ID   RNH2A_DICDI             Reviewed;         289 AA.
AC   Q54D13;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Ribonuclease H2 subunit A;
DE            Short=RNase H2 subunit A;
DE            EC=3.1.26.4;
GN   Name=rnaseh2A; ORFNames=DDB_G0292584;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. Participates in DNA replication (By similarity).
CC       {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; AAFI02000194; EAL61095.1; -; Genomic_DNA.
DR   RefSeq; XP_629507.1; XM_629505.1.
DR   AlphaFoldDB; Q54D13; -.
DR   SMR; Q54D13; -.
DR   STRING; 44689.DDB0266383; -.
DR   PaxDb; Q54D13; -.
DR   EnsemblProtists; EAL61095; EAL61095; DDB_G0292584.
DR   GeneID; 8628758; -.
DR   KEGG; ddi:DDB_G0292584; -.
DR   dictyBase; DDB_G0292584; rnaseh2A.
DR   eggNOG; KOG2299; Eukaryota.
DR   HOGENOM; CLU_036532_0_4_1; -.
DR   InParanoid; Q54D13; -.
DR   OMA; REECRFF; -.
DR   PhylomeDB; Q54D13; -.
DR   PRO; PR:Q54D13; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0032299; C:ribonuclease H2 complex; ISS:dictyBase.
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:dictyBase.
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:0016070; P:RNA metabolic process; IC:dictyBase.
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   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..289
FT                   /note="Ribonuclease H2 subunit A"
FT                   /id="PRO_0000327562"
FT   DOMAIN          20..249
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         26
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         27
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  33083 MW;  ED769C6E595BBD7C CRC64;
     MDNKIIYLTE LDSSVDKSEP FVMGIDEAGR GPVMGPMVYG CCYAPISKST TLKSMKFNDS
     KKLTEQQRDQ LFDKMGESNK ILAYETDVIT AEILSEKMLY KKPISLNVIS HESAIGLIRS
     VLKKGVNVQE LYLDTVGPPD KYQLMLKKLF PEIGKIIVSK KADSLYPIVS AASIAAKVVR
     DFEITNKNFD YLNIYDQDEQ LSTDFGSGYP SDPLSKKWLV KNRDKVFGYP NFIRFSWKTT
     ETAMRGACFG VDWVLENDKL KQHFQENQND KKRFMFFKEN NIENCINDF