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Conserved domains on  [gi|1768535678|ref|XP_031286533|]
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fimbrin-1-like [Pistacia vera]

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 ...
391-503 3.43e-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: 252.42  E-value: 3.43e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 391 TSREERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPPIKMPFRKVENCNQVVRIGKQLKFSL 470
Cdd:cd21299     2 TSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFSL 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1768535678 471 VNVAGNDIVQGNKKLILAFLWQLMRYNMLQLLK 503
Cdd:cd21299    82 VNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
123-238 4.90e-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: 249.37  E-value: 4.90e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 123 SEKASYVAHINSYLGDDPFLKQFLPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLN 202
Cdd:cd21293     1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1768535678 203 SAKAIGCTVVNIGTQDLIEGRSHLVLGLISQIIKIQ 238
Cdd:cd21293    81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116
SAC6 super family cl26648
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
74-617 2.83e-77

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


The actual alignment was detected with superfamily member COG5069:

Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 261.41  E-value: 2.83e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678  74 DTSDEIGFEAFLRAYLNLQGRASTKLGNAKNSSSFLKAATTTL-LHTISESEKasYVAHINSYLGDDPFLKQFLPlDPAT 152
Cdd:COG5069    71 NVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLtIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDT 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 153 NDLFELAKDGVLLCKLINVAVPGTIDERAINTKR---VLNPWERNENHTLCLNSAKAIG-CTVVNIGTQDlieGRSHLVL 228
Cdd:COG5069   148 FDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKknkALNNFQAFENANKVIGIARLIGvEDIVNVSIPD---ERSIMTY 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 229 gLISQIIKIQLLA--DLNLKKTPQLVELVEDSSDveelMGLAPEKVLLKWMNFHLKKAGYKkPVTNFSSDLKDGEAYAYL 306
Cdd:COG5069   225 -VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEIILLRLLNLIHLKQANW-KVVNFSKDVSDGENYTDL 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 307 LNVLApEHCSPATLDTKDASERAKLVLDHAEKMDCKRYLTPKdiveGSTNLNLAFVAQIFHQRSGLTTdSKNVSFAEMMT 386
Cdd:COG5069   299 LNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQEP-LEEEEKPEIEE 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 387 DDVLTSREERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKV-SPGSVNWKHASKPPIK----MPFRKVENCNQVVR 461
Cdd:COG5069   373 FDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASgieeNRFKAFENENYAVD 452
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 462 IGKQLKFSLVNVAGNDIVQGNKkLILAFLWQLMRYNMLQLLKNLRSrsQGKEITDADILNWANNKVKSTGRTSQTESFKD 541
Cdd:COG5069   453 LGITEGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKK--DGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGD 529
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 542 KSLS-SGLFFLELLSSVEPRVVNWNLVTKGESDEEKRLNA-TYIIS--VARKLGCSIFLLPEDIMEVNQKM-ILTLTASI 616
Cdd:COG5069   530 PAGSvSGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESL 609

                  .
gi 1768535678 617 M 617
Cdd:COG5069   610 M 610
 
Name Accession Description Interval E-value
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
391-503 3.43e-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: 252.42  E-value: 3.43e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 391 TSREERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPPIKMPFRKVENCNQVVRIGKQLKFSL 470
Cdd:cd21299     2 TSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFSL 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1768535678 471 VNVAGNDIVQGNKKLILAFLWQLMRYNMLQLLK 503
Cdd:cd21299    82 VNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
123-238 4.90e-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: 249.37  E-value: 4.90e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 123 SEKASYVAHINSYLGDDPFLKQFLPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLN 202
Cdd:cd21293     1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1768535678 203 SAKAIGCTVVNIGTQDLIEGRSHLVLGLISQIIKIQ 238
Cdd:cd21293    81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
74-617 2.83e-77

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 261.41  E-value: 2.83e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678  74 DTSDEIGFEAFLRAYLNLQGRASTKLGNAKNSSSFLKAATTTL-LHTISESEKasYVAHINSYLGDDPFLKQFLPlDPAT 152
Cdd:COG5069    71 NVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLtIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDT 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 153 NDLFELAKDGVLLCKLINVAVPGTIDERAINTKR---VLNPWERNENHTLCLNSAKAIG-CTVVNIGTQDlieGRSHLVL 228
Cdd:COG5069   148 FDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKknkALNNFQAFENANKVIGIARLIGvEDIVNVSIPD---ERSIMTY 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 229 gLISQIIKIQLLA--DLNLKKTPQLVELVEDSSDveelMGLAPEKVLLKWMNFHLKKAGYKkPVTNFSSDLKDGEAYAYL 306
Cdd:COG5069   225 -VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEIILLRLLNLIHLKQANW-KVVNFSKDVSDGENYTDL 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 307 LNVLApEHCSPATLDTKDASERAKLVLDHAEKMDCKRYLTPKdiveGSTNLNLAFVAQIFHQRSGLTTdSKNVSFAEMMT 386
Cdd:COG5069   299 LNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQEP-LEEEEKPEIEE 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 387 DDVLTSREERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKV-SPGSVNWKHASKPPIK----MPFRKVENCNQVVR 461
Cdd:COG5069   373 FDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASgieeNRFKAFENENYAVD 452
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 462 IGKQLKFSLVNVAGNDIVQGNKkLILAFLWQLMRYNMLQLLKNLRSrsQGKEITDADILNWANNKVKSTGRTSQTESFKD 541
Cdd:COG5069   453 LGITEGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKK--DGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGD 529
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 542 KSLS-SGLFFLELLSSVEPRVVNWNLVTKGESDEEKRLNA-TYIIS--VARKLGCSIFLLPEDIMEVNQKM-ILTLTASI 616
Cdd:COG5069   530 PAGSvSGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESL 609

                  .
gi 1768535678 617 M 617
Cdd:COG5069   610 M 610
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
513-621 1.75e-69

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: 223.58  E-value: 1.75e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 513 EITDADILNWANNKVKSTGRTSQTESFKDKSLSSGLFFLELLSSVEPRVVNWNLVTKGESDEEKRLNATYIISVARKLGC 592
Cdd:cd21302     1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80
                          90       100
                  ....*....|....*....|....*....
gi 1768535678 593 SIFLLPEDIMEVNQKMILTLTASIMYWSL 621
Cdd:cd21302    81 SIFLLPEDIVEVNQKMILILTASIMYWSL 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
267-367 1.66e-24

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 98.51  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 267 LAPEKVLLKWMNFHLKKAGYKKPVTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTK--DASERAKLVLDHAE-KMDCKR 343
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEkKLGVPK 80
                          90       100
                  ....*....|....*....|....*
gi 1768535678 344 YL-TPKDIVEGSTNLNLAFVAQIFH 367
Cdd:pfam00307  81 VLiEPEDLVEGDNKSVLTYLASLFR 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
398-496 4.20e-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: 83.13  E-value: 4.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678  398 FRLWINSLGVATYC---NNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPpiKMPFRKVENCNQVVRIGKQLKFSLVNVA 474
Cdd:smart00033   3 LLRWVNSLLAEYDKppvTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 1768535678  475 GNDIVQGnKKLILAFLWQLMRY 496
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
271-366 2.84e-17

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: 77.74  E-value: 2.84e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678  271 KVLLKWMNFHLKKAGyKKPVTNFSSDLKDGEAYAYLLNVLAP----EHCSPATLDTKDASERAKLVLDHAEKMDCKR-YL 345
Cdd:smart00033   1 KTLLRWVNSLLAEYD-KPPVTNFSSDLKDGVALCALLNSLSPglvdKKKVAASLSRFKKIENINLALSFAEKLGGKVvLF 79
                           90       100
                   ....*....|....*....|.
gi 1768535678  346 TPKDIVEGStNLNLAFVAQIF 366
Cdd:smart00033  80 EPEDLVEGP-KLILGVIWTLI 99
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
394-498 1.11e-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: 76.17  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINSL----GVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHaskpPIKMPFRKVENCNQVVRIG-KQLKF 468
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK----LNKSEFDKLENINLALDVAeKKLGV 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1768535678 469 SLVNVAGNDIVQGNKKLILAFLWQLMRYNM 498
Cdd:pfam00307  79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
149-237 1.53e-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: 75.82  E-value: 1.53e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678  149 DPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKrvLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRsHLVL 228
Cdd:smart00033  16 KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFEPEDLVEGP-KLIL 92

