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Database: UniProt
Entry: R6E5G8_9BACT
LinkDB: R6E5G8_9BACT
Original site: R6E5G8_9BACT 
ID   R6E5G8_9BACT            Unreviewed;       157 AA.
AC   R6E5G8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Ribonuclease H {ECO:0000256|PIRNR:PIRNR037839};
DE            EC=3.1.26.4 {ECO:0000256|PIRNR:PIRNR037839};
GN   ORFNames=BN487_01245 {ECO:0000313|EMBL:CDA95015.1};
OS   Prevotella sp. CAG:1320.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262922 {ECO:0000313|EMBL:CDA95015.1, ECO:0000313|Proteomes:UP000018111};
RN   [1] {ECO:0000313|EMBL:CDA95015.1, ECO:0000313|Proteomes:UP000018111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1320 {ECO:0000313|Proteomes:UP000018111};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDA95015.1}.
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DR   EMBL; CBCU010000061; CDA95015.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6E5G8; -.
DR   STRING; 1262922.BN487_01245; -.
DR   Proteomes; UP000018111; 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   InterPro; IPR017290; RNase_H_bac.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00075; RNase_H; 1.
DR   PIRSF; PIRSF037839; Ribonuclease_H; 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:UP000018111}.
FT   DOMAIN          23..157
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   BINDING         32
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT   BINDING         93
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
SQ   SEQUENCE   157 AA;  17639 MW;  461D281211353BD7 CRC64;
     MAKKKLENPP EWRNDTVLPL PLEVKANAWA VDAGCSGNPG PMEYQAIDLA TGEKVFHYGP
     LHGTNNIGEF LAIVHALALM EQRGITDKVI YSDSVNAMLW VSKKQCKTKL ERTPQTAELY
     DIIARAEAWL RTHAVKTPIL KWETKKWGEI PADFGRK
//
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