##gff-version 3 Q99IB8 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26664 Q99IB8 UniProtKB Chain 2 3033 . . . ID=PRO_0000450856;Note=Genome polyprotein Q99IB8 UniProtKB Chain 2 191 . . . ID=PRO_0000045592;Note=Core protein precursor Q99IB8 UniProtKB Chain 2 177 . . . ID=PRO_0000045593;Note=Mature core protein Q99IB8 UniProtKB Propeptide 178 191 . . . ID=PRO_0000045594;Note=ER anchor for the core protein%2C removed in mature form by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Chain 192 383 . . . ID=PRO_0000045595;Note=Envelope glycoprotein E1 Q99IB8 UniProtKB Chain 384 750 . . . ID=PRO_0000045596;Note=Envelope glycoprotein E2 Q99IB8 UniProtKB Chain 751 813 . . . ID=PRO_0000045597;Note=Viroporin p7 Q99IB8 UniProtKB Chain 814 1030 . . . ID=PRO_0000045598;Note=Protease NS2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 Q99IB8 UniProtKB Chain 1031 1661 . . . ID=PRO_0000045599;Note=Serine protease/helicase NS3 Q99IB8 UniProtKB Chain 1662 1715 . . . ID=PRO_0000045600;Note=Non-structural protein 4A Q99IB8 UniProtKB Chain 1716 1976 . . . ID=PRO_0000045601;Note=Non-structural protein 4B Q99IB8 UniProtKB Chain 1977 2442 . . . ID=PRO_0000045602;Note=Non-structural protein 5A Q99IB8 UniProtKB Chain 2443 3033 . . . ID=PRO_0000045603;Note=RNA-directed RNA polymerase Q99IB8 UniProtKB Topological domain 2 168 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Transmembrane 169 189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Topological domain 190 358 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Transmembrane 359 379 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Topological domain 380 729 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Transmembrane 730 750 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Topological domain 751 761 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29253880;Dbxref=PMID:29253880 Q99IB8 UniProtKB Transmembrane 762 782 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Topological domain 783 785 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Transmembrane 786 807 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Topological domain 808 817 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Transmembrane 818 838 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 Q99IB8 UniProtKB Topological domain 839 842 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 Q99IB8 UniProtKB Transmembrane 843 863 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 Q99IB8 UniProtKB Topological domain 864 885 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 Q99IB8 UniProtKB Transmembrane 886 906 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 Q99IB8 UniProtKB Topological domain 907 1661 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 Q99IB8 UniProtKB Transmembrane 1662 1682 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Topological domain 1683 1809 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Transmembrane 1810 1830 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Topological domain 1831 1832 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Transmembrane 1833 1853 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Topological domain 1854 1854 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Transmembrane 1855 1875 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Topological domain 1876 1885 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Transmembrane 1886 1906 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Topological domain 1907 1976 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Intramembrane 1977 2007 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Topological domain 2008 3012 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Transmembrane 3013 3033 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Domain 907 1030 . . . Note=Peptidase C18;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 Q99IB8 UniProtKB Domain 1031 1212 . . . Note=Peptidase S29;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 Q99IB8 UniProtKB Domain 1221 1373 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 Q99IB8 UniProtKB Domain 2656 2774 . . . Note=RdRp catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00539 Q99IB8 UniProtKB Region 2 75 . . . Note=Disordered;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Region 2 59 . . . Note=Interaction with DDX3X;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5EG65 Q99IB8 UniProtKB Region 2 58 . . . Note=Interaction with EIF2AK2/PKR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 Q99IB8 UniProtKB Region 2 23 . . . Note=Interaction with STAT1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 Q99IB8 UniProtKB Region 112 152 . . . Note=Important for endoplasmic reticulum and mitochondrial localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 Q99IB8 UniProtKB Region 122 173 . . . Note=Interaction with APOA2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29846 Q99IB8 UniProtKB Region 164 167 . . . Note=Important for lipid droplets localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Region 265 296 . . . Note=Important for fusion;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Region 385 411 . . . Note=HVR1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Region 484 496 . . . Note=CD81-binding 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 Q99IB8 UniProtKB Region 524 555 . . . Note=CD81-binding 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 Q99IB8 UniProtKB Region 664 675 . . . Note=EIF2AK2/eIF2-alpha phosphorylation homology domain (PePHD) Q99IB8 UniProtKB Region 908 1210 . . . Note=Protease NS2-3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 Q99IB8 UniProtKB Region 933 953 . . . Note=Interaction with human SCPS1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24009510;Dbxref=PMID:24009510 Q99IB8 UniProtKB Region 1481 1501 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99IB8 UniProtKB Region 1490 1501 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 Q99IB8 UniProtKB Region 1683 1694 . . . Note=NS3-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Region 1837 1865 . . . Note=Glycine zipper;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29167346;Dbxref=PMID:29167346 Q99IB8 UniProtKB