RRP6_YEAST
ID RRP6_YEAST Reviewed; 733 AA.
AC Q12149; D6W267; Q6B280;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Exosome complex exonuclease RRP6;
DE EC=3.1.13.-;
DE AltName: Full=Ribosomal RNA-processing protein 6;
GN Name=RRP6; Synonyms=UNC733; OrderedLocusNames=YOR001W;
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 [GENOMIC DNA].
RX PubMed=8896276;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1091::aid-yea22>3.0.co;2-i;
RA Sterky F., Holmberg A., Pettersson B., Uhlen M.;
RT "The sequence of a 30 kb fragment on the left arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 15 open reading frames, five of which
RT correspond to previously identified genes.";
RL Yeast 12:1091-1095(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=9582370; DOI=10.1074/jbc.273.21.13255;
RA Briggs M.W., Burkard K.T.D., Butler J.S.;
RT "Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is
RT essential for efficient 5.8 S rRNA 3' end formation.";
RL J. Biol. Chem. 273:13255-13263(1998).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE RNA EXOSOME COMPLEX BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=10465791; DOI=10.1101/gad.13.16.2148;
RA Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D.,
RA Mitchell P.;
RT "The yeast exosome and human PM-Scl are related complexes of 3'-->5'
RT exonucleases.";
RL Genes Dev. 13:2148-2158(1999).
RN [7]
RP CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH NPL3 AND PAP1, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=10611239; DOI=10.1128/mcb.20.2.604-616.2000;
RA Burkard K.T.D., Butler J.S.;
RT "A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with
RT Poly(A) polymerase and the hnRNA protein Npl3p.";
RL Mol. Cell. Biol. 20:604-616(2000).
RN [8]
RP INTERACTION WITH LRP1.
RX PubMed=12972615; DOI=10.1128/mcb.23.19.6982-6992.2003;
RA Mitchell P., Petfalski E., Houalla R., Podtelejnikov A., Mann M.,
RA Tollervey D.;
RT "Rrp47p is an exosome-associated protein required for the 3' processing of
RT stable RNAs.";
RL Mol. Cell. Biol. 23:6982-6992(2003).
RN [9]
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 [10]
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 [11]
RP FUNCTION, INTERACTION WITH LRP1, AND SUBCELLULAR LOCATION.
RX PubMed=15489286; DOI=10.1101/gad.1241204;
RA Hieronymus H., Yu M.C., Silver P.A.;
RT "Genome-wide mRNA surveillance is coupled to mRNA export.";
RL Genes Dev. 18:2652-2662(2004).
RN [12]
RP RECONSTITUTION OF THE RNA EXOSOME COMPLEX, AND EXONUCLEASE ACTIVITY.
RX PubMed=17174896; DOI=10.1016/j.cell.2006.10.037;
RA Liu Q., Greimann J.C., Lima C.D.;
RT "Reconstitution, activities, and structure of the eukaryotic RNA exosome.";
RL Cell 127:1223-1237(2006).
RN [13]
RP ERRATUM OF PUBMED:17174896.
RA Liu Q., Greimann J.C., Lima C.D.;
RL Cell 131:188-189(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-645, AND
RP IDENTIFICATION BY 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE RNA EXOSOME,
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=17173052; DOI=10.1038/nsmb1184;
RA Dziembowski A., Lorentzen E., Conti E., Seraphin B.;
RT "A single subunit, Dis3, is essentially responsible for yeast exosome core
RT activity.";
RL Nat. Struct. Mol. Biol. 14:15-22(2007).
RN [16]
RP INTERACTION WITH NOP53.
