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DNA polymerase alpha catalytic subunit (EC 2.7.7.7) (Exodeoxyribonuclease) (EC 3.1.11.1)

 DPOLA_DROME             Reviewed;        1488 AA.
P26019; O77034; Q8T992; Q9VD90;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
15-MAR-2004, sequence version 2.
18-JUL-2018, entry version 180.
RecName: Full=DNA polymerase alpha catalytic subunit;
EC=2.7.7.7;
AltName: Full=Exodeoxyribonuclease;
EC=3.1.11.1;
Name=DNApol-alpha180; Synonyms=DNApol-alpha, POLA; ORFNames=CG6349;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 131-136;
181-188 AND 238-251.
STRAIN=Oregon-R;
PubMed=1923767; DOI=10.1093/nar/19.18.4991;
Hirose F., Yamaguchi M., Nishida Y., Masutani M., Miyazawa H.,
Hanaoka F., Matsukage A.;
"Structure and expression during development of Drosophila
melanogaster gene for DNA polymerase alpha.";
Nucleic Acids Res. 19:4991-4998(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
PubMed=1429896;
Melov S., Vaughan H., Cotterill S.;
"Molecular characterisation of the gene for the 180 kDa subunit of the
DNA polymerase-primase of Drosophila melanogaster.";
J. Cell Sci. 102:847-856(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=Oregon-R;
PubMed=9858578; DOI=10.1128/MCB.19.1.547;
Sasaki T., Sawado T., Yamaguchi M., Shinomiya T.;
"Specification of regions of DNA replication initiation during
embryogenesis in the 65-kilobase DNApolalpha-dE2F locus of Drosophila
melanogaster.";
Mol. Cell. Biol. 19:547-555(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1488.
STRAIN=Berkeley; TISSUE=Ovary;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-262; SER-269;
THR-314 AND SER-317, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Polymerase alpha in a complex with DNA primase is a
replicative polymerase. In addition to polymerase activity, this
DNA polymerase exhibits 3' to 5' exonuclease activity.
{ECO:0000269|PubMed:9858578}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
direction to yield nucleoside 5'-phosphates.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000250};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1429896,
ECO:0000269|PubMed:9858578}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Highest level of zygotic expression seen in second-instar larva,
level is reduced at other stages of development.
{ECO:0000269|PubMed:1429896}.
-!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for
the formation of polymerase complexes. {ECO:0000250}.
-!- MISCELLANEOUS: In eukaryotes there are five DNA polymerases:
alpha, beta, gamma, delta, and epsilon which are responsible for
different reactions of DNA synthesis.
-!- SIMILARITY: Belongs to the DNA polymerase type-B family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL48000.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA14340.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAA32745.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; D90310; BAA14340.1; ALT_SEQ; Genomic_DNA.
EMBL; S48157; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AB011813; BAA32745.1; ALT_SEQ; Genomic_DNA.
EMBL; AE014297; AAF55908.2; -; Genomic_DNA.
EMBL; AY070529; AAL48000.1; ALT_INIT; mRNA.
PIR; S28079; S28079.
RefSeq; NP_536736.2; NM_080488.3.
UniGene; Dm.1592; -.
ProteinModelPortal; P26019; -.
SMR; P26019; -.
BioGrid; 67519; 14.
ComplexPortal; CPX-2090; DNA polymerase alpha:primase complex.
DIP; DIP-23937N; -.
IntAct; P26019; 10.
STRING; 7227.FBpp0083514; -.
BindingDB; P26019; -.
ChEMBL; CHEMBL6039; -.
iPTMnet; P26019; -.
PaxDb; P26019; -.
PRIDE; P26019; -.
EnsemblMetazoa; FBtr0084115; FBpp0083514; FBgn0259113.
GeneID; 42553; -.
KEGG; dme:Dmel_CG6349; -.
CTD; 42553; -.
FlyBase; FBgn0259113; DNApol-alpha180.
eggNOG; KOG0970; Eukaryota.
eggNOG; COG0417; LUCA.
GeneTree; ENSGT00550000074891; -.
InParanoid; P26019; -.
KO; K02320; -.
OMA; PKDCIFP; -.
OrthoDB; EOG091G00RR; -.
PhylomeDB; P26019; -.
Reactome; R-DME-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
Reactome; R-DME-174411; Polymerase switching on the C-strand of the telomere.
Reactome; R-DME-174430; Telomere C-strand synthesis initiation.
Reactome; R-DME-68952; DNA replication initiation.