                   ....*....
gi 1768535678  229 GLISQIIKI 237
Cdd:smart00033  93 GVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
122-236 3.13e-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: 75.02  E-value: 3.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 122 ESEKASYVAHINSYLGDDPflkqflpLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKrvlnPWERNENHTLCL 201
Cdd:pfam00307   1 LELEKELLRWINSHLAEYG-------PGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLAL 69
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1768535678 202 NSA-KAIGCTVVNIGTQDLIEGRSHLVLGLISQIIK 236
Cdd:pfam00307  70 DVAeKKLGVPKVLIEPEDLVEGDNKSVLTYLASLFR 105
 
Name Accession Description Interval E-value
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
391-503 3.43e-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: 252.42  E-value: 3.43e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 391 TSREERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPPIKMPFRKVENCNQVVRIGKQLKFSL 470
Cdd:cd21299     2 TSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFSL 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1768535678 471 VNVAGNDIVQGNKKLILAFLWQLMRYNMLQLLK 503
Cdd:cd21299    82 VNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
123-238 4.90e-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: 249.37  E-value: 4.90e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 123 SEKASYVAHINSYLGDDPFLKQFLPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLN 202
Cdd:cd21293     1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1768535678 203 SAKAIGCTVVNIGTQDLIEGRSHLVLGLISQIIKIQ 238
Cdd:cd21293    81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
74-617 2.83e-77

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 261.41  E-value: 2.83e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678  74 DTSDEIGFEAFLRAYLNLQGRASTKLGNAKNSSSFLKAATTTL-LHTISESEKasYVAHINSYLGDDPFLKQFLPlDPAT 152
Cdd:COG5069    71 NVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLtIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDT 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 153 NDLFELAKDGVLLCKLINVAVPGTIDERAINTKR---VLNPWERNENHTLCLNSAKAIG-CTVVNIGTQDlieGRSHLVL 228
Cdd:COG5069   148 FDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKknkALNNFQAFENANKVIGIARLIGvEDIVNVSIPD---ERSIMTY 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 229 gLISQIIKIQLLA--DLNLKKTPQLVELVEDSSDveelMGLAPEKVLLKWMNFHLKKAGYKkPVTNFSSDLKDGEAYAYL 306
Cdd:COG5069   225 -VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEIILLRLLNLIHLKQANW-KVVNFSKDVSDGENYTDL 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 307 LNVLApEHCSPATLDTKDASERAKLVLDHAEKMDCKRYLTPKdiveGSTNLNLAFVAQIFHQRSGLTTdSKNVSFAEMMT 386
Cdd:COG5069   299 LNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQEP-LEEEEKPEIEE 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 387 DDVLTSREERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKV-SPGSVNWKHASKPPIK----MPFRKVENCNQVVR 461
Cdd:COG5069   373 FDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASgieeNRFKAFENENYAVD 452
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 462 IGKQLKFSLVNVAGNDIVQGNKkLILAFLWQLMRYNMLQLLKNLRSrsQGKEITDADILNWANNKVKSTGRTSQTESFKD 541
Cdd:COG5069   453 LGITEGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKK--DGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGD 529
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 542 KSLS-SGLFFLELLSSVEPRVVNWNLVTKGESDEEKRLNA-TYIIS--VARKLGCSIFLLPEDIMEVNQKM-ILTLTASI 616
Cdd:COG5069   530 PAGSvSGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESL 609

                  .
gi 1768535678 617 M 617
Cdd:COG5069   610 M 610
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
513-621 1.75e-69

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: 223.58  E-value: 1.75e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 513 EITDADILNWANNKVKSTGRTSQTESFKDKSLSSGLFFLELLSSVEPRVVNWNLVTKGESDEEKRLNATYIISVARKLGC 592
Cdd:cd21302     1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80
                          90       100
                  ....*....|....*....|....*....
gi 1768535678 593 SIFLLPEDIMEVNQKMILTLTASIMYWSL 621
Cdd:cd21302    81 SIFLLPEDIVEVNQKMILILTASIMYWSL 109
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
260-367 2.59e-68

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: 220.47  E-value: 2.59e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 260 DVEELMGLAPEKVLLKWMNFHLKKAGYKKPVTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTKDASERAKLVLDHAEKM 339
Cdd:cd21296     2 DVEELLRLPPEKVLLKWMNFHLKKAGYKKTVTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEKM 81
                          90       100
                  ....*....|....*....|....*...
gi 1768535678 340 DCKRYLTPKDIVEGSTNLNLAFVAQIFH 367
Cdd:cd21296    82 NCKRYLTAKDIVEGSANLNLAFVAQIFH 109
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
392-502 3.17e-62

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: 204.44  E-value: 3.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 392 SREERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPPIKMPFRKVENCNQVVRIGKQLKFSLV 471
Cdd:cd21219     3 SREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKPLNKFKKVENCNYAVDLAKKLGFSLV 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1768535678 472 NVAGNDIVQGNKKLILAFLWQLMRYNMLQLL 502
Cdd:cd21219    83 GIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
102-245 1.49e-56

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: 190.18  E-value: 1.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 102 AKNSSSFLKAATTTllHTISESEKASYVAHINSYLGDDPFLKQFLPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERA 181
Cdd:cd21292     5 AKGGTSEASSEGTT--HSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDERA 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1768535678 182 INTKRvLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRSHLVLGLISQIIKIQLLADLNL 245
Cdd:cd21292    83 INKKK-LTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
123-236 1.42e-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: 186.24  E-value: 1.42e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 123 SEKASYVAHINSYLGDDPFLKQFLPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLN 202
Cdd:cd21217     1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKNIFEATENLNLALN 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1768535678 203 SAKAIGCTVVNIGTQDLIEGRSHLVLGLISQIIK 236
Cdd:cd21217    81 AAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
514-618 5.24e-52

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: 175.92  E-value: 5.24e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 514 ITDADILNWANNKVKSTGRTSQTESFKDKSLSSGLFFLELLSSVEPRVVNWNLVTKGESDEEKRLNATYIISVARKLGCS 593
Cdd:cd21220     1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLVTEGETDEEKEQNAKYAISLARKIGAV 80
                          90       100
                  ....*....|....*....|....*
gi 1768535678 594 IFLLPEDIMEVNQKMILTLTASIMY 618
Cdd:cd21220    81 IFLLWEDIVEVKPKMILTFVASLMA 105
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
118-245 1.28e-45

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: 159.82  E-value: 1.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 118 HTISESEKASYVAHINSYLGDDPFLKQFLPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKRvLNPWERNENH 197
Cdd:cd21323    19 HSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDERAINKKK-LTPFTISENL 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1768535678 198 TLCLNSAKAIGCTVVNIGTQDLIEGRSHLVLGLISQIIKIQLLADLNL 245
Cdd:cd21323    98 NLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
392-502 5.11e-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: 154.32  E-value: 5.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 392 SREERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPPIKMP--FRKVENCNQVVRIGKQLKFS 469
Cdd:cd21298     5 TREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGanMKKIENCNYAVELGKKLKFS 84
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1768535678 470 LVNVAGNDIVQGNKKLILAFLWQLMRYNMLQLL 502
Cdd:cd21298    85 LVGIGGKDIYDGNRTLTLALVWQLMRAYTLSIL 117
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
257-366 6.14e-43

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: 151.27  E-value: 6.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 257 DSSDVEELMGLAPEKVLLKWMNFHLKKAGYKKPVTNFSSDLKDGEAYAYLLNVLAPEHCSPAT--LDTKDASERAKLVLD 334
Cdd:cd21295     1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRRIKNFSGDIKDSEAYTHLLKQIAPKDAGVDTsaLRESDLLQRAELMLQ 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1768535678 335 HAEKMDCKRYLTPKDIVEGSTNLNLAFVAQIF 366
Cdd:cd21295    81 NADKIGCRKFVTPKDVVTGNPKLNLAFVANLF 112
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
118-236 2.23e-41

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: 147.21  E-value: 2.23e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 118 HTISESEKASYVAHINSYLGDDPFLKQFLPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTK----RVLNPWER 193
Cdd:cd21294     1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPprknKPLNNFQM 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1768535678 194 NENHTLCLNSAKAIGCTVVNIGTQDLIEGRSHLVLGLISQIIK 236
Cdd:cd21294    81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIR 123
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
393-502 2.68e-41

