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Conserved domains on  [gi|2274899071|emb|CAH8277121|]
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unnamed protein product [Arabidopsis lyrata]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
390-503 6.25e-81

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: 252.04  E-value: 6.25e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 390 ETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNEVIKIGKDLRFS 469
Cdd:cd21299     1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFS 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2274899071 470 LVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLLR 503
Cdd:cd21299    81 LVNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
123-238 6.49e-80

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: 6.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 123 SEKASYVSHINNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLN 202
Cdd:cd21293     1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2274899071 203 SAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQ 238
Cdd:cd21293    81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116
SAC6 super family cl26648
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
74-611 9.13e-73

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: 247.16  E-value: 9.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071  74 NADEEVDFETFLRAFL-NVQARGVEKTGGSKGSSSFLKTSTTTVHHAINESEKasYVSHINNYLRDDPFLKSYLPiDPAT 152
Cdd:COG5069    71 NVSGRLEFIKGKGVKLfNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDT 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 153 NAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKT---LNPWERNENLTLGLNSAKAIG-CTVVNIGTQDiaeGRPYLVL 228
Cdd:COG5069   148 FDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKnkaLNNFQAFENANKVIGIARLIGvEDIVNVSIPD---ERSIMTY 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 229 gLISQIIKIQMLA--DLNFKKTPSLFQLVDDTQDaeelMGLAPEKVLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYL 306
Cdd:COG5069   225 -VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEIILLRLLNLIHLKQANWK-VVNFSKDVSDGENYTDL 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 307 LNALAPEHSTHVaLETKDPTERAKKVLEQAEKLDCKRYLSPKdivdGSANLNLAFVAQIFQHRNGLTVDDSkTSFAEMMT 386
Cdd:COG5069   299 LNQLNALCSRAP-LETTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQEPLEE-EEKPEIEE 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 387 DDVETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKV-SPGSVNWKHANKPPIK----MPFKKVENCNEVIK 461
Cdd:COG5069   373 FDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASgieeNRFKAFENENYAVD 452
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 462 IGKDLRFSLVNVAGNDIVQGNkKLLLAFLWQLMRYTMLQLLRNLRshSQGKEITDVDILNWANRKVKRGGRTSQADSFRD 541
Cdd:COG5069   453 LGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHVLK--KDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGD 529
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274899071 542 KNLS-SGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNA-TYIIS--VARKLGCSIFLLPEDIIEVNQKMMLI 611
Cdd:COG5069   530 PAGSvSGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSLAISskILRSLGAIIKFLPEDINGVRPRLDVL 603
 
Name Accession Description Interval E-value
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
390-503 6.25e-81

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: 252.04  E-value: 6.25e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 390 ETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNEVIKIGKDLRFS 469
Cdd:cd21299     1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFS 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2274899071 470 LVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLLR 503
Cdd:cd21299    81 LVNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
123-238 6.49e-80

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: 6.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 123 SEKASYVSHINNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLN 202
Cdd:cd21293     1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2274899071 203 SAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQ 238
Cdd:cd21293    81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
74-611 9.13e-73

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 247.16  E-value: 9.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071  74 NADEEVDFETFLRAFL-NVQARGVEKTGGSKGSSSFLKTSTTTVHHAINESEKasYVSHINNYLRDDPFLKSYLPiDPAT 152
Cdd:COG5069    71 NVSGRLEFIKGKGVKLfNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDT 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 153 NAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKT---LNPWERNENLTLGLNSAKAIG-CTVVNIGTQDiaeGRPYLVL 228
Cdd:COG5069   148 FDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKnkaLNNFQAFENANKVIGIARLIGvEDIVNVSIPD---ERSIMTY 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 229 gLISQIIKIQMLA--DLNFKKTPSLFQLVDDTQDaeelMGLAPEKVLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYL 306
Cdd:COG5069   225 -VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEIILLRLLNLIHLKQANWK-VVNFSKDVSDGENYTDL 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 307 LNALAPEHSTHVaLETKDPTERAKKVLEQAEKLDCKRYLSPKdivdGSANLNLAFVAQIFQHRNGLTVDDSkTSFAEMMT 386
Cdd:COG5069   299 LNQLNALCSRAP-LETTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQEPLEE-EEKPEIEE 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 387 DDVETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKV-SPGSVNWKHANKPPIK----MPFKKVENCNEVIK 461
Cdd:COG5069   373 FDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASgieeNRFKAFENENYAVD 452
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 462 IGKDLRFSLVNVAGNDIVQGNkKLLLAFLWQLMRYTMLQLLRNLRshSQGKEITDVDILNWANRKVKRGGRTSQADSFRD 541
Cdd:COG5069   453 LGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHVLK--KDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGD 529
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274899071 542 KNLS-SGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNA-TYIIS--VARKLGCSIFLLPEDIIEVNQKMMLI 611
Cdd:COG5069   530 PAGSvSGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSLAISskILRSLGAIIKFLPEDINGVRPRLDVL 603
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
513-621 6.45e-71

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: 225.51  E-value: 6.45e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 513 EITDVDILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGC 592
Cdd:cd21302     1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80
                          90       100
                  ....*....|....*....|....*....
gi 2274899071 593 SIFLLPEDIIEVNQKMMLILAASIMYWSL 621
Cdd:cd21302    81 SIFLLPEDIVEVNQKMILILTASIMYWSL 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
267-371 2.70e-22

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 92.35  E-value: 2.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 267 LAPEKVLLKWMNFHLKKAGYEKQVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETK--DPTERAKKVLEQAE-KLDCKR 343
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEkKLGVPK 80
                          90       100
                  ....*....|....*....|....*....
gi 2274899071 344 YLS-PKDIVDGSANLNLAFVAQIFQHRNG 371
Cdd:pfam00307  81 VLIePEDLVEGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
398-496 3.70e-20

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 85.83  E-value: 3.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071  398 FRLWINSLG---TATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpiKMPFKKVENCNEVIKIGKDLRFSLVNVA 474
Cdd:smart00033   3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 2274899071  475 GNDIVQGnKKLLLAFLWQLMRY 496
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
394-496 2.95e-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: 77.71  E-value: 2.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINSL----GTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpikmPFKKVENCNEVIKIG-KDLRF 468
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLALDVAeKKLGV 78
                          90       100
                  ....*....|....*....|....*...
gi 2274899071 469 SLVNVAGNDIVQGNKKLLLAFLWQLMRY 496
Cdd:pfam00307  79 PKVLIEPEDLVEGDNKSVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
148-237 5.88e-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: 5.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071  148 IDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKtlNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPyLV 227
Cdd:smart00033  15 DKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL--SRFKKIENINLALSFAEKLGGKVVLFEPEDLVEGPK-LI 91
                           90
                   ....*....|
gi 2274899071  228 LGLISQIIKI 237
Cdd:smart00033  92 LGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
142-236 1.00e-15

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 73.47  E-value: 1.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 142 LKSYLPIDPATNaFFDLVKDGVLLCKLINVAVPGTIDERAINTKktlnPWERNENLTLGLNSA-KAIGCTVVNIGTQDIA 220
Cdd:pfam00307  15 LAEYGPGVRVTN-FTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLALDVAeKKLGVPKVLIEPEDLV 89
                          90
                  ....*....|....*.
gi 2274899071 221 EGRPYLVLGLISQIIK 236
Cdd:pfam00307  90 EGDNKSVLTYLASLFR 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
271-368 8.91e-15

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: 70.42  E-value: 8.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071  271 KVLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETK----DPTERAKKVLEQAEKLDCKR-YL 345
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVvLF 79
                           90       100
                   ....*....|....*....|...
gi 2274899071  346 SPKDIVDGSaNLNLAFVAQIFQH 368
Cdd:smart00033  80 EPEDLVEGP-KLILGVIWTLISL 101
SCP1 COG5199
Calponin [Cytoskeleton];
391-467 5.17e-03

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 38.36  E-value: 5.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274899071 391 TSREERCFRLWI-NSLGTATYVNNVFED-LRNGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNEVIKIGKDLR 467
Cdd:COG5199    11 MDKQQKEVTLWIeTVLGEKFEPPGDLLSlLKDGVRLCRILNEASPLDIKYKES-----KMPFVQMENISSFINGLKKLR 84
 
Name Accession Description Interval E-value
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
390-503 6.25e-81

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: 252.04  E-value: 6.25e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 390 ETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNEVIKIGKDLRFS 469
Cdd:cd21299     1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFS 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2274899071 470 LVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLLR 503
Cdd:cd21299    81 LVNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
123-238 6.49e-80

