RPM1_SCHPO
ID RPM1_SCHPO Reviewed; 957 AA.
AC Q1MTN7;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Exoribonuclease II, mitochondrial;
DE Short=RNase II;
DE Short=Ribonuclease II;
DE EC=3.1.13.1;
DE AltName: Full=Processome-associated RNase;
DE Flags: Precursor;
GN Name=rpm1; Synonyms=par1; ORFNames=SPCC1322.01;
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).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=18304578; DOI=10.1016/j.jmb.2008.01.038;
RA Hoffmann B., Nickel J., Speer F., Schafer B.;
RT "The 3' ends of mature transcripts are generated by a processosome complex
RT in fission yeast mitochondria.";
RL J. Mol. Biol. 377:1024-1037(2008).
CC -!- FUNCTION: Required for intron-independent turnover and processing of
CC mitochondrial RNA. Participates in 3'-mtRNA processing where it
CC hydrolyzes single-stranded RNA or partially double-stranded RNA with
CC 3'-single-stranded tails. {ECO:0000269|PubMed:18304578}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: Up-regulated in cells metabolizing nonfermentable carbon
CC sources. {ECO:0000269|PubMed:18304578}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
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DR EMBL; CU329672; CAB51565.2; -; Genomic_DNA.
DR RefSeq; NP_588129.2; NM_001023119.2.
DR AlphaFoldDB; Q1MTN7; -.
DR SMR; Q1MTN7; -.
DR BioGRID; 275379; 3.
DR STRING; 4896.SPCC1322.01.1; -.
DR MaxQB; Q1MTN7; -.
DR PaxDb; Q1MTN7; -.
DR PRIDE; Q1MTN7; -.
DR EnsemblFungi; SPCC1322.01.1; SPCC1322.01.1:pep; SPCC1322.01.
DR GeneID; 2538798; -.
DR KEGG; spo:SPCC1322.01; -.
DR PomBase; SPCC1322.01; rpm1.
DR VEuPathDB; FungiDB:SPCC1322.01; -.
DR eggNOG; KOG2102; Eukaryota.
DR HOGENOM; CLU_308393_0_0_1; -.
DR InParanoid; Q1MTN7; -.
DR OMA; ISECMIL; -.
DR PhylomeDB; Q1MTN7; -.
DR PRO; PR:Q1MTN7; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0008859; F:exoribonuclease II activity; ISO:PomBase.
DR GO; GO:0003723; F:RNA binding; ISS:PomBase.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IMP:PomBase.
DR GO; GO:0007005; P:mitochondrion organization; NAS:PomBase.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 2: Evidence at transcript level;
KW Exonuclease; Hydrolase; Mitochondrion; Nuclease; Reference proteome;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..54
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 55..957
FT /note="Exoribonuclease II, mitochondrial"
FT /id="PRO_0000353825"
SQ SEQUENCE 957 AA; 109979 MW; 15EFAC3D6B61786E CRC64;
MNYRQLFLLQ NVNLESNYLL KRVCLSLKLS PCKLTRKFHH ACPSSSKVLK YFRITGCLIN
FGKQPANDHH LWGHCGARLK HTQSDLIDRF KNANLKSVNE ENLKKFFSEL ENHGNIRQWL
KDKFEKDKRA AVCPTTTKSE EEKLENDFEY SFDLEDFSSE NFRQYDRGDL LVFYRGSEGI
ELAACTGTNV WNYSNVLTSI NENGTIKEFR TSRVLLRCPN VFKKLKEVQQ PLSDVSVPSD
VLPFTIKLLK KISQRAQDLS RSHRNEFLRI LTEFNIPNKL DNSASFSDLL KFVYKTSKPS
PYAKISLLHF LLTESKHFLI SDHIFSEIQK VYFLPSSQND SFDDVVACLR QKSTPYLSFI
KKARHLIQVS RDKYKLPIST EEIKPVVYSQ VTWTEFEKKL LRYLVQEMIA KSIQSLPNTH
LCQVYKEVGL QTHERGLTSD QFAKFLTDIG VWASWQPPRL FQQEYSIAGL GTNPQLDAVY
ERECNHFKKF VKNELKDSLE SQRVDLRHLK AFAFDSSSTK EIDDAISVEE LGMSNSWLHI
HVANPTSTVD IRSPLGTFAE RNFQTIYHPN KIVYMLPLNI TQKYWSLDSS STAQRALTFS
AKISKNGDIL DYKVRPSFIS SVIKYTPQQL DKALHSNRSI AKDIVSGPVD EETKGVSNDH
MKDILRIYEL SKQACFSRLQ KFAFVIAQPT PTVELLPNNV PYNLGDLNHP VYWSSFPTIS
LNVSEGYSLA ESVISECMIL AGRVSSLFFQ EHKLPGIFRG QPYPIMDGVR RKAFETLLSN
RSSWGLVETK YSLSVMPLFE SSHLASTPVS HFSLGLKDGY IQSTSPLRRF TDFFTHHQIQ
SVLLKTPKNT IPDGILRGKL NLYNQKEKSI KTIGRYINRF WALKYIERLP KVQKNIYHGY
LMVSELSTPQ VMLEELGVKA HIDILPDEAF RLANTRQAFT IKDVFPESNI LLVALAT
