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Conserved domains on  [gi|226423897|ref|NP_034052|]
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calponin-1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
27-134 3.66e-78

calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), also called basic calponin, or smooth muscle calponin H1, is a thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C, and tropomyosin. Calponin-1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409131 [Multi-domain]  Cd Length: 108  Bit Score: 232.84  E-value: 3.66e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  27 DHQREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKPHDIF 106
Cdd:cd21282    1 DPQTEEELRVWIEGVTGRRIGDNFMDGLKDGVILCELINKLQPGSVRKINESTQNWHKLENIGNFIKAIMHYGVKPHDIF 80
                         90       100
                 ....*....|....*....|....*...
gi 226423897 107 EANDLFENTNHTQVQSTLLALASMAKTK 134
Cdd:cd21282   81 EANDLFENTNHTQVQSTLIALASMAKTK 108
Calponin pfam00402
Calponin family repeat;
164-188 1.00e-10

Calponin family repeat;


:

Pssm-ID: 459803  Cd Length: 25  Bit Score: 55.60  E-value: 1.00e-10
                          10        20
                  ....*....|....*....|....*
gi 226423897  164 IGLQMGTNKFASQQGMTAYGTRRHL 188
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25
Calponin pfam00402
Calponin family repeat;
204-228 3.63e-10

Calponin family repeat;


:

Pssm-ID: 459803  Cd Length: 25  Bit Score: 54.06  E-value: 3.63e-10
                          10        20
                  ....*....|....*....|....*
gi 226423897  204 ISLQMGTNKGASQAGMTAPGTKRQI 228
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25
Calponin pfam00402
Calponin family repeat;
243-267 1.93e-08

Calponin family repeat;


:

Pssm-ID: 459803  Cd Length: 25  Bit Score: 49.06  E-value: 1.93e-08
                          10        20
                  ....*....|....*....|....*
gi 226423897  243 VSLQMGSNKGASQRGMTVYGLPRQV 267
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25
 
Name Accession Description Interval E-value
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
27-134 3.66e-78

calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), also called basic calponin, or smooth muscle calponin H1, is a thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C, and tropomyosin. Calponin-1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409131 [Multi-domain]  Cd Length: 108  Bit Score: 232.84  E-value: 3.66e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  27 DHQREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKPHDIF 106
Cdd:cd21282    1 DPQTEEELRVWIEGVTGRRIGDNFMDGLKDGVILCELINKLQPGSVRKINESTQNWHKLENIGNFIKAIMHYGVKPHDIF 80
                         90       100
                 ....*....|....*....|....*...
gi 226423897 107 EANDLFENTNHTQVQSTLLALASMAKTK 134
Cdd:cd21282   81 EANDLFENTNHTQVQSTLIALASMAKTK 108
SCP1 COG5199
Calponin [Cytoskeleton];
18-188 2.26e-27

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 104.62  E-value: 2.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  18 VKNKLAQKYDHQREQELREWIEGVTGRRIG--NNFMDGLKDGIILCEFINKLQPGSVKkVNESTQNWHQLENIGNFIKAI 95
Cdd:COG5199    2 VNTKNRCPGMDKQQKEVTLWIETVLGEKFEppGDLLSLLKDGVRLCRILNEASPLDIK-YKESKMPFVQMENISSFINGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  96 TKYGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTK--GNKVNVGVKYAEKQERRFE-PEKLREGRNIIGLQMGTNK 172
Cdd:COG5199   81 KKLRVPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQKErmFSGPFLGPHLATKKPRVFSsQEVLDRSKGAIHLQYGYSD 160
                        170
                 ....*....|....*..
gi 226423897 173 FASQQG-MTAYGTRRHL 188
Cdd:COG5199  161 LSEQSTeKGASNVRRDL 177
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
28-133 1.09e-25

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: 98.13  E-value: 1.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897   28 HQREQELREWIEGVTGRRIGN----NFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIK-AITKYGVKP 102
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGvrvtNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDvAEKKLGVPK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 226423897  103 HDIfEANDLFENtNHTQVQSTLLALASMAKT 133
Cdd:pfam00307  81 VLI-EPEDLVEG-DNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
33-127 1.70e-20

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: 84.29  E-value: 1.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897    33 ELREWIEGVTGRRIG---NNFMDGLKDGIILCEFINKLQPGSV--KKVNESTQNWHQLENIGNFIKAITKYGVKPhDIFE 107
Cdd:smart00033   2 TLLRWVNSLLAEYDKppvTNFSSDLKDGVALCALLNSLSPGLVdkKKVAASLSRFKKIENINLALSFAEKLGGKV-VLFE 80
                           90       100
                   ....*....|....*....|.
gi 226423897   108 ANDLFENTNHT-QVQSTLLAL 127
Cdd:smart00033  81 PEDLVEGPKLIlGVIWTLISL 101
Calponin pfam00402
Calponin family repeat;
164-188 1.00e-10

Calponin family repeat;


Pssm-ID: 459803  Cd Length: 25  Bit Score: 55.60  E-value: 1.00e-10
                          10        20
                  ....*....|....*....|....*
gi 226423897  164 IGLQMGTNKFASQQGMTAYGTRRHL 188
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25
Calponin pfam00402
Calponin family repeat;
204-228 3.63e-10

