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Database: UniProt
Entry: O18475
LinkDB: O18475
Original site: O18475 
ID   DPOLQ_DROME             Reviewed;        2059 AA.
AC   O18475; Q5BI65;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-OCT-2019, entry version 168.
DE   RecName: Full=DNA polymerase theta {ECO:0000250|UniProtKB:O75417};
DE            EC=2.7.7.7 {ECO:0000250|UniProtKB:O75417};
DE   AltName: Full=Mutagen-sensitive protein 308 {ECO:0000303|PubMed:8816490};
GN   Name=mus308 {ECO:0000303|PubMed:8816490,
GN   ECO:0000312|FlyBase:FBgn0002905};
GN   ORFNames=CG6019 {ECO:0000312|FlyBase:FBgn0002905};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=Iso-1;
RX   PubMed=8816490; DOI=10.1128/mcb.16.10.5764;
RA   Harris P.V., Mazina O.M., Leonhardt E.A., Case R.B., Boyd J.B.,
RA   Burtis K.C.;
RT   "Molecular cloning of Drosophila mus308, a gene involved in DNA cross-
RT   link repair with homology to prokaryotic DNA polymerase I genes.";
RL   Mol. Cell. Biol. 16:5764-5771(1996).
RN   [2]
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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION.
RX   PubMed=10343651; DOI=10.1016/s0921-8777(99)00005-1;
RA   Oshige M., Aoyagi N., Harris P.V., Burtis K.C., Sakaguchi K.;
RT   "A new DNA polymerase species from Drosophila melanogaster: a probable
RT   mus308 gene product.";
RL   Mutat. Res. 433:183-192(1999).
RN   [6]
RP   FUNCTION.
RX   PubMed=10732683; DOI=10.1007/s004380050041;
RA   Tosal L., Comendador M.A., Sierra L.M.;
RT   "The mus308 locus of Drosophila melanogaster is implicated in the
RT   bypass of ENU-induced O-alkylpyrimidine adducts.";
RL   Mol. Gen. Genet. 263:144-151(2000).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15961355; DOI=10.1016/j.dnarep.2005.04.020;
RA   Pang M., McConnell M., Fisher P.A.;
RT   "The Drosophila mus 308 gene product, implicated in tolerance of DNA
RT   interstrand crosslinks, is a nuclear protein found in both ovaries and
RT   embryos.";
RL   DNA Repair 4:971-982(2005).
RN   [8]
RP   FUNCTION.
RX   PubMed=20936147; DOI=10.4061/2010/416364;
RA   Diaz-Valdes N., Comendador M.A., Sierra L.M.;
RT   "Mus308 processes oxygen and nitrogen ethylation DNA damage in germ
RT   cells of Drosophila.";
RL   J. Nucleic Acids 2010:H1947-1958(2010).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF GLY-621 AND PRO-781.
RX   PubMed=20617203; DOI=10.1371/journal.pgen.1001005;
RA   Chan S.H., Yu A.M., McVey M.;
RT   "Dual roles for DNA polymerase theta in alternative end-joining repair
RT   of double-strand breaks in Drosophila.";
RL   PLoS Genet. 6:E1001005-E1001005(2010).
CC   -!- FUNCTION: DNA polymerase that promotes microhomology-mediated end-
CC       joining (MMEJ), an alternative non-homologous end-joining (NHEJ)
CC       machinery triggered in response to double-strand breaks in DNA
CC       (PubMed:20617203). MMEJ is an error-prone repair pathway that
CC       produces deletions of sequences from the strand being repaired and
CC       promotes genomic rearrangements, such as telomere fusions.
CC       {ECO:0000269|PubMed:20617203, ECO:0000305|PubMed:10343651,
CC       ECO:0000305|PubMed:10732683, ECO:0000305|PubMed:15961355,
CC       ECO:0000305|PubMed:20936147}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000250|UniProtKB:O75417};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15961355}.
CC   -!- DISRUPTION PHENOTYPE: Hypersensitivity to DNA-cross-linking
CC       agents. {ECO:0000269|PubMed:8816490}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000305}.
