DPOLA_DROME
ID DPOLA_DROME Reviewed; 1488 AA.
AC P26019; O77034; Q8T992; Q9VD90;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=DNA polymerase alpha catalytic subunit;
DE EC=2.7.7.7 {ECO:0000269|PubMed:6409898, ECO:0000269|PubMed:6773966, ECO:0000269|PubMed:6806812, ECO:0000269|PubMed:7592543};
DE AltName: Full=3'-5' exodeoxyribonuclease {ECO:0000305};
DE EC=3.1.11.- {ECO:0000269|PubMed:3112771, ECO:0000269|PubMed:3129427};
GN Name=PolA1 {ECO:0000312|FlyBase:FBgn0259113};
GN Synonyms=DNApol-alpha {ECO:0000312|FlyBase:FBgn0259113},
GN DNApol-alpha180 {ECO:0000312|FlyBase:FBgn0259113},
GN POLA {ECO:0000312|FlyBase:FBgn0259113};
GN ORFNames=CG6349 {ECO:0000312|FlyBase:FBgn0259113};
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 131-136; 181-188
RP AND 238-251.
RC STRAIN=Oregon-R;
RX PubMed=1923767; DOI=10.1093/nar/19.18.4991;
RA Hirose F., Yamaguchi M., Nishida Y., Masutani M., Miyazawa H., Hanaoka F.,
RA Matsukage A.;
RT "Structure and expression during development of Drosophila melanogaster
RT gene for DNA polymerase alpha.";
RL Nucleic Acids Res. 19:4991-4998(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=1429896; DOI=10.1242/jcs.102.4.847;
RA Melov S., Vaughan H., Cotterill S.;
RT "Molecular characterisation of the gene for the 180 kDa subunit of the DNA
RT polymerase-primase of Drosophila melanogaster.";
RL J. Cell Sci. 102:847-856(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Oregon-R;
RX PubMed=9858578; DOI=10.1128/mcb.19.1.547;
RA Sasaki T., Sawado T., Yamaguchi M., Shinomiya T.;
RT "Specification of regions of DNA replication initiation during
RT embryogenesis in the 65-kilobase DNApolalpha-dE2F locus of Drosophila
RT melanogaster.";
RL Mol. Cell. Biol. 19:547-555(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1488.
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE DNA POLYMERASE ALPHA
RP COMPLEX, AND TISSUE SPECIFICITY.
RX PubMed=6773966; DOI=10.1016/s0021-9258(19)70587-0;
RA Villani G., Sauer B., Lehman I.R.;
RT "DNA polymerase alpha from Drosophila melanogaster embryos. Subunit
RT structure.";
RL J. Biol. Chem. 255:9479-9483(1980).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=6806812; DOI=10.1073/pnas.79.8.2523;
RA Conaway R.C., Lehman I.R.;
RT "A DNA primase activity associated with DNA polymerase alpha from
RT Drosophila melanogaster embryos.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:2523-2527(1982).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE DNA POLYMERASE ALPHA COMPLEX, AND TISSUE
RP SPECIFICITY.
RX PubMed=6403945; DOI=10.1073/pnas.80.8.2221;
RA Kaguni L.S., Rossignol J.M., Conaway R.C., Lehman I.R.;
RT "Isolation of an intact DNA polymerase-primase from embryos of Drosophila
RT melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:2221-2225(1983).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE DNA POLYMERASE ALPHA
RP COMPLEX, AND TISSUE SPECIFICITY.
RX PubMed=6409898; DOI=10.1016/s0021-9258(17)44626-6;
RA Kaguni L.S., Rossignol J.M., Conaway R.C., Banks G.R., Lehman I.R.;
RT "Association of DNA primase with the beta/gamma subunits of DNA polymerase
RT alpha from Drosophila melanogaster embryos.";
RL J. Biol. Chem. 258:9037-9039(1983).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3112771; DOI=10.1073/pnas.84.16.5635;
RA Cotterill S.M., Reyland M.E., Loeb L.A., Lehman I.R.;
RT "A cryptic proofreading 3'----5' exonuclease associated with the polymerase
RT subunit of the DNA polymerase-primase from Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5635-5639(1987).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=3129427; DOI=10.1016/s0021-9258(18)68672-7;
RA Reyland M.E., Lehman I.R., Loeb L.A.;
RT "Specificity of proofreading by the 3'----5' exonuclease of the DNA
RT polymerase-primase of Drosophila melanogaster.";
RL J. Biol. Chem. 263:6518-6524(1988).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=7592543; DOI=10.1093/oxfordjournals.jbchem.a124780;
RA Kuroda K., Ueda R.;
RT "A 130 kDa polypeptide immunologically related to the 180 kDa catalytic
RT subunit of DNA polymerase alpha-primase complex is detected in early
RT embryos of Drosophila.";
RL J. Biochem. 117:809-818(1995).
RN [14]
RP INTERACTION WITH DPIT47.
