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Conserved domains on  [gi|297737515|emb|CBI26716|]
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unnamed protein product, partial [Vitis vinifera]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
123-238 1.07e-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: 251.68  E-value: 1.07e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 123 SEKASYVAHINSYLGDDPFLKQYLPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLN 202
Cdd:cd21293    1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 297737515 203 SAKAIGCTVVNIGTQDLIEGRPHLLLGLISQIIKIQ 238
Cdd:cd21293   81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
391-503 4.45e-78

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: 244.72  E-value: 4.45e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 391 ISREERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPPIKMPFRKVENCNQVIGIGKQLKFSL 470
Cdd:cd21299    2 TSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFSL 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 297737515 471 VNVAGEDIVQGNKKLILAFLWQLMRYNMLQLLK 503
Cdd:cd21299   82 VNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
SAC6 super family cl26648
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
123-617 5.73e-77

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


The actual alignment was detected with superfamily member COG5069:

Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 258.33  E-value: 5.73e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 123 SEKASYVAHINSYLGDDPFLKQYLPlDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKR---VLNPWERNENHTL 199
Cdd:COG5069  119 NEEGELTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKknkALNNFQAFENANK 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 200 CLNSAKAIG-CTVVNIGTQDlieGRPHLLLgLISQIIKIQLLA--DLNLKKTPQLVELVDDGNDveelMGLAPEKVLLKW 276
Cdd:COG5069  198 VIGIARLIGvEDIVNVSIPD---ERSIMTY-VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEIILLRL 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 277 MNFHLKKAGYKkPITNFSSDLKDGEAYAYLLNVLApEHCSPATLDAKDPTHRAKLVLDHAERMDCKRYLSPKdiveGSPN 356
Cdd:COG5069  270 LNLIHLKQANW-KVVNFSKDVSDGENYTDLLNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPPA----GNPK 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 357 LNLAFVAQIFHQRSGLSAdCKNISFAEMMTDDVLISREERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKV-SPGS 435
Cdd:COG5069  344 LDLAFVAHLFNTHPGQEP-LEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMT 422
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 436 VNWKRASKPPIK----MPFRKVENCNQVIGIGKQLKFSLVNVAGEDIVQGNkKLILAFLWQLMRYNMLQLLKNLRfhSQG 511
Cdd:COG5069  423 VTHKLVKKQPASgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHVLK--KDG 499
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 512 KEMTDADILKWANNKVKRTGRTSQMESFKDKNLSN-GIFFLDLLSAVEPRVVNWNLVTKGESEEEKKLNA-TYIIS--VA 587
Cdd:COG5069  500 CGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVsGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSLAISskIL 579
                        490       500       510
                 ....*....|....*....|....*....|.
gi 297737515 588 RKLGCSIFLLPEDIMEVNQKM-ILTLTASIM 617
Cdd:COG5069  580 RSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
 
Name Accession Description Interval E-value
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
123-238 1.07e-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: 251.68  E-value: 1.07e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 123 SEKASYVAHINSYLGDDPFLKQYLPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLN 202
Cdd:cd21293    1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 297737515 203 SAKAIGCTVVNIGTQDLIEGRPHLLLGLISQIIKIQ 238
Cdd:cd21293   81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
391-503 4.45e-78

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: 244.72  E-value: 4.45e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 391 ISREERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPPIKMPFRKVENCNQVIGIGKQLKFSL 470
Cdd:cd21299    2 TSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFSL 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 297737515 471 VNVAGEDIVQGNKKLILAFLWQLMRYNMLQLLK 503
Cdd:cd21299   82 VNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
123-617 5.73e-77

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 258.33  E-value: 5.73e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 123 SEKASYVAHINSYLGDDPFLKQYLPlDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKR---VLNPWERNENHTL 199
Cdd:COG5069  119 NEEGELTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKknkALNNFQAFENANK 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 200 CLNSAKAIG-CTVVNIGTQDlieGRPHLLLgLISQIIKIQLLA--DLNLKKTPQLVELVDDGNDveelMGLAPEKVLLKW 276
Cdd:COG5069  198 VIGIARLIGvEDIVNVSIPD---ERSIMTY-VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEIILLRL 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 277 MNFHLKKAGYKkPITNFSSDLKDGEAYAYLLNVLApEHCSPATLDAKDPTHRAKLVLDHAERMDCKRYLSPKdiveGSPN 356
Cdd:COG5069  270 LNLIHLKQANW-KVVNFSKDVSDGENYTDLLNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPPA----GNPK 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 357 LNLAFVAQIFHQRSGLSAdCKNISFAEMMTDDVLISREERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKV-SPGS 435
Cdd:COG5069  344 LDLAFVAHLFNTHPGQEP-LEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMT 422
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 436 VNWKRASKPPIK----MPFRKVENCNQVIGIGKQLKFSLVNVAGEDIVQGNkKLILAFLWQLMRYNMLQLLKNLRfhSQG 511
Cdd:COG5069  423 VTHKLVKKQPASgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHVLK--KDG 499
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 512 KEMTDADILKWANNKVKRTGRTSQMESFKDKNLSN-GIFFLDLLSAVEPRVVNWNLVTKGESEEEKKLNA-TYIIS--VA 587
Cdd:COG5069  500 CGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVsGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSLAISskIL 579
                        490       500       510
                 ....*....|....*....|....*....|.
gi 297737515 588 RKLGCSIFLLPEDIMEVNQKM-ILTLTASIM 617
Cdd:COG5069  580 RSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
513-621 6.29e-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: 225.90  E-value: 6.29e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 513 EMTDADILKWANNKVKRTGRTSQMESFKDKNLSNGIFFLDLLSAVEPRVVNWNLVTKGESEEEKKLNATYIISVARKLGC 592
Cdd:cd21302    1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80
                         90       100
                 ....*....|....*....|....*....
gi 297737515 593 SIFLLPEDIMEVNQKMILTLTASIMYWSL 621
Cdd:cd21302   81 SIFLLPEDIVEVNQKMILILTASIMYWSL 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
267-367 4.72e-24

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 97.36  E-value: 4.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515  267 LAPEKVLLKWMNFHLKKAGYKKPITNFSSDLKDGEAYAYLLNVLAPEHCSPATL--DAKDPTHRAKLVLDHAER-MDCKR 343
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKkLGVPK 80
                          90       100
                  ....*....|....*....|....*
gi 297737515  344 YLS-PKDIVEGSPNLNLAFVAQIFH 367
Cdd:pfam00307  81 VLIePEDLVEGDNKSVLTYLASLFR 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
398-496 2.21e-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: 86.60  E-value: 2.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515   398 FRLWINSLG---IVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPpiKMPFRKVENCNQVIGIGKQLKFSLVNVA 474
Cdd:smart00033   3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 297737515   475 GEDIVQGnKKLILAFLWQLMRY 496
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
394-498 3.00e-18

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: 80.79  E-value: 3.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515  394 EERCFRLWINSL----GIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRaskpPIKMPFRKVENCNQVIGIG-KQLKF 468
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK----LNKSEFDKLENINLALDVAeKKLGV 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 297737515  469 SLVNVAGEDIVQGNKKLILAFLWQLMRYNM 498
Cdd:pfam00307  79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
149-237 1.01e-16

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 75.82  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515   149 DPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKrvLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGrPHLLL 228
Cdd:smart00033  16 KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFEPEDLVEG-PKLIL 92

                   ....*....
gi 297737515   229 GLISQIIKI 237
Cdd:smart00033  93 GVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
122-236 6.99e-16

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 73.86  E-value: 6.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515  122 ESEKASYVAHINSYLGDDPflkqylpLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKrvlnPWERNENHTLCL 201
Cdd:pfam00307   1 LELEKELLRWINSHLAEYG-------PGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLAL 69
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 297737515  202 NSA-KAIGCTVVNIGTQDLIEGRPHLLLGLISQIIK 236
Cdd:pfam00307  70 DVAeKKLGVPKVLIEPEDLVEGDNKSVLTYLASLFR 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
271-366 7.16e-16

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 73.50  E-value: 7.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515   271 KVLLKWMNFHLKKAGyKKPITNFSSDLKDGEAYAYLLNVLAP----EHCSPATLDAKDPTHRAKLVLDHAERMDCKR-YL 345
Cdd:smart00033   1 KTLLRWVNSLLAEYD-KPPVTNFSSDLKDGVALCALLNSLSPglvdKKKVAASLSRFKKIENINLALSFAEKLGGKVvLF 79
                           90       100
                   ....*....|....*....|.
gi 297737515   346 SPKDIVEGsPNLNLAFVAQIF 366
Cdd:smart00033  80 EPEDLVEG-PKLILGVIWTLI 99
 
Name Accession Description Interval E-value
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
123-238 1.07e-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: 251.68  E-value: 1.07e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 123 SEKASYVAHINSYLGDDPFLKQYLPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLN 202
Cdd:cd21293    1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 297737515 203 SAKAIGCTVVNIGTQDLIEGRPHLLLGLISQIIKIQ 238
Cdd:cd21293   81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
391-503 4.45e-78

