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Conserved domains on  [gi|45550944|ref|NP_723253|]
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male specific transcript 27D, isoform A [Drosophila melanogaster]

Protein Classification

calponin homology domain-containing protein( domain architecture ID 10447812)

calponin homology domain-containing protein such as alpha parvin, which plays a role in sarcomere organization and in smooth muscle cell contraction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 27-128 2.23e-06

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


:

Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 46.13  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550944    27 VSVKTLLMFINSKLDCELRG------FEDLKTGAVYCQLMHRLFPNSIQIHKVKFYTNDISDfqlNFRL-LNNCFQKLRV 99
Cdd:pfam00307   2 ELEKELLRWINSHLAEYGPGvrvtnfTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLE---NINLaLDVAEKKLGV 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 45550944   100 TVYMP-VHELTLGHNQVVfCNWIYKFYEAN 128
Cdd:pfam00307  79 PKVLIePEDLVEGDNKSV-LTYLASLFRRF 107
 
Name Accession Description Interval E-value
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 27-128 2.23e-06

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 46.13  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550944    27 VSVKTLLMFINSKLDCELRG------FEDLKTGAVYCQLMHRLFPNSIQIHKVKFYTNDISDfqlNFRL-LNNCFQKLRV 99
Cdd:pfam00307   2 ELEKELLRWINSHLAEYGPGvrvtnfTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLE---NINLaLDVAEKKLGV 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 45550944   100 TVYMP-VHELTLGHNQVVfCNWIYKFYEAN 128
Cdd:pfam00307  79 PKVLIePEDLVEGDNKSV-LTYLASLFRRF 107
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 28-161 7.22e-06

Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton];


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 47.68  E-value: 7.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550944  28 SVKTLLMFINSKLDCELRGFEDLKTGAVYCQLMHRLFPNsIQIHKVKFYTNDISDFQLNFRLLNNCFQK--LRVTVYMPV 105
Cdd:COG5217   8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIYVD-LPDSLVRFPWIAEYKHPGNGKILQLLFSDygIDKAVLVLV 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 45550944 106 HELTLGHNQVVFCNWIYKFYEANDKGNEYDARKVRKG-SPIGLDNSY-KVASISTGST 161
Cdd:COG5217  87 LVRCKLQDNLEFLQWLKDHWVRNLGHISYDRNARRLGrTPKSTRELIeWIRSLGIPIS 144
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 30-84 1.89e-03

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 37.68  E-value: 1.89e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550944     30 KTLLMFINSKLDCELRG-----FEDLKTGAVYCQLMHRLFPNSIqihKVKFYTNDISDFQ 84
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPpvtnfSSDLKDGVALCALLNSLSPGLV---DKKKVAASLSRFK 57
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 29-68 4.34e-03

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 36.55  E-value: 4.34e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 45550944  29 VKTLLMFINSKLDCELRG-----FEDLKTGAVYCQLMHRLFPNSI 68
Cdd:cd00014   1 EEELLKWINEVLGEELPVsitdlFESLRDGVLLCKLINKLSPGSI 45
 
Name Accession Description Interval E-value
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 27-128 2.23e-06

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 46.13  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550944    27 VSVKTLLMFINSKLDCELRG------FEDLKTGAVYCQLMHRLFPNSIQIHKVKFYTNDISDfqlNFRL-LNNCFQKLRV 99
Cdd:pfam00307   2 ELEKELLRWINSHLAEYGPGvrvtnfTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLE---NINLaLDVAEKKLGV 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 45550944   100 TVYMP-VHELTLGHNQVVfCNWIYKFYEAN 128
Cdd:pfam00307  79 PKVLIePEDLVEGDNKSV-LTYLASLFRRF 107
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 28-161 7.22e-06

Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton];


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 47.68  E-value: 7.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550944  28 SVKTLLMFINSKLDCELRGFEDLKTGAVYCQLMHRLFPNsIQIHKVKFYTNDISDFQLNFRLLNNCFQK--LRVTVYMPV 105
Cdd:COG5217   8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIYVD-LPDSLVRFPWIAEYKHPGNGKILQLLFSDygIDKAVLVLV 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 45550944 106 HELTLGHNQVVFCNWIYKFYEANDKGNEYDARKVRKG-SPIGLDNSY-KVASISTGST 161
Cdd:COG5217  87 LVRCKLQDNLEFLQWLKDHWVRNLGHISYDRNARRLGrTPKSTRELIeWIRSLGIPIS 144
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 30-84 1.89e-03

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 37.68  E-value: 1.89e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550944     30 KTLLMFINSKLDCELRG-----FEDLKTGAVYCQLMHRLFPNSIqihKVKFYTNDISDFQ 84
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPpvtnfSSDLKDGVALCALLNSLSPGLV---DKKKVAASLSRFK 57
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 29-68 4.34e-03

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 36.55  E-value: 4.34e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 45550944  29 VKTLLMFINSKLDCELRG-----FEDLKTGAVYCQLMHRLFPNSI 68
Cdd:cd00014   1 EEELLKWINEVLGEELPVsitdlFESLRDGVLLCKLINKLSPGSI 45
 
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.
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