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Exosome complex exonuclease DIS3 (EC 3.1.13.-) (EC 3.1.26.-) (Chromosome disjunction protein 3) (Ribosomal RNA-processing protein 44)

 RRP44_YEAST             Reviewed;        1001 AA.
Q08162; D6W244;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
25-OCT-2017, entry version 151.
RecName: Full=Exosome complex exonuclease DIS3;
EC=3.1.13.-;
EC=3.1.26.-;
AltName: Full=Chromosome disjunction protein 3;
AltName: Full=Ribosomal RNA-processing protein 44;
Name=DIS3; Synonyms=RRP44; OrderedLocusNames=YOL021C; ORFNames=O2197;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH
GSP1.
PubMed=8896453;
Noguchi E., Hayashi N., Azuma Y., Seki T., Nakamura M., Nakashima N.,
Yanagida M., He X., Mueller U., Sazer S., Nishimoto T.;
"Dis3, implicated in mitotic control, binds directly to Ran and
enhances the GEF activity of RCC1.";
EMBO J. 15:5595-5605(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION, AND
SUBUNIT.
PubMed=9390555; DOI=10.1016/S0092-8674(00)80432-8;
Mitchell P., Petfalski E., Shevchenko A., Mann M., Tollervey D.;
"The exosome: a conserved eukaryotic RNA processing complex containing
multiple 3'-->5' exoribonucleases.";
Cell 91:457-466(1997).
[5]
IDENTIFICATION IN THE EXOSOME COMPLEX BY MASS SPECTROMETRY.
PubMed=10465791; DOI=10.1101/gad.13.16.2148;
Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D.,
Mitchell P.;
"The yeast exosome and human PM-Scl are related complexes of 3'-->5'
exonucleases.";
Genes Dev. 13:2148-2158(1999).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[9]
EXOSOME EXONUCLEASE ACTIVITY, AND SUBUNIT.
PubMed=17174896; DOI=10.1016/j.cell.2006.10.037;
Liu Q., Greimann J.C., Lima C.D.;
"Reconstitution, activities, and structure of the eukaryotic RNA
exosome.";
Cell 127:1223-1237(2006).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823961; DOI=10.1021/pr050477f;
Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
"Toward the complete yeast mitochondrial proteome: multidimensional
separation techniques for mitochondrial proteomics.";
J. Proteome Res. 5:1543-1554(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION,
COFACTOR, INTERACTION OF THE EXOSOME WITH RRP6 AND SKI7, SUBUNIT, AND
MUTAGENESIS OF ASP-551.
PubMed=17173052; DOI=10.1038/nsmb1184;
Dziembowski A., Lorentzen E., Conti E., Seraphin B.;
"A single subunit, Dis3, is essentially responsible for yeast exosome
core activity.";
Nat. Struct. Mol. Biol. 14:15-22(2007).
[12]
CATALYTIC ACTIVITY AS ENDONUCLEASE, AND MUTAGENESIS OF CYS-47; CYS-52;
CYS-55; ASP-171; ASP-198 AND ASP-551.
PubMed=19060898; DOI=10.1038/nsmb.1528;
Schaeffer D., Tsanova B., Barbas A., Reis F.P., Dastidar E.G.,
Sanchez-Rotunno M., Arraiano C.M., van Hoof A.;
"The exosome contains domains with specific endoribonuclease,
exoribonuclease and cytoplasmic mRNA decay activities.";
Nat. Struct. Mol. Biol. 16:56-62(2009).
[13]
CATALYTIC ACTIVITY, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 242-1001
IN COMPLEX WITH SINGLE-STRANDED RNA AND MAGNESIUM ION, AND MUTAGENESIS
OF ASP-551.
PubMed=18374646; DOI=10.1016/j.molcel.2008.02.018;
Lorentzen E., Basquin J., Tomecki R., Dziembowski A., Conti E.;
"Structure of the active subunit of the yeast exosome core, Rrp44:
diverse modes of substrate recruitment in the RNase II nuclease
family.";
Mol. Cell 29:717-728(2008).
[14]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH SKI6 AND RRP45.
