Summary: Roadblock/LC7 domain
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Roadblock/LC7 domain Provide feedback
This family includes proteins that are about 100 amino acids long and have been shown to be related . Members of this family of proteins are associated with both flagellar outer arm dynein and Drosophila and rat brain cytoplasmic dynein. It is proposed that roadblock/LC7 family members may modulate specific dynein functions . This family also includes Q9Y2Q5 Golgi-associated MP1 adapter protein and MglB from Myxococcus xanthus Q50883 a protein involved in gliding motility . However the family also includes members from non-motile bacteria such as Streptomyces coelicolor, suggesting that the protein may play a structural or regulatory role.
Hodgson JW, Argiropoulos B, Brock HW; , Mol Cell Biol 2001;21:4528-4543.: Site-specific recognition of a 70-base-pair element containing d(GA)(n) repeats mediates bithoraxoid polycomb group response element-dependent silencing. PUBMED:11416132 EPMC:11416132
Bowman AB, Patel-King RS, Benashski SE, McCaffery JM, Goldstein LS, King SM; , J Cell Biol 1999;146:165-180.: Drosophila roadblock and Chlamydomonas LC7: a conserved family of dynein-associated proteins involved in axonal transport, flagellar motility, and mitosis. PUBMED:10402468 EPMC:10402468
Koonin EV, Aravind L; , Curr Biol 2000;10:774-776.: Dynein light chains of the Roadblock/LC7 group belong to an ancient protein superfamily implicated in NTPase regulation. PUBMED:11084347 EPMC:11084347
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR004942
This family includes proteins that are about 100 amino acids long and have been shown to be related [PUBMED:11084347]. Members of this family of proteins are associated with both flagellar outer arm dynein and Drosophila and rat brain cytoplasmic dynein. It is proposed that roadblock/LC7 family members may modulate specific dynein functions [PUBMED:10402468]. This family also includes Golgi-associated MP1 adapter protein (SWISSPROT) and MglB from Myxococcus xanthus (SWISSPROT), a protein involved in gliding motility [PUBMED:2464581]. However the family also includes members from non-motile bacteria such as Streptomyces coelicolor, suggesting that the protein may play a structural or regulatory role.
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The families here all show the Profilin-like fold, and represent both the Profilin (actin-binding protein) (55770) and the Roadblock/LC7 domain-type (103196) superfamilies.
The clan contains the following 4 members:LAMTOR5 MAPKK1_Int Profilin Robl_LC7
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Aravind L|
|Author:||Mifsud W, Bateman A|
|Number in seed:||38|
|Number in full:||4889|
|Average length of the domain:||90.30 aa|
|Average identity of full alignment:||34 %|
|Average coverage of the sequence by the domain:||66.94 %|
|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:||13|
|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.
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 Robl_LC7 domain has been found. There are 43 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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