ID   DPOLA_ARATH             Reviewed;        1524 AA.
AC   Q9FHA3; F4K285;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=DNA polymerase alpha catalytic subunit;
DE            EC=2.7.7.7;
GN   Name=POLA; OrderedLocusNames=At5g67100; ORFNames=K21H1.14;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- FUNCTION: Polymerase alpha in a complex with DNA primase is a
CC       replicative polymerase.
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;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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=BAB10944.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB020742; BAB10944.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED98300.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70090.1; -; Genomic_DNA.
DR   RefSeq; NP_001331725.1; NM_001345811.1.
DR   RefSeq; NP_201511.2; NM_126110.3.
DR   AlphaFoldDB; Q9FHA3; -.
DR   SMR; Q9FHA3; -.
DR   BioGRID; 22087; 5.
DR   STRING; 3702.AT5G67100.1; -.
DR   iPTMnet; Q9FHA3; -.
DR   PaxDb; Q9FHA3; -.
DR   PRIDE; Q9FHA3; -.
DR   ProteomicsDB; 222159; -.
DR   EnsemblPlants; AT5G67100.1; AT5G67100.1; AT5G67100.
DR   EnsemblPlants; AT5G67100.2; AT5G67100.2; AT5G67100.
DR   GeneID; 836845; -.
DR   Gramene; AT5G67100.1; AT5G67100.1; AT5G67100.
DR   Gramene; AT5G67100.2; AT5G67100.2; AT5G67100.
DR   KEGG; ath:AT5G67100; -.
DR   Araport; AT5G67100; -.
DR   TAIR; locus:2155593; AT5G67100.
DR   eggNOG; KOG0970; Eukaryota.
DR   HOGENOM; CLU_001718_0_1_1; -.
DR   InParanoid; Q9FHA3; -.
DR   OMA; WLKIEDA; -.
DR   OrthoDB; 293315at2759; -.
DR   PRO; PR:Q9FHA3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FHA3; baseline and differential.
DR   Genevisible; Q9FHA3; AT.
DR   GO; GO:0005658; C:alpha DNA polymerase:primase complex; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003896; F:DNA primase activity; IEA:EnsemblPlants.
DR   GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
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:0006273; P:lagging strand elongation; IBA:GO_Central.
DR   GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR   GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
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; -; 1.
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   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1524
FT                   /note="DNA polymerase alpha catalytic subunit"
FT                   /id="PRO_0000046437"
FT   ZN_FING         1333..1378
FT                   /note="CysA-type"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          68..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1414..1446
FT                   /note="CysB motif"
FT   COMPBIAS        8..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P09884"
FT   BINDING         1336
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P09884"
FT   BINDING         1375
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         1378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P09884"
FT   BINDING         1414
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P09884"
FT   BINDING         1419
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P09884"
FT   BINDING         1440
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P09884"
FT   BINDING         1446
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1524 AA;  170479 MW;  542AF3E02320ED68 CRC64;
     MSGDNSTETG RRRSRGAEAS SRKDTLERLK AIRQGGIRSA SGGGYDIRLQ KPIFDTVDDE
     EYDALVSRRR EEARGFVVED GEGGDLGYLD EGEEEDWSKP SGPESTDESD DGGRFSGRLK
     KKKKGKEQTQ QPQVKKVNPA LKAAATITGE GRLSSMFTSS SFKKVKETDK AQYEGILDEI
     IAQVTPDESD RKKHTRRKLP GTVPVTIFKN KKLFSVASSM GMKESEPTPS TYEGDSVSMD
     NELMKEEDMK ESEVIPSETM ELLGSDIVKE DGSNKIRKTE VKSELGVKEV FTLNATIDMK
     EKDSALSATA GWKEAMGKVG TENGALLGSS SEGKTEFDLD ADGSLRFFIL DAYEEAFGAS
     MGTIYLFGKV KMGDTYKSCC VVVKNIQRCV YAIPNDSIFP SHELIMLEQE VKDSRLSPES
     FRGKLHEMAS KLKNEIAQEL LQLNVSNFSM APVKRNYAFE RPDVPAGEQY VLKINYSFKD
     RPLPEDLKGE SFSALLGSHT SALEHFILKR KIMGPCWLKI SSFSTCSPSE GVSWCKFEVT
     VQSPKDITIL VSEEKVVHPP AVVTAINLKT IVNEKQNISE IVSASVLCFH NAKIDVPMPA
     PERKRSGILS HFTVVRNPEG TGYPIGWKKE VSDRNSKNGC NVLSIENSER ALLNRLFLEL
     NKLDSDILVG HNISGFDLDV LLQRAQACKV QSSMWSKIGR LKRSFMPKLK GNSNYGSGAT
     PGLMSCIAGR LLCDTDLCSR DLLKEVSYSL TDLSKTQLNR DRKEIAPNDI PKMFQSSKTL
     VELIECGETD AWLSMELMFH LSVLPLTLQL TNISGNLWGK TLQGARAQRI EYYLLHTFHS
     KKFILPDKIS QRMKEIKSSK RRMDYAPEDR NVDELDADLT LENDPSKGSK TKKGPAYAGG
     LVLEPKRGLY DKYVLLLDFN SLYPSIIQEY NICFTTIPRS EDGVPRLPSS QTPGILPKLM
     EHLVSIRKSV KLKMKKETGL KYWELDIRQQ ALKLTANSMY GCLGFSNSRF YAKPLAELIT
     LQGRDILQRT VDLVQNHLNL EVIYGDTDSI MIHSGLDDIE EVKAIKSKVI QEVNKKYRCL
     KIDCDGIYKR MLLLRKKKYA AVKLQFKDGK PCEDIERKGV DMVRRDWSLL SKEIGDLCLS
     KILYGGSCED VVEAIHNELM KIKEEMRNGQ VALEKYVITK TLTKPPAAYP DSKSQPHVQV
     ALRMRQRGYK EGFNAKDTVP YIICYEQGNA SSASSAGIAE RARHPDEVKS EGSRWLVDID
     YYLAQQIHPV VSRLCAEIQG TSPERLAECL GLDPSKYRSK SNDATSSDPS TSLLFATSDE
     ERYKSCEPLA LTCPSCSTAF NCPSIISSVC ASISKKPATP ETEESDSTFW LKLHCPKCQQ
     EDSTGIISPA MIANQVKRQI DGFVSMYYKG IMVCEDESCK HTTRSPNFRL LGERERGTVC
     PNYPNCNGTL LRKYTEADLY KQLSYFCHIL DTQCSLEKMD VGVRIQVEKA MTKIRPAVKS
     AAAITRSSRD RCAYGWMQLT DIVI