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Conserved domains on  [gi|15236837|ref|NP_194400|]
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fimbrin 1 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
390-503 3.10e-80

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: 250.11  E-value: 3.10e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 390 ETCRDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMPFRKVENCNQVIKIGKQLKFS 469
Cdd:cd21299   1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFS 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 15236837 470 LVNVAGNDIVQGNKKLILGLLWQLMRFHMLQLLK 503
Cdd:cd21299  81 LVNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
124-239 1.41e-79

first 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, and are probably involved in the 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409142  Cd Length: 116  Bit Score: 248.60  E-value: 1.41e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 124 SEKGPFVQHINRYLGDDPFLKQFLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLN 203
Cdd:cd21293   1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15236837 204 SAKAVGCSVVNIGTQDLAEGRPHLVLGLISQLIKIQ 239
Cdd:cd21293  81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
513-621 2.47e-73

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


:

Pssm-ID: 409151  Cd Length: 109  Bit Score: 232.06  E-value: 2.47e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 513 EMTDADILSWANRKVRTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNATYIVSVARKLGC 592
Cdd:cd21302   1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80
                        90       100
                ....*....|....*....|....*....
gi 15236837 593 SVFLLPEDIVEVNQKMILILTASIMYWSL 621
Cdd:cd21302  81 SIFLLPEDIVEVNQKMILILTASIMYWSL 109
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
260-368 2.76e-69

second 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, and are probably involved in the 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409145  Cd Length: 109  Bit Score: 221.24  E-value: 2.76e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 260 DDVEELLRLPPEKVLLKWMNFHLKKGGYKKTVSNFSADLKDAQAYAFLLNVLAPEHCDPATLDAKDPLERAELVLSHAER 339
Cdd:cd21296   1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKTVTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEK 80
                        90       100
                ....*....|....*....|....*....
gi 15236837 340 MNCKRYLTAEEIVEGSSTLNLAFVAQIFH 368
Cdd:cd21296  81 MNCKRYLTAKDIVEGSANLNLAFVAQIFH 109
EF-hand_7 pfam13499
EF-hand domain pair;
34-89 3.46e-04

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.16  E-value: 3.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15236837    34 KNQNGKVTIEDLPPLFAKLkALSATFKEDEIKGMLGELGSDTSTDVSFEEFLKIYL 89
Cdd:pfam13499  13 SDGDGYLDVEELKKLLRKL-EEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
390-503 3.10e-80

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: 250.11  E-value: 3.10e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 390 ETCRDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMPFRKVENCNQVIKIGKQLKFS 469
Cdd:cd21299   1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFS 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 15236837 470 LVNVAGNDIVQGNKKLILGLLWQLMRFHMLQLLK 503
Cdd:cd21299  81 LVNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
124-239 1.41e-79

first 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, and are probably involved in the 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409142  Cd Length: 116  Bit Score: 248.60  E-value: 1.41e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 124 SEKGPFVQHINRYLGDDPFLKQFLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLN 203
Cdd:cd21293   1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15236837 204 SAKAVGCSVVNIGTQDLAEGRPHLVLGLISQLIKIQ 239
Cdd:cd21293  81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
513-621 2.47e-73

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


Pssm-ID: 409151  Cd Length: 109  Bit Score: 232.06  E-value: 2.47e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 513 EMTDADILSWANRKVRTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNATYIVSVARKLGC 592
Cdd:cd21302   1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80
                        90       100
                ....*....|....*....|....*....
gi 15236837 593 SVFLLPEDIVEVNQKMILILTASIMYWSL 621
Cdd:cd21302  81 SIFLLPEDIVEVNQKMILILTASIMYWSL 109
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
62-617 2.95e-72

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 245.62  E-value: 2.95e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837  62 DEIKGMLGELGSDTSTDVSFEEFLKIYLNLLSKAAEKSGGHHKNSSSFLKACTTTLLHTIyqSEKGPFVQHINRYLGDDP 141
Cdd:COG5069  59 NETPETRIHVMENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATI--NEEGELTKHINLLLWCDE 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 142 FLKQFLPlDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKR---VLNPWERNENHTLCLNSAKAVG-CSVVNIGT 217
Cdd:COG5069 137 DTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKknkALNNFQAFENANKVIGIARLIGvEDIVNVSI 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 218 QDlaeGRPHLVLgLISQLIKIQVLA--DLNLKKTPQLVELLEDSDDveelLRLPPEKVLLKWMN-FHLKKGGYKktVSNF 294
Cdd:COG5069 216 PD---ERSIMTY-VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEIILLRLLNlIHLKQANWK--VVNF 285
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 295 SADLKDAQAYAFLLNVLApEHCDPATLDAKDPLERAELVLSHAERMNCKRYLTAEeiveGSSTLNLAFVAQIFHERNGLN 374
Cdd:COG5069 286 SKDVSDGENYTDLLNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQE 360
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 375 KDGKYAFAEMMTEDVETCRDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKV-SPSSVNWKHASKPPIK----MP 449
Cdd:COG5069 361 PLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASgieeNR 440
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 450 FRKVENCNQVIKIGKQLKFSLVNVAGNDIVQGNkKLILGLLWQLMRFHMLQLLKSLRSRtlGKEMTDADILSWANRKVRT 529
Cdd:COG5069 441 FKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHVLKKD--GCGLSDSDLCAWLGSLGLK 517
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 530 MGRKLQIESFKDKSLS-SGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNA-TYIVS--VARKLGCSVFLLPEDIVEVN 605
Cdd:COG5069 518 GDKEEGIRSFGDPAGSvSGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSLAISskILRSLGAIIKFLPEDINGVR 597
                       570
                ....*....|...
gi 15236837 606 QKM-ILILTASIM 617
Cdd:COG5069 598 PRLdVLTFIESLM 610
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
260-368 2.76e-69

second 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, and are probably involved in the 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409145  Cd Length: 109  Bit Score: 221.24  E-value: 2.76e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 260 DDVEELLRLPPEKVLLKWMNFHLKKGGYKKTVSNFSADLKDAQAYAFLLNVLAPEHCDPATLDAKDPLERAELVLSHAER 339
Cdd:cd21296   1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKTVTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEK 80
                        90       100
                ....*....|....*....|....*....
gi 15236837 340 MNCKRYLTAEEIVEGSSTLNLAFVAQIFH 368
Cdd:cd21296  81 MNCKRYLTAKDIVEGSANLNLAFVAQIFH 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
268-368 1.53e-22

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: 92.73  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837   268 LPPEKVLLKWMNFHLKKGGYKKTVSNFSADLKDAQAYAFLLNVLAPEHCDPATL--DAKDPLERAELVLSHAER-MNCKR 344
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKkLGVPK 80
                          90       100
                  ....*....|....*....|....*
gi 15236837   345 YL-TAEEIVEGSSTLNLAFVAQIFH 368
Cdd:pfam00307  81 VLiEPEDLVEGDNKSVLTYLASLFR 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
398-496 1.61e-19

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: 83.90  E-value: 1.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837    398 YRLWINSLG---IDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPpiKMPFRKVENCNQVIKIGKQLKFSLVNVA 474
Cdd:smart00033   3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 15236837    475 GNDIVQGnKKLILGLLWQLMRF 496
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
133-237 1.89e-16

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: 75.40  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837   133 INRYLGDDPflkqflpLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKrvlnPWERNENHTLCLNSA-KAVGCS 211
Cdd:pfam00307  11 INSHLAEYG-------PGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLALDVAeKKLGVP 79
                          90       100
                  ....*....|....*....|....*.
gi 15236837   212 VVNIGTQDLAEGRPHLVLGLISQLIK 237
Cdd:pfam00307  80 KVLIEPEDLVEGDNKSVLTYLASLFR 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
399-498 3.45e-16

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: 74.63  E-value: 3.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837   399 RLWINSL----GIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHaskpPIKMPFRKVENCNQVIKIG-KQLKFSLVNV 473
Cdd:pfam00307   8 LRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK----LNKSEFDKLENINLALDVAeKKLGVPKVLI 83
                          90       100
                  ....*....|....*....|....*
gi 15236837   474 AGNDIVQGNKKLILGLLWQLMRFHM 498
Cdd:pfam00307  84 EPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
129-238 4.37e-16

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: 74.27  E-value: 4.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837    129 FVQHINRYLGDDPflkqflplDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKrvLNPWERNENHTLCLNSAKAV 208
Cdd:smart00033   3 LLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKL 72
                           90       100       110
                   ....*....|....*....|....*....|
gi 15236837    209 GCSVVNIGTQDLAEGrPHLVLGLISQLIKI 238
Cdd:smart00033  73 GGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
518-617 1.15e-15

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: 73.09  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837   518 DILSWANRKVRTMGRKLQIESFKdKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDdeKRLNATYIVSVAR-KLGCSVFL 596
Cdd:pfam00307   6 ELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKLNKSEFD--KLENINLALDVAEkKLGVPKVL 82
                          90       100
                  ....*....|....*....|..
gi 15236837   597 L-PEDIVEVNQKMILILTASIM 617
Cdd:pfam00307  83 IePEDLVEGDNKSVLTYLASLF 104
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
272-367 2.10e-14

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: 69.27  E-value: 2.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837    272 KVLLKWMNFHLKKGGyKKTVSNFSADLKDAQAYAFLLNVLAPEHCDPATLDAK----DPLERAELVLSHAERMNCKR-YL 346
Cdd:smart00033   1 KTLLRWVNSLLAEYD-KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVvLF 79
                           90       100
                   ....*....|....*....|.
gi 15236837    347 TAEEIVEGsSTLNLAFVAQIF 367
Cdd:smart00033  80 EPEDLVEG-PKLILGVIWTLI 99
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
518-619 6.94e-14