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: 244.72  E-value: 4.45e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 391 ISREERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPPIKMPFRKVENCNQVIGIGKQLKFSL 470
Cdd:cd21299    2 TSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFSL 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 297737515 471 VNVAGEDIVQGNKKLILAFLWQLMRYNMLQLLK 503
Cdd:cd21299   82 VNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
123-617 5.73e-77

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 258.33  E-value: 5.73e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 123 SEKASYVAHINSYLGDDPFLKQYLPlDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKR---VLNPWERNENHTL 199
Cdd:COG5069  119 NEEGELTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKknkALNNFQAFENANK 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 200 CLNSAKAIG-CTVVNIGTQDlieGRPHLLLgLISQIIKIQLLA--DLNLKKTPQLVELVDDGNDveelMGLAPEKVLLKW 276
Cdd:COG5069  198 VIGIARLIGvEDIVNVSIPD---ERSIMTY-VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEIILLRL 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 277 MNFHLKKAGYKkPITNFSSDLKDGEAYAYLLNVLApEHCSPATLDAKDPTHRAKLVLDHAERMDCKRYLSPKdiveGSPN 356
Cdd:COG5069  270 LNLIHLKQANW-KVVNFSKDVSDGENYTDLLNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPPA----GNPK 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 357 LNLAFVAQIFHQRSGLSAdCKNISFAEMMTDDVLISREERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKV-SPGS 435
Cdd:COG5069  344 LDLAFVAHLFNTHPGQEP-LEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMT 422
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 436 VNWKRASKPPIK----MPFRKVENCNQVIGIGKQLKFSLVNVAGEDIVQGNkKLILAFLWQLMRYNMLQLLKNLRfhSQG 511
Cdd:COG5069  423 VTHKLVKKQPASgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHVLK--KDG 499
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 512 KEMTDADILKWANNKVKRTGRTSQMESFKDKNLSN-GIFFLDLLSAVEPRVVNWNLVTKGESEEEKKLNA-TYIIS--VA 587
Cdd:COG5069  500 CGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVsGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSLAISskIL 579
                        490       500       510
                 ....*....|....*....|....*....|.
gi 297737515 588 RKLGCSIFLLPEDIMEVNQKM-ILTLTASIM 617
Cdd:COG5069  580 RSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
513-621 6.29e-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: 225.90  E-value: 6.29e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 513 EMTDADILKWANNKVKRTGRTSQMESFKDKNLSNGIFFLDLLSAVEPRVVNWNLVTKGESEEEKKLNATYIISVARKLGC 592
Cdd:cd21302    1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80
                         90       100
                 ....*....|....*....|....*....
gi 297737515 593 SIFLLPEDIMEVNQKMILTLTASIMYWSL 621
Cdd:cd21302   81 SIFLLPEDIVEVNQKMILILTASIMYWSL 109
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
260-367 2.69e-69

second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409145  Cd Length: 109  Bit Score: 221.24  E-value: 2.69e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 260 DVEELMGLAPEKVLLKWMNFHLKKAGYKKPITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAKLVLDHAERM 339
Cdd:cd21296    2 DVEELLRLPPEKVLLKWMNFHLKKAGYKKTVTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEKM 81
                         90       100
                 ....*....|....*....|....*...
gi 297737515 340 DCKRYLSPKDIVEGSPNLNLAFVAQIFH 367
Cdd:cd21296   82 NCKRYLTAKDIVEGSANLNLAFVAQIFH 109
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
392-502 3.61e-61

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 199.82  E-value: 3.61e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 392 SREERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPPIKMPFRKVENCNQVIGIGKQLKFSLV 471
Cdd:cd21219    3 SREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKPLNKFKKVENCNYAVDLAKKLGFSLV 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 297737515 472 NVAGEDIVQGNKKLILAFLWQLMRYNMLQLL 502
Cdd:cd21219   83 GIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
123-236 1.90e-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: 187.40  E-value: 1.90e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 123 SEKASYVAHINSYLGDDPFLKQYLPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLN 202
Cdd:cd21217    1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKNIFEATENLNLALN 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 297737515 203 SAKAIGCTVVNIGTQDLIEGRPHLLLGLISQIIK 236
Cdd:cd21217   81 AAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
101-245 4.02e-56

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


Pssm-ID: 409141  Cd Length: 145  Bit Score: 187.49  E-value: 4.02e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 101 GSNHSSSflkattttllhtiiESEKASYVAHINSYLGDDPFLKQYLPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDER 180
Cdd:cd21292   16 GTTHSYS--------------EEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDER 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297737515 181 AINTKRvLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRPHLLLGLISQIIKIQLLADLNL 245
Cdd:cd21292   82 AINKKK-LTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
514-618 2.81e-52

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


Pssm-ID: 409069  Cd Length: 105  Bit Score: 175.92  E-value: 2.81e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 514 MTDADILKWANNKVKRTGRTSQMESFKDKNLSNGIFFLDLLSAVEPRVVNWNLVTKGESEEEKKLNATYIISVARKLGCS 593
Cdd:cd21220    1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLVTEGETDEEKEQNAKYAISLARKIGAV 80
                         90       100
                 ....*....|....*....|....*
gi 297737515 594 IFLLPEDIMEVNQKMILTLTASIMY 618
Cdd:cd21220   81 IFLLWEDIVEVKPKMILTFVASLMA 105
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
392-502 1.64e-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: 157.78  E-value: 1.64e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 392 SREERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPPIKMP--FRKVENCNQVIGIGKQLKFS 469
Cdd:cd21298    5 TREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGanMKKIENCNYAVELGKKLKFS 84
                         90       100       110
                 ....*....|....*....|....*....|...
gi 297737515 470 LVNVAGEDIVQGNKKLILAFLWQLMRYNMLQLL 502
Cdd:cd21298   85 LVGIGGKDIYDGNRTLTLALVWQLMRAYTLSIL 117
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
122-245 2.38e-45

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 158.28  E-value: 2.38e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 122 ESEKASYVAHINSYLGDDPFLKQYLPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKRvLNPWERNENHTLCL 201
Cdd:cd21323   23 EEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDERAINKKK-LTPFTISENLNLAL 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 297737515 202 NSAKAIGCTVVNIGTQDLIEGRPHLLLGLISQIIKIQLLADLNL 245
Cdd:cd21323  102 NSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
257-366 2.15e-44

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: 154.74  E-value: 2.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 257 DGNDVEELMGLAPEKVLLKWMNFHLKKAGYKKPITNFSSDLKDGEAYAYLLNVLAPEHCSPAT--LDAKDPTHRAKLVLD 334
Cdd:cd21295    1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRRIKNFSGDIKDSEAYTHLLKQIAPKDAGVDTsaLRESDLLQRAELMLQ 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 297737515 335 HAERMDCKRYLSPKDIVEGSPNLNLAFVAQIF 366
Cdd:cd21295   81 NADKIGCRKFVTPKDVVTGNPKLNLAFVANLF 112
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
511-617 9.06e-43

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: 149.88  E-value: 9.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 511 GKEMTDADILKWANNKVKRTGRTSQMESFKDKNLSNGIFFLDLLSAVEPRVVNWNLVTKGESEEEKKLNATYIISVARKL 590
Cdd:cd21303    1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLVTPGNTEDEAYLNAKLAISIARKL 80
                         90       100
                 ....*....|....*....|....*..
gi 297737515 591 GCSIFLLPEDIMEVNQKMILTLTASIM 617
Cdd:cd21303   81 GALIFLVPEDIVEVRPRLVLTFIGSLM 107
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
260-367 2.35e-42

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: 148.99  E-value: 2.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 260 DVEELMGLAPEKVLLKWMNFHLKKAGY-KKPITNFSSDLKDGEAYAYLLNVLAPEHCSPA----TLDAKDPTHRAKLVLD 334
Cdd:cd21218    2 TLESLLYLPPEEILLRWVNYHLKKAGPtKKRVTNFSSDLKDGEVYALLLHSLAPELCDKElvleVLSEEDLEKRAEKVLQ 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 297737515 335 HAERMDCKRYLSPKDIVEGSPNLNLAFVAQIFH 367
Cdd:cd21218   82 AAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
393-502 3.40e-42

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: 148.73  E-value: 3.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 393 REERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPP---IKMPFRKVENCNQVIGIGKQLKFS 469
Cdd:cd21300    7 REARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaEISRFKAVENTNYAVELGKQLGFS 86
                         90       100       110
                 ....*....|....*....|....*....|...
gi 297737515 470 LVNVAGEDIVQGNKKLILAFLWQLMRYNMLQLL 502
Cdd:cd21300   87 LVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
122-247 8.53e-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: 140.58  E-value: 8.53e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 122 ESEKASYVAHINSYLGDDPFLKQYLPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKRvLNPWERNENHTLCL 201
Cdd:cd21325   23 EEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKK-LTPFIIQENLNLAL 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 297737515 202 NSAKAIGCTVVNIGTQDLIEGRPHLLLGLISQIIKIQLLADLNLKK 247
Cdd:cd21325  102 NSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSR 147
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
122-236 1.63e-38

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 138.73  E-value: 1.63e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 122 ESEKASYVAHINSYLGDDPFLKQYLPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTK----RVLNPWERNENH 197
Cdd:cd21294    5 EDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPprknKPLNNFQMIENN 84
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 297737515 198 TLCLNSAKAIGCTVVNIGTQDLIEGRPHLLLGLISQIIK 236
Cdd:cd21294   85 NIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIR 123
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
122-245 4.80e-38