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: 146.80  E-value: 2.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 393 REERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPP---IKMPFRKVENCNQVVRIGKQLKFS 469
Cdd:cd21300     7 REARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaEISRFKAVENTNYAVELGKQLGFS 86
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1768535678 470 LVNVAGNDIVQGNKKLILAFLWQLMRYNMLQLL 502
Cdd:cd21300    87 LVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
260-367 3.05e-41

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: 146.29  E-value: 3.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 260 DVEELMGLAPEKVLLKWMNFHLKKAGY-KKPVTNFSSDLKDGEAYAYLLNVLAPEHCSPA----TLDTKDASERAKLVLD 334
Cdd:cd21218     2 TLESLLYLPPEEILLRWVNYHLKKAGPtKKRVTNFSSDLKDGEVYALLLHSLAPELCDKElvleVLSEEDLEKRAEKVLQ 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1768535678 335 HAEKMDCKRYLTPKDIVEGSTNLNLAFVAQIFH 367
Cdd:cd21218    82 AAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
511-617 2.76e-40

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: 143.72  E-value: 2.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 511 GKEITDADILNWANNKVKSTGRTSQTESFKDKSLSSGLFFLELLSSVEPRVVNWNLVTKGESDEEKRLNATYIISVARKL 590
Cdd:cd21303     1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLVTPGNTEDEAYLNAKLAISIARKL 80
                          90       100
                  ....*....|....*....|....*..
gi 1768535678 591 GCSIFLLPEDIMEVNQKMILTLTASIM 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 ...
118-247 5.70e-39

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: 141.35  E-value: 5.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 118 HTISESEKASYVAHINSYLGDDPFLKQFLPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKRvLNPWERNENH 197
Cdd:cd21325    19 HSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKK-LTPFIIQENL 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1768535678 198 TLCLNSAKAIGCTVVNIGTQDLIEGRSHLVLGLISQIIKIQLLADLNLKK 247
Cdd:cd21325    98 NLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSR 147
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
514-617 1.51e-38

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: 138.57  E-value: 1.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 514 ITDADILNWANNKVKSTGRTSQTESFKDKSLSSGLFFLELLSSVEPRVVNWNLVTKGESDEEKRLNATYIISVARKLGCS 593
Cdd:cd21301     1 ISDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLVLEGNSEEDKLSNAKYAISMARKIGAR 80
                          90       100
                  ....*....|....*....|....
gi 1768535678 594 IFLLPEDIMEVNQKMILTLTASIM 617
Cdd:cd21301    81 VYALPEDIVEVKPKMVMTVFACLM 104
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
117-245 2.60e-38

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: 139.37  E-value: 2.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 117 LHTISESEKASYVAHINSYLGDDPFLKQFLPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKRvLNPWERNEN 196
Cdd:cd21324    18 QHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKK-LTPFTIQEN 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1768535678 197 HTLCLNSAKAIGCTVVNIGTQDLIEGRSHLVLGLISQIIKIQLLADLNL 245
Cdd:cd21324    97 LNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
261-367 5.09e-38

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: 137.31  E-value: 5.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 261 VEELMGLAPEKVLLKWMNFHLKKAGYKKPVTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTKDASERAKLVLDHAEKMD 340
Cdd:cd21297     3 LEQFLRLPPEQILLRWFNYHLKAANWPRRVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDLLQRAEQVLQNAEKLD 82
                          90       100
                  ....*....|....*....|....*..
gi 1768535678 341 CKRYLTPKDIVEGSTNLNLAFVAQIFH 367
Cdd:cd21297    83 CRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
254-367 2.18e-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: 2.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 254 LVEDSSDVEELMGLAPEKVLLKWMNFHLKKAGYKKpVTNFSSDLKDGEAYAYLLNVLAPE---------HCSPATLDTKD 324
Cdd:cd21328     1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQK-INNFSSDIKDSRAYFHLLNQIAPKgqkegepriDINMSGFNEKD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1768535678 325 ASERAKLVLDHAEKMDCKRYLTPKDIVEGSTNLNLAFVAQIFH 367
Cdd:cd21328    80 DLKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
254-368 8.55e-30

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: 114.29  E-value: 8.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 254 LVEDSSDVEELMGLAPEKVLLKWMNFHLKKAGYKKpVTNFSSDLKDGEAYAYLLNVLAP---EHCSPAT------LDTKD 324
Cdd:cd21327     1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNK-INNFSSDIKDSKAYYHLLNQVAPkgdEEGIPAIvidmsgLREKD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1768535678 325 ASERAKLVLDHAEKMDCKRYLTPKDIVEGSTNLNLAFVAQIFHQ 368
Cdd:cd21327    80 DLKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNK 123
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
260-367 3.27e-29

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: 112.67  E-value: 3.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 260 DVEELMGLAPEKVLLKWMNFHLKKAGYKKpVTNFSSDLKDGEAYAYLLNVLAPE--------HCSPATLDTKDASERAKL 331
Cdd:cd21326     4 ELEELMKLSPEELLLRWVNYHLTNAGWQN-ISNFSQDIKDSRAYFHLLNQIAPKgdvfdeniEIDFSGFNEKNDLKRAEY 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1768535678 332 VLDHAEKMDCKRYLTPKDIVEGSTNLNLAFVAQIFH 367
Cdd:cd21326    83 MLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 118
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
392-502 3.61e-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: 109.30  E-value: 3.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 392 SREERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKVSPgSVNWKHASKPPIKM---PFRKVENCNQVVRIGK-QLK 467
Cdd:cd21329     5 SSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRV-PVDWGHVNKPPYPAlggNMKKIENCNYAVELGKnKAK 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1768535678 468 FSLVNVAGNDIVQGNKKLILAFLWQLMRYNMLQLL 502
Cdd:cd21329    84 FSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
509-617 9.65e-26

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: 102.38  E-value: 9.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 509 SQGKEITDADILNWANNKVKSTGRTSQTESFKDKSLSSGLFFLELLSSVEPRVVNWNLV-TKGESDEEKRLNATYIISVA 587
Cdd:cd21333     1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLkTEDLNDEEKLNNAKYAISMA 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1768535678 588 RKLGCSIFLLPEDIMEVNQKMILTLTASIM 617
Cdd:cd21333    81 RKIGARVYALPEDLVEVKPKMVMTVFACLM 110
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
514-617 2.29e-25

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: 101.12  E-value: 2.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 514 ITDADILNWANNKVKSTGRTSQTESFKDKSLSSGLFFLELLSSVEPRVVNWNLVTKGE-SDEEKRLNATYIISVARKLGC 592
Cdd:cd21334     1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNlTDDDKLDNAKYAVSMARKIGA 80
                          90       100
                  ....*....|....*....|....*
gi 1768535678 593 SIFLLPEDIMEVNQKMILTLTASIM 617
Cdd:cd21334    81 RVYALPEDLVEVKPKMVMTVFACLM 105
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
392-502 3.98e-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: 101.23  E-value: 3.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 392 SREERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKVSPgSVNWKHASKPP---IKMPFRKVENCNQVVRIGKQ-LK 467
Cdd:cd21331    21 TREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKV-PVDWNKVNKPPypkLGANMKKLENCNYAVELGKHpAK 99
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1768535678 468 FSLVNVAGNDIVQGNKKLILAFLWQLMRYNMLQLL 502
Cdd:cd21331   100 FSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
392-502 1.53e-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: 1.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 392 SREERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKVSPgSVNWKHASKPP---IKMPFRKVENCNQVVRIGK-QLK 467
Cdd:cd21330    12 TREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKV-PVDWNRVNKPPypkLGENMKKLENCNYAVELGKnKAK 90
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1768535678 468 FSLVNVAGNDIVQGNKKLILAFLWQLMRYNMLQLL 502
Cdd:cd21330    91 FSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 125
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
267-367 1.66e-24

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 98.51  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 267 LAPEKVLLKWMNFHLKKAGYKKPVTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTK--DASERAKLVLDHAE-KMDCKR 343
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEkKLGVPK 80
                          90       100
                  ....*....|....*....|....*
gi 1768535678 344 YL-TPKDIVEGSTNLNLAFVAQIFH 367
Cdd:pfam00307  81 VLiEPEDLVEGDNKSVLTYLASLFR 105
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
510-617 1.10e-23

