imported>GydbAdmin at 10:43, 7 November 2011

2011-11-07T10:43:05Z

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The presence of a [http://supfam.cs.bris.ac.uk/SUPERFAMILY/cgi-bin/scop.cgi?sunid=140466 ''SCAN''] domain ([[literature:100844|Williams ''et al''. 1995]]) define a subfamily of associated modules of C2H2 zinc finger proteins involved in protein-protein interactions (for a review see [[literature:100845|Edelstein and Collins 2005]]).

''SCAN-A2'' domain is a group of [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=153421 SCAN] oligomerization domains (cd07936 in Conserved Domain Database) that is present at N-terminus in ''ZNF452/SCAND3'' variants of [[SCAN/KRAB|''SCAN/KRAB'']] cellular integrases. In ''ZNF452/SCAND3'' proteins, no additional zinc finger domain more than that of [[Integrase|Integrase]] can be identified making the ''SCAN'' domain of ''ZNF452/SCAND3'' a particular subgroup probably related with those found in lower vertebrates that are contained in large retrovirus-like polyproteins ([http://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=eurekah&part=A31264| Collins & Sander 2010]; [[literature:33941|Ivanov ''et al.'' 2005]]). We have named it "''SCAN-A2''” domain because according to aminoacid sequence and length, the ''SCAN'' domain identified in ''ZNF452/SCAND3'' C-INTs resembles more that of group A2 described in the mouse genome with a longer C-terminal extension ([[literature:100845|Edelstein and Collins 2005]]).

SCAN - Revision history

imported>GydbAdmin at 10:43, 7 November 2011