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: 67.73  E-value: 6.94e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837    518 DILSWANRKvrTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNATYIVSVARKLGCSVFLL 597
Cdd:smart00033   2 TLLRWVNSL--LAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79
                           90       100
                   ....*....|....*....|...
gi 15236837    598 -PEDIVEVNqKMILILTASIMYW 619
Cdd:smart00033  80 ePEDLVEGP-KLILGVIWTLISL 101
EF-hand_7 pfam13499
EF-hand domain pair;
34-89 3.46e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.16  E-value: 3.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15236837    34 KNQNGKVTIEDLPPLFAKLkALSATFKEDEIKGMLGELGSDTSTDVSFEEFLKIYL 89
Cdd:pfam13499  13 SDGDGYLDVEELKKLLRKL-EEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
34-87 1.30e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 37.53  E-value: 1.30e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15236837  34 KNQNGKVTIEDLpplFAKLKALSATFKEDEIKGMLGELGSDTSTDVSFEEFLKI 87
Cdd:cd00051  11 KDGDGTISADEL---KAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
 
Name Accession Description Interval E-value
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
390-503 3.10e-80

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: 250.11  E-value: 3.10e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 390 ETCRDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMPFRKVENCNQVIKIGKQLKFS 469
Cdd:cd21299   1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFS 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 15236837 470 LVNVAGNDIVQGNKKLILGLLWQLMRFHMLQLLK 503
Cdd:cd21299  81 LVNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
124-239 1.41e-79

first 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, and are probably involved in the 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409142  Cd Length: 116  Bit Score: 248.60  E-value: 1.41e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 124 SEKGPFVQHINRYLGDDPFLKQFLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLN 203
Cdd:cd21293   1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15236837 204 SAKAVGCSVVNIGTQDLAEGRPHLVLGLISQLIKIQ 239
Cdd:cd21293  81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
513-621 2.47e-73

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


Pssm-ID: 409151  Cd Length: 109  Bit Score: 232.06  E-value: 2.47e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 513 EMTDADILSWANRKVRTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNATYIVSVARKLGC 592
Cdd:cd21302   1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80
                        90       100
                ....*....|....*....|....*....
gi 15236837 593 SVFLLPEDIVEVNQKMILILTASIMYWSL 621
Cdd:cd21302  81 SIFLLPEDIVEVNQKMILILTASIMYWSL 109
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
62-617 2.95e-72

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 245.62  E-value: 2.95e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837  62 DEIKGMLGELGSDTSTDVSFEEFLKIYLNLLSKAAEKSGGHHKNSSSFLKACTTTLLHTIyqSEKGPFVQHINRYLGDDP 141
Cdd:COG5069  59 NETPETRIHVMENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATI--NEEGELTKHINLLLWCDE 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 142 FLKQFLPlDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKR---VLNPWERNENHTLCLNSAKAVG-CSVVNIGT 217
Cdd:COG5069 137 DTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKknkALNNFQAFENANKVIGIARLIGvEDIVNVSI 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 218 QDlaeGRPHLVLgLISQLIKIQVLA--DLNLKKTPQLVELLEDSDDveelLRLPPEKVLLKWMN-FHLKKGGYKktVSNF 294
Cdd:COG5069 216 PD---ERSIMTY-VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEIILLRLLNlIHLKQANWK--VVNF 285
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 295 SADLKDAQAYAFLLNVLApEHCDPATLDAKDPLERAELVLSHAERMNCKRYLTAEeiveGSSTLNLAFVAQIFHERNGLN 374
Cdd:COG5069 286 SKDVSDGENYTDLLNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQE 360
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 375 KDGKYAFAEMMTEDVETCRDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKV-SPSSVNWKHASKPPIK----MP 449
Cdd:COG5069 361 PLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASgieeNR 440
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 450 FRKVENCNQVIKIGKQLKFSLVNVAGNDIVQGNkKLILGLLWQLMRFHMLQLLKSLRSRtlGKEMTDADILSWANRKVRT 529
Cdd:COG5069 441 FKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHVLKKD--GCGLSDSDLCAWLGSLGLK 517
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 530 MGRKLQIESFKDKSLS-SGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNA-TYIVS--VARKLGCSVFLLPEDIVEVN 605
Cdd:COG5069 518 GDKEEGIRSFGDPAGSvSGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSLAISskILRSLGAIIKFLPEDINGVR 597
                       570
                ....*....|...
gi 15236837 606 QKM-ILILTASIM 617
Cdd:COG5069 598 PRLdVLTFIESLM 610
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
260-368 2.76e-69

second 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, and are probably involved in the 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409145  Cd Length: 109  Bit Score: 221.24  E-value: 2.76e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 260 DDVEELLRLPPEKVLLKWMNFHLKKGGYKKTVSNFSADLKDAQAYAFLLNVLAPEHCDPATLDAKDPLERAELVLSHAER 339
Cdd:cd21296   1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKTVTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEK 80
                        90       100
                ....*....|....*....|....*....
gi 15236837 340 MNCKRYLTAEEIVEGSSTLNLAFVAQIFH 368
Cdd:cd21296  81 MNCKRYLTAKDIVEGSANLNLAFVAQIFH 109
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
390-502 8.64e-61

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: 198.66  E-value: 8.64e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 390 ETCRDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMPFRKVENCNQVIKIGKQLKFS 469
Cdd:cd21219   1 EGSREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKPLNKFKKVENCNYAVDLAKKLGFS 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 15236837 470 LVNVAGNDIVQGNKKLILGLLWQLMRFHMLQLL 502
Cdd:cd21219  81 LVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
124-237 2.95e-55

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: 183.93  E-value: 2.95e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 124 SEKGPFVQHINRYLGDDPFLKQFLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLN 203
Cdd:cd21217   1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKNIFEATENLNLALN 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 15236837 204 SAKAVGCSVVNIGTQDLAEGRPHLVLGLISQLIK 237
Cdd:cd21217  81 AAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
119-246 1.14e-54

first calponin homology (CH) domain found in the plastin family; The plastin family includes 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. 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: 409141  Cd Length: 145  Bit Score: 183.64  E-value: 1.14e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 119 HTIYQSEKGPFVQHINRYLGDDPFLKQFLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRvLNPWERNENH 198
Cdd:cd21292  19 HSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDERAINKKK-LTVFTIHENL 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15236837 199 TLCLNSAKAVGCSVVNIGTQDLAEGRPHLVLGLISQLIKIQVLADLNL 246
Cdd:cd21292  98 TLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
514-618 1.16e-53

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


Pssm-ID: 409069  Cd Length: 105  Bit Score: 179.39  E-value: 1.16e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 514 MTDADILSWANRKVRTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNATYIVSVARKLGCS 593
Cdd:cd21220   1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLVTEGETDEEKEQNAKYAISLARKIGAV 80
                        90       100
                ....*....|....*....|....*
gi 15236837 594 VFLLPEDIVEVNQKMILILTASIMY 618
Cdd:cd21220  81 IFLLWEDIVEVKPKMILTFVASLMA 105
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
119-246 1.47e-44

first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains 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: 409172  Cd Length: 145  Bit Score: 156.36  E-value: 1.47e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 119 HTIYQSEKGPFVQHINRYLGDDPFLKQFLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRvLNPWERNENH 198
Cdd:cd21323  19 HSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDERAINKKK-LTPFTISENL 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15236837 199 TLCLNSAKAVGCSVVNIGTQDLAEGRPHLVLGLISQLIKIQVLADLNL 246
Cdd:cd21323  98 NLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
390-502 6.99e-44

third calponin homology (CH) domain found in the plastin family; The plastin family includes 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. 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: 409147  Cd Length: 117  Bit Score: 153.16  E-value: 6.99e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 390 ETcRDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMP--FRKVENCNQVIKIGKQLK 467
Cdd:cd21298   4 ET-REEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGanMKKIENCNYAVELGKKLK 82
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15236837 468 FSLVNVAGNDIVQGNKKLILGLLWQLMRFHMLQLL 502
Cdd:cd21298  83 FSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLSIL 117
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
387-502 9.19e-43

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: 150.27  E-value: 9.19e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 387 EDVETCRDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPP---IKMPFRKVENCNQVIKIG 463
Cdd:cd21300   1 FDAEGEREARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaEISRFKAVENTNYAVELG 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15236837 464 KQLKFSLVNVAGNDIVQGNKKLILGLLWQLMRFHMLQLL 502
Cdd:cd21300  81 KQLGFSLVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
258-367 1.97e-41

second calponin homology (CH) domain found in the family of plastin; The plastin family includes 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. 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: 409144  Cd Length: 113  Bit Score: 146.27  E-value: 1.97e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 258 DSDDVEELLRLPPEKVLLKWMNFHLKKGGYKKTVSNFSADLKDAQAYAFLLNVLAPEHCDPAT--LDAKDPLERAELVLS 335
Cdd:cd21295   1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRRIKNFSGDIKDSEAYTHLLKQIAPKDAGVDTsaLRESDLLQRAELMLQ 80
                        90       100       110
                ....*....|....*....|....*....|..
gi 15236837 336 HAERMNCKRYLTAEEIVEGSSTLNLAFVAQIF 367
Cdd:cd21295  81 NADKIGCRKFVTPKDVVTGNPKLNLAFVANLF 112
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
260-368 4.51e-40

