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P28339 (DPOD1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
DNA polymerase delta catalytic subunit

EC=2.7.7.7
Gene names
Name:POLD1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length1106 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex.

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Subunit structure

Heterotetramer composed of subunits of 125 kDa, 50 kDa, 66 kDa and 12 kDa. The 125 kDa subunit contains the polymerase active site and most likely the active site for the 3'-5' exonuclease activity. Interacts with WRNIP1. Interacts with POLD4 and PCNA By similarity. Ref.2

Subcellular location

Nucleus.

Miscellaneous

In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.

Sequence similarities

Belongs to the DNA polymerase type-B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11061106DNA polymerase delta catalytic subunit
PRO_0000046441

Regions

Zinc finger1011 – 102818C4-type Potential
Zinc finger1057 – 107519C4-type Potential
Motif4 – 1916Nuclear localization signal Potential

Amino acid modifications

Modified residue9131Phosphoserine By similarity
Modified residue9161Phosphoserine By similarity
Modified residue10061N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P28339 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: EFC2ED155B290431

FASTA1,106123,709
        10         20         30         40         50         60 
MDGKRRPGPG PGVPPKRARG GLWDEDEAYR PSQFEEELAL MEEMEAERRL QEQEEEELQS 

        70         80         90        100        110        120 
ALEAADGQFS PTAIDARWLR PAPPALDPQM EPLIFQQLEI DHYVAPARPL PGAPPPSQDS 

       130        140        150        160        170        180 
VPILRAFGVT NEGVSVCCHI HGFAPYFYTP APPGFGPEHL SELQRELSAA ISRDQRGGKE 

       190        200        210        220        230        240 
LTGPAVLAVE LCSRESMFGY HGHGPSPFLR ITLALPRLMA PARRLLEQGI RLAGLGTPSF 

       250        260        270        280        290        300 
APYEANVDFE IRFMVDTDIV GCNWLELPAG KYILRPEGKA TLCQLEADVL WSDVISHPPE 

       310        320        330        340        350        360 
GEWQRIAPLR VLSFDIECAG RKGIFPEPER DPVIQICSLG LRWGEPEPFL RLALTLRPCA 

       370        380        390        400        410        420 
PILGAKVQSY EREEDLLQAW STFIRIMDPD VITGYNIQNF DLPYLISRAQ TLKVPGFPLL 

       430        440        450        460        470        480 
GRVIGLRSNI RESSFQSRQT GRRDSKVVSM VGRVQMDMLQ VLLREYKLRS YTLNAVSFHF 

       490        500        510        520        530        540 
LGEQKEDVQH SIITDLQNGN DQTRRRLAVY CLKDAFLPLR LLERLMVLVN AMEMARVTGV 

       550        560        570        580        590        600 
PLGYLLSRGQ QVKVVSQLLR QAMRQGLLMP VVKTEGGEDY TGATVIEPLK GYYDVPIATL 

       610        620        630        640        650        660 
DFSSLYPSIM MAHNLCYTTL LRPGAAQKLG LTEDQFIKTP TGDEFVKASV RKGLLPQILE 

       670        680        690        700        710        720 
NLLSARKRAK AELAKETDPL RRQVLDGRQL ALKVSANSVY GFTGAQVGRL PCLEISQSVT 

       730        740        750        760        770        780 
GFGRQMIEKT KQLVETKYTV ENGYSTSAKV VYGDTDSVMC RFGVSSVAEA MALGREAADW 

       790        800        810        820        830        840 
VSGHFPSPIR LEFEKVYFPY LLISKKRYAG LLFSSRPDAH DRMDCKGLEA VRRDNCPLVA 

       850        860        870        880        890        900 
NLVTASLRRL LIDRDPSGAV AHAQDVISDL LCNRIDISQL VITKELTRAA ADYAGKQAHV 

       910        920        930        940        950        960 
ELAERMRKRD PGSAPSLGDR VPYVIISAAK GVAAYMKSED PLFVLEHSLP IDTQYYLEQQ 

       970        980        990       1000       1010       1020 
LAKPLLRIFE PILGEGRAEA VLLRGDHTRC KTVLTGKVGG LLAFAKRRNC CIGCRTVLSH 

      1030       1040       1050       1060       1070       1080 
QGAVCKFCQP RESELYQKEV SHLSALEERF SRLWTQCQRC QGSLHEDVIC TSRDCPIFYM 

      1090       1100 
RKKVRKDLED QERLLRRFGP PGPEAW 

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References

[1]"Primary structure of the catalytic subunit of calf thymus DNA polymerase delta: sequence similarities with other DNA polymerases."
Zhang J., Chung D.W., Tan C.-K., Downey K.M., Davie E.W., So A.G.
Biochemistry 30:11742-11750(1991) [PubMed: 1721537] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification of a fourth subunit of mammalian DNA polymerase delta."
Liu L., Mo J.-Y., Rodriguez-Belmonte E.M., Lee M.Y.W.T.
J. Biol. Chem. 275:18739-18744(2000) [PubMed: 10751307] [Abstract]
Cited for: PROTEIN SEQUENCE OF 910-930 AND 968-977, SUBUNIT.
Tissue: Thymus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80395 mRNA. Translation: AAA30493.1.
IPIIPI00706072.
PIRA39299.
RefSeqNP_776852.1. NM_174427.2.
UniGeneBt.4749.

3D structure databases

ProteinModelPortalP28339.
ModBaseSearch...

Protein-protein interaction databases

IntActP28339. 4 interactions.
STRINGP28339.

Proteomic databases

PRIDEP28339.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281990.
KEGGbta:281990.

Organism-specific databases

CTD5424.

Phylogenomic databases

eggNOGmaNOG14787.
HOVERGENHBG051395.
PhylomeDBP28339.

Family and domain databases

InterProIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR004578. DNA-dir_DNA_pol_B_pol2.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
Gene3DG3DSA:3.90.1600.10. DNA_pol_palm_dom. 2 hits.
KOK02327.
PfamPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
[Graphical view]
PRINTSPR00106. DNAPOLB.
SMARTSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMSSF53098. RNaseH_fold. 1 hit.
TIGRFAMsTIGR00592. Pol2. 1 hit.
PROSITEPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPOD1_BOVIN
AccessionPrimary (citable) accession number: P28339
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: December 14, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families