Reactome; R-DME-68962; Activation of the pre-replicative complex.
Reactome; R-DME-69091; Polymerase switching.
Reactome; R-DME-69166; Removal of the Flap Intermediate.
Reactome; R-DME-69183; Processive synthesis on the lagging strand.
ChiTaRS; DNApol-alpha50; fly.
GenomeRNAi; 42553; -.
PRO; PR:P26019; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0259113; -.
Genevisible; P26019; DM.
GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:FlyBase.
GO; GO:0008852; F:exodeoxyribonuclease I activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0001882; F:nucleoside binding; IEA:InterPro.
GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
GO; GO:0006260; P:DNA replication; IDA:FlyBase.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
Gene3D; 1.10.3200.20; -; 1.
Gene3D; 3.30.420.10; -; 1.
Gene3D; 3.90.1600.10; -; 2.
InterPro; IPR006172; DNA-dir_DNA_pol_B.
InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
InterPro; IPR024647; DNA_pol_a_cat_su_N.
InterPro; IPR023211; DNA_pol_palm_dom_sf.
InterPro; IPR038256; Pol_alpha_znc_sf.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
Pfam; PF12254; DNA_pol_alpha_N; 1.
Pfam; PF00136; DNA_pol_B; 1.
Pfam; PF03104; DNA_pol_B_exo1; 1.
Pfam; PF08996; zf-DNA_Pol; 1.
PRINTS; PR00106; DNAPOLB.
SMART; SM00486; POLBc; 1.
SUPFAM; SSF53098; SSF53098; 2.
PROSITE; PS00116; DNA_POLYMERASE_B; 1.
1: Evidence at protein level;
4Fe-4S; Complete proteome; Direct protein sequencing; DNA damage;
DNA repair; DNA replication; DNA-binding; DNA-directed DNA polymerase;
Exonuclease; Hydrolase; Iron; Iron-sulfur; Metal-binding;
Multifunctional enzyme; Nuclease; Nucleotidyltransferase; Nucleus;
Phosphoprotein; Reference proteome; Transferase; Zinc; Zinc-finger.
CHAIN 1 1488 DNA polymerase alpha catalytic subunit.
/FTId=PRO_0000046432.
ZN_FING 1296 1327 CysA-type.
REGION 638 758 Contains conserved residues essential for
3' -> 5' exonuclease activities.
REGION 675 734 DNA-binding region. {ECO:0000255}.
REGION 1255 1380 DNA-binding region. {ECO:0000255}.
MOTIF 96 103 Nuclear localization signal.
{ECO:0000255}.
MOTIF 1362 1388 CysB motif.
METAL 1296 1296 Zinc. {ECO:0000250}.
METAL 1299 1299 Zinc. {ECO:0000250}.
METAL 1324 1324 Zinc. {ECO:0000250}.
METAL 1329 1329 Zinc. {ECO:0000250}.
METAL 1362 1362 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 1367 1367 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 1385 1385 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 1388 1388 Iron-sulfur (4Fe-4S). {ECO:0000250}.
MOD_RES 239 239 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 314 314 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 317 317 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 99 99 S -> L (in Ref. 2; S48157).
{ECO:0000305}.
CONFLICT 117 117 E -> A (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 137 137 K -> KK (in Ref. 2; S48157).
{ECO:0000305}.
CONFLICT 148 148 D -> DD (in Ref. 2; S48157).
{ECO:0000305}.
CONFLICT 200 200 I -> M (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 210 227 AEASSDNEMLERILKPKA -> RRPVAITRCWSAFSPRQ
(in Ref. 2; S48157). {ECO:0000305}.
CONFLICT 364 364 F -> L (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 376 376 M -> I (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 379 379 E -> Q (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 478 478 K -> N (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 739 739 E -> G (in Ref. 2; S48157).
{ECO:0000305}.
CONFLICT 818 819 FH -> ST (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 819 819 H -> Y (in Ref. 6; AAL48000).
{ECO:0000305}.
CONFLICT 842 842 A -> R (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 881 881 F -> L (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 897 898 TT -> NP (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 992 993 EI -> D (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 1155 1157 EYA -> DYR (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 1178 1178 R -> L (in Ref. 2; S48157).
{ECO:0000305}.
CONFLICT 1187 1189 YVI -> LCD (in Ref. 1; BAA14340 and 3;
BAA32745). {ECO:0000305}.
CONFLICT 1197 1205 AAMQRAYHL -> WPCSEHTIS (in Ref. 2;
S48157). {ECO:0000305}.
