RNH_CAMJJ
ID RNH_CAMJJ Reviewed; 146 AA.
AC A1W1N8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=CJJ81176_1627;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) 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}.
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; CP000538; EAQ72858.1; -; Genomic_DNA.
DR RefSeq; WP_002851277.1; NC_008787.1.
DR AlphaFoldDB; A1W1N8; -.
DR SMR; A1W1N8; -.
DR STRING; 354242.CJJ81176_1627; -.
DR PRIDE; A1W1N8; -.
DR EnsemblBacteria; EAQ72858; EAQ72858; CJJ81176_1627.
DR KEGG; cjj:CJJ81176_1627; -.
DR eggNOG; COG0328; Bacteria.
DR HOGENOM; CLU_030894_6_2_7; -.
DR OMA; MQEIEIF; -.
DR Proteomes; UP000000646; Chromosome.
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..146
FT /note="Ribonuclease H"
FT /id="PRO_0000332573"
FT DOMAIN 1..136
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 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
SQ SEQUENCE 146 AA; 16978 MW; 861A825C8ECF341B CRC64;
MKHIEIYTDG SCLNNPGFGG WAYILRYKEY QKEGFGAEAN TTNNRMELMA IIESLKALKE
PCEISLFTDS NLMVQSINEW LEGWIKKDFK GKKNIDLWKE YIKVAKSHKI KAFWVKAHNG
HLENERCDTL AREAALKIAR ENDEKH
