##gff-version 3 Q03468 UniProtKB Chain 1 1493 . . . ID=PRO_0000074314;Note=DNA excision repair protein ERCC-6 Q03468 UniProtKB Domain 519 695 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 Q03468 UniProtKB Domain 843 1002 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 Q03468 UniProtKB Region 1 510 . . . Note=N-terminal domain%3B essential for its chromatin remodeling activity;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29203878;Dbxref=PMID:29203878 Q03468 UniProtKB Region 1 39 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Region 287 323 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Region 344 453 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Region 1042 1147 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Region 1181 1247 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Region 1318 1384 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Region 1400 1428 . . . Note=Ubiquitin-binding domain (UBD);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20541997;Dbxref=PMID:20541997 Q03468 UniProtKB Region 1429 1493 . . . Note=Winged-helix domain (WHD);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:29203878;Dbxref=PMID:29203878 Q03468 UniProtKB Region 1446 1493 . . . Note=Essential for its interaction with RNA polymerase II%2C transcription-coupled nucleotide excision repair activity%2C association with chromatin after UV irradiation and for mediating the UV-induced translocation of ERRC8 to the nuclear matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26620705;Dbxref=PMID:26620705 Q03468 UniProtKB Motif 646 649 . . . Note=DEAH box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 Q03468 UniProtKB Compositional bias 1 31 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Compositional bias 363 396 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Compositional bias 405 422 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Compositional bias 1095 1110 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Compositional bias 1124 1142 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Compositional bias 1181 1202 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Compositional bias 1211 1247 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Compositional bias 1335 1353 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Compositional bias 1354 1375 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03468 UniProtKB Binding site 532 539 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 Q03468 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine%3B by ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29203878;Dbxref=PMID:29203878 Q03468 UniProtKB Modified residue 158 158 . . . Note=Phosphoserine%3B by CDK2;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:29203878,ECO:0007744|PubMed:16964243,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:18691976,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:16964243,PMID:18669648,PMID:18691976,PMID:20068231,PMID:23186163,PMID:29203878 Q03468 UniProtKB Modified residue 170 170 . . . Note=N6-methylated lysine%3B by EHMT2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18438403;Dbxref=PMID:18438403 Q03468 UniProtKB Modified residue 297 297 . . . Note=N6-methylated lysine%3B by EHMT2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18438403;Dbxref=PMID:18438403 Q03468 UniProtKB Modified residue 429 429 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:21406692;Dbxref=PMID:18669648,PMID:21406692 Q03468 UniProtKB Modified residue 430 430 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:21406692;Dbxref=PMID:18669648,PMID:21406692 Q03468 UniProtKB Modified residue 448 448 . . . Note=N6-methylated lysine%3B by EHMT2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18438403;Dbxref=PMID:18438403 Q03468 UniProtKB Modified residue 486 486 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21406692;Dbxref=PMID:21406692 Q03468 UniProtKB Modified residue 489 489 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21406692;Dbxref=PMID:21406692 Q03468 UniProtKB Modified residue 1054 1054 . . . Note=N6-methylated lysine%3B by EHMT2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18438403;Dbxref=PMID:18438403 Q03468 UniProtKB Modified residue 1142 1142 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q03468 UniProtKB Modified residue 1348 1348 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q03468 UniProtKB Cross-link 205 205 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26620705;Dbxref=PMID:26620705 Q03468 UniProtKB Cross-link 255 255 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q03468 UniProtKB Natural variant 134 134 . . . ID=VAR_054153;Note=R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18987736;Dbxref=dbSNP:rs148095899,PMID:18987736 Q03468 UniProtKB Natural variant 255 255 . . . ID=VAR_001216;Note=K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9443879;Dbxref=PMID:9443879 Q03468 UniProtKB Natural variant 399 399 . . . ID=VAR_001217;Note=G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9443879,ECO:0000269|Ref.3;Dbxref=dbSNP:rs2228528,PMID:9443879 Q03468 UniProtKB Natural variant 425 425 . . . ID=VAR_016301;Note=D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs4253046 Q03468 UniProtKB Natural variant 446 446 . . . ID=VAR_016302;Note=G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs4253047 Q03468 UniProtKB Natural variant 591 591 . . . ID=VAR_036021;Note=In a colorectal cancer sample%3B somatic mutation. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=dbSNP:rs1184760254,PMID:16959974 Q03468 UniProtKB Natural variant 652 652 . . . ID=VAR_036022;Note=In a colorectal cancer sample%3B somatic mutation. