ID DPOLA_DICDI Reviewed; 1509 AA.
AC Q54SV8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 122.
DE RecName: Full=DNA polymerase alpha catalytic subunit;
DE EC=2.7.7.7;
GN Name=pola1; ORFNames=DDB_G0282191;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Polymerase alpha in a complex with DNA primase is a
CC replicative polymerase. {ECO:0000250}.
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}.
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DR EMBL; AAFI02000046; EAL66301.1; -; Genomic_DNA.
DR RefSeq; XP_640277.1; XM_635185.1.
DR AlphaFoldDB; Q54SV8; -.
DR SMR; Q54SV8; -.
DR STRING; 44689.Q54SV8; -.
DR PaxDb; 44689-DDB0232274; -.
DR EnsemblProtists; EAL66301; EAL66301; DDB_G0282191.
DR GeneID; 8623451; -.
DR KEGG; ddi:DDB_G0282191; -.
DR dictyBase; DDB_G0282191; polA1.
DR eggNOG; KOG0970; Eukaryota.
DR HOGENOM; CLU_001718_0_0_1; -.
DR InParanoid; Q54SV8; -.
DR OMA; MTKMNVG; -.
DR PhylomeDB; Q54SV8; -.
DR Reactome; R-DDI-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-DDI-68952; DNA replication initiation.
DR Reactome; R-DDI-68962; Activation of the pre-replicative complex.
DR Reactome; R-DDI-69091; Polymerase switching.
DR Reactome; R-DDI-69166; Removal of the Flap Intermediate.
DR Reactome; R-DDI-69183; Processive synthesis on the lagging strand.
DR PRO; PR:Q54SV8; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; ISS:dictyBase.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; ISS:dictyBase.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006270; P:DNA replication initiation; ISS:dictyBase.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISS:dictyBase.
DR GO; GO:0006273; P:lagging strand elongation; ISS:dictyBase.
DR GO; GO:0006272; P:leading strand elongation; ISS:dictyBase.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR CDD; cd05776; DNA_polB_alpha_exo; 1.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 1.
DR Gene3D; 1.10.3200.20; DNA Polymerase alpha, zinc finger; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; 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 NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR45861; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45861:SF1; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW Coiled coil; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1509
FT /note="DNA polymerase alpha catalytic subunit"
FT /id="PRO_0000327697"
FT ZN_FING 1328..1358
FT /note="CysA-type"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 27..67
FT /evidence="ECO:0000255"
FT COILED 234..263
FT /evidence="ECO:0000255"
FT COILED 958..989
FT /evidence="ECO:0000255"
FT MOTIF 1389..1411
FT /note="CysB motif"
FT COMPBIAS 1..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..119
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
FT BINDING 1411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13382"
SQ SEQUENCE 1509 AA; 172818 MW; B41EC2A803C5C243 CRC64;
MNRPKREKKS ITDVSTLKSL EQIKRARDGE KRTDQLQEED DERKRLEQLK EQETEFDKEE
RKRKNRDFIE GDSGYRETSD NEDEDEDEDD DGDNSDDDYS LDEDDEDGGG DGENNDSDQE
EAIEVGRKKK RQVKKKSKKD ENGEPKVKTP RVKKTKEKKN EIVPEKNRII QFINNPTESK
STSNNESFFF DKLKKSNSNT LNSTNSTLNS NELSSGGTMS SLDIESMLND LQSAPDSELD
LEKLKEKQLE LEKKLEKEAL LNKPTISTET IITEGVELDD NYEFDFDFNN PITTNNNNNN
NTKTTTTTTT TTITNKNLNK VNSMSLPTRP QAQQFISPKQ TNQEDWWSKT GVDSVVLVKK
LEEIMPKNSD LLKMNMDGSL DFFLLTTEED KQGRIILFGK VKLQASKSNK PGGGGGATKQ
TSITDEPVTK VPLKYASCCI IIEKMERNVF FLPRDYKLDQ DGESTTIQVT DTMIEAELKQ
LVDRSKIKDY KLKKVKRTSA FDYSVPHKNG PVGEQHYVWK LSYPSNQMVF PNDIKGSTFR
CAYGITSSPV ELFLIKRKIM GPTWLTVSGI TLNFDQKKSF ARYEATVKSF KSIKPSMYKN
EPSPPLTVMS ISTKSVMKGS SHEVVMISSV IHESISADGP TENQDSIKYI TAIRPLTGQV
FPPDFQKPGA STTKQNVTIC TSERNLLSFF CETVLNADPD VFAGHNIIGY DIEVILDRLE
KLKVMEWAFI GRLKRSSFDR FNHISGRLIC DSYLVCKEFL PKEKNYSLVE LSKNQLSINK
PEINYLSIEP YFETTKKLNI FIEINENDCY IIFLLIFKLL VFPLTKQLTN LAGNQWDKSL
KSNRAERIEY LLLHNFHEKK YLLPDKIYQK SSSSGGGGGA KDKDNHAAYS GGLVLDPKID
FYDRYVVLLD FNSLYPSIIQ EYNVCFTTIN RVKRDDGKWE EAMPPPSSIE KGILPKVLHG
LVSKRREIKK RMEQEKNKII KAQYDIQQQA VKLIANSMYG CLGFSHSRFY ALPLAELVTR
KGRENLQKGA SIVNKMCYDV IYGDTDSLMI YTGVGTFNEA ETIGKEIQKK INDQYRGSVM
EIGLDGIFKR LLLFKKKKYA CLKEFRIDST TTKCERENKG IDIVRRDYCD LTKDIGQWVL
NLILGGEEKI ALFSLIKEYL ESVQQQIKDN TLAVEKFIIT KTLSKQPEEY NDADIQPHVQ
VALQMRAKGL HVQPGEQVPY IITHGNSSSD IKEEWHHRAR APSDVESIQD VDIDWYLSQQ
ILPSIQRNTG PIGMEPHELA QWLGMTGTKY QKQFDHLQQQ SNQDFKPRYT LSTEDLRYKQ
CKSFNFECPY CGQNNEFTGI VKIDSEGKSE SGFDCNQCHA KIPLKKLANQ LQLNIRTYLK
QYNDWDLRCT ECEKVSKNYK ETSYRCARPQ CRGKMIQIMT SSKLFNQISF FSKLFRNDLS
NSDNTTTIIP NEDQNTLKQA KQIIDSFLSK FDQYNVNLNS LLTPSQTLDS FNNYLASSRA
SIQYPILNK
//
