RNH3_BACC3
ID RNH3_BACC3 Reviewed; 311 AA.
AC C1ETZ4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=BCA_4661;
OS Bacillus cereus (strain 03BB102).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=572264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03BB102;
RA Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA Tapia R., Han C., Sutton G., Sims D.;
RT "Genome sequence of Bacillus cereus 03BB102.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001407; ACO31145.1; -; Genomic_DNA.
DR RefSeq; WP_000071580.1; NZ_CP009318.1.
DR AlphaFoldDB; C1ETZ4; -.
DR SMR; C1ETZ4; -.
DR PRIDE; C1ETZ4; -.
DR EnsemblBacteria; ACO31145; ACO31145; BCA_4661.
DR KEGG; bcx:BCA_4661; -.
DR PATRIC; fig|572264.18.peg.4610; -.
DR OMA; TGDYFGP; -.
DR Proteomes; UP000002210; 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..311
FT /note="Ribonuclease HIII"
FT /id="PRO_1000117700"
FT DOMAIN 95..311
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 311 AA; 34227 MW; D650F39DE7AF308D CRC64;
MSNSIVIQTN STVIEDMKQQ YKHSLSPKTP QGGIFMAKVP SCTITAYKSG KVMFQGGRAE
AEAARWQTVS QTPKTAVKKS VDSHRFAPPA SIGTMSIVGS DEVGTGDFFG PMTVVAVYVD
AKQIPLLKEL GVKDSKNLND EQITAIAKQL LHVVPYSSLV LHNEKYNELF DKGNNQGKLK
ALLHNKAITN LLAKMAPTKP EGVLIDQFTQ PDTYYKYLAK QKQVQRENVY FATKGESVHL
AVAAASILAR YSFVKQFNEL SKKAGMPLPK GAGKQVDIAA AKLIQKLGKE RLPEFVKLHF
ANTEKAFRLL K