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BPT7:DPOL

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Species (Taxon ID) Enterobacteria phage T7 (Bacteriophage T7). (10760)
Gene Name(s) No Information Provided.
Protein Name(s) DNA-directed DNA polymerase

DNA polymerase gp5 Gene product 5 Gp5 T7 DNA polymerase

External Links
UniProt P00581
EMBL V01146
PIR A00716
RefSeq NP_041982.1
PDB 1SKR
1SKS
1SKW
1SL0
1SL1
1SL2
1T7P
1T8E
1TK0
1TK5
1TK8
1TKD
1X9M
1X9S
1X9W
1ZYQ
2AJQ
PDBsum 1SKR
1SKS
1SKW
1SL0
1SL1
1SL2
1T7P
1T8E
1TK0
1TK5
1TK8
1TKD
1X9M
1X9S
1X9W
1ZYQ
2AJQ
ProteinModelPortal P00581
SMR P00581
DIP DIP-41665N
IntAct P00581
MINT MINT-1513442
GeneID 1261044
EvolutionaryTrace P00581
Proteomes UP000000840
GO GO:0003677
GO:0003887
GO:0004527
GO:0006261
GO:0016032
Gene3D 3.30.420.10
InterPro IPR019760
IPR001098
IPR002298
IPR012337
Pfam PF00476
PRINTS PR00868
SMART SM00482
SUPFAM SSF53098
PROSITE PS00447

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0003887

DNA-directed DNA polymerase activity

PMID:23012374[1]

ECO:0000314

F

Fig 3

complete
CACAO 11449

GO:0004527

exonuclease activity

2703498:2703498

ECO:0000315

F

The experiment shows that mutation at His residue within the gene cause inactive exonuclease.

complete
CACAO 11487

GO:0090592

DNA synthesis involved in DNA replication

PMID:21606333[2]

ECO:0000315

P

Figure 2 compared the activities of both gp5/trx and its mutated form Gp5-Fbpneu/trx in the presence of gp4 by looking at how much nucleotide (dTMP) had been incorporated in a sample of dsDNA . According to the paper and from the results, Gp5-Fbpneu/trx did not mediate the synthesis in the presence of gp4 over a large range of concentrations of gp5/trx and gp4. This means that a mutated gp5 would result in disrupted DNA synthesis in the presence of gp4 as compared to a normal version of gp5, showing its critical function for DNA replication.

complete
CACAO 13104

GO:0004529

exodeoxyribonuclease activity

PMID:1846298[3]

ECO:0000315

F

Table 3 (specifically k_exo) compares the rates of exonuclease activity between the wild-type enzyme (105 1/s) and mutant enzyme (6.9e-4 1/s), revealing that the wild-type exonuclease rates are dramatically higher than that of the mutant enzyme's exonuclease rates. This shows that this domain of DNA polymerase has exonuclease activity.

complete
CACAO 11980

enables

GO:0008408

3'-5' exonuclease activity

PMID:2703498[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0071897

DNA biosynthetic process

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0003887

P

Seeded From UniProt

complete

involved_in

GO:0071897

DNA biosynthetic process

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0003887

P

Seeded From UniProt

complete

involved_in

GO:0071897

DNA biosynthetic process

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0003887

P

Seeded From UniProt

complete

involved_in

GO:0071897

DNA biosynthetic process

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0003887

P

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0008408

P

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0008408

P

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0008408

P

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004527

P

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004518

P

Seeded From UniProt

complete

enables

GO:0003676

nucleic acid binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR036397

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001098

F

Seeded From UniProt

complete

enables

GO:0003887

DNA-directed DNA polymerase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001098
InterPro:IPR002298
InterPro:IPR019760

F

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001098
InterPro:IPR019760

P

Seeded From UniProt

complete

involved_in

GO:0006261

DNA-dependent DNA replication

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002298
InterPro:IPR034699

P

Seeded From UniProt

complete

enables

GO:0008408

3'-5' exonuclease activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR034699

F

Seeded From UniProt

complete

enables

GO:0003887

DNA-directed DNA polymerase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.7.7

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000351416

F

Seeded From UniProt

complete

enables

GO:0008408

3'-5' exonuclease activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000351416

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000351416

F

Seeded From UniProt

complete

enables

GO:0003887

DNA-directed DNA polymerase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000351416

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511

P

Seeded From UniProt

complete

enables

GO:0004527

exonuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0269

F

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0235

P

Seeded From UniProt

complete

involved_in

GO:0016032

viral process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0945

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511

F

Seeded From UniProt

complete

enables

GO:0004518

nuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0540

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0039693

viral DNA genome replication

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1194

P

Seeded From UniProt

complete

enables

GO:0003887

DNA-directed DNA polymerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0239

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

enables

GO:0016779

nucleotidyltransferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0548

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Tran, NQ et al. (2012) Thioredoxin, the processivity factor, sequesters an exposed cysteine in the thumb domain of bacteriophage T7 DNA polymerase. J. Biol. Chem. 287 39732-41 PubMed GONUTS page
  2. Zhang, H et al. (2011) Helicase-DNA polymerase interaction is critical to initiate leading-strand DNA synthesis. Proc. Natl. Acad. Sci. U.S.A. 108 9372-7 PubMed GONUTS page
  3. Patel, SS et al. (1991) Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant. Biochemistry 30 511-25 PubMed GONUTS page
  4. Tabor, S & Richardson, CC (1989) Selective inactivation of the exonuclease activity of bacteriophage T7 DNA polymerase by in vitro mutagenesis. J. Biol. Chem. 264 6447-58 PubMed GONUTS page