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: 142.44  E-value: 4.51e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 260 DDVEELLRLPPEKVLLKWMNFHLKKGGY-KKTVSNFSADLKDAQAYAFLLNVLAPEHCDPA----TLDAKDPLERAELVL 334
Cdd:cd21218   1 ETLESLLYLPPEEILLRWVNYHLKKAGPtKKRVTNFSSDLKDGEVYALLLHSLAPELCDKElvleVLSEEDLEKRAEKVL 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 15236837 335 SHAERMNCKRYLTAEEIVEGSSTLNLAFVAQIFH 368
Cdd:cd21218  81 QAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
511-617 1.19e-38

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


Pssm-ID: 409152  Cd Length: 108  Bit Score: 138.33  E-value: 1.19e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 511 GKEMTDADILSWANRKVRTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNATYIVSVARKL 590
Cdd:cd21303   1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLVTPGNTEDEAYLNAKLAISIARKL 80
                        90       100
                ....*....|....*....|....*..
gi 15236837 591 GCSVFLLPEDIVEVNQKMILILTASIM 617
Cdd:cd21303  81 GALIFLVPEDIVEVRPRLVLTFIGSLM 107
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
119-248 2.13e-38

first calponin homology (CH) domain found in plastin-3; 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. Plastin- 3 contains 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: 409174  Cd Length: 148  Bit Score: 139.42  E-value: 2.13e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 119 HTIYQSEKGPFVQHINRYLGDDPFLKQFLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRvLNPWERNENH 198
Cdd:cd21325  19 HSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKK-LTPFIIQENL 97
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15236837 199 TLCLNSAKAVGCSVVNIGTQDLAEGRPHLVLGLISQLIKIQVLADLNLKK 248
Cdd:cd21325  98 NLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSR 147
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
119-237 5.28e-38

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 137.19  E-value: 5.28e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 119 HTIYQSEKGPFVQHINRYLGDDPFLKQFLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTK----RVLNPWER 194
Cdd:cd21294   1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPprknKPLNNFQM 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15236837 195 NENHTLCLNSAKAVGCSVVNIGTQDLAEGRPHLVLGLISQLIK 237
Cdd:cd21294  81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIR 123
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
118-246 1.00e-37

first calponin homology (CH) domain found in plastin-2; 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-2 contains 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: 409173  Cd Length: 145  Bit Score: 137.45  E-value: 1.00e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 118 LHTIYQSEKGPFVQHINRYLGDDPFLKQFLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRvLNPWERNEN 197
Cdd:cd21324  18 QHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKK-LTPFTIQEN 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15236837 198 HTLCLNSAKAVGCSVVNIGTQDLAEGRPHLVLGLISQLIKIQVLADLNL 246
Cdd:cd21324  97 LNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
262-368 7.05e-37

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


Pssm-ID: 409146  Cd Length: 109  Bit Score: 133.46  E-value: 7.05e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 262 VEELLRLPPEKVLLKWMNFHLKKGGYKKTVSNFSADLKDAQAYAFLLNVLAPEHCDPATLDAKDPLERAELVLSHAERMN 341
Cdd:cd21297   3 LEQFLRLPPEQILLRWFNYHLKAANWPRRVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDLLQRAEQVLQNAEKLD 82
                        90       100
                ....*....|....*....|....*..
gi 15236837 342 CKRYLTAEEIVEGSSTLNLAFVAQIFH 368
Cdd:cd21297  83 CRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
515-617 5.17e-36

fourth calponin homology (CH) domain found in the plastin family; The plastin family includes 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. Members of this family contain four copies of the CH domain. This model corresponds to the fourth CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409150  Cd Length: 107  Bit Score: 130.86  E-value: 5.17e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 515 TDADILSWANRKVRTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNATYIVSVARKLGCSV 594
Cdd:cd21301   2 SDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLVLEGNSEEDKLSNAKYAISMARKIGARV 81
                        90       100
                ....*....|....*....|...
gi 15236837 595 FLLPEDIVEVNQKMILILTASIM 617
Cdd:cd21301  82 YALPEDIVEVKPKMVMTVFACLM 104
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
255-369 1.30e-31

second calponin homology (CH) domain found in plastin-2; 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-2 contaisn 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: 409176  Cd Length: 125  Bit Score: 119.29  E-value: 1.30e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 255 LLEDSDDVEELLRLPPEKVLLKWMNFHLKKGGYKKtVSNFSADLKDAQAYAFLLNVLAP---EHCDPAT------LDAKD 325
Cdd:cd21327   1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNK-INNFSSDIKDSKAYYHLLNQVAPkgdEEGIPAIvidmsgLREKD 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15236837 326 PLERAELVLSHAERMNCKRYLTAEEIVEGSSTLNLAFVAQIFHE 369
Cdd:cd21327  80 DLKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNK 123
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
255-368 1.84e-30

second calponin homology (CH) domain found in plastin-3; 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. Plastin-3 contains 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: 409177 [Multi-domain]  Cd Length: 122  Bit Score: 115.83  E-value: 1.84e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 255 LLEDSDDVEELLRLPPEKVLLKWMNFHLKKGGYKKtVSNFSADLKDAQAYAFLLNVLAPE---------HCDPATLDAKD 325
Cdd:cd21328   1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQK-INNFSSDIKDSRAYFHLLNQIAPKgqkegepriDINMSGFNEKD 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15236837 326 PLERAELVLSHAERMNCKRYLTAEEIVEGSSTLNLAFVAQIFH 368
Cdd:cd21328  80 DLKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
393-502 4.47e-28

third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains 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: 409178  Cd Length: 118  Bit Score: 108.92  E-value: 4.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 393 RDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKVSpSSVNWKHASKPPIKM---PFRKVENCNQVIKIGK-QLKF 468
Cdd:cd21329   6 SEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTR-VPVDWGHVNKPPYPAlggNMKKIENCNYAVELGKnKAKF 84
                        90       100       110
                ....*....|....*....|....*....|....
gi 15236837 469 SLVNVAGNDIVQGNKKLILGLLWQLMRFHMLQLL 502
Cdd:cd21329  85 SLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
258-368 8.96e-28

second calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains 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: 409175  Cd Length: 121  Bit Score: 108.43  E-value: 8.96e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 258 DSDDVEELLRLPPEKVLLKWMNFHLKKGGYKKtVSNFSADLKDAQAYAFLLNVLAPE--------HCDPATLDAKDPLER 329
Cdd:cd21326   1 EGEELEELMKLSPEELLLRWVNYHLTNAGWQN-ISNFSQDIKDSRAYFHLLNQIAPKgdvfdeniEIDFSGFNEKNDLKR 79
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15236837 330 AELVLSHAERMNCKRYLTAEEIVEGSSTLNLAFVAQIFH 368
Cdd:cd21326  80 AEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 118
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
516-623 6.50e-26

fourth calponin homology (CH) domain found in plastin-3; 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. Plastin-3 contains four copies of the CH domain. This model corresponds to the fourth CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409183  Cd Length: 112  Bit Score: 102.66  E-value: 6.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 516 DADILSWANRKVRTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGE-TDDEKRLNATYIVSVARKLGCSV 594
Cdd:cd21334   3 DDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNlTDDDKLDNAKYAVSMARKIGARV 82
                        90       100
                ....*....|....*....|....*....
gi 15236837 595 FLLPEDIVEVNQKMILILTASIMYWSLQR 623
Cdd:cd21334  83 YALPEDLVEVKPKMVMTVFACLMGRGMKR 111
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
393-502 6.10e-25

third calponin homology (CH) domain found in plastin-3; 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. Plastin-3 contains 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: 409180  Cd Length: 134  Bit Score: 100.85  E-value: 6.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 393 RDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKVSpSSVNWKHASKPP---IKMPFRKVENCNQVIKIGKQ-LKF 468
Cdd:cd21331  22 REERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIK-VPVDWNKVNKPPypkLGANMKKLENCNYAVELGKHpAKF 100
                        90       100       110
                ....*....|....*....|....*....|....
gi 15236837 469 SLVNVAGNDIVQGNKKLILGLLWQLMRFHMLQLL 502
Cdd:cd21331 101 SLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
511-617 1.22e-24

fourth calponin homology (CH) domain found in plastin-2; 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-2 contains four copies of the CH domain. This model corresponds to the fourth CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409182  Cd Length: 115  Bit Score: 99.29  E-value: 1.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 511 GKEMTDADILSWANRKVRTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLN-ATYIVSVARK 589
Cdd:cd21333   3 GQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNnAKYAISMARK 82
                        90       100
                ....*....|....*....|....*...
gi 15236837 590 LGCSVFLLPEDIVEVNQKMILILTASIM 617
Cdd:cd21333  83 IGARVYALPEDLVEVKPKMVMTVFACLM 110
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
393-502 1.45e-24

third calponin homology (CH) domain found in plastin-2; 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-2 contains 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: 409179  Cd Length: 125  Bit Score: 99.29  E-value: 1.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 393 RDERCYRLWINSLGIDSYVNNVFEDVRNGWILLEVLDKVSpSSVNWKHASKPP---IKMPFRKVENCNQVIKIGK-QLKF 468
Cdd:cd21330  13 REERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIK-VPVDWNRVNKPPypkLGENMKKLENCNYAVELGKnKAKF 91
                        90       100       110
                ....*....|....*....|....*....|....
gi 15236837 469 SLVNVAGNDIVQGNKKLILGLLWQLMRFHMLQLL 502
Cdd:cd21330  92 SLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 125
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
268-368 1.53e-22