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: 6.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 123 SEKASYVSHINNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLN 202
Cdd:cd21293     1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2274899071 203 SAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQ 238
Cdd:cd21293    81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
74-611 9.13e-73

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 247.16  E-value: 9.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071  74 NADEEVDFETFLRAFL-NVQARGVEKTGGSKGSSSFLKTSTTTVHHAINESEKasYVSHINNYLRDDPFLKSYLPiDPAT 152
Cdd:COG5069    71 NVSGRLEFIKGKGVKLfNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDT 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 153 NAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKT---LNPWERNENLTLGLNSAKAIG-CTVVNIGTQDiaeGRPYLVL 228
Cdd:COG5069   148 FDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKnkaLNNFQAFENANKVIGIARLIGvEDIVNVSIPD---ERSIMTY 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 229 gLISQIIKIQMLA--DLNFKKTPSLFQLVDDTQDaeelMGLAPEKVLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYL 306
Cdd:COG5069   225 -VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEIILLRLLNLIHLKQANWK-VVNFSKDVSDGENYTDL 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 307 LNALAPEHSTHVaLETKDPTERAKKVLEQAEKLDCKRYLSPKdivdGSANLNLAFVAQIFQHRNGLTVDDSkTSFAEMMT 386
Cdd:COG5069   299 LNQLNALCSRAP-LETTDLHSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQEPLEE-EEKPEIEE 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 387 DDVETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKV-SPGSVNWKHANKPPIK----MPFKKVENCNEVIK 461
Cdd:COG5069   373 FDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASgieeNRFKAFENENYAVD 452
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 462 IGKDLRFSLVNVAGNDIVQGNkKLLLAFLWQLMRYTMLQLLRNLRshSQGKEITDVDILNWANRKVKRGGRTSQADSFRD 541
Cdd:COG5069   453 LGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHVLK--KDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGD 529
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274899071 542 KNLS-SGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNA-TYIIS--VARKLGCSIFLLPEDIIEVNQKMMLI 611
Cdd:COG5069   530 PAGSvSGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSLAISskILRSLGAIIKFLPEDINGVRPRLDVL 603
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
513-621 6.45e-71

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: 225.51  E-value: 6.45e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 513 EITDVDILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGC 592
Cdd:cd21302     1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80
                          90       100
                  ....*....|....*....|....*....
gi 2274899071 593 SIFLLPEDIIEVNQKMMLILAASIMYWSL 621
Cdd:cd21302    81 SIFLLPEDIVEVNQKMILILTASIMYWSL 109
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
259-367 1.14e-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: 219.70  E-value: 1.14e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 259 QDAEELMGLAPEKVLLKWMNFHLKKAGYEKQVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEK 338
Cdd:cd21296     1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKTVTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEK 80
                          90       100
                  ....*....|....*....|....*....
gi 2274899071 339 LDCKRYLSPKDIVDGSANLNLAFVAQIFQ 367
Cdd:cd21296    81 MNCKRYLTAKDIVEGSANLNLAFVAQIFH 109
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
390-502 3.34e-60

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: 197.12  E-value: 3.34e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 390 ETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNEVIKIGKDLRFS 469
Cdd:cd21219     1 EGSREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKPLNKFKKVENCNYAVDLAKKLGFS 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2274899071 470 LVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLL 502
Cdd:cd21219    81 LVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
95-244 1.69e-58

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: 194.04  E-value: 1.69e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071  95 GVEKTGGSKGSSSflkTSTTtvhHAINESEKASYVSHINNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVP 174
Cdd:cd21292     2 GIDAKGGTSEASS---EGTT---HSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVP 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 175 GTIDERAINTKKtLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQMLADLN 244
Cdd:cd21292    76 DTIDERAINKKK-LTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIE 144
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
123-236 5.66e-56

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: 185.86  E-value: 5.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 123 SEKASYVSHINNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLN 202
Cdd:cd21217     1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKNIFEATENLNLALN 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2274899071 203 SAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIK 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 1.17e-49

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: 168.60  E-value: 1.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 514 ITDVDILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGCS 593
Cdd:cd21220     1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLVTEGETDEEKEQNAKYAISLARKIGAV 80
                          90       100
                  ....*....|....*....|....*
gi 2274899071 594 IFLLPEDIIEVNQKMMLILAASIMY 618
Cdd:cd21220    81 IFLLWEDIVEVKPKMILTFVASLMA 105
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
95-243 3.02e-48

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: 166.37  E-value: 3.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071  95 GVEKTGGSKGsssflkTSTTTVHHAINESEKASYVSHINNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVP 174
Cdd:cd21323     2 GITAIGGTSA------ISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQP 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274899071 175 GTIDERAINTKKtLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQMLADL 243
Cdd:cd21323    76 DTIDERAINKKK-LTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADI 143
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
390-502 3.50e-45

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: 157.01  E-value: 3.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 390 ETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMP--FKKVENCNEVIKIGKDLR 467
Cdd:cd21298     3 EETREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGanMKKIENCNYAVELGKKLK 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2274899071 468 FSLVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLL 502
Cdd:cd21298    83 FSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLSIL 117
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
388-502 6.47e-43

third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409149  Cd Length: 119  Bit Score: 150.65  E-value: 6.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 388 DVETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPP---IKMPFKKVENCNEVIKIGK 464
Cdd:cd21300     2 DAEGEREARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaEISRFKAVENTNYAVELGK 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2274899071 465 DLRFSLVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLL 502
Cdd:cd21300    82 QLGFSLVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
257-366 1.21e-41

second calponin homology (CH) domain found in the family of plastin; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409144  Cd Length: 113  Bit Score: 147.04  E-value: 1.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 257 DTQDAEELMGLAPEKVLLKWMNFHLKKAGYEKQVTNFSSDVKDGEAYAYLLNALAPEHST--HVALETKDPTERAKKVLE 334
Cdd:cd21295     1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRRIKNFSGDIKDSEAYTHLLKQIAPKDAGvdTSALRESDLLQRAELMLQ 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2274899071 335 QAEKLDCKRYLSPKDIVDGSANLNLAFVAQIF 366
Cdd:cd21295    81 NADKIGCRKFVTPKDVVTGNPKLNLAFVANLF 112
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
118-236 2.77e-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: 146.44  E-value: 2.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 118 HAINESEKASYVSHINNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTK----KTLNPWER 193
Cdd:cd21294     1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPprknKPLNNFQM 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2274899071 194 NENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIK 236
Cdd:cd21294    81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIR 123
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
259-367 1.15e-40

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 144.36  E-value: 1.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 259 QDAEELMGLAPEKVLLKWMNFHLKKAGYEK-QVTNFSSDVKDGEAYAYLLNALAPEHSTHV----ALETKDPTERAKKVL 333
Cdd:cd21218     1 ETLESLLYLPPEEILLRWVNYHLKKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELCDKElvleVLSEEDLEKRAEKVL 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2274899071 334 EQAEKLDCKRYLSPKDIVDGSANLNLAFVAQIFQ 367
Cdd:cd21218    81 QAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
110-243 7.42e-40

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: 143.23  E-value: 7.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 110 KTSTTTVHHAINESEKASYVSHINNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKtLN 189
Cdd:cd21324    11 EQSSAGTQHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKK-LT 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2274899071 190 PWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQMLADL 243
Cdd:cd21324    90 PFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADI 143
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
104-247 3.79e-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: 3.79e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 104 GSSSFLKTSTTtvHHAINESEKASYVSHINNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAIN 183
Cdd:cd21325     7 GGTSELSSEGT--QHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAIN 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274899071 184 tKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQMLADLNFKK 247
Cdd:cd21325    85 -KKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSR 147
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
511-617 5.94e-39

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: 139.48  E-value: 5.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 511 GKEITDVDILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKL 590
Cdd:cd21303     1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLVTPGNTEDEAYLNAKLAISIARKL 80
                          90       100
                  ....*....|....*....|....*..
gi 2274899071 591 GCSIFLLPEDIIEVNQKMMLILAASIM 617
Cdd:cd21303    81 GALIFLVPEDIVEVRPRLVLTFIGSLM 107
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
262-366 1.04e-37

second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409146  Cd Length: 109  Bit Score: 135.77  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 262 EELMGLAPEKVLLKWMNFHLKKAGYEKQVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDC 341
Cdd:cd21297     4 EQFLRLPPEQILLRWFNYHLKAANWPRRVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDLLQRAEQVLQNAEKLDC 83
                          90       100
                  ....*....|....*....|....*
gi 2274899071 342 KRYLSPKDIVDGSANLNLAFVAQIF 366
Cdd:cd21297    84 RKFLTPTSLVAGNPKLNLAFVANLF 108
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
514-617 1.85e-35