RX PubMed=11493638; DOI=10.1242/jcs.114.11.2015;
RA Crevel G., Bates H., Huikeshoven H., Cotterill S.;
RT "The Drosophila Dpit47 protein is a nuclear Hsp90 co-chaperone that
RT interacts with DNA polymerase alpha.";
RL J. Cell Sci. 114:2015-2025(2001).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-262; SER-269;
RP THR-314 AND SER-317, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Catalytic subunit of the DNA polymerase alpha complex (also
CC known as the alpha DNA polymerase-primase complex) which plays an
CC essential role in the initiation of DNA synthesis (PubMed:9858578,
CC PubMed:6773966, PubMed:6806812, PubMed:6403945, PubMed:6409898). During
CC the S phase of the cell cycle, the DNA polymerase alpha complex
CC (composed of a catalytic subunit PolA1, an accessory subunit PolA2 and
CC two primase subunits, the catalytic subunit Prim1 and the regulatory
CC subunit Prim2) is recruited to DNA at the replicative forks
CC (PubMed:9858578, PubMed:6773966, PubMed:6806812, PubMed:6409898). The
CC primase subunit of the polymerase alpha complex initiates DNA synthesis
CC by oligomerising short RNA primers on both leading and lagging strands
CC (By similarity). These primers are initially extended by the polymerase
CC alpha catalytic subunit and subsequently transferred to polymerase
CC delta and polymerase epsilon for processive synthesis on the lagging
CC and leading strand, respectively (By similarity). In addition to
CC polymerase activity, exhibits 3' to 5' exonuclease activity
CC (PubMed:3112771, PubMed:3129427). {ECO:0000250|UniProtKB:P09884,
CC ECO:0000269|PubMed:3112771, ECO:0000269|PubMed:3129427,
CC ECO:0000269|PubMed:6403945, ECO:0000269|PubMed:6409898,
CC ECO:0000269|PubMed:6773966, ECO:0000269|PubMed:6806812,
CC ECO:0000269|PubMed:9858578}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:6409898,
CC ECO:0000269|PubMed:6773966, ECO:0000269|PubMed:6806812,
CC ECO:0000269|PubMed:7592543};
CC -!- ACTIVITY REGULATION: Inhibited by N2-(p-n-butylphenyl) deoxyguanosine
CC 5'-triphosphate and N2-(p-n-butylphenyl) deoxyadenosine 5'-triphosphate
CC (PubMed:3129427). DNA synthesis is not inhibited by fungal toxin alpha-
CC amaitin (PubMed:6806812). The 3'-5' exonuclease activity is inhibited
CC by 10mM dGMP (PubMed:3129427). {ECO:0000269|PubMed:3129427,
CC ECO:0000269|PubMed:6806812}.
CC -!- SUBUNIT: Component of the alpha DNA polymerase complex (also known as
CC the alpha DNA polymerase-primase complex) consisting of four subunits:
CC the catalytic subunit PolA1, the regulatory subunit PolA2, and the
CC primase complex subunits Prim1 and Prim2 respectively (PubMed:6773966,
CC PubMed:6403945, PubMed:6409898, PubMed:7592543). PolA1 associates with
CC the DNA primase complex before association with PolA2 (PubMed:6409898).
CC Interacts with Dpit47; the interaction inhibits the activity of the DNA
CC polymerase and occurs only in proliferating cells but not in quiescent
CC cells (PubMed:11493638). {ECO:0000269|PubMed:11493638,
CC ECO:0000269|PubMed:6403945, ECO:0000269|PubMed:6409898,
CC ECO:0000269|PubMed:6773966, ECO:0000269|PubMed:7592543}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1429896,
CC ECO:0000269|PubMed:6403945, ECO:0000269|PubMed:9858578}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos (at protein level).
CC {ECO:0000269|PubMed:6403945, ECO:0000269|PubMed:6409898,
CC ECO:0000269|PubMed:6773966, ECO:0000269|PubMed:7592543}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Highest
CC level of zygotic expression seen in second-instar larva, level is
CC reduced at other stages of development. {ECO:0000269|PubMed:1429896}.
CC -!- DOMAIN: The CysA-type zinc finger is required for PCNA-binding.
CC {ECO:0000250|UniProtKB:P15436}.
CC -!- PTM: In embryos, a cleaved form of 130 kDa is produced up to cycle 14
CC and then disappears. {ECO:0000269|PubMed:7592543}.
CC -!- MISCELLANEOUS: In eukaryotes there are five DNA polymerases: alpha,
CC beta, gamma, delta, and epsilon which are responsible for different
CC reactions of DNA synthesis.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48000.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA14340.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA32745.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D90310; BAA14340.1; ALT_SEQ; Genomic_DNA.
DR EMBL; S48157; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB011813; BAA32745.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014297; AAF55908.2; -; Genomic_DNA.
DR EMBL; AY070529; AAL48000.1; ALT_INIT; mRNA.
DR PIR; S28079; S28079.
DR RefSeq; NP_536736.2; NM_080488.3.
DR AlphaFoldDB; P26019; -.
DR SMR; P26019; -.
DR BioGRID; 67519; 15.
DR ComplexPortal; CPX-2090; DNA polymerase alpha:primase complex.
DR DIP; DIP-23937N; -.
