ID   DPOLA_TRYBB             Reviewed;        1339 AA.
AC   P27727;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=DNA polymerase alpha catalytic subunit;
DE            EC=2.7.7.7;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S427;
RX   PubMed=1754381; DOI=10.1093/nar/19.23.6441;
RA   Leegwater P.A.J., Strating M.S., Murphy N.B., Kooy R.F.,
RA   van der Vliet P.C., Overdulve J.P.;
RT   "The Trypanosoma brucei DNA polymerase alpha core subunit gene is
RT   developmentally regulated and linked to a constitutively expressed open
RT   reading frame.";
RL   Nucleic Acids Res. 19:6441-6447(1991).
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.
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}.
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DR   EMBL; X60951; CAA43287.1; -; Genomic_DNA.
DR   PIR; S20052; S20052.
DR   AlphaFoldDB; P27727; -.
DR   SMR; P27727; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
DR   CDD; cd05532; POLBc_alpha; 1.
DR   Gene3D; 1.10.132.60; -; 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; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR045846; POLBc_alpha.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 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; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1339
FT                   /note="DNA polymerase alpha catalytic subunit"
FT                   /id="PRO_0000046436"
FT   ZN_FING         1179..1218
FT                   /note="CysA-type"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          60..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1244..1274
FT                   /note="CysB motif"
FT   COMPBIAS        74..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P09884"
FT   BINDING         1182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P09884"
FT   BINDING         1215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P09884"
FT   BINDING         1218
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         1235
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P13382"
FT   BINDING         1244
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         1274
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P09884"
FT   BINDING         1289
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1339 AA;  151613 MW;  9FF159412F2B7FBA CRC64;
     MEDWVSCRSE EQKRCEEKGQ STFDESEEEQ WRRLKEEAMI DSDDSEGAAG DEGAVVLAEA
     KRRKPRKSGK VIATQKCAQP QNQHRHQQKL TKSLSTYDME NLLKQYRNIS AEEEDEVDVD
     ITKFLQDDGV DSEDGEGPSV TATELLSSLI SGRSADTNKT EELADSFPLA NLNDEVFTYE
     NEAAVKKTPR NKEKRTNKSG ANYVIKETVV EELNVVTDLA EVRTGSQHAS TDFLNGCPPK
     ALFYWFDAKE QPHTLTAPGT ILLFGKVCMN EEDEEFRSCC VRIQHVHRNV FLLPKEGSTD
     AEVVQEINAI CRGSGIEERR IKFVERYYAF EEPGVPREKN RWAKLVYPGR YPPFPNKGGL
     THVQVVVGAS RSLLELFLIK KRLMGPSYLE IEHLVTAMDR VSHCKTEFLV PSPKDIKVYN
     SSKPPPPFTV ASIQLHAQLD SDGVKNEVIA ASIALYGDVS IDGERKPNIT ECFTGVRQLS
     PDAPLPLDLE TYCLSKRMPG VHRFINERAL LTWFAETLAA LDPDIIVGHN IIGYTVETLL
     NRYQELNIVR WSTIGRLDVR RFPRIQGNNF NLAIEKEACV GRLVVDTYLL AREYYKSTNY
     KLLSLSTQME IKGITDNRGH FEPGSTVLVK DSMMSSEALC PILLQLLNCA VLSFNVASFL
     DVIPLTKRLT LLAGNLWSRT LYGARSERIE YLLLHAFHNL KFVTPDKKKR DLKRGREDDD
     DEGKRKTKYQ GGMVLEPKSG LYSEYILLLD FNSLYPSLIQ EFNVCYTTID RDENTVSAEV
     PPPESLICLS CRAAGLPSPC LHKCILPKVI RGLVDSRREI KRMMKSEKDP GNLAMLEIRQ
     LALKLTANSM YGCLGFEYSR FYAQPLAELV TRQGRLALQN TVELIPQISP SIRVIYGDTD
     SVMIQTGIKD DIVKVRNLGF EIKGKVNQRY QSLELDIDGV FRAMLLLRKK KYAALSVVDW
     QGEGKVYKRE VKGLDMVRRD WCPLSQHVSD AVLKRILNAE GGEDILDFVI KYMKGVAQDV
     RSGNVYPLEE FVISKSLTKE PESYHGTGYP HAVVALRMKQ RKEGVRVGDL IPYVICEGDE
     HIDDKAYHID EVRRSDGLSV DVEWYLSSQL YPPVMRLCEH IQGFVPEQLS EAMCIASHMR
     TERDVKEEDT ANDFSHCSIF KSRALSECFP TATALQVQCT HCQLVVPVDP HKYINDMFSS
     REKPPPTAPF ELYVCFNCGR SLPLAYLANC MTQMCHTIIR QFYCSGGNVA SVRALRAQFT
     YLRAMFDVPQ ALNCPSAVKN AHRVLSLRCL GTDRKLYTLA DVERFPDVEP VDPLLACAES
     FYRRIDHLFV SLDKLFDTP