##gff-version 3 P26663 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26664 P26663 UniProtKB Chain 2 3010 . . . ID=PRO_0000450852;Note=Genome polyprotein P26663 UniProtKB Chain 2 191 . . . ID=PRO_0000037529;Note=Core protein precursor P26663 UniProtKB Chain 2 177 . . . ID=PRO_0000037530;Note=Mature core protein P26663 UniProtKB Propeptide 178 191 . . . ID=PRO_0000037531;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 P26663 UniProtKB Chain 192 383 . . . ID=PRO_0000037532;Note=Envelope glycoprotein E1 P26663 UniProtKB Chain 384 746 . . . ID=PRO_0000037533;Note=Envelope glycoprotein E2 P26663 UniProtKB Chain 747 809 . . . ID=PRO_0000037534;Note=Viroporin p7 P26663 UniProtKB Chain 810 1026 . . . ID=PRO_0000037535;Note=Protease NS2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 P26663 UniProtKB Chain 1027 1657 . . . ID=PRO_0000037536;Note=Serine protease/helicase NS3 P26663 UniProtKB Chain 1658 1711 . . . ID=PRO_0000037537;Note=Non-structural protein 4A P26663 UniProtKB Chain 1712 1972 . . . ID=PRO_0000037538;Note=Non-structural protein 4B P26663 UniProtKB Chain 1973 2419 . . . ID=PRO_0000037539;Note=Non-structural protein 5A P26663 UniProtKB Chain 2420 3010 . . . ID=PRO_0000037540;Note=RNA-directed RNA polymerase P26663 UniProtKB Topological domain 190 358 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Transmembrane 359 379 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Topological domain 380 725 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Transmembrane 726 746 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Topological domain 747 757 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Transmembrane 758 778 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Topological domain 779 781 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Transmembrane 782 803 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Topological domain 804 813 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Transmembrane 814 834 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Topological domain 835 838 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Transmembrane 839 859 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Topological domain 860 881 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Transmembrane 882 902 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Topological domain 903 1657 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Transmembrane 1658 1678 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Topological domain 1679 1805 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Transmembrane 1806 1826 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Topological domain 1827 1828 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Transmembrane 1829 1849 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Topological domain 1850 1850 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Transmembrane 1851 1871 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Topological domain 1872 1881 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Transmembrane 1882 1902 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Topological domain 1903 1972 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Intramembrane 1973 2003 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Topological domain 2004 2989 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Transmembrane 2990 3010 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Domain 903 1026 . . . Note=Peptidase C18;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 P26663 UniProtKB Domain 1027 1208 . . . Note=Peptidase S29;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 P26663 UniProtKB Domain 1217 1369 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 P26663 UniProtKB Domain 2633 2751 . . . Note=RdRp catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00539 P26663 UniProtKB Region 2 75 . . . Note=Disordered;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8189501;Dbxref=PMID:8189501 P26663 UniProtKB Region 2 59 . . . Note=Interaction with DDX3X;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5EG65 P26663 UniProtKB Region 2 58 . . . Note=Interaction with EIF2AK2/PKR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26663 UniProtKB Region 2 23 . . . Note=Interaction with STAT1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26663 UniProtKB Region 112 152 . . . Note=Important for endoplasmic reticulum and mitochondrial localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26663 UniProtKB Region 122 173 . . . Note=Interaction with APOA2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29846 P26663 UniProtKB Region 164 167 . . . Note=Important for lipid droplets localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Region 265 296 . . . Note=Important for fusion;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Region 385 411 . . . Note=HVR1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Region 474 482 . . . Note=HVR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Region 480 494 . . . Note=CD81-binding 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12660945;Dbxref=PMID:12660945 P26663 UniProtKB Region 544 552 . . . Note=CD81-binding 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12660945;Dbxref=PMID:12660945 P26663 UniProtKB Region 660 671 . . . Note=EIF2AK2/eIF2-alpha phosphorylation homology domain (PePHD) P26663 UniProtKB Region 904 1206 . . . Note=Protease NS2-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11591719;Dbxref=PMID:11591719 P26663 UniProtKB Region 929 949 . . . Note=Interaction with host SCPS1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26663 UniProtKB Region 1486 1497 . . . Note=RNA-binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9614113;Dbxref=PMID:9614113 P26663 UniProtKB Region 1679 1690 . . . Note=NS3-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Region 1833 1861 . . . Note=Glycine zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26663 UniProtKB Region 1978 1998 . . . Note=Membrane-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Region 2005 2221 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Region 2120 2332 . . . Note=Transcriptional activation;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Region 2120 2208 . . . Note=FKBP8-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26663 UniProtKB Region 2135 2139 . . . Note=Interaction with non-structural protein 4A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26663 UniProtKB Region 2189 2441 . . . Note=Interaction with host SKP2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Region 2210 2275 . . . Note=EIF2AK2/PKR-binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9710605;Dbxref=PMID:9710605 P26663 UniProtKB Region 2210 2249 . . . Note=ISDR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9710605;Dbxref=PMID:9710605 P26663 UniProtKB Region 2249 2306 . . . Note=NS4B-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Region 2332 2441 . . . Note=Interaction with host IFI27;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Region 2351 2407 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26663 UniProtKB Region 2354 2377 . . . Note=V3 P26663 UniProtKB Motif 5 13 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26663 UniProtKB Motif 38 43 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26663 UniProtKB Motif 58 64 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26663 UniProtKB Motif 66 71 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26663 UniProtKB Motif 1316 1319 . . . Note=DECH box;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26663 UniProtKB Motif 2322 2325 . . . Note=SH3-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Motif 2326 2334 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26663 UniProtKB Compositional bias 47 69 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26663 UniProtKB Compositional bias 2351 2369 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26663 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 P26663 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 P26663 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 P26663 UniProtKB Active site 1083 1083 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01166,ECO:0000269|PubMed:8861916;Dbxref=PMID:8861916 P26663 UniProtKB Active site 1107 1107 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01166,ECO:0000269|PubMed:8861916;Dbxref=PMID:8861916 P26663 UniProtKB Active site 1165 1165 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01166,ECO:0000269|PubMed:8861916,ECO:0000269|PubMed:9568891;Dbxref=PMID:8861916,PMID:9568891 P26663 UniProtKB Binding site 1123 1123 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01166,ECO:0000269|PubMed:10366511,ECO:0000269|PubMed:8861916,ECO:0000269|PubMed:9568891;Dbxref=PMID:10366511,PMID:8861916,PMID:9568891 P26663 UniProtKB Binding site 1125 1125 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01166,ECO:0000269|PubMed:10366511,ECO:0000269|PubMed:8861916,ECO:0000269|PubMed:9568891;Dbxref=PMID:10366511,PMID:8861916,PMID:9568891 P26663 UniProtKB Binding site 1171 1171 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01166,ECO:0000269|PubMed:10366511,ECO:0000269|PubMed:8861916;Dbxref=PMID:10366511,PMID:8861916 P26663 UniProtKB Binding site 1175 1175 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01166,ECO:0000269|PubMed:10366511,ECO:0000269|PubMed:8861916;Dbxref=PMID:10366511,PMID:8861916 P26663 UniProtKB Binding site 1230 1237 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 P26663 UniProtKB Binding site 1237 1237 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Binding site 1317 1317 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Binding site 2011 2011 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Binding site 2029 2029 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Binding site 2031 2031 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Binding site 2052 2052 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Binding site 2639 2639 . . . Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:10557268,ECO:0000305|PubMed:11884572;Dbxref=PMID:10557268,PMID:11884572 P26663 UniProtKB Binding site 2737 2737 . . . Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:10557268,ECO:0000305|PubMed:11884572;Dbxref=PMID:10557268,PMID:11884572 P26663 UniProtKB Binding site 2738 2738 . . . Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:10557268,ECO:0000305|PubMed:11884572;Dbxref=PMID:10557268,PMID:11884572 P26663 UniProtKB Site 177 178 . . . Note=Cleavage%3B by host signal peptide peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26663 UniProtKB Site 191 192 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26663 UniProtKB Site 383 384 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26663 UniProtKB Site 746 747 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250 P26663 UniProtKB Site 809 810 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250 P26663 UniProtKB Site 1026 1027 . . . Note=Cleavage%3B by protease NS2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 P26663 UniProtKB Site 1657 1658 . . . Note=Cleavage%3B by serine protease/helicase NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Site 1711 1712 . . . Note=Cleavage%3B by serine protease/helicase NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Site 1972 1973 . . . Note=Cleavage%3B by serine protease/helicase NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Site 2419 2420 . . . Note=Cleavage%3B by serine protease/helicase NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q913V3 P26663 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 P26663 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 P26663 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine%3B by host PKA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 P26663 UniProtKB Modified residue 2194 2194 . . . Note=Phosphoserine%3B by host%3B in p56;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11118372;Dbxref=PMID:11118372 P26663 UniProtKB Modified residue 2197 2197 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Modified residue 2201 2201 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Modified residue 2204 2204 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 P26663 UniProtKB Modified residue 2207 2207 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26663 UniProtKB Modified residue 2210 2210 . . . Note=Phosphoserine%3B by host%3B in p58;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 P26663 UniProtKB Modified residue 2448 2448 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26663 UniProtKB Modified residue 2461 2461 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 P26663 UniProtKB Lipidation 922 922 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Lipidation 1968 1968 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Lipidation 1972 1972 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Glycosylation 196 196 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8862403;Dbxref=PMID:8862403 P26663 UniProtKB Glycosylation 209 209 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Glycosylation 234 234 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Glycosylation 