RNH2_METM5
ID RNH2_METM5 Reviewed; 239 AA.
AC A4FWE5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=MmarC5_0204;
OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=402880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC BAA-1333;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000609; ABO34520.1; -; Genomic_DNA.
DR RefSeq; WP_011867978.1; NC_009135.1.
DR AlphaFoldDB; A4FWE5; -.
DR SMR; A4FWE5; -.
DR STRING; 402880.MmarC5_0204; -.
DR EnsemblBacteria; ABO34520; ABO34520; MmarC5_0204.
DR GeneID; 4928181; -.
DR KEGG; mmq:MmarC5_0204; -.
DR eggNOG; arCOG04121; Archaea.
DR HOGENOM; CLU_036532_0_4_2; -.
DR OMA; REECRFF; -.
DR OrthoDB; 105421at2157; -.
DR Proteomes; UP000000253; 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.
FT CHAIN 1..239
FT /note="Ribonuclease HII"
FT /id="PRO_0000334980"
FT DOMAIN 18..231
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 24
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT BINDING 25
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 239 AA; 27111 MW; 8D665A01EA45ABD6 CRC64;
MNEDIKNNLN NSDESNGKII VGLDEAGRGP VIGPMVIASV KINEKDLPRL DDLGLRDSKQ
LSKKKREELY TKISEICDVK KVVINPEKID EQMEIINLNK IELGAFSKLA NHFIKENENI
SIYIDACSSN EQSFSNQFKA KLINKNVEII AEHKADENYK IVSAASIIAK VTRDNVIEEY
KKTFGEIGSG YPSDPKTKKF LKNYVHENKG LPKIARKSWA TSKNLLKEIE ESKIFQWVK