ID   RNH2A_CAEEL             Reviewed;         297 AA.
AC   Q9U6P6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Ribonuclease H2 subunit A;
DE            Short=RNase H2 subunit A;
DE            EC=3.1.26.4;
DE   AltName: Full=RNase H(35);
DE   AltName: Full=Ribonuclease HI large subunit;
DE            Short=RNase HI large subunit;
DE   AltName: Full=Ribonuclease HI subunit A;
GN   Name=rnh-2; Synonyms=rnh2; ORFNames=T13H5.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12411600; DOI=10.1093/oxfordjournals.molbev.a004015;
RA   Arudchandran A.P., Cerritelli S.M., Bowen N.J., Chen X., Krause M.W.,
RA   Crouch R.J.;
RT   "Multiple ribonuclease H-encoding genes in the Caenorhabditis elegans
RT   genome contrasts with the two typical ribonuclease H-encoding genes in the
RT   human genome.";
RL   Mol. Biol. Evol. 19:1910-1919(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Catalytic subunit of RNase HII, an endonuclease that
CC       specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA
CC       replication, possibly by mediating the removal of lagging-strand
CC       Okazaki fragment RNA primers during DNA replication. Mediates the
CC       excision of single ribonucleotides from DNA:RNA duplexes (By
CC       similarity). {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   -!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF181619; AAF01208.1; -; mRNA.
DR   EMBL; Z66524; CAC70103.1; -; Genomic_DNA.
DR   RefSeq; NP_495796.1; NM_063395.3.
DR   AlphaFoldDB; Q9U6P6; -.
DR   SMR; Q9U6P6; -.
DR   BioGRID; 57346; 3.
DR   STRING; 6239.T13H5.7; -.
DR   EPD; Q9U6P6; -.
DR   PaxDb; Q9U6P6; -.
DR   PeptideAtlas; Q9U6P6; -.
DR   EnsemblMetazoa; T13H5.7.1; T13H5.7.1; WBGene00004383.
DR   GeneID; 266861; -.
DR   KEGG; cel:CELE_T13H5.7; -.
DR   UCSC; T13H5.7; c. elegans.
DR   CTD; 266861; -.
DR   WormBase; T13H5.7; CE28960; WBGene00004383; rnh-2.
DR   eggNOG; KOG2299; Eukaryota.
DR   GeneTree; ENSGT00390000010768; -.
DR   HOGENOM; CLU_036532_0_3_1; -.
DR   InParanoid; Q9U6P6; -.
DR   OMA; REECRFF; -.
DR   OrthoDB; 1354466at2759; -.
DR   PhylomeDB; Q9U6P6; -.
DR   PRO; PR:Q9U6P6; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00004383; Expressed in embryo and 4 other tissues.
DR   GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Gene3D; 1.10.10.460; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR004649; RNase_H2_suA.
DR   InterPro; IPR001352; RNase_HII/HIII.
DR   InterPro; IPR024567; RNase_HII/HIII_dom.
DR   InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10954; PTHR10954; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   TIGRFAMs; TIGR00729; TIGR00729; 1.
DR   PROSITE; PS51975; RNASE_H_2; 1.
PE   2: Evidence at transcript level;
KW   Endonuclease; Hydrolase; Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..297
FT                   /note="Ribonuclease H2 subunit A"
FT                   /id="PRO_0000111713"
FT   DOMAIN          21..248
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         27
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         28
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   297 AA;  33191 MW;  233C11EDD4A7B5B2 CRC64;
     MSLKCETERS KTWNNFGNGI PCVLGIDEAG RGPVLGPMVY AAAISPLDQN VELKNLGVDD
     SKALNEAKRE EIFNKMNEDE DIQQIIAYAL RCLSPELISC SMLKRQKYSL NEVSHEAAIT
     LIRDALACNV NVVEIKVDTV GPKATYQAKL EKLFPGISIC VTEKADSLFP IVSAASIAAK
     VTRDSRLRNW QFREKNIKVP DAGYGSGYPG DPNTKKFLQL SVEPVFGFCS LVRSSWKTAS
     TIVEKRCVPG SWEDDEEEGK SQSKRMTSWM VPKNETEVVP KRNVYFKERH MSNILTF