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Links from Protein

Items: 16

1.

DNA polymerase I, ribonuclease H-like domain

This domain is responsible for the 3'-5' exonuclease proofreading activity of E. coli DNA polymerase I (polI) and other related enzymes. It is one of the constituent domains of Klenow fragment. Paper describing PDB structure 1d8y. [1]. 10588690. Structural origins of the exonuclease resistance of a zwitterionic RNA. Teplova M, Wallace ST, Tereshko V, Minasov G, Symons AM, Cook PD, Manoharan M, Egli M;. Proc Natl Acad Sci U S A. 1999;96:14240-14245. Paper describing PDB structure 1dpi. [2]. 3883192. Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Ollis DL, Brick P, Hamlin R, Xuong NG, Steitz TA;. Nature 1985;313:762-766. Paper describing PDB structure 1kln. [3]. 8469987. Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Beese LS, Derbyshire V, Steitz TA;. Science. 1993;260:352-355. Paper describing PDB structure 1l3s. [4]. 12649320. Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Johnson SJ, Taylor JS, Beese LS;. Proc Natl Acad Sci U S A. 2003;100:3895-3900. Paper describing PDB structure 1u45. [5]. 15322558. Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase. Hsu GW, Ober M, Carell T, Beese LS;. Nature. 2004;431:217-221. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046329.1
Method:
HMM
2.

5'-3' exonuclease, N-terminal resolvase-like domain

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Date:
2024-08-14
Family Accession:
NF014759.5
Method:
HMM
3.

3'-5' exonuclease

This domain is responsible for the 3'-5' exonuclease proofreading activity of E. coli DNA polymerase I (polI) and other enzymes, it catalyses the hydrolysis of unpaired or mismatched nucleotides. This domain consists of the amino-terminal half of the Klenow fragment in E. coli polI it is also found in the Werner syndrome helicase (WRN), focus forming activity 1 protein (FFA-1) and ribonuclease D (RNase D). Werner syndrome is a human genetic disorder causing premature aging; the WRN protein has helicase activity in the 3'-5' direction [4,5]. The FFA-1 protein is required for formation of a replication foci and also has helicase activity; it is a homologue of the WRN protein [3]. RNase D is a 3'-5' exonuclease involved in tRNA processing. Also found in this family is the autoantigen PM/Scl thought to be involved in polymyositis-scleroderma overlap syndrome. [1]. 3883192. Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Ollis DL, Brick P, Hamlin R, Xuong NG, Steitz TA;. Nature 1985;313:762-766. [2]. 9396823. The proofreading domain of Escherichia coli DNA polymerase I and other DNA and/or RNA exonuclease domains. Moser MJ, Holley WR, Chatterjee A, Mian IS;. Nucleic Acids Res 1997;25:5110-5118. [3]. 9697700. Replication focus-forming activity 1 and the Werner syndrome gene product. Yan H, Chen CY, Kobayashi R, Newport J;. Nat Genet 1998;19:375-378. [4]. 9288107. The Werner syndrome protein is a DNA helicase. Gray MD, Shen JC, Kamath-Loeb AS, Blank A, Sopher BL, Martin GM, Oshima J, Loeb LA;. Nat Genet 1997;17:100-103. [5]. 9224595. DNA helicase activity in Werner's syndrome gene product s. TRUNCATED at 1650 bytes (from Pfam)

GO Terms:
Molecular Function:
nucleic acid binding (GO:0003676)
Biological Process:
nucleobase-containing compound metabolic process (GO:0006139)
Molecular Function:
3'-5' exonuclease activity (GO:0008408)
Date:
2024-10-16
Family Accession:
NF013755.5
Method:
HMM
4.

DNA polymerase

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Molecular Function:
DNA-directed DNA polymerase activity (GO:0003887)
Biological Process:
DNA replication (GO:0006260)
Date:
2024-08-14
Family Accession:
NF012688.5
Method:
HMM
5.

5'-3' exonuclease H3TH domain-containing protein

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Molecular Function:
catalytic activity (GO:0003824)
Date:
2024-08-14
Family Accession:
NF013527.5
Method:
HMM
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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13.
new record, indexing in progress
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14.

DNA polymerase I

DNA polymerase I is a family A polymerase which functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication and it has two functional domains, a 5'-3' polymerase and 5'-3' exonuclease domain.

Date:
2022-08-04
Family Accession:
11481601
Method:
Sparcle
15.

DNA polymerase I

Has 3'-5' exonuclease, 5'-3' exonuclease and 5'-3'polymerase activities, primarily functions to fill gaps during DNA replication and repair

Gene:
polA
GO Terms:
Molecular Function:
nucleic acid binding (GO:0003676)
Molecular Function:
DNA binding (GO:0003677)
Molecular Function:
DNA-directed DNA polymerase activity (GO:0003887)
Biological Process:
DNA-templated DNA replication (GO:0006261)
Molecular Function:
3'-5' exonuclease activity (GO:0008408)
Date:
2021-07-21
Family Accession:
NF004397.1
Method:
HMM
16.

DNA polymerase I

All proteins in this family for which functions are known are DNA polymerases Many also have an exonuclease motif. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).

Gene:
polA
GO Terms:
Molecular Function:
DNA-directed DNA polymerase activity (GO:0003887)
Biological Process:
DNA replication (GO:0006260)
Date:
2021-04-27
Family Accession:
TIGR00593.1
Method:
HMM
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