NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1021311779|ref|NP_001310549|]
View 

protein unc-45 homolog A isoform 4 [Homo sapiens]

Protein Classification

UNC45-central domain-containing protein( domain architecture ID 10569479)

UNC45-central domain-containing protein similar to Homo sapiens SWI5-dependent HO expression protein 4 (SHE4) required for mother cell-specific ho expression

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
UNC45-central pfam11701
Myosin-binding striated muscle assembly central; The UNC-45 or small muscle protein 1 of C. ...
 218-360 8.66e-31

Myosin-binding striated muscle assembly central; 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 pfam00514 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 organized myofibrils. 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. 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.


:

Pssm-ID: 432011  Cd Length: 151  Bit Score: 118.02  E-value: 8.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311779 218 VTANSRMSASILLSKLfddlkCDAERENFHRLCENYIKSWFEGQGLAGKLRAIQTVSCLLQGPCDAGNRALELSGVMESV 297
Cdd:pfam11701  14 LPESVRSLALLILSKL-----LEAAKEEFEEKFSEFITSLLADGTNDDLIIAFSALAALFPVPPDVASALFLSEGFLESL 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021311779 298 IALCAS-EQEEEQLVAVEALIHAAGKAKRASFITANGVSLLKDLYKcSEKDSIRIRALVGLCKL 360
Cdd:pfam11701  89 LPLVESkKSRKVELAALELLSAACIDKACREAISKNYVDWLEELLK-SSDDEIKALAAVVLAKL 151
 
Name Accession Description Interval E-value
UNC45-central pfam11701
Myosin-binding striated muscle assembly central; The UNC-45 or small muscle protein 1 of C. ...
 218-360 8.66e-31

Myosin-binding striated muscle assembly central; 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 pfam00514 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 organized myofibrils. 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. 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.


Pssm-ID: 432011  Cd Length: 151  Bit Score: 118.02  E-value: 8.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311779 218 VTANSRMSASILLSKLfddlkCDAERENFHRLCENYIKSWFEGQGLAGKLRAIQTVSCLLQGPCDAGNRALELSGVMESV 297
Cdd:pfam11701  14 LPESVRSLALLILSKL-----LEAAKEEFEEKFSEFITSLLADGTNDDLIIAFSALAALFPVPPDVASALFLSEGFLESL 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021311779 298 IALCAS-EQEEEQLVAVEALIHAAGKAKRASFITANGVSLLKDLYKcSEKDSIRIRALVGLCKL 360
Cdd:pfam11701  89 LPLVESkKSRKVELAALELLSAACIDKACREAISKNYVDWLEELLK-SSDDEIKALAAVVLAKL 151
 
Name Accession Description Interval E-value
UNC45-central pfam11701
Myosin-binding striated muscle assembly central; The UNC-45 or small muscle protein 1 of C. ...
 218-360 8.66e-31

Myosin-binding striated muscle assembly central; 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 pfam00514 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 organized myofibrils. 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. 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.


Pssm-ID: 432011  Cd Length: 151  Bit Score: 118.02  E-value: 8.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311779 218 VTANSRMSASILLSKLfddlkCDAERENFHRLCENYIKSWFEGQGLAGKLRAIQTVSCLLQGPCDAGNRALELSGVMESV 297
Cdd:pfam11701  14 LPESVRSLALLILSKL-----LEAAKEEFEEKFSEFITSLLADGTNDDLIIAFSALAALFPVPPDVASALFLSEGFLESL 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021311779 298 IALCAS-EQEEEQLVAVEALIHAAGKAKRASFITANGVSLLKDLYKcSEKDSIRIRALVGLCKL 360
Cdd:pfam11701  89 LPLVESkKSRKVELAALELLSAACIDKACREAISKNYVDWLEELLK-SSDDEIKALAAVVLAKL 151
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH