ID   RNH3_MYCGE              Reviewed;         235 AA.
AC   P47441;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2017, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Ribonuclease HIII {ECO:0000303|PubMed:16407165};
DE            Short=RNase HIII;
DE            EC=3.1.26.4 {ECO:0000250|UniProtKB:Q8EPH7};
GN   Name=rnhC {ECO:0000303|PubMed:16407165}; OrderedLocusNames=MG199;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16407165; DOI=10.1073/pnas.0510013103;
RA   Glass J.I., Assad-Garcia N., Alperovich N., Yooseph S., Lewis M.R.,
RA   Maruf M., Hutchison C.A. III, Smith H.O., Venter J.C.;
RT   "Essential genes of a minimal bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:425-430(2006).
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   -!- DISRUPTION PHENOTYPE: Probably essential, it was not disrupted in a
CC       global transposon mutagenesis study. {ECO:0000269|PubMed:16407165}.
CC   -!- SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L43967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; I64221; I64221.
DR   RefSeq; WP_009885740.1; NZ_AAGX01000004.1.
DR   AlphaFoldDB; P47441; -.
DR   SMR; P47441; -.
DR   OrthoDB; 1685277at2; -.
DR   BioCyc; MGEN243273:G1GJ2-231-MON; -.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR   GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
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..235
FT                   /note="Ribonuclease HIII"
FT                   /id="PRO_0000210450"
FT   DOMAIN          9..235
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   235 AA;  26746 MW;  F5A51AB3B5A86451 CRC64;
     MQHYKPADFY LIGSDESGKG DSFGGICVSA VLIEKKQLIN LENLQVTDSK KLSDHTVKLL
     AKSIQTTVMD HHTITLDPKQ YNDLTKSLKN TNLLLTNLHC QLYQKLLEKN QLLRQTVTIS
     IDQFANQELF VNYLNKLTNF TDKTVLLPDQ FLINGETKSL VIAAASILAR DSFINQLQLL
     NQKVNYDLPK GSSHGIEQAL LFLNQQRGFS QIEQFKQVAK LNFKNVTKFL QQLVY