PAC1_SCHPO
ID PAC1_SCHPO Reviewed; 363 AA.
AC P22192; Q4JFF8; Q670L9;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Double-strand-specific pac1 ribonuclease;
DE EC=3.1.26.3;
DE AltName: Full=Protein hcs;
GN Name=pac1; Synonyms=hcs; ORFNames=SPBC119.11c;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=1989884; DOI=10.1002/j.1460-2075.1991.tb07939.x;
RA Iino Y., Sugimoto A., Yamamoto M.;
RT "S. pombe pac1+, whose overexpression inhibits sexual development, encodes
RT a ribonuclease III-like RNase.";
RL EMBO J. 10:221-226(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2205842; DOI=10.1093/nar/18.17.5304;
RA Xu H.-P., Riggs M., Rodgers L., Wigler M.;
RT "A gene from S. pombe with homology to E. coli RNase III blocks conjugation
RT and sporulation when overexpressed in wild type cells.";
RL Nucleic Acids Res. 18:5304-5304(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2.1459, and 2.274;
RA Zheng Y., Li S.;
RT "Cloning, sequencing, prokaryotic expression and in vitro activity analysis
RT of double-stranded RNA-specific nuclease gene from yeast.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-178.
RX PubMed=7616961; DOI=10.1007/bf00290401;
RA Rotondo G., Gillespie M., Frendewey D.;
RT "Rescue of the fission yeast snRNA synthesis mutant snm1 by overexpression
RT of the double-strand-specific Pac1 ribonuclease.";
RL Mol. Gen. Genet. 247:698-708(1995).
RN [5]
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 [6]
RP COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8710510; DOI=10.1093/nar/24.12.2377;
RA Rotondo G., Frendewey D.;
RT "Purification and characterization of the Pac1 ribonuclease of
RT Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 24:2377-2386(1996).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Digests double-stranded RNA. Converts long double-stranded
CC RNAs into short oligonucleotides, leaving 5'-phosphates on their
CC cleavage products. Probably inhibits mating and meiosis by degrading a
CC specific mRNA required for sexual development.
CC {ECO:0000269|PubMed:1989884}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8710510};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. No activity at pH below 6.5 or above 9.5.
CC {ECO:0000269|PubMed:8710510};
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DR EMBL; X54998; CAA38745.1; -; Genomic_DNA.
DR EMBL; X53769; CAJ14141.1; -; Genomic_DNA.
DR EMBL; S78982; AAB34897.1; -; Genomic_DNA.
DR EMBL; AY695821; AAU05314.1; -; Genomic_DNA.
DR EMBL; AY695822; AAU05315.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA17926.1; -; Genomic_DNA.
DR PIR; S12605; S12605.
DR RefSeq; NP_595292.1; NM_001021199.2.
DR AlphaFoldDB; P22192; -.
DR SMR; P22192; -.
DR BioGRID; 276622; 3.
DR STRING; 4896.SPBC119.11c.1; -.
DR iPTMnet; P22192; -.
DR MaxQB; P22192; -.
DR PaxDb; P22192; -.
DR PRIDE; P22192; -.
DR EnsemblFungi; SPBC119.11c.1; SPBC119.11c.1:pep; SPBC119.11c.
DR GeneID; 2540084; -.
DR KEGG; spo:SPBC119.11c; -.
DR PomBase; SPBC119.11c; pac1.
DR VEuPathDB; FungiDB:SPBC119.11c; -.
DR eggNOG; KOG1817; Eukaryota.
DR HOGENOM; CLU_062290_0_0_1; -.
DR InParanoid; P22192; -.
DR OMA; RAWGANQ; -.
DR PhylomeDB; P22192; -.
DR PRO; PR:P22192; -.
DR Proteomes; UP000002485; Chromosome II.
DR ExpressionAtlas; P22192; differential.
DR GO; GO:0005730; C:nucleolus; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; IDA: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:0000182; F:rDNA binding; IDA:PomBase.
DR GO; GO:0004525; F:ribonuclease III activity; IDA:PomBase.
DR GO; GO:0035613; F:RNA stem-loop binding; IDA:PomBase.
DR GO; GO:0106410; P:box C/D RNA 5'-end processing; IMP:PomBase.
DR GO; GO:0000478; P:endonucleolytic cleavage involved in rRNA processing; IDA:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; IMP:PomBase.
DR GO; GO:0031053; P:primary miRNA processing; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0016070; P:RNA metabolic process; IDA:PomBase.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IMP:PomBase.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:PomBase.
DR GO; GO:0034474; P:U2 snRNA 3'-end processing; IDA:PomBase.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IMP:PomBase.
DR CDD; cd19876; DSRM_RNT1p-like; 1.
DR CDD; cd00593; RIBOc; 1.
DR Gene3D; 1.10.1520.10; -; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR InterPro; IPR044449; Rnt1/Pac1_DSRM_fungi.
DR PANTHER; PTHR11207; PTHR11207; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF00636; Ribonuclease_3; 1.
DR SMART; SM00358; DSRM; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Magnesium; Meiosis; Metal-binding; Nuclease;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..363
FT /note="Double-strand-specific pac1 ribonuclease"
FT /id="PRO_0000180467"
FT DOMAIN 139..262
FT /note="RNase III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 285..356
FT /note="DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 178
FT /note="G->D,S: In snm1-1 and ran1-114; loss of activity."
FT /evidence="ECO:0000269|PubMed:7616961"
FT CONFLICT 144
FT /note="E -> K (in Ref. 4; AAU05314/AAU05315)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 41539 MW; BB866CD6AC5AF33A CRC64;
MGRFKRHHEG DSDSSSSASD SLSRGRRSLG HKRSSHIKNR QYYILEKKIR KLMFAMKALL
EETKHSTKDD VNLVIPGSTW SHIEGVYEML KSRHDRQNEP VIEEPSSHPK NQKNQENNEP
TSEEFEEGEY PPPLPPLRSE KLKEQVFMHI SRAYEIYPNQ SNPNELLDIH NERLEFLGDS
FFNLFTTRII FSKFPQMDEG SLSKLRAKFV GNESADKFAR LYGFDKTLVL SYSAEKDQLR
KSQKVIADTF EAYLGALILD GQEETAFQWV SRLLQPKIAN ITVQRPIDKL AKSKLFHKYS
TLGHIEYRWV DGAGGSAEGY VIACIFNGKE VARAWGANQK DAGSRAAMQA LEVLAKDYSK
FAR
