ID C3Q939_9BACE Unreviewed; 211 AA.
AC C3Q939;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Ribonuclease H {ECO:0000256|PIRNR:PIRNR037839};
DE EC=3.1.26.4 {ECO:0000256|PIRNR:PIRNR037839};
GN Name=rnhA {ECO:0000313|EMBL:EEO48473.1};
GN ORFNames=BSAG_00183 {ECO:0000313|EMBL:EEO48473.1};
OS Bacteroides sp. D1.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=556258 {ECO:0000313|EMBL:EEO48473.1, ECO:0000313|Proteomes:UP000003361};
RN [1] {ECO:0000313|EMBL:EEO48473.1, ECO:0000313|Proteomes:UP000003361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1 {ECO:0000313|EMBL:EEO48473.1,
RC ECO:0000313|Proteomes:UP000003361};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C.,
RA White A., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. D1.";
RL Submitted (MAY-2011) 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:EEO48473.1}.
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DR EMBL; ACAB02000085; EEO48473.1; -; Genomic_DNA.
DR RefSeq; WP_004314488.1; NZ_JH114344.1.
DR AlphaFoldDB; C3Q939; -.
DR HOGENOM; CLU_080985_1_0_10; -.
DR Proteomes; UP000003361; 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 Pfam; PF00075; RNase_H; 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, ECO:0000313|EMBL:EEO48473.1};
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}.
FT DOMAIN 78..211
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
SQ SEQUENCE 211 AA; 23715 MW; 31F9914220074E08 CRC64;
MAKQKFYVVW EGVTPGIYTS WTDCQLQIKG YEAAKYKSFD TREEAERALT MSPYAYIGKN
AKSKSGGSKP SSDTLPSCVI DNSLAVDAAC SGNPGPMEYR GVHIASRQEI FHFGPMKGTN
NIGEFLAIVH GLALLKNKGF DMPIYSDSAN AISWVRQKKC KTKLPRTPET EELFLLIERA
EKWLQGNTYT TRILKWETKE WGEIPADFGR K
//
