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RNH2A_DROME
ID   RNH2A_DROME             Reviewed;         347 AA.
AC   Q9VPP5; Q4V3V1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 145.
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   ORFNames=CG13690;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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; AE014134; AAF51500.1; -; Genomic_DNA.
DR   EMBL; BT023255; AAY55671.1; -; mRNA.
DR   RefSeq; NP_608521.1; NM_134677.4.
DR   AlphaFoldDB; Q9VPP5; -.
DR   SMR; Q9VPP5; -.
DR   BioGRID; 59469; 1.
DR   STRING; 7227.FBpp0077750; -.
DR   PaxDb; Q9VPP5; -.
DR   PRIDE; Q9VPP5; -.
DR   EnsemblMetazoa; FBtr0078090; FBpp0077750; FBgn0031252.
DR   GeneID; 33213; -.
DR   KEGG; dme:Dmel_CG13690; -.
DR   UCSC; CG13690-RA; d. melanogaster.
DR   FlyBase; FBgn0031252; CG13690.
DR   VEuPathDB; VectorBase:FBgn0031252; -.
DR   eggNOG; KOG2299; Eukaryota.
DR   GeneTree; ENSGT00390000010768; -.
DR   HOGENOM; CLU_036532_0_3_1; -.
DR   InParanoid; Q9VPP5; -.
DR   OMA; REECRFF; -.
DR   OrthoDB; 1354466at2759; -.
DR   PhylomeDB; Q9VPP5; -.
DR   BioGRID-ORCS; 33213; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 33213; -.
DR   PRO; PR:Q9VPP5; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0031252; Expressed in secondary oocyte and 12 other tissues.
DR   ExpressionAtlas; Q9VPP5; baseline and differential.
DR   Genevisible; Q9VPP5; DM.
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..347
FT                   /note="Ribonuclease H2 subunit A"
FT                   /id="PRO_0000111714"
FT   DOMAIN          70..296
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         76
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   347 AA;  38750 MW;  BF60C8C89D712110 CRC64;
     MSDQEDVVVK KEKKCIENID ENDEEPDDVD FKDSGKISSL KALGPFIAGK ENSRNTVYLS
     DVPDICKDKP CMLGVDEAGR GPVLGPMVYG ISYCPLESNK ALEDLGCADS KQLTEGKRDI
     IFNDINTKEY ATSCVGWAVE IISPNTISTS MYRRSKCSLN EVSMDSAMGL IQQAIDAGVN
     IAEVYVDTVG PPEKYQEKLL KRFPSFKITV AKKADSTYPI VSAASICAKV TRDHALKVWS
     FPEGLVIKDN EFGSGYPGDP VTRRFLTEYI DLVFGFPRLV RFSWSTAENA LADKAYDMEF
     DEPDSEKPKY AGTKLTKFFK GTTKSGEIIR EECRFFKQRH LESVMEF
 
 
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