RNH1_ALKHC
ID RNH1_ALKHC Reviewed; 196 AA.
AC Q9KEI9;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ribonuclease H;
DE Short=RNase H;
DE EC=3.1.26.4;
GN Name=rnhA; OrderedLocusNames=BH0863;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 59-196 OF MUTANT ASN-132 IN
RP COMPLEX WITH MAGNESIUM AND SUBSTRATE, FUNCTION, AND MUTAGENESIS OF GLU-109;
RP ASP-132; GLU-188 AND ASP-192.
RX PubMed=15989951; DOI=10.1016/j.cell.2005.04.024;
RA Nowotny M., Gaidamakov S.A., Crouch R.J., Yang W.;
RT "Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate
RT specificity and metal-dependent catalysis.";
RL Cell 121:1005-1016(2005).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000269|PubMed:15989951}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 2 metal ions per subunit. Manganese or magnesium.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
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DR EMBL; BA000004; BAB04582.1; -; Genomic_DNA.
DR PIR; G83757; G83757.
DR RefSeq; WP_010897036.1; NC_002570.2.
DR PDB; 1ZBF; X-ray; 1.50 A; A=59-196.
DR PDB; 1ZBI; X-ray; 1.85 A; A/B=59-196.
DR PDB; 1ZBL; X-ray; 2.20 A; A/B=59-191.
DR PDB; 2G8F; X-ray; 1.65 A; A=59-196.
DR PDB; 2G8H; X-ray; 1.85 A; A=59-196.
DR PDB; 2G8I; X-ray; 1.65 A; A=59-196.
DR PDB; 2G8K; X-ray; 1.65 A; A=59-196.
DR PDB; 2G8U; X-ray; 2.70 A; A=59-196.
DR PDB; 2G8V; X-ray; 1.85 A; A=59-196.
DR PDB; 2G8W; X-ray; 2.05 A; A=59-196.
DR PDB; 2R7Y; X-ray; 1.80 A; A=62-193.
DR PDB; 3D0P; X-ray; 1.80 A; A/C=61-194.
DR PDB; 3EY1; X-ray; 1.60 A; A=59-196.
DR PDB; 3I8D; X-ray; 1.61 A; A/C=62-193.
DR PDB; 3TWH; X-ray; 1.79 A; A=59-196.
DR PDB; 3ULD; X-ray; 1.60 A; A=59-196.
DR PDB; 4HTU; X-ray; 1.49 A; A/B=61-194.
DR PDB; 4HUE; X-ray; 1.56 A; A/B=61-194.
DR PDB; 4HUF; X-ray; 1.69 A; A/B=61-194.
DR PDB; 4HUG; X-ray; 1.64 A; A/B=61-194.
DR PDB; 4OPJ; X-ray; 1.54 A; A/C=59-196.
DR PDB; 4OPK; X-ray; 1.54 A; A/C=59-196.
DR PDB; 5SWM; X-ray; 1.50 A; A/B=59-196.
DR PDB; 5US2; X-ray; 1.90 A; A=59-196.
DR PDB; 5USA; X-ray; 1.80 A; A=59-196.
DR PDB; 5USE; X-ray; 1.73 A; A=59-196.
DR PDB; 5USG; X-ray; 1.70 A; A=59-196.
DR PDB; 5VAJ; X-ray; 1.95 A; A/B=59-196.
DR PDB; 5W7N; X-ray; 1.80 A; A=62-193.
DR PDB; 5W7O; X-ray; 1.75 A; A=62-193.
DR PDB; 5WJR; X-ray; 1.70 A; A=59-196.
DR PDB; 6DMN; X-ray; 1.27 A; A=59-196.
DR PDB; 6DMV; X-ray; 1.52 A; A=59-196.
DR PDB; 6DO8; X-ray; 1.41 A; A=59-196.
DR PDB; 6DO9; X-ray; 1.36 A; A=61-196.
DR PDB; 6DOA; X-ray; 1.47 A; A=61-196.
DR PDB; 6DOB; X-ray; 1.34 A; A=59-196.
DR PDB; 6DOC; X-ray; 1.50 A; A=59-196.
DR PDB; 6DOD; X-ray; 1.53 A; A=59-196.
DR PDB; 6DOE; X-ray; 1.45 A; A=61-196.
DR PDB; 6DOF; X-ray; 1.43 A; A=59-196.
DR PDB; 6DOG; X-ray; 1.28 A; A=59-196.
DR PDB; 6DOH; X-ray; 1.36 A; A=61-193.
DR PDB; 6DOI; X-ray; 1.95 A; A=61-193.
DR PDB; 6DOJ; X-ray; 1.40 A; A=61-195.
DR PDB; 6DOK; X-ray; 1.38 A; A=61-195.
DR PDB; 6DOL; X-ray; 1.43 A; A=61-195.