PubMed=19879841; DOI=10.1016/j.cell.2009.08.042;
Bonneau F., Basquin J., Ebert J., Lorentzen E., Conti E.;
"The yeast exosome functions as a macromolecular cage to channel RNA
substrates for degradation.";
Cell 139:547-559(2009).
-!- FUNCTION: Catalytic component of the RNA exosome complex which has
3'->5' exoribonuclease activity and participates in a multitude of
cellular RNA processing and degradation events. In the nucleus,
the RNA exosome complex is involved in proper maturation of stable
RNA species such as rRNA, snRNA and snoRNA, in the elimination of
RNA processing by-products and non-coding 'pervasive' transcripts,
such as antisense RNA species and cryptic unstable transcripts
(CUTs), and of mRNAs with processing defects, thereby limiting or
excluding their export to the cytoplasm. In the cytoplasm, the RNA
exosome complex is involved in general mRNA turnover and in RNA
surveillance pathways, preventing translation of aberrant mRNAs.
The catalytic inactive RNA exosome core complex of 9 subunits
(Exo-9) is proposed to play a pivotal role in the binding and
presentation of RNA for ribonucleolysis, and to serve as a
scaffold for the association with catalytic subunits and accessory
proteins or complexes. DIS3 has both 3'-5' exonuclease and
endonuclease activities. The exonuclease activity of DIS3 is down-
regulated upon association with Exo-9 possibly involving a
conformational change in the catalytic domain and threading of the
RNA substrate through the complex central channel. Structured
substrates can be degraded if they have a 3' single-stranded
extension sufficiently long (such as 35 nt poly(A)) to span the
proposed complex inner RNA-binding path and to reach the
exonuclease site provided by DIS3. Plays a role in mitotic
control. {ECO:0000269|PubMed:17173052, ECO:0000269|PubMed:8896453,
ECO:0000269|PubMed:9390555}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17173052};
-!- SUBUNIT: Component of the RNA exosome complex. The catalytically
inactive RNA exosome core (Exo-9) complex which is believed to
associate with catalytic subunits DIS3 and RRP6 in
cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9
is formed by a hexameric ring of RNase PH domain-containing
subunits and peripheral S1 domain-containing components CSL4, RRP4
and RRP40 located on the top of the ring structure. DIS3
associates at the respective bottom side with Exo-9. Interacts
with GSP1. {ECO:0000269|PubMed:10465791,
ECO:0000269|PubMed:17173052, ECO:0000269|PubMed:17174896,
ECO:0000269|PubMed:18374646, ECO:0000269|PubMed:19879841,
ECO:0000269|PubMed:8896453, ECO:0000269|PubMed:9390555}.
-!- INTERACTION:
P38792:RRP4; NbExp=5; IntAct=EBI-1740, EBI-1757;
Q08285:RRP40; NbExp=3; IntAct=EBI-1740, EBI-1831;
P53256:RRP46; NbExp=5; IntAct=EBI-1740, EBI-1842;
P46948:SKI6; NbExp=9; IntAct=EBI-1740, EBI-1788;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Mitochondrion {ECO:0000269|PubMed:14576278,
ECO:0000269|PubMed:16823961}. Nucleus, nucleolus
{ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: Mn(2+) doesn't support the hydrolytic activity.
Activity is KCl or NaCl dependent and activity is slightly
increased in the presence of reducing agents such as DTT or beta-
mercaptoethanol and doesn't vary notably between pH 6.8 and 8.8.
-!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
-!- CAUTION: It was originally thought that there are multiple
subunits in the exosome that have exonuclease activity but it was
later shown (PubMed:17173052 and PubMed:17174896) that only this
DIS3/RRP44 subunit of the exosome core has this activity.
{ECO:0000305|PubMed:9390555}.
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EMBL; D76430; BAA11176.1; -; Genomic_DNA.
EMBL; Z74763; CAA99021.1; -; Genomic_DNA.
EMBL; BK006948; DAA10760.1; -; Genomic_DNA.
PIR; S66704; S66704.
RefSeq; NP_014621.1; NM_001183275.1.
PDB; 2VNU; X-ray; 2.30 A; D=242-1001.
PDB; 2WP8; X-ray; 3.00 A; J=25-1001.
