RNH_MYCSM
ID RNH_MYCSM Reviewed; 159 AA.
AC Q07705;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ribonuclease H;
DE Short=RNase H;
DE EC=3.1.26.4;
GN Name=rnhA;
OS Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1772;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LR222;
RA Dawes S.S., Crouch R.J., Morris S.L., Mizrahi V.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-110.
RC STRAIN=LR222;
RX PubMed=8294019; DOI=10.1016/0378-1119(93)90481-h;
RA Mizrahi V., Huberts P., Dawes S.S., Dudding L.R.;
RT "A PCR method for the sequence analysis of the gyrA, polA and rnhA gene
RT segments from mycobacteria.";
RL Gene 136:287-290(1993).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a
CC regulatory site, or after substrate binding. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
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DR EMBL; U20115; AAA62124.1; -; Genomic_DNA.
DR RefSeq; WP_003896965.1; NZ_UGQO01000001.1.
DR AlphaFoldDB; Q07705; -.
DR SMR; Q07705; -.
DR GeneID; 66736859; -.
DR KEGG; msh:LI98_27505; -.
DR KEGG; msn:LI99_27500; -.
DR OMA; MQEIEIF; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; cd09278; RNase_HI_prokaryote_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00042; RNase_H; 1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR022892; RNaseHI.
DR Pfam; PF00075; RNase_H; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.
FT CHAIN 1..159
FT /note="Ribonuclease H"
FT /id="PRO_0000195382"
FT DOMAIN 2..144
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 45
FT /note="S -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="M -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 17529 MW; EF0875F3B6D9F2BF CRC64;
MSQDPVIIHT DGGCRPNPGP GGWGAVLRHR EHVREMFGGE AAVTSNNRME LTAPIMALEA
LTRPVTVHLY TDSTYVRNGI TKWVLGWERN GWMTAAKQPV KNVDLWQRLQ AACARHQVEW
FWVKGHSGIG DNELADELAT RGLQEAVGLT TSSAGTSLR