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


Pssm-ID: 409173  Cd Length: 145  Bit Score: 138.22  E-value: 4.80e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 122 ESEKASYVAHINSYLGDDPFLKQYLPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKRvLNPWERNENHTLCL 201
Cdd:cd21324   23 EEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKK-LTPFTIQENLNLAL 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 297737515 202 NSAKAIGCTVVNIGTQDLIEGRPHLLLGLISQIIKIQLLADLNL 245
Cdd:cd21324  102 NSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
515-617 7.44e-38

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


Pssm-ID: 409150  Cd Length: 107  Bit Score: 136.26  E-value: 7.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 515 TDADILKWANNKVKRTGRTSQMESFKDKNLSNGIFFLDLLSAVEPRVVNWNLVTKGESEEEKKLNATYIISVARKLGCSI 594
Cdd:cd21301    2 SDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLVLEGNSEEDKLSNAKYAISMARKIGARV 81
                         90       100
                 ....*....|....*....|...
gi 297737515 595 FLLPEDIMEVNQKMILTLTASIM 617
Cdd:cd21301   82 YALPEDIVEVKPKMVMTVFACLM 104
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
261-367 9.98e-37

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


Pssm-ID: 409146  Cd Length: 109  Bit Score: 133.07  E-value: 9.98e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 261 VEELMGLAPEKVLLKWMNFHLKKAGYKKPITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAKLVLDHAERMD 340
Cdd:cd21297    3 LEQFLRLPPEQILLRWFNYHLKAANWPRRVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDLLQRAEQVLQNAEKLD 82
                         90       100
                 ....*....|....*....|....*..
gi 297737515 341 CKRYLSPKDIVEGSPNLNLAFVAQIFH 367
Cdd:cd21297   83 CRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
254-367 8.18e-32

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: 119.69  E-value: 8.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 254 LVDDGNDVEELMGLAPEKVLLKWMNFHLKKAGYKKpITNFSSDLKDGEAYAYLLNVLAPE---------HCSPATLDAKD 324
Cdd:cd21328    1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQK-INNFSSDIKDSRAYFHLLNQIAPKgqkegepriDINMSGFNEKD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 297737515 325 PTHRAKLVLDHAERMDCKRYLSPKDIVEGSPNLNLAFVAQIFH 367
Cdd:cd21328   80 DLKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
254-368 1.70e-31

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


Pssm-ID: 409176  Cd Length: 125  Bit Score: 118.91  E-value: 1.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 254 LVDDGNDVEELMGLAPEKVLLKWMNFHLKKAGYKKpITNFSSDLKDGEAYAYLLNVLAP---EHCSPAT------LDAKD 324
Cdd:cd21327    1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNK-INNFSSDIKDSKAYYHLLNQVAPkgdEEGIPAIvidmsgLREKD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 297737515 325 PTHRAKLVLDHAERMDCKRYLSPKDIVEGSPNLNLAFVAQIFHQ 368
Cdd:cd21327   80 DLKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNK 123
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
257-367 2.94e-30

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: 115.37  E-value: 2.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 257 DGNDVEELMGLAPEKVLLKWMNFHLKKAGYKKpITNFSSDLKDGEAYAYLLNVLAPE--------HCSPATLDAKDPTHR 328
Cdd:cd21326    1 EGEELEELMKLSPEELLLRWVNYHLTNAGWQN-ISNFSQDIKDSRAYFHLLNQIAPKgdvfdeniEIDFSGFNEKNDLKR 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 297737515 329 AKLVLDHAERMDCKRYLSPKDIVEGSPNLNLAFVAQIFH 367
Cdd:cd21326   80 AEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 118
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
392-502 1.46e-28

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 110.46  E-value: 1.46e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 392 SREERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKVSPgSVNWKRASKPPIKM---PFRKVENCNQVIGIGK-QLK 467
Cdd:cd21329    5 SSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRV-PVDWGHVNKPPYPAlggNMKKIENCNYAVELGKnKAK 83
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 297737515 468 FSLVNVAGEDIVQGNKKLILAFLWQLMRYNMLQLL 502
Cdd:cd21329   84 FSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
392-502 3.19e-26

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: 104.31  E-value: 3.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 392 SREERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKVSPgSVNWKRASKPP---IKMPFRKVENCNQVIGIGKQ-LK 467
Cdd:cd21331   21 TREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKV-PVDWNKVNKPPypkLGANMKKLENCNYAVELGKHpAK 99
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 297737515 468 FSLVNVAGEDIVQGNKKLILAFLWQLMRYNMLQLL 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 8.26e-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: 8.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 392 SREERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKVSPgSVNWKRASKPP---IKMPFRKVENCNQVIGIGK-QLK 467
Cdd:cd21330   12 TREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKV-PVDWNRVNKPPypkLGENMKKLENCNYAVELGKnKAK 90
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 297737515 468 FSLVNVAGEDIVQGNKKLILAFLWQLMRYNMLQLL 502
Cdd:cd21330   91 FSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 125
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
516-617 1.08e-25

fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the fourth CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409183  Cd Length: 112  Bit Score: 101.89  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 516 DADILKWANNKVKRTGRTSQMESFKDKNLSNGIFFLDLLSAVEPRVVNWNLVTKGE-SEEEKKLNATYIISVARKLGCSI 594
Cdd:cd21334    3 DDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNlTDDDKLDNAKYAVSMARKIGARV 82
                         90       100
                 ....*....|....*....|...
gi 297737515 595 FLLPEDIMEVNQKMILTLTASIM 617
Cdd:cd21334   83 YALPEDLVEVKPKMVMTVFACLM 105
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
509-617 3.32e-25

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: 100.83  E-value: 3.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 509 SQGKEMTDADILKWANNKVKRTGRTSQMESFKDKNLSNGIFFLDLLSAVEPRVVNWNLVTKGESEEEKKLN-ATYIISVA 587
Cdd:cd21333    1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNnAKYAISMA 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 297737515 588 RKLGCSIFLLPEDIMEVNQKMILTLTASIM 617
Cdd:cd21333   81 RKIGARVYALPEDLVEVKPKMVMTVFACLM 110
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
267-367 4.72e-24

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 97.36  E-value: 4.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515  267 LAPEKVLLKWMNFHLKKAGYKKPITNFSSDLKDGEAYAYLLNVLAPEHCSPATL--DAKDPTHRAKLVLDHAER-MDCKR 343
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKkLGVPK 80
                          90       100
                  ....*....|....*....|....*
gi 297737515  344 YLS-PKDIVEGSPNLNLAFVAQIFH 367
Cdd:pfam00307  81 VLIePEDLVEGDNKSVLTYLASLFR 105
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
510-617 2.98e-23

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


Pssm-ID: 409181  Cd Length: 115  Bit Score: 95.01  E-value: 2.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 510 QGKEMTDADILKWANNKVKRTGRTSQMESFKDKNLSNGIFFLDLLSAVEPRVVNWNLVTKGESEEEKKLN-ATYIISVAR 588
Cdd:cd21332    4 EGEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDLSDADKLNnAKYAISVAR 83
                         90       100
                 ....*....|....*....|....*....
gi 297737515 589 KLGCSIFLLPEDIMEVNQKMILTLTASIM 617
Cdd:cd21332   84 KIGARVYALPEDLVEVKPKMVMTVFACLM 112
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
398-496 2.21e-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: 86.60  E-value: 2.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515   398 FRLWINSLG---IVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPpiKMPFRKVENCNQVIGIGKQLKFSLVNVA 474
Cdd:smart00033   3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 297737515   475 GEDIVQGnKKLILAFLWQLMRY 496
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
394-498 3.00e-18

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: 80.79  E-value: 3.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515  394 EERCFRLWINSL----GIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRaskpPIKMPFRKVENCNQVIGIG-KQLKF 468
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK----LNKSEFDKLENINLALDVAeKKLGV 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 297737515  469 SLVNVAGEDIVQGNKKLILAFLWQLMRYNM 498
Cdd:pfam00307  79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
394-495 5.60e-18

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 79.93  E-value: 5.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS-----------LGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPPIKMPFRKVENCNQVIGI 462
Cdd:cd21217    2 EKEAFVEHINSlladdpdlkhlLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKNIFEATENLNLALNA 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 297737515 463 GKQLKFSLVNVAGEDIVQGNKKLILAFLWQLMR 495
Cdd:cd21217   82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
149-237 1.01e-16

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 75.82  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515   149 DPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKrvLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGrPHLLL 228
Cdd:smart00033  16 KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFEPEDLVEG-PKLIL 92

                   ....*....
gi 297737515   229 GLISQIIKI 237
Cdd:smart00033  93 GVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
518-617 1.05e-16

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 76.17  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515  518 DILKWANNKVKRTGRTSQMESFKdKNLSNGIFFLDLLSAVEPRVVNWNLVTKgeSEEEKKLNATYIISVAR-KLGCSIFL 596
Cdd:pfam00307   6 ELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKLNK--SEFDKLENINLALDVAEkKLGVPKVL 82
                          90       100
                  ....*....|....*....|..
gi 297737515  597 L-PEDIMEVNQKMILTLTASIM 617
Cdd:pfam00307  83 IePEDLVEGDNKSVLTYLASLF 104
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
122-236 6.99e-16

