RRP44_YEAST
ID RRP44_YEAST Reviewed; 1001 AA.
AC Q08162; D6W244;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Exosome complex exonuclease DIS3;
DE EC=3.1.13.-;
DE EC=3.1.26.-;
DE AltName: Full=Chromosome disjunction protein 3;
DE AltName: Full=Ribosomal RNA-processing protein 44;
GN Name=DIS3; Synonyms=RRP44; OrderedLocusNames=YOL021C; ORFNames=O2197;
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], FUNCTION, AND INTERACTION WITH GSP1.
RX PubMed=8896453; DOI=10.1002/j.1460-2075.1996.tb00944.x;
RA Noguchi E., Hayashi N., Azuma Y., Seki T., Nakamura M., Nakashima N.,
RA Yanagida M., He X., Mueller U., Sazer S., Nishimoto T.;
RT "Dis3, implicated in mitotic control, binds directly to Ran and enhances
RT the GEF activity of RCC1.";
RL EMBO J. 15:5595-5605(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 IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION, AND
RP SUBUNIT.
RX PubMed=9390555; DOI=10.1016/s0092-8674(00)80432-8;
RA Mitchell P., Petfalski E., Shevchenko A., Mann M., Tollervey D.;
RT "The exosome: a conserved eukaryotic RNA processing complex containing
RT multiple 3'-->5' exoribonucleases.";
RL Cell 91:457-466(1997).
RN [5]
RP IDENTIFICATION IN THE EXOSOME COMPLEX BY MASS SPECTROMETRY.
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 [6]
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 [7]
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 [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [9]
RP EXOSOME EXONUCLEASE ACTIVITY, AND SUBUNIT.
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION,
RP COFACTOR, INTERACTION OF THE EXOSOME WITH RRP6 AND SKI7, SUBUNIT, AND
RP MUTAGENESIS OF ASP-551.
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 [11]
RP CATALYTIC ACTIVITY AS ENDONUCLEASE, AND MUTAGENESIS OF CYS-47; CYS-52;
RP CYS-55; ASP-171; ASP-198 AND ASP-551.
RX PubMed=19060898; DOI=10.1038/nsmb.1528;
RA Schaeffer D., Tsanova B., Barbas A., Reis F.P., Dastidar E.G.,
RA Sanchez-Rotunno M., Arraiano C.M., van Hoof A.;
RT "The exosome contains domains with specific endoribonuclease,
RT exoribonuclease and cytoplasmic mRNA decay activities.";
RL Nat. Struct. Mol. Biol. 16:56-62(2009).
RN [12]
RP CATALYTIC ACTIVITY, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 242-1001 IN
RP COMPLEX WITH SINGLE-STRANDED RNA AND MAGNESIUM ION, AND MUTAGENESIS OF
RP ASP-551.
RX PubMed=18374646; DOI=10.1016/j.molcel.2008.02.018;
RA Lorentzen E., Basquin J., Tomecki R., Dziembowski A., Conti E.;
RT "Structure of the active subunit of the yeast exosome core, Rrp44: diverse
RT modes of substrate recruitment in the RNase II nuclease family.";
RL Mol. Cell 29:717-728(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH SKI6 AND RRP45.
RX PubMed=19879841; DOI=10.1016/j.cell.2009.08.042;
RA Bonneau F., Basquin J., Ebert J., Lorentzen E., Conti E.;
RT "The yeast exosome functions as a macromolecular cage to channel RNA
RT substrates for degradation.";
RL Cell 139:547-559(2009).
