RNH_FRATO
ID RNH_FRATO Reviewed; 152 AA.
AC Q0BMB7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=FTH_0843;
OS Francisella tularensis subsp. holarctica (strain OSU18).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=393011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSU18;
RX PubMed=16980500; DOI=10.1128/jb.00506-06;
RA Petrosino J.F., Xiang Q., Karpathy S.E., Jiang H., Yerrapragada S., Liu Y.,
RA Gioia J., Hemphill L., Gonzalez A., Raghavan T.M., Uzman A., Fox G.E.,
RA Highlander S., Reichard M., Morton R.J., Clinkenbeard K.D., Weinstock G.M.;
RT "Chromosome rearrangement and diversification of Francisella tularensis
RT revealed by the type B (OSU18) genome sequence.";
RL J. Bacteriol. 188:6977-6985(2006).
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; CP000437; ABI82767.1; -; Genomic_DNA.
DR RefSeq; WP_003015471.1; NC_017463.1.
DR AlphaFoldDB; Q0BMB7; -.
DR SMR; Q0BMB7; -.
DR GeneID; 60806475; -.
DR KEGG; fth:FTH_0843; -.
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..152
FT /note="Ribonuclease H"
FT /id="PRO_0000332600"
FT DOMAIN 6..147
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
SQ SEQUENCE 152 AA; 16976 MW; 227BC97A79CCFD80 CRC64;
MEIFKKKNRV IAYTDGACKG NPGIGGWGAI LSYNGVDKEI YGSEKDTTNN RMELMAAIKT
LQALKRKCDI TIYTDSKYLQ NGINEWLANW KANGWKTAAK KEVKNKDLWQ ELDSLTNKHN
VTWGWVKGHS GNAGNEKADE LANKAIAELI GK