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 73.86  E-value: 6.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515  122 ESEKASYVAHINSYLGDDPflkqylpLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKrvlnPWERNENHTLCL 201
Cdd:pfam00307   1 LELEKELLRWINSHLAEYG-------PGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLAL 69
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 297737515  202 NSA-KAIGCTVVNIGTQDLIEGRPHLLLGLISQIIK 236
Cdd:pfam00307  70 DVAeKKLGVPKVLIEPEDLVEGDNKSVLTYLASLFR 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
271-366 7.16e-16

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 73.50  E-value: 7.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515   271 KVLLKWMNFHLKKAGyKKPITNFSSDLKDGEAYAYLLNVLAP----EHCSPATLDAKDPTHRAKLVLDHAERMDCKR-YL 345
Cdd:smart00033   1 KTLLRWVNSLLAEYD-KPPVTNFSSDLKDGVALCALLNSLSPglvdKKKVAASLSRFKKIENINLALSFAEKLGGKVvLF 79
                           90       100
                   ....*....|....*....|.
gi 297737515   346 SPKDIVEGsPNLNLAFVAQIF 366
Cdd:smart00033  80 EPEDLVEG-PKLILGVIWTLI 99
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
518-619 8.78e-16

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 73.50  E-value: 8.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515   518 DILKWANNKVKrtGRTSQMESFKDKNLSNGIFFLDLLSAVEPRVVNWNLVTKGESEEEKKLNATYIISVARKLGCSIFLL 597
Cdd:smart00033   2 TLLRWVNSLLA--EYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79
                           90       100
                   ....*....|....*....|...
gi 297737515   598 -PEDIMEVNqKMILTLTASIMYW 619
Cdd:smart00033  80 ePEDLVEGP-KLILGVIWTLISL 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
125-236 3.78e-15

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 71.60  E-value: 3.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 125 KASYVAHINSYLGDDpflkqylpLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKrvlNPWERNENHTLCLNSA 204
Cdd:cd00014    1 EEELLKWINEVLGEE--------LPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPK---SPFKKRENINLFLNAC 69
                         90       100       110
                 ....*....|....*....|....*....|....
gi 297737515 205 KAIG-CTVVNIGTQDLIEGR-PHLLLGLISQIIK 236
Cdd:cd00014   70 KKLGlPELDLFEPEDLYEKGnLKKVLGTLWALAL 103
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
146-240 3.02e-14

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 69.23  E-value: 3.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 146 LPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRPH 225
Cdd:cd21219   16 LGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKPLNKFKKVENCNYAVDLAKKLGFSLVGIGGKDIADGNRK 95
                         90
                 ....*....|....*
gi 297737515 226 LLLGLISQIIKIQLL 240
Cdd:cd21219   96 LTLALVWQLMRYHVL 110
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
395-495 2.64e-11

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 60.82  E-value: 2.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 395 ERCFRLWINSL---GIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKrasKPPIKMPFRKVENCNQVIGIGKQLKF-SL 470
Cdd:cd00014    1 EEELLKWINEVlgeELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI---NKKPKSPFKKRENINLFLNACKKLGLpEL 77
                         90       100
                 ....*....|....*....|....*.
gi 297737515 471 VNVAGEDIVQ-GNKKLILAFLWQLMR 495
Cdd:cd00014   78 DLFEPEDLYEkGNLKKVLGTLWALAL 103
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
391-494 2.85e-10

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: 57.80  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 391 ISREERCFRLWIN----SLGIVtyVNNLFEDVRNGWILLEVLDKVSPGSVNwKRASKPpiKMPFRKVENCNQVIGIGKQL 466
Cdd:cd21215    2 VDVQKKTFTKWLNtklsSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLG-RYNKNP--KMRVQKLENVNKALEFIKSR 76
                         90       100
                 ....*....|....*....|....*...
gi 297737515 467 KFSLVNVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21215   77 GVKLTNIGAEDIVDGNLKLILGLLWTLI 104
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
394-494 4.82e-10

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: 57.69  E-value: 4.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS--LGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRAskppiKMPFRKVENCNQVIGIGKQLKFSLV 471
Cdd:cd21236   18 QKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKG-----RMRFHRLQNVQIALDYLKRRQVKLV 92
                         90       100
                 ....*....|....*....|...
gi 297737515 472 NVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21236   93 NIRNDDITDGNPKLTLGLIWTII 115
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
394-491 6.24e-10

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


Pssm-ID: 409037  Cd Length: 105  Bit Score: 56.64  E-value: 6.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS--LGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRAskppiKMPFRKVENCNQVIGIGKQLKFSLV 471
Cdd:cd21188    4 QKKTFTKWVNKhlIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERG-----RMRFHRLQNVQTALDFLKYRKIKLV 78
                         90       100
                 ....*....|....*....|
gi 297737515 472 NVAGEDIVQGNKKLILAFLW 491
Cdd:cd21188   79 NIRAEDIVDGNPKLTLGLIW 98
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
269-357 6.52e-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: 56.48  E-value: 6.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 269 PEKVLLKWMNFHLkkAGYKkpITNFSSDLKDGEAYAYLLNVLAPEHCSP-ATLDAKDPTHRAKLVLDHAER-MDCKRYLS 346
Cdd:cd21184    2 GKSLLLEWVNSKI--PEYK--VKNFTTDWNDGKALAALVDALKPGLIPDnESLDKENPLENATKAMDIAEEeLGIPKIIT 77
                         90
                 ....*....|.
gi 297737515 347 PKDIVegSPNL 357
Cdd:cd21184   78 PEDMV--SPNV 86
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
394-491 6.59e-10

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: 56.62  E-value: 6.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINSLGIVT---YVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASkppikMPFRKVENCNQVIGIGKQLKFSL 470
Cdd:cd21186    3 QKKTFTKWINSQLSKAnkpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGR-----MRVHHLNNVNRALQVLEQNNVKL 77
                         90       100
                 ....*....|....*....|.
gi 297737515 471 VNVAGEDIVQGNKKLILAFLW 491
Cdd:cd21186   78 VNISSNDIVDGNPKLTLGLVW 98
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
391-495 8.30e-10

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 57.07  E-value: 8.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 391 ISREERC-FRLWINS-----------LGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPPIKM----PFRKVE 454
Cdd:cd21294    3 INEDERReFTKHINAvlagdpdvgsrLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPPRKNkplnNFQMIE 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 297737515 455 NCNQVIGIGKQLKFSLVNVAGEDIVQGNKKLILAFLWQLMR 495
Cdd:cd21294   83 NNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIR 123
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
394-494 6.36e-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: 55.03  E-value: 6.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS-LGIVT-YVNNLFEDVRNGWILLEVLDKVSPgsvnwKRASKPPI-KMPFRKVENCNQVIGIGKQLKFSL 470
Cdd:cd21318   39 QKKTFTKWVNShLARVPcRINDLYTDLRDGYVLTRLLEVLSG-----EQLPKPTRgRMRIHSLENVDKALQFLKEQRVHL 113
                         90       100
                 ....*....|....*....|....
gi 297737515 471 VNVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21318  114 ENVGSHDIVDGNHRLTLGLIWTII 137
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
270-353 9.54e-09

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: 53.50  E-value: 9.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 270 EKVLLKWMNFHLKKAGyKKPITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAK---LVLDHAER--MDCKRY 344
Cdd:cd00014    1 EEELLKWINEVLGEEL-PVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKREninLFLNACKKlgLPELDL 79

                 ....*....
gi 297737515 345 LSPKDIVEG 353
Cdd:cd00014   80 FEPEDLYEK 88
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
520-616 1.09e-08

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 53.46  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 520 LKWANNKVKRTGRT-SQMESFkDKNLSNGIFFLDLLSAVEPRVVNWNLVTKGESEEEKKLNATYIISVARKLGCSIFLLP 598
Cdd:cd21218   16 LRWVNYHLKKAGPTkKRVTNF-SSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYFLTP 94
                         90
                 ....*....|....*...
gi 297737515 599 EDIMEVNQKMILTLTASI 616
Cdd:cd21218   95 EDIVSGNPRLNLAFVATL 112
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
394-495 1.43e-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: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINSL----GIVTyVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPpiKMPFRKVENCNQVIG-IGKQLKF 468
Cdd:cd21225    5 QIKAFTAWVNSVlekrGIPK-ISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEP--KNRIQMIQNLHLAMLfIEEDLKI 81
                         90       100
                 ....*....|....*....|....*..
gi 297737515 469 SLVNVAGEDIVQGNKKLILAFLWQLMR 495
Cdd:cd21225   82 RVQGIGAEDFVDNNKKLILGLLWTLYR 108
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
394-491 1.48e-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: 53.14  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS-LGIVT-YVNNLFEDVRNGWILLEVLDKVSPgsvnwKRASKP-PIKMPFRKVENCNQVIGIGKQLKFSL 470
Cdd:cd21246   17 QKKTFTKWVNShLARVGcRINDLYTDLRDGRMLIKLLEVLSG-----ERLPKPtKGKMRIHCLENVDKALQFLKEQRVHL 91
                         90       100
                 ....*....|....*....|.
gi 297737515 471 VNVAGEDIVQGNKKLILAFLW 491
Cdd:cd21246   92 ENMGSHDIVDGNHRLTLGLIW 112
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
391-491 1.61e-08

