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Exosome complex exonuclease RRP6 (EC 3.1.13.-) (Ribosomal RNA-processing protein 6)

 RRP6_YEAST              Reviewed;         733 AA.
Q12149; D6W267; Q6B280;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 160.
RecName: Full=Exosome complex exonuclease RRP6;
EC=3.1.13.-;
AltName: Full=Ribosomal RNA-processing protein 6;
Name=RRP6; Synonyms=UNC733; OrderedLocusNames=YOR001W;
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].
PubMed=8896276;
DOI=10.1002/(SICI)1097-0061(199609)12:10B<1091::AID-YEA22>3.3.CO;2-9;
Sterky F., Holmberg A., Pettersson B., Uhlen M.;
"The sequence of a 30 kb fragment on the left arm of chromosome XV
from Saccharomyces cerevisiae reveals 15 open reading frames, five of
which correspond to previously identified genes.";
Yeast 12:1091-1095(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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
FUNCTION.
PubMed=9582370; DOI=10.1074/jbc.273.21.13255;
Briggs M.W., Burkard K.T.D., Butler J.S.;
"Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen,
is essential for efficient 5.8 S rRNA 3' end formation.";
J. Biol. Chem. 273:13255-13263(1998).
[6]
FUNCTION, IDENTIFICATION IN THE RNA EXOSOME COMPLEX BY MASS
SPECTROMETRY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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).
[7]
CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH NPL3 AND PAP1,
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=10611239; DOI=10.1128/MCB.20.2.604-616.2000;
Burkard K.T.D., Butler J.S.;
"A nuclear 3'-5' exonuclease involved in mRNA degradation interacts
with Poly(A) polymerase and the hnRNA protein Npl3p.";
Mol. Cell. Biol. 20:604-616(2000).
[8]
INTERACTION WITH LRP1.
PubMed=12972615; DOI=10.1128/MCB.23.19.6982-6992.2003;
Mitchell P., Petfalski E., Houalla R., Podtelejnikov A., Mann M.,
Tollervey D.;
"Rrp47p is an exosome-associated protein required for the 3'
processing of stable RNAs.";
Mol. Cell. Biol. 23:6982-6992(2003).
[9]
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).
[10]
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).
[11]
FUNCTION, INTERACTION WITH LRP1, AND SUBCELLULAR LOCATION.
PubMed=15489286; DOI=10.1101/gad.1241204;
Hieronymus H., Yu M.C., Silver P.A.;
"Genome-wide mRNA surveillance is coupled to mRNA export.";
Genes Dev. 18:2652-2662(2004).
[12]
RECONSTITUTION OF THE RNA EXOSOME COMPLEX, AND EXONUCLEASE ACTIVITY.
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).
[13]
ERRATUM.
Liu Q., Greimann J.C., Lima C.D.;
Cell 131:188-189(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-645, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[15]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE RNA EXOSOME,
SUBUNIT, AND DISRUPTION PHENOTYPE.
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).
[16]
INTERACTION WITH NOP53.
PubMed=18631361; DOI=10.1111/j.1742-4658.2008.06565.x;
Granato D.C., Machado-Santelli G.M., Oliveira C.C.;
"Nop53p interacts with 5.8S rRNA co-transcriptionally, and regulates
processing of pre-rRNA by the exosome.";
FEBS J. 275:4164-4178(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-520 AND SER-645, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-645, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Nuclear-specific 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. 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. RRP6 has 3'-5' exonuclease activity which is not
modulated upon association with Exo-9 suggesting that the complex
inner RNA-binding path is not used to access its active site.
{ECO:0000269|PubMed:10465791, ECO:0000269|PubMed:10611239,
ECO:0000269|PubMed:15489286, ECO:0000269|PubMed:9582370}.
-!- SUBUNIT: Component of the RNA exosome complex. The catalytically
inactive RNA exosome core (Exo-9) complex associates 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. RRP6 specifically is part of the
nuclear form of the RNA exosome complex; the association appears
to be mediated by Exo-9 and not by DIS3. Interacts with LRP1.
Interacts with NPL3, NOP53 and PAP1. {ECO:0000269|PubMed:10465791,
ECO:0000269|PubMed:10611239, ECO:0000269|PubMed:12972615,
ECO:0000269|PubMed:15489286, ECO:0000269|PubMed:17173052,
ECO:0000269|PubMed:18631361}.
-!- INTERACTION:
P46948:SKI6; NbExp=3; IntAct=EBI-1782, EBI-1788;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:10465791, ECO:0000269|PubMed:10611239,
ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15489286}.