Calponin family repeat;


Pssm-ID: 459803  Cd Length: 25  Bit Score: 54.06  E-value: 3.63e-10
                          10        20
                  ....*....|....*....|....*
gi 226423897  204 ISLQMGTNKGASQAGMTAPGTKRQI 228
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25
Calponin pfam00402
Calponin family repeat;
243-267 1.93e-08

Calponin family repeat;


Pssm-ID: 459803  Cd Length: 25  Bit Score: 49.06  E-value: 1.93e-08
                          10        20
                  ....*....|....*....|....*
gi 226423897  243 VSLQMGSNKGASQRGMTVYGLPRQV 267
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25
 
Name Accession Description Interval E-value
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
27-134 3.66e-78

calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), also called basic calponin, or smooth muscle calponin H1, is a thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C, and tropomyosin. Calponin-1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409131 [Multi-domain]  Cd Length: 108  Bit Score: 232.84  E-value: 3.66e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  27 DHQREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKPHDIF 106
Cdd:cd21282    1 DPQTEEELRVWIEGVTGRRIGDNFMDGLKDGVILCELINKLQPGSVRKINESTQNWHKLENIGNFIKAIMHYGVKPHDIF 80
                         90       100
                 ....*....|....*....|....*...
gi 226423897 107 EANDLFENTNHTQVQSTLLALASMAKTK 134
Cdd:cd21282   81 EANDLFENTNHTQVQSTLIALASMAKTK 108
CH_CNN cd21211
calponin homology (CH) domain found in the calponin family; Calponin is an actin ...
27-134 1.78e-77

calponin homology (CH) domain found in the calponin family; Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and many types of non-muscle cells. There are three calponin isoforms, calponin-1, -2, -3. All of them are actin-binding proteins with functions in inhibiting actin-activated myosin ATPase and stabilizing the actin cytoskeleton. Calponin-1 is specifically expressed in smooth muscle cells and plays a role in fine-tuning smooth muscle contractility. Calponin-2 is expressed in both smooth muscle and non-muscle cells and regulates multiple actin cytoskeleton-based functions. Calponin-3 is expressed in the brain and participates in actin cytoskeleton-based activities in embryonic development and myogenesis. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409060 [Multi-domain]  Cd Length: 108  Bit Score: 231.04  E-value: 1.78e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  27 DHQREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKPHDIF 106
Cdd:cd21211    1 DHQKEAELRTWIEGVTGLSIGPNFQKGLKDGIILCELINKLQPGSVKKINESMQNWHQLENIGNFIKAIVSYGMKPHDIF 80
                         90       100
                 ....*....|....*....|....*...
gi 226423897 107 EANDLFENTNHTQVQSTLLALASMAKTK 134
Cdd:cd21211   81 EANDLFENGNMTQVQVTLLALAGKAKTK 108
CH_CNN3 cd21284
calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic ...
25-135 2.96e-66

calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic isoform calponin, is an F-actin-binding protein that is expressed in the brain and has been shown to control dendritic spine morphology, density, and plasticity by regulating actin cytoskeletal reorganization and dynamics. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409133 [Multi-domain]  Cd Length: 111  Bit Score: 202.44  E-value: 2.96e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  25 KYDHQREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKPHD 104
Cdd:cd21284    1 KYDPQKEEELRNWIEEVTGMSIGENFQKGLKDGVILCELINKLQPGSIRKINESKLNWHQLENIGNFIKAIQAYGMKPHD 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 226423897 105 IFEANDLFENTNHTQVQSTLLALASMAKTKG 135
Cdd:cd21284   81 IFEANDLFENGNMTQVQTTLLALAGLAKTKG 111
CH_CNN2 cd21283
calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral ...
27-135 2.76e-63

calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral calponin, or smooth muscle calponin H2, is an actin cytoskeleton-associated regulatory protein that inhibits the activity of myosin-ATPase and cytoskeleton dynamics. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409132 [Multi-domain]  Cd Length: 109  Bit Score: 195.15  E-value: 2.76e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  27 DHQREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKPHDIF 106
Cdd:cd21283    1 DPQKEAELRTWIEGLTGRSIGPDFQKGLKDGVILCELMNKLQPGSVPKINRSMQNWHQLENLSNFIKAMVSYGMKPVDLF 80
                         90       100
                 ....*....|....*....|....*....
gi 226423897 107 EANDLFENTNHTQVQSTLLALASMAKTKG 135
Cdd:cd21283   81 EANDLFESGNMTQVQVSLLALAGMAKTKG 109
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
25-129 1.93e-38

calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 (dMP20) and similar domains; This subfamily contains Drosophila melanogaster muscle-specific protein 20 (dMP20), Echinococcus granulosus myophilin, Dictyostelium discoideum Rac guanine nucleotide exchange factor B (also called Trix), and similar proteins. dMP20 is present only in the synchronous muscles of D. melanogaster. It may be involved in the system linking the nerve impulse with the contraction or the relaxation process. Trix is involved in the regulation of the late steps of the endocytic pathway. dMP20 contains a single copy of the CH domain, while Trix (triple CH-domain array exchange factor) contains three, two type 3 CH domains which are included in this model, and one type 1 CH domain that is not included in this subfamily, but is part of the superfamily. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409056 [Multi-domain]  Cd Length: 107  Bit Score: 131.28  E-value: 1.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  25 KYDHQREQELREWIEGVTGRRI--GNNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKP 102
Cdd:cd21207    1 KRDPALEAEALDWIEAVTGEKLddGKDYEDVLKDGVILCKLINILKPGSVKKINTSKMAFKLMENIENFLTACKGYGVPK 80
                         90       100
                 ....*....|....*....|....*..
gi 226423897 103 HDIFEANDLFENTNHTQVQSTLLALAS 129
Cdd:cd21207   81 TDLFQTVDLYEKKNIPQVTNCLFALGR 107
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
31-129 9.47e-31

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: 111.28  E-value: 9.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  31 EQELREWIEGVTGRRIG---NNFMDGLKDGIILCEFINKLQPGSVKKVN-ESTQNWHQLENIGNFIKAITKYGVKPHDIF 106
Cdd:cd00014    1 EEELLKWINEVLGEELPvsiTDLFESLRDGVLLCKLINKLSPGSIPKINkKPKSPFKKRENINLFLNACKKLGLPELDLF 80
                         90       100
                 ....*....|....*....|...
gi 226423897 107 EANDLFENTNHTQVQSTLLALAS 129
Cdd:cd00014   81 EPEDLYEKGNLKKVLGTLWALAL 103
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
31-128 1.58e-29

calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar proteins; The family includes transgelins from Saccharomyces cerevisiae and Schizosaccharomyces pombe, which are also called SCP1 and STG1, respectively. Transgelin, also called calponin homolog 1, has actin-binding and actin-bundling activity. It stabilizes actin filaments against disassembly. Transgelin contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409059 [Multi-domain]  Cd Length: 101  Bit Score: 107.84  E-value: 1.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  31 EQELREWIEGVTGRRIGN-NFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKPHDIFEAN 109
Cdd:cd21210    2 EQEAREWIEEVLGEKLAQgDLLDALKDGVVLCKLANRILPADIRKYKESKMPFVQMENISAFLNAARKLGVPENDLFQTV 81
                         90
                 ....*....|....*....
gi 226423897 110 DLFENTNHTQVQSTLLALA 128
Cdd:cd21210   82 DLFERKNPAQVLQCLHALS 100
SCP1 COG5199
Calponin [Cytoskeleton];
18-188 2.26e-27

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 104.62  E-value: 2.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  18 VKNKLAQKYDHQREQELREWIEGVTGRRIG--NNFMDGLKDGIILCEFINKLQPGSVKkVNESTQNWHQLENIGNFIKAI 95
Cdd:COG5199    2 VNTKNRCPGMDKQQKEVTLWIETVLGEKFEppGDLLSLLKDGVRLCRILNEASPLDIK-YKESKMPFVQMENISSFINGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  96 TKYGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTK--GNKVNVGVKYAEKQERRFE-PEKLREGRNIIGLQMGTNK 172
Cdd:COG5199   81 KKLRVPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQKErmFSGPFLGPHLATKKPRVFSsQEVLDRSKGAIHLQYGYSD 160
                        170
                 ....*....|....*..
gi 226423897 173 FASQQG-MTAYGTRRHL 188
Cdd:COG5199  161 LSEQSTeKGASNVRRDL 177
CH_TAGLN2 cd21280
calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis ...
24-141 3.01e-26

calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis tissue protein Li 7e, or SM22-alpha homolog, acts as an actin-binding protein that induces actin gelation and regulates the actin cytoskeleton. It may participate in the development and progression of multiple cancers. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409129 [Multi-domain]  Cd Length: 137  Bit Score: 100.72  E-value: 3.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  24 QKYDHQREQELREWIEGVTGRRIGN------NFMDGLKDGIILCEFINKLQPGS---VKKVNESTQNWHQLENIGNFIKA 94
Cdd:cd21280    3 KQYDADLEQILIQWITAQCGKQVGRpqpgreNFQNWLKDGTVLCHLINSLYPKGqapVKKIQASTMAFKQMEQISQFLQA 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 226423897  95 ITKYGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTKGNKVNVG 141
Cdd:cd21280   83 AERYGINTTDIFQTVDLWEGKNMASVQRTLMNLGGLAVTRDDGLFVG 129
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
28-133 1.09e-25