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


Pssm-ID: 409042  Cd Length: 116  Bit Score: 53.07  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 391 ISREERCFRLWINSLGIVT--YVNNLFEDVRNGWILLEVLDKVSPGSVNwkRASKPpiKMPFRKVENCNQVIGIGKQlKF 468
Cdd:cd21193   14 INIQKKTFTKWINSFLEKAnlEIGDLFTDLSDGKLLLKLLEIISGEKLG--KPNRG--RLRVQKIENVNKALAFLKT-KV 88
                         90       100
                 ....*....|....*....|...
gi 297737515 469 SLVNVAGEDIVQGNKKLILAFLW 491
Cdd:cd21193   89 RLENIGAEDIVDGNPRLILGLIW 111
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
394-494 2.56e-08

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: 52.32  E-value: 2.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINSLGIVT---YVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPpikmpFRKVENCNQVIGIGKQLKFSL 470
Cdd:cd21232    3 QKKTFTKWINARFSKSgkpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTR-----VHALNNVNRVLQVLHQNNVEL 77
                         90       100
                 ....*....|....*....|....
gi 297737515 471 VNVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21232   78 VNIGGTDIVDGNHKLTLGLLWSII 101
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
394-494 2.86e-08

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


Pssm-ID: 409086  Cd Length: 118  Bit Score: 52.34  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS--LGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRAskppiKMPFRKVENCNQVIGIGKQLKFSLV 471
Cdd:cd21237    7 QKKTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKG-----RMRFHRLQNVQIALDFLKQRQVKLV 81
                         90       100
                 ....*....|....*....|...
gi 297737515 472 NVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21237   82 NIRNDDITDGNPKLTLGLIWTII 104
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
394-494 6.08e-08

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


Pssm-ID: 409084  Cd Length: 119  Bit Score: 51.56  E-value: 6.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS--LGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRAskppiKMPFRKVENCNQVIGIGKQLKFSLV 471
Cdd:cd21235    7 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 81
                         90       100
                 ....*....|....*....|...
gi 297737515 472 NVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21235   82 NIRNDDIADGNPKLTLGLIWTII 104
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
394-495 6.58e-08

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: 52.28  E-value: 6.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS-----------LGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNwKRASKPPIKMPFRKVENCNQVIGI 462
Cdd:cd21292   25 EKVAFVNWINKnlgddpdckhlLPMDPNTDDLFEKVKDGILLCKMINLSVPDTID-ERAINKKKLTVFTIHENLTLALNS 103
                         90       100       110
                 ....*....|....*....|....*....|...
gi 297737515 463 GKQLKFSLVNVAGEDIVQGNKKLILAFLWQLMR 495
Cdd:cd21292  104 ASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIR 136
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
394-494 6.64e-08

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


Pssm-ID: 409166  Cd Length: 132  Bit Score: 51.98  E-value: 6.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS-LGIVT-YVNNLFEDVRNGWILLEVLDKVSPgsvnwKRASKPPI-KMPFRKVENCNQVIGIGKQLKFSL 470
Cdd:cd21317   32 QKKTFTKWVNShLARVTcRIGDLYTDLRDGRMLIRLLEVLSG-----EQLPKPTKgRMRIHCLENVDKALQFLKEQKVHL 106
                         90       100
                 ....*....|....*....|....
gi 297737515 471 VNVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21317  107 ENMGSHDIVDGNHRLTLGLIWTII 130
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
161-235 9.93e-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: 9.93e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297737515 161 DGVLLCKLINVavpgtIDERAIN--TKRVLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRPHLLLGLISQII 235
Cdd:cd21227   33 DGVKLIALVEI-----LQGRKLGrvIKKPLNQHQKLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLI 104
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
394-494 1.04e-07

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: 50.47  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS----LGivTYVNNLFEDVRNGWILLEVLDKVSPgsvnwKRASKPP-IKMPFRKVENCNQVIGIGKQLKF 468
Cdd:cd21214    6 QRKTFTAWCNShlrkAG--TQIENIEEDFRDGLKLMLLLEVISG-----ERLPKPErGKMRFHKIANVNKALDFIASKGV 78
                         90       100
                 ....*....|....*....|....*.
gi 297737515 469 SLVNVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21214   79 KLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
146-244 1.41e-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: 50.19  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 146 LPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRPH 225
Cdd:cd21299   16 LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFSLVNVAGNDIVQGNKK 95
                         90
                 ....*....|....*....
gi 297737515 226 LLLGLISQIIKIQLLADLN 244
Cdd:cd21299   96 LILALLWQLMRYHMLQLLK 114
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
256-351 2.73e-07

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: 49.78  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 256 DDGNDVEELMGLAPEKVLLKWMNFHLKKagykKPITNFSSDLKDGEAYAYLLNVLAPEHCSP-ATLDAKDPTHRAKLVLD 334
Cdd:cd21315    4 GEDDGPDDGKGPTPKQRLLGWIQSKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCPDwEDWDPKDAVKNAKEAMD 79
                         90
                 ....*....|....*...
gi 297737515 335 HAER-MDCKRYLSPKDIV 351
Cdd:cd21315   80 LAEDwLDVPQLIKPEEMV 97
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
394-494 3.37e-07

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 49.02  E-value: 3.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWIN----SLGIVtyVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPpiKMPFRKVENCNQVIGIGKQLKFS 469
Cdd:cd21183    5 QANTFTRWCNehlkERGMQ--IHDLATDFSDGLCLIALLENLSTRPLKRSYNRRP--AFQQHYLENVSTALKFIEADHIK 80
                         90       100
                 ....*....|....*....|....*
gi 297737515 470 LVNVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21183   81 LVNIGSGDIVNGNIKLILGLIWTLI 105
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
394-496 5.30e-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: 48.72  E-value: 5.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS----LGIVTYVNNLFEDVRNGWILLEVLDKVSpgsvnwkrASKPPIKMPfRKVENCNQVIGIGKQLKF- 468
Cdd:cd21190    6 QKKTFTNWINShlakLSQPIVINDLFVDIKDGTALLRLLEVLS--------GQKLPIESG-RVLQRAHKLSNIRNALDFl 76
                         90       100       110
                 ....*....|....*....|....*....|...
gi 297737515 469 -----SLVNVAGEDIVQGNKKLILAFLWQLMRY 496
Cdd:cd21190   77 tkrciKLVNINSTDIVDGKPSIVLGLIWTIILY 109
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
411-494 5.41e-07

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


Pssm-ID: 409072  Cd Length: 113  Bit Score: 48.74  E-value: 5.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 411 VNNLFEDVRNGWIL---LEVLDKVSPGSvnwKRASKPPIKMPfRKVENCNQVI----GIGKQLKFSLVNVAGEDIVQGNK 483
Cdd:cd21223   26 VTNLAVDLRDGVRLcrlVELLTGDWSLL---SKLRVPAISRL-QKLHNVEVALkalkEAGVLRGGDGGGITAKDIVDGHR 101
                         90
                 ....*....|.
gi 297737515 484 KLILAFLWQLM 494
Cdd:cd21223  102 EKTLALLWRII 112
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
398-496 6.48e-07

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


Pssm-ID: 409076  Cd Length: 109  Bit Score: 48.44  E-value: 6.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 398 FRLWINS----LGIVtyVNNLFEDVRNGWILLEVLDKVSPGSVnwKRASKPPiKMPFRKVENCNQVIGIGKQLKFSLVNV 473
Cdd:cd21227    9 FTNWVNEqlkpTGMS--VEDLATDLEDGVKLIALVEILQGRKL--GRVIKKP-LNQHQKLENVTLALKAMAEDGIKLVNI 83
                         90       100
                 ....*....|....*....|....
gi 297737515 474 AGEDIVQGNKKLILAFLWQL-MRY 496
Cdd:cd21227   84 GNEDIVNGNLKLILGLIWHLiLRY 107
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
124-235 1.05e-06

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


Pssm-ID: 409090  Cd Length: 113  Bit Score: 47.75  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 124 EKASYVAHINSYLgddpfLKQYLPLdpSTNDLFDLVKDGVLLCKLINV----AVPGtidERAINTKRVlnPWERNENHTL 199
Cdd:cd21241    6 QKKTFTNWINSYL-----AKRKPPM--KVEDLFEDIKDGTKLLALLEVlsgeKLPC---EKGRRLKRV--HFLSNINTAL 73
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 297737515 200 CLNSAKAIgcTVVNIGTQDLIEGRPHLLLGLISQII 235
Cdd:cd21241   74 KFLESKKI--KLVNINPTDIVDGKPSIVLGLIWTII 107
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
146-243 1.27e-06

