GenomeNet

Database: UniProt
Entry: A0A1G8GIL2_9MICO
LinkDB: A0A1G8GIL2_9MICO
Original site: A0A1G8GIL2_9MICO 
ID   A0A1G8GIL2_9MICO        Unreviewed;       218 AA.
AC   A0A1G8GIL2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE            EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN   ORFNames=SAMN04489720_2946 {ECO:0000313|EMBL:SDH94127.1};
OS   Agrococcus jejuensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agrococcus.
OX   NCBI_TaxID=399736 {ECO:0000313|EMBL:SDH94127.1, ECO:0000313|Proteomes:UP000198822};
RN   [1] {ECO:0000313|EMBL:SDH94127.1, ECO:0000313|Proteomes:UP000198822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22002 {ECO:0000313|EMBL:SDH94127.1,
RC   ECO:0000313|Proteomes:UP000198822};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000256|ARBA:ARBA00004065,
CC       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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT629695; SDH94127.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8GIL2; -.
DR   STRING; 399736.SAMN04489720_2946; -.
DR   Proteomes; UP000198822; Chromosome i.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd07182; RNase_HII_bacteria_HII_like; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; RIBONUCLEASE H2 SUBUNIT A; 1.
DR   PANTHER; PTHR10954:SF18; RIBONUCLEASE HII; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW   ProRule:PRU01319};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01319}; Manganese {ECO:0000256|ARBA:ARBA00023211};
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}.
FT   DOMAIN          18..217
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51975"
FT   BINDING         24
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT   BINDING         25
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT   BINDING         121
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
SQ   SEQUENCE   218 AA;  22850 MW;  BC901510CB3A3A4E CRC64;
     MSVAPTLEVE TALWDRRPLV IGMDEVGRGA LAGPVSVGAF ALTRCDVVPE GLRDSKAMTA
     RARERTAPIV REWGIAAVGH ASAAEIDAVG IMAALAIAGR RALEELHAAG VDVVSSALLL
     DGSHDWLSPR LRRPLAITLR PKADRDCGSV AGAACVAKVE RDALMVAHDA EHPGYGWASN
     KGYAAAVHMD AIRTLGPTRL HRRTWLKSDG AVSASAAA
//
DBGET integrated database retrieval system