##gff-version 3 O39929 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26664 O39929 UniProtKB Chain 2 3008 . . . ID=PRO_0000450900;Note=Genome polyprotein O39929 UniProtKB Chain 2 191 . . . ID=PRO_0000045532;Note=Core protein precursor O39929 UniProtKB Chain 2 177 . . . ID=PRO_0000045533;Note=Mature core protein O39929 UniProtKB Propeptide 178 191 . . . ID=PRO_0000045534;Note=ER anchor for the core protein%2C removed in mature form by host signal peptidase O39929 UniProtKB Chain 192 383 . . . ID=PRO_0000045535;Note=Envelope glycoprotein E1 O39929 UniProtKB Chain 384 746 . . . ID=PRO_0000045536;Note=Envelope glycoprotein E2 O39929 UniProtKB Chain 747 809 . . . ID=PRO_0000045537;Note=Viroporin p7 O39929 UniProtKB Chain 810 1026 . . . ID=PRO_0000045538;Note=Protease NS2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O39929 UniProtKB Chain 1027 1657 . . . ID=PRO_0000045539;Note=Serine protease/helicase NS3 O39929 UniProtKB Chain 1658 1711 . . . ID=PRO_0000045540;Note=Non-structural protein 4A O39929 UniProtKB Chain 1712 1972 . . . ID=PRO_0000045541;Note=Non-structural protein 4B O39929 UniProtKB Chain 1973 2417 . . . ID=PRO_0000045542;Note=Non-structural protein 5A O39929 UniProtKB Chain 2418 3008 . . . ID=PRO_0000045543;Note=RNA-directed RNA polymerase O39929 UniProtKB Topological domain 2 168 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Transmembrane 169 189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Topological domain 190 358 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Transmembrane 359 379 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Topological domain 380 725 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Transmembrane 726 746 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Topological domain 747 757 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Transmembrane 758 778 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Topological domain 779 782 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Transmembrane 783 803 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Topological domain 804 813 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Transmembrane 814 834 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Topological domain 835 881 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Transmembrane 882 902 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Topological domain 903 928 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Transmembrane 929 949 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Topological domain 950 1657 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Transmembrane 1658 1678 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Topological domain 1679 1805 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Transmembrane 1806 1826 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Topological domain 1827 1828 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Transmembrane 1829 1849 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Topological domain 1850 1850 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Transmembrane 1851 1871 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Topological domain 1872 1881 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Transmembrane 1882 1902 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Topological domain 1903 1972 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Intramembrane 1973 2002 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Topological domain 2003 2987 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Transmembrane 2988 3008 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Domain 903 1026 . . . Note=Peptidase C18;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O39929 UniProtKB Domain 1027 1208 . . . Note=Peptidase S29;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39929 UniProtKB Domain 1217 1369 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 O39929 UniProtKB Domain 2631 2749 . . . Note=RdRp catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00539 O39929 UniProtKB Region 2 75 . . . Note=Disordered;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Region 2 59 . . . Note=Interaction with DDX3X;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5EG65 O39929 UniProtKB Region 2 58 . . . Note=Interaction with EIF2AK2/PKR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39929 UniProtKB Region 2 23 . . . Note=Interaction with STAT1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39929 UniProtKB Region 112 152 . . . Note=Important for endoplasmic reticulum and mitochondrial localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39929 UniProtKB Region 122 173 . . . Note=Interaction with APOA2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29846 O39929 UniProtKB Region 164 167 . . . Note=Important for lipid droplets localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Region 265 296 . . . Note=Important for fusion;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Region 385 412 . . . Note=HVR1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Region 475 479 . . . Note=HVR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Region 481 494 . . . Note=CD81-binding 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39929 UniProtKB Region 545 552 . . . Note=CD81-binding 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39929 UniProtKB Region 660 671 . . . Note=PKR/eIF2-alpha phosphorylation homology domain (PePHD);Ontology_term=ECO:0000250;evidence=ECO:0000250 O39929 UniProtKB Region 904 1206 . . . Note=Protease NS2-3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39929 UniProtKB Region 929 949 . . . Note=Interaction with host SCPS1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39929 UniProtKB Region 1486 1498 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39929 UniProtKB Region 1679 1690 . . . Note=NS3-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Region 2120 2329 . . . Note=Transcriptional activation;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Region 2120 2208 . . . Note=FKBP8-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39929 UniProtKB Region 2135 2139 . . . Note=Interaction with non-structural protein 4A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39929 UniProtKB Region 2189 2435 . . . Note=Interaction with host SKP2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Region 2210 2272 . . . Note=Interaction with EIF2AK2/PKR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39929 UniProtKB Region 2210 2245 . . . Note=ISDR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39929 UniProtKB Region 2245 2303 . . . Note=NS4B-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Region 2296 2373 . . . Note=V3 O39929 UniProtKB Region 2346 2406 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O39929 UniProtKB Motif 5 13 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39929 UniProtKB Motif 38 43 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39929 UniProtKB Motif 58 64 