RNH3_STAAR
ID RNH3_STAAR Reviewed; 312 AA.
AC Q6GHU5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=SAR1113;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG40116.1; -; Genomic_DNA.
DR RefSeq; WP_001284266.1; NC_002952.2.
DR AlphaFoldDB; Q6GHU5; -.
DR SMR; Q6GHU5; -.
DR KEGG; sar:SAR1113; -.
DR HOGENOM; CLU_059546_1_0_9; -.
DR OMA; TGDYFGP; -.
DR OrthoDB; 1685277at2; -.
DR Proteomes; UP000000596; 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_0000111694"
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 312 AA; 34978 MW; B843FF965CDD6CA2 CRC64;
MANIVFKLSD KDITTLMSRI SFDTENLPQG MKARAKYQNT TVNIYQSGKV MFQGNHAEAV
SEELLPQHSQ LNTNKTKKKN TANSSLEQTL MYDQFNCIGS DEAGSGDYFG PLTVCAAFVT
KEHVPILKTL GVDDSKKLTD TKIVELAEQL VTFIPHSLLT LHNEKYNIQQ AKGWTQVKMK
AVLHNEAIKN VLEKIDSSQL DYIVIDQFAK REVYSHYALS DIPLPKKTKF ETKGESKSLA
IAVASIISRY AFITYMDQIS KNINMTIPKG AGAKVDVIAA KIIKNYGISR LDSISKKHFK
NREKAQKILK PL