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: 129.32  E-value: 1.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 514 ITDVDILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGCS 593
Cdd:cd21301     1 ISDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLVLEGNSEEDKLSNAKYAISMARKIGAR 80
                          90       100
                  ....*....|....*....|....
gi 2274899071 594 IFLLPEDIIEVNQKMMLILAASIM 617
Cdd:cd21301    81 VYALPEDIVEVKPKMVMTVFACLM 104
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
254-366 1.25e-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: 116.60  E-value: 1.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 254 LVDDTQDAEELMGLAPEKVLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAPEHSTH---------VALETKD 324
Cdd:cd21328     1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQK-INNFSSDIKDSRAYFHLLNQIAPKGQKEgepridinmSGFNEKD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2274899071 325 PTERAKKVLEQAEKLDCKRYLSPKDIVDGSANLNLAFVAQIF 366
Cdd:cd21328    80 DLKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLF 121
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
392-502 9.35e-30

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: 113.93  E-value: 9.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 392 SREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPgSVNWKHANKPPIKM---PFKKVENCNEVIKIGKD-LR 467
Cdd:cd21329     5 SSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRV-PVDWGHVNKPPYPAlggNMKKIENCNYAVELGKNkAK 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2274899071 468 FSLVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLL 502
Cdd:cd21329    84 FSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
259-366 2.13e-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: 113.05  E-value: 2.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 259 QDAEELMGLAPEKVLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAPEHSTHV--------ALETKDPTERAK 330
Cdd:cd21326     3 EELEELMKLSPEELLLRWVNYHLTNAGWQN-ISNFSQDIKDSRAYFHLLNQIAPKGDVFDenieidfsGFNEKNDLKRAE 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2274899071 331 KVLEQAEKLDCKRYLSPKDIVDGSANLNLAFVAQIF 366
Cdd:cd21326    82 YMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLF 117
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
254-366 4.67e-29

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: 111.98  E-value: 4.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 254 LVDDTQDAEELMGLAPEKVLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAPEHSTH---------VALETKD 324
Cdd:cd21327     1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNK-INNFSSDIKDSKAYYHLLNQVAPKGDEEgipaividmSGLREKD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2274899071 325 PTERAKKVLEQAEKLDCKRYLSPKDIVDGSANLNLAFVAQIF 366
Cdd:cd21327    80 DLKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLF 121
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
392-502 3.42e-27

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: 107.01  E-value: 3.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 392 SREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPgSVNWKHANKPP---IKMPFKKVENCNEVIKIGKD-LR 467
Cdd:cd21331    21 TREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKV-PVDWNKVNKPPypkLGANMKKLENCNYAVELGKHpAK 99
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2274899071 468 FSLVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLL 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 8.51e-26

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: 102.76  E-value: 8.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 392 SREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPgSVNWKHANKPP---IKMPFKKVENCNEVIKIGKD-LR 467
Cdd:cd21330    12 TREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKV-PVDWNRVNKPPypkLGENMKKLENCNYAVELGKNkAK 90
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2274899071 468 FSLVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLL 502
Cdd:cd21330    91 FSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 125
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
509-617 2.51e-24

fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the fourth CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409182  Cd Length: 115  Bit Score: 98.14  E-value: 2.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 509 SQGKEITDVDILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKL-NATYIISVA 587
Cdd:cd21333     1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLnNAKYAISMA 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2274899071 588 RKLGCSIFLLPEDIIEVNQKMMLILAASIM 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 2.56e-24

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: 98.04  E-value: 2.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 514 ITDVDILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGE-TEEDKKLNATYIISVARKLGC 592
Cdd:cd21334     1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNlTDDDKLDNAKYAVSMARKIGA 80
                          90       100
                  ....*....|....*....|....*
gi 2274899071 593 SIFLLPEDIIEVNQKMMLILAASIM 617
Cdd:cd21334    81 RVYALPEDLVEVKPKMVMTVFACLM 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
267-371 2.70e-22

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 92.35  E-value: 2.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 267 LAPEKVLLKWMNFHLKKAGYEKQVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETK--DPTERAKKVLEQAE-KLDCKR 343
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEkKLGVPK 80
                          90       100
                  ....*....|....*....|....*....
gi 2274899071 344 YLS-PKDIVDGSANLNLAFVAQIFQHRNG 371
Cdd:pfam00307  81 VLIePEDLVEGDNKSVLTYLASLFRRFQA 109
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
510-617 2.18e-20

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: 86.93  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 510 QGKEITDVDILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGE-TEEDKKLNATYIISVAR 588
Cdd:cd21332     4 EGEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDlSDADKLNNAKYAISVAR 83
                          90       100
                  ....*....|....*....|....*....
gi 2274899071 589 KLGCSIFLLPEDIIEVNQKMMLILAASIM 617
Cdd:cd21332    84 KIGARVYALPEDLVEVKPKMVMTVFACLM 112
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
398-496 3.70e-20

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 85.83  E-value: 3.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071  398 FRLWINSLG---TATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpiKMPFKKVENCNEVIKIGKDLRFSLVNVA 474
Cdd:smart00033   3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 2274899071  475 GNDIVQGnKKLLLAFLWQLMRY 496
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLISL 101
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
394-495 1.37e-17

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: 78.77  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS-----------LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNEVIKI 462
Cdd:cd21217     2 EKEAFVEHINSlladdpdlkhlLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKNIFEATENLNLALNA 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2274899071 463 GKDLRFSLVNVAGNDIVQGNKKLLLAFLWQLMR 495
Cdd:cd21217    82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
394-496 2.95e-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: 77.71  E-value: 2.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINSL----GTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpikmPFKKVENCNEVIKIG-KDLRF 468
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLALDVAeKKLGV 78
                          90       100
                  ....*....|....*....|....*...
gi 2274899071 469 SLVNVAGNDIVQGNKKLLLAFLWQLMRY 496
Cdd:pfam00307  79 PKVLIEPEDLVEGDNKSVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
148-237 5.88e-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: 5.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071  148 IDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKtlNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPyLV 227
Cdd:smart00033  15 DKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL--SRFKKIENINLALSFAEKLGGKVVLFEPEDLVEGPK-LI 91
                           90
                   ....*....|
gi 2274899071  228 LGLISQIIKI 237
Cdd:smart00033  92 LGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
142-236 1.00e-15

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 73.47  E-value: 1.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 142 LKSYLPIDPATNaFFDLVKDGVLLCKLINVAVPGTIDERAINTKktlnPWERNENLTLGLNSA-KAIGCTVVNIGTQDIA 220
Cdd:pfam00307  15 LAEYGPGVRVTN-FTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLALDVAeKKLGVPKVLIEPEDLV 89
                          90
                  ....*....|....*.
gi 2274899071 221 EGRPYLVLGLISQIIK 236
Cdd:pfam00307  90 EGDNKSVLTYLASLFR 105
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
146-240 3.11e-15

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 72.31  E-value: 3.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 146 LPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPY 225
Cdd:cd21219    16 LGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKPLNKFKKVENCNYAVDLAKKLGFSLVGIGGKDIADGNRK 95
                          90
                  ....*....|....*
gi 2274899071 226 LVLGLISQIIKIQML 240
Cdd:cd21219    96 LTLALVWQLMRYHVL 110
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
518-617 4.57e-15

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 71.55  E-value: 4.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 518 DILNWANRKVKRGGRTSQADSFRdKNLSSGMFFLELLSAVEPRVVNWSLVTNgeTEEDKKLNATYIISVAR-KLGCSIFL 596
Cdd:pfam00307   6 ELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKLNK--SEFDKLENINLALDVAEkKLGVPKVL 82
                          90       100
                  ....*....|....*....|..
gi 2274899071 597 L-PEDIIEVNQKMMLILAASIM 617
Cdd:pfam00307  83 IePEDLVEGDNKSVLTYLASLF 104
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
271-368 8.91e-15

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: 70.42  E-value: 8.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071  271 KVLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETK----DPTERAKKVLEQAEKLDCKR-YL 345
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVvLF 79
                           90       100
                   ....*....|....*....|...
gi 2274899071  346 SPKDIVDGSaNLNLAFVAQIFQH 368
Cdd:smart00033  80 EPEDLVEGP-KLILGVIWTLISL 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
125-236 1.13e-13

