RRP6_SCHPO
ID RRP6_SCHPO Reviewed; 777 AA.
AC Q10146;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Exosome complex exonuclease rrp6;
DE EC=3.1.13.-;
DE AltName: Full=Ribosomal RNA-processing protein 6;
GN Name=rrp6; ORFNames=SPAC1F3.01, SPAC3H8.11;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 (By similarity).
CC {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the exosome component 10/RRP6 family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA93168.1; -; Genomic_DNA.
DR PIR; T38769; T38769.
DR RefSeq; NP_593004.2; NM_001018403.2.
DR AlphaFoldDB; Q10146; -.
DR SMR; Q10146; -.
DR BioGRID; 280044; 65.
DR IntAct; Q10146; 2.
DR MINT; Q10146; -.
DR STRING; 4896.SPAC1F3.01.1; -.
DR iPTMnet; Q10146; -.
DR SwissPalm; Q10146; -.
DR MaxQB; Q10146; -.
DR PaxDb; Q10146; -.
DR PRIDE; Q10146; -.
DR EnsemblFungi; SPAC1F3.01.1; SPAC1F3.01.1:pep; SPAC1F3.01.
DR GeneID; 2543630; -.
DR KEGG; spo:SPAC1F3.01; -.
DR PomBase; SPAC1F3.01; rrp6.
DR VEuPathDB; FungiDB:SPAC1F3.01; -.
DR eggNOG; KOG2206; Eukaryota.
DR HOGENOM; CLU_010129_0_1_1; -.
DR InParanoid; Q10146; -.
DR OMA; KAVHQWR; -.
DR PhylomeDB; Q10146; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q10146; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0000178; C:exosome (RNase complex); IDA:PomBase.
DR GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); EXP:PomBase.
DR GO; GO:1990251; C:nuclear exosome focus; IDA:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISO:PomBase.
DR GO; GO:0004532; F:exoribonuclease activity; IDA:PomBase.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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); ISO:PomBase.
DR GO; GO:0071044; P:histone mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0110064; P:lncRNA catabolic process; IMP:PomBase.
DR GO; GO:0070651; P:nonfunctional rRNA decay; ISO:PomBase.
DR GO; GO:0071028; P:nuclear mRNA surveillance; TAS:PomBase.
DR GO; GO:0071040; P:nuclear polyadenylation-dependent antisense transcript catabolic process; IBA:GO_Central.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IBA:GO_Central.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; ISO:PomBase.
DR GO; GO:0071046; P:nuclear polyadenylation-dependent ncRNA catabolic process; IDA:PomBase.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; ISO:PomBase.
DR GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; ISO:PomBase.
DR GO; GO:0033621; P:nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts; IMP:PomBase.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:1902794; P:siRNA-independent facultative heterochromatin assembly; IMP:PomBase.
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 3: Inferred from homology;
KW Exonuclease; Exosome; Hydrolase; Nuclease; Nucleus; Reference proteome;
KW RNA-binding; rRNA processing.
FT CHAIN 1..777
FT /note="Exosome complex exonuclease rrp6"
FT /id="PRO_0000116595"
FT DOMAIN 442..522
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 630..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 89560 MW; DB1FAC172BFB14A2 CRC64;
MDESELFKGL MNSTAYCSEL AKVDIPFYKS IDTEFNENIK SVSSRFMRLI ELLLSKVDRS
RAEDIVDVED IDNRWAEVSD TLDILFEKAD YSIDKAQGLL KKPAIETHAS TSDVANKKPK
KEKLPYKVIH AAHLTKPQLR FRVQPNNSRE FVWSWKLTEK PHSLVPLEKI IAQVKLDPSL
KNSLPHPYEP EIQNSVYPPW VSEMSNPIDT GSVDETEPIW VSTESQLSDM LKELQNSKEI
AVDLEHHDYR SFRGFVCLMQ ISNREKDWIV DTLELREELE ALNVVFTNPN IIKVFHGATM
DIIWLQRDFG LYVVNLFDTY YATKVLGFEG HGLAFLLQKY CDYDADKRYQ MADWRIRPLP
REMLKYAQSD THYLLYIWDH LRNELISKSA ERKENLMQSV FNSSKQISLR KYELEPYDPI
YGLGTDGWRN VLTKFGSSKI IGREALMIYR ALHDWRDSVA RKEDESVRYV LPNRLLIAIA
ASKPVEAADV FSISKQLTPI ARMYVEDIVK VVQEAEKLYN EQVDREKSQF KEVEKQNQPL
AVFSESNTLG DYKVDSSVFE ISKQNRSKLK TLLANGSAFW IEGQSQDDLR KARKERLFIV
NQNIPFSLTL PCTQGHVESE LNVKQSTVTE AANPSLNGEK KQEPIVIRDL GLNKQKRDSS
KLNHKEPSNP IEERNEDIEP SEASTSVSKK RKQKKKKKNS GKLTIEAEHV SNDSPIINEA
PFDYKNQKNF IADLDSDVGK NKFGKRGFNP LNKVSLPKRN TRELKKRKVS DGKSTSY
