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Conserved domains on  [gi|1034674093|ref|XP_016884941|]
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cilia- and flagella-associated protein 47 isoform X1 [Homo sapiens]

Protein Classification

calponin homology domain-containing protein( domain architecture ID 289)

calponin homology (CH) domain-containing protein may bind actin filament (F-actin) or serve a regulatory function

CATH:  1.10.418.10
Gene Ontology:  GO:0008017
PubMed:  12186940|11911887

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 1741-1865 8.86e-16

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).


The actual alignment was detected with superfamily member cd21218:

Pssm-ID: 469584  Cd Length: 114  Bit Score: 75.41  E-value: 8.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674093 1741 SSNIYSDSERILLSWMNINYENTRhviwknchkdviPSERWIVNFDKDLSDGLVFATQLGAYCPFLIESHFINMytrPKS 1820
Cdd:cd21218      4 ESLLYLPPEEILLRWVNYHLKKAG------------PTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLE---VLS 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034674093 1821 PEEYLHNCLIIVNTLYEIDFDVEIQATDICDPNPILMLMLCVYMY 1865
Cdd:cd21218     69 EEDLEKRAEKVLQAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLF 113
 
Name Accession Description Interval E-value
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 1741-1865 8.86e-16

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 75.41  E-value: 8.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674093 1741 SSNIYSDSERILLSWMNINYENTRhviwknchkdviPSERWIVNFDKDLSDGLVFATQLGAYCPFLIESHFINMytrPKS 1820
Cdd:cd21218      4 ESLLYLPPEEILLRWVNYHLKKAG------------PTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLE---VLS 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034674093 1821 PEEYLHNCLIIVNTLYEIDFDVEIQATDICDPNPILMLMLCVYMY 1865
Cdd:cd21218     69 EEDLEKRAEKVLQAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLF 113
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 1748-1870 4.05e-05

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: 44.97  E-value: 4.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674093 1748 SERILLSWMNinyentrhviwkNCHKDVIPSERwIVNFDKDLSDGLVFAtqlgaycpFLIESHF---INMYTRPKSPEEY 1824
Cdd:pfam00307    3 LEKELLRWIN------------SHLAEYGPGVR-VTNFTTDLRDGLALC--------ALLNKLApglVDKKKLNKSEFDK 61

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1034674093 1825 LHNCLIIVNTLyEIDFDV---EIQATDICDPNPILMLMLCVYMYERLPT 1870
Cdd:pfam00307   62 LENINLALDVA-EKKLGVpkvLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
 
Name Accession Description Interval E-value
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 1741-1865 8.86e-16

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 75.41  E-value: 8.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674093 1741 SSNIYSDSERILLSWMNINYENTRhviwknchkdviPSERWIVNFDKDLSDGLVFATQLGAYCPFLIESHFINMytrPKS 1820
Cdd:cd21218      4 ESLLYLPPEEILLRWVNYHLKKAG------------PTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLE---VLS 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034674093 1821 PEEYLHNCLIIVNTLYEIDFDVEIQATDICDPNPILMLMLCVYMY 1865
Cdd:cd21218     69 EEDLEKRAEKVLQAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLF 113
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 1748-1870 4.05e-05

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: 44.97  E-value: 4.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674093 1748 SERILLSWMNinyentrhviwkNCHKDVIPSERwIVNFDKDLSDGLVFAtqlgaycpFLIESHF---INMYTRPKSPEEY 1824
Cdd:pfam00307    3 LEKELLRWIN------------SHLAEYGPGVR-VTNFTTDLRDGLALC--------ALLNKLApglVDKKKLNKSEFDK 61

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1034674093 1825 LHNCLIIVNTLyEIDFDV---EIQATDICDPNPILMLMLCVYMYERLPT 1870
Cdd:pfam00307   62 LENINLALDVA-EKKLGVpkvLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
 
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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