RNH2_CHLFF
ID RNH2_CHLFF Reviewed; 209 AA.
AC Q255A9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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}; OrderedLocusNames=CF0357;
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_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}.
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DR EMBL; AP006861; BAE81129.1; -; Genomic_DNA.
DR RefSeq; WP_011457909.1; NC_007899.1.
DR AlphaFoldDB; Q255A9; -.
DR SMR; Q255A9; -.
DR STRING; 264202.CF0357; -.
DR KEGG; cfe:CF0357; -.
DR eggNOG; COG0164; Bacteria.
DR HOGENOM; CLU_036532_3_2_0; -.
DR OMA; YPTKLHL; -.
DR OrthoDB; 1685277at2; -.
DR Proteomes; UP000001260; 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..209
FT /note="Ribonuclease HII"
FT /id="PRO_0000334873"
FT DOMAIN 26..209
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 32
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT BINDING 33
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT BINDING 125
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
SQ SEQUENCE 209 AA; 23019 MW; FA8C960FABC8A4F2 CRC64;
MHTLVEEQLF LSKTIFEEEV FSEGFSIIAG VDEVGRGPLA GPVVAGACIL PRGKIFAGVN
DSKKLSPKER GRMRDILVND PDVYYGIGVV SVERIDEINI LEATKEAMAV AIANLPVHPD
FLLVDGLHLP HKIPCKKIIK GDSKVASIAA ASIIAKEYRD DLMRELHQRY PDYGFDKHKG
YGTAAHLAAL KAFGPCDCHR KSFAPIRRR