-!- DISRUPTION PHENOTYPE: Deletion mutant is impaired in growth at all
temperatures and is nonviable at 37 degrees Celsius. It is
defective in the 3' processing of the 5.8S rRNA and accumulates a
discrete species, 5.8S + 30, that is 3' extended by about 30
nucleotides. Deletion also causes an accumulation of 7S RNA and 5'
ETS and increases the level of poly(A)+ mRNA.
{ECO:0000269|PubMed:10465791, ECO:0000269|PubMed:10611239,
ECO:0000269|PubMed:17173052}.
-!- MISCELLANEOUS: Present with 2160 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the exosome component 10/RRP6 family.
{ECO:0000305}.
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EMBL; Z74909; CAA99189.1; -; Genomic_DNA.
EMBL; U43491; AAC49480.1; -; Genomic_DNA.
EMBL; AY692850; AAT92869.1; -; Genomic_DNA.
EMBL; BK006948; DAA10783.1; -; Genomic_DNA.
PIR; S61984; S61984.
RefSeq; NP_014643.1; NM_001183420.1.
PDB; 1M0Y; Model; -; A=207-382.
PDB; 2HBJ; X-ray; 2.10 A; A=129-536.
PDB; 2HBK; X-ray; 2.25 A; A=129-536.
PDB; 2HBL; X-ray; 2.30 A; A=129-536.
PDB; 2HBM; X-ray; 2.70 A; A=129-536.
PDB; 4IFD; X-ray; 2.80 A; K=518-693.
PDB; 4OO1; X-ray; 3.30 A; J=129-685.
PDB; 4WFC; X-ray; 2.35 A; A/C/E=1-111.
PDB; 4WFD; X-ray; 2.40 A; A/D/G=1-111.
PDB; 5C0W; X-ray; 4.60 A; K=1-693.
PDB; 5C0X; X-ray; 3.81 A; K=1-693.
PDB; 5C0Y; X-ray; 2.10 A; A/B=122-518.
PDB; 5K36; X-ray; 3.10 A; J=129-684.
PDB; 5VZJ; X-ray; 3.30 A; J=129-684.
PDBsum; 1M0Y; -.
PDBsum; 2HBJ; -.
PDBsum; 2HBK; -.
PDBsum; 2HBL; -.
PDBsum; 2HBM; -.
PDBsum; 4IFD; -.
PDBsum; 4OO1; -.
PDBsum; 4WFC; -.
PDBsum; 4WFD; -.
PDBsum; 5C0W; -.
PDBsum; 5C0X; -.
PDBsum; 5C0Y; -.
PDBsum; 5K36; -.
PDBsum; 5VZJ; -.
ProteinModelPortal; Q12149; -.
SMR; Q12149; -.
BioGrid; 34404; 583.
DIP; DIP-4560N; -.
IntAct; Q12149; 27.
MINT; MINT-534618; -.
STRING; 4932.YOR001W; -.
iPTMnet; Q12149; -.
MaxQB; Q12149; -.
PRIDE; Q12149; -.
EnsemblFungi; YOR001W; YOR001W; YOR001W.
GeneID; 854162; -.
KEGG; sce:YOR001W; -.
EuPathDB; FungiDB:YOR001W; -.
SGD; S000005527; RRP6.
GeneTree; ENSGT00390000015408; -.
HOGENOM; HOG000196525; -.
InParanoid; Q12149; -.
KO; K12591; -.
OMA; DSVEDNW; -.
OrthoDB; EOG092C15WQ; -.
BioCyc; YEAST:G3O-33552-MONOMER; -.
Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
EvolutionaryTrace; Q12149; -.
PRO; PR:Q12149; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:SGD.
GO; GO:0005730; C:nucleolus; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:SGD.
GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0071044; P:histone mRNA catabolic process; IMP:SGD.
GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
GO; GO:0071040; P:nuclear polyadenylation-dependent antisense transcript catabolic process; IMP:SGD.
GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IMP:SGD.
GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IMP:SGD.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IMP:SGD.
GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IMP:SGD.
GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IDA:SGD.
GO; GO:0071033; P:nuclear retention of pre-mRNA at the site of transcription; IGI:SGD.
GO; GO:0071049; P:nuclear retention of pre-mRNA with aberrant 3'-ends at the site of transcription; IGI:SGD.
GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IMP:SGD.
GO; GO:0000973; P:posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
GO; GO:0034473; P:U1 snRNA 3'-end processing; IMP:SGD.
GO; GO:0034475; P:U4 snRNA 3'-end processing; IMP:SGD.
GO; GO:0034476; P:U5 snRNA 3'-end processing; IMP:SGD.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR002562; 3'-5'_exonuclease_dom.
InterPro; IPR012588; Exosome-assoc_fac_Rrp6_N.
InterPro; IPR010997; HRDC-like.
InterPro; IPR002121; HRDC_dom.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF01612; DNA_pol_A_exo1; 1.
Pfam; PF00570; HRDC; 1.