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: 92.73  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837   268 LPPEKVLLKWMNFHLKKGGYKKTVSNFSADLKDAQAYAFLLNVLAPEHCDPATL--DAKDPLERAELVLSHAER-MNCKR 344
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKkLGVPK 80
                          90       100
                  ....*....|....*....|....*
gi 15236837   345 YL-TAEEIVEGSSTLNLAFVAQIFH 368
Cdd:pfam00307  81 VLiEPEDLVEGDNKSVLTYLASLFR 105
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
511-617 1.11e-21

fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the fourth CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409181  Cd Length: 115  Bit Score: 90.78  E-value: 1.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 511 GKEMTDADILSWANRKVRTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLN-ATYIVSVARK 589
Cdd:cd21332   5 GEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDLSDADKLNnAKYAISVARK 84
                        90       100
                ....*....|....*....|....*...
gi 15236837 590 LGCSVFLLPEDIVEVNQKMILILTASIM 617
Cdd:cd21332  85 IGARVYALPEDLVEVKPKMVMTVFACLM 112
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
398-496 1.61e-19

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: 83.90  E-value: 1.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837    398 YRLWINSLG---IDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPpiKMPFRKVENCNQVIKIGKQLKFSLVNVA 474
Cdd:smart00033   3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 15236837    475 GNDIVQGnKKLILGLLWQLMRF 496
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLISL 101
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
401-495 6.94e-18

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: 79.93  E-value: 6.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 401 WINS-----------LGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMPFRKVENCNQVIKIGKQLKFS 469
Cdd:cd21217   9 HINSlladdpdlkhlLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKNIFEATENLNLALNAAKKIGCK 88
                        90       100
                ....*....|....*....|....*.
gi 15236837 470 LVNVAGNDIVQGNKKLILGLLWQLMR 495
Cdd:cd21217  89 VVNIGPQDILDGNPHLVLGLLWQIIR 114
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
133-237 1.89e-16

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: 75.40  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837   133 INRYLGDDPflkqflpLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKrvlnPWERNENHTLCLNSA-KAVGCS 211
Cdd:pfam00307  11 INSHLAEYG-------PGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLALDVAeKKLGVP 79
                          90       100
                  ....*....|....*....|....*.
gi 15236837   212 VVNIGTQDLAEGRPHLVLGLISQLIK 237
Cdd:pfam00307  80 KVLIEPEDLVEGDNKSVLTYLASLFR 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
399-498 3.45e-16

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: 74.63  E-value: 3.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837   399 RLWINSL----GIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHaskpPIKMPFRKVENCNQVIKIG-KQLKFSLVNV 473
Cdd:pfam00307   8 LRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK----LNKSEFDKLENINLALDVAeKKLGVPKVLI 83
                          90       100
                  ....*....|....*....|....*
gi 15236837   474 AGNDIVQGNKKLILGLLWQLMRFHM 498
Cdd:pfam00307  84 EPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
129-238 4.37e-16

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: 74.27  E-value: 4.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837    129 FVQHINRYLGDDPflkqflplDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKrvLNPWERNENHTLCLNSAKAV 208
Cdd:smart00033   3 LLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKL 72
                           90       100       110
                   ....*....|....*....|....*....|
gi 15236837    209 GCSVVNIGTQDLAEGrPHLVLGLISQLIKI 238
Cdd:smart00033  73 GGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
518-617 1.15e-15

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: 73.09  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837   518 DILSWANRKVRTMGRKLQIESFKdKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDdeKRLNATYIVSVAR-KLGCSVFL 596
Cdd:pfam00307   6 ELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKLNKSEFD--KLENINLALDVAEkKLGVPKVL 82
                          90       100
                  ....*....|....*....|..
gi 15236837   597 L-PEDIVEVNQKMILILTASIM 617
Cdd:pfam00307  83 IePEDLVEGDNKSVLTYLASLF 104
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
129-237 1.99e-15

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: 72.37  E-value: 1.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 129 FVQHINRYLGDDpflkqflpLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKrvlNPWERNENHTLCLNSAKAV 208
Cdd:cd00014   4 LLKWINEVLGEE--------LPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPK---SPFKKRENINLFLNACKKL 72
                        90       100       110
                ....*....|....*....|....*....|.
gi 15236837 209 G-CSVVNIGTQDLAEGR-PHLVLGLISQLIK 237
Cdd:cd00014  73 GlPELDLFEPEDLYEKGnLKKVLGTLWALAL 103
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
147-241 3.97e-15

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: 71.93  E-value: 3.97e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 147 LPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLNSAKAVGCSVVNIGTQDLAEGRPH 226
Cdd:cd21219  16 LGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKPLNKFKKVENCNYAVDLAKKLGFSLVGIGGKDIADGNRK 95
                        90
                ....*....|....*
gi 15236837 227 LVLGLISQLIKIQVL 241
Cdd:cd21219  96 LTLALVWQLMRYHVL 110
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
272-367 2.10e-14

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: 69.27  E-value: 2.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837    272 KVLLKWMNFHLKKGGyKKTVSNFSADLKDAQAYAFLLNVLAPEHCDPATLDAK----DPLERAELVLSHAERMNCKR-YL 346
Cdd:smart00033   1 KTLLRWVNSLLAEYD-KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVvLF 79
                           90       100
                   ....*....|....*....|.
gi 15236837    347 TAEEIVEGsSTLNLAFVAQIF 367
Cdd:smart00033  80 EPEDLVEG-PKLILGVIWTLI 99
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
518-619 6.94e-14

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: 67.73  E-value: 6.94e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837    518 DILSWANRKvrTMGRKLQIESFKDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNATYIVSVARKLGCSVFLL 597
Cdd:smart00033   2 TLLRWVNSL--LAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79
                           90       100
                   ....*....|....*....|...
gi 15236837    598 -PEDIVEVNqKMILILTASIMYW 619
Cdd:smart00033  80 ePEDLVEGP-KLILGVIWTLISL 101
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
401-491 6.51e-12

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409035  Cd Length: 107  Bit Score: 62.40  E-value: 6.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 401 WINSLGIDS---YVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASkppikMPFRKVENCNQVIKIGKQLKFSLVNVAGND 477
Cdd:cd21186  10 WINSQLSKAnkpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGR-----MRVHHLNNVNRALQVLEQNNVKLVNISSND 84
                        90
                ....*....|....
gi 15236837 478 IVQGNKKLILGLLW 491
Cdd:cd21186  85 IVDGNPKLTLGLVW 98
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
395-496 9.85e-12

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 62.03  E-value: 9.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 395 ERCYRLWIN----SLGIDsyVNNVFEDVRNGWILLEVLDKVSPSSVNwKHASKPpiKMPFRKVENCNQVIKIGKQLKFSL 470
Cdd:cd21215   6 KKTFTKWLNtklsSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLG-RYNKNP--KMRVQKLENVNKALEFIKSRGVKL 80
                        90       100
                ....*....|....*....|....*..
gi 15236837 471 VNVAGNDIVQGNKKLILGLLWQL-MRF 496
Cdd:cd21215  81 TNIGAEDIVDGNLKLILGLLWTLiLRF 107
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
395-495 1.64e-11

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: 61.20  E-value: 1.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 395 ERCYRLWINS-LGIDSY--VNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKppiKMPFRKVENCNQVIKIGKQLKF-SL 470
Cdd:cd00014   1 EEELLKWINEvLGEELPvsITDLFESLRDGVLLCKLINKLSPGSIPKINKKP---KSPFKKRENINLFLNACKKLGLpEL 77
                        90       100
                ....*....|....*....|....*.
gi 15236837 471 VNVAGNDIVQ-GNKKLILGLLWQLMR 495
Cdd:cd00014  78 DLFEPEDLYEkGNLKKVLGTLWALAL 103
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
383-498 3.44e-11

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409085  Cd Length: 128  Bit Score: 61.15  E-value: 3.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 383 EMMTEDVETCRDER------CYRLWINS--LGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHAskppiKMPFRKVE 454
Cdd:cd21236   1 QAYENVLERYKDERdkvqkkTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKG-----RMRFHRLQ 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15236837 455 NCNQVIKIGKQLKFSLVNVAGNDIVQGNKKLILGLLW------QLMRFHM 498
Cdd:cd21236  76 NVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWtiilhfQISDIHV 125
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
414-495 3.65e-10

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 58.23  E-value: 3.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 414 VFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKM----PFRKVENCNQVIKIGKQLKFSLVNVAGNDIVQGNKKLILGL 489
Cdd:cd21294  38 LFDECKDGLVLSKLINDSVPDTIDERVLNKPPRKNkplnNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGL 117

                ....*.
gi 15236837 490 LWQLMR 495
Cdd:cd21294 118 IWQIIR 123
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
401-491 4.36e-10

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 57.41  E-value: 4.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 401 WINS--LGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHAskppiKMPFRKVENCNQVIKIGKQLKFSLVNVAGNDI 478
Cdd:cd21188  11 WVNKhlIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERG-----RMRFHRLQNVQTALDFLKYRKIKLVNIRAEDI 85
                        90
                ....*....|...
gi 15236837 479 VQGNKKLILGLLW 491
Cdd:cd21188  86 VDGNPKLTLGLIW 98
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
395-494 1.01e-09

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409167  Cd Length: 139  Bit Score: 57.34  E-value: 1.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 395 ERCYRLWINS--LGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVnwkhaSKPPI-KMPFRKVENCNQVIKIGKQLKFSLV 471
Cdd:cd21318  40 KKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLEVLSGEQL-----PKPTRgRMRIHSLENVDKALQFLKEQRVHLE 114
                        90       100
                ....*....|....*....|...
gi 15236837 472 NVAGNDIVQGNKKLILGLLWQLM 494
Cdd:cd21318 115 NVGSHDIVDGNHRLTLGLIWTII 137
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
411-494 2.66e-09

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409032  Cd Length: 108  Bit Score: 55.18  E-value: 2.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 411 VNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPpiKMPFRKVENCNQVIKIGKQLKFSLVNVAGNDIVQGNKKLILGLL 490
Cdd:cd21183  24 IHDLATDFSDGLCLIALLENLSTRPLKRSYNRRP--AFQQHYLENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLI 101

                ....
gi 15236837 491 WQLM 494
Cdd:cd21183 102 WTLI 105
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
395-494 4.81e-09

first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.


