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3  structures 207  species 0  interactions 280  sequences 10  architectures

Family: UNC45-central (PF11701)

Summary: Myosin-binding striated muscle assembly central

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Myosin-binding striated muscle assembly central Provide feedback

The UNC-45 or small muscle protein 1 of C.elegans is expressed in two forms from different genomic positions in mammals, as a general tissue protein UNC-45a and a specific form Unc-45b expressed only in striated and skeletal muscle. All members carry up to three amino-terminal tetratricopeptide repeat (TPR) domains towards their N-terminal, a UCS domain at the C-terminal that contains a number of Arm repeats PF00514 and this central region of approximately 400 residues. Both the general form and the muscle form of UNC-45 function in myotube formation through cell fusion. Myofibril formation requires both GC and SM UNC-45, consistent with the fact that the cytoskeleton is necessary for the development and maintenance of organised myofibrils [1]. The S. pombe Rng3p, is crucial for cell shape, normal actin cytoskeleton, and contractile ring assembly, and is essential for assembly of the myosin II-containing progenitors of the contractile ring. Widespread defects in the cytoskeleton are found in null mutants of all three fungal proteins [2]. Mammalian Unc45 is found to act as a specific chaperone during the folding of myosin and the assembly of striated muscle by forming a stable complex with the general chaperone Hsp90. The exact function of this central region is not known [3].

Literature references

  1. Price MG, Landsverk ML, Barral JM, Epstein HF; , J Cell Sci. 2002;115:4013-4023.: Two mammalian UNC-45 isoforms are related to distinct cytoskeletal and muscle-specific functions. PUBMED:12356907 EPMC:12356907

  2. Lord M, Sladewski TE, Pollard TD; , Proc Natl Acad Sci U S A. 2008;105:8014-8019.: Yeast UCS proteins promote actomyosin interactions and limit myosin turnover in cells. PUBMED:18523008 EPMC:18523008

  3. Srikakulam R, Liu L, Winkelmann DA; , PLoS ONE. 2008;3:e2137.: Unc45b forms a cytosolic complex with Hsp90 and targets the unfolded myosin motor domain. PUBMED:18478096 EPMC:18478096


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR024660

The UNC-45 or small muscle protein 1 of Caenorhabditis elegans is expressed in two forms from different genomic positions in mammals: as a general tissue protein (UNC-45a) and as a specific form (UNC-45b) expressed only in striated and skeletal muscle. Myofibril formation requires both UNC-45 forms, consistent with the fact that the cytoskeleton is necessary for the development and maintenance of organised myofibrils [PUBMED:12356907]. Rng3 (Ring assembly protein 3), the homologue in Schizosaccharomyces pombe, is crucial for cell shape, normal actin cytoskeleton, and contractile ring assembly, and is essential for assembly of the myosin II-containing progenitors of the contractile ring. Widespread defects in the cytoskeleton are found in null mutants of all three fungal proteins [PUBMED:18523008]. Mammalian Unc45 is found to act as a specific chaperone during the folding of myosin and the assembly of striated muscle by forming a stable complex with the general chaperone Hsp90 [PUBMED:18478096]. All members carry up to three amino-terminal tetratricopeptide repeat (TPR) and a UCS domain at the C terminus that contains a number of Arm repeats.

Domain organisation

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Alignments

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(31)
Full
(280)
Representative proteomes NCBI
(266)
Meta
(1)
RP15
(46)
RP35
(82)
RP55
(138)
RP75
(188)
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  Seed
(31)
Full
(280)
Representative proteomes NCBI
(266)
Meta
(1)
RP15
(46)
RP35
(82)
RP55
(138)
RP75
(188)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(31)
Full
(280)
Representative proteomes NCBI
(266)
Meta
(1)
RP15
(46)
RP35
(82)
RP55
(138)
RP75
(188)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

HMM logo

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Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: manual
Previous IDs: none
Type: Family
Author: Wood V, Coggill P
Number in seed: 31
Number in full: 280
Average length of the domain: 194.20 aa
Average identity of full alignment: 28 %
Average coverage of the sequence by the domain: 23.10 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 25.1 29.8
Noise cut-off 24.9 24.9
Model length: 157
Family (HMM) version: 3
Download: download the raw HMM for this family

Species distribution

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Structures

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 UNC45-central 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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