ID SKI2_YEAST Reviewed; 1287 AA. AC P35207; D6VZ33; Q06047; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 27-MAR-2024, entry version 208. DE RecName: Full=Antiviral helicase SKI2; DE EC=3.6.4.13; DE AltName: Full=Superkiller protein 2; GN Name=SKI2; OrderedLocusNames=YLR398C; ORFNames=L8084.17; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=8321235; DOI=10.1128/mcb.13.7.4331-4341.1993; RA Widner W.R., Wickner R.B.; RT "Evidence that the SKI antiviral system of Saccharomyces cerevisiae acts by RT blocking expression of viral mRNA."; RL Mol. Cell. Biol. 13:4331-4341(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., RA Zollner A., Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-162. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7816623; DOI=10.1093/nar/22.24.5332; RA Lygerou Z., Conesa C., Lesage P., Swanson R.N., Ruet A., Carlson M., RA Sentenac A., Seraphin B.; RT "The yeast BDF1 gene encodes a transcription factor involved in the RT expression of a broad class of genes including snRNAs."; RL Nucleic Acids Res. 22:5332-5340(1994). RN [5] RP FUNCTION. RX PubMed=363683; DOI=10.1128/jb.136.3.1002-1007.1978; RA Toh-e A., Guerry P., Wickner R.B.; RT "Chromosomal superkiller mutants of Saccharomyces cerevisiae."; RL J. Bacteriol. 136:1002-1007(1978). RN [6] RP FUNCTION. RX PubMed=6371496; DOI=10.1128/mcb.4.4.761-770.1984; RA Ridley S.P., Sommer S.S., Wickner R.B.; RT "Superkiller mutations in Saccharomyces cerevisiae suppress exclusion of M2 RT double-stranded RNA by L-A-HN and confer cold sensitivity in the presence RT of M and L-A-HN."; RL Mol. Cell. Biol. 4:761-770(1984). RN [7] RP FUNCTION. RX PubMed=7739552; DOI=10.1128/mcb.15.5.2719; RA Johnson A.W., Kolodner R.D.; RT "Synthetic lethality of sep1 (xrn1) ski2 and sep1 (xrn1) ski3 mutants of RT Saccharomyces cerevisiae is independent of killer virus and suggests a RT general role for these genes in translation control."; RL Mol. Cell. Biol. 15:2719-2727(1995). RN [8] RP FUNCTION. RX PubMed=7739557; DOI=10.1128/mcb.15.5.2763; RA Masison D.C., Blanc A., Ribas J.C., Carroll K., Sonenberg N., Wickner R.B.; RT "Decoying the cap- mRNA degradation system by a double-stranded RNA virus RT and poly(A)- mRNA surveillance by a yeast antiviral system."; RL Mol. Cell. Biol. 15:2763-2771(1995). RN [9] RP FUNCTION. RX PubMed=9482746; DOI=10.1093/emboj/17.5.1497; RA Anderson J.S.J., Parker R.P.; RT "The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA RT turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases RT of the exosome complex."; RL EMBO J. 17:1497-1506(1998). RN [10] RP FUNCTION. RX PubMed=10611222; DOI=10.1128/mcb.20.2.441-452.2000; RA van Hoof A., Lennertz P., Parker R.; RT "Yeast exosome mutants accumulate 3'-extended polyadenylated forms of U4 RT small nuclear RNA and small nucleolar RNAs."; RL Mol. Cell. Biol. 20:441-452(2000). RN [11] RP FUNCTION, INTERACTION WITH SKI3 AND SKI8, AND SUBCELLULAR LOCATION. RX PubMed=10744028; DOI=10.1017/s1355838200991787; RA Brown J.T., Bai X., Johnson A.W.; RT "The yeast antiviral proteins Ski2p, Ski3p, and Ski8p exist as a complex in RT vivo."; RL RNA 6:449-457(2000). RN [12] RP FUNCTION. RX PubMed=10922069; DOI=10.1073/pnas.97.16.9133; RA Searfoss A.M., Wickner R.B.; RT "3' poly(A) is dispensable for translation."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9133-9137(2000). RN [13] RP FUNCTION OF THE SKI COMPLEX. RX PubMed=11532933; DOI=10.1093/emboj/20.17.4684; RA Araki Y., Takahashi S., Kobayashi T., Kajiho H., Hoshino S., Katada T.; RT "Ski7p G protein interacts with the exosome and the Ski complex for 3'-to- RT 5' mRNA decay in yeast."; RL EMBO J. 20:4684-4693(2001). RN [14] RP FUNCTION OF THE SKI COMPLEX. RX PubMed=11720286; RA Brown J.T., Johnson A.W.; RT "A cis-acting element known to block 3' mRNA degradation enhances RT expression of polyA-minus mRNA in wild-type yeast cells and phenocopies a RT ski mutant."; RL RNA 7:1566-1577(2001). RN [15] RP FUNCTION. RX PubMed=12769863; DOI=10.1016/s1097-2765(03)00190-4; RA Mitchell P., Tollervey D.; RT "An NMD pathway in