SMART: Pfam domain SBP

SBP

PFAM accession number:	PF03110
Interpro abstract (IPR004333):	SBP (for SQUAMOSA-pROMOTER BINDING PROTEIN) domain is a sequence specific DNA-binding domain found in plant proteins [ (PUBMED:8569690) ]. Members of family probably function as transcription factors involved in the control of early flower development [ (PUBMED:8569690) ]. They share a highly conserved DNA-binding domain that contains two zinc-binding sites. Among the 11 possible ligands for the zinc atoms that are conserved in the SBP zinc finger, only 8 are used. The SBP zinc finger follows the general pattern C-x4-C-x16-C-x2-[HC]-x15-C-x2-C-x3-H-x11-C. Three other histidines are well conserved but not involved in zinc binding [ (PUBMED:8569690) (PUBMED:15001351) ]. In vitro experiments show that the SBP zinc finger preferentially binds the consensus sequence -TNCGTACAA- [ (PUBMED:10524240) ]. However, little is known of the physiological functions of these putative transcriptional regulators beyond their ability to bind DNA. The solution structure of the SBP zinc finger has been solved [ (PUBMED:15001351) ]. The first four Cys or His coordinate one zinc ion and the last four coordinate the other. It can be viewed as two structural subdomains, each subdomain containing a single zinc-binding pocket. The N-terminal subdomain consists of two short alpha helices whereas the C-terminal one contains a three-stranded antiparallel beta-sheet.
GO function:	DNA binding (GO:0003677)

PFAM accession number:

PF03110

Interpro abstract (IPR004333):

SBP (for SQUAMOSA-pROMOTER BINDING PROTEIN) domain is a sequence specific DNA-binding domain found in plant proteins [ (PUBMED:8569690) ]. Members of family probably function as transcription factors involved in the control of early flower development [ (PUBMED:8569690) ]. They share a highly conserved DNA-binding domain that contains two zinc-binding sites. Among the 11 possible ligands for the zinc atoms that are conserved in the SBP zinc finger, only 8 are used. The SBP zinc finger follows the general pattern C-x4-C-x16-C-x2-[HC]-x15-C-x2-C-x3-H-x11-C. Three other histidines are well conserved but not involved in zinc binding [ (PUBMED:8569690) (PUBMED:15001351) ].

In vitro experiments show that the SBP zinc finger preferentially binds the consensus sequence -TNCGTACAA- [ (PUBMED:10524240) ]. However, little is known of the physiological functions of these putative transcriptional regulators beyond their ability to bind DNA.

The solution structure of the SBP zinc finger has been solved [ (PUBMED:15001351) ]. The first four Cys or His coordinate one zinc ion and the last four coordinate the other. It can be viewed as two structural subdomains, each subdomain containing a single zinc-binding pocket. The N-terminal subdomain consists of two short alpha helices whereas the C-terminal one contains a three-stranded antiparallel beta-sheet.

GO function:

DNA binding (GO:0003677)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SBP