RNH2_ALKHC
ID RNH2_ALKHC Reviewed; 263 AA.
AC Q9Z9S0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ribonuclease HII;
DE Short=RNase HII;
DE EC=3.1.26.4;
GN Name=rnhB; Synonyms=rnh; OrderedLocusNames=BH2475;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=10086841; DOI=10.1007/s007920050095;
RA Takami H., Nakasone K., Hirama C., Takaki Y., Masui N., Fuji F.,
RA Nakamura Y., Inoue A.;
RT "An improved physical and genetic map of the genome of alkaliphilic
RT Bacillus sp. C-125.";
RL Extremophiles 3:21-28(1999).
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; BA000004; BAB06194.1; -; Genomic_DNA.
DR EMBL; AB013365; BAA75362.1; -; Genomic_DNA.
DR PIR; C83959; C83959.
DR RefSeq; WP_010898627.1; NC_002570.2.
DR AlphaFoldDB; Q9Z9S0; -.
DR SMR; Q9Z9S0; -.
DR STRING; 272558.10175095; -.
DR EnsemblBacteria; BAB06194; BAB06194; BAB06194.
DR KEGG; bha:BH2475; -.
DR eggNOG; COG0164; Bacteria.
DR HOGENOM; CLU_036532_2_1_9; -.
DR OMA; YPTKLHL; -.
DR OrthoDB; 1685277at2; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
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..263
FT /note="Ribonuclease HII"
FT /id="PRO_0000111538"
FT DOMAIN 74..262
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 80
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 263 AA; 29333 MW; 6F3B069211DE5D1E CRC64;
MSKRLSIKEI DALLRQGDAS IDETFLAMLK ADERKGVQSA LKRYERQLEK EKALWMEHEE
MLAYEKDLWA KGYEHVAGLD EVGRGPLAGP VVTAAVILPK DVQLPGLTDS KKLAKETRES
FYDRIKEVAL AWSVAIVPVT VIDEVNIYQA TKQGMMSAID QLSVNPDALL LDAMNLPLSL
PQQSLIKGDQ KSLSIAASSV LAKVTRDRYM ADLANRYPEY GFERHVGYGT EEHLAALNAH
GITPEHRRSF RPVQETAATR QTS
