Summary: Type IV pilin N-term methylation site GFxxxE
Type IV pilin N-term methylation site GFxxxE Provide feedback
This short sequence motif appears a the N-terminus of type IV prokaryotic filamentous adhesins or pilins. The N-terminal residue, which is methylated, is hydrophobic (generally a phenylalanine or a methionine), and this leader peptide is hydrophilic. The fifth residue of the mature sequence is a glutamate which seems to be required for the methylation step.
Internal database links
|SCOOP:||N_methyl_3 DUF4330 TadF|
|Similarity to PfamA using HHSearch:||N_methyl N_methyl_3|
This tab holds annotation information from the InterPro database.
InterPro entry IPR012902
This short motif directs methylation of the conserved phenylalanine residue. It is most often found at the N terminus of pilins and other proteins involved in secretion (see INTERPRO, INTERPRO, INTERPRO and INTERPRO).
There is a cleavage site G^FxxxE followed by a hydrophobic stretch. The new N-terminal residue produced after cleavage, usually Phe, is methylated. Separate domains of the prepilin peptidase appear to be responsible for cleavage and methylation. Proteins with this N-terminal region include type IV pilins and other components of pilus biogenesis, competence proteins, and type II secretion proteins. Typically several proteins in a single operon have this region.
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
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This is a clan contains bacterial pilus subunits and proteins involved in secretion. Pili proteins enable the transfer of plasmid between bacteria. The families in this clan adopt an alpha helical structure which is packed against a beta sheet [2-3].
The clan contains the following 14 members:Bundlin ComP_DUS N_methyl N_methyl_2 N_methyl_3 Pilin Pilin_GH Pilin_PilX PilS T2SSG T2SSI T2SSJ TcpA YadA_anchor
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Number in seed:||255|
|Number in full:||2013|
|Average length of the domain:||25.90 aa|
|Average identity of full alignment:||38 %|
|Average coverage of the sequence by the domain:||12.44 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||3|
|Download:||download the raw HMM for this family|
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There are 3 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.