RNH2_LIMRD
ID RNH2_LIMRD Reviewed; 256 AA.
AC A5VJL7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Ribonuclease HII {ECO:0000255|HAMAP-Rule:MF_00052};
DE Short=RNase HII {ECO:0000255|HAMAP-Rule:MF_00052};
DE EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00052};
GN Name=rnhB {ECO:0000255|HAMAP-Rule:MF_00052}; OrderedLocusNames=Lreu_0777;
OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557436;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20016;
RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA Kyrpides N.C., Walter J.;
RT "The evolution of host specialization in the vertebrate gut symbiont
RT Lactobacillus reuteri.";
RL PLoS Genet. 7:E1001314-E1001314(2011).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000255|HAMAP-Rule:MF_00052}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
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_00052};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00052}.
CC -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000255|HAMAP-
CC Rule:MF_00052}.
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DR EMBL; CP000705; ABQ83041.1; -; Genomic_DNA.
DR RefSeq; WP_003668089.1; NZ_AZDD01000015.1.
DR AlphaFoldDB; A5VJL7; -.
DR SMR; A5VJL7; -.
DR STRING; 557436.Lreu_0777; -.
DR EnsemblBacteria; ABQ83041; ABQ83041; Lreu_0777.
DR GeneID; 66470922; -.
DR KEGG; lre:Lreu_0777; -.
DR PATRIC; fig|557436.17.peg.451; -.
DR eggNOG; COG0164; Bacteria.
DR HOGENOM; CLU_036532_2_1_9; -.
DR OMA; YPTKLHL; -.
DR Proteomes; UP000001991; 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..256
FT /note="Ribonuclease HII"
FT /id="PRO_1000057379"
FT DOMAIN 72..256
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 78
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT BINDING 79
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT BINDING 170
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
SQ SEQUENCE 256 AA; 29011 MW; 08DB35367F9E7676 CRC64;
MNKETISQIK ARLQTITDTT DPYLQTIHDD SRKGVQTAIQ QFERRLARQK EAEEAFNNRF
KYEKYYWENG CQYIAGMDEV GRGPLAGPVV TCAVILNADF DLIGVTDSKQ LTRHERENLY
LRIVDEAVEV SIAVNDAPVI DQMNIYAATQ DAMIRAVNHL HHRPDHLIVD AVPLAIDIPQ
TTLIKGDQKS ISVAAASIVA KEYRDHLMRD YDYVYPGYGF AQNMGYGTKE HLAGLEKMGA
TPIHRRSFNP VPKYLN
