SKI2_YEAST
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 03-AUG-2022, entry version 201.
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}.
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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 PDBsum; 4A4K; -.
DR PDBsum; 4A4Z; -.
DR PDBsum; 4BUJ; -.
DR PDBsum; 5MC6; -.
DR AlphaFoldDB; P35207; -.
DR SMR; P35207; -.
DR BioGRID; 31657; 253.
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; P35207; -.
DR PRIDE; P35207; -.
DR EnsemblFungi; YLR398C_mRNA; YLR398C; YLR398C.
DR GeneID; 851114; -.
DR KEGG; sce:YLR398C; -.
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; DRNIWVH; -.
DR BioCyc; YEAST:G3O-32462-MON; -.
DR Reactome; R-SCE-429958; mRNA decay by 3' to 5' exoribonuclease.
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 GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR025696; rRNA_proc-arch_dom.
DR InterPro; IPR016438; Ski2-like.
DR InterPro; IPR012961; Ski2_C.
DR InterPro; IPR040801; Ski2_N.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13234; rRNA_proc-arch; 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; SSF52540; 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