Pfam; PF08066; PMC2NT; 1.
SMART; SM00474; 35EXOc; 1.
SMART; SM00341; HRDC; 1.
SUPFAM; SSF47819; SSF47819; 1.
SUPFAM; SSF53098; SSF53098; 1.
PROSITE; PS50967; HRDC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Exonuclease; Exosome; Hydrolase;
Nuclease; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
rRNA processing.
CHAIN 1 733 Exosome complex exonuclease RRP6.
/FTId=PRO_0000097456.
DOMAIN 435 515 HRDC. {ECO:0000255|PROSITE-
ProRule:PRU00328}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
MOD_RES 520 520 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 640 640 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 645 645 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
CONFLICT 402 402 E -> G (in Ref. 4; AAT92869).
{ECO:0000305}.
HELIX 8 25 {ECO:0000244|PDB:4WFC}.
HELIX 28 34 {ECO:0000244|PDB:4WFC}.
HELIX 36 60 {ECO:0000244|PDB:4WFC}.
HELIX 76 105 {ECO:0000244|PDB:4WFC}.
HELIX 132 135 {ECO:0000244|PDB:2HBJ}.
STRAND 136 138 {ECO:0000244|PDB:4OO1}.
HELIX 162 165 {ECO:0000244|PDB:2HBJ}.
STRAND 173 175 {ECO:0000244|PDB:2HBJ}.
HELIX 184 189 {ECO:0000244|PDB:2HBJ}.
HELIX 194 196 {ECO:0000244|PDB:2HBJ}.
HELIX 208 210 {ECO:0000244|PDB:2HBJ}.
STRAND 214 216 {ECO:0000244|PDB:2HBJ}.
HELIX 219 229 {ECO:0000244|PDB:2HBJ}.
STRAND 233 242 {ECO:0000244|PDB:2HBJ}.
STRAND 244 248 {ECO:0000244|PDB:2HBJ}.
STRAND 250 257 {ECO:0000244|PDB:2HBJ}.
STRAND 262 266 {ECO:0000244|PDB:2HBJ}.
TURN 267 273 {ECO:0000244|PDB:2HBJ}.
HELIX 274 277 {ECO:0000244|PDB:2HBJ}.
HELIX 278 281 {ECO:0000244|PDB:2HBJ}.
STRAND 286 292 {ECO:0000244|PDB:2HBJ}.
HELIX 294 304 {ECO:0000244|PDB:2HBJ}.
STRAND 309 313 {ECO:0000244|PDB:2HBJ}.
HELIX 314 321 {ECO:0000244|PDB:2HBJ}.
HELIX 328 335 {ECO:0000244|PDB:2HBJ}.
TURN 343 346 {ECO:0000244|PDB:2HBJ}.
STRAND 351 353 {ECO:0000244|PDB:5K36}.
HELIX 356 367 {ECO:0000244|PDB:2HBJ}.
HELIX 369 382 {ECO:0000244|PDB:2HBJ}.
HELIX 386 398 {ECO:0000244|PDB:2HBJ}.
HELIX 404 406 {ECO:0000244|PDB:2HBJ}.
STRAND 413 416 {ECO:0000244|PDB:2HBJ}.
STRAND 421 427 {ECO:0000244|PDB:2HBJ}.
HELIX 436 438 {ECO:0000244|PDB:5C0Y}.
HELIX 439 456 {ECO:0000244|PDB:2HBJ}.
HELIX 460 463 {ECO:0000244|PDB:2HBJ}.
HELIX 466 475 {ECO:0000244|PDB:2HBJ}.
HELIX 480 484 {ECO:0000244|PDB:2HBJ}.
HELIX 492 496 {ECO:0000244|PDB:2HBJ}.
HELIX 498 515 {ECO:0000244|PDB:2HBJ}.
TURN 534 536 {ECO:0000244|PDB:4IFD}.
HELIX 539 553 {ECO:0000244|PDB:4IFD}.
TURN 555 558 {ECO:0000244|PDB:4OO1}.
STRAND 570 572 {ECO:0000244|PDB:4IFD}.
TURN 573 577 {ECO:0000244|PDB:4IFD}.
STRAND 582 585 {ECO:0000244|PDB:4IFD}.
STRAND 591 594 {ECO:0000244|PDB:4IFD}.
HELIX 596 611 {ECO:0000244|PDB:4IFD}.
HELIX 612 614 {ECO:0000244|PDB:4IFD}.
STRAND 617 619 {ECO:0000244|PDB:4IFD}.