Pssm-ID: 409081  Cd Length: 107  Bit Score: 54.24  E-value: 4.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 395 ERCYRLWINSLGIDS---YVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPpikmpFRKVENCNQVIKIGKQLKFSLV 471
Cdd:cd21232   4 KKTFTKWINARFSKSgkpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTR-----VHALNNVNRVLQVLHQNNVELV 78
                        90       100
                ....*....|....*....|...
gi 15236837 472 NVAGNDIVQGNKKLILGLLWQLM 494
Cdd:cd21232  79 NIGGTDIVDGNHKLTLGLLWSII 101
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
147-244 5.37e-09

third calponin homology (CH) domain found in the plastin family; The plastin family includes 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. 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: 409147  Cd Length: 117  Bit Score: 54.55  E-value: 5.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 147 LPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINT--KRVLNPWERNENHTLCLNSAKAVGCSVVNIGTQDLAEGR 224
Cdd:cd21298  18 LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKpfKKLGANMKKIENCNYAVELGKKLKFSLVGIGGKDIYDGN 97
                        90       100
                ....*....|....*....|
gi 15236837 225 PHLVLGLISQLIKIQVLADL 244
Cdd:cd21298  98 RTLTLALVWQLMRAYTLSIL 117
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
401-491 5.51e-09

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409095  Cd Length: 117  Bit Score: 54.30  E-value: 5.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 401 WINS--LGIDSYVNNVFEDVRNGWILLEVLDKVSPssvnwKHASKP-PIKMPFRKVENCNQVIKIGKQLKFSLVNVAGND 477
Cdd:cd21246  24 WVNShlARVGCRINDLYTDLRDGRMLIKLLEVLSG-----ERLPKPtKGKMRIHCLENVDKALQFLKEQRVHLENMGSHD 98
                        90
                ....*....|....
gi 15236837 478 IVQGNKKLILGLLW 491
Cdd:cd21246  99 IVDGNHRLTLGLIW 112
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
401-491 6.47e-09

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409042  Cd Length: 116  Bit Score: 54.22  E-value: 6.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 401 WINSL--GIDSYVNNVFEDVRNGWILLEVLDKVSPSSVnwkhaSKPPI-KMPFRKVENCNQVIKIGKQlKFSLVNVAGND 477
Cdd:cd21193  24 WINSFleKANLEIGDLFTDLSDGKLLLKLLEIISGEKL-----GKPNRgRLRVQKIENVNKALAFLKT-KVRLENIGAED 97
                        90
                ....*....|....
gi 15236837 478 IVQGNKKLILGLLW 491
Cdd:cd21193  98 IVDGNPRLILGLIW 111
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
395-495 7.26e-09

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409074  Cd Length: 111  Bit Score: 54.07  E-value: 7.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 395 ERCYRLWINSL----GIDSyVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPpiKMPFRKVENCNQVIK-IGKQLKFS 469
Cdd:cd21225   6 IKAFTAWVNSVlekrGIPK-ISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEP--KNRIQMIQNLHLAMLfIEEDLKIR 82
                        90       100
                ....*....|....*....|....*.
gi 15236837 470 LVNVAGNDIVQGNKKLILGLLWQLMR 495
Cdd:cd21225  83 VQGIGAEDFVDNNKKLILGLLWTLYR 108
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
407-494 7.96e-09

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409077  Cd Length: 108  Bit Score: 53.65  E-value: 7.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 407 IDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMpfRKVENCNQVIKIGKQLKFSLVNVAGNDIVQGNKKLI 486
Cdd:cd21228  20 VNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRPTFRQ--MKLENVSVALEFLERESIKLVSIDSSAIVDGNLKLI 97

                ....*...
gi 15236837 487 LGLLWQLM 494
Cdd:cd21228  98 LGLIWTLI 105
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
147-245 1.17e-08

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: 53.27  E-value: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 147 LPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLNSAKAVGCSVVNIGTQDLAEGRPH 226
Cdd:cd21299  16 LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFSLVNVAGNDIVQGNKK 95
                        90
                ....*....|....*....
gi 15236837 227 LVLGLISQLIKIQVLADLN 245
Cdd:cd21299  96 LILALLWQLMRYHMLQLLK 114
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
269-352 1.34e-08

second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409033  Cd Length: 103  Bit Score: 53.01  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 269 PPEKVLLKWMNFHLkkGGYKktVSNFSADLKDAQAYAFLLNVLAPEHC-DPATLDAKDPLERAELVLSHAER-MNCKRYL 346
Cdd:cd21184   1 SGKSLLLEWVNSKI--PEYK--VKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEeLGIPKII 76

                ....*.
gi 15236837 347 TAEEIV 352
Cdd:cd21184  77 TPEDMV 82
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
520-616 1.72e-08

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: 53.07  E-value: 1.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 520 LSWANRKVRTMGR-KLQIESFkDKSLSSGLFFLNLLWAVEPRVVNWNLVTKGETDDEKRLNATYIVSVARKLGCSVFLLP 598
Cdd:cd21218  16 LRWVNYHLKKAGPtKKRVTNF-SSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYFLTP 94
                        90
                ....*....|....*...
gi 15236837 599 EDIVEVNQKMILILTASI 616
Cdd:cd21218  95 EDIVSGNPRLNLAFVATL 112
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
395-494 1.85e-08

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409086  Cd Length: 118  Bit Score: 53.11  E-value: 1.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 395 ERCYRLWINS--LGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHAskppiKMPFRKVENCNQVIKIGKQLKFSLVN 472
Cdd:cd21237   8 KKTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKG-----RMRFHRLQNVQIALDFLKQRQVKLVN 82
                        90       100
                ....*....|....*....|..
gi 15236837 473 VAGNDIVQGNKKLILGLLWQLM 494
Cdd:cd21237  83 IRNDDITDGNPKLTLGLIWTII 104
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
395-494 2.14e-08

first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409084  Cd Length: 119  Bit Score: 52.72  E-value: 2.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 395 ERCYRLWINS--LGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHAskppiKMPFRKVENCNQVIKIGKQLKFSLVN 472
Cdd:cd21235   8 KKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLVN 82
                        90       100
                ....*....|....*....|..
gi 15236837 473 VAGNDIVQGNKKLILGLLWQLM 494
Cdd:cd21235  83 IRNDDIADGNPKLTLGLIWTII 104
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
401-494 3.72e-08

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 51.62  E-value: 3.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 401 WINSL--GIDSYVNNVFEDVRNGWILLEVLDKVSPSSVnwkhaSKPP-IKMPFRKVENCNQVIKIGKQLKFSLVNVAGND 477
Cdd:cd21214  13 WCNSHlrKAGTQIENIEEDFRDGLKLMLLLEVISGERL-----PKPErGKMRFHKIANVNKALDFIASKGVKLVSIGAEE 87
                        90
                ....*....|....*..
gi 15236837 478 IVQGNKKLILGLLWQLM 494
Cdd:cd21214  88 IVDGNLKMTLGMIWTII 104
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
162-236 4.44e-08

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: 51.52  E-value: 4.44e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15236837 162 DGVLLCKLINVavpgtIDERAIN--TKRVLNPWERNENHTLCLNSAKAVGCSVVNIGTQDLAEGRPHLVLGLISQLI 236
Cdd:cd21227  33 DGVKLIALVEI-----LQGRKLGrvIKKPLNQHQKLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLI 104
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
395-498 4.74e-08

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409039  Cd Length: 113  Bit Score: 51.80  E-value: 4.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 395 ERCYRLWINS----LGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVnwkHASKPPIKMPFRKVENCNQVIKIGKQLKFSL 470
Cdd:cd21190   7 KKTFTNWINShlakLSQPIVINDLFVDIKDGTALLRLLEVLSGQKL---PIESGRVLQRAHKLSNIRNALDFLTKRCIKL 83
                        90       100
                ....*....|....*....|....*....
gi 15236837 471 VNVAGNDIVQGNKKLILGLLWQ-LMRFHM 498
Cdd:cd21190  84 VNINSTDIVDGKPSIVLGLIWTiILYFQI 112
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
395-494 9.60e-08

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409166  Cd Length: 132  Bit Score: 51.21  E-value: 9.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 395 ERCYRLWINS-LG-IDSYVNNVFEDVRNGWILLEVLDKVSPSSVnwkhaSKPPI-KMPFRKVENCNQVIKIGKQLKFSLV 471
Cdd:cd21317  33 KKTFTKWVNShLArVTCRIGDLYTDLRDGRMLIRLLEVLSGEQL-----PKPTKgRMRIHCLENVDKALQFLKEQKVHLE 107
                        90       100
                ....*....|....*....|...
gi 15236837 472 NVAGNDIVQGNKKLILGLLWQLM 494
Cdd:cd21317 108 NMGSHDIVDGNHRLTLGLIWTII 130
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
395-498 1.10e-07

