ID   RNH3_CHLFF              Reviewed;         300 AA.
AC   Q253Q7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Ribonuclease HIII {ECO:0000255|HAMAP-Rule:MF_00053};
DE            Short=RNase HIII {ECO:0000255|HAMAP-Rule:MF_00053};
DE            EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00053};
GN   Name=rnhC {ECO:0000255|HAMAP-Rule:MF_00053}; OrderedLocusNames=CF0709;
OS   Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=264202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fe/C-56;
RX   PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA   Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA   Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA   Hattori M., Kuhara S., Shirai M.;
RT   "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL   DNA Res. 13:15-23(2006).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000255|HAMAP-Rule:MF_00053}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00053};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00053};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00053};
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_00053};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00053}.
CC   -!- SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00053}.
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DR   EMBL; AP006861; BAE81481.1; -; Genomic_DNA.
DR   RefSeq; WP_011458259.1; NC_007899.1.
DR   AlphaFoldDB; Q253Q7; -.
DR   SMR; Q253Q7; -.
DR   STRING; 264202.CF0709; -.
DR   KEGG; cfe:CF0709; -.
DR   eggNOG; COG1039; Bacteria.
DR   HOGENOM; CLU_059546_0_0_0; -.
DR   OMA; TGDYFGP; -.
DR   OrthoDB; 1685277at2; -.
DR   Proteomes; UP000001260; 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..300
FT                   /note="Ribonuclease HIII"
FT                   /id="PRO_1000031227"
FT   DOMAIN          86..300
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:0000255|HAMAP-Rule:MF_00053"
FT   BINDING         93
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00053"
FT   BINDING         196
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00053"
SQ   SEQUENCE   300 AA;  33312 MW;  CA8E87C8C7FD8042 CRC64;
     MSTPFVTTLS SSLYGLLKDR LEEKGFILTQ PQYTIFQARS PSVMCTLYSS GKLVVQGKGS
     KEFIEFFLEP EILLTFTHNR VEADLRPRLG VDESGKGDFF GPLCIAGVYA RDEETLKSLY
     KTKIQDSKLL NDAQILSLAK TIRSSCTYDV MILYPEKYNE LYGKFHNLNI LLAWAHATII
     DKLAPRPSGE VFAISDQFAS SESVLLNALK KKNTDISVIQ KVRAEQDIVV AAASILAREA
     FITTMTNLEQ RFSLKLPKGA SAQVKSVGKS ILNSRGKEVL SLVCKTHFKT FNEICDSASA