DPOD_CANAX
ID DPOD_CANAX Reviewed; 1038 AA.
AC P46588; Q9URM0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DNA polymerase delta catalytic subunit;
DE EC=2.7.7.7;
DE AltName: Full=DNA polymerase III;
GN Name=POL3; ORFNames=Ca35A5.06c;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CA124;
RA Ball T., Rosamond J.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1161;
RA Oliver K., Harris D., Barrell B.G., Rajandream M.A.;
RT "Candida albicans strain 1161 genome pilot sequencing project.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer with subunits of 125 kDa and 50 kDa. The 125 kDa
CC subunit contains the polymerase active site and most likely the active
CC site for the 3'-5' exonuclease activity.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {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; X88804; CAA61282.1; -; Genomic_DNA.
DR EMBL; AL033396; CAA21949.1; -; Genomic_DNA.
DR PIR; JC5757; JC5757.
DR PIR; T18222; T18222.
DR AlphaFoldDB; P46588; -.
DR SMR; P46588; -.
DR CGD; CAL0000185849; POL3.
DR VEuPathDB; FungiDB:C7_02790C_A; -.
DR VEuPathDB; FungiDB:CAWG_05613; -.
DR PhylomeDB; P46588; -.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IEA:EnsemblFungi.
DR GO; GO:0043625; C:delta DNA polymerase complex; IEA:EnsemblFungi.
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; IGI:CGD.
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:1904161; P:DNA synthesis involved in UV-damage excision repair; IEA:EnsemblFungi.
DR GO; GO:1903459; P:mitotic DNA replication lagging strand elongation; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW 4Fe-4S; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Exonuclease; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nuclease;
KW Nucleotidyltransferase; Nucleus; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1038
FT /note="DNA polymerase delta catalytic subunit"
FT /id="PRO_0000046452"
FT ZN_FING 942..961
FT /note="CysA-type"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 992..1010
FT /note="CysB motif"
FT BINDING 942
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 945
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 958
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 961
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 992
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 995
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1005
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1010
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT CONFLICT 172
FT /note="H -> P (in Ref. 1; CAA61282)"
FT /evidence="ECO:0000305"
FT CONFLICT 772
FT /note="R -> Q (in Ref. 1; CAA61282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1038 AA; 118875 MW; CD43A51985AD299F CRC64;
MSHSIPITSS PPPALKKLKL PNGSEEPSEF ERELLDITQA VHDSTDQTWD RPPLPSSFED
ISFQQLDAEE YHDRGNTYAR FFGITQEGHS VLCNVTGFIH YFYCPVPKGF EENLTEFTNY
LKATFDGIER VEITSKESIW GYSNNIKTPF FKIFAKNNIS KIRSAFQNGQ VHNIDPCITY
DNINYLLRLM IDCKITGMSW ITLPRDKYKI VNNKISTCQI ECSIDYRDLI SHPPEGEWLK
MAPLRILSFD IECAGRKGVF PEAEHDPVIQ IANVVQKSGE SKPFVRNVFT VNTCSSIIGS
QIFEHQREED MLMHWKEFIT KVDPDVIIGY NTANFDIPYV LNRAKALGLN DFPFFGRLKR
VKQEIKDAVF SSRAYGTREN KVVNIDGRMQ LDLLQFIQRE YKLRSYTLNS VSAHFLGEQK
EDVQHSIITD LQNGTKETRR RLAVYCLKDA FLPLRLLDKL MCLVNYTEMA RVTGVPFSYL
LSRGQQIKVI SQLFRKCLQE DIVIPNLKSE GSNEEYEGAT VIEPERGYYD VPIATLDFSS
LYPSIMMAHN LCYTTLLNKN SIKAFGLTED DYTKTPNGDY FVHSNLRKGI LPTILDELLT
ARKKAKADLK KETDPFKKDV LNGRQLALKI SANSVYGFTG ATVGKLPCLA ISSSVTAFGR
EMIEKTKNEV QEYYSKKNGH PYDAKVIYGD TDSVMVKFGY QDLETCMKLG EEAANYVSTK
FKNPIKLEFE KVYFPYLLIN KKRYAGLYWT RPEKFDKMDT KGIETVRRDN CRLVQNVITK
VLEFILEERD VPKAQRFVKQ TIADLLQNRI DLSQLVITKA YSKHDYSAKQ AHVELAERMR
KRDPGSAPTL GDRVAYVIIK TGGDKNYEKS EDPLYVLENS LPIDVKYYLD QQLTKPLERI
FIPILGETKT KELLTGSHTR TIKVAAPKTG GLLRFAKKSE VCVSCRTPLK KDNLGALCPN
CIKDGKGPDL YGNALSQMNY LENKFSRLWT ECQRCQGSLH QEVLCSNKDC PIFYMRTKAQ
KDVHQQALEL VKWDNTNW
