Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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SAM_PNT SAM / Pointed domain

SMART accession number:	SM00251
Description:	A subfamily of the SAM domain
Interpro abstract (IPR003118):	Transcription factors are protein molecules that bind to specific DNA sequences in the genome, resulting in the induction or inhibition of gene transcription [(PUBMED:2163347)]. The ets oncogene is such a factor, possessing a region of 85-90 amino acids known as the ETS (erythroblast transformation specific) domain [(PUBMED:2163347), (PUBMED:2253872)]. This domain is rich in positively-charged and aromatic residues, and binds to purine-rich segments of DNA. The ETS domain IPR000418 has been identified in other transcription factors such as PU.1, human erg, human elf-1, human elk-1, GA binding protein, and a number of others [(PUBMED:2163347), (PUBMED:2253872), (PUBMED:8425553)]. It is generally localized at the C terminus of the protein, with the exception of ELF-1, ELK-1, ELK-3, ELK-4 and ERF where it is found at the N terminus. This entry describes the highly conserved PNT (or Pointed) domain which is found within a subset of the ETs domain (IPR000418 ), including mammalian Ets-1, Ets-2, Erg, Fli-1, GABPalpha, and Tel, as well as Drosophila Pnt-P2 and Yan. The PNT domain (IPR001660 ) through a common tertiary arrangement of four alpha-helices. A role in protein-protein association has been established for the PNT domain [(PUBMED:10828014), (PUBMED:15351649)].
GO component:	nucleus (GO:0005634)
GO function:	sequence-specific DNA binding (GO:0043565)
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 560 SAM_PNT domains in 559 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a SAM_PNT domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with SAM_PNT domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Takifugu rubripes

• Metabolism (metabolic pathways involving proteins which contain this domain)

• % proteins involved KEGG pathway ID Description 100.00 map04320 Dorso-ventral axis formation This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with SAM_PNT domain which could be assigned to a KEGG orthologous group, and not all proteins containing SAM_PNT domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

• Structure (3D structures containing this domain)

• 3D Structures of SAM_PNT domains in PDB

  PDB code	Main view	Title
  1ji7		Crystal structure of tel sam polymer
  1lky		Structure of the wild-type tel-sam polymer
  1sv0		Crystal structure of yan-sam/mae-sam complex
  1sv4		Crystal structure of yan-sam
  1sxd		Solution structure of the pointed (pnt) domain from mgabpa
  1sxe		The solution structure of the pointed (pnt) domain from the transcrition factor erg
  1x66		Solution structure of the sam_pnt-domain of the human friend leukemiaintegration 1 transcription factor
  2dkx		Solution structure of the sam_pnt-domain of ets transcription factor pdef (prostate ets)
  2e8p		Solution structure of the n-terminal sam-domain of e74-like factor 3
  2jv3		Ets-1 pnt domain (29-138) nmr structure ensemble
  2qar		Structure of the 2tel crystallization module fused to t4 lysozyme with a helical linker.
  2qb0		Structure of the 2tel crystallization module fused to t4 lysozyme with an ala-gly-pro linker.
  2qb1		2tel crystallization module
  2ytu		Solution structure of the sam_pnt-domain of the human friend leukemiaintegration 1 transcription factor

• Links (links to other resources describing this domain)

• INTERPRO	IPR003118

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