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


Pssm-ID: 409149  Cd Length: 119  Bit Score: 47.80  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 146 LPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKRVLNPWER-----NENHTLCLnsAKAIGCTVVNIGTQDLI 220
Cdd:cd21300   19 LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPASAEISRfkaveNTNYAVEL--GKQLGFSLVGIQGADIT 96
                         90       100
                 ....*....|....*....|...
gi 297737515 221 EGRPHLLLGLISQIIKIQLLADL 243
Cdd:cd21300   97 DGSRTLTLALVWQLMRFHITKTL 119
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
394-494 1.77e-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: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINSLGIVT---YVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPpikmpFRKVENCNQVIGIGKQLKFSL 470
Cdd:cd21231    7 QKKTFTKWINAQFAKFgkpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTR-----VHALNNVNKALQVLQKNNVDL 81
                         90       100
                 ....*....|....*....|....
gi 297737515 471 VNVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21231   82 VNIGSADIVDGNHKLTLGLIWSII 105
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
394-494 2.24e-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: 46.75  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINSL----GIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPpikmpFRKVENCNQVIGIGKQLKFS 469
Cdd:cd21242    6 QKRTFTNWINSQlakhSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNV-----FQCRSNIETALSFLKNKSIK 80
                         90       100
                 ....*....|....*....|....*
gi 297737515 470 LVNVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21242   81 LINIHVPDIIEGKPSIILGLIWTII 105
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
260-358 3.07e-06

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: 46.60  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 260 DVEELMGLAPEKVLLKWMNFHLKKAgykkPITNFSSDLKDGEAYAYLLNVLAPEHCSP-ATLDAKDPTHRAKLVLDHAER 338
Cdd:cd21314    3 DEEDARKQTPKQRLLGWIQNKVPQL----PITNFNRDWQDGKALGALVDNCAPGLCPDwESWDPNQPVQNAREAMQQADD 78
                         90       100
                 ....*....|....*....|.
gi 297737515 339 -MDCKRYLSPKDIVEgsPNLN 358
Cdd:cd21314   79 wLGVPQVIAPEEIVD--PNVD 97
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
265-366 5.22e-06

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: 45.82  E-value: 5.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 265 MGLAPEKVLLKWMnfHLKKAGYKK-PITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAKLVLDHAERMDCKR 343
Cdd:cd21199    5 YGGSKRNALLKWC--QEKTQGYKGiDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGIPT 82
                         90       100
                 ....*....|....*....|....*.
gi 297737515 344 YLSPKDIVEGS-PNLN--LAFVAQIF 366
Cdd:cd21199   83 TLTIDEMVSMErPDWQsvMSYVTAIY 108
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
151-236 6.13e-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: 45.47  E-value: 6.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 151 STNDLFDLVKDGVLLCKLINVAVPGTIDERAINTK-RVlnpwERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRPHLLLG 229
Cdd:cd21215   23 SITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKmRV----QKLENVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILG 98

                 ....*..
gi 297737515 230 LISQIIK 236
Cdd:cd21215   99 LLWTLIL 105
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
257-358 6.17e-06

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: 45.57  E-value: 6.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 257 DGNDVEELMGLAPEKVLLKWMNFHLKKAgykkPITNFSSDLKDGEAYAYLLNVLAPEHCSP-ATLDAKDPTHRAKLVLDH 335
Cdd:cd21312    1 DEEEDEEAKKQTPKQRLLGWIQNKLPQL----PITNFSRDWQSGRALGALVDSCAPGLCPDwDSWDASKPVTNAREAMQQ 76
                         90       100
                 ....*....|....*....|....
gi 297737515 336 AER-MDCKRYLSPKDIVEgsPNLN 358
Cdd:cd21312   77 ADDwLGIPQVITPEEIVD--PNVD 98
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
394-494 8.70e-06

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


Pssm-ID: 409077  Cd Length: 108  Bit Score: 45.17  E-value: 8.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS-LGIVT-YVNNLFEDVRNGWILLEVLDKVSPgsvnwKRASKPPIKMP-FR--KVENCNQVIGIGKQLKF 468
Cdd:cd21228    5 QQNTFTRWCNEhLKCVNkRIYNLETDLSDGLRLIALLEVLSQ-----KRMYKKYNKRPtFRqmKLENVSVALEFLERESI 79
                         90       100
                 ....*....|....*....|....*.
gi 297737515 469 SLVNVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21228   80 KLVSIDSSAIVDGNLKLILGLIWTLI 105
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
124-235 8.84e-06

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


Pssm-ID: 409039  Cd Length: 113  Bit Score: 45.25  E-value: 8.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 124 EKASYVAHINSYLGddpflKQYLPLdpSTNDLFDLVKDGVLLCKLINVAvpgTIDERAINTKRVLNPWERNEN--HTLCL 201
Cdd:cd21190    6 QKKTFTNWINSHLA-----KLSQPI--VINDLFVDIKDGTALLRLLEVL---SGQKLPIESGRVLQRAHKLSNirNALDF 75
                         90       100       110
                 ....*....|....*....|....*....|....
gi 297737515 202 NSAKAIgcTVVNIGTQDLIEGRPHLLLGLISQII 235
Cdd:cd21190   76 LTKRCI--KLVNINSTDIVDGKPSIVLGLIWTII 107
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
146-236 9.19e-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: 45.30  E-value: 9.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 146 LPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINT--KRVLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGR 223
Cdd:cd21298   18 LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKpfKKLGANMKKIENCNYAVELGKKLKFSLVGIGGKDIYDGN 97
                         90
                 ....*....|...
gi 297737515 224 PHLLLGLISQIIK 236
Cdd:cd21298   98 RTLTLALVWQLMR 110
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
269-356 9.57e-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: 44.68  E-value: 9.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 269 PEKVLLKWMNFHLKKagykKPITNFSSDLKDGEAYAYLLNVLAPEHCSPA-TLDAKDPTHRAKLVLDHAER-MDCKRYLS 346
Cdd:cd21230    2 PKQRLLGWIQNKIPQ----LPITNFTTDWNDGRALGALVDSCAPGLCPDWeTWDPNDALENATEAMQLAEDwLGVPQLIT 77
                         90
                 ....*....|
gi 297737515 347 PKDIVegSPN 356
Cdd:cd21230   78 PEEII--NPN 85
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
122-235 1.08e-05

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: 44.82  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 122 ESEKASYVAHINSYLGDDPflkqylplDPST-NDLFDLVKDGVLLCKLINVAVPGTID-ERAINTKRvlnpWERNENHTL 199
Cdd:cd21242    4 QTQKRTFTNWINSQLAKHS--------PPSVvSDLFTDIQDGHRLLDLLEVLSGQQLPrEKGHNVFQ----CRSNIETAL 71
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 297737515 200 CLNSAKAIgcTVVNIGTQDLIEGRPHLLLGLISQII 235
Cdd:cd21242   72 SFLKNKSI--KLINIHVPDIIEGKPSIILGLIWTII 105
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
394-494 1.20e-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: 45.80  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINS--LGIVTYVNNLFEDVRNGWILLEVLDKVSPgsvnwKRASKPPI-KMPFRKVENCNQVIGIGKQLKFSL 470
Cdd:cd21316   54 QKKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLEVLSG-----ERLPKPTKgRMRIHCLENVDKALQFLKEQRVHL 128
                         90       100
                 ....*....|....*....|....
gi 297737515 471 VNVAGEDIVQGNKKLILAFLWQLM 494
Cdd:cd21316  129 ENMGSHDIVDGNHRLTLGLIWTII 152
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
153-235 1.26e-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: 44.78  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 153 NDLFDLVKDGVLLCKLINVaVPGTIDERAINtKRVLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRPHLLLGLIS 232
Cdd:cd21183   25 HDLATDFSDGLCLIALLEN-LSTRPLKRSYN-RRPAFQQHYLENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLIW 102

                 ...
gi 297737515 233 QII 235
Cdd:cd21183  103 TLI 105
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
413-499 1.59e-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: 45.42  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 413 NLFEDVRNGWILLEVLDKVSPGSVNWKRASKPPIKmPFRKVENCNQVIGIGKQLKFSLVNVAGEDIVQGNKKLILAFLWQ 492
Cdd:cd21323   55 SLFKSLADGILLCKMINLSQPDTIDERAINKKKLT-PFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQ 133

                 ....*..
gi 297737515 493 LMRYNML 499
Cdd:cd21323  134 IIKVGLF 140
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
273-367 1.88e-05

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: 44.23  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 273 LLKWMnfHLKKAGYKK-PITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAKLVLDHAER-MDCKRYLSPKDI 350
Cdd:cd21319   10 LLLWC--QMKTAGYPNvNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERqLGITKLLDPEDV 87
                         90
                 ....*....|....*....
gi 297737515 351 VEGSPNLN--LAFVAQIFH 367
Cdd:cd21319   88 FTENPDEKsiITYVVAFYH 106
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
150-223 2.03e-05

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


Pssm-ID: 409056 [Multi-domain]  Cd Length: 107  Bit Score: 43.84  E-value: 2.03e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297737515 150 PSTNDLFDLVKDGVLLCKLINVAVPGTIdeRAINTKRVlnPWERNENHTLCLNSAKAIGCTVVNI-GTQDLIEGR 223
Cdd:cd21207   23 DDGKDYEDVLKDGVILCKLINILKPGSV--KKINTSKM--AFKLMENIENFLTACKGYGVPKTDLfQTVDLYEKK 93
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
269-367 2.32e-05