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=dbSNP:rs1365187961,PMID:16959974 Q03468 UniProtKB Natural variant 670 670 . . . ID=VAR_001218;Note=In CSB. R->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19894250,ECO:0000269|PubMed:9443879;Dbxref=dbSNP:rs202080674,PMID:19894250,PMID:9443879 Q03468 UniProtKB Natural variant 680 680 . . . ID=VAR_063511;Note=In CSB. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19894250;Dbxref=dbSNP:rs1554788393,PMID:19894250 Q03468 UniProtKB Natural variant 686 686 . . . ID=VAR_063512;Note=In CSB. W->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19894250;Dbxref=dbSNP:rs751292948,PMID:19894250 Q03468 UniProtKB Natural variant 687 687 . . . ID=VAR_063513;Note=In CSB. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19894250;Dbxref=dbSNP:rs1026438103,PMID:19894250 Q03468 UniProtKB Natural variant 851 851 . . . ID=VAR_001219;Note=In CSB%3B DNA-dependent ATPase-dead mutant%3B loss of chromatin remodeling activity%3B loss of its ability to inhibit non-homologous end joining-mediated repair and promote homologous recombination-mediated repair of DNA double-strand breaks%3B loss of its ability to suppress premature exit from G2/M checkpoint%3B abrogation of its UV-induced chromatin association. W->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19894250,ECO:0000269|PubMed:25820262,ECO:0000269|PubMed:29203878,ECO:0000269|PubMed:9443879;Dbxref=dbSNP:rs368728467,PMID:19894250,PMID:25820262,PMID:29203878,PMID:9443879 Q03468 UniProtKB Natural variant 871 871 . . . ID=VAR_063514;Note=In COFS1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19894250;Dbxref=PMID:19894250 Q03468 UniProtKB Natural variant 942 942 . . . ID=VAR_016303;Note=T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs2228525 Q03468 UniProtKB Natural variant 957 957 . . . ID=VAR_001220;Note=In CSB. V->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19894250,ECO:0000269|PubMed:9443879;Dbxref=PMID:19894250,PMID:9443879 Q03468 UniProtKB Natural variant 987 987 . . . ID=VAR_063515;Note=In COFS1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19894250;Dbxref=dbSNP:rs121917905,PMID:19894250 Q03468 UniProtKB Natural variant 1002 1002 . . . ID=VAR_016304;Note=Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs4253206 Q03468 UniProtKB Natural variant 1038 1038 . . . ID=VAR_036023;Note=In a breast cancer sample%3B somatic mutation. R->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974 Q03468 UniProtKB Natural variant 1042 1042 . . . ID=VAR_001221;Note=In CSB. P->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19894250,ECO:0000269|PubMed:9443879;Dbxref=PMID:19894250,PMID:9443879 Q03468 UniProtKB Natural variant 1095 1095 . . . ID=VAR_001222;Note=P->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19894250,ECO:0000269|PubMed:9443879,ECO:0000269|Ref.3;Dbxref=dbSNP:rs4253208,PMID:19894250,PMID:9443879 Q03468 UniProtKB Natural variant 1097 1097 . . . ID=VAR_001223;Note=M->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9443879,ECO:0000269|Ref.3;Dbxref=dbSNP:rs2228526,PMID:9443879 Q03468 UniProtKB Natural variant 1119 1119 . . . ID=VAR_036024;Note=In a breast cancer sample%3B somatic mutation. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974 Q03468 UniProtKB Natural variant 1119 1119 . . . ID=VAR_036025;Note=In a breast cancer sample%3B somatic mutation. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974 Q03468 UniProtKB Natural variant 1213 1213 . . . ID=VAR_001224;Note=R->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19894250,ECO:0000269|PubMed:9443879,ECO:0000269|Ref.3;Dbxref=dbSNP:rs2228527,PMID:19894250,PMID:9443879 Q03468 UniProtKB Natural variant 1220 1220 . . . ID=VAR_037436;Note=T->I;Dbxref=dbSNP:rs34704611 Q03468 UniProtKB Natural variant 1230 1230 . . . ID=VAR_016305;Note=R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs4253211 Q03468 UniProtKB Natural variant 1308 1308 . . . ID=VAR_016306;Note=V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs2229761 Q03468 UniProtKB Natural variant 1322 1322 . . . ID=VAR_016307;Note=G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs4253219 Q03468 UniProtKB Natural variant 1355 1355 . . . ID=VAR_037437;Note=D->E;Dbxref=dbSNP:rs34917815 Q03468 UniProtKB Natural variant 1372 1372 . . . ID=VAR_016308;Note=G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs4253227 Q03468 UniProtKB Natural variant 1382 1382 . . . ID=VAR_016309;Note=G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs4253228 Q03468 UniProtKB Natural variant 1410 1410 . . . ID=VAR_016310;Note=G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs4253229 Q03468 UniProtKB Natural variant 1413 1413 . . . ID=VAR_001225;Note=Q->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9443879,ECO:0000269|Ref.3;Dbxref=dbSNP:rs2228529,PMID:9443879 Q03468 UniProtKB Natural variant 1441 1441 . . . ID=VAR_016311;Note=T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs4253230 Q03468 UniProtKB Mutagenesis 10 10 . . . Note=Non-phosphorylatable by ATM. Loss of chromatin remodeling activity and its ability to promote the intramolecular interaction of the N-terminal domain with the helicase ATP-binding domain. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29203878;Dbxref=PMID:29203878 Q03468 UniProtKB Mutagenesis 10 10 . . . Note=Phosphomimetic mutant. No loss of chromatin remodeling activity and its ability to promote the intramolecular interaction of the N-terminal domain with the helicase ATP-binding domain. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29203878;Dbxref=PMID:29203878 Q03468 UniProtKB Mutagenesis 158 158 . . . Note=Non-phosphorylatable by CDK2. Loss of chromatin remodeling activity and its ability to promote the intramolecular interaction of the N-terminal domain with the helicase ATP-binding domain. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29203878;Dbxref=PMID:29203878 Q03468 UniProtKB Mutagenesis 158 158 . . . Note=Phosphomimetic mutant. No loss of chromatin remodeling activity and its ability to promote the intramolecular interaction of the N-terminal domain with the helicase ATP-binding domain. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29203878;Dbxref=PMID:29203878 Q03468 UniProtKB Mutagenesis 205 205 . . . Note=Loss of sumoylation and defects in transcription-coupled nucleotide excision repair. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26620705;Dbxref=PMID:26620705 Q03468 UniProtKB Mutagenesis 1427 1428 . . . Note=Fails to bind polyubiquitin chains. LL->GG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20541997;Dbxref=PMID:20541997 Q03468 UniProtKB Mutagenesis 1457 1457 . . . Note=No loss of sumoylation%3B when associated with R-1487 and R-1489. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26620705;Dbxref=PMID:26620705 Q03468 UniProtKB Mutagenesis 1470 1470 . . . Note=Loss of interaction with RIF1%3B when associated with G-1486 and G-1488. L->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29203878;Dbxref=PMID:29203878 Q03468 UniProtKB Mutagenesis 1486 1486 . . . Note=Loss of interaction with RIF1%3B when associated with G-1470 and G-1488. W->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29203878;Dbxref=PMID:29203878 Q03468 UniProtKB Mutagenesis 1487 1487 . . . Note=No loss of sumoylation%3B when associated with R-1457 and R-1489. No loss of sumoylation%3B when associated with R-1489. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26620705;Dbxref=PMID:26620705 Q03468 UniProtKB Mutagenesis 1488 1488 . . . Note=Loss of interaction with RIF1%3B when associated with G-1470 and G-1486. L->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29203878;Dbxref=PMID:29203878 Q03468 UniProtKB Mutagenesis 1489 1489 . . . Note=No loss of sumoylation%3B when associated with R-1457 and R-1487. No loss of sumoylation%3B when associated with R-1487. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26620705;Dbxref=PMID:26620705 Q03468 UniProtKB Helix 93 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CVO Q03468 UniProtKB Helix 102 104 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CVO Q03468 UniProtKB Helix 109 155 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CVO Q03468 UniProtKB Beta strand 494 496 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 501 506 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 509 524 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 528 530 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 539 551 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 564 566 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 569 572 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 575 577 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 578 588 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 594 602 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 607 617 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 620 623 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 625 630 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 632 635 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 636 638 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 641 646 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7OO3 Q03468 UniProtKB Helix 648 651 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 654 656 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7OO3 Q03468 UniProtKB Helix 657 662 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 671 673 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 679 681 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 682 692 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 700 706 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 708 713 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 721 738 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Turn 739 741 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 747 751 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Turn 752 754 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 759 766 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7OOB Q03468 UniProtKB Helix 770 780 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 783 789 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 796 807 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 809 813 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7OO3 Q03468 UniProtKB Helix 835 837 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 839 853 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 858 863 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 865 877 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 882 885 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 891 893 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 894 903 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 909 913 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Turn 914 917 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 918 920 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 928 931 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 938 946 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Beta strand 957 961 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 968 987 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D Q03468 UniProtKB Helix 998 1002 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7OO3 Q03468 UniProtKB Beta strand 1012 1014 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7OO3 Q03468 UniProtKB Helix 1017 1021 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7OO3 Q03468 UniProtKB Helix 1388 1398 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8B3D