RNH_COXBR
ID RNH_COXBR Reviewed; 154 AA.
AC A9NB52;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
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};
GN OrderedLocusNames=COXBURSA331_A0424;
OS Coxiella burnetii (strain RSA 331 / Henzerling II).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=360115;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 331 / Henzerling II;
RA Seshadri R., Samuel J.E.;
RT "Genome sequencing of phylogenetically and phenotypically diverse Coxiella
RT burnetii isolates.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000890; ABX77470.1; -; Genomic_DNA.
DR RefSeq; WP_010957501.1; NC_010117.1.
DR AlphaFoldDB; A9NB52; -.
DR SMR; A9NB52; -.
DR KEGG; cbs:COXBURSA331_A0424; -.
DR HOGENOM; CLU_030894_6_0_6; -.
DR OMA; MQEIEIF; -.
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..154
FT /note="Ribonuclease H"
FT /id="PRO_0000332586"
FT DOMAIN 5..146
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
SQ SEQUENCE 154 AA; 17662 MW; 82DC0A4806EAD4DF CRC64;
MAKQEQNIVY LYCDGACRGN PGPGGWGVLL RYNQHERQLH GGVANTTNNQ MELTAAIEGL
KSLKKPCQVV VTTDSQYLRR GITEWLPVWK RRGWRTSNKK PVKNQPLWET LEREVERHTI
VWHWVKGHSG HAENEIADEL ANRGIDEVLK RGVQ