PDB; 4IFD; X-ray; 2.80 A; J=1-1001.
PDB; 5C0W; X-ray; 4.60 A; J=1-1001.
PDB; 5C0X; X-ray; 3.81 A; J=1-1001.
PDB; 5G06; EM; 4.20 A; J=1-1001.
PDB; 5JEA; X-ray; 2.65 A; J=1-1001.
PDB; 5K36; X-ray; 3.10 A; K=1-1001.
PDB; 5VZJ; X-ray; 3.30 A; K=1-1001.
PDBsum; 2VNU; -.
PDBsum; 2WP8; -.
PDBsum; 4IFD; -.
PDBsum; 5C0W; -.
PDBsum; 5C0X; -.
PDBsum; 5G06; -.
PDBsum; 5JEA; -.
PDBsum; 5K36; -.
PDBsum; 5VZJ; -.
ProteinModelPortal; Q08162; -.
SMR; Q08162; -.
BioGrid; 34381; 204.
DIP; DIP-2355N; -.
IntAct; Q08162; 22.
MINT; MINT-614156; -.
STRING; 4932.YOL021C; -.
MaxQB; Q08162; -.
PRIDE; Q08162; -.
EnsemblFungi; YOL021C; YOL021C; YOL021C.
GeneID; 854138; -.
KEGG; sce:YOL021C; -.
EuPathDB; FungiDB:YOL021C; -.
SGD; S000005381; DIS3.
GeneTree; ENSGT00530000063106; -.
HOGENOM; HOG000191945; -.
InParanoid; Q08162; -.
KO; K12585; -.
OMA; WRQYVGH; -.
OrthoDB; EOG092C0VEN; -.
BioCyc; YEAST:G3O-33437-MONOMER; -.
BRENDA; 3.1.13.1; 984.
Reactome; R-SCE-429958; mRNA decay by 3' to 5' exoribonuclease.
EvolutionaryTrace; Q08162; -.
PRO; PR:Q08162; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IDA:SGD.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:SGD.
GO; GO:0005730; C:nucleolus; IDA:SGD.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:SGD.
GO; GO:0004521; F:endoribonuclease activity; IDA:SGD.
GO; GO:0000049; F:tRNA binding; IDA:SGD.
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.
GO; GO:0043628; P:ncRNA 3'-end processing; IMP:SGD.
GO; GO:0070651; P:nonfunctional rRNA decay; IMP:SGD.
GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IMP:SGD.
GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IC:SGD.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IDA:SGD.
GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IC:SGD.
GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IC:SGD.
GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IC:SGD.
GO; GO:0016075; P:rRNA catabolic process; IMP:SGD.
Gene3D; 3.40.50.1010; -; 1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR002716; PIN_dom.
InterPro; IPR029060; PIN_domain-like.
InterPro; IPR022966; RNase_II/R_CS.
InterPro; IPR033771; Rrp44_CSD1.
InterPro; IPR033770; RRP44_S1.
InterPro; IPR022967; S1_dom.
InterPro; IPR003029; S1_domain.
Pfam; PF13638; PIN_4; 1.
Pfam; PF17216; Rrp44_CSD1; 1.
Pfam; PF17215; Rrp44_S1; 1.
SMART; SM00670; PINc; 1.
SMART; SM00316; S1; 1.
SUPFAM; SSF50249; SSF50249; 4.
SUPFAM; SSF88723; SSF88723; 1.
PROSITE; PS01175; RIBONUCLEASE_II; 1.
PROSITE; PS50126; S1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Endonuclease; Exonuclease;
Exosome; Hydrolase; Mitochondrion; Nuclease; Nucleus;
Reference proteome; RNA-binding; rRNA processing.
CHAIN 1 1001 Exosome complex exonuclease DIS3.
/FTId=PRO_0000166423.
DOMAIN 904 1001 S1 motif. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
REGION 1 235 Endoribonuclease.
MUTAGEN 47 47 C->S: Slow growth; when associated with
S-52 and S-55.
{ECO:0000269|PubMed:19060898}.
MUTAGEN 52 52 C->S: Slow growth; when associated with
S-47 and S-55.
{ECO:0000269|PubMed:19060898}.
