RNH3_CHLPN
ID RNH3_CHLPN Reviewed; 298 AA.
AC Q9Z6J1; Q9JQD2; Q9K1Y6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ribonuclease HIII;
DE Short=RNase HIII;
DE EC=3.1.26.4;
GN Name=rnhC; OrderedLocusNames=CPn_1068, CP_0782, CpB1112;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.
CC {ECO:0000305}.
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DR EMBL; AE001363; AAD19205.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38581.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA99275.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP99040.1; -; Genomic_DNA.
DR PIR; A86624; A86624.
DR PIR; C81538; C81538.
DR PIR; F72000; F72000.
DR RefSeq; NP_225262.1; NC_000922.1.
DR RefSeq; WP_010883701.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z6J1; -.
DR SMR; Q9Z6J1; -.
DR STRING; 115711.CP_0782; -.
DR EnsemblBacteria; AAD19205; AAD19205; CPn_1068.
DR EnsemblBacteria; AAF38581; AAF38581; CP_0782.
DR GeneID; 45051125; -.
DR KEGG; cpa:CP_0782; -.
DR KEGG; cpj:rnhB_2; -.
DR KEGG; cpn:CPn_1068; -.
DR KEGG; cpt:CpB1112; -.
DR PATRIC; fig|115713.3.peg.1168; -.
DR eggNOG; COG1039; Bacteria.
DR HOGENOM; CLU_059546_0_0_0; -.
DR OrthoDB; 1685277at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium 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; cd14796; RNAse_HIII_N; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00053; RNase_HIII; 1.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR004641; RNase_HIII.
DR InterPro; IPR024568; RNase_HIII_N.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR10954; PTHR10954; 1.
DR Pfam; PF11858; DUF3378; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR PIRSF; PIRSF037748; RnhC; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00716; rnhC; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.
FT CHAIN 1..298
FT /note="Ribonuclease HIII"
FT /id="PRO_0000111684"
FT DOMAIN 86..298
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 92
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 298 AA; 33272 MW; 637BF1AB648FC9FF CRC64;
MPPPFVVTLT TSAQNNLRDQ LKEKNFIFSQ PQNTVFQARS NTVTCTLYPS GKLVIQGKGS
EEFIEFFLEP EILHTFTHAR VEQDLRPRLG VDESGKGDFF GPLCIAAVYA SNAEILKKLY
ENKVQDSKNL KDTKIASLAR IIRSLCVCDV IILYPEKYNE LYGKFQNLNT LLAWAHATVI
NNLAPKPAGD VFAISDQFAA SEYTLLKALQ KKETDITLIQ KPRAEQDVVV AAASILARDA
FVQSIQKLEE QYQVQLPKGA GFNVKAAGRE IAKQRGKELL AKISKTHFKT FDEICSGK
