ID R5MVJ7_9FIRM Unreviewed; 314 AA.
AC R5MVJ7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Ribonuclease HIII {ECO:0000256|HAMAP-Rule:MF_00053};
DE Short=RNase HIII {ECO:0000256|HAMAP-Rule:MF_00053};
DE EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_00053};
GN Name=rnhC {ECO:0000256|HAMAP-Rule:MF_00053};
GN ORFNames=BN804_00358 {ECO:0000313|EMBL:CCY93714.1};
OS Firmicutes bacterium CAG:884.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1262990 {ECO:0000313|EMBL:CCY93714.1, ECO:0000313|Proteomes:UP000018073};
RN [1] {ECO:0000313|EMBL:CCY93714.1, ECO:0000313|Proteomes:UP000018073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:884 {ECO:0000313|Proteomes:UP000018073};
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|ARBA:ARBA00004065, ECO:0000256|HAMAP-
CC Rule:MF_00053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077, ECO:0000256|HAMAP-
CC Rule:MF_00053, ECO:0000256|PROSITE-ProRule:PRU01319};
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|HAMAP-Rule:MF_00053,
CC ECO:0000256|PROSITE-ProRule:PRU01319};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00053,
CC 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|HAMAP-Rule:MF_00053, ECO:0000256|PROSITE-
CC ProRule:PRU01319};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00053}.
CC -!- SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.
CC {ECO:0000256|ARBA:ARBA00008378, ECO:0000256|HAMAP-Rule:MF_00053}.
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:CCY93714.1}.
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DR EMBL; CAZD010000018; CCY93714.1; -; Genomic_DNA.
DR AlphaFoldDB; R5MVJ7; -.
DR STRING; 1262990.BN804_00358; -.
DR Proteomes; UP000018073; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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; cd06590; RNase_HII_bacteria_HIII_like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 3.30.310.10; TATA-Binding Protein; 1.
DR HAMAP; MF_00053; RNase_HIII; 1.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR004641; RNase_HIII.
DR InterPro; IPR024568; RNase_HIII_N.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR NCBIfam; TIGR00716; rnhC; 1.
DR PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR PANTHER; PTHR10954:SF25; RIBONUCLEASE HIII; 1.
DR Pfam; PF11858; DUF3378; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR PIRSF; PIRSF037748; RnhC; 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, ECO:0000256|HAMAP-Rule:MF_00053};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00053};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00053};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00053};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00053};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00053};
KW Reference proteome {ECO:0000313|Proteomes:UP000018073}.
FT DOMAIN 104..314
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT BINDING 110
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00053,
FT ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 111
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00053,
FT ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 212
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00053,
FT ECO:0000256|PROSITE-ProRule:PRU01319"
SQ SEQUENCE 314 AA; 36206 MW; B60F6E79CE2E1006 CRC64;
MKQKTITLKV SENTRKEMEE FFQDLKREKT PPYAVFQADD CDTVVTLYES GKAVFQGHDA
DLSSQFWIER EKHLNPLKKV ETTDSSNNTK EKKEIIKNPK LYNATTIGSD EVGTGDYFGP
IIVTATYVEK ENVPFLEELG IRDSKKMTDE KILEVVPLII KKIPYNSIML TNKEYNSNHD
KYNMNKVKAI LHNKMLYKTK MEHPNYEYIV VDQFAEKYVY FNYLKESSNV VRDITFLTKA
EDQVLSVACA SVISRYLFLK EYDKLSGELG FILPKGAGPI VDEIGKKIVQ KFGKEKLNEV
AKLSFKNTEK ILNK
//