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409091  Cd Length: 111  Bit Score: 50.60  E-value: 1.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 395 ERCYRLWINSL----GIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPpikmpFRKVENCNQVIKIGKQLKFSL 470
Cdd:cd21242   7 KRTFTNWINSQlakhSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNV-----FQCRSNIETALSFLKNKSIKL 81
                        90       100
                ....*....|....*....|....*....
gi 15236837 471 VNVAGNDIVQGNKKLILGLLWQ-LMRFHM 498
Cdd:cd21242  82 INIHVPDIIEGKPSIILGLIWTiILHFHI 110
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
394-495 1.14e-07

first calponin homology (CH) domain found in the plastin family; The plastin family includes 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. 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: 409141  Cd Length: 145  Bit Score: 51.51  E-value: 1.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 394 DERCYRLWINS-----------LGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKmPFRKVENCNQVIKI 462
Cdd:cd21292  25 EKVAFVNWINKnlgddpdckhlLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDERAINKKKLT-VFTIHENLTLALNS 103
                        90       100       110
                ....*....|....*....|....*....|...
gi 15236837 463 GKQLKFSLVNVAGNDIVQGNKKLILGLLWQLMR 495
Cdd:cd21292 104 ASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIR 136
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
401-493 2.46e-07

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: 49.59  E-value: 2.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 401 WINSL--GIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNwKHASKPpiKMPFRKVENCNQVIKIGKQLKFSLVNVAGNDI 478
Cdd:cd21227  12 WVNEQlkPTGMSVEDLATDLEDGVKLIALVEILQGRKLG-RVIKKP--LNQHQKLENVTLALKAMAEDGIKLVNIGNEDI 88
                        90
                ....*....|....*
gi 15236837 479 VQGNKKLILGLLWQL 493
Cdd:cd21227  89 VNGNLKLILGLIWHL 103
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
387-494 3.33e-07

first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.


Pssm-ID: 409080  Cd Length: 111  Bit Score: 49.15  E-value: 3.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 387 EDVEtcrdERCYRLWINSLGID---SYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPpikmpFRKVENCNQVIKIG 463
Cdd:cd21231   4 EDVQ----KKTFTKWINAQFAKfgkPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTR-----VHALNNVNKALQVL 74
                        90       100       110
                ....*....|....*....|....*....|.
gi 15236837 464 KQLKFSLVNVAGNDIVQGNKKLILGLLWQLM 494
Cdd:cd21231  75 QKNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
407-494 5.58e-07

first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409072  Cd Length: 113  Bit Score: 48.74  E-value: 5.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 407 IDSYVNNVFEDVRNGWILLEVLDKVSpssVNWKHASK---PPIKMPfRKVENCNQVIK----IGKQLKFSLVNVAGNDIV 479
Cdd:cd21223  22 FDFAVTNLAVDLRDGVRLCRLVELLT---GDWSLLSKlrvPAISRL-QKLHNVEVALKalkeAGVLRGGDGGGITAKDIV 97
                        90
                ....*....|....*
gi 15236837 480 QGNKKLILGLLWQLM 494
Cdd:cd21223  98 DGHREKTLALLWRII 112
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
395-500 7.09e-07

first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409040  Cd Length: 114  Bit Score: 48.34  E-value: 7.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 395 ERCYRLWINsLGIDS-----YVNNVFEDVRNGWILLEVLDKVSPSSVNWKHasKPPIKMPFRkVENCNQVIKIGKQLKFS 469
Cdd:cd21191   7 KRTFTRWIN-LHLEKcnpplEVKDLFVDIQDGKILMALLEVLSGQNLLQEY--KPSSHRIFR-LNNIAKALKFLEDSNVK 82
                        90       100       110
                ....*....|....*....|....*....|.
gi 15236837 470 LVNVAGNDIVQGNKKLILGLLWQLMRFHMLQ 500
Cdd:cd21191  83 LVSIDAAEIADGNPSLVLGLIWNIILFFQIK 113
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
374-495 8.40e-07

first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains 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: 409172  Cd Length: 145  Bit Score: 48.89  E-value: 8.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 374 NKDGKYAFAEMMTEDVETcrDERCYRLwinsLGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKmPFRKV 453
Cdd:cd21323  22 SEEEKVAFVNWINKALEG--DPDCKHV----VPMNPTDESLFKSLADGILLCKMINLSQPDTIDERAINKKKLT-PFTIS 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15236837 454 ENCNQVIKIGKQLKFSLVNVAGNDIVQGNKKLILGLLWQLMR 495
Cdd:cd21323  95 ENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIK 136
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
147-244 1.10e-06

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: 47.80  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 147 LPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWER-----NENHTLCLnsAKAVGCSVVNIGTQDLA 221
Cdd:cd21300  19 LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPASAEISRfkaveNTNYAVEL--GKQLGFSLVGIQGADIT 96
                        90       100
                ....*....|....*....|...
gi 15236837 222 EGRPHLVLGLISQLIKIQVLADL 244
Cdd:cd21300  97 DGSRTLTLALVWQLMRFHITKTL 119
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
370-499 1.13e-06

first calponin homology (CH) domain found in plastin-3; 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. Plastin- 3 contains 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: 409174  Cd Length: 148  Bit Score: 48.52  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 370 RNGLNKDGKYAFAEMMTEDVETCRDERcyrlwiNSLGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKmP 449
Cdd:cd21325  18 QHSYSEEEKYAFVNWINKALENDPDCR------HVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLT-P 90
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15236837 450 FRKVENCNQVIKIGKQLKFSLVNVAGNDIVQGNKKLILGLLWQLMRFHML 499
Cdd:cd21325  91 FIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLF 140
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
374-495 1.26e-06

first calponin homology (CH) domain found in plastin-2; 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-2 contains 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: 409173  Cd Length: 145  Bit Score: 48.47  E-value: 1.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 374 NKDGKYAFAEMMTEDVEtcRDERCYRLwinsLGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKmPFRKV 453
Cdd:cd21324  22 SEEEKYAFVNWINKALE--NDPDCKHV----IPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKKLT-PFTIQ 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15236837 454 ENCNQVIKIGKQLKFSLVNVAGNDIVQGNKKLILGLLWQLMR 495
Cdd:cd21324  95 ENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 136
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
405-495 8.43e-06

first 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, and are probably involved in the 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409142  Cd Length: 116  Bit Score: 45.21  E-value: 8.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 405 LGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMPFRKVENCNQVIKIGKQLKFSLVNVAGNDIVQGNKK 484
Cdd:cd21293  24 LPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLNSAKAIGCSVVNIGTQDLAEGRPH 103
                        90
                ....*....|.
gi 15236837 485 LILGLLWQLMR 495
Cdd:cd21293 104 LVLGLISQIIK 114
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
395-494 8.77e-06

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409165  Cd Length: 154  Bit Score: 46.19  E-value: 8.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 395 ERCYRLWINS--LGIDSYVNNVFEDVRNGWILLEVLDKVSPSSVnwkhaSKPPI-KMPFRKVENCNQVIKIGKQLKFSLV 471
Cdd:cd21316  55 KKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLEVLSGERL-----PKPTKgRMRIHCLENVDKALQFLKEQRVHLE 129
                        90       100
                ....*....|....*....|...
gi 15236837 472 NVAGNDIVQGNKKLILGLLWQLM 494
Cdd:cd21316 130 NMGSHDIVDGNHRLTLGLIWTII 152
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
269-352 1.33e-05

second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409079  Cd Length: 103  Bit Score: 44.30  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 269 PPEKVLLKWMNFHLKKggykKTVSNFSADLKDAQAYAFLLNVLAPEHC-DPATLDAKDPLERAELVLSHAER-MNCKRYL 346
Cdd:cd21230   1 TPKQRLLGWIQNKIPQ----LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDwLGVPQLI 76

                ....*.
gi 15236837 347 TAEEIV 352
Cdd:cd21230  77 TPEEII 82
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
154-237 1.50e-05

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 44.31  E-value: 1.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 154 NQLYELVKDGVLLCKLINVAVPGTIDERAINTK-RVlnpwERNENHTLCLNSAKAVGCSVVNIGTQDLAEGRPHLVLGLI 232
Cdd:cd21215  25 TDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKmRV----QKLENVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILGLL 100

                ....*
gi 15236837 233 SQLIK 237
Cdd:cd21215 101 WTLIL 105
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
271-354 1.50e-05

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: 44.25  E-value: 1.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 271 EKVLLKWMNFHLKKGGyKKTVSNFSADLKDAQAYAFLLNVLAPEHCDPATLDAKDP---LERAELVLSHAERMNCKR--Y 345
Cdd:cd00014   1 EEELLKWINEVLGEEL-PVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLGLPEldL 79

                ....*....
gi 15236837 346 LTAEEIVEG 354
Cdd:cd00014  80 FEPEDLYEK 88
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
401-496 2.30e-05

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 43.72  E-value: 2.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 401 WINSL----GIDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHaSKPpiKMPFRKVENCNQVIKIGKQLKFSLVNVAGN 476
Cdd:cd21212   8 WANHYlekgGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIH-SRP--KTRAQKLENIQACLQFLAALGVDVQGITAE 84
                        90       100
                ....*....|....*....|
gi 15236837 477 DIVQGNKKLILGLLWQLMRF 496
Cdd:cd21212  85 DIVDGNLKAILGLFFSLSRY 104
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
276-362 3.63e-05

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 43.34  E-value: 3.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 276 KWMNFHLKKGGYKKTVSNFSADLKDAQAYAFLLNVLAPE-----HCDPATldAKDPLERAELVLSHAERMNCK-RYLTAE 349
Cdd:cd21212   7 DWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEkvpgiHSRPKT--RAQKLENIQACLQFLAALGVDvQGITAE 84
                        90
                ....*....|....*
gi 15236837 350 EIVEGS--STLNLAF 362
Cdd:cd21212  85 DIVDGNlkAILGLFF 99
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
401-491 4.02e-05