DR PDB; 6DOM; X-ray; 1.43 A; A=61-196.
DR PDB; 6DON; X-ray; 1.42 A; A=61-196.
DR PDB; 6DOO; X-ray; 1.44 A; A=61-196.
DR PDB; 6DOP; X-ray; 1.25 A; A=59-196.
DR PDB; 6DOQ; X-ray; 1.42 A; A=59-196.
DR PDB; 6DOR; X-ray; 1.50 A; A=61-196.
DR PDB; 6DOS; X-ray; 1.32 A; A=61-195.
DR PDB; 6DOT; X-ray; 1.42 A; A=61-196.
DR PDB; 6DOU; X-ray; 1.49 A; A=61-196.
DR PDB; 6DOV; X-ray; 1.52 A; A=61-196.
DR PDB; 6DOW; X-ray; 1.50 A; A=61-196.
DR PDB; 6DOX; X-ray; 1.45 A; A=61-196.
DR PDB; 6DOY; X-ray; 1.45 A; A=59-196.
DR PDB; 6DOZ; X-ray; 1.57 A; A=59-196.
DR PDB; 6DP0; X-ray; 1.45 A; A=61-195.
DR PDB; 6DP1; X-ray; 1.42 A; A=59-196.
DR PDB; 6DP2; X-ray; 1.66 A; A=59-196.
DR PDB; 6DP3; X-ray; 1.46 A; A=59-196.
DR PDB; 6DP4; X-ray; 1.37 A; A=59-196.
DR PDB; 6DP5; X-ray; 1.43 A; A=59-196.
DR PDB; 6DP6; X-ray; 1.40 A; A=59-196.
DR PDB; 6DP7; X-ray; 1.38 A; A=61-195.
DR PDB; 6DP8; X-ray; 1.32 A; A=59-196.
DR PDB; 6DP9; X-ray; 1.40 A; A=61-196.
DR PDB; 6DPA; X-ray; 1.49 A; A=61-196.
DR PDB; 6DPB; X-ray; 1.32 A; A=61-196.
DR PDB; 6DPC; X-ray; 1.34 A; A=61-196.
DR PDB; 6DPD; X-ray; 1.46 A; A=61-196.
DR PDB; 6DPE; X-ray; 1.56 A; A=61-196.
DR PDB; 6DPF; X-ray; 1.56 A; A=61-196.
DR PDB; 6DPG; X-ray; 1.38 A; A=59-196.
DR PDB; 6DPH; X-ray; 1.34 A; A=59-196.
DR PDB; 6DPI; X-ray; 1.35 A; A=59-196.
DR PDB; 6DPJ; X-ray; 1.55 A; A=59-196.
DR PDB; 6DPK; X-ray; 1.39 A; A=59-196.
DR PDB; 6DPL; X-ray; 1.45 A; A=59-196.
DR PDB; 6DPM; X-ray; 1.68 A; A=59-196.
DR PDB; 6DPN; X-ray; 1.49 A; A=59-196.
DR PDB; 6DPO; X-ray; 1.45 A; A=59-196.
DR PDB; 6DPP; X-ray; 1.45 A; A=61-196.
DR PDBsum; 1ZBF; -.
DR PDBsum; 1ZBI; -.
DR PDBsum; 1ZBL; -.
DR PDBsum; 2G8F; -.
DR PDBsum; 2G8H; -.
DR PDBsum; 2G8I; -.
DR PDBsum; 2G8K; -.
DR PDBsum; 2G8U; -.
DR PDBsum; 2G8V; -.
DR PDBsum; 2G8W; -.
DR PDBsum; 2R7Y; -.
DR PDBsum; 3D0P; -.
DR PDBsum; 3EY1; -.
DR PDBsum; 3I8D; -.
DR PDBsum; 3TWH; -.
DR PDBsum; 3ULD; -.
DR PDBsum; 4HTU; -.
DR PDBsum; 4HUE; -.
DR PDBsum; 4HUF; -.
DR PDBsum; 4HUG; -.
DR PDBsum; 4OPJ; -.
DR PDBsum; 4OPK; -.
DR PDBsum; 5SWM; -.
DR PDBsum; 5US2; -.
DR PDBsum; 5USA; -.
DR PDBsum; 5USE; -.
DR PDBsum; 5USG; -.
DR PDBsum; 5VAJ; -.
DR PDBsum; 5W7N; -.
DR PDBsum; 5W7O; -.
DR PDBsum; 5WJR; -.
DR PDBsum; 6DMN; -.
DR PDBsum; 6DMV; -.
DR PDBsum; 6DO8; -.
DR PDBsum; 6DO9; -.
DR PDBsum; 6DOA; -.
DR PDBsum; 6DOB; -.
DR PDBsum; 6DOC; -.
DR PDBsum; 6DOD; -.
DR PDBsum; 6DOE; -.