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: 67.36  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 125 KASYVSHINNYLRDDPFLKSylpidpatNAFFDLVKDGVLLCKLINVAVPGTIDERAintKKTLNPWERNENLTLGLNSA 204
Cdd:cd00014     1 EEELLKWINEVLGEELPVSI--------TDLFESLRDGVLLCKLINKLSPGSIPKIN---KKPKSPFKKRENINLFLNAC 69
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2274899071 205 KAIG-CTVVNIGTQDIAEGR-PYLVLGLISQIIK 236
Cdd:cd00014    70 KKLGlPELDLFEPEDLYEKGnLKKVLGTLWALAL 103
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
518-619 2.09e-12

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: 63.87  E-value: 2.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071  518 DILNWANRKVKrgGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGCSIFLL 597
Cdd:smart00033   2 TLLRWVNSLLA--EYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79
                           90       100
                   ....*....|....*....|...
gi 2274899071  598 -PEDIIEVNqKMMLILAASIMYW 619
Cdd:smart00033  80 ePEDLVEGP-KLILGVIWTLISL 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
395-495 1.01e-11

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 61.97  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 395 ERCFRLWINSLgTATY----VNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKppiKMPFKKVENCNEVIKIGKDLRF-S 469
Cdd:cd00014     1 EEELLKWINEV-LGEElpvsITDLFESLRDGVLLCKLINKLSPGSIPKINKKP---KSPFKKRENINLFLNACKKLGLpE 76
                          90       100
                  ....*....|....*....|....*..
gi 2274899071 470 LVNVAGNDIVQ-GNKKLLLAFLWQLMR 495
Cdd:cd00014    77 LDLFEPEDLYEkGNLKKVLGTLWALAL 103
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
520-616 3.35e-11

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: 60.78  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 520 LNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGCSIFLLPE 599
Cdd:cd21218    16 LRWVNYHLKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYFLTPE 95
                          90
                  ....*....|....*..
gi 2274899071 600 DIIEVNQKMMLILAASI 616
Cdd:cd21218    96 DIVSGNPRLNLAFVATL 112
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
269-354 2.22e-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: 58.02  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 269 PEKVLLKWMNFHLKkagyEKQVTNFSSDVKDGEAYAYLLNALAPE-HSTHVALETKDPTERAKKVLEQAE-KLDCKRYLS 346
Cdd:cd21184     2 GKSLLLEWVNSKIP----EYKVKNFTTDWNDGKALAALVDALKPGlIPDNESLDKENPLENATKAMDIAEeELGIPKIIT 77

                  ....*...
gi 2274899071 347 PKDIVDGS 354
Cdd:cd21184    78 PEDMVSPN 85
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
394-491 1.00e-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: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS-LGTA--TYVNNVFEDLRNGWVLLEVLDKVSPgsvnwKHANKPPIKMPFKKVENCNEVIKIGKDLRFSL 470
Cdd:cd21186     3 QKKTFTKWINSqLSKAnkPPIKDLFEDLRDGTRLLALLEVLTG-----KKLKPEKGRMRVHHLNNVNRALQVLEQNNVKL 77
                          90       100
                  ....*....|....*....|.
gi 2274899071 471 VNVAGNDIVQGNKKLLLAFLW 491
Cdd:cd21186    78 VNISSNDIVDGNPKLTLGLVW 98
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
388-494 1.47e-09

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


Pssm-ID: 409167  Cd Length: 139  Bit Score: 56.96  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 388 DVETSREERCFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPgsvnwKHANKPPI-KMPFKKVENCNEVIKIGK 464
Cdd:cd21318    33 DEREAVQKKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLEVLSG-----EQLPKPTRgRMRIHSLENVDKALQFLK 107
                          90       100       110
                  ....*....|....*....|....*....|
gi 2274899071 465 DLRFSLVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21318   108 EQRVHLENVGSHDIVDGNHRLTLGLIWTII 137
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
383-494 3.83e-09

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: 55.38  E-value: 3.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 383 EMMTDDVETSREER------CFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVE 454
Cdd:cd21236     1 QAYENVLERYKDERdkvqkkTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKG-----RMRFHRLQ 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2274899071 455 NCNEVIKIGKDLRFSLVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21236    76 NVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTII 115
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
414-495 7.07e-09

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: 54.38  E-value: 7.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 414 VFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKM----PFKKVENCNEVIKIGKDLRFSLVNVAGNDIVQGNKKLLLAF 489
Cdd:cd21294    38 LFDECKDGLVLSKLINDSVPDTIDERVLNKPPRKNkplnNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGL 117

                  ....*.
gi 2274899071 490 LWQLMR 495
Cdd:cd21294   118 IWQIIR 123
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
394-495 1.21e-08

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: 53.30  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINSL---GTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpiKMPFKKVENCNEVIK-IGKDLRFS 469
Cdd:cd21225     5 QIKAFTAWVNSVlekRGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEP--KNRIQMIQNLHLAMLfIEEDLKIR 82
                          90       100
                  ....*....|....*....|....*.
gi 2274899071 470 LVNVAGNDIVQGNKKLLLAFLWQLMR 495
Cdd:cd21225    83 VQGIGAEDFVDNNKKLILGLLWTLYR 108
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
394-494 1.32e-08

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: 53.17  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS-LGTATY-VNNVFEDLRNGWVLLEVLDKVSPGSVNwKHANKPpiKMPFKKVENCNEVIKIGKDLRFSLV 471
Cdd:cd21215     5 QKKTFTKWLNTkLSSRGLsITDLVTDLSDGVRLIQLLEIIGDESLG-RYNKNP--KMRVQKLENVNKALEFIKSRGVKLT 81
                          90       100
                  ....*....|....*....|...
gi 2274899071 472 NVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21215    82 NIGAEDIVDGNLKLILGLLWTLI 104
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
394-491 3.58e-08

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: 51.98  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS-LGTAT-YVNNVFEDLRNGWVLLEVLDKVSPgsvnwKHANKP-PIKMPFKKVENCNEVIKIGKDLRFSL 470
Cdd:cd21246    17 QKKTFTKWVNShLARVGcRINDLYTDLRDGRMLIKLLEVLSG-----ERLPKPtKGKMRIHCLENVDKALQFLKEQRVHL 91
                          90       100
                  ....*....|....*....|.
gi 2274899071 471 VNVAGNDIVQGNKKLLLAFLW 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 6.04e-08

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: 51.33  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpiKMPFKKVENCNEVIKIGKDLRFSLV 471
Cdd:cd21183     5 QANTFTRWCNEhlKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYNRRP--AFQQHYLENVSTALKFIEADHIKLV 82
                          90       100
                  ....*....|....*....|...
gi 2274899071 472 NVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21183    83 NIGSGDIVNGNIKLILGLIWTLI 105
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
146-243 6.85e-08

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: 51.27  E-value: 6.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 146 LPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKK---TLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEG 222
Cdd:cd21300    19 LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaEISRFKAVENTNYAVELGKQLGFSLVGIQGADITDG 98
                          90       100
                  ....*....|....*....|.
gi 2274899071 223 RPYLVLGLISQIIKIQMLADL 243
Cdd:cd21300    99 SRTLTLALVWQLMRFHITKTL 119
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
394-491 7.35e-08

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: 50.86  E-value: 7.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNEVIKIGKDLRFSLV 471
Cdd:cd21188     4 QKKTFTKWVNKhlIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERG-----RMRFHRLQNVQTALDFLKYRKIKLV 78
                          90       100
                  ....*....|....*....|
gi 2274899071 472 NVAGNDIVQGNKKLLLAFLW 491
Cdd:cd21188    79 NIRAEDIVDGNPKLTLGLIW 98
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
161-235 9.66e-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: 50.75  E-value: 9.66e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274899071 161 DGVLLCKLINVavpgtIDERAIN--TKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQII 235
Cdd:cd21227    33 DGVKLIALVEI-----LQGRKLGrvIKKPLNQHQKLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLI 104
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
394-494 1.34e-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: 50.79  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNEVIKIGKDLRFSLV 471
Cdd:cd21235     7 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 81
                          90       100
                  ....*....|....*....|...
gi 2274899071 472 NVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21235    82 NIRNDDIADGNPKLTLGLIWTII 104
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
394-494 1.75e-07

