Protein hinderin shares structural similarity to the SMC family members. It interacts with SMC3 and may affect the availability of SMC3 to engage in the formation of multimeric protein complexes [].
The Wapl domain is found at the C terminus of fungal Wpl1 proteins (also known as Rad61), which are subunits of a complex that inhibits sister chromatid cohesion. The Wapl domain binds to the ATPase domain of cohesin subunit Smc3 [].
The Wapl domain is found at the C terminus of fungal Wpl1 proteins (also known as Rad61), which are subunits of a complex that inhibits sister chromatid cohesion. The Wapl domain binds to the ATPase domain of cohesin subunit Smc3 [].
This entry represents the acetyl-transferase domain of the acetyl-transferase ESCO. N-acetyltransferase ESCO1 and ESCO2 are required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. They act by mediating the acetylation of cohesin component SMC3 []. They feature a conserved C-terminal domain consisting of a H2C2 zinc finger motif () and an acetyltransferase domain, while the diverse N-terminal domain is involved in chromosome binding and could target these proteins to different chromosome structures [].
This entry represents the zinc-inger domain of the acetyl-transferase ESCO. N-acetyltransferase ESCO1 and ESCO2 are required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. They act by mediating the acetylation of cohesin component SMC3 []. They feature a conserved C-terminal domain consisting of a H2C2 zinc finger motif and an acetyltransferase domain (), while the diverse N-terminal domain is involved in chromosome binding and could target these proteins to different chromosome structures [].
N-acetyltransferase ESCO1 (also known as ECO1/EFO1) and ESCO2 are required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. They act by mediating the acetylation of cohesin component SMC3 []. They feature a conserved C-terminal domain consisting of a H2C2 zinc finger motif () and an acetyltransferase domain (), while the diverse N-terminal domain is involved in chromosome binding and could target these proteins to different chromosome structures [].This entry represents ESCO1.
The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'WalkerA' nucleotide-binding domain (GxxGxGKS/T), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 [].This entry represents the ATP-binding cassette domain of eukaryotic SMC3 proteins, which is found at the N terminus.
Structural maintenance of chromosomes protein 1A (SMC1A) is a homologue of the yeast Smc1 protein, which is a component of the cohesin complex required for sister chromatid cohesion []. In human, it is part of the core cohesion complex composed of SMC1A, SMC3, RAD21 and STAG proteins []. These proteins form a ring structure that encircles sister chromatids to mediate sister chromatid cohesion []. SMC1A binds to SMC3 through its hinge domain []. Besides sister chromatid cohesion function, SMC1A-SMC3 heterodimer can also found in the RC-1 complex, a mammalian protein complex that promotes repair of DNA gaps and deletions through recombination [, ]. This entry also includes Smc1 homologue from Caenorhabditis elegans, SMCL-1. Unlike canonical SMC proteins, SMCL-1 lacks hinge and coil domains, and its ATPase domain lacks conserved amino acids required for ATP hydrolysis []. Mutations in SMC1A gene cause Cornelia de Lange syndrome 2 (CDLS2), which is a form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems [, ].