DR PDBsum; 6DOF; -.
DR PDBsum; 6DOG; -.
DR PDBsum; 6DOH; -.
DR PDBsum; 6DOI; -.
DR PDBsum; 6DOJ; -.
DR PDBsum; 6DOK; -.
DR PDBsum; 6DOL; -.
DR PDBsum; 6DOM; -.
DR PDBsum; 6DON; -.
DR PDBsum; 6DOO; -.
DR PDBsum; 6DOP; -.
DR PDBsum; 6DOQ; -.
DR PDBsum; 6DOR; -.
DR PDBsum; 6DOS; -.
DR PDBsum; 6DOT; -.
DR PDBsum; 6DOU; -.
DR PDBsum; 6DOV; -.
DR PDBsum; 6DOW; -.
DR PDBsum; 6DOX; -.
DR PDBsum; 6DOY; -.
DR PDBsum; 6DOZ; -.
DR PDBsum; 6DP0; -.
DR PDBsum; 6DP1; -.
DR PDBsum; 6DP2; -.
DR PDBsum; 6DP3; -.
DR PDBsum; 6DP4; -.
DR PDBsum; 6DP5; -.
DR PDBsum; 6DP6; -.
DR PDBsum; 6DP7; -.
DR PDBsum; 6DP8; -.
DR PDBsum; 6DP9; -.
DR PDBsum; 6DPA; -.
DR PDBsum; 6DPB; -.
DR PDBsum; 6DPC; -.
DR PDBsum; 6DPD; -.
DR PDBsum; 6DPE; -.
DR PDBsum; 6DPF; -.
DR PDBsum; 6DPG; -.
DR PDBsum; 6DPH; -.
DR PDBsum; 6DPI; -.
DR PDBsum; 6DPJ; -.
DR PDBsum; 6DPK; -.
DR PDBsum; 6DPL; -.
DR PDBsum; 6DPM; -.
DR PDBsum; 6DPN; -.
DR PDBsum; 6DPO; -.
DR PDBsum; 6DPP; -.
DR AlphaFoldDB; Q9KEI9; -.
DR SMR; Q9KEI9; -.
DR STRING; 272558.10173478; -.
DR DrugBank; DB07652; 1-[2-DEOXYRIBOFURANOSYL]-2,4-DIFLUORO-5-METHYL-BENZENE-5'MONOPHOSPHATE.
DR EnsemblBacteria; BAB04582; BAB04582; BAB04582.
DR KEGG; bha:BH0863; -.
DR eggNOG; COG0328; Bacteria.
DR eggNOG; COG3341; Bacteria.
DR HOGENOM; CLU_080985_1_0_9; -.
DR OMA; KWETKAW; -.
DR OrthoDB; 1953872at2; -.
DR BRENDA; 3.1.13.2; 661.
DR BRENDA; 3.1.26.4; 661.
DR EvolutionaryTrace; Q9KEI9; -.
DR Proteomes; UP000001258; Chromosome.
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:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.40.970.10; -; 1.
DR InterPro; IPR009027; Ribosomal_L9/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; IPR036397; RNaseH_sf.
DR Pfam; PF01693; Cauli_VI; 1.
DR PIRSF; PIRSF037839; Ribonuclease_H; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55658; SSF55658; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..196
FT /note="Ribonuclease H"
FT /id="PRO_0000195430"
FT DOMAIN 58..196
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15989951"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15989951"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15989951"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15989951"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15989951"
FT MUTAGEN 109
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15989951"
FT MUTAGEN 132
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15989951"
FT MUTAGEN 188
FT /note="E->A: Strongly reduces activity."
FT /evidence="ECO:0000269|PubMed:15989951"
FT MUTAGEN 188
FT /note="E->Q: No effect."
FT /evidence="ECO:0000269|PubMed:15989951"
FT MUTAGEN 192
FT /note="D->N: Strongly reduced activity with manganese. Loss
FT of activity with magnesium."
FT /evidence="ECO:0000269|PubMed:15989951"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:6DOP"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:6DOP"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:6DOP"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:6DOP"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:6DOP"
FT HELIX 105..122
FT /evidence="ECO:0007829|PDB:6DOP"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6DOP"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:6DOP"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:6DOP"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:6DOP"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6DOP"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:6DOP"
SQ SEQUENCE 196 AA; 22373 MW; 4130558FA37D2A86 CRC64;
MAKSKYYVVW NGRKPGIYTS WSACEAQVKG YTGAKFKSYP SKEEAEAAFR GEEATPKLAK
EEIIWESLSV DVGSQGNPGI VEYKGVDTKT GEVLFEREPI PIGTNNMGEF LAIVHGLRYL
KERNSRKPIY SDSQTAIKWV KDKKAKSTLV RNEETALIWK LVDEAEEWLN THTYETPILK
WQTDKWGEIK ADYGRK