MUTAGEN 55 55 C->S: Slow growth; when associated with
S-47 and S-52.
{ECO:0000269|PubMed:19060898}.
MUTAGEN 171 171 D->A: Abolishes endoribonucleolytic
activity; no effect on growth. No growth;
when associated with N-551.
{ECO:0000269|PubMed:19060898}.
MUTAGEN 198 198 D->A: Abolishes endoribonucleolytic
activity; no effect on growth. No growth;
when associated with N-551.
{ECO:0000269|PubMed:19060898}.
MUTAGEN 551 551 D->N: Exoribonucleolytic activity
abolished. Accumulation of partially
processed 5.8S rRNA and partially
degraded 5' ETS. No growth; when
associated with A-171. No growth; when
associated with A-198.
{ECO:0000269|PubMed:17173052,
ECO:0000269|PubMed:18374646,
ECO:0000269|PubMed:19060898}.
STRAND 10 12 {ECO:0000244|PDB:5K36}.
STRAND 14 16 {ECO:0000244|PDB:5JEA}.
STRAND 18 26 {ECO:0000244|PDB:5JEA}.
STRAND 33 43 {ECO:0000244|PDB:5JEA}.
STRAND 49 51 {ECO:0000244|PDB:4IFD}.
HELIX 55 58 {ECO:0000244|PDB:5JEA}.
TURN 80 83 {ECO:0000244|PDB:4IFD}.
STRAND 85 90 {ECO:0000244|PDB:5JEA}.
HELIX 92 102 {ECO:0000244|PDB:5JEA}.
TURN 105 107 {ECO:0000244|PDB:2WP8}.
STRAND 110 114 {ECO:0000244|PDB:5JEA}.
HELIX 115 124 {ECO:0000244|PDB:5JEA}.
HELIX 126 137 {ECO:0000244|PDB:5JEA}.
STRAND 144 148 {ECO:0000244|PDB:5JEA}.
TURN 150 152 {ECO:0000244|PDB:5JEA}.
TURN 154 156 {ECO:0000244|PDB:5JEA}.
HELIX 166 185 {ECO:0000244|PDB:5JEA}.
TURN 186 189 {ECO:0000244|PDB:5JEA}.
STRAND 191 195 {ECO:0000244|PDB:5JEA}.
HELIX 199 206 {ECO:0000244|PDB:4IFD}.
HELIX 209 211 {ECO:0000244|PDB:5K36}.
STRAND 214 216 {ECO:0000244|PDB:5JEA}.
HELIX 218 223 {ECO:0000244|PDB:5JEA}.
HELIX 228 231 {ECO:0000244|PDB:5JEA}.
HELIX 232 234 {ECO:0000244|PDB:4IFD}.
HELIX 261 269 {ECO:0000244|PDB:2VNU}.
STRAND 272 280 {ECO:0000244|PDB:2VNU}.
STRAND 282 284 {ECO:0000244|PDB:2VNU}.
STRAND 287 290 {ECO:0000244|PDB:2VNU}.
STRAND 293 297 {ECO:0000244|PDB:2VNU}.
STRAND 299 303 {ECO:0000244|PDB:2VNU}.
HELIX 304 307 {ECO:0000244|PDB:2VNU}.
STRAND 315 320 {ECO:0000244|PDB:2VNU}.
HELIX 323 325 {ECO:0000244|PDB:2VNU}.
TURN 336 338 {ECO:0000244|PDB:2VNU}.
HELIX 367 383 {ECO:0000244|PDB:5JEA}.
STRAND 385 387 {ECO:0000244|PDB:5JEA}.
STRAND 389 397 {ECO:0000244|PDB:2VNU}.
STRAND 402 407 {ECO:0000244|PDB:2VNU}.
HELIX 409 411 {ECO:0000244|PDB:2VNU}.
STRAND 420 428 {ECO:0000244|PDB:2VNU}.
STRAND 434 438 {ECO:0000244|PDB:2VNU}.
HELIX 441 444 {ECO:0000244|PDB:2VNU}.
STRAND 447 455 {ECO:0000244|PDB:2VNU}.
STRAND 458 462 {ECO:0000244|PDB:5K36}.