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


Pssm-ID: 409075  Cd Length: 103  Bit Score: 43.61  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 269 PEKVLLKWMNFHLKkaGYKKP-ITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAKLVLDHAER-MDCKRYLS 346
Cdd:cd21226    1 SEDGLLAWCRQTTE--GYDGVnITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLE 78
                         90       100
                 ....*....|....*....|..
gi 297737515 347 PKDIVEGSP-NLNLAFVAQIFH 367
Cdd:cd21226   79 AEDVMTGNPdERSIVLYTSLFY 100
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
266-366 2.67e-05

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: 43.87  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 266 GLAPEKVLLKWMnfHLKKAGYKK-PITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAKLVLDHAERMDCKRY 344
Cdd:cd21257    6 GGSKRNALLKWC--QKKTEGYPNiDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGIKPS 83
                         90       100
                 ....*....|....*....|....*
gi 297737515 345 LSPKDIVEGS-PNLN--LAFVAQIF 366
Cdd:cd21257   84 LELSEMMYTDrPDWQsvMQYVAQIY 108
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
276-353 3.09e-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: 43.44  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 276 WMNFHLKKAGYKKPITNFSSDLKDGEAYAYLLNVLAPE-----HCSPATLDAKDPTHRAKLVLDHAERMDCKRyLSPKDI 350
Cdd:cd21213    8 WVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEklpgiDWNPTTDAERKENVEKVLQFMASKRIRMHQ-TSAKDI 86

                 ...
gi 297737515 351 VEG 353
Cdd:cd21213   87 VDG 89
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
275-313 3.23e-05

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


Pssm-ID: 409061  Cd Length: 105  Bit Score: 43.34  E-value: 3.23e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 297737515 275 KWMNFHLKKAGYKKPITNFSSDLKDGEAYAYLLNVLAPE 313
Cdd:cd21212    7 DWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGE 45
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
394-496 3.74e-05

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


Pssm-ID: 409040  Cd Length: 114  Bit Score: 43.34  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWIN----SLGIVTYVNNLFEDVRNGWILLEVLDKVSpgSVNWKRASKPPIKMPFRkVENCNQVIGIGKQLKFS 469
Cdd:cd21191    6 QKRTFTRWINlhleKCNPPLEVKDLFVDIQDGKILMALLEVLS--GQNLLQEYKPSSHRIFR-LNNIAKALKFLEDSNVK 82
                         90       100
                 ....*....|....*....|....*..
gi 297737515 470 LVNVAGEDIVQGNKKLILAFLWQLMRY 496
Cdd:cd21191   83 LVSIDAAEIADGNPSLVLGLIWNIILF 109
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
274-367 4.58e-05

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: 42.67  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 274 LKWMNFHLKKAgykkPITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAKLVLDHAERMDCKRYLSPKDIVeg 353
Cdd:cd21185    7 LRWVRQLLPDV----DVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEMA-- 80
                         90
                 ....*....|....*...
gi 297737515 354 SPNLN----LAFVAQIFH 367
Cdd:cd21185   81 DPEVEhlgiMAYAAQLQK 98
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
271-365 4.87e-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: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 271 KVLLKWMNFHLKKAGykKPITNFSSDLKDGEAYAYLLNVLAPEHCspatldakdPTHRAKL----------VLDHAERMD 340
Cdd:cd21188    6 KTFTKWVNKHLIKAR--RRVVDLFEDLRDGHNLISLLEVLSGESL---------PRERGRMrfhrlqnvqtALDFLKYRK 74
                         90       100
                 ....*....|....*....|....*.
gi 297737515 341 CKRY-LSPKDIVEGSPNLNLAFVAQI 365
Cdd:cd21188   75 IKLVnIRAEDIVDGNPKLTLGLIWTI 100
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
270-366 5.08e-05

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: 42.64  E-value: 5.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 270 EKVLLKWMNFHLKKAGYKKPITNFSS-DLKDGEAYAYLLNVLAPEHCSPA----TLDAKDPTHRAKLVLDHAERMDCKRY 344
Cdd:cd21220    3 DADILAWANSKVREAGKSSPISSFKDpSLSTGLFLLDLLAAIDPGAVDYDlvteGETDEEKEQNAKYAISLARKIGAVIF 82
                         90       100
                 ....*....|....*....|..
gi 297737515 345 LSPKDIVEGSPNLNLAFVAQIF 366
Cdd:cd21220   83 LLWEDIVEVKPKMILTFVASLM 104
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
412-499 5.22e-05

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: 43.89  E-value: 5.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 412 NNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPPIKmPFRKVENCNQVIGIGKQLKFSLVNVAGEDIVQGNKKLILAFLW 491
Cdd:cd21325   54 DDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLT-PFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLW 132

                 ....*...
gi 297737515 492 QLMRYNML 499
Cdd:cd21325  133 QIIKIGLF 140
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
412-499 6.09e-05

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: 43.46  E-value: 6.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 412 NNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPPIKmPFRKVENCNQVIGIGKQLKFSLVNVAGEDIVQGNKKLILAFLW 491
Cdd:cd21324   54 DDLFKAVGDGIVLCKMINFSVPDTIDERTINKKKLT-PFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLW 132

                 ....*...
gi 297737515 492 QLMRYNML 499
Cdd:cd21324  133 QVIKIGLF 140
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
405-495 1.28e-04

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: 42.13  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 405 LGIVTYVNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPPIKMPFRKVENCNQVIGIGKQLKFSLVNVAGEDIVQGNKK 484
Cdd:cd21293   24 LPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLNSAKAIGCSVVNIGTQDLAEGRPH 103
                         90
                 ....*....|.
gi 297737515 485 LILAFLWQLMR 495
Cdd:cd21293  104 LVLGLISQIIK 114
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
266-351 1.75e-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: 41.60  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 266 GLAPEKVLLKWMnfHLKKAGYKK-PITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAKLVLDHAERMDCKRY 344
Cdd:cd21256   12 GGSKRNALLKWC--QKKTEGYQNiDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAESVGIKST 89

                 ....*..
gi 297737515 345 LSPKDIV 351
Cdd:cd21256   90 LDINEMV 96
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
270-351 1.96e-04

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


Pssm-ID: 409110  Cd Length: 107  Bit Score: 41.10  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 270 EKVLLKWMnfHLKKAGYKK-PITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAKLVLDHAERM-DCKRYLSP 347
Cdd:cd21261    3 KQILLEWC--RSKTIGYKNiDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80

                 ....
gi 297737515 348 KDIV 351
Cdd:cd21261   81 EDMM 84
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
271-365 2.37e-04

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


Pssm-ID: 409035  Cd Length: 107  Bit Score: 40.83  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 271 KVLLKWMNFHLKKAGyKKPITNFSSDLKDGEAYAYLLNVL-----APEHCSPATLDAKDPTHRAKLVLDHAERMdckRYL 345
Cdd:cd21186    5 KTFTKWINSQLSKAN-KPPIKDLFEDLRDGTRLLALLEVLtgkklKPEKGRMRVHHLNNVNRALQVLEQNNVKL---VNI 80
                         90       100
                 ....*....|....*....|
gi 297737515 346 SPKDIVEGSPNLNLAFVAQI 365
Cdd:cd21186   81 SSNDIVDGNPKLTLGLVWSI 100
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
394-496 2.84e-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: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 394 EERCFRLWINSlgivtY---------VNNLFEDVRNGWILLEVLDKVSpGSvnwkraskppiKMPFRKVENCNQ---VIG 461
Cdd:cd21241    6 QKKTFTNWINS-----YlakrkppmkVEDLFEDIKDGTKLLALLEVLS-GE-----------KLPCEKGRRLKRvhfLSN 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 297737515 462 IGKQLKF------SLVNVAGEDIVQGNKKLILAFLWQLMRY 496
Cdd:cd21241   69 INTALKFleskkiKLVNINPTDIVDGKPSIVLGLIWTIILY 109
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
147-221 5.71e-04

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


Pssm-ID: 409050  Cd Length: 117  Bit Score: 39.93  E-value: 5.71e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297737515 147 PLDPSTNDLFDLV---KDGVLLCKLINVAVPGTIDERAINTKRVLNPWERNENHTLCLNSAkaigCTVVNIGTQDLIE 221
Cdd:cd21201   21 RATQPNATVFDLAqalRDGVLLCQLLNRLSPGSVDDREINLRPQMSQFLCLKNIRTFLQAC----RTVFGLRSADLFE 94
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
153-208 6.67e-04

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


Pssm-ID: 409057 [Multi-domain]  Cd Length: 119  Bit Score: 40.02  E-value: 6.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 297737515 153 NDLF-DLVKDGVLLCKLINVAVPGTIdeRAINTKRvlNPWERNENHTLCLNSAKAIG 208
Cdd:cd21208   19 SDDFrESLEDGILLCELINAIKPGSI--KKINRLP--TPIAGLDNLNLFLKACEDLG 71
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
152-234 9.32e-04

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: 39.59  E-value: 9.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 152 TNDLfdlvKDGVLLCKLINVAVPGTIDERAIntKRVLNPWERNENHTLCLNSAKAIGCTVVnIGTQDLIEGRPHLLLGLI 231
Cdd:cd21218   37 SSDL----KDGEVYALLLHSLAPELCDKELV--LEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPEDIVSGNPRLNLAFV 109

