ID   RNH2_STRAW              Reviewed;         233 AA.
AC   Q82KF0;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   28-JAN-2026, entry version 114.
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}; Synonyms=rnh;
GN   OrderedLocusNames=SAV_2453;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC70164.1; -; Genomic_DNA.
DR   RefSeq; WP_010983890.1; NC_003155.5.
DR   AlphaFoldDB; Q82KF0; -.
DR   SMR; Q82KF0; -.
DR   GeneID; 41539540; -.
DR   KEGG; sma:SAVERM_2453; -.
DR   eggNOG; COG0164; Bacteria.
DR   HOGENOM; CLU_036532_3_0_11; -.
DR   OrthoDB; 9803420at2; -.
DR   Proteomes; UP000000428; 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:000167; 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   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..233
FT                   /note="Ribonuclease HII"
FT                   /id="PRO_0000111631"
FT   DOMAIN          21..211
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         27
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT   BINDING         28
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT   BINDING         119
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
SQ   SEQUENCE   233 AA;  25206 MW;  ADD09E963161FE19 CRC64;
     MPYEPPTHTV ERSLRATTGA KVIAGVDEVG RGAWAGPVTV CAAITGLRRP PEGLTDSKLL
     TVKRRTVLAE ELRKWVTSYA LGHASPEEID ALGMTAALRL AAVRALEALP VRPDAVILDG
     KHDYLGSPWK VRTVIKGDQS CVAVAAASVI AKVQRDKMMA ELGIEHADFG FAANAGYPSP
     VHKAALAERG PTPYHRLSWA YLDALPQWRH LKKVRSWADG SVPEIEGQLG FDF
//