STRAND 464 475 {ECO:0000244|PDB:2VNU}.
HELIX 478 487 {ECO:0000244|PDB:2VNU}.
HELIX 497 500 {ECO:0000244|PDB:2VNU}.
HELIX 507 509 {ECO:0000244|PDB:2VNU}.
HELIX 519 524 {ECO:0000244|PDB:2VNU}.
HELIX 526 530 {ECO:0000244|PDB:2VNU}.
STRAND 531 533 {ECO:0000244|PDB:2VNU}.
STRAND 540 546 {ECO:0000244|PDB:2VNU}.
STRAND 552 558 {ECO:0000244|PDB:2VNU}.
STRAND 564 571 {ECO:0000244|PDB:2VNU}.
HELIX 573 576 {ECO:0000244|PDB:2VNU}.
STRAND 579 581 {ECO:0000244|PDB:2WP8}.
HELIX 582 590 {ECO:0000244|PDB:2VNU}.
STRAND 594 596 {ECO:0000244|PDB:2WP8}.
STRAND 599 601 {ECO:0000244|PDB:2WP8}.
HELIX 606 609 {ECO:0000244|PDB:2VNU}.
TURN 610 612 {ECO:0000244|PDB:2VNU}.
STRAND 619 630 {ECO:0000244|PDB:2VNU}.
STRAND 636 653 {ECO:0000244|PDB:2VNU}.
HELIX 654 662 {ECO:0000244|PDB:2VNU}.
STRAND 663 665 {ECO:0000244|PDB:4IFD}.
HELIX 669 690 {ECO:0000244|PDB:2VNU}.
STRAND 701 705 {ECO:0000244|PDB:2VNU}.
STRAND 707 710 {ECO:0000244|PDB:2VNU}.
STRAND 712 717 {ECO:0000244|PDB:2VNU}.
HELIX 722 745 {ECO:0000244|PDB:2VNU}.
TURN 747 749 {ECO:0000244|PDB:2VNU}.
STRAND 751 755 {ECO:0000244|PDB:2VNU}.
HELIX 760 763 {ECO:0000244|PDB:2VNU}.
HELIX 764 774 {ECO:0000244|PDB:2VNU}.
HELIX 783 791 {ECO:0000244|PDB:2VNU}.
HELIX 801 810 {ECO:0000244|PDB:2VNU}.
STRAND 817 820 {ECO:0000244|PDB:2VNU}.
HELIX 821 823 {ECO:0000244|PDB:2VNU}.
HELIX 826 829 {ECO:0000244|PDB:2VNU}.
TURN 832 835 {ECO:0000244|PDB:2VNU}.
STRAND 836 838 {ECO:0000244|PDB:2WP8}.
TURN 845 847 {ECO:0000244|PDB:2VNU}.
HELIX 849 861 {ECO:0000244|PDB:2VNU}.
HELIX 869 872 {ECO:0000244|PDB:2VNU}.
HELIX 874 908 {ECO:0000244|PDB:2VNU}.
STRAND 912 922 {ECO:0000244|PDB:2VNU}.
STRAND 925 929 {ECO:0000244|PDB:2VNU}.
TURN 931 933 {ECO:0000244|PDB:2VNU}.
STRAND 936 940 {ECO:0000244|PDB:2VNU}.
HELIX 941 944 {ECO:0000244|PDB:2VNU}.
HELIX 948 950 {ECO:0000244|PDB:2VNU}.
STRAND 952 954 {ECO:0000244|PDB:2VNU}.
TURN 955 958 {ECO:0000244|PDB:2VNU}.
STRAND 959 962 {ECO:0000244|PDB:2VNU}.
STRAND 964 967 {ECO:0000244|PDB:5JEA}.
STRAND 971 974 {ECO:0000244|PDB:2VNU}.
STRAND 978 983 {ECO:0000244|PDB:2VNU}.
STRAND 985 987 {ECO:0000244|PDB:4IFD}.
TURN 989 991 {ECO:0000244|PDB:4IFD}.
STRAND 995 997 {ECO:0000244|PDB:2VNU}.
STRAND 998 1000 {ECO:0000244|PDB:5JEA}.
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


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