CC -!- FUNCTION: Catalytic component of the RNA exosome complex which has
CC 3'->5' exoribonuclease activity and participates in a multitude of
CC cellular RNA processing and degradation events. In the nucleus, the RNA
CC exosome complex is involved in proper maturation of stable RNA species
CC such as rRNA, snRNA and snoRNA, in the elimination of RNA processing
CC by-products and non-coding 'pervasive' transcripts, such as antisense
CC RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with
CC processing defects, thereby limiting or excluding their export to the
CC cytoplasm. In the cytoplasm, the RNA exosome complex is involved in
CC general mRNA turnover and in RNA surveillance pathways, preventing
CC translation of aberrant mRNAs. 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. DIS3 has both 3'-5' exonuclease and endonuclease
CC activities. The exonuclease activity of DIS3 is down-regulated upon
CC association with Exo-9 possibly involving a conformational change in
CC the catalytic domain and threading of the RNA substrate through the
CC complex central channel. Structured substrates can be degraded if they
CC have a 3' single-stranded extension sufficiently long (such as 35 nt
CC poly(A)) to span the proposed complex inner RNA-binding path and to
CC reach the exonuclease site provided by DIS3. Plays a role in mitotic
CC control. {ECO:0000269|PubMed:17173052, ECO:0000269|PubMed:8896453,
CC ECO:0000269|PubMed:9390555}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17173052};
CC -!- SUBUNIT: Component of the RNA exosome complex. The catalytically
CC inactive RNA exosome core (Exo-9) complex which is believed to
CC associate with catalytic subunits DIS3 and RRP6 in cytoplasmic- and
CC nuclear-specific RNA exosome complex forms. Exo-9 is formed by a
CC hexameric ring of RNase PH domain-containing subunits and peripheral S1
CC domain-containing components CSL4, RRP4 and RRP40 located on the top of
CC the ring structure. DIS3 associates at the respective bottom side with
CC Exo-9. Interacts with GSP1. {ECO:0000269|PubMed:10465791,
CC ECO:0000269|PubMed:17173052, ECO:0000269|PubMed:17174896,
CC ECO:0000269|PubMed:18374646, ECO:0000269|PubMed:19879841,
CC ECO:0000269|PubMed:8896453, ECO:0000269|PubMed:9390555}.
CC -!- INTERACTION:
CC Q08162; P38792: RRP4; NbExp=5; IntAct=EBI-1740, EBI-1757;
CC Q08162; Q08285: RRP40; NbExp=3; IntAct=EBI-1740, EBI-1831;
CC Q08162; P53256: RRP46; NbExp=5; IntAct=EBI-1740, EBI-1842;
CC Q08162; P46948: SKI6; NbExp=9; IntAct=EBI-1740, EBI-1788;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Mitochondrion {ECO:0000269|PubMed:14576278}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Mn(2+) doesn't support the hydrolytic activity. Activity
CC is KCl or NaCl dependent and activity is slightly increased in the
CC presence of reducing agents such as DTT or beta-mercaptoethanol and
CC doesn't vary notably between pH 6.8 and 8.8.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
CC -!- CAUTION: It was originally thought that there are multiple subunits in
CC the exosome that have exonuclease activity but it was later shown
CC (PubMed:17173052 and PubMed:17174896) that only this DIS3/RRP44 subunit
CC of the exosome core has this activity. {ECO:0000305|PubMed:9390555}.
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DR EMBL; D76430; BAA11176.1; -; Genomic_DNA.
DR EMBL; Z74763; CAA99021.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10760.1; -; Genomic_DNA.
DR PIR; S66704; S66704.
DR RefSeq; NP_014621.1; NM_001183275.1.
DR PDB; 2VNU; X-ray; 2.30 A; D=242-1001.
DR PDB; 2WP8; X-ray; 3.00 A; J=25-1001.
DR PDB; 4IFD; X-ray; 2.80 A; J=1-1001.
DR PDB; 5C0W; X-ray; 4.60 A; J=1-1001.
DR PDB; 5C0X; X-ray; 3.81 A; J=1-1001.
DR PDB; 5G06; EM; 4.20 A; J=1-1001.
DR PDB; 5JEA; X-ray; 2.65 A; J=1-1001.
DR PDB; 5K36; X-ray; 3.10 A; K=1-1001.
DR PDB; 5VZJ; X-ray; 3.30 A; K=1-1001.
DR PDB; 6FSZ; EM; 4.60 A; JJ=1-1001.
DR PDB; 6LQS; EM; 3.80 A; R4=1-1001.
DR PDB; 7AJT; EM; 4.60 A; EK=1-1001.
DR PDB; 7AJU; EM; 3.80 A; EK=1-1001.
DR PDB; 7D4I; EM; 4.00 A; R4=1-1001.
DR PDBsum; 2VNU; -.
DR PDBsum; 2WP8; -.
DR PDBsum; 4IFD; -.
DR PDBsum; 5C0W; -.
DR PDBsum; 5C0X; -.
DR PDBsum; 5G06; -.
DR PDBsum; 5JEA; -.
DR PDBsum; 5K36; -.
DR PDBsum; 5VZJ; -.
DR PDBsum; 6FSZ; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR AlphaFoldDB; Q08162; -.
DR SMR; Q08162; -.
DR BioGRID; 34381; 241.