250 250 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Glycosylation 305 305 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Glycosylation 417 417 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 P26663 UniProtKB Glycosylation 423 423 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Glycosylation 430 430 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Glycosylation 448 448 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Glycosylation 532 532 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Glycosylation 540 540 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Glycosylation 556 556 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Glycosylation 576 576 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Glycosylation 623 623 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Glycosylation 645 645 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Disulfide bond 429 552 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Disulfide bond 452 459 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Disulfide bond 486 494 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Disulfide bond 503 508 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Disulfide bond 564 569 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Disulfide bond 581 585 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Disulfide bond 597 620 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Disulfide bond 607 644 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 UniProtKB Disulfide bond 652 677 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 P26663 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 P26663 UniProtKB Mutagenesis 2194 2194 . . . Note=Loss of phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11118372;Dbxref=PMID:11118372 P26663 UniProtKB Mutagenesis 2322 2322 . . . Note=Complete loss of binding to GRB2. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10318918;Dbxref=PMID:10318918 P26663 UniProtKB Mutagenesis 2323 2323 . . . Note=Complete loss of binding to GRB2. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10318918;Dbxref=PMID:10318918 P26663 UniProtKB Mutagenesis 2326 2326 . . . Note=Complete loss of binding to GRB2. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10318918;Dbxref=PMID:10318918 P26663 UniProtKB Mutagenesis 2639 2639 . . . Note=Complete loss of RdRp activity. D->C%2CG%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9343198;Dbxref=PMID:9343198 P26663 UniProtKB Mutagenesis 2644 2644 . . . Note=Complete loss of RdRp activity. D->G%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9343198;Dbxref=PMID:9343198 P26663 UniProtKB Mutagenesis 2702 2702 . . . Note=Complete loss of RdRp activity. G->D%2CL%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9343198;Dbxref=PMID:9343198 P26663 UniProtKB Mutagenesis 2705 2705 . . . Note=Almost complete loss of RdRp activity. T->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9343198;Dbxref=PMID:9343198 P26663 UniProtKB Mutagenesis 2706 2706 . . . Note=Almost complete loss of RdRp activity. T->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9343198;Dbxref=PMID:9343198 P26663 UniProtKB Mutagenesis 2706 2706 . . . Note=Complete loss of RdRp activity. T->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9343198;Dbxref=PMID:9343198 P26663 UniProtKB Mutagenesis 2710 2710 . . . Note=Complete loss of RdRp activity. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9343198;Dbxref=PMID:9343198 P26663 UniProtKB Mutagenesis 2736 2736 . . . Note=Almost complete loss of RdRp activity. G->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9343198;Dbxref=PMID:9343198 P26663 UniProtKB Mutagenesis 2737 2737 . . . Note=Complete loss of RdRp activity. D->E%2CH%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9343198;Dbxref=PMID:9343198 P26663 UniProtKB Mutagenesis 2738 2738 . . . Note=Complete loss of RdRp activity. D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9343198;Dbxref=PMID:9343198 P26663 UniProtKB Beta strand 413 416 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DGY P26663 UniProtKB Beta strand 419 422 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DGY P26663 UniProtKB Beta strand 1017 1023 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Beta strand 1031 1035 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Helix 1039 1048 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Beta strand 1057 1063 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Beta strand 1068 1074 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Beta strand 1077 1080 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Helix 1082 1085 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Beta strand 1090 1092 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JXP P26663 UniProtKB Beta strand 1095 1097 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JXP P26663 UniProtKB Beta strand 1100 1103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Turn 1104 1107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Beta strand 1108 1112 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Beta strand 1128 1133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Beta strand 1135 1137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BT7 P26663 UniProtKB Beta strand 1139 1144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Beta strand 1146 1157 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Helix 1158 1161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Beta strand 1168 1170 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Turn 1172 1174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JXP P26663 UniProtKB Beta strand 1176 1186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Beta strand 1189 1197 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Helix 1198 1206 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Beta strand 1224 1229 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1232 1235 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CU1 P26663 UniProtKB Turn 1236 1238 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1239 1246 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1251 1256 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1258 1272 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1277 1279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1290 1295 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1296 1301 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1307 1309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1311 1315 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Turn 1316 