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: 96.56  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 510 QGKEITDADILNWANNKVKSTGRTSQTESFKDKSLSSGLFFLELLSSVEPRVVNWNLVTKGE-SDEEKRLNATYIISVAR 588
Cdd:cd21332     4 EGEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDlSDADKLNNAKYAISVAR 83
                          90       100
                  ....*....|....*....|....*....
gi 1768535678 589 KLGCSIFLLPEDIMEVNQKMILTLTASIM 617
Cdd:cd21332    84 KIGARVYALPEDLVEVKPKMVMTVFACLM 112
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
398-496 4.20e-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: 83.13  E-value: 4.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678  398 FRLWINSLGVATYC---NNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPpiKMPFRKVENCNQVVRIGKQLKFSLVNVA 474
Cdd:smart00033   3 LLRWVNSLLAEYDKppvTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 1768535678  475 GNDIVQGnKKLILAFLWQLMRY 496
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
513-617 2.62e-17

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: 78.10  E-value: 2.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 513 EITDADILNWANNKVKSTGRTSQTESFKdKSLSSGLFFLELLSSVEPRVVNWNLVTKGEsdEEKRLNATYIISVAR-KLG 591
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKLNKSE--FDKLENINLALDVAEkKLG 77
                          90       100
                  ....*....|....*....|....*..
gi 1768535678 592 CSIFLL-PEDIMEVNQKMILTLTASIM 617
Cdd:pfam00307  78 VPKVLIePEDLVEGDNKSVLTYLASLF 104
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
271-366 2.84e-17

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: 77.74  E-value: 2.84e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678  271 KVLLKWMNFHLKKAGyKKPVTNFSSDLKDGEAYAYLLNVLAP----EHCSPATLDTKDASERAKLVLDHAEKMDCKR-YL 345
Cdd:smart00033   1 KTLLRWVNSLLAEYD-KPPVTNFSSDLKDGVALCALLNSLSPglvdKKKVAASLSRFKKIENINLALSFAEKLGGKVvLF 79
                           90       100
                   ....*....|....*....|.
gi 1768535678  346 TPKDIVEGStNLNLAFVAQIF 366
Cdd:smart00033  80 EPEDLVEGP-KLILGVIWTLI 99
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
518-619 6.36e-17

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: 76.59  E-value: 6.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678  518 DILNWANNKVKstGRTSQTESFKDKSLSSGLFFLELLSSVEPRVVNWNLVTKGESDEEKRLNATYIISVARKLGCSIFLL 597
Cdd:smart00033   2 TLLRWVNSLLA--EYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79
                           90       100
                   ....*....|....*....|...
gi 1768535678  598 -PEDIMEVNqKMILTLTASIMYW 619
Cdd:smart00033  80 ePEDLVEGP-KLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
394-498 1.11e-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: 76.17  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINSL----GVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHaskpPIKMPFRKVENCNQVVRIG-KQLKF 468
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK----LNKSEFDKLENINLALDVAeKKLGV 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1768535678 469 SLVNVAGNDIVQGNKKLILAFLWQLMRYNM 498
Cdd:pfam00307  79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
149-237 1.53e-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: 75.82  E-value: 1.53e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678  149 DPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKrvLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRsHLVL 228
Cdd:smart00033  16 KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFEPEDLVEGP-KLIL 92

                   ....*....
gi 1768535678  229 GLISQIIKI 237
Cdd:smart00033  93 GVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
122-236 3.13e-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: 75.02  E-value: 3.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 122 ESEKASYVAHINSYLGDDPflkqflpLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKrvlnPWERNENHTLCL 201
Cdd:pfam00307   1 LELEKELLRWINSHLAEYG-------PGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLAL 69
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1768535678 202 NSA-KAIGCTVVNIGTQDLIEGRSHLVLGLISQIIK 236
Cdd:pfam00307  70 DVAeKKLGVPKVLIEPEDLVEGDNKSVLTYLASLFR 105
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
412-495 7.51e-16

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: 74.15  E-value: 7.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 412 NNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPPIKMPFRKVENCNQVVRIGKQLKFSLVNVAGNDIVQGNKKLILAFLW 491
Cdd:cd21217    31 DDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKNIFEATENLNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLW 110

                  ....
gi 1768535678 492 QLMR 495
Cdd:cd21217   111 QIIR 114
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
125-236 1.17e-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: 73.14  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 125 KASYVAHINSYLGDDpflkqflpLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKrvlNPWERNENHTLCLNSA 204
Cdd:cd00014     1 EEELLKWINEVLGEE--------LPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPK---SPFKKRENINLFLNAC 69
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1768535678 205 KAIG-CTVVNIGTQDLIEGRS-HLVLGLISQIIK 236
Cdd:cd00014    70 KKLGlPELDLFEPEDLYEKGNlKKVLGTLWALAL 103
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
146-240 3.83e-14

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: 69.23  E-value: 3.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 146 LPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRSH 225
Cdd:cd21219    16 LGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKPLNKFKKVENCNYAVDLAKKLGFSLVGIGGKDIADGNRK 95
                          90
                  ....*....|....*
gi 1768535678 226 LVLGLISQIIKIQLL 240
Cdd:cd21219    96 LTLALVWQLMRYHVL 110
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
269-351 1.92e-10

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: 58.40  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 269 PEKVLLKWMNFHLkkAGYKkpVTNFSSDLKDGEAYAYLLNVLAPEHCSP-ATLDTKDASERAKLVLDHAE-KMDCKRYLT 346
Cdd:cd21184     2 GKSLLLEWVNSKI--PEYK--VKNFTTDWNDGKALAALVDALKPGLIPDnESLDKENPLENATKAMDIAEeELGIPKIIT 77

                  ....*
gi 1768535678 347 PKDIV 351
Cdd:cd21184    78 PEDMV 82
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
395-495 2.69e-10

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: 58.12  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 395 ERCFRLWINS-LGV--ATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHASKppiKMPFRKVENCNQVVRIGKQLKF-SL 470
Cdd:cd00014     1 EEELLKWINEvLGEelPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKP---KSPFKKRENINLFLNACKKLGLpEL 77
                          90       100
                  ....*....|....*....|....*.
gi 1768535678 471 VNVAGNDIVQ-GNKKLILAFLWQLMR 495
Cdd:cd00014    78 DLFEPEDLYEkGNLKKVLGTLWALAL 103
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
394-491 1.21e-09

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: 56.24  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINSLGVATYC---NNVFEDVRTGWILLEVLDKVSPGSVNWKHASkppikMPFRKVENCNQVVRIGKQLKFSL 470
Cdd:cd21186     3 QKKTFTKWINSQLSKANKppiKDLFEDLRDGTRLLALLEVLTGKKLKPEKGR-----MRVHHLNNVNRALQVLEQNNVKL 77
                          90       100
                  ....*....|....*....|.
gi 1768535678 471 VNVAGNDIVQGNKKLILAFLW 491
Cdd:cd21186    78 VNISSNDIVDGNPKLTLGLVW 98
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
394-494 1.55e-09

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: 55.87  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINS-LGVATY-CNNVFEDVRTGWILLEVLDKVSPGSVNwKHASKPpiKMPFRKVENCNQVVRIGKQLKFSLV 471
Cdd:cd21215     5 QKKTFTKWLNTkLSSRGLsITDLVTDLSDGVRLIQLLEIIGDESLG-RYNKNP--KMRVQKLENVNKALEFIKSRGVKLT 81
                          90       100
                  ....*....|....*....|...
gi 1768535678 472 NVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21215    82 NIGAEDIVDGNLKLILGLLWTLI 104
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
520-616 8.02e-09

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: 54.23  E-value: 8.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 520 LNWANNKVKSTGRTSQT-ESFkDKSLSSGLFFLELLSSVEPRVVNWNLVTKGESDEEKRLNATYIISVARKLGCSIFLLP 598
Cdd:cd21218    16 LRWVNYHLKKAGPTKKRvTNF-SSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYFLTP 94
                          90
                  ....*....|....*...
gi 1768535678 599 EDIMEVNQKMILTLTASI 616
Cdd:cd21218    95 EDIVSGNPRLNLAFVATL 112
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
256-351 1.67e-08

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: 53.25  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 256 EDSSDVEElmGLAPEKVLLKWMNFHLKKagykKPVTNFSSDLKDGEAYAYLLNVLAPEHCSP-ATLDTKDASERAKLVLD 334
Cdd:cd21315     6 DDGPDDGK--GPTPKQRLLGWIQSKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCPDwEDWDPKDAVKNAKEAMD 79
                          90
                  ....*....|....*...
gi 1768535678 335 HAEK-MDCKRYLTPKDIV 351
Cdd:cd21315    80 LAEDwLDVPQLIKPEEMV 97
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
270-353 1.73e-08

