The Filament domain within your query sequence starts at position 166 and ends at position 479, and its E-value is 6.11e-149.

QEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRTSSLEPVFEEFISQLQRQVDVLTTEQLRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVDAAFMGKSDLQSKVDTLYGEINFLKYLFDTELSQIQTHVSDTNVILSMDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESR

Filament Intermediate filament protein
SMART ACC:	SM001391
Description:	-
InterPro ACC:	IPR039008
InterPro abstract:	Intermediate filaments (IF) [ PUBMED:2183847 PUBMED:28101862 ] are proteins which are primordial components of the cytoskeleton and the nuclear envelope. They generally form filamentous structures 8 to 14 nm wide. IF proteins are members of … expand Intermediate filaments (IF) [ PUBMED:2183847 PUBMED:28101862 ] are proteins which are primordial components of the cytoskeleton and the nuclear envelope. They generally form filamentous structures 8 to 14 nm wide. IF proteins are members of a very large multigene family of proteins which has been subdivided in six types: Type I: Acidic cytokeratins. Type II: Basic cytokeratins. Type III: Vimentin, desmin, glial fibrillary acidic protein (GFAP), peripherin, and plasticin. Type IV: Neurofilaments L, H and M, alpha-internexin and nestin. Type V: Nuclear lamins A, B1, B2 and C. Type VI: 'Orphan' IF proteins, which are more distant in terms of their amino acid sequences. All IF proteins are structurally similar in that they consist of: a central rod domain comprising some 300 to 350 residues which is arranged in coiled- coiled α-helices, with at least two short characteristic interruptions; a N-terminal non-helical domain (head) of variable length; and a C-terminal domain (tail) which is also non-helical, and which shows extreme length variation between different IF proteins. While IF proteins are evolutionary and structurally related, they have limited sequence homologies except in several regions of the rod domain. The IF rod domain is approximately 310 residues long in all cytoplasmic IF proteins and close to 350 residues in the nuclear ones. The IF rod domain exhibits an interrupted α-helical conformation and reveals a pronounced seven-residue periodicity in the distribution of apolar residues. The heptad periodicity within the rod domain is interrupted in several places, which generates four consecutive α-helical segments: 1A and 1B, which together form the so-called coil 1, and 2A and 2B, which form coil 2. The four α-helical segments are interconnected by relatively short, variable linkers L1, L12 and L2 [ PUBMED:12596228 PUBMED:22869704 ]. IF proteins have a very strong tendency to dimerize via the formation of an α-helical coiled coil (CC) by their rod domains [ PUBMED:22869704 ]. collapse
Family alignment:	View the Family alignment or the Alignment consensus sequence
There are 20 668 Filament domains in 20 433 proteins in SMART's NRDB database.

Taxonomic distribution of proteins containing Filament domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing Filament domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Relevant references for this domain

Primary literature for the Filament domain is listed below. Automatically-derived, secondary literature is also available.

KEGG pathways involving proteins which contain this domain

This information is based on the mapping of SMART genomic protein database to KEGG orthologous groups. Percentages are related to the number of proteins containing a Filament domain which could be assigned to a KEGG orthologous group, and not all proteins containing Filament domains. Please note that proteins can be included in multiple pathways, ie. the numbers below will not add to 100%.

KEGG pathways

Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

Some of these KOs are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

3D structures in PDB containing this domain

Links to other resources describing this domain

Pfam	Filament
InterPro	IPR039008