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: 98.13  E-value: 1.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897   28 HQREQELREWIEGVTGRRIGN----NFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIK-AITKYGVKP 102
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGvrvtNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDvAEKKLGVPK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 226423897  103 HDIfEANDLFENtNHTQVQSTLLALASMAKT 133
Cdd:pfam00307  81 VLI-EPEDLVEG-DNKSVLTYLASLFRRFQA 109
CH_TAGLN-like cd21209
calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family ...
27-134 4.34e-25

calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family includes transgelin, transgelin-2 and transgelin-3. Transgelin, also called 22 kDa actin-binding protein, protein WS3-10, or smooth muscle protein 22-alpha (SM22-alpha), acts as an actin cross-linking/gelling protein that may be involved in calcium interactions and in regulating contractile properties of the cell. Transgelin-2, also called epididymis tissue protein Li 7e, or SM22-alpha homolog, acts as an actin-binding protein that induces actin gelation and regulates actin cytoskeleton. It may participate in the development and progression of multiple cancers. Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409058 [Multi-domain]  Cd Length: 119  Bit Score: 96.81  E-value: 4.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  27 DHQREQELREWIEGVTGRRIGN------NFMDGLKDGIILCEFINKLQP---GSVKKVNESTQNWHQLENIGNFIKAITK 97
Cdd:cd21209    1 DPELESRLVEWIVAQCGSDVGRpdpgrlGFQKWLKDGTVLCKLINSLYPegsKPVKKIQSSKMAFKQMEQISQFLKAAED 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 226423897  98 YGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTK 134
Cdd:cd21209   81 YGVRTTDIFQTVDLWEGKDMAAVQRTLMALGSLAVTK 117
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
31-116 3.22e-22

calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This family includes LIM domain only protein 7 (LMO-7) and LIM and calponin homology domains-containing protein 1 (LIMCH1), and similar proteins. LMO-7, also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. LIMCH1 acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409057 [Multi-domain]  Cd Length: 119  Bit Score: 89.32  E-value: 3.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  31 EQELREWIEGVTGRRIGN-NFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKPHDIFEAN 109
Cdd:cd21208    2 LKEARTWIEAVTGKKFPSdDFRESLEDGILLCELINAIKPGSIKKINRLPTPIAGLDNLNLFLKACEDLGLKDSQLFDPT 81

                 ....*..
gi 226423897 110 DLFENTN 116
Cdd:cd21208   82 DLQDLSN 88
CH_TAGLN3 cd21281
calponin homology (CH) domain found in transgelin-3; Transgelin-3, also called neuronal ...
27-134 1.28e-21

calponin homology (CH) domain found in transgelin-3; Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409130 [Multi-domain]  Cd Length: 119  Bit Score: 87.71  E-value: 1.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  27 DHQREQELREWIEGVTGRRIGN------NFMDGLKDGIILCEFINKLQPGS---VKKVNESTQNWHQLENIGNFIKAITK 97
Cdd:cd21281    1 DPDLESRLVDWIIIQCGGDIERpqpgrqNFQKWLMDGTILCRLINSLYPPGkepIKKISETKMAFKQMEKISQFLQAAEA 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 226423897  98 YGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTK 134
Cdd:cd21281   81 YGVITTDIFQTVDLWEGKDMAAVQRTLMALGSVAVTK 117
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
33-127 1.70e-20

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: 84.29  E-value: 1.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897    33 ELREWIEGVTGRRIG---NNFMDGLKDGIILCEFINKLQPGSV--KKVNESTQNWHQLENIGNFIKAITKYGVKPhDIFE 107
Cdd:smart00033   2 TLLRWVNSLLAEYDKppvTNFSSDLKDGVALCALLNSLSPGLVdkKKVAASLSRFKKIENINLALSFAEKLGGKV-VLFE 80
                           90       100
                   ....*....|....*....|.
gi 226423897   108 ANDLFENTNHT-QVQSTLLAL 127
Cdd:smart00033  81 PEDLVEGPKLIlGVIWTLISL 101
CH_TAGLN cd21279
calponin homology (CH) domain found in transgelin; Transgelin, also called 22 kDa ...
27-136 2.26e-18

calponin homology (CH) domain found in transgelin; Transgelin, also called 22 kDa actin-binding protein, protein WS3-10, or smooth muscle protein 22-alpha (SM22-alpha), acts as an actin cross-linking/gelling protein that may be involved in calcium interactions and in regulating contractile properties of the cell. It may also contribute to replicative senescence. Transgelin contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409128 [Multi-domain]  Cd Length: 121  Bit Score: 79.28  E-value: 2.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  27 DHQREQELREWIEGVTGRRIGN------NFMDGLKDGIILCEFINKLQPGSVKKV----NESTQNWHQLENIGNFIKAIT 96
Cdd:cd21279    1 DEELEERLVEWIVVQCGPDVGRpdrgrlGFQVWLKNGVVLSKLVNSLYPDGSKPVkipdNPPSMVFKQMEQVAQFLKAAE 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 226423897  97 KYGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTKGN 136
Cdd:cd21279   81 DYGVVKTDMFQTVDLYEGKDMAAVQRTLVALGSLAVTKND 120
CH_LIMCH1 cd21278
calponin homology (CH) domain found in LIM and calponin homology domains-containing protein 1; ...
32-123 9.61e-17

calponin homology (CH) domain found in LIM and calponin homology domains-containing protein 1; LIM and calponin homology domains-containing protein 1 (LIMCH1) acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. LIMCH1 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409127 [Multi-domain]  Cd Length: 118  Bit Score: 74.52  E-value: 9.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  32 QELREWIEGVTGRRIGN-NFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKPHDIFEAND 110
Cdd:cd21278    3 TEAQKWIEQVTGRSFGDkDFRSGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNITLFLRGCKELGLKESQLFDPGD 82
                         90
                 ....*....|...
gi 226423897 111 LFENTNHTQVQST 123
Cdd:cd21278   83 LQDTSNRVTIKSS 95
CH_LMO7 cd21277
calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 ...
33-121 5.14e-16

calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 (LMO-7), also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. It contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409126 [Multi-domain]  Cd Length: 116  Bit Score: 72.56  E-value: 5.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  33 ELREWIEGVTGRRIGN-NFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKPHDIFEANDL 111
Cdd:cd21277    4 EAQRWIEAVTGKNFGNkDFRSALENGVLLCDLINKIKPGIIKKINRLSTPIAGLDNINVFLKACEKLGLKEAQLFHPGDL 83
                         90
                 ....*....|
gi 226423897 112 FENTNHTQVQ 121
Cdd:cd21277   84 QDLSTRVTVK 93
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
30-129 3.42e-15

calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. This family includes a group of kinesin-like proteins belonging to KIN-14 protein family. They all contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409052 [Multi-domain]  Cd Length: 112  Bit Score: 70.14  E-value: 3.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  30 REQELREWIEGVTGRRIG-----NNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQ--------LENIGNFIKAIT 96
Cdd:cd21203    1 RRYEAAEWIQNVLGVLVLpdpseEEFRLCLRDGVVLCKLLNKLQPGAVPKVVESPDDPDGaagsafqyFENVRNFLVAIE 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 226423897  97 KYGVKphdIFEANDL--FENTNHTQVQSTLLALAS 129
Cdd:cd21203   81 EMGLP---TFEASDLeqGGGGSRPRVVDCILALKS 112
CH_PIX cd21202
calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak ...
52-131 7.52e-14

calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak Interactive eXchange factor (PIX) proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX family, alpha-PIX and beta-PIX. Alpha-PIX, also called Rho guanine nucleotide exchange factor 6 (ARHGEF6), is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX, also called Rho guanine nucleotide exchange factor 7 (ARHGEF7), plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. Both alpha-PIX and beta-PIX contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409051 [Multi-domain]  Cd Length: 114  Bit Score: 66.79  E-value: 7.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  52 DGLKDGIILCEFINKLQPGSVKKV-NESTQNWHQLENIGNFIKAITKYGVKPHDIFEANDLFENTNHTQVQSTLLALASM 130
Cdd:cd21202   32 ESLKNGVVLCRLVNRLKPGTVEKIyDEPTTEEECLYNFESFLKACQELGILAEEIFDPNDLYSGGNFQKVLSTLERLEKV 111

                 .
gi 226423897 131 A 131
Cdd:cd21202  112 A 112
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
30-135 3.58e-13

calponin homology (CH) domain found in the IQ motif containing GTPase activating protein family; Members of the IQ motif containing GTPase activating protein (IQGAP) family are associated with the Ras GTP-binding protein and act as essential regulators of cytoskeletal function. There are three known IQGAP family members: IQGAP1, IQGAP2, and IQGAP3. They are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity. It lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3 regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton.


Pssm-ID: 409055 [Multi-domain]  Cd Length: 118  Bit Score: 64.94  E-value: 3.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  30 REQELREWIEGVTGRRIGN--NFMDGLKDGIILCEFINKLQPGSV--KKVNESTQNWHQLENIGNFIKAITKYGVKPHDI 105
Cdd:cd21206    9 RLEEAKQWIEACLNEELPPttEFEEELRNGVVLAKLANKFAPKLVplKKIYDVGLQFRHTDNINHFLRALKKIGLPKIFH 88
                         90       100       110
                 ....*....|....*....|....*....|
gi 226423897 106 FEANDLFENTNHTQVQSTLLALASMAKTKG 135
Cdd:cd21206   89 FETTDLYEKKNIPKVIYCLHALSLLLFKLG 118
CH_alphaPIX cd21265
calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak ...
54-127 1.66e-12

calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak Interactive eXchange factor (alpha-PIX), also called PAK-interacting exchange factor alpha, Rho guanine nucleotide exchange factor 6 (ARHGEF6), Rac/Cdc42 guanine nucleotide exchange factor 6, or Cool (Cloned out of Library)-2, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac1, and is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Alpha-PIX contains a single copy of the CH domain at its N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409114  Cd Length: 117  Bit Score: 62.92  E-value: 1.66e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226423897  54 LKDGIILCEFINKLQPGSVKKVNESTQNWHQ-LENIGNFIKAITKYGVkphDIFEANDLFENTNHTQVQSTLLAL 127
Cdd:cd21265   35 LKDGVVLCKLIERLLPGSVEKYCLEPKTEADcIGNIKEFLKGCAALKV---ETFEPDDLYTGENFSKVLSTLLAV 106
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
54-124 1.96e-11

calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV proteins.


