RNH_THET8
ID RNH_THET8 Reviewed; 166 AA.
AC P29253; Q5SI24;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Ribonuclease H;
DE Short=RNase H;
DE EC=3.1.26.4;
GN Name=rnhA; OrderedLocusNames=TTHA1556;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1653414; DOI=10.1093/nar/19.16.4443;
RA Itaya M., Kondo K.;
RT "Molecular cloning of a ribonuclease H (RNase HI) gene from an extreme
RT thermophile Thermus thermophilus HB8: a thermostable RNase H can
RT functionally replace the Escherichia coli enzyme in vivo.";
RL Nucleic Acids Res. 19:4443-4449(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PARTIAL PROTEIN SEQUENCE, SEQUENCE REVISION, AND CHARACTERIZATION.
RX PubMed=1315754; DOI=10.1016/s0021-9258(19)50217-4;
RA Kanaya S., Itaya M.;
RT "Expression, purification, and characterization of a recombinant
RT ribonuclease H from Thermus thermophilus HB8.";
RL J. Biol. Chem. 267:10184-10192(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=8385228; DOI=10.1006/jmbi.1993.1169;
RA Ishikawa K., Okumura M., Katayanagi K., Kimura S., Kanaya S., Nakamura H.,
RA Morikawa K.;
RT "Crystal structure of ribonuclease H from Thermus thermophilus HB8 refined
RT at 2.8-A resolution.";
RL J. Mol. Biol. 230:529-542(1993).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids.
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;
CC Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a
CC regulatory site, or after substrate binding.;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
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DR EMBL; X60507; CAA43026.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71379.1; -; Genomic_DNA.
DR RefSeq; WP_011228761.1; NC_006461.1.
DR RefSeq; YP_144822.1; NC_006461.1.
DR PDB; 1JL2; X-ray; 1.76 A; A/B/C/D=46-129.
DR PDB; 1RIL; X-ray; 2.80 A; A=1-166.
DR PDB; 2RPI; NMR; -; A=1-127.
DR PDBsum; 1JL2; -.
DR PDBsum; 1RIL; -.
DR PDBsum; 2RPI; -.
DR AlphaFoldDB; P29253; -.
DR BMRB; P29253; -.
DR SMR; P29253; -.
DR STRING; 300852.55772938; -.
DR EnsemblBacteria; BAD71379; BAD71379; BAD71379.
DR GeneID; 3168213; -.
DR KEGG; ttj:TTHA1556; -.
DR PATRIC; fig|300852.9.peg.1527; -.
DR eggNOG; COG0328; Bacteria.
DR HOGENOM; CLU_030894_6_2_0; -.
DR OMA; MQEIEIF; -.
DR PhylomeDB; P29253; -.
DR BRENDA; 3.1.26.4; 2305.
DR EvolutionaryTrace; P29253; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endonuclease; Hydrolase;
KW Magnesium; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..166
FT /note="Ribonuclease H"
FT /id="PRO_0000195410"
FT DOMAIN 5..147
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT REGION 128..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 45
FT /note="C -> W (in Ref. 1; CAA43026)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:2RPI"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:1RIL"
FT STRAND 22..30
FT /evidence="ECO:0007829|PDB:1RIL"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1RIL"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:1JL2"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1JL2"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:1JL2"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:1JL2"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1JL2"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1JL2"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:1JL2"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1JL2"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1RIL"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:1RIL"
SQ SEQUENCE 166 AA; 18728 MW; 6B152B4901BD7172 CRC64;
MNPSPRKRVA LFTDGACLGN PGPGGWAALL RFHAHEKLLS GGEACTTNNR MELKAAIEGL
KALKEPCEVD LYTDSHYLKK AFTEGWLEGW RKRGWRTAEG KPVKNRDLWE ALLLAMAPHR
VRFHFVKGHT GHPENERVDR EARRQAQSQA KTPCPPRAPT LFHEEA
