ID RNH_SHEON Reviewed; 158 AA.
AC Q8EE30;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Ribonuclease HI {ECO:0000255|HAMAP-Rule:MF_00042};
DE Short=RNase HI {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=SO_2560;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN55590.1; -; Genomic_DNA.
DR RefSeq; NP_718146.1; NC_004347.2.
DR RefSeq; WP_011072513.1; NZ_CP053946.1.
DR PDB; 2E4L; X-ray; 2.00 A; A=1-158.
DR PDB; 2ZQB; X-ray; 2.49 A; A/B/C/D=1-158.
DR PDBsum; 2E4L; -.
DR PDBsum; 2ZQB; -.
DR AlphaFoldDB; Q8EE30; -.
DR SMR; Q8EE30; -.
DR STRING; 211586.SO_2560; -.
DR PaxDb; 211586-SO_2560; -.
DR KEGG; son:SO_2560; -.
DR PATRIC; fig|211586.12.peg.2464; -.
DR eggNOG; COG0328; Bacteria.
DR HOGENOM; CLU_030894_6_0_6; -.
DR OrthoDB; 7845843at2; -.
DR PhylomeDB; Q8EE30; -.
DR BioCyc; SONE211586:G1GMP-2347-MONOMER; -.
DR BRENDA; 3.1.26.4; 11242.
DR EvolutionaryTrace; Q8EE30; -.
DR Proteomes; UP000008186; 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; IBA:GO_Central.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR CDD; cd09278; RNase_HI_prokaryote_like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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 PANTHER; PTHR10642; RIBONUCLEASE H1; 1.
DR PANTHER; PTHR10642:SF26; RIBONUCLEASE H1; 1.
DR Pfam; PF00075; RNase_H; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Reference proteome.
FT CHAIN 1..158
FT /note="Ribonuclease HI"
FT /id="PRO_0000195403"
FT DOMAIN 3..144
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 72
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"
FT STRAND 6..30
FT /evidence="ECO:0007829|PDB:2E4L"
FT STRAND 33..44
FT /evidence="ECO:0007829|PDB:2E4L"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:2E4L"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:2E4L"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:2E4L"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:2E4L"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2E4L"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2E4L"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:2E4L"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:2E4L"
FT HELIX 130..144
FT /evidence="ECO:0007829|PDB:2E4L"
SQ SEQUENCE 158 AA; 17782 MW; BDEBAE51CC162E4B CRC64;
MTELKLIHIF TDGSCLGNPG PGGYGIVMNY KGHTKEMSDG FSLTTNNRME LLAPIVALEA
LKEPCKIILT SDSQYMRQGI MTWIHGWKKK GWMTSNRTPV KNVDLWKRLD KAAQLHQIDW
RWVKGHAGHA ENERCDQLAR AAAEANPTQI DTGYQAES
//