RX PubMed=18631361; DOI=10.1111/j.1742-4658.2008.06565.x;
RA Granato D.C., Machado-Santelli G.M., Oliveira C.C.;
RT "Nop53p interacts with 5.8S rRNA co-transcriptionally, and regulates
RT processing of pre-rRNA by the exosome.";
RL FEBS J. 275:4164-4178(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-520 AND SER-645, AND
RP IDENTIFICATION BY 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-645, AND
RP IDENTIFICATION BY 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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Nuclear-specific catalytic component of the RNA exosome
CC complex which has 3'->5' exoribonuclease activity and participates in a
CC multitude of cellular RNA processing and degradation events. In the
CC nucleus, the RNA exosome complex is involved in proper maturation of
CC stable RNA species such as rRNA, snRNA and snoRNA, in the elimination
CC of RNA processing by-products and non-coding 'pervasive' transcripts,
CC such as antisense RNA species and cryptic unstable transcripts (CUTs),
CC and of mRNAs with processing defects, thereby limiting or excluding
CC their export to the cytoplasm. The catalytic inactive RNA exosome core
CC complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the
CC binding and presentation of RNA for ribonucleolysis, and to serve as a
CC scaffold for the association with catalytic subunits and accessory
CC proteins or complexes. RRP6 has 3'-5' exonuclease activity which is not
CC modulated upon association with Exo-9 suggesting that the complex inner
CC RNA-binding path is not used to access its active site.
CC {ECO:0000269|PubMed:10465791, ECO:0000269|PubMed:10611239,
CC ECO:0000269|PubMed:15489286, ECO:0000269|PubMed:9582370}.
CC -!- SUBUNIT: Component of the RNA exosome complex. The catalytically
CC inactive RNA exosome core (Exo-9) complex associates with catalytic
CC subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome
CC complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-
CC containing subunits and peripheral S1 domain-containing components
CC CSL4, RRP4 and RRP40 located on the top of the ring structure. RRP6
CC specifically is part of the nuclear form of the RNA exosome complex;
CC the association appears to be mediated by Exo-9 and not by DIS3.
CC Interacts with LRP1. Interacts with NPL3, NOP53 and PAP1.
CC {ECO:0000269|PubMed:10465791, ECO:0000269|PubMed:10611239,
CC ECO:0000269|PubMed:12972615, ECO:0000269|PubMed:15489286,
CC ECO:0000269|PubMed:17173052, ECO:0000269|PubMed:18631361}.
CC -!- INTERACTION:
CC Q12149; P53617: NRD1; NbExp=4; IntAct=EBI-1782, EBI-12228;
CC Q12149; P46948: SKI6; NbExp=3; IntAct=EBI-1782, EBI-1788;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10465791,
CC ECO:0000269|PubMed:10611239, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15489286}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is impaired in growth at all
CC temperatures and is nonviable at 37 degrees Celsius. It is defective in
CC the 3' processing of the 5.8S rRNA and accumulates a discrete species,
CC 5.8S + 30, that is 3' extended by about 30 nucleotides. Deletion also
CC causes an accumulation of 7S RNA and 5' ETS and increases the level of
CC poly(A)+ mRNA. {ECO:0000269|PubMed:10465791,
CC ECO:0000269|PubMed:10611239, ECO:0000269|PubMed:17173052}.
CC -!- MISCELLANEOUS: Present with 2160 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the exosome component 10/RRP6 family.
CC {ECO:0000305}.
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DR EMBL; Z74909; CAA99189.1; -; Genomic_DNA.
DR EMBL; U43491; AAC49480.1; -; Genomic_DNA.
DR EMBL; AY692850; AAT92869.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10783.1; -; Genomic_DNA.
DR PIR; S61984; S61984.
DR RefSeq; NP_014643.1; NM_001183420.1.
DR PDB; 2HBJ; X-ray; 2.10 A; A=129-536.
DR PDB; 2HBK; X-ray; 2.25 A; A=129-536.
DR PDB; 2HBL; X-ray; 2.30 A; A=129-536.
DR PDB; 2HBM; X-ray; 2.70 A; A=129-536.
DR PDB; 4IFD; X-ray; 2.80 A; K=518-693.
DR PDB; 4OO1; X-ray; 3.30 A; J=129-685.
