Summary: SMI1 / KNR4 family (SUKH-1)
SMI1 / KNR4 family (SUKH-1) Provide feedback
Proteins in this family are involved in the regulation of 1,3-beta-glucan synthase activity and cell-wall formation . Genome contextual information showed that SMI1 are primary immunity proteins in bacterial toxin systems .
Enderlin CS, Selitrennikoff CP; , Proc Natl Acad Sci U S A. 1994;91:9500-9504.: Cloning and characterization of a Neurospora crassa gene required for (1,3) beta-glucan synthase activity and cell wall formation. PUBMED:7937796 EPMC:7937796
Hong Z, Mann P, Brown NH, Tran LE, Shaw KJ, Hare RS, DiDomenico B; , Mol Cell Biol. 1994;14:1017-1025.: Cloning and characterization of KNR4, a yeast gene involved in (1,3)-beta-glucan synthesis. PUBMED:8289782 EPMC:8289782
Zhang D, Iyer LM, Aravind L;, Nucleic Acids Res. 2011;39:4532-4552.: A novel immunity system for bacterial nucleic acid degrading toxins and its recruitment in various eukaryotic and DNA viral systems. PUBMED:21306995 EPMC:21306995
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR018958
Saccharomyces cerevisiae protein Smi1 has a regulatory role in chitin deposition and in cell wall assembly [PUBMED:10206705].
KNR4 is believed to connect the PKC1-SLT2 MAPK pathway with cell proliferation. It has been shown to interact with BCK2, a gene involved in cell cycle progression in S. cerevisiae (forming a complex) to allow PKC1 to coordinate the cell cycle (cell proliferation) with cell wall integrity [PUBMED:12185498, PUBMED:12823808]. KNR4 also interacts with the tyrosine-tRNA synthetase protein encoded by TYS1 and is involved in sporulation process [PUBMED:11410349].
Proteins containing this domain also include the animal F-box only protein 3 (FBXO3). In humans, FBXO3 is a substrate recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex [PUBMED:18809579].
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SUKH superfamily unites a diverse group of proteins including Smi1/Knr4, PGs2, Fbxo3, Skip16, Syd, herpesviral US22, IRS1 and TRS1, and their bacterial homologs .
The clan contains the following 7 members:SMI1_KNR4 SUKH-3 SUKH-4 SUKH_5 SUKH_6 Syd US22
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||PSI2 target BIG_91|
|Number in seed:||177|
|Number in full:||5598|
|Average length of the domain:||130.90 aa|
|Average identity of full alignment:||16 %|
|Average coverage of the sequence by the domain:||58.34 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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There is 1 interaction 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.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the SMI1_KNR4 domain has been found. There are 3 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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