ERI1_SCHPO
ID ERI1_SCHPO Reviewed; 313 AA.
AC Q08I43; O13668;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=3'-5' exonuclease eri1;
DE EC=3.1.-.-;
DE AltName: Full=Enhanced RNAi protein;
GN Name=eri1; ORFNames=pi077, SPBC30B4.08;
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=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
RN [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-264 AND ASP-268.
RX PubMed=16797182; DOI=10.1016/j.cub.2006.05.061;
RA Iida T., Kawaguchi R., Nakayama J.;
RT "Conserved ribonuclease, Eri1, negatively regulates heterochromatin
RT assembly in fission yeast.";
RL Curr. Biol. 16:1459-1464(2006).
RN [4]
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).
RN [5]
RP FUNCTION.
RX PubMed=18438419; DOI=10.1038/nsmb.1411;
RA Gabel H.W., Ruvkun G.;
RT "The exonuclease ERI-1 has a conserved dual role in 5.8S rRNA processing
RT and RNAi.";
RL Nat. Struct. Mol. Biol. 15:531-533(2008).
CC -!- FUNCTION: RNA exonuclease that acts as a negative regulator of RNA
CC interference (RNAi). Acts by degrading the 3'-overhangs of double-
CC stranded short interfering RNAs (siRNAs). Represses the accumulation of
CC heterochromatic siRNAs leading to negative regulation of the RNAi-
CC mediated heterochromoatin assembly. Also involved in rRNA biogenesis,
CC trimming the 5.8S ribosomal RNA (rRNA) from a slightly longer pre-5.8S
CC RNA in the cytoplasm. {ECO:0000269|PubMed:16797182,
CC ECO:0000269|PubMed:18438419}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16797182,
CC ECO:0000269|PubMed:16823372}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA21459.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB004539; BAA21459.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CU329671; CAL48264.1; -; Genomic_DNA.
DR RefSeq; XP_001713129.1; XM_001713077.2.
DR AlphaFoldDB; Q08I43; -.
DR SMR; Q08I43; -.
DR BioGRID; 276876; 40.
DR STRING; 4896.SPBC30B4.08.1; -.
DR MaxQB; Q08I43; -.
DR PaxDb; Q08I43; -.
DR EnsemblFungi; SPBC30B4.08.1; SPBC30B4.08.1:pep; SPBC30B4.08.
DR PomBase; SPBC30B4.08; eri1.
DR VEuPathDB; FungiDB:SPBC30B4.08; -.
DR eggNOG; KOG0542; Eukaryota.
DR HOGENOM; CLU_037266_4_1_1; -.
DR InParanoid; Q08I43; -.
DR OMA; CRELTHI; -.
DR PhylomeDB; Q08I43; -.
DR PRO; PR:Q08I43; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; ISS:PomBase.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IMP:PomBase.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:PomBase.
DR GO; GO:0032296; F:double-stranded RNA-specific ribonuclease activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:PomBase.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0060906; P:negative regulation of heterochromatin assembly by small RNA; IMP:PomBase.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR003034; SAP_dom.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..313
FT /note="3'-5' exonuclease eri1"
FT /id="PRO_0000362146"
FT DOMAIN 20..54
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 82..277
FT /note="Exonuclease"
FT ACT_SITE 88
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MUTAGEN 264
FT /note="H->A: Disrupts exonuclease activity."
FT /evidence="ECO:0000269|PubMed:16797182"
FT MUTAGEN 268
FT /note="D->A: Disrupts exonuclease activity."
FT /evidence="ECO:0000269|PubMed:16797182"
SQ SEQUENCE 313 AA; 36966 MW; 091047C81D9EB737 CRC64;
MESPVQILVW PFPCDEMNQK TPSTVEEIRI ALQELGLSTN GNKEKLKRRW KFREKRLEEK
RKQERYQKFS TSNENKTCLR YLLIVDVEAT CEEGCGFSFE NEIIELPCLL FDLIEKSIID
EFHSYVRPSM NPTLSDYCKS LTGIQQCTVD KAPIFSDVLE ELFIFLRKHS NILVPSVDEI
EIIEPLKSVP RTQPKNWAWA CDGPWDMASF LAKQFKYDKM PIPDWIKGPF VDIRSFYKDV
YRVPRTNING MLEHWGLQFE GSEHRGIDDA RNLSRIVKKM CSENVEFECN RWWMEYEKNG
WIPNRSYPPY FAS