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: 52.73  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 270 EKVLLKWMNFHLKKAGyKKPVTNFSSDLKDGEAYAYLLNVLAPEHCS---PATLDTKDASERAKLVLDHAEK--MDCKRY 344
Cdd:cd00014     1 EEELLKWINEVLGEEL-PVSITDLFESLRDGVLLCKLINKLSPGSIPkinKKPKSPFKKRENINLFLNACKKlgLPELDL 79

                  ....*....
gi 1768535678 345 LTPKDIVEG 353
Cdd:cd00014    80 FEPEDLYEK 88
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
394-494 1.81e-08

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: 53.45  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINS--LGVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHAskppiKMPFRKVENCNQVVRIGKQLKFSLV 471
Cdd:cd21236    18 QKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKG-----RMRFHRLQNVQIALDYLKRRQVKLV 92
                          90       100
                  ....*....|....*....|...
gi 1768535678 472 NVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21236    93 NIRNDDITDGNPKLTLGLIWTII 115
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
161-235 2.29e-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: 52.67  E-value: 2.29e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1768535678 161 DGVLLCKLINVavpgtIDERAIN--TKRVLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRSHLVLGLISQII 235
Cdd:cd21227    33 DGVKLIALVEI-----LQGRKLGrvIKKPLNQHQKLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLI 104
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
394-494 3.27e-08

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: 53.11  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINS--LGVATYCNNVFEDVRTGWILLEVLDKVSPgsvnwKHASKPPI-KMPFRKVENCNQVVRIGKQLKFSL 470
Cdd:cd21318    39 QKKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLEVLSG-----EQLPKPTRgRMRIHSLENVDKALQFLKEQRVHL 113
                          90       100
                  ....*....|....*....|....
gi 1768535678 471 VNVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21318   114 ENVGSHDIVDGNHRLTLGLIWTII 137
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
389-495 4.73e-08

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: 52.06  E-value: 4.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 389 VLTSREERCFRLWINslgvaTYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPPIKM----PFRKVENCNQVVRIGK 464
Cdd:cd21294    18 VLAGDPDVGSRLPFP-----TDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPPRKNkplnNFQMIENNNIVINSAK 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1768535678 465 QLKFSLVNVAGNDIVQGNKKLILAFLWQLMR 495
Cdd:cd21294    93 AIGCSVVNIGAGDIIEGREHLILGLIWQIIR 123
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
146-244 5.90e-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: 51.73  E-value: 5.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 146 LPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRSH 225
Cdd:cd21299    16 LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFSLVNVAGNDIVQGNKK 95
                          90
                  ....*....|....*....
gi 1768535678 226 LVLGLISQIIKIQLLADLN 244
Cdd:cd21299    96 LILALLWQLMRYHMLQLLK 114
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
394-495 1.42e-07

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: 50.61  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINSLGVATYC---NNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPpiKMPFRKVENCNQVVR-IGKQLKFS 469
Cdd:cd21225     5 QIKAFTAWVNSVLEKRGIpkiSDLATDLSDGVRLIFFLELVSGKKFPKKFDLEP--KNRIQMIQNLHLAMLfIEEDLKIR 82
                          90       100
                  ....*....|....*....|....*.
gi 1768535678 470 LVNVAGNDIVQGNKKLILAFLWQLMR 495
Cdd:cd21225    83 VQGIGAEDFVDNNKKLILGLLWTLYR 108
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
146-243 2.47e-07

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: 50.11  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 146 LPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINTKRVLNPWER-----NENHTLCLnsAKAIGCTVVNIGTQDLI 220
Cdd:cd21300    19 LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPASAEISRfkaveNTNYAVEL--GKQLGFSLVGIQGADIT 96
                          90       100
                  ....*....|....*....|...
gi 1768535678 221 EGRSHLVLGLISQIIKIQLLADL 243
Cdd:cd21300    97 DGSRTLTLALVWQLMRFHITKTL 119
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
394-494 2.59e-07

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: 50.03  E-value: 2.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINS--LGVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHAskppiKMPFRKVENCNQVVRIGKQLKFSLV 471
Cdd:cd21237     7 QKKTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKG-----RMRFHRLQNVQIALDFLKQRQVKLV 81
                          90       100
                  ....*....|....*....|...
gi 1768535678 472 NVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21237    82 NIRNDDITDGNPKLTLGLIWTII 104
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
394-491 2.78e-07

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: 49.67  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINSLGVATYC--NNVFEDVRTGWILLEVLDKVSPgsvnwKHASKP-PIKMPFRKVENCNQVVRIGKQLKFSL 470
Cdd:cd21246    17 QKKTFTKWVNSHLARVGCriNDLYTDLRDGRMLIKLLEVLSG-----ERLPKPtKGKMRIHCLENVDKALQFLKEQRVHL 91
                          90       100
                  ....*....|....*....|.
gi 1768535678 471 VNVAGNDIVQGNKKLILAFLW 491
Cdd:cd21246    92 ENMGSHDIVDGNHRLTLGLIW 112
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
394-494 2.86e-07

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: 49.40  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINS--LGVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPpiKMPFRKVENCNQVVRIGKQLKFSLV 471
Cdd:cd21183     5 QANTFTRWCNEhlKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYNRRP--AFQQHYLENVSTALKFIEADHIKLV 82
                          90       100
                  ....*....|....*....|...
gi 1768535678 472 NVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21183    83 NIGSGDIVNGNIKLILGLIWTLI 105
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
394-494 3.41e-07

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: 49.24  E-value: 3.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINSLGVAT---YCNNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPpikmpFRKVENCNQVVRIGKQLKFSL 470
Cdd:cd21232     3 QKKTFTKWINARFSKSgkpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTR-----VHALNNVNRVLQVLHQNNVEL 77
                          90       100
                  ....*....|....*....|....
gi 1768535678 471 VNVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21232    78 VNIGGTDIVDGNHKLTLGLLWSII 101
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
153-236 4.63e-07

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: 48.94  E-value: 4.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 153 NDLFELAKDGVLLCKLINVAVPGTIDERAINTK-RVlnpwERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRSHLVLGLI 231
Cdd:cd21215    25 TDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKmRV----QKLENVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILGLL 100

                  ....*
gi 1768535678 232 SQIIK 236
Cdd:cd21215   101 WTLIL 105
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
394-491 5.90e-07

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: 48.55  E-value: 5.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINS--LGVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHAskppiKMPFRKVENCNQVVRIGKQLKFSLV 471
Cdd:cd21188     4 QKKTFTKWVNKhlIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERG-----RMRFHRLQNVQTALDFLKYRKIKLV 78
                          90       100
                  ....*....|....*....|
gi 1768535678 472 NVAGNDIVQGNKKLILAFLW 491
Cdd:cd21188    79 NIRAEDIVDGNPKLTLGLIW 98
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
394-494 7.89e-07

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: 48.48  E-value: 7.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINS--LGVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHAskppiKMPFRKVENCNQVVRIGKQLKFSLV 471
Cdd:cd21235     7 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 81
                          90       100
                  ....*....|....*....|...
gi 1768535678 472 NVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21235    82 NIRNDDIADGNPKLTLGLIWTII 104
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
269-351 1.03e-06

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: 47.76  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 269 PEKVLLKWMNFHLKKagykKPVTNFSSDLKDGEAYAYLLNVLAPEHCSPA-TLDTKDASERAKLVLDHAEK-MDCKRYLT 346
Cdd:cd21230     2 PKQRLLGWIQNKIPQ----LPITNFTTDWNDGRALGALVDSCAPGLCPDWeTWDPNDALENATEAMQLAEDwLGVPQLIT 77

                  ....*
gi 1768535678 347 PKDIV 351
Cdd:cd21230    78 PEEII 82
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
153-235 1.05e-06

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: 47.86  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 153 NDLFELAKDGVLLCKLINVaVPGTIDERAINtKRVLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRSHLVLGLIS 232
Cdd:cd21183    25 HDLATDFSDGLCLIALLEN-LSTRPLKRSYN-RRPAFQQHYLENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLIW 102

