ID   RNH3_STRZT              Reviewed;         293 AA.
AC   C1CPR4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=SPT_0441;
OS   Streptococcus pneumoniae (strain Taiwan19F-14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Taiwan19F-14;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000921; ACO23076.1; -; Genomic_DNA.
DR   RefSeq; WP_000146863.1; NC_012469.1.
DR   AlphaFoldDB; C1CPR4; -.
DR   SMR; C1CPR4; -.
DR   KEGG; snt:SPT_0441; -.
DR   HOGENOM; CLU_059546_1_0_9; -.
DR   OMA; TGDYFGP; -.
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..293
FT                   /note="Ribonuclease HIII"
FT                   /id="PRO_1000194459"
FT   DOMAIN          78..293
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   293 AA;  32357 MW;  1C3D67CFBD8B8B22 CRC64;
     MASITLTPSE KDIQAFLEHY QTSLAPSKNP YIRYFLKLPQ ATVSIYTSGK ILLQGEGAEK
     YASFFGYQAV EQTSGQNLPL IGTDEVGNGS YFGGLAVVAA FVTPDQHDFL RKLGVGDSKT
     LTDQKIRQIA PILKEKIQHQ ALLLSPSKYN EVIGNRYNAV SVKVALHNQA IYLLLQKGVQ
     PEKIVIDAFT SAKNYDKYLA QETNRFSNPI SLEEKAEGKY LAVAVSSVIA RDLFLENLEN
     LGRELGYQLP SGAGTASDKV ASQILQAYGM QGLNFCAKLH FKNTEKAKKR LER