RNH2_SALTY
ID RNH2_SALTY Reviewed; 198 AA.
AC P0A2C1; P40675;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Ribonuclease HII;
DE Short=RNase HII;
DE EC=3.1.26.4;
GN Name=rnhB; OrderedLocusNames=STM0230;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 155-198.
RX PubMed=2676978; DOI=10.1128/jb.171.10.5581-5586.1989;
RA Lancy E.D., Lifsics M.R., Munson P., Maurer R.;
RT "Nucleotide sequences of dnaE, the gene for the polymerase subunit of DNA
RT polymerase III in Salmonella typhimurium, and a variant that facilitates
RT growth in the absence of another polymerase subunit.";
RL J. Bacteriol. 171:5581-5586(1989).
RN [3]
RP IDENTIFICATION.
RX PubMed=7920643; DOI=10.1038/ng0694-205;
RA Robison K., Gilbert W., Church G.M.;
RT "Large scale bacterial gene discovery by similarity search.";
RL Nat. Genet. 7:205-214(1994).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000305}.
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DR EMBL; AE006468; AAL19194.1; -; Genomic_DNA.
DR EMBL; M26046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_459235.1; NC_003197.2.
DR RefSeq; WP_000569412.1; NC_003197.2.
DR AlphaFoldDB; P0A2C1; -.
DR SMR; P0A2C1; -.
DR STRING; 99287.STM0230; -.
DR PaxDb; P0A2C1; -.
DR EnsemblBacteria; AAL19194; AAL19194; STM0230.
DR GeneID; 1251748; -.
DR KEGG; stm:STM0230; -.
DR PATRIC; fig|99287.12.peg.243; -.
DR HOGENOM; CLU_036532_3_2_6; -.
DR OMA; YPTKLHL; -.
DR PhylomeDB; P0A2C1; -.
DR BioCyc; SENT99287:STM0230-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IBA:GO_Central.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR CDD; cd07182; RNase_HII_bacteria_HII_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00052_B; RNase_HII_B; 1.
DR InterPro; IPR022898; RNase_HII.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10954; PTHR10954; 1.
DR PANTHER; PTHR10954:SF18; PTHR10954:SF18; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Manganese; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..198
FT /note="Ribonuclease HII"
FT /id="PRO_0000111618"
FT DOMAIN 10..198
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 16
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT CONFLICT 182
FT /note="H -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21507 MW; 2228D600F5BF2D1B CRC64;
MIEFVYPHTH LVAGVDEVGR GPLVGAVVTA AVILDPARPI VGLNDSKKLS EKRRLSLYDE
IKEKALSWSL GRAEAHEIDE LNILHATMLA MQRAVAGLHI APEYVLIDGN RCPELPVPSM
AVVKGDSRVA EISAASILAK VTRDAEMAAL DIVFPQYGFA QHKGYPTAFH LEKLAQYGAT
AHHRRSFAPV KRALGLVS