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: 49.79  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS-LGTAT-YVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMpfKKVENCNEVIKIGKDLRFSLV 471
Cdd:cd21228     5 QQNTFTRWCNEhLKCVNkRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRPTFRQ--MKLENVSVALEFLERESIKLV 82
                          90       100
                  ....*....|....*....|...
gi 2274899071 472 NVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21228    83 SIDSSAIVDGNLKLILGLIWTLI 105
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
394-494 2.05e-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: 49.62  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINSLGTAT---YVNNVFEDLRNGWVLLEVLDKVSpGSVNWKHANKPPIKmpfkKVENCNEVIKIGKDLRFSL 470
Cdd:cd21232     3 QKKTFTKWINARFSKSgkpPIKDMFTDLRDGRKLLDLLEGLT-GKSLPKERGSTRVH----ALNNVNRVLQVLHQNNVEL 77
                          90       100
                  ....*....|....*....|....
gi 2274899071 471 VNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21232    78 VNIGGTDIVDGNHKLTLGLLWSII 101
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
394-496 3.47e-07

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: 49.11  E-value: 3.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS----LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVnwkHANKPPIKMPFKKVENCNEVIKIGKDLRFS 469
Cdd:cd21190     6 QKKTFTNWINShlakLSQPIVINDLFVDIKDGTALLRLLEVLSGQKL---PIESGRVLQRAHKLSNIRNALDFLTKRCIK 82
                          90       100
                  ....*....|....*....|....*..
gi 2274899071 470 LVNVAGNDIVQGNKKLLLAFLWQLMRY 496
Cdd:cd21190    83 LVNINSTDIVDGKPSIVLGLIWTIILY 109
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
270-353 3.68e-07

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: 48.87  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 270 EKVLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDP---TERAKKVLEQAEKL--DCKRY 344
Cdd:cd00014     1 EEELLKWINEVLGEELPVS-ITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLglPELDL 79

                  ....*....
gi 2274899071 345 LSPKDIVDG 353
Cdd:cd00014    80 FEPEDLYEK 88
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
146-244 4.02e-07

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: 49.04  E-value: 4.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 146 LPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPY 225
Cdd:cd21299    16 LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFSLVNVAGNDIVQGNKK 95
                          90
                  ....*....|....*....
gi 2274899071 226 LVLGLISQIIKIQMLADLN 244
Cdd:cd21299    96 LILALLWQLMRYHMLQLLK 114
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
388-494 4.08e-07

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: 49.67  E-value: 4.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 388 DVETSREERCFRLWINS-LGTAT-YVNNVFEDLRNGWVLLEVLDKVSPgsvnwKHANKPPI-KMPFKKVENCNEVIKIGK 464
Cdd:cd21317    26 DEREAVQKKTFTKWVNShLARVTcRIGDLYTDLRDGRMLIRLLEVLSG-----EQLPKPTKgRMRIHCLENVDKALQFLK 100
                          90       100       110
                  ....*....|....*....|....*....|
gi 2274899071 465 DLRFSLVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21317   101 EQKVHLENMGSHDIVDGNHRLTLGLIWTII 130
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
394-494 9.29e-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: 48.11  E-value: 9.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNEVIKIGKDLRFSLV 471
Cdd:cd21237     7 QKKTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKG-----RMRFHRLQNVQIALDFLKQRQVKLV 81
                          90       100
                  ....*....|....*....|...
gi 2274899071 472 NVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21237    82 NIRNDDITDGNPKLTLGLIWTII 104
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
398-496 1.04e-06

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: 47.67  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 398 FRLWINSL--GTATYVNNVFEDLRNGWVL---LEVLDKVSPGSVNwkhaNKPpiKMPFKKVENCNEVIKIGKDLRFSLVN 472
Cdd:cd21227     9 FTNWVNEQlkPTGMSVEDLATDLEDGVKLialVEILQGRKLGRVI----KKP--LNQHQKLENVTLALKAMAEDGIKLVN 82
                          90       100
                  ....*....|....*....|....*
gi 2274899071 473 VAGNDIVQGNKKLLLAFLWQL-MRY 496
Cdd:cd21227    83 IGNEDIVNGNLKLILGLIWHLiLRY 107
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
394-494 1.05e-06

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: 47.77  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS----LGTAtyVNNVFEDLRNGWVLLEVLDKVSPGSVnwKHANKPpiKMPFKKVENCNEVIKIGKDLRFS 469
Cdd:cd21214     6 QRKTFTAWCNShlrkAGTQ--IENIEEDFRDGLKLMLLLEVISGERL--PKPERG--KMRFHKIANVNKALDFIASKGVK 79
                          90       100
                  ....*....|....*....|....*
gi 2274899071 470 LVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21214    80 LVSIGAEEIVDGNLKMTLGMIWTII 104
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
411-494 1.62e-06

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: 47.20  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 411 VNNVFEDLRNG---WVLLEVLDKVSPGSvnwKHANKPPIKMPfKKVENCNEVIKI----GKDLRFSLVNVAGNDIVQGNK 483
Cdd:cd21223    26 VTNLAVDLRDGvrlCRLVELLTGDWSLL---SKLRVPAISRL-QKLHNVEVALKAlkeaGVLRGGDGGGITAKDIVDGHR 101
                          90
                  ....*....|.
gi 2274899071 484 KLLLAFLWQLM 494
Cdd:cd21223   102 EKTLALLWRII 112
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
269-352 1.78e-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: 46.99  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 269 PEKVLLKWMNFHLKkagyEKQVTNFSSDVKDGEAYAYLLNALAP----EHSTHVAletKDPTERAKKVLEQAEK-LDCKR 343
Cdd:cd21230     2 PKQRLLGWIQNKIP----QLPITNFTTDWNDGRALGALVDSCAPglcpDWETWDP---NDALENATEAMQLAEDwLGVPQ 74

                  ....*....
gi 2274899071 344 YLSPKDIVD 352
Cdd:cd21230    75 LITPEEIIN 83
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
394-494 1.91e-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: 47.22  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINSLGTAT---YVNNVFEDLRNGWVLLEVLDKVSpgsvnwkhANKPPIKMPFKKVE---NCNEVIKIGKDLR 467
Cdd:cd21231     7 QKKTFTKWINAQFAKFgkpPIEDLFTDLQDGRRLLELLEGLT--------GQKLVKEKGSTRVHalnNVNKALQVLQKNN 78
                          90       100
                  ....*....|....*....|....*..
gi 2274899071 468 FSLVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21231    79 VDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
394-496 2.16e-06

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: 46.80  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWIN----SLGTATYVNNVFEDLRNGWVLLEVLDKVSpgSVNWKHANKPPIKMPFKkVENCNEVIKIGKDLRFS 469
Cdd:cd21191     6 QKRTFTRWINlhleKCNPPLEVKDLFVDIQDGKILMALLEVLS--GQNLLQEYKPSSHRIFR-LNNIAKALKFLEDSNVK 82
                          90       100
                  ....*....|....*....|....*..
gi 2274899071 470 LVNVAGNDIVQGNKKLLLAFLWQLMRY 496
Cdd:cd21191    83 LVSIDAAEIADGNPSLVLGLIWNIILF 109
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
150-223 3.72e-06

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: 46.15  E-value: 3.72e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2274899071 150 PATNAFFDLVKDGVLLCKLINVAVPGTIdeRAINTKKTlnPWERNENLTLGLNSAKAIGCTVVNI-GTQDIAEGR 223
Cdd:cd21207    23 DDGKDYEDVLKDGVILCKLINILKPGSV--KKINTSKM--AFKLMENIENFLTACKGYGVPKTDLfQTVDLYEKK 93
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
394-494 3.91e-06

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: 45.98  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINSL----GTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpikmpFKKVENCNEVIKIGKDLRFS 469
Cdd:cd21242     6 QKRTFTNWINSQlakhSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNV-----FQCRSNIETALSFLKNKSIK 80
                          90       100
                  ....*....|....*....|....*
gi 2274899071 470 LVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21242    81 LINIHVPDIIEGKPSIILGLIWTII 105
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
150-236 5.20e-06

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: 45.85  E-value: 5.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 150 PATNAFFDLvKDGVLLCKLINVAVPGTIDERAINTKKTLnpwERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLG 229
Cdd:cd21215    23 SITDLVTDL-SDGVRLIQLLEIIGDESLGRYNKNPKMRV---QKLENVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILG 98

                  ....*..
gi 2274899071 230 LISQIIK 236
Cdd:cd21215    99 LLWTLIL 105
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
146-243 6.31e-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: 45.69  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 146 LPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINtkKTLNPWERN----ENLTLGLNSAKAIGCTVVNIGTQDIAE 221
Cdd:cd21298    18 LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVN--KPFKKLGANmkkiENCNYAVELGKKLKFSLVGIGGKDIYD 95
                          90       100
                  ....*....|....*....|..
gi 2274899071 222 GRPYLVLGLISQIIKIQMLADL 243
Cdd:cd21298    96 GNRTLTLALVWQLMRAYTLSIL 117
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
256-352 8.70e-06

