ID   RNH2_PASMU              Reviewed;         197 AA.
AC   P57986;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Ribonuclease HII;
DE            Short=RNase HII;
DE            EC=3.1.26.4;
GN   Name=rnhB; OrderedLocusNames=PM1998;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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. {ECO:0000305}.
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DR   EMBL; AE004439; AAK04082.1; -; Genomic_DNA.
DR   RefSeq; WP_005725099.1; NC_002663.1.
DR   AlphaFoldDB; P57986; -.
DR   SMR; P57986; -.
DR   STRING; 747.DR93_2101; -.
DR   EnsemblBacteria; AAK04082; AAK04082; PM1998.
DR   KEGG; pmu:PM1998; -.
DR   HOGENOM; CLU_036532_3_2_6; -.
DR   OMA; YPTKLHL; -.
DR   Proteomes; UP000000809; 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;
KW   Reference proteome.
FT   CHAIN           1..197
FT                   /note="Ribonuclease HII"
FT                   /id="PRO_0000111598"
FT   DOMAIN          10..197
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         16
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   197 AA;  21589 MW;  CAA9F9C64442C7BB CRC64;
     MVFEYPKGVE LIAGVDEVGR GPLVGAVVTA AVILDPHQPI LGLNDSKKLS EKKRLLLAEE
     IKQKALAWSL GRAEAEEIDQ LNILHATMLA MKRAVENLKI QPHFVLVDGN RVPELMIPAQ
     AIVKGDGLVA EISAASILAK VARDQEMAEL DKRYPEYAFA QHKGYPTALH LAKLAELGPL
     AQHRRSFAPV RKLLNTL