Protein Family Models

This is a SH3-like domain associated with the MutS-like ABC ATPase and Smr domains. It has been predicted to play a role in lesion recognition or alternatively in mediating contacts with RNA primers or misincorporated ribonucleotides during DNA repair or interacting with the ribosome at the intersection between DNA repair and ribosome rescue [1]. [1]. 32894288. Comprehensive classification of ABC ATPases and their functional. radiation in nucleoprotein dynamics and biological conflict. systems.. Krishnan A, Burroughs AM, Iyer LM, Aravind L;. Nucleic Acids Res. 2020;48:10045-10075. (from Pfam)

Date:

2024-08-14

This family includes the Smr (Small MutS Related) proteins, and the C-terminal region of the MutS2 protein. It has been suggested that this domain interacts with the MutS1 Swiss:P23909 protein in the case of Smr proteins and with the N-terminal MutS related region of MutS2 Swiss:P94545 [1]. This domain exhibits nicking endonuclease activity that might have a role in mismatch repair or genetic recombination. It shows no significant double strand cleavage or exonuclease activity [2]. The full-length Swiss:Q86UW6 also has the polynucleotide kinase activity. [1]. 10431172. Smr: a bacterial and eukaryotic homologue of the C-terminal. region of the MutS2 family.. Moreira D, Philippe H;. Trends Biochem Sci 1999;24:298-300.. [2]. 12730195. Identification and characterization of BCL-3-binding protein:. implications for transcription and DNA repair or recombination.. Watanabe N, Wachi S, Fujita T;. J Biol Chem. 2003;278:26102-26110. (from Pfam)

Date:

2024-08-14

This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with Pfam:PF01624, Pfam:PF05188, Pfam:PF05192 and Pfam:PF05190. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein [2]. The aligned region corresponds with domain V of Thermus aquaticus MutS as characterised in [4], which contains a Walker A motif, and is structurally similar to the ATPase domain of ABC transporters. [1]. 9722634. Domain organization and functional analysis of Thermus. thermophilus MutS protein [published erratum appears in Nucleic. Acids Res 1998 Oct 15;26(20):following 4789]. Tachiki H, Kato R, Masui R, Hasegawa K, Itakura H, Fukuyama K,. Kuramitsu S;. Nucleic Acids Res 1998;26:4153-4159.. [2]. 8036718. Colon cancer and DNA repair: have mismatches met their match?. Jiricny J;. Trends Genet 1994;10:164-168.. [3]. 8510668. The yeast gene MSH3 defines a new class of eukaryotic MutS. homologues.. New L, Liu K, Crouse GF;. Mol Gen Genet 1993;239:97-108.. [4]. 11048710. Crystal structures of mismatch repair protein MutS and its. complex with a substrate DNA.. Obmolova G, Ban C, Hsieh P, Yang W;. Nature 2000;407:703-710. (from Pfam)

Date:

2024-08-14

endonuclease MutS2 is a dsDNA-specific endonuclease/ATPase involved in the suppression of homologous recombination; have a role in the control of bacterial genetic diversity

Date:

2017-06-05

Function of MutS2 is unknown. It should not be considered a DNA mismatch repair protein. It is likely a DNA mismatch binding protein of unknown cellular function.

Date:

2024-05-30