ID   RNH_CUPPJ               Reviewed;         145 AA.
AC   Q46Z81;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Ribonuclease H {ECO:0000255|HAMAP-Rule:MF_00042};
DE            Short=RNase H {ECO:0000255|HAMAP-Rule:MF_00042};
DE            EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00042};
GN   Name=rnhA {ECO:0000255|HAMAP-Rule:MF_00042}; OrderedLocusNames=Reut_A2189;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000255|HAMAP-Rule:MF_00042}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00042};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00042};
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:0000255|HAMAP-
CC       Rule:MF_00042};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00042}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00042}.
CC   -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000255|HAMAP-
CC       Rule:MF_00042}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000090; AAZ61552.1; -; Genomic_DNA.
DR   RefSeq; WP_011298346.1; NC_007347.1.
DR   AlphaFoldDB; Q46Z81; -.
DR   SMR; Q46Z81; -.
DR   STRING; 264198.Reut_A2189; -.
DR   EnsemblBacteria; AAZ61552; AAZ61552; Reut_A2189.
DR   KEGG; reu:Reut_A2189; -.
DR   eggNOG; COG0328; Bacteria.
DR   HOGENOM; CLU_030894_6_0_4; -.
DR   OMA; MQEIEIF; -.
DR   OrthoDB; 1953872at2; -.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
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; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.
FT   CHAIN           1..145
FT                   /note="Ribonuclease H"
FT                   /id="PRO_0000332659"
FT   DOMAIN          1..141
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT   BINDING         133
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
SQ   SEQUENCE   145 AA;  15981 MW;  B162425935449D06 CRC64;
     MQEVIIYSDG ACKGNPGRGG WGAVLVAGTN EKELFGGEAN TTNNRMEMTA VIEALRALKR
     PCTVQVYTDS QYVQKGISEW LPGWKARGWK TADKKPVKNA DLWQELDTLV QPHKITWHWV
     RGHNGHPGNE RADALANRGV ASLAS