ID   RNH3_MYCPN              Reviewed;         236 AA.
AC   P75446;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Ribonuclease HIII;
DE            Short=RNase HIII;
DE            EC=3.1.26.4 {ECO:0000250|UniProtKB:Q8EPH7};
GN   Name=rnhC; OrderedLocusNames=MPN_118; ORFNames=C09_orf143b, MP036;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
RN   [2]
RP   SEQUENCE REVISION.
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=10954595; DOI=10.1093/nar/28.17.3278;
RA   Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U.,
RA   Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., Yuan Y.P.,
RA   Herrmann R., Bork P.;
RT   "Re-annotating the Mycoplasma pneumoniae genome sequence: adding value,
RT   function and reading frames.";
RL   Nucleic Acids Res. 28:3278-3288(2000).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000250|UniProtKB:Q8EPH7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000250|UniProtKB:Q8EPH7};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q8EPH7};
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|UniProtKB:Q8EPH7};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8EPH7}.
CC   -!- SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U00089; AAG34735.1; -; Genomic_DNA.
DR   PIR; S73362; S73362.
DR   RefSeq; NP_109806.1; NC_000912.1.
DR   RefSeq; WP_010874475.1; NC_000912.1.
DR   AlphaFoldDB; P75446; -.
DR   SMR; P75446; -.
DR   IntAct; P75446; 8.
DR   STRING; 272634.MPN_118; -.
DR   EnsemblBacteria; AAG34735; AAG34735; MPN_118.
DR   GeneID; 66609233; -.
DR   KEGG; mpn:MPN_118; -.
DR   PATRIC; fig|272634.6.peg.125; -.
DR   HOGENOM; CLU_059546_3_1_14; -.
DR   OMA; TGDYFGP; -.
DR   BioCyc; MPNE272634:G1GJ3-197-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.420.10; -; 1.
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   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; Metal-binding; Nuclease;
KW   Reference proteome.
FT   CHAIN           1..236
FT                   /note="Ribonuclease HIII"
FT                   /id="PRO_0000210451"
FT   DOMAIN          9..236
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         15
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EPH7"
FT   BINDING         16
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EPH7"
FT   BINDING         122
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EPH7"
SQ   SEQUENCE   236 AA;  26322 MW;  699BBEB5B3D79359 CRC64;
     MQHANTTALY LIGSDESGKG DSFGGIAVSA VLIHKDKINT LHQIGVGDSK QFNDYQIKAL
     VPKIKAAVHD QVTLSVDAKT YNQLVQSFKN VNVMLTFLHC KVYHQLLQQN KLTAQQCDIS
     IDEFANVKLF TQYTQKLTSL QNELKELVIP NHFLIRGESY SKVIAAASIL ARAAFIAQME
     QLSHQYGVQF PKGSAHGIVE ALHLLKTKRQ FHKFAQYSAV CKTTFKNVAS FLKQLA