ID G2EEM9_9FLAO Unreviewed; 213 AA.
AC G2EEM9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Ribonuclease H {ECO:0000256|PIRNR:PIRNR037839};
DE EC=3.1.26.4 {ECO:0000256|PIRNR:PIRNR037839};
GN ORFNames=BZARG_1131 {ECO:0000313|EMBL:EGV43135.1};
OS Bizionia argentinensis JUB59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Bizionia.
OX NCBI_TaxID=1046627 {ECO:0000313|EMBL:EGV43135.1, ECO:0000313|Proteomes:UP000003730};
RN [1] {ECO:0000313|EMBL:EGV43135.1, ECO:0000313|Proteomes:UP000003730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUB59 {ECO:0000313|EMBL:EGV43135.1,
RC ECO:0000313|Proteomes:UP000003730};
RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0;
RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M.,
RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., Criscuolo M.,
RA Memoli M., Arguelles M., Mac Cormack W.P.;
RT "Bizionia argentinensis sp. nov., isolated from surface marine water in
RT Antarctica.";
RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000256|PIRNR:PIRNR037839}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|PIRNR:PIRNR037839};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR037839-1};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR037839-1};
CC Note=Binds 2 metal ions per subunit. Manganese or magnesium.
CC {ECO:0000256|PIRSR:PIRSR037839-1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037839}.
CC -!- SIMILARITY: Belongs to the RNase H family.
CC {ECO:0000256|PIRNR:PIRNR037839}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGV43135.1}.
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DR EMBL; AFXZ01000034; EGV43135.1; -; Genomic_DNA.
DR RefSeq; WP_008637674.1; NZ_AFXZ01000034.1.
DR AlphaFoldDB; G2EEM9; -.
DR STRING; 1046627.BZARG_1131; -.
DR PATRIC; fig|1046627.3.peg.1970; -.
DR eggNOG; COG0328; Bacteria.
DR eggNOG; COG3341; Bacteria.
DR OrthoDB; 9811552at2; -.
DR Proteomes; UP000003730; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 3.40.970.10; Ribonuclease H1, N-terminal domain; 1.
DR InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR InterPro; IPR011320; RNase_H1_N.
DR InterPro; IPR037056; RNase_H1_N_sf.
DR InterPro; IPR017290; RNase_H_bac.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF01693; Cauli_VI; 1.
DR PIRSF; PIRSF037839; Ribonuclease_H; 1.
DR SUPFAM; SSF55658; L9 N-domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR037839};
KW Endonuclease {ECO:0000256|PIRNR:PIRNR037839};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037839};
KW Magnesium {ECO:0000256|PIRNR:PIRNR037839, ECO:0000256|PIRSR:PIRSR037839-1};
KW Manganese {ECO:0000256|PIRSR:PIRSR037839-1};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR037839,
KW ECO:0000256|PIRSR:PIRSR037839-1}; Nuclease {ECO:0000256|PIRNR:PIRNR037839};
KW Reference proteome {ECO:0000313|Proteomes:UP000003730}.
FT DOMAIN 79..213
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
SQ SEQUENCE 213 AA; 24353 MW; C8EB20F8E20607F3 CRC64;
MSKKKKKYYT VWKGHRTGVF ESWKDCKAQI KDYPSAVYKS FDTFDAAKKA LNSNYKDYIG
KKKGFKSELS DVQLKKIGLP NYNSISVDAA SSGNPGIMEY RGVDTKSKKQ LFIQGPFPEG
TNNIGEFLAL VHGLAFLKQH KSERILYTDS KIAMSWVRKK TCNTKLPRNA KNENLFVLVE
RAVNWLKENS YTTTVVKWET KAWGEIPADF GRK
//