DR IntAct; P26019; 6.
DR STRING; 7227.FBpp0083514; -.
DR BindingDB; P26019; -.
DR ChEMBL; CHEMBL6039; -.
DR iPTMnet; P26019; -.
DR PaxDb; P26019; -.
DR PRIDE; P26019; -.
DR EnsemblMetazoa; FBtr0084115; FBpp0083514; FBgn0259113.
DR GeneID; 42553; -.
DR KEGG; dme:Dmel_CG6349; -.
DR CTD; 42553; -.
DR FlyBase; FBgn0259113; PolA1.
DR VEuPathDB; VectorBase:FBgn0259113; -.
DR eggNOG; KOG0970; Eukaryota.
DR GeneTree; ENSGT00550000074891; -.
DR HOGENOM; CLU_001718_0_0_1; -.
DR InParanoid; P26019; -.
DR OMA; WLKIEDA; -.
DR OrthoDB; 293315at2759; -.
DR PhylomeDB; P26019; -.
DR Reactome; R-DME-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-DME-68952; DNA replication initiation.
DR Reactome; R-DME-68962; Activation of the pre-replicative complex.
DR Reactome; R-DME-69091; Polymerase switching.
DR Reactome; R-DME-69166; Removal of the Flap Intermediate.
DR Reactome; R-DME-69183; Processive synthesis on the lagging strand.
DR SignaLink; P26019; -.
DR BioGRID-ORCS; 42553; 0 hits in 3 CRISPR screens.
DR ChiTaRS; DNApol-alpha50; fly.
DR GenomeRNAi; 42553; -.
DR PRO; PR:P26019; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0259113; Expressed in ovary and 20 other tissues.
DR Genevisible; P26019; DM.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:FlyBase.
DR GO; GO:0016895; F:exodeoxyribonuclease activity, producing 5'-phosphomonoesters; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017076; F:purine nucleotide binding; IBA:GO_Central.
DR GO; GO:0019103; F:pyrimidine nucleotide binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0045004; P:DNA replication proofreading; IDA:FlyBase.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:FlyBase.
DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 1.10.3200.20; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 2.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR024647; DNA_pol_a_cat_su_N.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR Pfam; PF12254; DNA_pol_alpha_N; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08996; zf-DNA_Pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA damage; DNA repair; DNA replication;
KW DNA-binding; DNA-directed DNA polymerase; Exonuclease; Hydrolase;
KW Metal-binding; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1488
FT /note="DNA polymerase alpha catalytic subunit"
FT /id="PRO_0000046432"
FT ZN_FING 1296..1327
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..758
FT /note="Contains conserved residues essential for 3' -> 5'
FT exonuclease activities"
FT /evidence="ECO:0000303|PubMed:1923767"
FT REGION 675..734
FT /note="DNA-binding"
FT /evidence="ECO:0000255"
FT REGION 1255..1380
FT /note="DNA-binding"
FT /evidence="ECO:0000255"
FT MOTIF 96..103
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1362..1388
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT COMPBIAS 247..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 99
FT /note="S -> L (in Ref. 2; S48157)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="E -> A (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="K -> KK (in Ref. 2; S48157)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="D -> DD (in Ref. 2; S48157)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="I -> M (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..227
FT /note="AEASSDNEMLERILKPKA -> RRPVAITRCWSAFSPRQ (in Ref. 2;
FT S48157)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="F -> L (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="M -> I (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="E -> Q (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="K -> N (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="E -> G (in Ref. 2; S48157)"
FT /evidence="ECO:0000305"
FT CONFLICT 818..819
FT /note="FH -> ST (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="H -> Y (in Ref. 6; AAL48000)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="A -> R (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="F -> L (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 897..898
FT /note="TT -> NP (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 992..993
FT /note="EI -> D (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 1155..1157
FT /note="EYA -> DYR (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 1178
FT /note="R -> L (in Ref. 2; S48157)"
FT /evidence="ECO:0000305"
FT CONFLICT 1187..1189
FT /note="YVI -> LCD (in Ref. 1; BAA14340 and 3; BAA32745)"
FT /evidence="ECO:0000305"
FT CONFLICT 1197..1205
FT /note="AAMQRAYHL -> WPCSEHTIS (in Ref. 2; S48157)"
FT /evidence="ECO:0000305"
FT CONFLICT 1222..1223
FT /note="YY -> LL (in Ref. 2; S48157)"
FT /evidence="ECO:0000305"
FT CONFLICT 1292..1310
FT /note="FRFQCVTCKTEQLMASAYR -> SASSALPVRRSSWRLRTD (in Ref.
FT 2; S48157)"
FT /evidence="ECO:0000305"
FT CONFLICT 1325..1351
FT /note="AKSECQTAPIQYLASVRNQLQLSMRQY -> VSPSAKRHRFSTWQACAILQL
FT SM (in Ref. 1; BAA14340)"
FT /evidence="ECO:0000305"
FT CONFLICT 1392
FT /note="S -> T (in Ref. 2; S48157)"
FT /evidence="ECO:0000305"
SQ 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
