RNH2A_RAT
ID RNH2A_RAT Reviewed; 301 AA.
AC Q5U209;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ribonuclease H2 subunit A;
DE Short=RNase H2 subunit A;
DE EC=3.1.26.4;
DE AltName: Full=Ribonuclease HI large subunit;
DE Short=RNase HI large subunit;
DE AltName: Full=Ribonuclease HI subunit A;
GN Name=Rnaseh2a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- SUBUNIT: The RNase H2 complex is a heterotrimer composed of the
CC catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and
CC RNASEH2C. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
CC {ECO:0000305}.
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DR EMBL; BC086345; AAH86345.1; -; mRNA.
DR EMBL; BC086539; AAH86539.1; -; mRNA.
DR RefSeq; NP_001013252.1; NM_001013234.1.
DR RefSeq; XP_017456820.1; XM_017601331.1.
DR RefSeq; XP_017456821.1; XM_017601332.1.
DR RefSeq; XP_017456822.1; XM_017601333.1.
DR RefSeq; XP_017456823.1; XM_017601334.1.
DR RefSeq; XP_017456824.1; XM_017601335.1.
DR RefSeq; XP_017456825.1; XM_017601336.1.
DR RefSeq; XP_017456826.1; XM_017601337.1.
DR RefSeq; XP_017456827.1; XM_017601338.1.
DR AlphaFoldDB; Q5U209; -.
DR SMR; Q5U209; -.
DR STRING; 10116.ENSRNOP00000049148; -.
DR PhosphoSitePlus; Q5U209; -.
DR jPOST; Q5U209; -.
DR PaxDb; Q5U209; -.
DR PRIDE; Q5U209; -.
DR Ensembl; ENSRNOT00000046181; ENSRNOP00000049148; ENSRNOG00000068063.
DR GeneID; 364974; -.
DR KEGG; rno:364974; -.
DR CTD; 10535; -.
DR RGD; 1307248; Rnaseh2a.
DR VEuPathDB; HostDB:ENSRNOG00000003504; -.
DR eggNOG; KOG2299; Eukaryota.
DR GeneTree; ENSGT00390000010768; -.
DR HOGENOM; CLU_036532_0_3_1; -.
DR InParanoid; Q5U209; -.
DR OMA; REECRFF; -.
DR OrthoDB; 1354466at2759; -.
DR PhylomeDB; Q5U209; -.
DR PRO; PR:Q5U209; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000003504; Expressed in testis and 20 other tissues.
DR Genevisible; Q5U209; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0032299; C:ribonuclease H2 complex; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; ISO:RGD.
DR GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
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 Acetylation; Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..301
FT /note="Ribonuclease H2 subunit A"
FT /id="PRO_0000111712"
FT DOMAIN 28..251
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O75792"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75792"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CWY8"
SQ SEQUENCE 301 AA; 33286 MW; 57796835026A5201 CRC64;
MDLSELERDN TGRCRLSSPV PAVCLKEPCV LGVDEAGRGP VLGPMVYAIC YCPLSRLADL
EALKVADSKT LTENERERLF AKMEEDGDFV GWALDILSPN LISTSMLGRV KYNLNSMSHD
TAAGLIQHAM DQNVKVTQVF VDTVGMPETY QARLQQRFPG IEVTVKAKAD SLFPVVSAAS
IIAKVARDQA VKNWQFVESL QGLDSDYGSG YPNDPKTKAW LRKHVDPVFG FPQFVRFSWS
TAQAILEKEA ESVTWEDSAA EEDPEGPGRI TSYFSQGPQA CRPQVSHKYF QERGLETATS
L