                 ...
gi 297737515 232 SQI 234
Cdd:cd21218  110 ATL 112
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
124-234 1.06e-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: 39.10  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 124 EKASYVAHINSYLgddpflkQYLPLDPSTNDLFDLVKDGVLLCKLINVAVPGTIDerAINtKRVLNPWERNENHTLCLNS 203
Cdd:cd21212    1 EIEIYTDWANHYL-------EKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVP--GIH-SRPKTRAQKLENIQACLQF 70
                         90       100       110
                 ....*....|....*....|....*....|.
gi 297737515 204 AKAIGCTVVNIGTQDLIEGRPHLLLGLISQI 234
Cdd:cd21212   71 LAALGVDVQGITAEDIVDGNLKAILGLFFSL 101
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
269-358 1.12e-03

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


Pssm-ID: 409078  Cd Length: 105  Bit Score: 38.91  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 269 PEKVLLKWMNFHLKKAGykkpITNFSSDLKDGEAYAYLLnvlapEHCSPAT------LDAKDPTHRAKLVLDHAER-MDC 341
Cdd:cd21229    4 PKKLMLAWLQAVLPELK----ITNFSTDWNDGIALSALL-----DYCKPGLcpnwrkLDPSNSLENCRRAMDLAKReFNI 74
                         90
                 ....*....|....*..
gi 297737515 342 KRYLSPKDIveGSPNLN 358
Cdd:cd21229   75 PMVLSPEDL--SSPHLD 89
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
261-367 1.16e-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: 39.27  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 261 VEELMglAPEKVLLkWMnfHLKKAGYKK-PITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAKLVLDHAER- 338
Cdd:cd21216    6 VEELS--AKEGLLL-WC--QRKTAPYKNvNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKh 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 297737515 339 MDCKRYLSPKDIVEgSPNLN----LAFVAQIFH 367
Cdd:cd21216   81 LDIPKMLDAEDIVN-TPRPDersvMTYVSCYYH 112
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
124-246 2.77e-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: 38.43  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 124 EKASYVAHINSYLgddpflkqyLPLDPSTNDLFDLVKDGVLLCKLINVaVPGTIDERAINTKRvlnpWERNENHTLCLNS 203
Cdd:cd21236   18 QKKTFTKWINQHL---------MKVRKHVNDLYEDLRDGHNLISLLEV-LSGDTLPREKGRMR----FHRLQNVQIALDY 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 297737515 204 AKAIGCTVVNIGTQDLIEGRPHLLLGLISQIIKIQLLADLNLK 246
Cdd:cd21236   84 LKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVT 126
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
153-235 2.83e-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: 37.77  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 153 NDLFDLVKDGVLLCKLINVavpgtIDERAINTKRVLNPWERNENHTLCLNSAKAIGCTVVNIGTQDLIEGRPHLLLGLIS 232
Cdd:cd21188   24 VDLFEDLRDGHNLISLLEV-----LSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIW 98

                 ...
gi 297737515 233 QII 235
Cdd:cd21188   99 TII 101
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
270-365 3.17e-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: 38.43  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 270 EKVLLKWMNFHLKKAgyKKPITNFSSDLKDGEAYAYLLNVLAPEhcSPATLDAKDPTHR---AKLVLDHAERMDCKRY-L 345
Cdd:cd21236   19 KKTFTKWINQHLMKV--RKHVNDLYEDLRDGHNLISLLEVLSGD--TLPREKGRMRFHRlqnVQIALDYLKRRQVKLVnI 94
                         90       100
                 ....*....|....*....|
gi 297737515 346 SPKDIVEGSPNLNLAFVAQI 365
Cdd:cd21236   95 RNDDITDGNPKLTLGLIWTI 114
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
401-496 3.30e-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: 37.56  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 401 WINSL----GIVTYVNNLFEDVRNGWILLEVLDKVSPGSVN--WKRaskppIKMPFRKVENcnqvigIGKQLKF--SL-V 471
Cdd:cd21212    8 WANHYlekgGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPgiHSR-----PKTRAQKLEN------IQACLQFlaALgV 76
                         90       100
                 ....*....|....*....|....*...
gi 297737515 472 NVAG---EDIVQGNKKLILAFLWQLMRY 496
Cdd:cd21212   77 DVQGitaEDIVDGNLKAILGLFFSLSRY 104
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
154-235 4.22e-03

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


Pssm-ID: 409042  Cd Length: 116  Bit Score: 37.66  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 154 DLFDLVKDGVLLCKLINVaVPGTIDERAINTK-RVlnpwERNENHTLCLNSAKAiGCTVVNIGTQDLIEGRPHLLLGLIS 232
Cdd:cd21193   38 DLFTDLSDGKLLLKLLEI-ISGEKLGKPNRGRlRV----QKIENVNKALAFLKT-KVRLENIGAEDIVDGNPRLILGLIW 111

                 ...
gi 297737515 233 QII 235
Cdd:cd21193  112 TII 114
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
519-616 4.41e-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: 37.64  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 519 ILKWANNKVKRTGrTSQMESFKdKNLSNGIFFLDLLSAVEPrvvnwnlvtKGESEEEKKLN--------------ATYII 584
Cdd:cd21328   20 LLRWANFHLENAG-WQKINNFS-SDIKDSRAYFHLLNQIAP---------KGQKEGEPRIDinmsgfnekddlkrAEYML 88
                         90       100       110
                 ....*....|....*....|....*....|..
gi 297737515 585 SVARKLGCSIFLLPEDIMEVNQKMILTLTASI 616
Cdd:cd21328   89 QQADKLGCRQFVTPADVVSGNPKLNLAFVANL 120
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
273-365 4.72e-03

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


Pssm-ID: 409152  Cd Length: 108  Bit Score: 37.40  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 273 LLKWMNFHLKKAGYKKPITNF-SSDLKDGEAYAYLLNVLAPEHC-----SPATLDaKDPTHRAKLVLDHAERMDCKRYLS 346
Cdd:cd21303    9 MVKWANDMVAKGGKNSSIRSFkDPSLSTGHFFLDVLNGLKSGYVdydlvTPGNTE-DEAYLNAKLAISIARKLGALIFLV 87
                         90
                 ....*....|....*....
gi 297737515 347 PKDIVEGSPNLNLAFVAQI 365
Cdd:cd21303   88 PEDIVEVRPRLVLTFIGSL 106
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
411-494 5.34e-03

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


Pssm-ID: 409159  Cd Length: 125  Bit Score: 37.70  E-value: 5.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 411 VNNLFEDVRNGWILLEVLDKVSPGSVNWKRASKPPIKMpfRKVENCNQVIGIGKQLKFSLVNVAGEDIVQGNKKLILAFL 490
Cdd:cd21310   36 LNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQ--MKLENVSVALEFLDREHIKLVSIDSKAIVDGNLKLILGLI 113

                 ....
gi 297737515 491 WQLM 494
Cdd:cd21310  114 WTLI 117
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
395-436 5.83e-03

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


Pssm-ID: 409131 [Multi-domain]  Cd Length: 108  Bit Score: 37.16  E-value: 5.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 297737515 395 ERCFRLWINSLGIVTYVNNLFEDVRNGWILLEVLDKVSPGSV 436
Cdd:cd21282    5 EEELRVWIEGVTGRRIGDNFMDGLKDGVILCELINKLQPGSV 46
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
271-314 6.27e-03

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: 36.98  E-value: 6.27e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 297737515 271 KVLLKWMNFHLKKAGYKkpITNFSSDLKDGEAYAYLLNVLAPEH 314
Cdd:cd21214    8 KTFTAWCNSHLRKAGTQ--IENIEEDFRDGLKLMLLLEVISGER 49
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
269-351 7.29e-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: 36.63  E-value: 7.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 269 PEKVLLKWMNFHLKkaGYKK-PITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAKLVLDHAERMDCKRYLSP 347
Cdd:cd21198    2 SGQDLLEWCQEVTK--GYRGvKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDP 79

                 ....
gi 297737515 348 KDIV 351
Cdd:cd21198   80 ADMV 83
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
154-223 9.27e-03

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


Pssm-ID: 409059 [Multi-domain]  Cd Length: 101  Bit Score: 36.19  E-value: 9.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297737515 154 DLFDLVKDGVLLCKLINVAVPGTIdeRAINTKRVlnPWERNENHTLCLNSAKAIGCTVV-NIGTQDLIEGR 223
Cdd:cd21210   21 DLLDALKDGVVLCKLANRILPADI--RKYKESKM--PFVQMENISAFLNAARKLGVPENdLFQTVDLFERK 87
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
270-362 9.28e-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: 36.22  E-value: 9.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297737515 270 EKVLLKWMNFHLKKAGYkkPITNFSSDLKDGEAYAYLLNVLAPEHCSPATLDAKDPTHRAK---LVLDHAERMDCKRY-L 345
Cdd:cd21215    6 KKTFTKWLNTKLSSRGL--SITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLEnvnKALEFIKSRGVKLTnI 83
                         90
                 ....*....|....*..
gi 297737515 346 SPKDIVEGSPNLNLAFV 362
Cdd:cd21215   84 GAEDIVDGNLKLILGLL 100
 
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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