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Database: UniProt
Entry: A0A4X2L2F1_VOMUR
LinkDB: A0A4X2L2F1_VOMUR
Original site: A0A4X2L2F1_VOMUR 
ID   A0A4X2L2F1_VOMUR        Unreviewed;       374 AA.
AC   A0A4X2L2F1;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE            EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN   Name=RNASEH2A {ECO:0000313|Ensembl:ENSVURP00010016331.1};
OS   Vombatus ursinus (Common wombat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Vombatidae; Vombatus.
OX   NCBI_TaxID=29139 {ECO:0000313|Ensembl:ENSVURP00010016331.1, ECO:0000313|Proteomes:UP000314987};
RN   [1] {ECO:0000313|Proteomes:UP000314987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Yazar S.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSVURP00010016331.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024981}.
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000256|RuleBase:RU003515}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000077, ECO:0000256|PROSITE-
CC         ProRule:PRU01319, ECO:0000256|RuleBase:RU003515};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01319};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01319};
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:0000256|PROSITE-ProRule:PRU01319};
CC   -!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
CC       {ECO:0000256|ARBA:ARBA00007058}.
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DR   AlphaFoldDB; A0A4X2L2F1; -.
DR   STRING; 29139.ENSVURP00010016331; -.
DR   Ensembl; ENSVURT00010018570.1; ENSVURP00010016331.1; ENSVURG00010012512.1.
DR   GeneTree; ENSGT00390000010768; -.
DR   OMA; RLEWWES; -.
DR   Proteomes; UP000314987; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0032299; C:ribonuclease H2 complex; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006298; P:mismatch repair; IEA:Ensembl.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07181; RNase_HII_eukaryota_like; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 1.10.10.460; Ribonuclease hii. Domain 2; 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   NCBIfam; TIGR00729; ribonuclease HII; 1.
DR   PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR   PANTHER; PTHR10954:SF7; RIBONUCLEASE H2 SUBUNIT A; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS51975; RNASE_H_2; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW   ProRule:PRU01319};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01319};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01319};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE-
KW   ProRule:PRU01319}; Reference proteome {ECO:0000313|Proteomes:UP000314987}.
FT   DOMAIN          28..251
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51975"
FT   REGION          322..343
FT                   /note="Disordered"
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:0000256|PROSITE-ProRule:PRU01319"
FT   BINDING         35
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT   BINDING         142
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
SQ   SEQUENCE   374 AA;  41251 MW;  65A008E5899FB90D CRC64;
     MDLGDFERDN TGSCRLSSPV PELCRTEDCC LGIDEAGRGP VLGPMVYGIC FCPLSKLSNL
     EALKVADSKT LSEAERERLF GKLDQARSFV GWALDILSPN LISTSMQRRA KYNLNSLSHD
     TAMALVQLAL DQGVRVTQVF VDTVGPADKY QQKLQERFPE IEVTVRPKAD SLFPVVSAAS
     ICAKVARDHV VKKWKFLEDL GNLKMDYGSG YPNDPKTKEW LSQCLDPVFG FPQFVRFSWS
     TAQLILDGRA VPVRWWVTLS PLGGGTKELA GNMLTSALLG QVARGHSGPL GIGGGLGRRL
     EWWESLWLVH LPKLWHIPPP CREDSEEEAG GPPAAGRGSG TPSLLSYFAR TQAPTERQSH
     RFFHERGLET VADL
//
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