DPOD_PLAFK
ID DPOD_PLAFK Reviewed; 1094 AA.
AC P30315;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=DNA polymerase delta catalytic subunit {ECO:0000303|PubMed:1762904};
DE Short=PfPoldelta {ECO:0000303|PubMed:26911594};
DE EC=2.7.7.7 {ECO:0000269|PubMed:26911594};
DE AltName: Full=3'-5' exodeoxyribonuclease {ECO:0000305};
DE EC=3.1.11.- {ECO:0000269|PubMed:26911594};
GN Name=POLD;
OS Plasmodium falciparum (isolate K1 / Thailand).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1762904; DOI=10.1093/nar/19.24.6731;
RA Ridley R.G., White J.H., McAleese S.M., Goman M., Alano P., Devries E.,
RA Kilbey B.J.;
RT "DNA polymerase delta: gene sequences from Plasmodium falciparum indicate
RT that this enzyme is more highly conserved than DNA polymerase alpha.";
RL Nucleic Acids Res. 19:6731-6736(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1775172; DOI=10.1016/0166-6851(91)90072-e;
RA Fox B.A., Bzik D.J.;
RT "The primary structure of Plasmodium falciparum DNA polymerase delta is
RT similar to drug sensitive delta-like viral DNA polymerases.";
RL Mol. Biochem. Parasitol. 49:289-296(1991).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=8855554; DOI=10.1016/0166-6851(96)02657-6;
RA Horrocks P., Jackson M., Cheesman S., White J.H., Kilbey B.J.;
RT "Stage specific expression of proliferating cell nuclear antigen and DNA
RT polymerase delta from Plasmodium falciparum.";
RL Mol. Biochem. Parasitol. 79:177-182(1996).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=26911594; DOI=10.1186/s12936-016-1166-0;
RA Vasuvat J., Montree A., Moonsom S., Leartsakulpanich U., Petmitr S.,
RA Focher F., Wright G.E., Chavalitshewinkoon-Petmitr P.;
RT "Biochemical and functional characterization of Plasmodium falciparum DNA
RT polymerase delta.";
RL Malar. J. 15:116-116(2016).
CC -!- FUNCTION: This polymerase possesses two enzymatic activities: DNA
CC synthesis (polymerase) and an exonucleolytic activity that degrades
CC single-stranded DNA in the 3'- to 5'-direction.
CC {ECO:0000269|PubMed:26911594}.
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 Evidence={ECO:0000269|PubMed:26911594};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P15436};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P15436};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:26911594};
CC Note=May also use Mn(2+). {ECO:0000269|PubMed:26911594};
CC -!- ACTIVITY REGULATION: The small regulatory subunit delta and PCNA1
CC increase POLD catalytic activity. {ECO:0000269|PubMed:26911594}.
CC -!- SUBUNIT: Heterodimer composed of a catalytic subunit POLD and a small
CC regulatory subunit. {ECO:0000305|PubMed:26911594}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P15436}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual blood stage
CC specifically in trophozoites and schizonts (at protein level).
CC {ECO:0000269|PubMed:8855554}.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {ECO:0000250|UniProtKB:P15436}.
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; M64715; AAA29589.1; -; Genomic_DNA.
DR EMBL; X62423; CAA44289.1; -; Genomic_DNA.
DR EMBL; M63941; AAA29588.1; -; Genomic_DNA.
DR PIR; S22573; S22573.
DR AlphaFoldDB; P30315; -.
DR SMR; P30315; -.
DR GO; GO:0043625; C:delta DNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0004527; F:exonuclease 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF14260; zf-C4pol; 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 4Fe-4S; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Exonuclease; Hydrolase; Iron; Iron-sulfur; Magnesium; Metal-binding;
KW Nuclease; Nucleotidyltransferase; Nucleus; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1094
FT /note="DNA polymerase delta catalytic subunit"
FT /id="PRO_0000046448"
FT ZN_FING 1003..1019
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOTIF 1049..1067
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1003
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1006
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1016
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1019
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1049
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1052
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1062
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1067
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
SQ SEQUENCE 1094 AA; 126884 MW; 27DE7E1D652EDACE CRC64;
MEELKTCPFT NVIPYGLLYD KLKKEKNNDV PENYVIEEFD KLLKNYERPN VYDEIGNATF
KNDEDLITFQ IDLDYTVENI FKNMIYNESG SNNSILNDIY MPYRILLSKD KNYVSVPIIR
IYSLRKDGCS VLINVHNFFP YFYVEKPDDF DNEDLIKLEM LMNENLNLNS QYKIYEKKIL
KIEIVKTESL MYFKKNGKKD FLKITVLLPK MVPSLKKYFE GIVHVNNKSI GGIVYEANLP
FILRYIIDHK ITGSSWINCK KGHYYIRNKN KKISNCTFEI DISYEHVEPI TLENEYQQIP
KLRILSFDIE CIKLDGKGFP EAKNDPIIQI SSILYFQGEP IDNCTKFIFT LLECASIPGS
NVIWFNDEKT LLEAWNEFII RIDPDFLTGY NIINFDLPYI LNRGTALNLK KLKFLGRIKN
VASTVKDSSF SSKQFGTHET KEINIFGRIQ FDVYDLIKRD YKLKSYTLNY VSFEFLKEQK
EDVHYSIMND LQNESPESRK RIATYCIKDG VLPLRLIDKL LFIYNYVEMA RVTGTPFVYL
LTRGQQIKVT SQLYRKCKEL NYVIPSTYMK VNTNEKYEGA TVLEPIKGYY IEPISTLDFA
SLYPSIMIAH NLCYSTLIKS NHEVSDLQND DITTIQGKNN LKFVKKNVKK GILPLIVEEL
IEARKKVKLL IKNEKNNITK MVLNGRQLAL KISANSVYGY TGASSGGQLP CLEVAVSITT
LGRSMIEKTK ERVESFYCKS NGYEHNSTVI YGDTDSVMVK FGTNNIEEAM TLGKDAAERI
SKEFLSPIKL EFEKVYCPYL LLNKKRYAGL LYTNPNKHDK MDCKGIETVR RDFCILIQQM
METVLNKLLI EKNLNSAIEY TKSKIKELLT NNIDMSLLVV TKSLGKTDYE TRLPHVELAK
KLKQRDSATA PNVGDRVSYI IVKGVKGQAQ YERAEDPLYV LDNNLAIDYN HYLDAIKSPL
SRIFEVIMQN SDSLFSGDHT RHKTILTSSQ TALSKFLKKS VRCIGCNSSI KKPPLCNHCK
ENKEFSIYMQ KIKDFKNKQN EFFQLWTECQ RCQGNLHVDV ICMNRDCPIF YRRAKIKKDI
ANLQEQVTSL RMDW
