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 02-SEP-2026, entry version 172. 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; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae; OC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X60507; CAA43026.1; -; Genomic_DNA. DR EMBL; AP008226; BAD71379.1; -; Genomic_DNA. DR RefSeq; WP_011228761.1; NC_006461.1. DR PDB; 1JL2; X-ray; 1.76 A; A/B/C/D=54-129. DR PDB; 1RIL; X-ray; 2.80 A; A=1-166. DR PDB; 2RPI; NMR; -; A=1-127. DR AlphaFoldDB; P29253; -. DR BMRB; P29253; -. DR MDposit; P29253; -. DR SMR; P29253; -. 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 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:0043137; P:DNA replication, removal of RNA primer; IEA:TreeGrafter. DR CDD; cd09278; RNase_HI_prokaryote_like; 1. DR FunFam; 3.30.420.10:FF:000089; Ribonuclease H; 1. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1. DR HAMAP; MF_00042; RNase_H; 1. DR InterPro; IPR050092; RNase_H. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR002156; RNaseH_domain. DR InterPro; IPR036397; RNaseH_sf. DR InterPro; IPR022892; RNaseHI. DR NCBIfam; NF001236; PRK00203.1; 1. 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. DR PDBsum; 1JL2; -. DR PDBsum; 1RIL; -. DR PDBsum; 2RPI; -. 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 131..144 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 //