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: 45.54  E-value: 8.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 256 DDTQDAEELMGLAPEKVLLKWMNFHLKkagyEKQVTNFSSDVKDGEAYAYLLNALAPEHSTHVAL-ETKDPTERAKKVLE 334
Cdd:cd21315     4 GEDDGPDDGKGPTPKQRLLGWIQSKVP----DLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDwDPKDAVKNAKEAMD 79
                          90
                  ....*....|....*....
gi 2274899071 335 QAEK-LDCKRYLSPKDIVD 352
Cdd:cd21315    80 LAEDwLDVPQLIKPEEMVN 98
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
275-353 1.08e-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: 44.88  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 275 KWMNFHLKKAGYEKQVTNFSSDVKDGEAYAYLLNALAPEHSTHValeTKDPTERAKKVleqaEKLD-CKRYL-------- 345
Cdd:cd21212     7 DWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGI---HSRPKTRAQKL----ENIQaCLQFLaalgvdvq 79
                          90
                  ....*....|
gi 2274899071 346 --SPKDIVDG 353
Cdd:cd21212    80 giTAEDIVDG 89
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
259-352 1.15e-05

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


Pssm-ID: 409163  Cd Length: 115  Bit Score: 45.06  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 259 QDAEELMGLAPEKVLLKWMNFHLKKAgyekQVTNFSSDVKDGEAYAYLLNALAPEHSTH-VALETKDPTERAKKVLEQAE 337
Cdd:cd21314     2 EDEEDARKQTPKQRLLGWIQNKVPQL----PITNFNRDWQDGKALGALVDNCAPGLCPDwESWDPNQPVQNAREAMQQAD 77
                          90
                  ....*....|....*.
gi 2274899071 338 K-LDCKRYLSPKDIVD 352
Cdd:cd21314    78 DwLGVPQVIAPEEIVD 93
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
388-494 2.80e-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: 44.65  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 388 DVETSREERCFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPgsvnwKHANKPPI-KMPFKKVENCNEVIKIGK 464
Cdd:cd21316    48 DEREAVQKKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLEVLSG-----ERLPKPTKgRMRIHCLENVDKALQFLK 122
                          90       100       110
                  ....*....|....*....|....*....|
gi 2274899071 465 DLRFSLVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21316   123 EQRVHLENMGSHDIVDGNHRLTLGLIWTII 152
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
371-495 3.29e-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: 44.26  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 371 GLTVDDSKTSFAEMMTDDVETSREERCFRLWINS-----------LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWK 439
Cdd:cd21323     2 GITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKalegdpdckhvVPMNPTDESLFKSLADGILLCKMINLSQPDTIDER 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2274899071 440 HANKPPIKmPFKKVENCNEVIKIGKDLRFSLVNVAGNDIVQGNKKLLLAFLWQLMR 495
Cdd:cd21323    82 AINKKKLT-PFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIK 136
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
155-208 4.13e-05

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: 43.48  E-value: 4.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2274899071 155 FFDLVKDGVLLCKLINVAVPGTIdeRAINTKKTlnPWERNENLTLGLNSAKAIG 208
Cdd:cd21208    22 FRESLEDGILLCELINAIKPGSI--KKINRLPT--PIAGLDNLNLFLKACEDLG 71
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
271-368 4.52e-05

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: 42.77  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 271 KVLLKWMNFHLKKAGyeKQVTNFSSDVKDGEAYAYLLNALAPEHSthvaletkdPTERAK----KVLEQAEKLDCKRY-- 344
Cdd:cd21188     6 KTFTKWVNKHLIKAR--RRVVDLFEDLRDGHNLISLLEVLSGESL---------PRERGRmrfhRLQNVQTALDFLKYrk 74
                          90       100
                  ....*....|....*....|....*....
gi 2274899071 345 -----LSPKDIVDGSANLNLAFVAQIFQH 368
Cdd:cd21188    75 iklvnIRAEDIVDGNPKLTLGLIWTIILH 103
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
276-353 4.74e-05

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: 43.06  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 276 WMNFHLKKAGYEKQVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDCKR----YLSPKDIV 351
Cdd:cd21213     8 WVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRirmhQTSAKDIV 87

                  ..
gi 2274899071 352 DG 353
Cdd:cd21213    88 DG 89
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
394-495 4.92e-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: 43.81  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS-LGT----ATYV------NNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKmPFKKVENCNEVIKI 462
Cdd:cd21292    25 EKVAFVNWINKnLGDdpdcKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTIDERAINKKKLT-VFTIHENLTLALNS 103
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2274899071 463 GKDLRFSLVNVAGNDIVQGNKKLLLAFLWQLMR 495
Cdd:cd21292   104 ASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIR 136
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
265-368 7.32e-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: 42.35  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 265 MGLAPEKVLLKWMnfHLKKAGYEK-QVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDCKR 343
Cdd:cd21199     5 YGGSKRNALLKWC--QEKTQGYKGiDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGIPT 82
                          90       100
                  ....*....|....*....|....*...
gi 2274899071 344 YLSPKDIVDGSA---NLNLAFVAQIFQH 368
Cdd:cd21199    83 TLTIDEMVSMERpdwQSVMSYVTAIYKH 110
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
392-627 7.73e-05

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 46.09  E-value: 7.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 392 SREERCFRLWIN---SLGTATYVNNVFEDLRnGWV----LLEVLDKVSPGSVNwkhankPPIKMPFKKVENCNEVIKIGK 464
Cdd:COG5069     8 KVQKKTFTKWTNeklISGGQKEFGDLDTDLK-DGVklaqLLEALQKDNAGEYN------ETPETRIHVMENVSGRLEFIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 465 DLRFSLVNVAGNDIVQGNKKLLLAFLWqlmryTMLQLLRNLRSHSQGKEITDVDILNWANRKVkrGGRTSQADSFR-DKN 543
Cdd:COG5069    81 GKGVKLFNIGPQDIVDGNPKLILGLIW-----SLISRLTIATINEEGELTKHINLLLWCDEDT--GGYKPEVDTFDfFRS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 544 LSSGMFFLELLS-----AVEPRVVNWSlvtngetEEDKKLNATYIISVARK-LGCSIFLLPEDIIEVN----QKMMLILA 613
Cdd:COG5069   154 WRDGLAFSALIHdsrpdTLDPNVLDLQ-------KKNKALNNFQAFENANKvIGIARLIGVEDIVNVSipdeRSIMTYVS 226
                         250
                  ....*....|....
gi 2274899071 614 ASIMYWSLQQQSDT 627
Cdd:COG5069   227 WYIIRFGLLEKIDI 240
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
124-235 8.24e-05

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


Pssm-ID: 409090  Cd Length: 113  Bit Score: 42.36  E-value: 8.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 124 EKASYVSHINNYL-RDDPFLKsylpidpaTNAFFDLVKDGVLLCKLINV----AVPGtidERAINTKKTlnPWERNENLT 198
Cdd:cd21241     6 QKKTFTNWINSYLaKRKPPMK--------VEDLFEDIKDGTKLLALLEVlsgeKLPC---EKGRRLKRV--HFLSNINTA 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2274899071 199 LGLNSAKAIgcTVVNIGTQDIAEGRPYLVLGLISQII 235
Cdd:cd21241    73 LKFLESKKI--KLVNINPTDIVDGKPSIVLGLIWTII 107
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
161-235 9.37e-05

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 42.08  E-value: 9.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2274899071 161 DGVLLCKLINVaVPGTIDERAINtKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQII 235
Cdd:cd21183    33 DGLCLIALLEN-LSTRPLKRSYN-RRPAFQQHYLENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTLI 105
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
257-352 1.09e-04

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


Pssm-ID: 409161  Cd Length: 114  Bit Score: 42.10  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 257 DTQDAEELMGLAPEKVLLKWMNFHLKKAgyekQVTNFSSDVKDGEAYAYLLNALAPEHSTHV-ALETKDPTERAKKVLEQ 335
Cdd:cd21312     1 DEEEDEEAKKQTPKQRLLGWIQNKLPQL----PITNFSRDWQSGRALGALVDSCAPGLCPDWdSWDASKPVTNAREAMQQ 76
                          90
                  ....*....|....*...
gi 2274899071 336 AEK-LDCKRYLSPKDIVD 352
Cdd:cd21312    77 ADDwLGIPQVITPEEIVD 94
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
267-370 1.33e-04