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409090  Cd Length: 113  Bit Score: 43.13  E-value: 4.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 401 WINSLGIDS----YVNNVFEDVRNGWILLEVLDKVSPSsvnwkhaskppiKMPFRK---------VENCNQVIKIGKQLK 467
Cdd:cd21241  13 WINSYLAKRkppmKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKgrrlkrvhfLSNINTALKFLESKK 80
                        90       100
                ....*....|....*....|....
gi 15236837 468 FSLVNVAGNDIVQGNKKLILGLLW 491
Cdd:cd21241  81 IKLVNINPTDIVDGKPSIVLGLIW 104
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
125-247 5.60e-05

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409085  Cd Length: 128  Bit Score: 43.43  E-value: 5.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 125 EKGPFVQHINRYLgddpflkqfLPLDPHSNQLYELVKDGVLLCKLINVaVPGTIDERAINTKRvlnpWERNENHTLCLNS 204
Cdd:cd21236  18 QKKTFTKWINQHL---------MKVRKHVNDLYEDLRDGHNLISLLEV-LSGDTLPREKGRMR----FHRLQNVQIALDY 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15236837 205 AKAVGCSVVNIGTQDLAEGRPHLVLGLISQLIKIQVLADLNLK 247
Cdd:cd21236  84 LKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVT 126
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
154-236 6.87e-05

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409032  Cd Length: 108  Bit Score: 42.47  E-value: 6.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 154 NQLYELVKDGVLLCKLINVaVPGTIDERAINtKRVLNPWERNENHTLCLNSAKAVGCSVVNIGTQDLAEGRPHLVLGLIS 233
Cdd:cd21183  25 HDLATDFSDGLCLIALLEN-LSTRPLKRSYN-RRPAFQQHYLENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLIW 102

                ...
gi 15236837 234 QLI 236
Cdd:cd21183 103 TLI 105
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
519-616 7.84e-05

second calponin homology (CH) domain found in plastin-3; 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. Plastin-3 contains 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: 409177 [Multi-domain]  Cd Length: 122  Bit Score: 42.65  E-value: 7.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 519 ILSWANRKVRTMGRKlQIESFKDKSLSSGLFFlNLLWAVEPR-------VVNWNLVTKGETDDEKRlnATYIVSVARKLG 591
Cdd:cd21328  20 LLRWANFHLENAGWQ-KINNFSSDIKDSRAYF-HLLNQIAPKgqkegepRIDINMSGFNEKDDLKR--AEYMLQQADKLG 95
                        90       100
                ....*....|....*....|....*
gi 15236837 592 CSVFLLPEDIVEVNQKMILILTASI 616
Cdd:cd21328  96 CRQFVTPADVVSGNPKLNLAFVANL 120
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
158-224 1.09e-04

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: 41.91  E-value: 1.09e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15236837 158 ELVKDGVLLCKLINVAVPGTIdeRAINTKRVlnPWERNENHTLCLNSAKAVGCSVVNI-GTQDLAEGR 224
Cdd:cd21207  30 DVLKDGVILCKLINILKPGSV--KKINTSKM--AFKLMENIENFLTACKGYGVPKTDLfQTVDLYEKK 93
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
258-353 1.30e-04

second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409161  Cd Length: 114  Bit Score: 42.10  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 258 DSDDVEELLRLPPEKVLLKWMNFHLKKggykKTVSNFSADLKDAQAYAFLLNVLAPEHC-DPATLDAKDPLERAELVLSH 336
Cdd:cd21312   1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ----LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQ 76
                        90
                ....*....|....*...
gi 15236837 337 AER-MNCKRYLTAEEIVE 353
Cdd:cd21312  77 ADDwLGIPQVITPEEIVD 94
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
411-494 1.31e-04

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409159  Cd Length: 125  Bit Score: 42.33  E-value: 1.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 411 VNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMpfRKVENCNQVIKIGKQLKFSLVNVAGNDIVQGNKKLILGLL 490
Cdd:cd21310  36 LNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQ--MKLENVSVALEFLDREHIKLVSIDSKAIVDGNLKLILGLI 113

                ....
gi 15236837 491 WQLM 494
Cdd:cd21310 114 WTLI 117
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
125-236 2.03e-04

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409090  Cd Length: 113  Bit Score: 41.21  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 125 EKGPFVQHINRYLgddpfLKQFLPLdpHSNQLYELVKDGVLLCKLINV----AVPGtidERAINTKRVlnPWERNENHTL 200
Cdd:cd21241   6 QKKTFTNWINSYL-----AKRKPPM--KVEDLFEDIKDGTKLLALLEVlsgeKLPC---EKGRRLKRV--HFLSNINTAL 73
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15236837 201 CLNSAKAVgcSVVNIGTQDLAEGRPHLVLGLISQLI 236
Cdd:cd21241  74 KFLESKKI--KLVNINPTDIVDGKPSIVLGLIWTII 107
EF-hand_7 pfam13499
EF-hand domain pair;
34-89 3.46e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.16  E-value: 3.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15236837    34 KNQNGKVTIEDLPPLFAKLkALSATFKEDEIKGMLGELGSDTSTDVSFEEFLKIYL 89
Cdd:pfam13499  13 SDGDGYLDVEELKKLLRKL-EEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
407-494 4.67e-04

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409160  Cd Length: 124  Bit Score: 40.51  E-value: 4.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 407 IDSYVNNVFEDVRNGWILLEVLDKVSPSSVNwKHASKPPIKMpfRKVENCNQVIK-IGKQLKFSLVNVAGNDIVQGNKKL 485
Cdd:cd21311  31 ANKHIADLETDLSDGLRLIALVEVLSGKKFP-KFNKRPTFRS--QKLENVSVALKfLEEDEGIKIVNIDSSDIVDGKLKL 107

                ....*....
gi 15236837 486 ILGLLWQLM 494
Cdd:cd21311 108 ILGLIWTLI 116
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
407-501 5.95e-04

first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409157  Cd Length: 129  Bit Score: 40.45  E-value: 5.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 407 IDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMpfRKVENCNQVIKIGKQLKFSLVNVAGNDIVQGNKKLI 486
Cdd:cd21308  36 VSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQ--MQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLI 113
                        90
                ....*....|....*
gi 15236837 487 LGLLWQLMRFHMLQL 501
Cdd:cd21308 114 LGLIWTLILHYSISM 128
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
407-501 6.01e-04

first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409158  Cd Length: 131  Bit Score: 40.45  E-value: 6.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 407 IDSYVNNVFEDVRNGWILLEVLDKVSPSSVNWKHASKPPIKMpfRKVENCNQVIKIGKQLKFSLVNVAGNDIVQGNKKLI 486
Cdd:cd21309  33 VNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFRQ--MQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLI 110
                        90
                ....*....|....*
gi 15236837 487 LGLLWQLMRFHMLQL 501
Cdd:cd21309 111 LGLVWTLILHYSISM 125
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
154-236 7.65e-04

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409039  Cd Length: 113  Bit Score: 39.86  E-value: 7.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 154 NQLYELVKDGVLLCKLINVAvpgTIDERAINTKRVLNPWERNENHTLCLNSAKAVGCSVVNIGTQDLAEGRPHLVLGLIS 233
Cdd:cd21190  28 NDLFVDIKDGTALLRLLEVL---SGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIW 104

                ...
gi 15236837 234 QLI 236
Cdd:cd21190 105 TII 107
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
147-237 8.07e-04

third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains 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: 409178  Cd Length: 118  Bit Score: 39.58  E-value: 8.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 147 LPLDPHSNQLYELVKDGVLLCKL---INVAVP-GTIDERAI-----NTKRVlnpweRNENHTLCLNSAKAvGCSVVNIGT 217
Cdd:cd21329  18 LGVNPYVNHLYSDLCDALVIFQLyemTRVPVDwGHVNKPPYpalggNMKKI-----ENCNYAVELGKNKA-KFSLVGIAG 91
                        90       100
                ....*....|....*....|
gi 15236837 218 QDLAEGRPHLVLGLISQLIK 237
Cdd:cd21329  92 SDLNEGNKTLTLALIWQLMR 111
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
147-237 9.55e-04

third calponin homology (CH) domain found in plastin-3; 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. Plastin-3 contains 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: 409180  Cd Length: 134  Bit Score: 39.98  E-value: 9.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 147 LPLDPHSNQLYELVKDGVLLCKLIN-VAVPgtIDERAINTKrvlnPWER---------NENHTLCLNSAKAvGCSVVNIG 216
Cdd:cd21331  34 LGVNPHVNHLYGDLQDALVILQLYEkIKVP--VDWNKVNKP----PYPKlganmkkleNCNYAVELGKHPA-KFSLVGIG 106
                        90       100
                ....*....|....*....|.
gi 15236837 217 TQDLAEGRPHLVLGLISQLIK 237
Cdd:cd21331 107 GQDLNDGNPTLTLALVWQLMR 127
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
144-209 1.02e-03

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: 39.24  E-value: 1.02e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236837 144 KQFLPLDPHsnqlyELVKDGVLLCKLINVAVPGTIdeRAINTKRvlNPWERNENHTLCLNSAKAVG 209
Cdd:cd21208  15 KKFPSDDFR-----ESLEDGILLCELINAIKPGSI--KKINRLP--TPIAGLDNLNLFLKACEDLG 71
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
34-87 1.30e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 37.53  E-value: 1.30e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15236837  34 KNQNGKVTIEDLpplFAKLKALSATFKEDEIKGMLGELGSDTSTDVSFEEFLKI 87
Cdd:cd00051  11 KDGDGTISADEL---KAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
133-235 1.38e-03

