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   27-MAR-2024, entry version 162.
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; 284812.P22192; -.
DR   iPTMnet; P22192; -.
DR   MaxQB; P22192; -.
DR   PaxDb; 4896-SPBC119-11c-1; -.
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   GO; GO:0005730; C:nucleolus; ISO:PomBase.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
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:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:PomBase.
DR   GO; GO:0016070; P:RNA metabolic process; IDA:PomBase.
DR   GO; GO:0006364; P:rRNA processing; IDA:PomBase.
DR   GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR   GO; GO:0030847; P:termination of RNA polymerase II transcription, exosome-dependent; 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; 3.30.160.20; -; 1.
DR   Gene3D; 1.10.1520.10; Ribonuclease III domain; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   InterPro; IPR044449; Rnt1/Pac1_DSRM_fungi.
DR   PANTHER; PTHR11207:SF0; RIBONUCLEASE 3; 1.
DR   PANTHER; PTHR11207; RIBONUCLEASE III; 1.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF00636; Ribonuclease_3; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF69065; RNase III domain-like; 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
//