DR PDB; 4WFC; X-ray; 2.35 A; A/C/E=1-111.
DR PDB; 4WFD; X-ray; 2.40 A; A/D/G=1-111.
DR PDB; 5C0W; X-ray; 4.60 A; K=1-693.
DR PDB; 5C0X; X-ray; 3.81 A; K=1-693.
DR PDB; 5C0Y; X-ray; 2.10 A; A/B=122-518.
DR PDB; 5K36; X-ray; 3.10 A; J=129-684.
DR PDB; 5VZJ; X-ray; 3.30 A; J=129-684.
DR PDB; 6FSZ; EM; 4.60 A; KK=1-733.
DR PDB; 6FT6; EM; 3.90 A; KK=1-733.
DR PDB; 6LQS; EM; 3.80 A; r6=1-733.
DR PDB; 7D4I; EM; 4.00 A; r6=1-733.
DR PDBsum; 2HBJ; -.
DR PDBsum; 2HBK; -.
DR PDBsum; 2HBL; -.
DR PDBsum; 2HBM; -.
DR PDBsum; 4IFD; -.
DR PDBsum; 4OO1; -.
DR PDBsum; 4WFC; -.
DR PDBsum; 4WFD; -.
DR PDBsum; 5C0W; -.
DR PDBsum; 5C0X; -.
DR PDBsum; 5C0Y; -.
DR PDBsum; 5K36; -.
DR PDBsum; 5VZJ; -.
DR PDBsum; 6FSZ; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 7D4I; -.
DR AlphaFoldDB; Q12149; -.
DR SMR; Q12149; -.
DR BioGRID; 34404; 921.
DR ComplexPortal; CPX-599; Nuclear/nucleolar exosome complex, DIS3-RRP6 variant.
DR DIP; DIP-4560N; -.
DR IntAct; Q12149; 29.
DR MINT; Q12149; -.
DR STRING; 4932.YOR001W; -.
DR iPTMnet; Q12149; -.
DR MaxQB; Q12149; -.
DR PaxDb; Q12149; -.
DR PRIDE; Q12149; -.
DR EnsemblFungi; YOR001W_mRNA; YOR001W; YOR001W.
DR GeneID; 854162; -.
DR KEGG; sce:YOR001W; -.
DR SGD; S000005527; RRP6.
DR VEuPathDB; FungiDB:YOR001W; -.
DR eggNOG; KOG2206; Eukaryota.
DR GeneTree; ENSGT00390000015408; -.
DR HOGENOM; CLU_010129_3_2_1; -.
DR InParanoid; Q12149; -.
DR OMA; NRDQDWI; -.
DR BioCyc; YEAST:G3O-33552-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR EvolutionaryTrace; Q12149; -.
DR PRO; PR:Q12149; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12149; protein.
DR GO; GO:0000178; C:exosome (RNase complex); IPI:ComplexPortal.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:SGD.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:SGD.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0071044; P:histone mRNA catabolic process; IMP:SGD.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
DR GO; GO:0071040; P:nuclear polyadenylation-dependent antisense transcript catabolic process; IMP:SGD.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IMP:SGD.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IMP:SGD.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
DR GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IMP:SGD.
DR GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IMP:SGD.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IDA:SGD.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IMP:SGD.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:0006401; P:RNA catabolic process; IDA:ComplexPortal.
DR GO; GO:0006396; P:RNA processing; IDA:ComplexPortal.
DR GO; GO:0034473; P:U1 snRNA 3'-end processing; IMP:SGD.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IMP:SGD.
DR GO; GO:0034476; P:U5 snRNA 3'-end processing; IMP:SGD.
DR Gene3D; 1.10.150.80; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR012588; Exosome-assoc_fac_Rrp6_N.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR045092; Rrp6-like.
DR PANTHER; PTHR12124; PTHR12124; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF08066; PMC2NT; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00341; HRDC; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Exonuclease; Exosome; Hydrolase; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; rRNA processing.