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409093  Cd Length: 109  Bit Score: 41.74  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 267 LAPEKVLLKWMNFHLKKAGyEKQVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEK-LDCKRYL 345
Cdd:cd21244     4 MSARKALLLWAQEQCAKVG-SISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQeLKIPRLL 82
                          90       100
                  ....*....|....*....|....*..
gi 2274899071 346 SPKD--IVDGSANLNLAFVAQIFQHRN 370
Cdd:cd21244    83 EPEDvdVVNPDEKSIMTYVAQFLQYSK 109
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
266-368 1.49e-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: 41.55  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 266 GLAPEKVLLKWMnfHLKKAGYEK-QVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDCKRY 344
Cdd:cd21257     6 GGSKRNALLKWC--QKKTEGYPNiDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGIKPS 83
                          90       100
                  ....*....|....*....|....*..
gi 2274899071 345 LSPKDIVDGSA---NLNLAFVAQIFQH 368
Cdd:cd21257    84 LELSEMMYTDRpdwQSVMQYVAQIYKY 110
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
401-508 1.55e-04

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: 41.41  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 401 WINSL----GTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANkppIKMPFKKVENCNEVIKIGKDLRFSLVNVAGN 476
Cdd:cd21212     8 WANHYlekgGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSR---PKTRAQKLENIQACLQFLAALGVDVQGITAE 84
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2274899071 477 DIVQGNKKlllaflwqlmryTMLQLLRNLRSH 508
Cdd:cd21212    85 DIVDGNLK------------AILGLFFSLSRY 104
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
270-350 1.66e-04

second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409041  Cd Length: 107  Bit Score: 41.25  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 270 EKVLLKWMNfhlKKAG--YEKQVTNFSSDVKDGEAYAYLLNALAPEhstHVALET------KDPTERAKKVLEQAekLDC 341
Cdd:cd21192     5 EKALLKWVQ---AEIGkyYGIRVTDFDKSWRDGVAFLALIHAIRPD---LVDMKTvknrspRDNLELAFRIAEQH--LNI 76

                  ....*....
gi 2274899071 342 KRYLSPKDI 350
Cdd:cd21192    77 PRLLEVEDV 85
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
271-368 2.22e-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: 41.21  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 271 KVLLKWMNFHLKKAGYEkQVTNFSSDVKDGEAYAYLLNAL-----APEH-STHV-ALETKDpteRAKKVLEQAE-KLdck 342
Cdd:cd21186     5 KTFTKWINSQLSKANKP-PIKDLFEDLRDGTRLLALLEVLtgkklKPEKgRMRVhHLNNVN---RALQVLEQNNvKL--- 77
                          90       100
                  ....*....|....*....|....*.
gi 2274899071 343 RYLSPKDIVDGSANLNLAFVAQIFQH 368
Cdd:cd21186    78 VNISSNDIVDGNPKLTLGLVWSIILH 103
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
274-354 2.45e-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: 40.75  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 274 LKWMNFHLKkagyEKQVTNFSSDVKDGEAYAYLLNAL-----APEHSTHvaletKDPTERAKKVLEQAEKLDCKRYLSPK 348
Cdd:cd21185     7 LRWVRQLLP----DVDVNNFTTDWNDGRLLCGLVNALggsvpGWPNLDP-----EESENNIQRGLEAGKSLGVEPVLTAE 77

                  ....*.
gi 2274899071 349 DIVDGS 354
Cdd:cd21185    78 EMADPE 83
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
394-496 3.23e-04

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


Pssm-ID: 409090  Cd Length: 113  Bit Score: 40.82  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 394 EERCFRLWINS-LGTAT---YVNNVFEDLRNGWVLLEVLDKVSpGSvnwkhankppiKMPFKK---------VENCNEVI 460
Cdd:cd21241     6 QKKTFTNWINSyLAKRKppmKVEDLFEDIKDGTKLLALLEVLS-GE-----------KLPCEKgrrlkrvhfLSNINTAL 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2274899071 461 KIGKDLRFSLVNVAGNDIVQGNKKLLLAFLWQLMRY 496
Cdd:cd21241    74 KFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILY 109
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
412-504 4.21e-04

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: 41.20  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 412 NNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIkMPFKKVENCNEVIKIGKDLRFSLVNVAGNDIVQGNKKLLLAFLW 491
Cdd:cd21325    54 DDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKL-TPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLW 132
                          90
                  ....*....|....*.
gi 2274899071 492 QLMR---YTMLQLLRN 504
Cdd:cd21325   133 QIIKiglFADIELSRN 148
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
153-208 5.17e-04

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: 39.86  E-value: 5.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2274899071 153 NAFFDLVKDGVLLCKLINVAVPGTIdeRAINtKKTLNpWERNENLTlglNSAKAIG 208
Cdd:cd21282    22 DNFMDGLKDGVILCELINKLQPGSV--RKIN-ESTQN-WHKLENIG---NFIKAIM 70
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
273-350 5.33e-04

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) 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. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB 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: 409168  Cd Length: 112  Bit Score: 39.99  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 273 LLKWMnfHLKKAGYEK-QVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAE-KLDCKRYLSPKDI 350
Cdd:cd21319    10 LLLWC--QMKTAGYPNvNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGITKLLDPEDV 87
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
269-368 5.66e-04

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: 39.76  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 269 PEKVLLKWMNFHLKkaGYEKQ-VTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEK-LDCKRYLS 346
Cdd:cd21226     1 SEDGLLAWCRQTTE--GYDGVnITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLE 78
                          90       100
                  ....*....|....*....|...
gi 2274899071 347 PKDIVDGSA-NLNLAFVAQIFQH 368
Cdd:cd21226    79 AEDVMTGNPdERSIVLYTSLFYH 101
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
151-235 6.56e-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: 39.81  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 151 ATNAFFDLVKDGVLLCKLINVavpgtIDERAINTKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGL 230
Cdd:cd21242    26 VVSDLFTDIQDGHRLLDLLEV-----LSGQQLPREKGHNVFQCRSNIETALSFLKNKSIKLINIHVPDIIEGKPSIILGL 100

                  ....*
gi 2274899071 231 ISQII 235
Cdd:cd21242   101 IWTII 105
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
266-351 7.67e-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: 39.67  E-value: 7.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 266 GLAPEKVLLKWMnfHLKKAGYEK-QVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDCKRY 344
Cdd:cd21256    12 GGSKRNALLKWC--QKKTEGYQNiDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAESVGIKST 89

                  ....*..
gi 2274899071 345 LSPKDIV 351
Cdd:cd21256    90 LDINEMV 96
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
153-235 9.10e-04

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


Pssm-ID: 409039  Cd Length: 113  Bit Score: 39.48  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 153 NAFFDLVKDGVLLCKLINVAvpgTIDERAINTKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLIS 232
Cdd:cd21190    28 NDLFVDIKDGTALLRLLEVL---SGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIW 104

                  ...
gi 2274899071 233 QII 235
Cdd:cd21190   105 TII 107
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
395-461 9.81e-04

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: 39.09  E-value: 9.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274899071 395 ERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVnwKHANKPpiKMPFKKVENCNEVIK 461
Cdd:cd21282     5 EEELRVWIEGVTGRRIGDNFMDGLKDGVILCELINKLQPGSV--RKINES--TQNWHKLENIGNFIK 67
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
269-373 1.02e-03

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: 38.95  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 269 PEKVLLKWMNFHLKkaGYEK-QVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDCKRYLSP 347
Cdd:cd21198     2 SGQDLLEWCQEVTK--GYRGvKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDP 79
                          90       100
                  ....*....|....*....|....*.
gi 2274899071 348 KDIVDGSANLNLAFVAQIFQHRNGLT 373
Cdd:cd21198    80 ADMVLLSVPDKLSVMTYLHQIRAHFT 105
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
412-495 1.24e-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: 39.99  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 412 NNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKmPFKKVENCNEVIKIGKDLRFSLVNVAGNDIVQGNKKLLLAFLW 491
Cdd:cd21324    54 DDLFKAVGDGIVLCKMINFSVPDTIDERTINKKKLT-PFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLW 132

                  ....
gi 2274899071 492 QLMR 495
Cdd:cd21324   133 QVIK 136
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
398-494 1.30e-03