                  ...
gi 1768535678 233 QII 235
Cdd:cd21183   103 TLI 105
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
394-494 2.07e-06

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: 47.74  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINSLGVATYCN--NVFEDVRTGWILLEVLDKVSPgsvnwKHASKPPI-KMPFRKVENCNQVVRIGKQLKFSL 470
Cdd:cd21317    32 QKKTFTKWVNSHLARVTCRigDLYTDLRDGRMLIRLLEVLSG-----EQLPKPTKgRMRIHCLENVDKALQFLKEQKVHL 106
                          90       100
                  ....*....|....*....|....
gi 1768535678 471 VNVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21317   107 ENMGSHDIVDGNHRLTLGLIWTII 130
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
394-496 3.50e-06

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: 46.41  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINS----LGVATYCNNVFEDVRTGWILLEVLDKVSPGSVnwkHASKPPIKMPFRKVENCNQVVRIGKQLKFS 469
Cdd:cd21190     6 QKKTFTNWINShlakLSQPIVINDLFVDIKDGTALLRLLEVLSGQKL---PIESGRVLQRAHKLSNIRNALDFLTKRCIK 82
                          90       100
                  ....*....|....*....|....*..
gi 1768535678 470 LVNVAGNDIVQGNKKLILAFLWQLMRY 496
Cdd:cd21190    83 LVNINSTDIVDGKPSIVLGLIWTIILY 109
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
146-236 4.51e-06

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: 46.46  E-value: 4.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 146 LPLDPATNDLFELAKDGVLLCKLINVAVPGTIDERAINT--KRVLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGR 223
Cdd:cd21298    18 LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKpfKKLGANMKKIENCNYAVELGKKLKFSLVGIGGKDIYDGN 97
                          90
                  ....*....|...
gi 1768535678 224 SHLVLGLISQIIK 236
Cdd:cd21298    98 RTLTLALVWQLMR 110
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
124-235 5.36e-06

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: 45.83  E-value: 5.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 124 EKASYVAHINSYLgddpfLKQFLPLDpaTNDLFELAKDGVLLCKLINV----AVPGtidERAINTKRVlnPWERNENHTL 199
Cdd:cd21241     6 QKKTFTNWINSYL-----AKRKPPMK--VEDLFEDIKDGTKLLALLEVlsgeKLPC---EKGRRLKRV--HFLSNINTAL 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1768535678 200 CLNSAKAIgcTVVNIGTQDLIEGRSHLVLGLISQII 235
Cdd:cd21241    74 KFLESKKI--KLVNINPTDIVDGKPSIVLGLIWTII 107
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
394-494 6.64e-06

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: 45.56  E-value: 6.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINS--LGVATYCNNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPPIKMpfRKVENCNQVVRIGKQLKFSLV 471
Cdd:cd21228     5 QQNTFTRWCNEhlKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRPTFRQ--MKLENVSVALEFLERESIKLV 82
                          90       100
                  ....*....|....*....|...
gi 1768535678 472 NVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21228    83 SIDSSAIVDGNLKLILGLIWTLI 105
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
276-353 9.45e-06

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: 44.98  E-value: 9.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 276 WMNFHLKKAGYKKPVTNFSSDLKDGEAYAYLLNVLAPE-----HCSPATLdtKDASERAKLVLDHaekMDCKR----YLT 346
Cdd:cd21213     8 WVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEklpgiDWNPTTD--AERKENVEKVLQF---MASKRirmhQTS 82

                  ....*..
gi 1768535678 347 PKDIVEG 353
Cdd:cd21213    83 AKDIVDG 89
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
394-494 9.51e-06

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: 45.30  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINSLGVAT---YCNNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPpikmpFRKVENCNQVVRIGKQLKFSL 470
Cdd:cd21231     7 QKKTFTKWINAQFAKFgkpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTR-----VHALNNVNKALQVLQKNNVDL 81
                          90       100
                  ....*....|....*....|....
gi 1768535678 471 VNVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21231    82 VNIGSADIVDGNHKLTLGLIWSII 105
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
394-491 9.54e-06

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: 45.36  E-value: 9.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINSLGVATYC--NNVFEDVRTGWILLEVLDKVSPGSVnwkhaSKPPI-KMPFRKVENCNQVVRIGKQlKFSL 470
Cdd:cd21193    17 QKKTFTKWINSFLEKANLeiGDLFTDLSDGKLLLKLLEIISGEKL-----GKPNRgRLRVQKIENVNKALAFLKT-KVRL 90
                          90       100
                  ....*....|....*....|.
gi 1768535678 471 VNVAGNDIVQGNKKLILAFLW 491
Cdd:cd21193    91 ENIGAEDIVDGNPRLILGLIW 111
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
394-494 1.17e-05

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: 44.69  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINSL--GVATYCNNVFEDVRTGWILLEVLDKVSPgsvnwKHASKPP-IKMPFRKVENCNqvvrigKQLKF-- 468
Cdd:cd21214     6 QRKTFTAWCNSHlrKAGTQIENIEEDFRDGLKLMLLLEVISG-----ERLPKPErGKMRFHKIANVN------KALDFia 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 1768535678 469 ----SLVNVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21214    75 skgvKLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
265-351 1.96e-05

calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409048  Cd Length: 112  Bit Score: 44.27  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 265 MGLAPEKVLLKWMnfHLKKAGYKK-PVTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTKDASERAKLVLDHAEKMDCKR 343
Cdd:cd21199     5 YGGSKRNALLKWC--QEKTQGYKGiDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGIPT 82

                  ....*...
gi 1768535678 344 YLTPKDIV 351
Cdd:cd21199    83 TLTIDEMV 90
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
275-368 2.35e-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: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 275 KWMNFHLKKAGYKKPVTNFSSDLKDGEAYAYLLNVLAPEhCSPatldtkDASERAKLvldHAEKMD----CKRYL----- 345
Cdd:cd21212     7 DWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGE-KVP------GIHSRPKT---RAQKLEniqaCLQFLaalgv 76
                          90       100
                  ....*....|....*....|....*...
gi 1768535678 346 -----TPKDIVEGstnlNLAFVAQIFHQ 368
Cdd:cd21212    77 dvqgiTAEDIVDG----NLKAILGLFFS 100
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
411-494 3.32e-05

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: 43.73  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 411 CNNVFEDVRTGWILLEVLDKVSpgsVNWKHASK---PPIKMPfRKVENCNQVV----RIGKQLKFSLVNVAGNDIVQGNK 483
Cdd:cd21223    26 VTNLAVDLRDGVRLCRLVELLT---GDWSLLSKlrvPAISRL-QKLHNVEVALkalkEAGVLRGGDGGGITAKDIVDGHR 101
                          90
                  ....*....|.
gi 1768535678 484 KLILAFLWQLM 494
Cdd:cd21223   102 EKTLALLWRII 112
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
424-496 3.32e-05

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: 43.43  E-value: 3.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1768535678 424 LLEVLDKVSPGSVNwkhaSKPpiKMPFRKVENCNQVVRIGKQLKFSLVNVAGNDIVQGNKKLILAFLWQL-MRY 496
Cdd:cd21227    40 LVEILQGRKLGRVI----KKP--LNQHQKLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLiLRY 107
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
150-223 4.06e-05

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: 43.45  E-value: 4.06e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1768535678 150 PATNDLFELAKDGVLLCKLINVAVPGTIdeRAINTKRVlnPWERNENHTLCLNSAKAIGCTVVNI-GTQDLIEGR 223
Cdd:cd21207    23 DDGKDYEDVLKDGVILCKLINILKPGSV--KKINTSKM--AFKLMENIENFLTACKGYGVPKTDLfQTVDLYEKK 93
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
394-495 4.60e-05

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: 44.19  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINS-LGVATYC----------NNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPPIKmPFRKVENCNQVVRI 462
Cdd:cd21292    25 EKVAFVNWINKnLGDDPDCkhllpmdpntDDLFEKVKDGILLCKMINLSVPDTIDERAINKKKLT-VFTIHENLTLALNS 103
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1768535678 463 GKQLKFSLVNVAGNDIVQGNKKLILAFLWQLMR 495
Cdd:cd21292   104 ASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIR 136
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
124-235 6.41e-05