DR   EMBL; L76559; AAB67306.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF54858.1; -; Genomic_DNA.
DR   EMBL; BT021359; AAX33507.1; -; mRNA.
DR   EMBL; BT044169; ACH92234.1; -; mRNA.
DR   PIR; T13858; T13858.
DR   RefSeq; NP_524333.1; NM_079609.3.
DR   SMR; O18475; -.
DR   IntAct; O18475; 4.
DR   STRING; 7227.FBpp0082131; -.
DR   PaxDb; O18475; -.
DR   PRIDE; O18475; -.
DR   EnsemblMetazoa; FBtr0082662; FBpp0082131; FBgn0002905.
DR   GeneID; 41571; -.
DR   KEGG; dme:Dmel_CG6019; -.
DR   UCSC; CG6019-RA; d. melanogaster.
DR   CTD; 41571; -.
DR   FlyBase; FBgn0002905; mus308.
DR   eggNOG; KOG0950; Eukaryota.
DR   eggNOG; COG0749; LUCA.
DR   eggNOG; COG1204; LUCA.
DR   GeneTree; ENSGT00940000158694; -.
DR   InParanoid; O18475; -.
DR   KO; K02349; -.
DR   OMA; ALQIQVI; -.
DR   OrthoDB; 179246at2759; -.
DR   PhylomeDB; O18475; -.
DR   Reactome; R-DME-5685939; HDR through MMEJ (alt-NHEJ).
DR   GenomeRNAi; 41571; -.
DR   PRO; PR:O18475; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0002905; Expressed in 32 organ(s), highest expression level in embryo.
DR   Genevisible; O18475; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IMP:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:FlyBase.
DR   GO; GO:0004386; F:helicase activity; ISS:FlyBase.
DR   GO; GO:0071897; P:DNA biosynthetic process; IDA:FlyBase.
DR   GO; GO:0006281; P:DNA repair; TAS:FlyBase.
DR   GO; GO:0000731; P:DNA synthesis involved in DNA repair; IDA:FlyBase.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IBA:GO_Central.
DR   GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IMP:FlyBase.
DR   GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IMP:FlyBase.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10133; PTHR10133; 4.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; DNA damage; DNA repair;
KW   DNA-directed DNA polymerase; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT   CHAIN         1   2059       DNA polymerase theta.
FT                                /FTId=PRO_0000432704.
FT   DOMAIN      243    416       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      464    666       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     256    263       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       357    360       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MUTAGEN     621    621       G->S: In mus308(3294); flies are unable
FT                                to repair interstrand cross-links.
FT                                {ECO:0000269|PubMed:20617203}.
FT   MUTAGEN     781    781       P->L: In mus308(D5); flies are unable to
FT                                repair interstrand cross-links.
FT                                {ECO:0000269|PubMed:20617203}.