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


Pssm-ID: 409160  Cd Length: 124  Bit Score: 39.36  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 398 FRLWINS-LGTA-TYVNNVFEDLRNGWVLLEVLDKVSPGSVnwKHANKPPiKMPFKKVENCNEVIK-IGKDLRFSLVNVA 474
Cdd:cd21311    20 FTRWANEhLKTAnKHIADLETDLSDGLRLIALVEVLSGKKF--PKFNKRP-TFRSQKLENVSVALKfLEEDEGIKIVNID 96
                          90       100
                  ....*....|....*....|
gi 2274899071 475 GNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21311    97 SSDIVDGKLKLILGLIWTLI 116
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
273-365 1.31e-03

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: 39.07  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 273 LLKWMNFHLKKAGYEKQVTNF-SSDVKDGEAYAYLLNALAPEhSTHVALETKDPTERAKK-----VLEQAEKLDCKRYLS 346
Cdd:cd21302     7 ILSWANRKVRTMGRKSQIESFkDKSLSSGLFFLELLWAVEPR-VVNWNLVTKGETDEEKRlnatyIISVARKLGCSIFLL 85
                          90
                  ....*....|....*....
gi 2274899071 347 PKDIVDGSANLNLAFVAQI 365
Cdd:cd21302    86 PEDIVEVNQKMILILTASI 104
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
147-234 1.62e-03

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 38.82  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 147 PIDPATNaFFDLVKDGVLLCKLINVAVPGTIDERAIntKKTLNPWERNENLTLGLNSAKAIGCTVVnIGTQDIAEGRPYL 226
Cdd:cd21218    29 TKKRVTN-FSSDLKDGEVYALLLHSLAPELCDKELV--LEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPEDIVSGNPRL 104

                  ....*...
gi 2274899071 227 VLGLISQI 234
Cdd:cd21218   105 NLAFVATL 112
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
519-616 1.91e-03

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: 38.79  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 519 ILNWANRKVKRGGrTSQADSFRDKNLSSGMFFlELLSAV--------EPRV-VNWSlvtnGETEEDKKLNATYIISVARK 589
Cdd:cd21328    20 LLRWANFHLENAG-WQKINNFSSDIKDSRAYF-HLLNQIapkgqkegEPRIdINMS----GFNEKDDLKRAEYMLQQADK 93
                          90       100
                  ....*....|....*....|....*..
gi 2274899071 590 LGCSIFLLPEDIIEVNQKMMLILAASI 616
Cdd:cd21328    94 LGCRQFVTPADVVSGNPKLNLAFVANL 120
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
412-495 2.33e-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: 38.28  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 412 NNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNEVIKIGKDLRFSLVNVAGNDIVQGNKKLLLAFLW 491
Cdd:cd21293    31 NDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLNSAKAIGCSVVNIGTQDLAEGRPHLVLGLIS 110

                  ....
gi 2274899071 492 QLMR 495
Cdd:cd21293   111 QIIK 114
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
160-235 2.49e-03

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


Pssm-ID: 409069  Cd Length: 105  Bit Score: 38.02  E-value: 2.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274899071 160 KDGVLLCKLINVAVPGTIDERAIntKKTLNPWERNENLTLGLNSAKAIGCTvVNIGTQDIAEGRPYLVLGLISQII 235
Cdd:cd21220    32 STGLFLLDLLAAIDPGAVDYDLV--TEGETDEEKEQNAKYAISLARKIGAV-IFLLWEDIVEVKPKMILTFVASLM 104
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
270-351 3.28e-03

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: 37.64  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 270 EKVLLKWMnfHLKKAGYEK-QVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKL-DCKRYLSP 347
Cdd:cd21261     3 KQILLEWC--RSKTIGYKNiDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80

                  ....
gi 2274899071 348 KDIV 351
Cdd:cd21261    81 EDMM 84
CH_CNN3 cd21284
calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic ...
159-248 3.50e-03

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


Pssm-ID: 409133 [Multi-domain]  Cd Length: 111  Bit Score: 37.58  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 159 VKDGVLLCKLINVAVPGTIdeRAINTKKtLNpWERNENLTlglNSAKAIgcTVVNIGTQDIAEGRPYLVLGLISQiIKIQ 238
Cdd:cd21284    30 LKDGVILCELINKLQPGSI--RKINESK-LN-WHQLENIG---NFIKAI--QAYGMKPHDIFEANDLFENGNMTQ-VQTT 99
                          90
                  ....*....|
gi 2274899071 239 MLADLNFKKT 248
Cdd:cd21284   100 LLALAGLAKT 109
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
273-352 4.08e-03

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


Pssm-ID: 409065  Cd Length: 115  Bit Score: 37.73  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 273 LLKWMnfHLKKAGYEK-QVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEK-LDCKRYLSPKDI 350
Cdd:cd21216    15 LLLWC--QRKTAPYKNvNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKhLDIPKMLDAEDI 92

                  ..
gi 2274899071 351 VD 352
Cdd:cd21216    93 VN 94
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
124-234 4.73e-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: 37.18  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 124 EKASYVSHINNYLRDDpflkSYLPIDPatnaffDLVK---DGVLLCKLINVAVPGTIDerAINTKKTlNPWERNENLTLG 200
Cdd:cd21212     1 EIEIYTDWANHYLEKG----GHKRIIT------DLQKdlgDGLTLVNLIEAVAGEKVP--GIHSRPK-TRAQKLENIQAC 67
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2274899071 201 LNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQI 234
Cdd:cd21212    68 LQFLAALGVDVQGITAEDIVDGNLKAILGLFFSL 101
SCP1 COG5199
Calponin [Cytoskeleton];
391-467 5.17e-03

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 38.36  E-value: 5.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274899071 391 TSREERCFRLWI-NSLGTATYVNNVFED-LRNGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNEVIKIGKDLR 467
Cdd:COG5199    11 MDKQQKEVTLWIeTVLGEKFEPPGDLLSlLKDGVRLCRILNEASPLDIKYKES-----KMPFVQMENISSFINGLKKLR 84
CH_CNN2 cd21283
calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral ...
159-248 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: 36.83  E-value: 6.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 159 VKDGVLLCKLINVAVPGTIdeRAINTKKtlNPWERNENLTlglNSAKAIgcTVVNIGTQDIAEGRPYLVLGLISQiIKIQ 238
Cdd:cd21283    28 LKDGVILCELMNKLQPGSV--PKINRSM--QNWHQLENLS---NFIKAM--VSYGMKPVDLFEANDLFESGNMTQ-VQVS 97
                          90
                  ....*....|
gi 2274899071 239 MLADLNFKKT 248
Cdd:cd21283    98 LLALAGMAKT 107
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
193-235 6.48e-03

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: 36.61  E-value: 6.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2274899071 193 RNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQII 235
Cdd:cd21188    59 RLQNVQTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTII 101
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
270-350 6.67e-03

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


Pssm-ID: 409036  Cd Length: 104  Bit Score: 36.64  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 270 EKVLLKWMNFHLKkaGYEK-QVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQA-EKLDCKRYLSP 347
Cdd:cd21187     2 EKTLLAWCRQSTR--GYEQvDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLDP 79

                  ...
gi 2274899071 348 KDI 350
Cdd:cd21187    80 EDV 82
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
270-362 7.15e-03

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: 36.61  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 270 EKVLLKWMNFHLKKAGYEkqVTNFSSDVKDGEAYAYLLNALAPEHSTHVALETK---DPTERAKKVLEQAEKLDCKRY-L 345
Cdd:cd21215     6 KKTFTKWLNTKLSSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKmrvQKLENVNKALEFIKSRGVKLTnI 83
                          90
                  ....*....|....*..
gi 2274899071 346 SPKDIVDGSANLNLAFV 362
Cdd:cd21215    84 GAEDIVDGNLKLILGLL 100
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
124-246 7.53e-03

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: 37.27  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 124 EKASYVSHINNYLrddpflksyLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDEraintKKTLNPWERNENLTLGLNS 203
Cdd:cd21236    18 QKKTFTKWINQHL---------MKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-----EKGRMRFHRLQNVQIALDY 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2274899071 204 AKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQMLADLNFK 246
Cdd:cd21236    84 LKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVT 126
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
150-235 9.51e-03

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: 36.21  E-value: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274899071 150 PATNAFFDLvKDGVLLCKLINVAvpgtiderainTKKTLNPwERNENLTLGLNSA-KAI------GCTVVNIGTQDIAEG 222
Cdd:cd21186    22 PIKDLFEDL-RDGTRLLALLEVL-----------TGKKLKP-EKGRMRVHHLNNVnRALqvleqnNVKLVNISSNDIVDG 88
                          90
                  ....*....|...
gi 2274899071 223 RPYLVLGLISQII 235
Cdd:cd21186    89 NPKLTLGLVWSII 101
 
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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