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


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18-003-44218 Exosome complex exonuclease RRP4 - EC 3.1.13.-; Ribosomal RNA-processing protein 4; Exosome component 2 Polyclonal 0.1 mg Protein A
18-003-43636 Exosome complex exonuclease RRP42 - EC 3.1.13.-; Ribosomal RNA-processing protein 42; Exosome component 7; p8 Polyclonal 0.1 mg Protein A
18-003-43649 Exosome complex exonuclease RRP41 - EC 3.1.13.-; Ribosomal RNA-processing protein 41; Exosome component 4; p12A Polyclonal 0.1 mg Protein A
EIAAB13497 Exosc7,Exosome complex exonuclease RRP42,Exosome component 7,Mouse,Mus musculus,Ribosomal RNA-processing protein 42,Rrp42
EIAAB35999 Dis3,Exosome complex exonuclease RRP44,Kiaa1008,Mouse,Mus musculus,Protein DIS3 homolog,Ribosomal RNA-processing protein 44,Rrp44
EIAAB36000 DIS3,Exosome complex exonuclease RRP44,Homo sapiens,Human,KIAA1008,Protein DIS3 homolog,Ribosomal RNA-processing protein 44,RRP44
EIAAB13498 Bos taurus,Bovine,EXOSC8,Exosome complex component RRP43,Exosome component 8,Ribosomal RNA-processing protein 43
EIAAB13500 EXOSC8,Exosome complex component RRP43,Exosome component 8,Homo sapiens,Human,OIP2,OIP-2,Opa-interacting protein 2,p9,Ribosomal RNA-processing protein 43,RRP43
EIAAB13496 EXOSC7,Exosome complex component RRP42,Exosome component 7,Homo sapiens,Human,KIAA0116,p8,Ribosomal RNA-processing protein 42,RRP42
EIAAB13490 EXOSC4,Exosome complex component RRP41,Exosome component 4,Homo sapiens,Human,p12A,Ribosomal RNA-processing protein 41,RRP41,SKI6
EIAAB13488 CGI-102,EXOSC3,Exosome complex component RRP40,Exosome component 3,Homo sapiens,Human,p10,Ribosomal RNA-processing protein 40,RRP40
EIAAB13485 EXOSC2,Exosome complex component RRP4,Exosome component 2,Homo sapiens,Human,Ribosomal RNA-processing protein 4,RRP4
EIAAB13493 D7Wsu180e,Exosc5,Exosome complex component RRP46,Exosome component 5,Mouse,Mus musculus,Ribosomal RNA-processing protein 46,Rrp46
EIAAB13489 Bos taurus,Bovine,EXOSC4,Exosome complex component RRP41,Exosome component 4,Ribosomal RNA-processing protein 41,RRP41
EIAAB13499 Exosc8,Exosome complex component RRP43,Exosome component 8,Mouse,Mus musculus,Ribosomal RNA-processing protein 43,Rrp43
EIAAB13483 Exosc2,Exosome complex component RRP4,Exosome component 2,Mouse,Mus musculus,Ribosomal RNA-processing protein 4,Rrp4
EIAAB13491 Exosc4,Exosome complex component RRP41,Exosome component 4,Mouse,Mus musculus,Ribosomal RNA-processing protein 41,Rrp41
EIAAB13484 Bos taurus,Bovine,EXOSC2,Exosome complex component RRP4,Exosome component 2,Ribosomal RNA-processing protein 4,RRP4
EIAAB13486 Bos taurus,Bovine,EXOSC3,Exosome complex component RRP40,Exosome component 3,Ribosomal RNA-processing protein 40,RRP40
EIAAB13487 Exosc3,Exosome complex component RRP40,Exosome component 3,Mouse,Mus musculus,Ribosomal RNA-processing protein 40,Rrp40
EIAAB13492 Chronic myelogenous leukemia tumor antigen 28,CML28,EXOSC5,Exosome complex component RRP46,Exosome component 5,Homo sapiens,Human,p12B,Ribosomal RNA-processing protein 46,RRP46
18-003-44234 Exosome complex exonuclease MTR3 - EC 3.1.13.-; mRNA transport regulator 3 homolog; hMtr3; Exosome component 6; p11 Polyclonal 0.05 mg Aff Pur
18-003-43666 Exosome complex exonuclease MTR3 - EC 3.1.13.-; mRNA transport regulator 3 homolog; hMtr3; Exosome component 6; p11 Polyclonal 0.1 mg Protein A
20-372-60233 exosome component 7 (EXOSC7). mRNA - Mouse monoclonal anti-human EXOSC7 antibody; EC 3.1.13.-; Ribosomal RNA-processing protein 42; Exosome component 7; p8 Monoclonal 0.1 mg
20-372-60232 exosome component 2 (EXOSC2). mRNA - Mouse monoclonal anti-human EXOSC2 antibody; EC 3.1.13.-; Ribosomal RNA-processing protein 4; Exosome component 2 Monoclonal 0.1 mg


 

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