1319 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1323 1335 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Turn 1336 1340 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1342 1350 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1362 1366 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1371 1375 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1378 1380 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1382 1384 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1386 1393 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1397 1409 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1414 1417 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1419 1421 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8OHM P26663 UniProtKB Helix 1423 1425 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1428 1430 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1432 1436 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1438 1441 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Turn 1442 1444 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8OHM P26663 UniProtKB Beta strand 1448 1453 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1456 1463 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1467 1469 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1471 1478 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1481 1488 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1493 1495 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1497 1503 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1509 1511 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B76 P26663 UniProtKB Helix 1514 1526 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1532 1544 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1555 1563 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1570 1579 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1584 1596 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1606 1611 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Turn 1612 1614 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Helix 1615 1617 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1625 1629 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1635 1637 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8OHM P26663 UniProtKB Helix 1640 1650 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Turn 1653 1655 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WXP P26663 UniProtKB Beta strand 1680 1688 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JXP P26663 UniProtKB Beta strand 2421 2425 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2446 2449 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2453 2455 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2456 2458 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2461 2463 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2464 2471 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2481 2494 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2504 2509 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Turn 2519 2521 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WRM P26663 UniProtKB Helix 2524 2528 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2532 2547 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2549 2551 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2555 2559 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2563 2565 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Turn 2568 2571 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GX5 P26663 UniProtKB Beta strand 2578 2581 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2584 2606 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2607 2609 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2611 2613 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2616 2629 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2630 2638 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2643 2646 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2649 2659 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2666 2678 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Turn 2679 2681 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GX6 P26663 UniProtKB Beta strand 2683 2686 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2688 2690 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CSJ P26663 UniProtKB Beta strand 2692 2696 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2701 2703 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HWI P26663 UniProtKB Helix 2706 2724 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2728 2735 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2738 2744 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2748 2764 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2769 2771 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2776 2778 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2779 2781 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2787 2793 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2795 2797 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3CVK P26663 UniProtKB Beta strand 2799 2804 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2808 2819 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2826 2833 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Turn 2834 2836 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2838 2842 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2844 2854 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2858 2860 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BSA P26663 UniProtKB Beta strand 2862 2866 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2869 2873 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2875 2877 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2878 2886 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2888 2891 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2898 2911 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2916 2933 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2935 2944 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2946 2948 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2949 2951 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Helix 2959 2962 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Turn 2967 2970 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GIQ P26663 UniProtKB Beta strand 2976 2978 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KE5 P26663 UniProtKB Beta strand 2980 2982 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4EO6