RNH2_SACS2
ID RNH2_SACS2 Reviewed; 212 AA.
AC Q97W56;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=SSO2384;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; AE006641; AAK42532.1; -; Genomic_DNA.
DR PIR; E90409; E90409.
DR RefSeq; WP_009989457.1; NC_002754.1.
DR AlphaFoldDB; Q97W56; -.
DR SMR; Q97W56; -.
DR STRING; 273057.SSO2384; -.
DR EnsemblBacteria; AAK42532; AAK42532; SSO2384.
DR GeneID; 44128106; -.
DR KEGG; sso:SSO2384; -.
DR PATRIC; fig|273057.12.peg.2466; -.
DR eggNOG; arCOG04121; Archaea.
DR HOGENOM; CLU_036532_0_4_2; -.
DR InParanoid; Q97W56; -.
DR OMA; REECRFF; -.
DR PhylomeDB; Q97W56; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central.
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; 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; 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..212
FT /note="Ribonuclease HII"
FT /id="PRO_0000236286"
FT DOMAIN 1..204
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 6
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
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 103
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
SQ SEQUENCE 212 AA; 23925 MW; 2FCBF6D2623A488C CRC64;
MRVGIDEAGR GALIGPMIVA GVVISDTKLK FLKGIGVKDS KQLTRERREK LFDIVANTVE
AFTVVKVFPY EIDNYNLNDL TYDAVSKIIL SLSSFNPEIV TVDKVGDEKP VIELINKLGY
KSNVVHKADV LFVEASAASI IAKVIRDNYI DELKQVYGDF GSGYPADPRT IKWLKSFYEK
NPNPPPIIRR SWKILRSTAP LYYISKEGRR LW
