RNH2_THEMA
ID RNH2_THEMA Reviewed; 238 AA.
AC Q9X017;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ribonuclease HII;
DE Short=RNase HII;
DE EC=3.1.26.4;
GN Name=rnhB; OrderedLocusNames=TM_0915;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in
CC the absence of substrate. May bind a second metal ion after substrate
CC binding. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35996.1; -; Genomic_DNA.
DR PIR; B72320; B72320.
DR RefSeq; NP_228723.1; NC_000853.1.
DR RefSeq; WP_004080647.1; NZ_CP011107.1.
DR PDB; 2ETJ; X-ray; 1.74 A; A=1-238.
DR PDB; 3O3F; X-ray; 2.00 A; A=2-223.
DR PDB; 3O3G; X-ray; 2.10 A; A=2-223.
DR PDB; 3O3H; X-ray; 2.80 A; A=2-223.
DR PDB; 4HHT; X-ray; 3.10 A; A=2-238.
DR PDBsum; 2ETJ; -.
DR PDBsum; 3O3F; -.
DR PDBsum; 3O3G; -.
DR PDBsum; 3O3H; -.
DR PDBsum; 4HHT; -.
DR AlphaFoldDB; Q9X017; -.
DR SMR; Q9X017; -.
DR STRING; 243274.THEMA_00060; -.
DR EnsemblBacteria; AAD35996; AAD35996; TM_0915.
DR KEGG; tma:TM0915; -.
DR eggNOG; COG0164; Bacteria.
DR InParanoid; Q9X017; -.
DR OMA; YPTKLHL; -.
DR OrthoDB; 1685277at2; -.
DR BRENDA; 3.1.26.4; 6331.
DR EvolutionaryTrace; Q9X017; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA 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 GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR CDD; cd07182; RNase_HII_bacteria_HII_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00052_B; RNase_HII_B; 1.
DR InterPro; IPR022898; RNase_HII.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10954; PTHR10954; 1.
DR PANTHER; PTHR10954:SF18; PTHR10954:SF18; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Manganese; Metal-binding;
KW Nuclease; Reference proteome.
FT CHAIN 1..238
FT /note="Ribonuclease HII"
FT /id="PRO_0000111643"
FT DOMAIN 12..197
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 18
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:2ETJ"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:2ETJ"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:2ETJ"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2ETJ"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:2ETJ"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:4HHT"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3O3F"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:2ETJ"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:2ETJ"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:2ETJ"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:2ETJ"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2ETJ"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:2ETJ"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2ETJ"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:2ETJ"
FT HELIX 128..151
FT /evidence="ECO:0007829|PDB:2ETJ"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:2ETJ"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:2ETJ"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:2ETJ"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:2ETJ"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:2ETJ"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:3O3F"
SQ SEQUENCE 238 AA; 26630 MW; 2A0C0156954AE923 CRC64;
MGIDELYKKE FGIVAGVDEA GRGCLAGPVV AAAVVLEKEI EGINDSKQLS PAKRERLLDE
IMEKAAVGIG IASPEEIDLY NIFNATKLAM NRALENLSVK PSFVLVDGKG IELSVPGTCL
VKGDQKSKLI GAASIVAKVF RDRLMSEFHR MYPQFSFHKH KGYATKEHLN EIRKNGVLPI
HRLSFEPVLE LLTDDLLREF FEKGLISENR FERILNLLGA RKSVVFRKER TNHNLPLF