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39929 UniProtKB Motif 66 71 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39929 UniProtKB Motif 1316 1319 . . . Note=DECH box;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39929 UniProtKB Motif 2319 2322 . . . Note=SH3-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Motif 2324 2332 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39929 UniProtKB Compositional bias 47 69 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O39929 UniProtKB Compositional bias 2349 2373 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O39929 UniProtKB Active site 952 952 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O39929 UniProtKB Active site 972 972 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O39929 UniProtKB Active site 993 993 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O39929 UniProtKB Active site 1083 1083 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39929 UniProtKB Active site 1107 1107 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39929 UniProtKB Active site 1165 1165 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39929 UniProtKB Binding site 1123 1123 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39929 UniProtKB Binding site 1125 1125 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39929 UniProtKB Binding site 1171 1171 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39929 UniProtKB Binding site 1175 1175 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O39929 UniProtKB Binding site 1230 1237 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 O39929 UniProtKB Binding site 1237 1237 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Binding site 1317 1317 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Binding site 2029 2029 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Binding site 2031 2031 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Binding site 2052 2052 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Binding site 2637 2637 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39929 UniProtKB Binding site 2735 2735 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39929 UniProtKB Binding site 2736 2736 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O39929 UniProtKB Site 177 178 . . . Note=Cleavage%3B by host signal peptide peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39929 UniProtKB Site 191 192 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39929 UniProtKB Site 383 384 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39929 UniProtKB Site 746 747 . . . Note=Cleavage%3B by host signal peptidase O39929 UniProtKB Site 809 810 . . . Note=Cleavage%3B by host signal peptidase O39929 UniProtKB Site 1026 1027 . . . Note=Cleavage%3B by protease NS2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O39929 UniProtKB Site 1657 1658 . . . Note=Cleavage%3B by serine protease NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Site 1711 1712 . . . Note=Cleavage%3B by serine protease NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Site 1972 1973 . . . Note=Cleavage%3B by serine protease NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Site 2417 2418 . . . Note=Cleavage%3B by serine protease NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q913V3 O39929 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 O39929 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 O39929 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 O39929 UniProtKB Modified residue 2194 2194 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Modified residue 2197 2197 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Modified residue 2201 2201 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Modified residue 2204 2204 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O39929 UniProtKB Modified residue 2207 2207 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O39929 UniProtKB Modified residue 2446 2446 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O39929 UniProtKB Lipidation 922 922 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Lipidation 1972 1972 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Glycosylation 196 196 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Glycosylation 209 209 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Glycosylation 234 234 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Glycosylation 305 305 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Glycosylation 417 417 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Glycosylation 423 423 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Glycosylation 430 430 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Glycosylation 448 448 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Glycosylation 476 476 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Glycosylation 533 533 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Glycosylation 557 557 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O39929 UniProtKB Glycosylation 623 623 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Glycosylation 645 645 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Disulfide bond 429 553 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Disulfide bond 452 459 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Disulfide bond 487 495 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Disulfide bond 504 509 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Disulfide bond 565 570 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Disulfide bond 581 585 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Disulfide bond 597 620 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Disulfide bond 607 644 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Disulfide bond 652 677 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Cross-link 2347 2347 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O39929 UniProtKB Beta strand 1058 1063 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Beta strand 1068 1074 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Beta strand 1077 1081 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Helix 1082 1085 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Beta strand 1100 1103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Turn 1104 1107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Beta strand 1108 1112 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Beta strand 1128 1133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Beta strand 1139 1144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Beta strand 1146 1157 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Helix 1158 1161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Beta strand 1168 1170 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Beta strand 1176 1186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Beta strand 1189 1197 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z O39929 UniProtKB Helix 1198 1200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6P6Z