Protein Family Models

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)

Date:

2024-10-16

The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains [4]. [1]. 9397680. A putative nucleic acid-binding domain in Bloom's and Werner's syndrome helicases. Morozov V, Mushegian AR, Koonin EV, Bork P;. Trends Biochem Sci 1997;22:417-418. [2]. 15990871. The HRDC domain of BLM is required for the dissolution of double Holliday junctions. Wu L, Chan KL, Ralf C, Bernstein DA, Garcia PL, Bohr VA, Vindigni A, Janscak P, Keck JL, Hickson ID;. EMBO J. 2005;24:2679-2687. [3]. 10647186. The three-dimensional structure of the HRDC domain and implications for the Werner and Bloom syndrome proteins. Liu Z, Macias MJ, Bottomley MJ, Stier G, Linge JP, Nilges M, Bork P, Sattler M;. Structure. 1999;7:1557-1566. [4]. 17085080. Three tandem HRDC domains have synergistic effect on the RecQ functions in Deinococcus radiodurans. Huang L, Hua X, Lu H, Gao G, Tian B, Shen B, Hua Y;. DNA Repair (Amst). 2006; [Epub ahead of print] (from Pfam)

Date:

2024-10-16

This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA both in vitro and when overexpressed in vivo. Trusted members of this family are restricted to the Proteobacteria; Aquifex, Mycobacterial, and eukaryotic homologs are not full-length homologs. Ribonuclease D is not essential in E. coli and is deleterious when overexpressed. Its precise biological role is still unknown.

Gene:

rnd

Date:

2024-06-04

ribonuclease D family protein similar to Haemophilus influenzae ribonuclease D involved in the maturation of small stable RNAs and the 3' maturation of tRNA by catalyzing the exonucleolytic cleavage of extra residues from the 3'-terminus of tRNA, and to the ribonuclease D-like proteins, Bartonella birtlesii nanoRNase NrnC which exhibits oligo RNA degradation (nanoRNase) activity, and Agrobacterium tumefaciens nanoRNase NrnC which degrades dsDNA but leaves dsRNA intact

Date:

2021-01-16