RNH2A_BOVIN
ID RNH2A_BOVIN Reviewed; 299 AA.
AC Q2TBT5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 57-62; 158-165; 224-235; 241-247 AND 292-297, AND
RP FUNCTION.
RX PubMed=9789007; DOI=10.1073/pnas.95.22.12872;
RA Frank P., Braunshofer-Reiter C., Wintersberger U., Grimm R., Buesen W.;
RT "Cloning of the cDNA encoding the large subunit of human RNase HI, a
RT homologue of the prokaryotic RNase HII.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12872-12877(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.
CC {ECO:0000269|PubMed:9789007}.
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; BC109682; AAI09683.1; -; mRNA.
DR RefSeq; NP_001033623.1; NM_001038534.2.
DR AlphaFoldDB; Q2TBT5; -.
DR SMR; Q2TBT5; -.
DR STRING; 9913.ENSBTAP00000012731; -.
DR PaxDb; Q2TBT5; -.
DR PRIDE; Q2TBT5; -.
DR Ensembl; ENSBTAT00000012731; ENSBTAP00000012731; ENSBTAG00000009661.
DR GeneID; 512830; -.
DR KEGG; bta:512830; -.
DR CTD; 10535; -.
DR VEuPathDB; HostDB:ENSBTAG00000009661; -.
DR VGNC; VGNC:34000; RNASEH2A.
DR eggNOG; KOG2299; Eukaryota.
DR GeneTree; ENSGT00390000010768; -.
DR HOGENOM; CLU_036532_0_3_1; -.
DR InParanoid; Q2TBT5; -.
DR OMA; REECRFF; -.
DR OrthoDB; 1354466at2759; -.
DR TreeFam; TF314302; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000009661; Expressed in spermatid and 109 other tissues.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..299
FT /note="Ribonuclease H2 subunit A"
FT /id="PRO_0000247321"
FT DOMAIN 28..251
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT REGION 250..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 205
FT /note="Phosphothreonine"
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 299 AA; 33300 MW; 902422B95D793608 CRC64;
MDLSELERDN TGRCRLSSPV PPVCLKEPCV LGVDEAGRGP VLGPMVYAIC YCPLSRLEDL
EALKVADSKT LSESERDRLF AKMEEDGDFV GWALDVLSPN LISTSMLGRV KYNLNALSHD
TATGLVQFAL DQGVNVAQVF VDTVGLPETY QERLQQRFPG IEVTVKAKAD ALYPVVSAAS
ICAKVARDQA VKNWKFVEKL QDLDTDYGSG YPNDPKTKAW LRKHVDPVFG FPQFVRFSWR
TAQSILESEA EDVKWEDSET GDPKGPGKIK SYFSESPQTC LRLPHRYFQE RGLESATVL
