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RNH2_METBU
ID   RNH2_METBU              Reviewed;         213 AA.
AC   Q12YN9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Mbur_0450;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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; CP000300; ABE51437.1; -; Genomic_DNA.
DR   RefSeq; WP_011498599.1; NC_007955.1.
DR   AlphaFoldDB; Q12YN9; -.
DR   SMR; Q12YN9; -.
DR   STRING; 259564.Mbur_0450; -.
DR   EnsemblBacteria; ABE51437; ABE51437; Mbur_0450.
DR   GeneID; 3997646; -.
DR   KEGG; mbu:Mbur_0450; -.
DR   HOGENOM; CLU_036532_0_4_2; -.
DR   OMA; REECRFF; -.
DR   OrthoDB; 105421at2157; -.
DR   Proteomes; UP000001979; 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   Gene3D; 1.10.10.460; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00052_A; RNase_HII_A; 1.
DR   InterPro; IPR004649; RNase_H2_suA.
DR   InterPro; IPR001352; RNase_HII/HIII.
DR   InterPro; IPR024567; RNase_HII/HIII_dom.
DR   InterPro; IPR020787; RNase_HII_arc.
DR   InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_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   TIGRFAMs; TIGR00729; TIGR00729; 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..213
FT                   /note="Ribonuclease HII"
FT                   /id="PRO_0000334978"
FT   DOMAIN          1..213
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         7
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT   BINDING         8
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT   BINDING         105
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
SQ   SEQUENCE   213 AA;  23938 MW;  74EA43F6B5260DD8 CRC64;
     MKIIGIDEAG KGPVIGPMCI GGVRIDEDKS NALKNLGVAD SKKLSPKRRV HLAAQIKKYA
     DGWFVYEVSP NQIDELRKLM SMNDIMVLAF GSVIEELPSD KIYADAADVK EERFGKRLFD
     NYMEKHPDVS PPEVISKHGA DDLFPVVSAA SILAKVRRDE LIEKIKVDMG VDIGSGYPSD
     PKTKKFLENW YRENSSFPDI VRHSWKTAQK FIQ
 
 
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