ID   RNH2_RHOE4              Reviewed;         226 AA.
AC   C0ZXT2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   10-JUN-2026, entry version 75.
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};
GN   OrderedLocusNames=RER_24590;
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Nocardiaceae; Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00052};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         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; AP008957; BAH33167.1; -; Genomic_DNA.
DR   RefSeq; WP_020907294.1; NC_012490.1.
DR   AlphaFoldDB; C0ZXT2; -.
DR   SMR; C0ZXT2; -.
DR   GeneID; 57487492; -.
DR   KEGG; rer:RER_24590; -.
DR   eggNOG; COG0164; Bacteria.
DR   HOGENOM; CLU_036532_1_0_11; -.
DR   Proteomes; UP000002204; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032299; C:ribonuclease H2 complex; IEA:TreeGrafter.
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:0043137; P:DNA replication, removal of RNA primer; IEA:TreeGrafter.
DR   GO; GO:0006298; P:mismatch repair; IEA:TreeGrafter.
DR   CDD; cd07182; RNase_HII_bacteria_HII_like; 1.
DR   FunFam; 3.30.420.10:FF:000113; Ribonuclease HII; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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   NCBIfam; NF000595; PRK00015.1-3; 1.
DR   NCBIfam; NF000598; PRK00015.2-2; 1.
DR   NCBIfam; NF000600; PRK00015.2-4; 1.
DR   PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR   PANTHER; PTHR10954:SF18; RIBONUCLEASE HII; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 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..226
FT                   /note="Ribonuclease HII"
FT                   /id="PRO_1000202290"
FT   DOMAIN          29..220
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         35
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT   BINDING         36
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT   BINDING         129
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
SQ   SEQUENCE   226 AA;  23679 MW;  5441D0E411AF88B5 CRC64;
     MSSWPPRVVI RRSAGLRTME SALARTGLGP VAGVDEAGRG ACAGPLVIAA CVLAPKPQAA
     LARLDDSKKL TERAREELFP AIKRLALAWS VVSVPAAEVD QIGIHVANIE GMRRAVAGLD
     LEPGYVLTDG FRVPGLTAPS LPVIGGDGAA ACIAAASVLA KVTRDRVMTE MDETHPGYGF
     AIHKGYSTPL HMDALDELGP CPEHRMTYAN VVAAGVRLEQ RAGRTG
//