ID   RNH2_CAMC1              Reviewed;         184 AA.
AC   A7ZG16;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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};
GN   OrderedLocusNames=Ccon26_18890; ORFNames=CCC13826_0342;
OS   Campylobacter concisus (strain 13826).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13826;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., On S., Nelson K.E.;
RT   "Genome sequence of Campylobacter concisus 13826 isolated from human
RT   feces.";
RL   Submitted (OCT-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_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;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-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}.
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; CP000792; EAT97651.1; -; Genomic_DNA.
DR   RefSeq; WP_012140565.1; NC_009802.2.
DR   AlphaFoldDB; A7ZG16; -.
DR   SMR; A7ZG16; -.
DR   STRING; 360104.CCC13826_0342; -.
DR   EnsemblBacteria; EAT97651; EAT97651; CCC13826_0342.
DR   KEGG; cco:CCC13826_0342; -.
DR   eggNOG; COG0164; Bacteria.
DR   HOGENOM; CLU_036532_3_1_7; -.
DR   OMA; DGKHDYL; -.
DR   OrthoDB; 1685277at2; -.
DR   Proteomes; UP000001121; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07182; RNase_HII_bacteria_HII_like; 1.
DR   Gene3D; 3.30.420.10; -; 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   PANTHER; PTHR10954; PTHR10954; 1.
DR   PANTHER; PTHR10954:SF18; PTHR10954:SF18; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS51975; RNASE_H_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Manganese; Metal-binding; Nuclease.
FT   CHAIN           1..184
FT                   /note="Ribonuclease HII"
FT                   /id="PRO_0000334869"
FT   DOMAIN          2..184
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         8
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT   BINDING         9
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT   BINDING         95
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
SQ   SEQUENCE   184 AA;  20115 MW;  38085D4D8A6E1C36 CRC64;
     MAKICGIDEA GRGALAGPLS VAACVLNSEI SGLNDSKKLT AKRREELFKK ITKSSNFLIA
     YFSNAQIDEL GLSECLRRAL KLFKAHFESF EIIYDGNLDY GVGITTMIKA DGKVAGVSAA
     SILAKVSRDR LMNGWDKFYP AYGFAGHKGY GTKSHLDAIA KFGYSDFHRK SFVIKPKLAQ
     SSLF