yeast involving accelerated deadenylation and exosome- RT mediated 3'-->5' degradation."; RL Mol. Cell 11:1405-1413(2003). RN [16] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [17] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [18] RP FUNCTION. RX PubMed=14671320; DOI=10.1073/pnas.2536857100; RA Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M., RA Ahlquist P.; RT "Systematic, genome-wide identification of host genes affecting replication RT of a positive-strand RNA virus."; RL Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [22] RP MODELING OF THE SKI COMPLEX 3D-STRUCTURE. RX PubMed=15044803; DOI=10.1126/science.1092645; RA Aloy P., Boettcher B., Ceulemans H., Leutwein C., Mellwig C., Fischer S., RA Gavin A.-C., Bork P., Superti-Furga G., Serrano L., Russell R.B.; RT "Structure-based assembly of protein complexes in yeast."; RL Science 303:2026-2029(2004). CC -!- FUNCTION: RNA helicase component of the SKI complex involved in 3'-mRNA CC degradation pathway. Represses dsRNA virus propagation by specifically CC blocking translation of viral mRNAs, perhaps recognizing the absence of CC CAP or poly(A). Essential for cell growth only in the presence of M1 CC replicon. {ECO:0000269|PubMed:10611222, ECO:0000269|PubMed:10744028, CC ECO:0000269|PubMed:10922069, ECO:0000269|PubMed:11532933, CC ECO:0000269|PubMed:11720286, ECO:0000269|PubMed:12769863, CC ECO:0000269|PubMed:14671320, ECO:0000269|PubMed:363683, CC ECO:0000269|PubMed:6371496, ECO:0000269|PubMed:7739552, CC ECO:0000269|PubMed:7739557, ECO:0000269|PubMed:8321235, CC ECO:0000269|PubMed:9482746}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CC -!- SUBUNIT: Component of the SKI complex composed of at least SKI2, SKI3 CC and SKI8. The SKI complex interacts with SKI7, which makes the link CC between the SKI complex and the exosome in order to perform mRNA CC degradation. {ECO:0000269|PubMed:10744028}. CC -!- INTERACTION: CC P35207; P17883: SKI3; NbExp=11; IntAct=EBI-1851, EBI-1861; CC P35207; Q02793: SKI8; NbExp=11; IntAct=EBI-1851, EBI-17260; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10744028, CC ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 5770 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L13469; AAA35049.1; -; mRNA. DR EMBL; U19729; AAB82356.1; -; Genomic_DNA. DR EMBL; Z18944; CAA79378.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09699.1; -; Genomic_DNA. DR PIR; S55954; S55954. DR RefSeq; NP_013502.3; NM_001182286.3. DR PDB; 4A4K; X-ray; 3.25 A; A/C/E/G/I=835-1085. DR PDB; 4A4Z; X-ray; 2.40 A; A=296-1287. DR PDB; 4BUJ; X-ray; 3.70 A; A/E=1-208, A/E=301-834, A/E=1086-1287. DR PDB; 5MC6; EM; 3.80 A; h=1-1287. DR PDB; 8Q9T; EM; 2.84 A; A=1-1287. DR PDB; 8QCA; EM; 2.84 A; A=1-1287. DR PDB; 8QCB; EM; 2.80 A; A=1-1287. DR PDBsum; 4A4K; -. DR PDBsum; 4A4Z; -. DR PDBsum; 4BUJ; -. DR PDBsum; 5MC6; -. DR PDBsum; 8Q9T; -. DR PDBsum; 8QCA; -. DR PDBsum; 8QCB; -. DR AlphaFoldDB; P35207; -. DR EMDB; EMD-18288; -. DR EMDB; EMD-18326; -. DR EMDB; EMD-18328; -. DR EMDB; EMD-3461; -. DR SMR; P35207; -. DR BioGRID; 31657; 283. DR ComplexPortal; CPX-1040; SKI complex. DR DIP; DIP-5887N; -. DR IntAct; P35207; 15. DR MINT; P35207; -. DR STRING; 4932.YLR398C; -. DR iPTMnet; P35207; -. DR MaxQB; P35207; -. DR PaxDb; 4932-YLR398C; -. DR PeptideAtlas; P35207; -. DR EnsemblFungi; YLR398C_mRNA; YLR398C; YLR398C. DR GeneID; 851114; -. DR KEGG; sce:YLR398C; -. DR AGR; SGD:S000004390; -. DR SGD; S000004390; SKI2. DR VEuPathDB; FungiDB:YLR398C; -. DR eggNOG; KOG0947; Eukaryota. DR GeneTree; ENSGT00940000158255; -. DR HOGENOM; CLU_002902_1_4_1; -. DR InParanoid; P35207; -. DR OMA; CGSDITR; -. DR OrthoDB; 1352at2759; -. DR BioCyc; YEAST:G3O-32462-MONOMER; -. DR Reactome; R-SCE-429958; mRNA decay by 3' to 5' exoribonuclease. DR BioGRID-ORCS; 851114; 1 hit in 10 CRISPR screens. DR PRO; PR:P35207; -. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; P35207; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0055087; C:Ski complex; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003729; F:mRNA binding; HDA:SGD. DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:0006402; P:mRNA catabolic process; IDA:ComplexPortal. DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IMP:SGD. DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IDA:ComplexPortal. DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IMP:SGD. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR CDD; cd18795; SF2_C_Ski2; 1. DR Gene3D; 1.10.3380.30; -; 2. DR Gene3D; 2.30.30.1160; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR048392; MTR4-like_stalk. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR016438; SKI2-like. DR InterPro; IPR012961; Ski2/MTR4_C. DR InterPro; IPR048727; Ski2_beta-barrel. DR InterPro; IPR040801; Ski2_N. DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1. DR PANTHER; PTHR12131:SF8; HELICASE SKI2W; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF08148; DSHCT; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF21408; MTR4-like_stalk; 1. DR Pfam; PF21409; Ski2_beta-barrel; 1. DR Pfam; PF17911; Ski2_N; 1. DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM01142; DSHCT; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Antiviral defense; ATP-binding; Cytoplasm; DNA-binding; KW Helicase; Hydrolase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; RNA-binding; Translation regulation. FT CHAIN 1..1287 FT /note="Antiviral helicase SKI2" FT /id="PRO_0000102084" FT DOMAIN 338..496 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 638..815 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 540..608 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 556..577 FT /note="RNA-binding RGG-box" FT /evidence="ECO:0000250" FT MOTIF 444..447 FT /note="DEVH box" FT BINDING 351..358 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT CONFLICT 326 FT /note="W -> C (in Ref. 1; AAA35049)" FT /evidence="ECO:0000305" FT CONFLICT 759..760 FT /note="QM -> L (in Ref. 1; AAA35049)" FT /evidence="ECO:0000305" FT STRAND 302..305 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 315..318 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 332..342 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 346..350 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 358..370 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 374..380 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 382..384 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 385..393 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 401..404 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 414..420 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 421..430 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 434..437 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 438..443 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 458..464 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 470..475 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 481..492 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 496..500 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 508..514 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 517..522 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 530..540 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 613..623 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 628..632 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 636..644 FT /evidence="ECO:0007829|PDB:4A4Z" FT TURN 645..648 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 654..668 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 673..676 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 679..688 FT /evidence="ECO:0007829|PDB:4A4Z" FT TURN 689..691 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 692..695 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 701..712 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 717..721 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 724..727 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 734..739 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 741..745 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 748..751 