FT   CONFLICT   1930   1930       R -> H (in Ref. 4; AAX33507).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2059 AA;  229873 MW;  E93B3CD9A5F75F16 CRC64;
     MAFSQSFNFG NSTLMALEKG MQADDKENAQ PGNGNIQVQS AGNEVNSEIQ EINSEFFRDE
     FSYEVNQAHK PAEQSVVNVS QVQQHMAVVS NQDSEDQSRS SALNDQICTQ SSFEGEDAGA
     DAVLDQPNLD ENSFLCPAQD EEASEQLKED ILHSHSVLAK QEFYQEISQV TQNLSSMSPN
     QLRVSPNSSR IREAMPERPA MPLDLNTLRS ISAWNLPMSI QAEYKKKGVV DMFDWQVECL
     SKPRLLFEHC NLVYSAPTSA GKTLVSEILM LKTVLERGKK VLLILPFISV VREKMFYMQD
     LLTPAGYRVE GFYGGYTPPG GFESLHVAIC TIEKANSIVN KLMEQGKLET IGMVVVDEVH
     LISDKGRGYI LELLLAKILY MSRRNGLQIQ VITMSATLEN VQLLQSWLDA ELYITNYRPV
     ALKEMIKVGT VIYDHRLKLV RDVAKQKVLL KGLENDSDDV ALLCIETLLE GCSVIVFCPS
     KDWCENLAVQ LATAIHVQIK SETVLGQRLR TNLNPRAIAE VKQQLRDIPT GLDGVMSKAI
     TYACAFHHAG LTTEERDIIE ASFKAGALKV LVATSTLSSG VNLPARRVLI RSPLFGGKQM
     SSLTYRQMIG RAGRMGKDTL GESILICNEI NARMGRDLVV SELQPITSCL DMDGSTHLKR
     ALLEVISSGV ANTKEDIDFF VNCTLLSAQK AFHAKEKPPD EESDANYIND ALDFLVEYEF
     VRLQRNEERE TAVYVATRLG AACLASSMPP TDGLILFAEL QKSRRSFVLE SELHAVYLVT
     PYSVCYQLQD IDWLLYVHMW EKLSSPMKKV GELVGVRDAF LYKALRGQTK LDYKQMQIHK
     RFYIALALEE LVNETPINVV VHKYKCHRGM LQSLQQMAST FAGIVTAFCN SLQWSTLALI
     VSQFKDRLFF GIHRDLIDLM RIPDLSQKRA RALFDAGITS LVELAGADPV ELEKVLYNSI
     SFDSAKQHDH ENADEAAKRN VVRNFYITGK AGMTVSEAAK LLIGEARQFV QHEIGLGTIK
     WTQTQAGVEI ASRAIHDGGE VDLHMSLEEE QPPVKRKLSI EENGTANSQK NPRLETVVDT
     QRGYKVDKNI ANQSKMNPNL KEIDAQNKAR RNSTAHMDNL NPISNDPCQN NVNVKTAQPI
     ISNLNDIQKQ GSQIEKMKIN PATVVCSPQL ANEEKPSTSQ SARRKLVNEG MAERRRVALM
     KIQQRTQKEN QSKDQPIQAS RSNQLSSPVN RTPANRWTQS ENPNNEMNNS QLPRRNPRNQ
     SPVPNANRTA SRKVSNAEED LFMADDSFML NTGLAAALTA AESKIASCTE ADVIPSSQPK
     EPEVIGALTP HASRLKRSDQ LRSQRIQSPS PTPQREIEID LESKNESNGV SSMEISDMSM
     ENPLMKNPLH LNASHIMSCS KVDETASSFS SIDIIDVCGH RNAFQAAIIE INNATRLGFS
     VGLQAQAGKQ KPLIGSNLLI NQVAAAENRE AAARERVLFQ VDDTNFISGV SFCLADNVAY
     YWNMQIDERA AYQGVPTPLK VQELCNLMAR KDLTLVMHDG KEQLKMLRKA IPQLKRISAK
     LEDAKVANWL LQPDKTVNFL NMCQTFAPEC TGLANLCGSG RGYSSYGLDT SSAILPRIRT
     AIESCVTLHI LQGQTENLSR IGNGDLLKFF HDIEMPIQLT LCQMELVGFP AQKQRLQQLY
     QRMVAVMKKV ETKIYEQHGS RFNLGSSQAV AKVLGLHRKA KGRVTTSRQV LEKLNSPISH
     LILGYRKLSG LLAKSIQPLM ECCQADRIHG QSITYTATGR ISMTEPNLQN VAKEFSIQVG
     SDVVHISCRS PFMPTDESRC LLSADFCQLE MRILAHMSQD KALLEVMKSS QDLFIAIAAH
     WNKIEESEVT QDLRNSTKQV CYGIVYGMGM RSLAESLNCS EQEARMISDQ FHQAYKGIRD
     YTTRVVNFAR SKGFVETITG RRRYLENINS DVEHLKNQAE RQAVNSTIQG SAADIAKNAI
     LKMEKNIERY REKLALGDNS VDLVMHLHDE LIFEVPTGKA KKIAKVLSLT MENCVKLSVP
     LKVKLRIGRS WGEFKEVSV
//
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