ID   RNH3_BACMK              Reviewed;         312 AA.
AC   A9VJL6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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};
GN   OrderedLocusNames=BcerKBAB4_4384;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY45543.1; -; Genomic_DNA.
DR   RefSeq; WP_012261790.1; NC_010184.1.
DR   AlphaFoldDB; A9VJL6; -.
DR   SMR; A9VJL6; -.
DR   STRING; 315730.BcerKBAB4_4384; -.
DR   EnsemblBacteria; ABY45543; ABY45543; BcerKBAB4_4384.
DR   KEGG; bwe:BcerKBAB4_4384; -.
DR   eggNOG; COG1039; Bacteria.
DR   HOGENOM; CLU_059546_1_0_9; -.
DR   OMA; TGDYFGP; -.
DR   Proteomes; UP000002154; 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..312
FT                   /note="Ribonuclease HIII"
FT                   /id="PRO_1000091673"
FT   DOMAIN          95..312
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         101
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00053"
FT   BINDING         102
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00053"
FT   BINDING         206
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00053"
SQ   SEQUENCE   312 AA;  34350 MW;  46252DA23266BD89 CRC64;
     MSNSIVIQTS STVIEDMKQQ YKQALSPKIP QGGIFMAKVP SCTITAYKSG KVMFQGGRAE
     AEASRWQTVS QTPKSTVKKS VNSHQYAPPS SIGTMSILGS DEVGTGDYFG PMTVVAVYVD
     AKQIPLLKEL GVKDSKNLND AQIAEIAKQL LHVVPYSSLV LHNEKYNELF DKGNNQGKLK
     ALLHNKAITN LLAKIAPTKP EGILIDQFTQ PDTYYKYLAK QKQVQRENVY FATKGESVHL
     AVAAASILAR YSFVKQFDEL SKKAGMQLPK GAGKQVDIAA AKLIQKVGKE RLPEFVKVHF
     ANTEKAFRLL KK