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 754..761 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 762..764 FT /evidence="ECO:0007829|PDB:4A4Z" FT TURN 767..769 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 771..778 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 786..794 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 808..817 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 821..827 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 830..854 FT /evidence="ECO:0007829|PDB:4A4Z" FT TURN 862..864 FT /evidence="ECO:0007829|PDB:4A4K" FT STRAND 865..868 FT /evidence="ECO:0007829|PDB:4A4K" FT HELIX 871..889 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 895..898 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 903..908 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 914..923 FT /evidence="ECO:0007829|PDB:4A4Z" FT TURN 924..927 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 928..933 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 943..945 FT /evidence="ECO:0007829|PDB:4A4K" FT HELIX 955..961 FT /evidence="ECO:0007829|PDB:4A4Z" FT STRAND 971..976 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 977..979 FT /evidence="ECO:0007829|PDB:4A4K" FT STRAND 982..987 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 992..997 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1000..1015 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1031..1044 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1051..1053 FT /evidence="ECO:0007829|PDB:4A4K" FT HELIX 1061..1079 FT /evidence="ECO:0007829|PDB:4A4Z" FT TURN 1080..1082 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1088..1101 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1113..1118 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1126..1134 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1137..1140 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1143..1150 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1151..1153 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1169..1191 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1198..1202 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1203..1205 FT /evidence="ECO:0007829|PDB:4A4Z" FT TURN 1208..1211 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1212..1220 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1224..1229 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1235..1259 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1262..1275 FT /evidence="ECO:0007829|PDB:4A4Z" FT HELIX 1278..1281 FT /evidence="ECO:0007829|PDB:4A4Z" SQ SEQUENCE 1287 AA; 146059 MW; 7CCD36CFC0DF8C32 CRC64; MSEGFSSSSI QELYQSLKEI TNNADVELFE DRITKLDFES TDEPKHANDI IKDRFLRPSN ALPWSLLDMV QDVPHTSSPE DCSGKLDYKE LLKVPDPINR TSYQFKRTGL EGKISGYKEE VDLKEVANAN ASNSLSITRS INHNQNSVRG STAQLPFTPG GIPMKSVKTD SEQNGSSTMA NATKLLHKDG QGLFDIPEGM NRGIKPMDSP AENEDQNGQF KELKQLNEID NELDIRIEAN EAKLKEEEKS AKSISEEIME EATEETTADN ADDAEIDELL PIGIDFGRTK PVSKSVPVKK EWAHVVDLNH KIENFDELIP NPARSWPFEL DTFQKEAVYH LEQGDSVFVA AHTSAGKTVV AEYAIAMAHR NMTKTIYTSP IKALSNQKFR DFKETFDDVN IGLITGDVQI NPDANCLIMT TEILRSMLYR GADLIRDVEF VIFDEVHYVN DQDRGVVWEE VIIMLPQHVK FILLSATVPN TYEFANWIGR TKQKNIYVIS TPKRPVPLEI NIWAKKELIP VINQNSEFLE ANFRKHKEIL NGESAKGAPS KTDNGRGGST ARGGRGGSNT RDGRGGRGNS TRGGANRGGS RGAGAIGSNK RKFFTQDGPS KKTWPEIVNY LRKRELLPMV VFVFSKKRCE EYADWLEGIN FCNNKEKSQI HMFIEKSITR LKKEDRDLPQ ILKTRSLLER GIAVHHGGLL PIVKELIEIL FSKGFIKVLF ATETFAMGLN LPTRTVIFSS IRKHDGNGLR ELTPGEFTQM AGRAGRRGLD STGTVIVMAY NSPLSIATFK EVTMGVPTRL QSQFRLTYNM ILNLLRIEAL RVEEMIKYSF SENAKETLQP EHEKQIKVLQ EELQTIEYKS CEICDNDIEK FLELMLAYKE ATVNLMQEMV KSPSILHILK EGRLVAFRDP NDCLKLGFVF KVSLKDAVCV IMTFTKPYKL PNGEPNHLIY FPKADGYRRR NFPKFQKTDF YMEEVPVTAI EVITKRKFAA PLGKVIKKDV AALNEFNAET NNILDGKTLK EAINIEKQGL KIHQILLDRT NIRDEIFKLK SIKCPNLSQH IVPKFKAHVI KKKIEELYHL MSDQNLSLLP DYEKRLAVLK DTEFIDQNHN VLLKGRVACE INSGYELVLT ELILDNFLGS FEPEEIVALL SVFVYEGKTR EEEPPIVTPR LAKGKQRIEE IYKKMLCVFN THQIPLTQDE AEFLDRKRFA MMNVVYEWAR GLSFKEIMEM SPEAEGTVVR VITWLDEICR EVKTASIIIG NSTLHMKMSR AQELIKRDIV FAASLYL //