Protein Family Models

This domain is part of the LAGLIDADG superfamily [1]. [1]. 18974222. Crystal structure of I-DmoI in complex with its target DNA provides new insights into meganuclease engineering. Marcaida MJ, Prieto J, Redondo P, Nadra AD, Alibes A, Serrano L, Grizot S, Duchateau P, Paques F, Blanco FJ, Montoya G;. Proc Natl Acad Sci U S A. 2008;105:16888-16893. (from Pfam)

Date:

2024-10-16

This domain is found within the sporulation regulator WhiA. It is a LAGLIDADG superfamily like domain [1-2]. [1]. 17603302. Bacterial DUF199/COG1481 Proteins Including Sporulation Regulator WhiA are Distant Homologs of LAGLIDADG Homing Endonucleases That Retained Only DNA Binding. Knizewski L, Ginalski K;. Cell Cycle. 2007;6:1666-1670. [2]. 19836336. The structure of a bacterial DUF199/WhiA protein: domestication of an invasive endonuclease. Kaiser BK, Clifton MC, Shen BW, Stoddard BL;. Structure. 2009;17:1368-1376. (from Pfam)

Date:

2024-10-16

This domain is found at the N terminal of sporulation factor WhiA. This domain is related to the LAGLIDADG Homing endonuclease domain while the C terminal domain of WhiA is predicted to be a DNA binding helix-turn-helix domain [2]. [1]. 10986251. WhiA, a protein of unknown function conserved among gram-positive bacteria, is essential for sporulation in Streptomyces coelicolor A3(2). Ainsa JA, Ryding NJ, Hartley N, Findlay KC, Bruton CJ, Chater KF;. J Bacteriol. 2000;182:5470-5478. [2]. 17603302. Bacterial DUF199/COG1481 Proteins Including Sporulation Regulator WhiA are Distant Homologs of LAGLIDADG Homing Endonucleases That Retained Only DNA Binding. Knizewski L, Ginalski K;. Cell Cycle. 2007;6:1666-1670. [3]. 19836336. The structure of a bacterial DUF199/WhiA protein: domestication of an invasive endonuclease. Kaiser BK, Clifton MC, Shen BW, Stoddard BL;. Structure. 2009;17:1368-1376. (from Pfam)

Date:

2024-10-16

This domain is found at the C-terminus of the sporulation regulator WhiA. It is predicted to form a DNA-binding helix-turn-helix structure [2]. The WhiA protein also contains two N-terminal domains that are distant homologues of LAGLIDADG homing endonucleases [2]. [1]. 10986251. WhiA, a protein of unknown function conserved among gram-positive bacteria, is essential for sporulation in Streptomyces coelicolor A3(2). Ainsa JA, Ryding NJ, Hartley N, Findlay KC, Bruton CJ, Chater KF;. J Bacteriol. 2000;182:5470-5478. [2]. 17603302. Bacterial DUF199/COG1481 Proteins Including Sporulation Regulator WhiA are Distant Homologs of LAGLIDADG Homing Endonucleases That Retained Only DNA Binding. Knizewski L, Ginalski K;. Cell Cycle. 2007;6:1666-1670. [3]. 19836336. The structure of a bacterial DUF199/WhiA protein: domestication of an invasive endonuclease. Kaiser BK, Clifton MC, Shen BW, Stoddard BL;. Structure. 2009;17:1368-1376. (from Pfam)

Date:

2024-10-16

DNA-binding protein WhiA has been reported to be involved in cell division and chromosome segregation; while WhiA binds DNA, it may not function as a transcriptional regulator

Date:

2020-08-14

This family describes a DNA-binding protein widely conserved in Gram-positive bacteria, and occasionally occurring elsewhere, such as in Thermotoga. It is associated with cell division, and in sporulating organisms with sporulation.

Gene:

whiA

Date:

2021-07-29