Pssm-ID: 409050  Cd Length: 117  Bit Score: 59.96  E-value: 1.96e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226423897  54 LKDGIILCEFINKLQPGSV--KKVNESTQNwHQ---LENIGNFIKAI-TKYGVKPHDIFEANDLFENTNHTQVQSTL 124
Cdd:cd21201   36 LRDGVLLCQLLNRLSPGSVddREINLRPQM-SQflcLKNIRTFLQACrTVFGLRSADLFEPEDLYDVTNFGKVIRTL 111
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
7-135 3.08e-11

Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 63.75  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897    7 NRGPAYGLSAEVKNKLAQK-------YDHQ-REQELREWIEGVTGRRIG-NNFMDGLKDGIILCEFINKLQPGSVKKV-N 76
Cdd:COG5261    14 NLGRPIGTPSHLKTKTSAKnrsalraYEYLcRVSEAKIWIEEVIEEALPeLCFEDSLRNGVFLAKLTQRFNPDLTTVIfP 93
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 226423897   77 ESTQNWHQLENIGNFIKAITKYGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTKG 135
Cdd:COG5261    94 ADKLQFRHTDNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPG 152
CH_betaPIX cd21266
calponin homology (CH) domain found in beta-Pak Interactive eXchange factor; Beta-Pak ...
54-127 4.21e-11

calponin homology (CH) domain found in beta-Pak Interactive eXchange factor; Beta-Pak Interactive eXchange factor (beta-PIX), also called PAK-interacting exchange factor beta, Rho guanine nucleotide exchange factor 7 (ARHGEF7), p85, or Cool (Cloned out of Library)-1, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac1, and plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. Beta-PIX contains a single copy of the CH domain at its N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409115  Cd Length: 112  Bit Score: 59.16  E-value: 4.21e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226423897  54 LKDGIILCEFINKLQPGSVKKV-NESTQNWHQLENIGNFIKAITKYGVkphDIFEANDLFENTNHTQVQSTLLAL 127
Cdd:cd21266   33 LKDGVVLCRLLERLLPGSIDKVyPEPRTESECLSNIREFLRGCGALRL---ETFDANDLYQGQNFNKVLSSLVAL 104
Calponin pfam00402
Calponin family repeat;
164-188 1.00e-10

Calponin family repeat;


Pssm-ID: 459803  Cd Length: 25  Bit Score: 55.60  E-value: 1.00e-10
                          10        20
                  ....*....|....*....|....*
gi 226423897  164 IGLQMGTNKFASQQGMTAYGTRRHL 188
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25
CH_GAS2-like cd21204
calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth ...
32-135 1.01e-10

calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth arrest-specific protein 2 (GAS-2) family includes GAS-2, and GAS-2 like proteins, GAS2L1-3. GAS-2 may play a role in apoptosis by acting as a cell death substrate for caspases. GAS2L1 (also called GAS2-related protein on chromosome 22 or growth arrest-specific protein 2-like 1) and GAS2L2 (also called GAS2-related protein on chromosome 17 or growth arrest-specific protein 2-like 2) may be involved in the cross-linking of microtubules and microfilaments. GAS2L3, also called GAS2-like protein 3, is a cytoskeletal linker protein that may promote and stabilize the formation of the actin and microtubule network. Members of this family contain a single copy of the CH domain at the N-terminal region. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409053  Cd Length: 131  Bit Score: 58.43  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  32 QELREWIEGVTGRRI-GNNFMDGLKDGIILCEFINKLQPGSVK----------------KVNESTQ--NWHQLENIGNFI 92
Cdd:cd21204    9 EDLAEWLNDLLGDDLtPDNFLDELRNGVVLCQLAQKIQEAAEKareagkkngpppsyklKCNENAKpgSFFARDNVANFL 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 226423897  93 KAITKYGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTKG 135
Cdd:cd21204   89 RWCRKLGVDEVLLFESEDLVLHKNPRQVLLCLLELARIAARYG 131
Calponin pfam00402
Calponin family repeat;
204-228 3.63e-10

Calponin family repeat;


Pssm-ID: 459803  Cd Length: 25  Bit Score: 54.06  E-value: 3.63e-10
                          10        20
                  ....*....|....*....|....*
gi 226423897  204 ISLQMGTNKGASQAGMTAPGTKRQI 228
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25
CH_LRCH cd21205
calponin homology (CH) domain found in the leucine-rich repeat and calponin homology ...
32-127 6.85e-10

calponin homology (CH) domain found in the leucine-rich repeat and calponin homology domain-containing protein family; The leucine-rich repeat and calponin homology domain-containing protein (LRCH) family includes LRCH1-4. LRCH1, also called calponin homology domain-containing protein 1, or neuronal protein 81 (NP81), acts as a negative regulator of GTPase Cdc42 by sequestering Cdc42-guanine exchange factor DOCK8. LRCH2 may play a role in the organization of the cytoskeleton. LRCH3 is part of the DISP complex and may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. LRCH4, also called leucine-rich repeat neuronal protein 4, or leucine-rich neuronal protein, acts as a novel Toll-like receptor (TLR) accessory protein that regulates the innate immune response. Members of this family contain a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409054 [Multi-domain]  Cd Length: 107  Bit Score: 55.38  E-value: 6.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  32 QELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKK-------VNESTQNwHQLENIGNFIKAITKYGVKPHD 104
Cdd:cd21205    4 EQLRKSIESRLKVTLPDDLGEALMDGVVLCHLANHVRPRSVPSihvpspaVPKLSMA-KCRRNVENFLEACRKLGVPEER 82
                         90       100
                 ....*....|....*....|...
gi 226423897 105 IFEANDLFENTNHTQVQSTLLAL 127
Cdd:cd21205   83 LCSPGDILEEKGLVRVAVTVQAL 105
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
47-109 1.83e-09