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 38.72  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 133 INRYLgddpflkQFLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDerAINtKRVLNPWERNENHTLCLNSAKAVGCSV 212
Cdd:cd21212   9 ANHYL-------EKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVP--GIH-SRPKTRAQKLENIQACLQFLAALGVDV 78
                        90       100
                ....*....|....*....|...
gi 15236837 213 VNIGTQDLAEGRPHLVLGLISQL 235
Cdd:cd21212  79 QGITAEDIVDGNLKAILGLFFSL 101
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
519-616 1.59e-03

second calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains 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: 409175  Cd Length: 121  Bit Score: 39.10  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 519 ILSWANRKVRTMGRKlQIESFKDKSLSSGLFFlNLLWAVEPR------VVNWNLVTKGETDDEKRlnATYIVSVARKLGC 592
Cdd:cd21326  17 LLRWVNYHLTNAGWQ-NISNFSQDIKDSRAYF-HLLNQIAPKgdvfdeNIEIDFSGFNEKNDLKR--AEYMLQEADKLGC 92
                        90       100
                ....*....|....*....|....
gi 15236837 593 SVFLLPEDIVEVNQKMILILTASI 616
Cdd:cd21326  93 RQFVTPADVVSGNPKLNLAFVANL 116
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
274-366 1.79e-03

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


Pssm-ID: 409152  Cd Length: 108  Bit Score: 38.56  E-value: 1.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 274 LLKWMNFHLKKGGYKKTVSNF-SADLKDAQAYAFLLNVLAPEHCD-----PATLDaKDPLERAELVLSHAERMNCKRYLT 347
Cdd:cd21303   9 MVKWANDMVAKGGKNSSIRSFkDPSLSTGHFFLDVLNGLKSGYVDydlvtPGNTE-DEAYLNAKLAISIARKLGALIFLV 87
                        90
                ....*....|....*....
gi 15236837 348 AEEIVEGSSTLNLAFVAQI 366
Cdd:cd21303  88 PEDIVEVRPRLVLTFIGSL 106
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
257-352 1.88e-03

second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409164  Cd Length: 118  Bit Score: 38.61  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 257 EDSDDVEELLRLP-PEKVLLKWMNFHLKKggykKTVSNFSADLKDAQAYAFLLNVLAPEHC-DPATLDAKDPLERAELVL 334
Cdd:cd21315   3 EGEDDGPDDGKGPtPKQRLLGWIQSKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAM 78
                        90
                ....*....|....*....
gi 15236837 335 SHAER-MNCKRYLTAEEIV 352
Cdd:cd21315  79 DLAEDwLDVPQLIKPEEMV 97
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
519-616 3.13e-03

second 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, and are probably involved in the 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409145  Cd Length: 109  Bit Score: 37.88  E-value: 3.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 519 ILSWANRKVRTMGRKLQIESFKdKSLSSGLFFLNLLWAVEPRvvNWNLVTKGETDDEKRlnATYIVSVARKLGCSVFLLP 598
Cdd:cd21296  15 LLKWMNFHLKKAGYKKTVTNFS-SDVKDAEAYAYLLNVLAPE--HCDPATLEAKDPLER--AKLVLEQAEKMNCKRYLTA 89
                        90
                ....*....|....*...
gi 15236837 599 EDIVEVNQKMILILTASI 616
Cdd:cd21296  90 KDIVEGSANLNLAFVAQI 107
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
271-367 3.39e-03

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


Pssm-ID: 409069  Cd Length: 105  Bit Score: 37.63  E-value: 3.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 271 EKVLLKWMNFHLKKGGYKKTVSNFSaD--LKDAQAYAFLLNVLAPEHCDPA----TLDAKDPLERAELVLSHAERMNCKR 344
Cdd:cd21220   3 DADILAWANSKVREAGKSSPISSFK-DpsLSTGLFLLDLLAAIDPGAVDYDlvteGETDEEKEQNAKYAISLARKIGAVI 81
                        90       100
                ....*....|....*....|...
gi 15236837 345 YLTAEEIVEGSSTLNLAFVAQIF 367
Cdd:cd21220  82 FLLWEDIVEVKPKMILTFVASLM 104
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
275-368 3.41e-03

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


Pssm-ID: 409034  Cd Length: 98  Bit Score: 37.28  E-value: 3.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 275 LKWMNFHLKKGgykkTVSNFSADLKDAQAYAFLLNVLAPEHCDPATLDAKDPLERAELVLSHAERMNCKRYLTAEEIV-- 352
Cdd:cd21185   7 LRWVRQLLPDV----DVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEMAdp 82
                        90
                ....*....|....*.
gi 15236837 353 EGSSTLNLAFVAQIFH 368
Cdd:cd21185  83 EVEHLGIMAYAAQLQK 98
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
267-353 3.80e-03

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


Pssm-ID: 409078  Cd Length: 105  Bit Score: 37.37  E-value: 3.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 267 RLPPEKVLLKWMNFHLKKGgykkTVSNFSADLKDAQAYAFLLnvlapEHCDPATLDAKDPLERAElvlshaERMNCKRYL 346
Cdd:cd21229   1 KIPPKKLMLAWLQAVLPEL----KITNFSTDWNDGIALSALL-----DYCKPGLCPNWRKLDPSN------SLENCRRAM 65

                ....*...
gi 15236837 347 T-AEEIVE 353
Cdd:cd21229  66 DlAKREFN 73
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
160-235 4.69e-03

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: 37.28  E-value: 4.69e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236837 160 VKDGVLLCKLINVAVPGTIDERAIntKRVLNPWERNENHTLCLNSAKAVGCSVVnIGTQDLAEGRPHLVLGLISQL 235
Cdd:cd21218  40 LKDGEVYALLLHSLAPELCDKELV--LEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPEDIVSGNPRLNLAFVATL 112
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
277-354 5.26e-03

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. 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: 409062  Cd Length: 107  Bit Score: 37.28  E-value: 5.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 277 WMNFHLKKGGYKKTVSNFSADLKDAQAYAFLLNVLAPE-----HCDPATLDAKDplERAELVL----SHAERMnckRYLT 347
Cdd:cd21213   8 WVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEklpgiDWNPTTDAERK--ENVEKVLqfmaSKRIRM---HQTS 82

                ....*..
gi 15236837 348 AEEIVEG 354
Cdd:cd21213  83 AKDIVDG 89
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
144-236 5.54e-03

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409086  Cd Length: 118  Bit Score: 37.32  E-value: 5.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 144 KQFLPLDPHSNQLYELVKDGVLLCKLINVaVPGTIDERAINTKRvlnpWERNENHTLCLNSAKAVGCSVVNIGTQDLAEG 223
Cdd:cd21237  17 KHLMKVRKHINDLYEDLRDGHNLISLLEV-LSGVKLPREKGRMR----FHRLQNVQIALDFLKQRQVKLVNIRNDDITDG 91
                        90
                ....*....|...
gi 15236837 224 RPHLVLGLISQLI 236
Cdd:cd21237  92 NPKLTLGLIWTII 104
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
274-368 6.30e-03

second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409065  Cd Length: 115  Bit Score: 36.96  E-value: 6.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 274 LLKWMnfHLKKGGYKKT-VSNFSADLKDAQAYAFLLNVLAPEHCDPATLDAKDPLERAELVLSHAER-MNCKRYLTAEEI 351
Cdd:cd21216  15 LLLWC--QRKTAPYKNVnVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKhLDIPKMLDAEDI 92
                        90       100
                ....*....|....*....|...
gi 15236837 352 V------EGSStlnLAFVAQIFH 368
Cdd:cd21216  93 VntprpdERSV---MTYVSCYYH 112
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
148-184 6.58e-03

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: 37.23  E-value: 6.58e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15236837 148 PLDPHSNQLYELV---KDGVLLCKLINVAVPGTIDERAIN 184
Cdd:cd21201  21 RATQPNATVFDLAqalRDGVLLCQLLNRLSPGSVDDREIN 60
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
520-616 7.97e-03

second calponin homology (CH) domain found in the family of plastin; The plastin family includes 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. 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: 409144  Cd Length: 113  Bit Score: 36.87  E-value: 7.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 520 LSWANRKVRTMGRKLQIESF-KDKSLSSGLFFLnlLWAVEPRVVNWNLVTKGETDDEKRlnATYIVSVARKLGCSVFLLP 598
Cdd:cd21295  18 LRWVNYHLERAGCDRRIKNFsGDIKDSEAYTHL--LKQIAPKDAGVDTSALRESDLLQR--AELMLQNADKIGCRKFVTP 93
                        90
                ....*....|....*...
gi 15236837 599 EDIVEVNQKMILILTASI 616
Cdd:cd21295  94 KDVVTGNPKLNLAFVANL 111
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
125-236 9.28e-03

first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409084  Cd Length: 119  Bit Score: 36.54  E-value: 9.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236837 125 EKGPFVQHINRYLgddpflkqfLPLDPHSNQLYELVKDGVLLCKLINVAVPGTIDERAINTKrvlnpWERNENHTLCLNS 204
Cdd:cd21235   7 QKKTFTKWVNKHL---------IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDY 72
                        90       100       110
                ....*....|....*....|....*....|..
gi 15236837 205 AKAVGCSVVNIGTQDLAEGRPHLVLGLISQLI 236
Cdd:cd21235  73 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 104
 
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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