(data stored in ACNUC7421 zone)

SWISSPROT: RNH_SALTY

ID   RNH_SALTY               Reviewed;         155 AA.
AC   P0A2B9; P23329;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   11-DEC-2019, entry version 86.
DE   RecName: Full=Ribonuclease HI;
DE            Short=RNase HI;
DE            EC=3.1.26.4;
DE   AltName: Full=Ribonuclease H;
DE            Short=RNase H;
GN   Name=rnhA; Synonyms=rnh; OrderedLocusNames=STM0263;
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 [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=1650910; DOI=10.1007/bf00273935;
RA   Itaya M., McKelvin D., Chatterjie S.K., Crouch R.J.;
RT   "Selective cloning of genes encoding RNase H from Salmonella typhimurium,
RT   Saccharomyces cerevisiae and Escherichia coli rnh mutant.";
RL   Mol. Gen. Genet. 227:438-445(1991).
RN   [2]
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).
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=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a
CC       regulatory site, or after substrate binding. {ECO:0000250};
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
DR   EMBL; X57159; CAA40447.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19220.1; -; Genomic_DNA.
DR   PIR; S21659; S21659.
DR   RefSeq; NP_459261.1; NC_003197.2.
DR   RefSeq; WP_000917872.1; NC_003197.2.
DR   SMR; P0A2B9; -.
DR   PaxDb; P0A2B9; -.
DR   PRIDE; P0A2B9; -.
DR   EnsemblBacteria; AAL19220; AAL19220; STM0263.
DR   GeneID; 1251781; -.
DR   KEGG; stm:STM0263; -.
DR   PATRIC; fig|99287.12.peg.272; -.
DR   eggNOG; ENOG4108UMW; Bacteria.
DR   eggNOG; COG0328; LUCA.
DR   HOGENOM; HOG000040465; -.
DR   KO; K03469; -.
DR   OMA; MQEIEIF; -.
DR   PhylomeDB; P0A2B9; -.
DR   BioCyc; SENT99287:STM0263-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid 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:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR   CDD; cd09278; RNase_HI_prokaryote_like; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00042; RNase_H; 1.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR022892; RNaseHI.
DR   Pfam; PF00075; RNase_H; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS50879; RNASE_H; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0A2B9.
DR   SWISS-2DPAGE; P0A2B9.
KW   Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Reference proteome.
FT   CHAIN           1..155
FT                   /note="Ribonuclease HI"
FT                   /id="PRO_0000195402"
FT   DOMAIN          1..142
FT                   /note="RNase H"
FT   METAL           10
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000250"
FT   METAL           10
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000250"
FT   METAL           48
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000250"
FT   METAL           70
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000250"
FT   METAL           134
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   155 AA;  17510 MW;  AC48C60FD0881E74 CRC64;
     MLKQVEIFTD GSCLGNPGPG GYGAILRYRG HEKTFSEGYT LTTNNRMELM AAIVALEALK
     EHCEVTLSTD SQYVRQGITQ WIHNWKKRGW KTAEKKPVKN VDLWKRLDAA LGQHQIKWVW
     VKGHAGHPEN ERCDELARAA AMNPTQEDSG YQAEA
//

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