Protein Family Models

This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ [1-2]. [1]. 14517231. High-resolution structure of the E.coli RecQ helicase catalytic core. Bernstein DA, Zittel MC, Keck JL;. EMBO J. 2003;22:4910-4921. [2]. 19151156. Structure of the human RECQ1 helicase reveals a putative strand-separation pin. Pike AC, Shrestha B, Popuri V, Burgess-Brown N, Muzzolini L, Costantini S, Vindigni A, Gileadi O;. Proc Natl Acad Sci U S A. 2009;106:1039-1044. (from Pfam)

Date:

2024-10-16

The vast majority of proteins with this DNA-binding domain, called RQC, are RecQ itself, a DNA helicase involved in recombination, replication, and repair. But a few, including WP_003865531 and WP_016764356 represent distinct proteins families with different lengths and currently unknown functions.

Date:

2024-10-16

Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression. [1]. 10322435. Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families. de la Cruz J, Kressler D, Linder P;. Trends Biochem Sci 1999;24:192-198. [2]. 9862990. The DEAD box RNA helicase family in Arabidopsis thaliana. Aubourg S, Kreis M, Lecharny A;. Nucleic Acids Res 1999;27:628-636. (from Pfam)

Date:

2024-10-16

The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase. (from Pfam)

Date:

2024-08-14

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

The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ.

Gene:

recQ

Date:

2024-05-30

All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).

Date:

2021-04-27