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 54.50  E-value: 1.83e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226423897  47 GNNFMDGLKDGIILCEFINKLQPGSV--KKVNESTQN--WHQLENIGNFIKAITKYGVK-----PHDIFEAN 109
Cdd:cd21217   30 GDDLFEALRDGVLLCKLINKIVPGTIdeRKLNKKKPKniFEATENLNLALNAAKKIGCKvvnigPQDILDGN 101
CH_VAV1 cd21262
calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the ...
54-128 9.35e-09

calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV1 protein.


Pssm-ID: 409111  Cd Length: 120  Bit Score: 52.64  E-value: 9.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  54 LKDGIILCEFINKLQPGSV--KKVNESTQ--NWHQLENIGNFIKAIT-KYGVKPHDIFEANDLFENTNHTQVQSTLLALA 128
Cdd:cd21262   36 LRDGVLLCQLLNNLLPHAVnlREINLRPQmsQFLCLKNIRTFLSTCCeKFGLRKSELFEAFDLFDVRDFGKVIDTLSILS 115
Calponin pfam00402
Calponin family repeat;
243-267 1.93e-08

Calponin family repeat;


Pssm-ID: 459803  Cd Length: 25  Bit Score: 49.06  E-value: 1.93e-08
                          10        20
                  ....*....|....*....|....*
gi 226423897  243 VSLQMGSNKGASQRGMTVYGLPRQV 267
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25
CH_VAV3 cd21264
calponin homology (CH) domain found in VAV3 protein and similar proteins; VAV3 is ubiquitously ...
54-128 2.92e-08

calponin homology (CH) domain found in VAV3 protein and similar proteins; VAV3 is ubiquitously expressed and functions as a phosphorylation-dependent guanine nucleotide exchange factor (GEF) for RhoA, RhoG, and Rac1. Its function has been implicated in the hematopoietic, bone, cerebellar, and cardiovascular systems. VAV3 is essential in axon guidance in neurons that control blood pressure and respiration. It is overexpressed in prostate cancer cells and it plays a role in regulating androgen receptor transcriptional activity. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The model corresponds to CH domain, an actin-binding domain which is present as a single copy in VAV3 protein.


Pssm-ID: 409113  Cd Length: 117  Bit Score: 51.12  E-value: 2.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  54 LKDGIILCEFINKLQPGSV--KKVNESTQ--NWHQLENIGNFIKAITK-YGVKPHDIFEANDLFENTNHTQVQSTLLALA 128
Cdd:cd21264   36 LRDGVLLCQLLNNLRPHSInlKEINLRPQmsQFLCLKNIRTFLSACCEtFGMRKSELFEAFDLFDVRDFGKVIETLSKLS 115
CH_VAV2 cd21263
calponin homology (CH) domain found in VAV2 protein and similar proteins; VAV2 is widely ...
49-128 1.34e-05

calponin homology (CH) domain found in VAV2 protein and similar proteins; VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others. It has been reported to associate with Nek3. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The model corresponds to CH domain, an actin-binding domain which is present as a single copy in VAV2 protein.


Pssm-ID: 409112  Cd Length: 119  Bit Score: 43.79  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  49 NFMDGLKDGIILCEFINKLQPGSV--KKVNESTQ--NWHQLENIGNFIKAI-TKYGVKPHDIFEANDLFENTNHTQVQST 123
Cdd:cd21263   31 DLAQALRDGVLLCQLLHNLSPGSIdlKDINFRPQmsQFLCLKNIRTFLKVChDKFGLRNSELFDPFDLFDVRDFGKVISA 110

                 ....*
gi 226423897 124 LLALA 128
Cdd:cd21263  111 LSRLS 115
CH_LRCH4 cd21273
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
33-127 1.62e-05

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 4; Leucine-rich repeat and calponin homology domain-containing protein 4 (LRCH4), also called leucine-rich repeat neuronal protein 4, or leucine-rich neuronal protein, acts as a novel Toll-like receptor (TLR) accessory protein that regulates the innate immune response. LRCH4 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409122  Cd Length: 109  Bit Score: 43.35  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  33 ELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKVN------ESTQNWHQLENIGNFIKAITKYGVKPHDIF 106
Cdd:cd21273    8 QLRKTLESRLKVTLPEDLAEALSNGAVLCQLANQLRPRSVSIIHvpspavPKLSKAKCRKNVENFIEACRKMGVPEVDLC 87
                         90       100
                 ....*....|....*....|.
gi 226423897 107 EANDLFeNTNHTQVQSTLLAL 127
Cdd:cd21273   88 SPSDVL-LQGPAAVLRTVLAL 107
CH_LRCH3 cd21272
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
32-131 1.54e-04

