ID   RNH3_STRPI              Reviewed;         290 AA.
AC   B1I9J8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Ribonuclease HIII {ECO:0000255|HAMAP-Rule:MF_00053};
DE            Short=RNase HIII {ECO:0000255|HAMAP-Rule:MF_00053};
DE            EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00053};
GN   Name=rnhC {ECO:0000255|HAMAP-Rule:MF_00053}; OrderedLocusNames=SPH_0512;
OS   Streptococcus pneumoniae (strain Hungary19A-6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hungary19A-6;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000255|HAMAP-Rule:MF_00053}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00053};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00053};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00053};
CC       Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in
CC       the absence of substrate. May bind a second metal ion after substrate
CC       binding. {ECO:0000255|HAMAP-Rule:MF_00053};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00053}.
CC   -!- SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00053}.
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DR   EMBL; CP000936; ACA37430.1; -; Genomic_DNA.
DR   RefSeq; WP_000146861.1; NC_010380.1.
DR   AlphaFoldDB; B1I9J8; -.
DR   SMR; B1I9J8; -.
DR   EnsemblBacteria; ACA37430; ACA37430; SPH_0512.
DR   GeneID; 60233876; -.
DR   GeneID; 66805595; -.
DR   KEGG; spv:SPH_0512; -.
DR   HOGENOM; CLU_059546_1_0_9; -.
DR   OMA; TGDYFGP; -.
DR   Proteomes; UP000002163; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd14796; RNAse_HIII_N; 1.
DR   Gene3D; 3.30.310.10; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00053; RNase_HIII; 1.
DR   InterPro; IPR001352; RNase_HII/HIII.
DR   InterPro; IPR024567; RNase_HII/HIII_dom.
DR   InterPro; IPR004641; RNase_HIII.
DR   InterPro; IPR024568; RNase_HIII_N.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR012295; TBP_dom_sf.
DR   PANTHER; PTHR10954; PTHR10954; 1.
DR   Pfam; PF11858; DUF3378; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   PIRSF; PIRSF037748; RnhC; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   TIGRFAMs; TIGR00716; rnhC; 1.
DR   PROSITE; PS51975; RNASE_H_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.
FT   CHAIN           1..290
FT                   /note="Ribonuclease HIII"
FT                   /id="PRO_1000091681"
FT   DOMAIN          78..290
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         84
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00053"
FT   BINDING         85
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00053"
FT   BINDING         187
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00053"
SQ   SEQUENCE   290 AA;  31860 MW;  3902598B224F9E22 CRC64;
     MASITLTPSE KDIQAFLEHY QTSLAPSKNP YIRYFLKLPQ ATVSIYTSGK ILLQGEGAEK
     YASFFGYQAV EQTSGQNLPL IGTDEVGNGS YFGGLAVVAA FVTPDQHDFL RKLGVGDSKT
     LTDQKIRQIA PILKEKIQHQ ALLLSPSKYN EVIGDRYNAV SVKVALHNQA IYLLLQKGVQ
     PEKIVIDAFT SAKNYDKYLA QETNRFSNPI SLEEKAEGKY LAVAVSSVIA RDLFLENLEN
     LGRELGYQLP SGAGTASDKV ASQILQAYGM QGLNFCAKLH FKNTEKAKNA