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Protein

DNA-directed DNA polymerase

Gene

5

Organism
Enterobacteria phage T7 (Bacteriophage T7)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Replicates viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'-5' direction (By similarity). Non-processive DNA polymerase that achieves processivity by binding to host thioredoxin (TrxA). This interaction increases the rate of dNTP incorporation to yield a processivity of approximately 800 nucleotides (nt) per binding event. Interacts with DNA helicase gp4 to coordinate nucleotide polymerization with unwinding of the DNA. The leading strand is synthesized continuously while synthesis of the lagging strand requires the synthesis of oligoribonucleotides by the primase domain of gp4.UniRule annotation4 Publications

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi5Magnesium 1; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication1
Metal bindingi5Magnesium 2; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication1
Metal bindingi7Magnesium 2; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication1
Metal bindingi174Magnesium 2; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication1
Metal bindingi475Magnesium 3; catalytic; for polymerase activityUniRule annotation1 Publication1 Publication1
Metal bindingi475Magnesium 4; catalytic; for polymerase activityUniRule annotation1 Publication1 Publication1
Metal bindingi476Magnesium 4; catalytic; via carbonyl oxygen; for polymerase activityUniRule annotation1 Publication1 Publication1
Binding sitei506SubstrateUniRule annotation1 Publication1
Binding sitei518SubstrateUniRule annotation1 Publication1
Binding sitei522SubstrateUniRule annotation1 Publication1
Binding sitei526SubstrateUniRule annotation1 Publication1
Metal bindingi654Magnesium 3; catalytic; for polymerase activityUniRule annotation1 Publication1 Publication1
Metal bindingi654Magnesium 4; catalytic; for polymerase activityUniRule annotation1 Publication1 Publication1

GO - Molecular functioni

  • 3'-5' exonuclease activity Source: UniProtKB
  • DNA binding Source: UniProtKB-KW
  • DNA-directed DNA polymerase activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, DNA-directed DNA polymerase, Exonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Transferase
Biological processDNA replication, Host-virus interaction, Viral DNA replication
LigandMagnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed DNA polymeraseUniRule annotation (EC:2.7.7.7UniRule annotation1 Publication, EC:3.1.11.-UniRule annotation2 Publications)
Alternative name(s):
Gene product 5
Short name:
Gp5
Gene namesi
Ordered Locus Names:5
OrganismiEnterobacteria phage T7 (Bacteriophage T7)
Taxonomic identifieri10760 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7virus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000000840 Componenti: Genome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi123H → S: 83% loss of exonuclease activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001012691 – 704DNA-directed DNA polymeraseAdd BLAST704

Interactioni

Subunit structurei

Composed of two subunits. One is encoded by the phage and the other is encoded by the host thioredoxin. Interacts with helicase/primase gp4; this interaction is essential for the coordination of DNA unwinding and nucleotide polymerization on duplex DNA. Interacts with the ssDNA-binding protein gp2.5.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
trxAP0AA252EBI-8664634,EBI-368542From Escherichia coli (strain K12).

Protein-protein interaction databases

DIPiDIP-41665N
IntActiP00581, 4 interactors
MINTiP00581

Structurei

Secondary structure

1704
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP00581
SMRiP00581
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00581

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 1873'-5'exonucleaseUniRule annotation1 PublicationAdd BLAST187
Regioni202 – 704PolymeraseUniRule annotation1 PublicationAdd BLAST503
Regioni262 – 338Binding to host TrxA1 Publication1 PublicationAdd BLAST77

Sequence similaritiesi

Belongs to the DNA polymerase type-A family.UniRule annotation

Phylogenomic databases

KOiK21238
OrthoDBiVOG0900003U

Family and domain databases

Gene3Di3.30.420.10, 1 hit
HAMAPiMF_04101 DPOL_T7, 1 hit
InterProiView protein in InterPro
IPR019760 DNA-dir_DNA_pol_A_CS
IPR001098 DNA-dir_DNA_pol_A_palm_dom
IPR002298 DNA_polymerase_A
IPR034699 DPOL_T7
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
PANTHERiPTHR10133 PTHR10133, 1 hit
PfamiView protein in Pfam
PF00476 DNA_pol_A, 1 hit
PRINTSiPR00868 DNAPOLI
SMARTiView protein in SMART
SM00482 POLAc, 1 hit
SUPFAMiSSF53098 SSF53098, 1 hit
PROSITEiView protein in PROSITE
PS00447 DNA_POLYMERASE_A, 1 hit

Sequencei

Sequence statusi: Complete.

P00581-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIVSDIEANA LLESVTKFHC GVIYDYSTAE YVSYRPSDFG AYLDALEAEV
60 70 80 90 100
ARGGLIVFHN GHKYDVPALT KLAKLQLNRE FHLPRENCID TLVLSRLIHS
110 120 130 140 150
NLKDTDMGLL RSGKLPGKRF GSHALEAWGY RLGEMKGEYK DDFKRMLEEQ
160 170 180 190 200
GEEYVDGMEW WNFNEEMMDY NVQDVVVTKA LLEKLLSDKH YFPPEIDFTD
210 220 230 240 250
VGYTTFWSES LEAVDIEHRA AWLLAKQERN GFPFDTKAIE ELYVELAARR
260 270 280 290 300
SELLRKLTET FGSWYQPKGG TEMFCHPRTG KPLPKYPRIK TPKVGGIFKK
310 320 330 340 350
PKNKAQREGR EPCELDTREY VAGAPYTPVE HVVFNPSSRD HIQKKLQEAG
360 370 380 390 400
WVPTKYTDKG APVVDDEVLE GVRVDDPEKQ AAIDLIKEYL MIQKRIGQSA
410 420 430 440 450
EGDKAWLRYV AEDGKIHGSV NPNGAVTGRA THAFPNLAQI PGVRSPYGEQ
460 470 480 490 500
CRAAFGAEHH LDGITGKPWV QAGIDASGLE LRCLAHFMAR FDNGEYAHEI
510 520 530 540 550
LNGDIHTKNQ IAAELPTRDN AKTFIYGFLY GAGDEKIGQI VGAGKERGKE
560 570 580 590 600
LKKKFLENTP AIAALRESIQ QTLVESSQWV AGEQQVKWKR RWIKGLDGRK
610 620 630 640 650
VHVRSPHAAL NTLLQSAGAL ICKLWIIKTE EMLVEKGLKH GWDGDFAYMA
660 670 680 690 700
WVHDEIQVGC RTEEIAQVVI ETAQEAMRWV GDHWNFRCLL DTEGKMGPNW

AICH
Length:704
Mass (Da):79,692
Last modified:July 21, 1986 - v1
Checksum:i17089CE2AD9FB596
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01146 Genomic DNA Translation: CAA24412.1
PIRiA00716 DJBPT7
RefSeqiNP_041982.1, NC_001604.1

Genome annotation databases

GeneIDi1261044
KEGGivg:1261044

Similar proteinsi

Entry informationi

Entry nameiDPOL_BPT7
AccessioniPrimary (citable) accession number: P00581
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 12, 2018
This is version 127 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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