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RNH_DESVH
ID   RNH_DESVH               Reviewed;         156 AA.
AC   Q72E89;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Ribonuclease H {ECO:0000255|HAMAP-Rule:MF_00042};
DE            Short=RNase H {ECO:0000255|HAMAP-Rule:MF_00042};
DE            EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00042};
GN   Name=rnhA {ECO:0000255|HAMAP-Rule:MF_00042}; OrderedLocusNames=DVU_0689;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000255|HAMAP-Rule:MF_00042}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00042};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00042};
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:0000255|HAMAP-
CC       Rule:MF_00042};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00042}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00042}.
CC   -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000255|HAMAP-
CC       Rule:MF_00042}.
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DR   EMBL; AE017285; AAS95170.1; -; Genomic_DNA.
DR   RefSeq; WP_010937992.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_009911.1; NC_002937.3.
DR   AlphaFoldDB; Q72E89; -.
DR   SMR; Q72E89; -.
DR   STRING; 882.DVU_0689; -.
DR   PaxDb; Q72E89; -.
DR   EnsemblBacteria; AAS95170; AAS95170; DVU_0689.
DR   KEGG; dvu:DVU_0689; -.
DR   PATRIC; fig|882.5.peg.645; -.
DR   eggNOG; COG0328; Bacteria.
DR   HOGENOM; CLU_030894_6_2_7; -.
DR   OMA; MQEIEIF; -.
DR   PhylomeDB; Q72E89; -.
DR   Proteomes; UP000002194; Chromosome.
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;
KW   Reference proteome.
FT   CHAIN           1..156
FT                   /note="Ribonuclease H"
FT                   /id="PRO_0000332590"
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:0000255|HAMAP-Rule:MF_00042"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT   BINDING         49
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
SQ   SEQUENCE   156 AA;  17414 MW;  E3A557413846F140 CRC64;
     MSQFDVTVFT DGSCLGNPGP GGWAAIMRCN GCEKELSGGF ALTTNNRMEI LAVLEALEAL
     RDPCKVTLFT DSQYVRNAVE KKWLAGWQRN GWKTADKKPV KNRDLWERLV PLLAKHSVSF
     RWVRGHSGHP ENERCDVLAR AQASRRGLPE DPGFTA
 
 
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