DR ComplexPortal; CPX-599; Nuclear/nucleolar exosome complex, DIS3-RRP6 variant.
DR ComplexPortal; CPX-603; Cytoplasmic exosome complex, DIS3 variant.
DR DIP; DIP-2355N; -.
DR IntAct; Q08162; 24.
DR MINT; Q08162; -.
DR STRING; 4932.YOL021C; -.
DR MaxQB; Q08162; -.
DR PaxDb; Q08162; -.
DR PRIDE; Q08162; -.
DR EnsemblFungi; YOL021C_mRNA; YOL021C; YOL021C.
DR GeneID; 854138; -.
DR KEGG; sce:YOL021C; -.
DR SGD; S000005381; DIS3.
DR VEuPathDB; FungiDB:YOL021C; -.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00530000063106; -.
DR HOGENOM; CLU_002333_5_0_1; -.
DR InParanoid; Q08162; -.
DR OMA; VVKRNWR; -.
DR BioCyc; YEAST:G3O-33437-MON; -.
DR BRENDA; 3.1.13.1; 984.
DR Reactome; R-SCE-429958; mRNA decay by 3' to 5' exoribonuclease.
DR Reactome; R-SCE-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-SCE-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR EvolutionaryTrace; Q08162; -.
DR PRO; PR:Q08162; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08162; protein.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IDA:SGD.
DR GO; GO:0000178; C:exosome (RNase complex); IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
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:ComplexPortal.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:SGD.
DR GO; GO:0004519; F:endonuclease activity; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IDA:SGD.
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:0006397; P:mRNA processing; IMP:SGD.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IMP:SGD.
DR GO; GO:0071028; P:nuclear mRNA surveillance; 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; IC:SGD.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IDA:SGD.
DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IC:SGD.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IC:SGD.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IC:SGD.
DR GO; GO:0006401; P:RNA catabolic process; IDA:ComplexPortal.
DR GO; GO:0006396; P:RNA processing; IDA:ComplexPortal.
DR GO; GO:0016075; P:rRNA catabolic process; IMP:SGD.
DR GO; GO:0043628; P:small regulatory ncRNA 3'-end processing; IMP:SGD.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR033771; Rrp44_CSD1.
DR InterPro; IPR033770; RRP44_S1.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF13638; PIN_4; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF17216; Rrp44_CSD1; 1.
DR Pfam; PF17215; Rrp44_S1; 1.
DR SMART; SM00670; PINc; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 4.
DR SUPFAM; SSF88723; SSF88723; 1.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Exonuclease; Exosome; Hydrolase;
KW Mitochondrion; Nuclease; Nucleus; Reference proteome; RNA-binding;
KW rRNA processing.
FT CHAIN 1..1001
FT /note="Exosome complex exonuclease DIS3"
FT /id="PRO_0000166423"
FT DOMAIN 904..1001
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 1..235
FT /note="Endoribonuclease"
FT REGION 343..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 47
FT /note="C->S: Slow growth; when associated with S-52 and S-
FT 55."
FT /evidence="ECO:0000269|PubMed:19060898"
FT MUTAGEN 52
FT /note="C->S: Slow growth; when associated with S-47 and S-
FT 55."
FT /evidence="ECO:0000269|PubMed:19060898"
FT MUTAGEN 55
FT /note="C->S: Slow growth; when associated with S-47 and S-
FT 52."
FT /evidence="ECO:0000269|PubMed:19060898"
FT MUTAGEN 171
FT /note="D->A: Abolishes endoribonucleolytic activity; no
FT effect on growth. No growth; when associated with N-551."
FT /evidence="ECO:0000269|PubMed:19060898"
FT MUTAGEN 198
FT /note="D->A: Abolishes endoribonucleolytic activity; no
FT effect on growth. No growth; when associated with N-551."
FT /evidence="ECO:0000269|PubMed:19060898"
FT MUTAGEN 551
FT /note="D->N: Exoribonucleolytic activity abolished.
FT Accumulation of partially processed 5.8S rRNA and partially
FT degraded 5' ETS. No growth; when associated with A-171. No
FT growth; when associated with A-198."