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 3; Leucine-rich repeat and calponin homology domain-containing protein 3 (LRCH3) is part of the DISP (DOCK7-Induced Septin disPlacement) complex. It may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. LRCH3 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409121  Cd Length: 109  Bit Score: 40.36  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  32 QELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQL------ENIGNFIKAITKYGVKPHDI 105
Cdd:cd21272    4 EQLRKNIESRLKVSLPSDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLtmakcrRNVENFLEACRRIGVPQEQL 83
                         90       100
                 ....*....|....*....|....*.
gi 226423897 106 FEANDLFENTNHTQVQSTLLALASMA 131
Cdd:cd21272   84 CLPLHILEEKGLSQVAVTVQALLELA 109
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
53-109 5.85e-04

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409076  Cd Length: 109  Bit Score: 38.81  E-value: 5.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226423897  53 GLKDGIILCEFINKLQPGSVKKVNESTQNWHQ-LENIGNFIKAITKYGVK-----PHDIFEAN 109
Cdd:cd21227   30 DLEDGVKLIALVEILQGRKLGRVIKKPLNQHQkLENVTLALKAMAEDGIKlvnigNEDIVNGN 92
CH_LRCH1 cd21270
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
32-130 6.85e-04

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 1; Leucine-rich repeat and calponin homology domain-containing protein 1 (LRCH1), also called calponin homology domain-containing protein 1, or neuronal protein 81 (NP81), acts as a negative regulator of GTPase CDC42 by sequestering CDC42-guanine exchange factor DOCK8. LRCH1 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409119  Cd Length: 112  Bit Score: 38.68  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  32 QELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQL------ENIGNFIKAITKYGVKPHDI 105
Cdd:cd21270    7 EQLRENIETRLKVSLPEDLGAALMDGVVLCHLVNHVRPRSVASIHVPSPAVPKLsmakcrRNVENFLEACRKIGVPEADL 86
                         90       100
                 ....*....|....*....|....*
gi 226423897 106 FEANDLFEnTNHTQVQSTLLALASM 130
Cdd:cd21270   87 CSPYDILQ-LNLRGIRKTVETLLAL 110
CH_LRCH2 cd21271
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
29-111 8.30e-04

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 2; Leucine-rich repeat and calponin homology domain-containing protein 2 (LRCH2) may play a role in the organization of the cytoskeleton. It contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409120  Cd Length: 111  Bit Score: 38.37  E-value: 8.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  29 QREQ--ELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQL------ENIGNFIKAITKYGV 100
Cdd:cd21271    3 ELELieQLRENIESRLKVILPEDLGAALMDGVVLCHLANHIRPRSVGSIHVPSPAVPKLsmakcrRNVENFLDACRKLGV 82
                         90
                 ....*....|....*..
gi 226423897 101 K------PHDIFEANDL 111
Cdd:cd21271   83 PedklclPHHILEEKGL 99
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
29-76 8.30e-04

third 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. 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, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that 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 an actin-bundling protein 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, which 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 third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409068  Cd Length: 113  Bit Score: 38.42  E-value: 8.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 226423897  29 QREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSV--KKVN 76
Cdd:cd21219    4 REERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVnwKKVN 53
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
26-78 1.13e-03

third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; 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 third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409149  Cd Length: 119  Bit Score: 38.17  E-value: 1.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 226423897  26 YDHQREQELRE---WIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSV--KKVNES 78
Cdd:cd21300    1 FDAEGEREARVftlWLNSLDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVnwKKVNKA 58
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
27-109 1.75e-03

third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which 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. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409148  Cd Length: 114  Bit Score: 37.48  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  27 DHQREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSV--KKVN--------ESTQNWHQLENIGNFIKaIT 96
Cdd:cd21299    2 TSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVnwKHANkppikmpfKKVENCNQVVKIGKQLK-FS 80
                         90
                 ....*....|...
gi 226423897  97 KYGVKPHDIFEAN 109
Cdd:cd21299   81 LVNVAGNDIVQGN 93
CH_GAS2L3 cd21269
calponin homology (CH) domain found in growth arrest-specific protein 2-like 3; Growth ...
31-125 3.93e-03

calponin homology (CH) domain found in growth arrest-specific protein 2-like 3; Growth arrest-specific protein 2-like 3 (GAS2L3), also called GAS2-like protein 3, is a cytoskeletal linker protein that may promote and stabilize the formation of the actin and microtubule network. It contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409118  Cd Length: 130  Bit Score: 36.74  E-value: 3.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423897  31 EQELREWIEGVTGRRI-GNNFMDGLKDGIILCEFINKLQ-------------PGSVKKV----NESTQNWHQLENIGNFI 92
Cdd:cd21269    8 QEDLSIWLSGMLGKEVkAERFMEELDNGVLLCQLIGVLQskikeccsteelkHFPMRKVpckkDAPSGSFFARDNTANFL 87
                         90       100       110
                 ....*....|....*....|....*....|...
gi 226423897  93 KAITKYGVKPHDIFEANDLFENTNHTQVQSTLL 125
Cdd:cd21269   88 SWCRAIGVDETYLFESEGLVLHKDPRQVCLCLL 120
 
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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