FT CHAIN 1..733
FT /note="Exosome complex exonuclease RRP6"
FT /id="PRO_0000097456"
FT DOMAIN 435..515
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 662..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..733
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 520
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 402
FT /note="E -> G (in Ref. 4; AAT92869)"
FT /evidence="ECO:0000305"
FT HELIX 8..25
FT /evidence="ECO:0007829|PDB:4WFC"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:4WFC"
FT HELIX 36..60
FT /evidence="ECO:0007829|PDB:4WFC"
FT HELIX 76..105
FT /evidence="ECO:0007829|PDB:4WFC"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:2HBJ"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4OO1"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:2HBJ"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:2HBJ"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:2HBJ"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:2HBJ"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:2HBJ"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:2HBJ"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:2HBJ"
FT TURN 267..273
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:2HBJ"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:2HBJ"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:2HBJ"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:2HBJ"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:5K36"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 369..382
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 386..398
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:2HBJ"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:2HBJ"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:5C0Y"
FT HELIX 439..456
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 466..475
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 480..484
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 492..496
FT /evidence="ECO:0007829|PDB:2HBJ"
FT HELIX 498..515
FT /evidence="ECO:0007829|PDB:2HBJ"
FT TURN 534..536
FT /evidence="ECO:0007829|PDB:4IFD"
FT HELIX 539..553
FT /evidence="ECO:0007829|PDB:4IFD"
FT TURN 555..558
FT /evidence="ECO:0007829|PDB:4OO1"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:4IFD"
FT TURN 573..577
FT /evidence="ECO:0007829|PDB:4IFD"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:4IFD"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:5VZJ"
FT STRAND 591..594
FT /evidence="ECO:0007829|PDB:4IFD"
FT HELIX 596..611
FT /evidence="ECO:0007829|PDB:4IFD"
FT HELIX 612..614
FT /evidence="ECO:0007829|PDB:4IFD"
FT STRAND 617..619
FT /evidence="ECO:0007829|PDB:4IFD"
SQ SEQUENCE 733 AA; 84039 MW; B19A0B2ED74C6DA7 CRC64;
MTSENPDVLL SRVINVVRAA SSLASQDVDF YKNLDRGFSK DLKSKADKLA DMANEIILSI
DEHHESFELK EEDISDLWNN FGNIMDNLLE MSDHSLDKLN CAINSKSRGS DLQYLGEFSG
KNFSPTKRVE KPQLKFKSPI DNSESHPFIP LLKEKPNALK PLSESLRLVD DDENNPSHYP
HPYEYEIDHQ EYSPEILQIR EEIPSKSWDD SVPIWVDTST ELESMLEDLK NTKEIAVDLE
HHDYRSYYGI VCLMQISTRE RDYLVDTLKL RENLHILNEV FTNPSIVKVF HGAFMDIIWL
QRDLGLYVVG LFDTYHASKA IGLPRHSLAY LLENFANFKT SKKYQLADWR IRPLSKPMTA
YARADTHFLL NIYDQLRNKL IESNKLAGVL YESRNVAKRR FEYSKYRPLT PSSEVYSPIE
KESPWKILMY QYNIPPEREV LVRELYQWRD LIARRDDESP RFVMPNQLLA ALVAYTPTDV
IGVVSLTNGV TEHVRQNAKL LANLIRDALR NIKNTNEEAT PIPSSETKAD GILLETISVP
QIRDVMERFS VLCNSNISKS RAKPVTNSSI LLGKILPREE HDIAYSKDGL PNKVKTEDIR
IRAQNFKSAL ANLEDIIFEI EKPLVVPVKL EEIKTVDPAS APNHSPEIDN LDDLVVLKKK
NIQKKQPAKE KGVTEKDAVD YSKIPNILSN KPGQNNRQQK KRRFDPSSSD SNGPRAAKKR
RPAAKGKNLS FKR
