ID A4YEI4_METS5 Unreviewed; 208 AA.
AC A4YEI4;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN OrderedLocusNames=Msed_0661 {ECO:0000313|EMBL:ABP94836.1};
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP94836.1, ECO:0000313|Proteomes:UP000000242};
RN [1] {ECO:0000313|EMBL:ABP94836.1, ECO:0000313|Proteomes:UP000000242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
RC {ECO:0000313|Proteomes:UP000000242};
RX PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000256|RuleBase:RU003515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077, ECO:0000256|PROSITE-
CC ProRule:PRU01319, ECO:0000256|RuleBase:RU003515};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01319};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01319};
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:0000256|PROSITE-ProRule:PRU01319};
CC -!- SIMILARITY: Belongs to the RNase HII family.
CC {ECO:0000256|ARBA:ARBA00007383, ECO:0000256|RuleBase:RU003515}.
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DR EMBL; CP000682; ABP94836.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YEI4; -.
DR STRING; 399549.Msed_0661; -.
DR KEGG; mse:Msed_0661; -.
DR eggNOG; arCOG04121; Archaea.
DR HOGENOM; CLU_036532_0_4_2; -.
DR Proteomes; UP000000242; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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; cd07180; RNase_HII_archaea_like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 1.10.10.460; Ribonuclease hii. Domain 2; 1.
DR InterPro; IPR004649; RNase_H2_suA.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00729; ribonuclease HII; 1.
DR PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR PANTHER; PTHR10954:SF7; RIBONUCLEASE H2 SUBUNIT A; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE-
KW ProRule:PRU01319}; Reference proteome {ECO:0000313|Proteomes:UP000000242}.
FT DOMAIN 1..204
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT BINDING 6
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 7
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 103
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
SQ SEQUENCE 208 AA; 23120 MW; 49801B0B1221C4E6 CRC64;
MRIGIDEAGR GCLIGPMVVV GVALNERSIV ALKQSGVKDS KKLTRKKREE LFDLILSESE
GVAVAKALPE EIDNNNLNSL TYTKVIEIID ALSWLNPEVV TVDKVGKEIE VIRAIEDLGF
KPNVVHKADE LFVEASSASI VAKVIRDRLI ESLKKEFGDF GSGYPSDRKT VQWVLDLVSR
GEEPPNIIRR SWKLLLKYAP GFYVNKVS
//