Region 1982 2002 . . . Note=Membrane-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Region 2009 2225 . . . Note=D1%3B RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Region 2124 2332 . . . Note=Transcriptional activation;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Region 2124 2212 . . . Note=FKBP8-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 Q99IB8 UniProtKB Region 2139 2143 . . . Note=Interaction with non-structural protein 4A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 Q99IB8 UniProtKB Region 2192 2213 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99IB8 UniProtKB Region 2210 2249 . . . Note=ISDR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 Q99IB8 UniProtKB Region 2214 2275 . . . Note=Interaction with EIF2AK2/PKR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 Q99IB8 UniProtKB Region 2227 2315 . . . Note=D2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Region 2228 2315 . . . Note=Disordered;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Region 2249 2306 . . . Note=NS4B-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Region 2281 2297 . . . Note=Interaction with human PPIA/CYPA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21593166;Dbxref=PMID:21593166 Q99IB8 UniProtKB Region 2329 2442 . . . Note=D3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Region 2336 2447 . . . Note=Interaction with host IFI27;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Region 2352 2432 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99IB8 UniProtKB Region 2358 2381 . . . Note=V3 Q99IB8 UniProtKB Region 2371 2439 . . . Note=Interaction with host VAPB;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Motif 5 13 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25485706;Dbxref=PMID:25485706 Q99IB8 UniProtKB Motif 38 43 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25485706;Dbxref=PMID:25485706 Q99IB8 UniProtKB Motif 58 64 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25485706;Dbxref=PMID:25485706 Q99IB8 UniProtKB Motif 66 71 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25485706;Dbxref=PMID:25485706 Q99IB8 UniProtKB Motif 1320 1323 . . . Note=DECH box;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:30281972,ECO:0000269|PubMed:31511391;Dbxref=PMID:30281972,PMID:31511391 Q99IB8 UniProtKB Motif 2322 2325 . . . Note=SH3-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99IB8 UniProtKB Motif 2326 2334 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 Q99IB8 UniProtKB Compositional bias 47 75 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99IB8 UniProtKB Compositional bias 2199 2213 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99IB8 UniProtKB Compositional bias 2352 2371 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99IB8 UniProtKB Active site 956 956 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 Q99IB8 UniProtKB Active site 976 976 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 Q99IB8 UniProtKB Active site 997 997 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 Q99IB8 UniProtKB Active site 1087 1087 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 Q99IB8 UniProtKB Active site 1111 1111 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 Q99IB8 UniProtKB Active site 1169 1169 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 Q99IB8 UniProtKB Binding site 1127 1127 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 Q99IB8 UniProtKB Binding site 1129 1129 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 Q99IB8 UniProtKB Binding site 1175 1175 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 Q99IB8 UniProtKB Binding site 1179 1179 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 Q99IB8 UniProtKB Binding site 1234 1241 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 Q99IB8 UniProtKB Binding site 1241 1241 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 Q99IB8 UniProtKB Binding site 1321 1321 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:30281972;Dbxref=PMID:30281972 Q99IB8 UniProtKB Binding site 2015 2015 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 Q99IB8 UniProtKB Binding site 2033 2033 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 Q99IB8 UniProtKB Binding site 2035 2035 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 Q99IB8 UniProtKB Binding site 2056 2056 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 Q99IB8 UniProtKB Binding site 2662 2662 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 Q99IB8 UniProtKB Binding site 2760 2760 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 Q99IB8 UniProtKB Binding site 2761 2761 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 Q99IB8 UniProtKB Site 177 178 . . . Note=Cleavage%3B by signal peptide peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 Q99IB8 UniProtKB Site 191 192 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 Q99IB8 UniProtKB Site 383 384 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 Q99IB8 UniProtKB Site 750 751 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q99IB8 UniProtKB Site 813 814 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q99IB8 UniProtKB Site 1030 1031 . . . Note=Cleavage%3B by protease NS2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 Q99IB8 UniProtKB Site 1661 1662 . . . Note=Cleavage%3B by serine protease/helicase NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Site 1715 1716 . . . Note=Cleavage%3B by serine protease/helicase NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Site 1976 1977 . . . Note=Cleavage%3B by serine protease/helicase NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Site 2442 2443 . . . Note=Cleavage%3B by serine protease/helicase NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q913V3 Q99IB8 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 Q99IB8 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 Q99IB8 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine%3B by host PKA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 Q99IB8 UniProtKB Modified residue 2069 2069 . . . Note=Phosphotyrosine%3B by host;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30862675;Dbxref=PMID:30862675 Q99IB8 UniProtKB Modified residue 2198 2198 . . . Note=Phosphoserine%3B by host%3B in p56;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26874015,ECO:0000269|PubMed:28446668;Dbxref=PMID:26874015,PMID:28446668 Q99IB8 UniProtKB Modified residue 2201 2201 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 Q99IB8 UniProtKB Modified residue 2205 2205 . . . Note=Phosphoserine%3B by host%3B in p56 and p58%2C regulates intracellular NS5A distribution;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:30089697,ECO:0000269|PubMed:31511391;Dbxref=PMID:30089697,PMID:31511391 Q99IB8 UniProtKB Modified residue 2208 2208 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28446668,ECO:0000269|PubMed:30089697,ECO:0000269|PubMed:31511391;Dbxref=PMID:28446668,PMID:30089697,PMID:31511391 Q99IB8 UniProtKB Modified residue 2211 2211 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26874015,ECO:0000269|PubMed:28446668,ECO:0000269|PubMed:30089697,ECO:0000269|PubMed:31511391;Dbxref=PMID:26874015,PMID:28446668,PMID:30089697,PMID:31511391 Q99IB8 UniProtKB Modified residue 2214 2214 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31511391;Dbxref=PMID:31511391 Q99IB8 UniProtKB Modified residue 2324 2324 . . . Note=Phosphothreonine%3B by host;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26874015;Dbxref=PMID:26874015 Q99IB8 UniProtKB Lipidation 926 926 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Lipidation 1972 1972 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Lipidation 1976 1976 . . . Note=S-palmitoyl cysteine%3B by host%3B partial;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 196 196 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 209 209 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 234 234 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 305 305 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 417 417 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 423 423 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 430 430 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 448 448 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 477 477 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 534 534 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 542 542 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 558 558 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 578 578 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 627 627 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Glycosylation 649 649 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Disulfide bond 429 554 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Disulfide bond 452 459 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Disulfide bond 488 496 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Disulfide bond 505 510 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Disulfide bond 566 571 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Disulfide bond 585 589 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Disulfide bond 601 624 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Disulfide bond 611 648 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Disulfide bond 656 681 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Cross-link 2350 2350 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 Q99IB8 UniProtKB Mutagenesis 1322 1322 . . . Note=Cleaves ATP 50%25 slower and unwinds DNA 18%25 more slowly. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30281972;Dbxref=PMID:30281972 Q99IB8 UniProtKB Mutagenesis 1322 1322 . . . Note=No effect on NS3 helicase activity%3B 50%25 decreased in nucleic acid binding%3B decreases the affinity of NS3 helicase for Mg2+ by 2 orders of magnitude. C->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30281972;Dbxref=PMID:30281972 Q99IB8 UniProtKB Mutagenesis 2011 2011 . . . Note=Slight reduction in infectivity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29352312;Dbxref=PMID:29352312 Q99IB8 UniProtKB Mutagenesis 2019 2019 . . . Note=Complete loss of viral replication. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29352312;Dbxref=PMID:29352312 Q99IB8 UniProtKB Mutagenesis 2021 2021 . . . Note=Complete loss of viral replication. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29352312;Dbxref=PMID:29352312 Q99IB8 UniProtKB Mutagenesis 2023 2023 . . . Note=Complete loss of viral replication. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29352312;Dbxref=PMID:29352312 Q99IB8 UniProtKB Mutagenesis 2027 2027 . . . Note=Complete loss of viral replication. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29352312;Dbxref=PMID:29352312 Q99IB8 UniProtKB Mutagenesis 2035 2035 . . . Note=Complete loss of viral replication. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29352312;Dbxref=PMID:29352312 Q99IB8 UniProtKB Mutagenesis 2036 2036 . . . Note=Complete loss of viral replication. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29352312;Dbxref=PMID:29352312 Q99IB8 UniProtKB Mutagenesis 2043 2043 . . . Note=Complete loss of virus production. Disrupts the dimerization and localization of NS5A to lipid droplets. NS5A binding to HCV 3'UTRRNA. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29352312;Dbxref=PMID:29352312 Q99IB8 UniProtKB Mutagenesis 2072 2072 . . . Note=Complete loss of viral replication. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29352312;Dbxref=PMID:29352312 Q99IB8 UniProtKB Mutagenesis 2110 2110 . . . Note=Complete loss of viral replication. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29352312;Dbxref=PMID:29352312 Q99IB8 UniProtKB Mutagenesis 2121 2121 . . . Note=Complete loss of virus production. Disrupts the dimerization and localization of NS5A to lipid droplets. Increased affinity of NS5A binding to HCV 3'UTRRNA. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29352312;Dbxref=PMID:29352312 Q99IB8 UniProtKB Mutagenesis 2205 2205 . . . Note=Complete loss of phosphorylation at S-2205%2C S-2208 and S-2211. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28446668;Dbxref=PMID:28446668 Q99IB8 UniProtKB Mutagenesis 2208 2208 . . . Note=Complete loss of phosphorylation at S-2208 and S-2211. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28446668;Dbxref=PMID:28446668 Q99IB8 UniProtKB Mutagenesis 2211 2211 . . . Note=Complete loss of phosphorylation of S-2211. Increases phosphorylation of S-2205. Complete loss of infectivity. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26874015,ECO:0000269|PubMed:31511391;Dbxref=PMID:26874015,PMID:31511391 Q99IB8 UniProtKB Mutagenesis 2211 2211 . . . Note=Alters virus-induced membrane rearrangements%2C no effect on virus infectivity. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26874015;Dbxref=PMID:26874015 Q99IB8 UniProtKB Mutagenesis 2292 2292 . . . Note=No loss of its RNA-binding ability or interaction with human PPIA/CYPA but loss of PPIA/CYPA-mediated stimulation of its RNA-binding ability%3B alone or when associated with N-2293. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21593166;Dbxref=PMID:21593166 Q99IB8 UniProtKB Mutagenesis 2293 2293 . . . Note=No loss of its RNA-binding ability or interaction with human PPIA/CYPA but loss of PPIA/CYPA-mediated stimulation of its RNA-binding ability%3B when associated with E-2292. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21593166;Dbxref=PMID:21593166 Q99IB8 UniProtKB Mutagenesis 2324 2324 . . . Note=No effect on viral replication and virus production. T->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26874015;Dbxref=PMID:26874015 Q99IB8 UniProtKB Mutagenesis 2428 2433 . . . Note=Complete loss of interaction with mature core protein. SWSTCS->AWATCA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18524832;Dbxref=PMID:18524832 Q99IB8 UniProtKB Mutagenesis 2428 2430 . . . Note=No effect on the interaction with mature core protein. SWS->EWE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18524832;Dbxref=PMID:18524832 Q99IB8 UniProtKB Helix 175 185 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LIF Q99IB8 UniProtKB Helix 189 194 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LIF Q99IB8 UniProtKB Helix 537 541 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NPJ Q99IB8 UniProtKB Helix 692 701 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KZQ Q99IB8 UniProtKB Turn 702 706 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KZQ Q99IB8 UniProtKB Helix 710 714 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KZQ Q99IB8 UniProtKB Turn 715 718 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KZQ Q99IB8 UniProtKB Helix 1719 1748 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LVG Q99IB8 UniProtKB Beta strand 2444 2448 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2467 2470 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2476 2478 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2479 2481 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2484 2486 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2487 2494 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2504 2517 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2527 2532 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2542 2544 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TWM Q99IB8 UniProtKB Helix 2547 2552 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2557 2570 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2572 2574 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XXD Q99IB8 UniProtKB Beta strand 2578 2582 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2586 2588 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2591 2593 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2601 2604 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2607 2629 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2630 2632 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2634 2636 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2639 2651 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2653 2663 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2666 2669 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2672 2684 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2689 2701 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Turn 2702 2704 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2706 2709 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2715 2719 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2729 2748 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2754 2758 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2761 2767 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2771 2787 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2792 2794 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2799 2801 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2802 2804 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2810 2816 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2818 2820 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2822 2828 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2831 2842 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2846 2849 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2850 2856 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Turn 2857 2859 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2861 2865 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2867 2878 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2881 2883 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4E76 Q99IB8 UniProtKB Beta strand 2885 2889 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2892 2896 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2898 2900 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2901 2909 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2911 2914 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2921 2934 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2939 2955 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2958 2967 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2969 2971 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Beta strand 2972 2974 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WTL Q99IB8 UniProtKB Helix 2982 2986 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2992 2996 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XYM Q99IB8 UniProtKB Helix 2998 3000 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AEP Q99IB8 UniProtKB Beta strand 3002 3004 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TWM