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: 42.94  E-value: 6.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 124 EKASYVAHINSYLGddpflKQFLPLdpATNDLFELAKDGVLLCKLINVAvpgTIDERAINTKRVLNPWERNEN--HTLCL 201
Cdd:cd21190     6 QKKTFTNWINSHLA-----KLSQPI--VINDLFVDIKDGTALLRLLEVL---SGQKLPIESGRVLQRAHKLSNirNALDF 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1768535678 202 NSAKAIgcTVVNIGTQDLIEGRSHLVLGLISQII 235
Cdd:cd21190    76 LTKRCI--KLVNINSTDIVDGKPSIVLGLIWTII 107
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
394-494 6.55e-05

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: 43.88  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINSLGVATYC--NNVFEDVRTGWILLEVLDKVSPgsvnwKHASKPPI-KMPFRKVENCNQVVRIGKQLKFSL 470
Cdd:cd21316    54 QKKTFTKWVNSHLARVSCriTDLYMDLRDGRMLIKLLEVLSG-----ERLPKPTKgRMRIHCLENVDKALQFLKEQRVHL 128
                          90       100
                  ....*....|....*....|....
gi 1768535678 471 VNVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21316   129 ENMGSHDIVDGNHRLTLGLIWTII 152
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
257-352 6.99e-05

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: 42.87  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 257 DSSDVEELMGLAPEKVLLKWMNFHLKKAgykkPVTNFSSDLKDGEAYAYLLNVLAPEHCspATLDTKDASE---RAKLVL 333
Cdd:cd21312     1 DEEEDEEAKKQTPKQRLLGWIQNKLPQL----PITNFSRDWQSGRALGALVDSCAPGLC--PDWDSWDASKpvtNAREAM 74
                          90       100
                  ....*....|....*....|
gi 1768535678 334 DHAEK-MDCKRYLTPKDIVE 352
Cdd:cd21312    75 QQADDwLGIPQVITPEEIVD 94
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
269-367 7.55e-05

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


Pssm-ID: 409075  Cd Length: 103  Bit Score: 42.45  E-value: 7.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 269 PEKVLLKWMNFHLKkaGYKKP-VTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTKDASERAKLVLDHAEK-MDCKRYLT 346
Cdd:cd21226     1 SEDGLLAWCRQTTE--GYDGVnITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLE 78
                          90       100
                  ....*....|....*....|..
gi 1768535678 347 PKDIVEGST-NLNLAFVAQIFH 367
Cdd:cd21226    79 AEDVMTGNPdERSIVLYTSLFY 100
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
394-496 8.06e-05

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: 42.57  E-value: 8.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWIN----SLGVATYCNNVFEDVRTGWILLEVLDKVSpgSVNWKHASKPPIKMPFRkVENCNQVVRIGKQLKFS 469
Cdd:cd21191     6 QKRTFTRWINlhleKCNPPLEVKDLFVDIQDGKILMALLEVLS--GQNLLQEYKPSSHRIFR-LNNIAKALKFLEDSNVK 82
                          90       100
                  ....*....|....*....|....*..
gi 1768535678 470 LVNVAGNDIVQGNKKLILAFLWQLMRY 496
Cdd:cd21191    83 LVSIDAAEIADGNPSLVLGLIWNIILF 109
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
371-499 9.14e-05

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: 43.11  E-value: 9.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 371 GLTTDSKNVSFAEMMTDDVLTSREERCFRLWIN-SLGVATYCNNV----------FEDVRTGWILLEVLDKVSPGSVNWK 439
Cdd:cd21323     2 GITAIGGTSAISSEGTQHSYSEEEKVAFVNWINkALEGDPDCKHVvpmnptdeslFKSLADGILLCKMINLSQPDTIDER 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 440 HASKPPIKmPFRKVENCNQVVRIGKQLKFSLVNVAGNDIVQGNKKLILAFLWQLMRYNML 499
Cdd:cd21323    82 AINKKKLT-PFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLF 140
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
270-366 1.06e-04

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: 41.87  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 270 EKVLLKWMNFHLKKAGYKKPVTNFSS-DLKDGEAYAYLLNVLAPEHCSPATL-DTKDASER---AKLVLDHAEKMDCKRY 344
Cdd:cd21220     3 DADILAWANSKVREAGKSSPISSFKDpSLSTGLFLLDLLAAIDPGAVDYDLVtEGETDEEKeqnAKYAISLARKIGAVIF 82
                          90       100
                  ....*....|....*....|..
gi 1768535678 345 LTPKDIVEGSTNLNLAFVAQIF 366
Cdd:cd21220    83 LLWEDIVEVKPKMILTFVASLM 104
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
269-373 1.44e-04

calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409047  Cd Length: 105  Bit Score: 41.64  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 269 PEKVLLKWMNFHLKkaGYKK-PVTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTKDASERAKLVLDHAEKMDCKRYLTP 347
Cdd:cd21198     2 SGQDLLEWCQEVTK--GYRGvKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDP 79
                          90       100
                  ....*....|....*....|....*.
gi 1768535678 348 KDIVEGSTNLNLAFVAQIFHQRSGLT 373
Cdd:cd21198    80 ADMVLLSVPDKLSVMTYLHQIRAHFT 105
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
519-616 1.95e-04

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: 41.88  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 519 ILNWANNKVKSTGrTSQTESFKDKSLSSGLFFlELLSSVEPR-------VVNWNLVTKGESDEEKRlnATYIISVARKLG 591
Cdd:cd21328    20 LLRWANFHLENAG-WQKINNFSSDIKDSRAYF-HLLNQIAPKgqkegepRIDINMSGFNEKDDLKR--AEYMLQQADKLG 95
                          90       100
                  ....*....|....*....|....*
gi 1768535678 592 CSIFLLPEDIMEVNQKMILTLTASI 616
Cdd:cd21328    96 CRQFVTPADVVSGNPKLNLAFVANL 120
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
147-221 1.98e-04

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: 41.47  E-value: 1.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1768535678 147 PLDPATNDLFELA---KDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLNSAkaigCTVVNIGTQDLIE 221
Cdd:cd21201    21 RATQPNATVFDLAqalRDGVLLCQLLNRLSPGSVDDREINLRPQMSQFLCLKNIRTFLQAC----RTVFGLRSADLFE 94
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
266-366 2.56e-04

calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409106  Cd Length: 112  Bit Score: 41.17  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 266 GLAPEKVLLKWMnfHLKKAGYKK-PVTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTKDASERAKLVLDHAEKMDCKRY 344
Cdd:cd21257     6 GGSKRNALLKWC--QKKTEGYPNiDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGIKPS 83
                          90       100
                  ....*....|....*....|....*
gi 1768535678 345 LTPKDIVEGST---NLNLAFVAQIF 366
Cdd:cd21257    84 LELSEMMYTDRpdwQSVMQYVAQIY 108
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
261-367 2.86e-04

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: 41.19  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 261 VEELMglAPEKVLLkWMnfHLKKAGYKK-PVTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTKDASERAKLVLDHAEK- 338
Cdd:cd21216     6 VEELS--AKEGLLL-WC--QRKTAPYKNvNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKh 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1768535678 339 MDCKRYLTPKDIV------EGSTnlnLAFVAQIFH 367
Cdd:cd21216    81 LDIPKMLDAEDIVntprpdERSV---MTYVSCYYH 112
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
122-235 3.37e-04

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: 40.97  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 122 ESEKASYVAHINSYLGDDPflkqflplDPAT-NDLFELAKDGVLLCKLINVAVPGTID-ERAINTKRvlnpWERNENHTL 199
Cdd:cd21242     4 QTQKRTFTNWINSQLAKHS--------PPSVvSDLFTDIQDGHRLLDLLEVLSGQQLPrEKGHNVFQ----CRSNIETAL 71
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1768535678 200 CLNSAKAIgcTVVNIGTQDLIEGRSHLVLGLISQII 235
Cdd:cd21242    72 SFLKNKSI--KLINIHVPDIIEGKPSIILGLIWTII 105
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
394-494 3.46e-04

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: 40.97  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINSLGVATYC----NNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPpikmpFRKVENCNQVVRIGKQLKFS 469
Cdd:cd21242     6 QKRTFTNWINSQLAKHSPpsvvSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNV-----FQCRSNIETALSFLKNKSIK 80
                          90       100
                  ....*....|....*....|....*
gi 1768535678 470 LVNVAGNDIVQGNKKLILAFLWQLM 494
Cdd:cd21242    81 LINIHVPDIIEGKPSIILGLIWTII 105
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
266-351 3.69e-04

calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409105  Cd Length: 119  Bit Score: 40.83  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 266 GLAPEKVLLKWMnfHLKKAGYKK-PVTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTKDASERAKLVLDHAEKMDCKRY 344
Cdd:cd21256    12 GGSKRNALLKWC--QKKTEGYQNiDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAESVGIKST 89