FT /evidence="ECO:0000269|PubMed:17173052,
FT ECO:0000269|PubMed:18374646, ECO:0000269|PubMed:19060898"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:5K36"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 33..43
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4IFD"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:5JEA"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:4IFD"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:5JEA"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2WP8"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:5JEA"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:5JEA"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 166..185
FT /evidence="ECO:0007829|PDB:5JEA"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:4IFD"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:5K36"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:4IFD"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2VNU"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 367..383
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 389..397
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 420..428
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 447..455
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:5K36"
FT STRAND 464..475
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 478..487
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 497..500
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 519..524
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 526..530
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 540..546
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 552..558
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 564..571
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 573..576
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:2WP8"
FT HELIX 582..590
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:2WP8"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:2WP8"
FT HELIX 606..609
FT /evidence="ECO:0007829|PDB:2VNU"
FT TURN 610..612
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 619..630
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 636..653
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 654..662
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:4IFD"
FT HELIX 669..690
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 701..705
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 707..710
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 712..717
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 722..745
FT /evidence="ECO:0007829|PDB:2VNU"
FT TURN 747..749
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 751..755
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 760..763
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 764..774
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 783..791
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 801..810
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 817..820
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 821..823
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 826..829
FT /evidence="ECO:0007829|PDB:2VNU"
FT TURN 832..835
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 836..838
FT /evidence="ECO:0007829|PDB:2WP8"
FT TURN 845..847
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 849..861
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 869..872
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 874..908
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 912..922
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 925..929
FT /evidence="ECO:0007829|PDB:2VNU"
FT TURN 931..933
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 936..940
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 941..944
FT /evidence="ECO:0007829|PDB:2VNU"
FT HELIX 948..950
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 952..954
FT /evidence="ECO:0007829|PDB:2VNU"
FT TURN 955..958
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 959..962
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 964..967
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 971..974
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 978..983
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 985..987
FT /evidence="ECO:0007829|PDB:4IFD"
FT TURN 989..991
FT /evidence="ECO:0007829|PDB:4IFD"
FT STRAND 995..997
FT /evidence="ECO:0007829|PDB:2VNU"
FT STRAND 998..1000
FT /evidence="ECO:0007829|PDB:5JEA"
SQ SEQUENCE 1001 AA; 113707 MW; 00DD31BD2D6904F4 CRC64;
MSVPAIAPRR KRLADGLSVT QKVFVRSRNG GATKIVREHY LRSDIPCLSR SCTKCPQIVV
PDAQNELPKF ILSDSPLELS APIGKHYVVL DTNVVLQAID LLENPNCFFD VIVPQIVLDE
VRNKSYPVYT RLRTLCRDSD DHKRFIVFHN EFSEHTFVER LPNETINDRN DRAIRKTCQW
YSEHLKPYDI NVVLVTNDRL NREAATKEVE SNIITKSLVQ YIELLPNADD IRDSIPQMDS
FDKDLERDTF SDFTFPEYYS TARVMGGLKN GVLYQGNIQI SEYNFLEGSV SLPRFSKPVL
IVGQKNLNRA FNGDQVIVEL LPQSEWKAPS SIVLDSEHFD VNDNPDIEAG DDDDNNESSS
NTTVISDKQR RLLAKDAMIA QRSKKIQPTA KVVYIQRRSW RQYVGQLAPS SVDPQSSSTQ
NVFVILMDKC LPKVRIRTRR AAELLDKRIV ISIDSWPTTH KYPLGHFVRD LGTIESAQAE
TEALLLEHDV EYRPFSKKVL ECLPAEGHDW KAPTKLDDPE AVSKDPLLTK RKDLRDKLIC
SIDPPGCVDI DDALHAKKLP NGNWEVGVHI ADVTHFVKPG TALDAEGAAR GTSVYLVDKR
IDMLPMLLGT DLCSLKPYVD RFAFSVIWEL DDSANIVNVN FMKSVIRSRE AFSYEQAQLR
IDDKTQNDEL TMGMRALLKL SVKLKQKRLE AGALNLASPE VKVHMDSETS DPNEVEIKKL
LATNSLVEEF MLLANISVAR KIYDAFPQTA MLRRHAAPPS TNFEILNEML NTRKNMSISL
ESSKALADSL DRCVDPEDPY FNTLVRIMST RCMMAAQYFY SGAYSYPDFR HYGLAVDIYT
HFTSPIRRYC DVVAHRQLAG AIGYEPLSLT HRDKNKMDMI CRNINRKHRN AQFAGRASIE
YYVGQVMRNN ESTETGYVIK VFNNGIVVLV PKFGVEGLIR LDNLTEDPNS AAFDEVEYKL
TFVPTNSDKP RDVYVFDKVE VQVRSVMDPI TSKRKAELLL K
