 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Binding site 2060 2060 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Site 25 25 . . . Note=Involved in the interaction with host RTN3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17182608;Dbxref=PMID:17182608 Q66478 UniProtKB Site 69 70 . . . Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31195113;Dbxref=PMID:31195113 Q66478 UniProtKB Site 323 324 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03301 Q66478 UniProtKB Site 862 863 . . . Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03301 Q66478 UniProtKB Site 1012 1013 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03301 Q66478 UniProtKB Site 1111 1112 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03301 Q66478 UniProtKB Site 1136 1136 . . . Note=Involved in the interaction with host RTN3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17182608;Dbxref=PMID:17182608 Q66478 UniProtKB Site 1440 1441 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03301 Q66478 UniProtKB Site 1526 1527 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03301 Q66478 UniProtKB Site 1548 1549 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03301 Q66478 UniProtKB Site 1731 1732 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03301 Q66478 UniProtKB Modified residue 1529 1529 . . . Note=O-(5'-phospho-RNA)-tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66478 UniProtKB Mutagenesis 69 70 . . . Note=Lethal. KS->FK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31195113;Dbxref=PMID:31195113 Q66478 UniProtKB Mutagenesis 69 70 . . . Note=Lethal. KS->TP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31195113;Dbxref=PMID:31195113 Q66478 UniProtKB Mutagenesis 69 69 . . . Note=No effect on VP0 cleavage and viral infectivity. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31195113;Dbxref=PMID:31195113 Q66478 UniProtKB Mutagenesis 69 69 . . . Note=No effect on VP0 cleavage and viral infectivity. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31195113;Dbxref=PMID:31195113 Q66478 UniProtKB Mutagenesis 70 70 . . . Note=Lethal. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31195113;Dbxref=PMID:31195113 Q66478 UniProtKB Mutagenesis 70 70 . . . Note=Lethal. S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31195113;Dbxref=PMID:31195113 Q66478 UniProtKB Mutagenesis 972 972 . . . Note=Complete loss of cleavage of host MAVS. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28253362;Dbxref=PMID:28253362 Q66478 UniProtKB Mutagenesis 1121 1121 . . . Note=No effect on the interaction with RTN3%3B when associated with V-1130. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17182608;Dbxref=PMID:17182608 Q66478 UniProtKB Mutagenesis 1127 1127 . . . Note=No effect on the interaction with RTN3%3B when associated with T-1135. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17182608;Dbxref=PMID:17182608 Q66478 UniProtKB Mutagenesis 1130 1130 . . . Note=No effect on the interaction with RTN3%3B when associated with E-1121. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17182608;Dbxref=PMID:17182608 Q66478 UniProtKB Mutagenesis 1135 1135 . . . Note=No effect on the interaction with RTN3%3B when associated with T-1127. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17182608;Dbxref=PMID:17182608 Q66478 UniProtKB Mutagenesis 1136 1136 . . . Note=Loss of interaction with RTN3 and reduced viral cytopathicity. I->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17182608;Dbxref=PMID:17182608 Q66478 UniProtKB Mutagenesis 1588 1588 . . . Note=Complete loss of RIGI inhibition. Complete loss of cleavage of host GSDMD and IRF7. H->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20519382,ECO:0000269|PubMed:28679757;Dbxref=PMID:20519382,PMID:28679757 Q66478 UniProtKB Mutagenesis 1632 1632 . . . Note=No effect on the ability to mediate RIGI inhibition. No effect on the ability to cleave host GSDMD and IRF7. R->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20519382,ECO:0000269|PubMed:28679757;Dbxref=PMID:20519382,PMID:28679757 Q66478 UniProtKB Mutagenesis 1695 1695 . . . Note=Complete loss of the ability to cleave host GSDMD and PINX1. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27847364,ECO:0000269|PubMed:28679757;Dbxref=PMID:27847364,PMID:28679757 Q66478 UniProtKB Mutagenesis 1702 1702 . . . Note=No effect on the ability to cleave host PML. V->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34930370;Dbxref=PMID:34930370 Q66478 UniProtKB Mutagenesis 1702 1702 . . . Note=No effect on the ability to mediate RIGI inhibition. No effect on the ability to cleave host GSDMD and IRF7. V->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20519382,ECO:0000269|PubMed:28679757;Dbxref=PMID:20519382,PMID:28679757 Q66478 UniProtKB Mutagenesis 1989 1989 . . . Note=Loss of host PPP1R15A translation activation. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34985336;Dbxref=PMID:34985336