CONFLICT 1222 1223 YY -> LL (in Ref. 2; S48157).
{ECO:0000305}.
CONFLICT 1292 1310 FRFQCVTCKTEQLMASAYR -> SASSALPVRRSSWRLRTD
(in Ref. 2; S48157). {ECO:0000305}.
CONFLICT 1325 1351 AKSECQTAPIQYLASVRNQLQLSMRQY -> VSPSAKRHRF
STWQACAILQLSM (in Ref. 1; BAA14340).
{ECO:0000305}.
CONFLICT 1392 1392 S -> T (in Ref. 2; S48157).
{ECO:0000305}.
SEQUENCE 1488 AA; 169903 MW; 76C65EE2E2D5B065 CRC64;
MSESPSEPRA KRQRVDKNGR FAAMERLRQL KGTKNKCKVE DQVDDVYDVV DEREYAKRAQ
EKYGDDWIEE DGTGYAEDLR DFFEDEDEYS DGEEDRKDSK KKKGVAPNSK KRPRENEKPV
TGKASIKNLF SNAVPKKMDV KTSVKDDDIL ADILGEIKEE PAATSEKAEK VIAPAKISVT
SRKFDAAAAK EYMNSFLNNI KVQEQERKKA EASSDNEMLE RILKPKAAVP NTKVAFFSSP
TIKKEPMPEK TPAKKATEDP FSDNEMDFSC LDDDENQFDV EKTQQTEKVS QTKTAAEKTS
QSKVAEKSAP KKETTGSPKE SESEDISRLL NNWESICQMD DDFEKSVLTT EQDSTISSDQ
QLRFWYWEAY EDPVKMPGEV FLFGRTADGK SVCLRVQNIN RVLYLLPRQF LLDPISKEPT
KQKVTVADIY KEFDSEVANQ LKLEFFRSRK VTKSFAHHAI GIEVPQSCDY LEVHYDGKKP
LPNLSADKKY NSIAHIFGAT TNALERFLLD RKIKGPCWLQ VTGFKVSPTP MSWCNTEVTL
TEPKNVELVQ DKGKPAPPPP LTLLSLNVRT SMNPKTSRNE ICMISMLTHN RFHIDRPAPQ
PAFNRHMCAL TRPAVVSWPL DLNFEMAKYK STTVHKHDSE RALLSWFLAQ YQKIDADLIV
TFDSMDCQLN VITDQIVALK IPQWSRMGRL RLSQSFGKRL LEHFVGRMVC DVKRSAEECI
RARSYDLQTL CKQVLKLKES ERMEVNADDL LEMYEKGESI TKLISLTMQD NSYLLRLMCE
LNIMPLALQI TNICGNTMTR TLQGGRSERN EFLLLHAFHE KNYIVPDKKP VSKRSGAGDT
DATLSGADAT MQTKKKAAYA GGLVLEPMRG LYEKYVLLMD FNSLYPSIIQ EYNICFTTVQ
QPVDADELPT LPDSKTEPGI LPLQLKRLVE SRKEVKKLMA APDLSPELQM QYHIRQMALK
LTANSMYGCL GFAHSRFFAQ HLAALVTHKG REILTNTQQL VQKMNYDVVY GDTDSLMINT
NITDYDQVYK IGHNIKQSVN KLYKQLELDI DGVFGCLLLL KKKKYAAIKL SKDSKGNLRR
EQEHKGLDIV RRDWSQLAVM VGKAVLDEVL SEKPLEEKLD AVHAQLEKIK TQIAEGVVPL
PLFVITKQLT RTPQEYANSA SLPHVQVALR MNRERNRRYK KGDMVDYVIC LDGTTNAAMQ
RAYHLDELKT SEDKKLQLDT NYYLGHQIHP VVTRMVEVLE GTDASRIAEC LGMDPTKFRQ
NAQRTQRENT EQSEGESLLK TTLQLYRLCE PFRFQCVTCK TEQLMASAYR PGPSNSHIAV
LQQCAKSECQ TAPIQYLASV RNQLQLSMRQ YVQRFYKNWL VCDHPDCNFN TRTHSLRKKS
HRPLCQKCRS GSLLRQYTER DLYNQLCYLR FMFDLGKQTL QQKPTLTPEL EQAYQLLYET
VDQQLQSSSY VIISLSKLFA RSLAQMSLQP SVAQPQIEAI PSALADVV


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