RNH3_AQUAE
ID RNH3_AQUAE Reviewed; 257 AA.
AC O67644;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Ribonuclease HIII;
DE Short=RNase HIII;
DE EC=3.1.26.4;
GN Name=rnhC; OrderedLocusNames=aq_1768;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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. RnhC subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC07614.1; -; Genomic_DNA.
DR PIR; B70452; B70452.
DR RefSeq; NP_214210.1; NC_000918.1.
DR RefSeq; WP_010881147.1; NC_000918.1.
DR PDB; 3VN5; X-ray; 1.98 A; A=1-257.
DR PDBsum; 3VN5; -.
DR AlphaFoldDB; O67644; -.
DR SMR; O67644; -.
DR STRING; 224324.aq_1768; -.
DR EnsemblBacteria; AAC07614; AAC07614; aq_1768.
DR KEGG; aae:aq_1768; -.
DR PATRIC; fig|224324.8.peg.1363; -.
DR eggNOG; COG1039; Bacteria.
DR HOGENOM; CLU_059546_3_0_0; -.
DR InParanoid; O67644; -.
DR OMA; EITETCH; -.
DR OrthoDB; 1685277at2; -.
DR BRENDA; 3.1.26.4; 396.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium 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; cd14796; RNAse_HIII_N; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00053; RNase_HIII; 1.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR004641; RNase_HIII.
DR InterPro; IPR024568; RNase_HIII_N.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR10954; PTHR10954; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR PIRSF; PIRSF037748; RnhC; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00716; rnhC; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Reference proteome.
FT CHAIN 1..257
FT /note="Ribonuclease HIII"
FT /id="PRO_0000111674"
FT DOMAIN 71..257
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 77
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 8..20
FT /evidence="ECO:0007829|PDB:3VN5"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3VN5"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3VN5"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3VN5"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:3VN5"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3VN5"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:3VN5"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3VN5"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 152..171
FT /evidence="ECO:0007829|PDB:3VN5"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3VN5"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3VN5"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 201..225
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:3VN5"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:3VN5"
SQ SEQUENCE 257 AA; 29539 MW; 184FC7B5431F9607 CRC64;
MPSLKISPSE AEKIQNYLVS SGFRKINAPY TLWALEGNGV KVYYYKTGSL LIQGKNSEKV
LKEVLNLLEK KKLPGCDESG KGDIFGSLVL CCVCIPEENY LKVSSLNPRD TKRLSDKRVE
RLYLALKPLV KAYCYEIKPE EYNKLYRKFR NLNKMMTHFY KLLIERVKEE CGVSEVVVDK
YQPSNPFGED VIFETEAERN LAVAVASIFA RYKFLQSLKE VERELGIKIP KGTSKEVKEL
AKSLKNPERF IKLNFNV