                  ....*..
gi 1768535678 345 LTPKDIV 351
Cdd:cd21256    90 LDINEMV 96
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
271-310 4.83e-04

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: 40.06  E-value: 4.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1768535678 271 KVLLKWMNFHLKKAGyKKPVTNFSSDLKDGEAYAYLLNVL 310
Cdd:cd21186     5 KTFTKWINSQLSKAN-KPPIKDLFEDLRDGTRLLALLEVL 43
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
271-314 5.39e-04

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: 40.08  E-value: 5.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1768535678 271 KVLLKWMNFHLKKAGykKPVTNFSSDLKDGEAYAYLLNVLAPEH 314
Cdd:cd21188     6 KTFTKWVNKHLIKAR--RRVVDLFEDLRDGHNLISLLEVLSGES 47
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
274-367 5.66e-04

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: 39.98  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 274 LKWMNFHLKKAgykkPVTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTKDASERAKLVLDHAEKMDCKRYLTPKDIVEG 353
Cdd:cd21185     7 LRWVRQLLPDV----DVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEMADP 82
                          90
                  ....*....|....*.
gi 1768535678 354 STN-LN-LAFVAQIFH 367
Cdd:cd21185    83 EVEhLGiMAYAAQLQK 98
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
153-208 6.08e-04

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: 40.40  E-value: 6.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1768535678 153 NDLF-ELAKDGVLLCKLINVAVPGTIdeRAINTKRvlNPWERNENHTLCLNSAKAIG 208
Cdd:cd21208    19 SDDFrESLEDGILLCELINAIKPGSI--KKINRLP--TPIAGLDNLNLFLKACEDLG 71
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
270-351 7.22e-04

calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409110  Cd Length: 107  Bit Score: 39.95  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 270 EKVLLKWMnfHLKKAGYKK-PVTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTKDASERAKLVLDHAEKM-DCKRYLTP 347
Cdd:cd21261     3 KQILLEWC--RSKTIGYKNiDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80

                  ....
gi 1768535678 348 KDIV 351
Cdd:cd21261    81 EDMM 84
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
273-365 1.76e-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: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 273 LLKWMNFHLKKAGYKKPVTNF-SSDLKDGEAYAYLLNVLAPEHC-----SPATLDtKDASERAKLVLDHAEKMDCKRYLT 346
Cdd:cd21303     9 MVKWANDMVAKGGKNSSIRSFkDPSLSTGHFFLDVLNGLKSGYVdydlvTPGNTE-DEAYLNAKLAISIARKLGALIFLV 87
                          90
                  ....*....|....*....
gi 1768535678 347 PKDIVEGSTNLNLAFVAQI 365
Cdd:cd21303    88 PEDIVEVRPRLVLTFIGSL 106
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
412-499 2.33e-03

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: 39.27  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 412 NNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPPIkMPFRKVENCNQVVRIGKQLKFSLVNVAGNDIVQGNKKLILAFLW 491
Cdd:cd21325    54 DDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKL-TPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLW 132

                  ....*...
gi 1768535678 492 QLMRYNML 499
Cdd:cd21325   133 QIIKIGLF 140
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
269-350 2.73e-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: 38.14  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 269 PEKVLLKWMNFHLKKAGykkpVTNFSSDLKDGEAYAYLLnvlapEHCSPAT------LDTKDASERAKLVLDHAE-KMDC 341
Cdd:cd21229     4 PKKLMLAWLQAVLPELK----ITNFSTDWNDGIALSALL-----DYCKPGLcpnwrkLDPSNSLENCRRAMDLAKrEFNI 74

                  ....*....
gi 1768535678 342 KRYLTPKDI 350
Cdd:cd21229    75 PMVLSPEDL 83
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
124-234 2.88e-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: 37.95  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 124 EKASYVAHINSYLgddpflkQFLPLDPATNDLFELAKDGVLLCKLINVAVPGTIDerAINtKRVLNPWERNENHTLCLNS 203
Cdd:cd21212     1 EIEIYTDWANHYL-------EKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVP--GIH-SRPKTRAQKLENIQACLQF 70
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1768535678 204 AKAIGCTVVNIGTQDLIEGRSHLVLGLISQI 234
Cdd:cd21212    71 LAALGVDVQGITAEDIVDGNLKAILGLFFSL 101
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
412-499 3.30e-03

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: 38.84  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 412 NNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPPIKmPFRKVENCNQVVRIGKQLKFSLVNVAGNDIVQGNKKLILAFLW 491
Cdd:cd21324    54 DDLFKAVGDGIVLCKMINFSVPDTIDERTINKKKLT-PFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLW 132

                  ....*...
gi 1768535678 492 QLMRYNML 499
Cdd:cd21324   133 QVIKIGLF 140
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
394-496 4.13e-03

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: 37.74  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 394 EERCFRLWINS--------LGVatycNNVFEDVRTGWILLEVLDKVSpGSvnwkhaskppiKMPFRK---------VENC 456
Cdd:cd21241     6 QKKTFTNWINSylakrkppMKV----EDLFEDIKDGTKLLALLEVLS-GE-----------KLPCEKgrrlkrvhfLSNI 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1768535678 457 NQVVRIGKQLKFSLVNVAGNDIVQGNKKLILAFLWQLMRY 496
Cdd:cd21241    70 NTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILY 109
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
268-352 4.32e-03

calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409188  Cd Length: 105  Bit Score: 37.65  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 268 APEKvLLKWMNFHLkkAGYKK-PVTNFSSDLKDGEAYAYLLNVLAPEHCSPATLDTKDASERAKLVLDHAEK-MDCKRYL 345
Cdd:cd22198     1 RPEE-LLSWCQEQT--EGYRGvKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVM 77

                  ....*..
gi 1768535678 346 TPKDIVE 352
Cdd:cd22198    78 TGQEMAS 84
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
412-495 4.73e-03

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: 37.51  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 412 NNVFEDVRTGWILLEVLDKVSPGSVNWKHASKPPIKMPFRKVENCNQVVRIGKQLKFSLVNVAGNDIVQGNKKLILAFLW 491
Cdd:cd21293    31 NDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLNSAKAIGCSVVNIGTQDLAEGRPHLVLGLIS 110

                  ....
gi 1768535678 492 QLMR 495
Cdd:cd21293   111 QIIK 114
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
124-235 4.95e-03

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: 37.66  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 124 EKASYVAHINSYLGDDPFlkqflpldpATNDLFELAKDGVLLCKLINVaVPGTIDERAINTK-RVlnpwERNENHTLCLN 202
Cdd:cd21193    17 QKKTFTKWINSFLEKANL---------EIGDLFTDLSDGKLLLKLLEI-ISGEKLGKPNRGRlRV----QKIENVNKALA 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1768535678 203 SAKAiGCTVVNIGTQDLIEGRSHLVLGLISQII 235
Cdd:cd21193    83 FLKT-KVRLENIGAEDIVDGNPRLILGLIWTII 114
CH_CNN2 cd21283
calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral ...
160-248 6.08e-03

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


Pssm-ID: 409132 [Multi-domain]  Cd Length: 109  Bit Score: 37.22  E-value: 6.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768535678 160 KDGVLLCKLINVAVPGTIdeRAINTKRvlNPWERNENHTlclNSAKAIgcTVVNIGTQDLIEGRSHLVLGLISQiIKIQL 239
Cdd:cd21283    29 KDGVILCELMNKLQPGSV--PKINRSM--QNWHQLENLS---NFIKAM--VSYGMKPVDLFEANDLFESGNMTQ-VQVSL 98

                  ....*....
gi 1768535678 240 LADLNLKKT 248
Cdd:cd21283    99 LALAGMAKT 107
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
395-436 8.37e-03

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


Pssm-ID: 409131 [Multi-domain]  Cd Length: 108  Bit Score: 36.78  E-value: 8.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1768535678 395 ERCFRLWINSLGVATYCNNVFEDVRTGWILLEVLDKVSPGSV 436
Cdd:cd21282     5 EEELRVWIEGVTGRRIGDNFMDGLKDGVILCELINKLQPGSV 46
 
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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