NCBI Conserved Domain Search

third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

390-503

1.12e-81

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

Pssm-ID: 409148 Cd Length: 114 Bit Score: 253.96 E-value: 1.12e-81

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 390 ETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNEVIKIGKELRFS 469
Cdd:cd21299   1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFS 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 15027847 470 LVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLLR 503
Cdd:cd21299  81 LVNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114

CH_AtFIM_like_rpt1

first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

123-238

1.09e-79

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

Pssm-ID: 409142 Cd Length: 116 Bit Score: 248.98 E-value: 1.09e-79

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 123 SEKASYVSHVNNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLN 202
Cdd:cd21293   1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15027847 203 SAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQ 238
Cdd:cd21293  81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116

CH_AtFIM_like_rpt4

fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

513-621

5.72e-72

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: 228.21 E-value: 5.72e-72

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 513 EITDADILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGC 592
Cdd:cd21302   1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80

                        90       100
                ....*....|....*....|....*....
gi 15027847 593 SIFLLPEDIIEVNQKMMLILAASIMYWSL 621
Cdd:cd21302  81 SIFLLPEDIVEVNQKMILILTASIMYWSL 109

CH_AtFIM_like_rpt2

cd21296

second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

259-367

1.75e-68

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

Pssm-ID: 409145 Cd Length: 109 Bit Score: 219.31 E-value: 1.75e-68

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 259 QDAEELMGLAPEKVLLKWMNFHLKKAGYEKQVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEK 338
Cdd:cd21296   1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKTVTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEK 80

                        90       100
                ....*....|....*....|....*....
gi 15027847 339 LDCKRYLSPKDIVDGSANLNLAFVAQIFQ 367
Cdd:cd21296  81 MNCKRYLTAKDIVEGSANLNLAFVAQIFH 109

Name

Accession

Description

Interval

E-value

CH_AtFIM_like_rpt3

third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

390-503

1.12e-81

Pssm-ID: 409148 Cd Length: 114 Bit Score: 253.96 E-value: 1.12e-81

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 390 ETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNEVIKIGKELRFS 469
Cdd:cd21299   1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFS 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 15027847 470 LVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLLR 503
Cdd:cd21299  81 LVNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114

CH_AtFIM_like_rpt1

first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

123-238

1.09e-79

Pssm-ID: 409142 Cd Length: 116 Bit Score: 248.98 E-value: 1.09e-79

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 123 SEKASYVSHVNNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLN 202
Cdd:cd21293   1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15027847 203 SAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQ 238
Cdd:cd21293  81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116

CH_AtFIM_like_rpt4

fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

513-621

5.72e-72

Pssm-ID: 409151 Cd Length: 109 Bit Score: 228.21 E-value: 5.72e-72

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 513 EITDADILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGC 592
Cdd:cd21302   1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80

                        90       100
                ....*....|....*....|....*....
gi 15027847 593 SIFLLPEDIIEVNQKMMLILAASIMYWSL 621
Cdd:cd21302  81 SIFLLPEDIVEVNQKMILILTASIMYWSL 109

SAC6

COG5069

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

110-611

4.85e-71

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

Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 242.54 E-value: 4.85e-71

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 110 KTSTTTVHHAINESEKasYVSHVNNYLRDDPFLKSYLPiDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKT-- 187
Cdd:COG5069 108 SLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKnk 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 188 -LNPWERNENLTLGLNSAKAIG-CTVVNIGTQDiaeGRPYLVLgLISQIIKIQMLA--DLNFKKTPSLFQLVDDTQDaee 263
Cdd:COG5069 185 aLNNFQAFENANKVIGIARLIGvEDIVNVSIPD---ERSIMTY-VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ--- 257

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 264 lMGLAPEKVLLKWMNFHLKKAGYEKqVTNFSSDLKDGEAYAYLLNALAPEHSTHVaLETKDPTERAKKVLEQAEKLDCKR 343
Cdd:COG5069 258 -LRLPYEIILLRLLNLIHLKQANWK-VVNFSKDVSDGENYTDLLNQLNALCSRAP-LETTDLHSLAGQILQNAEKYDCRK 334

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 344 YLSPKdivdGSANLNLAFVAQIFQHRNGLTVDDSkTSFAEMMTDDVETSREERCFRLWINSLGTATYVNNVFEDLRNGWV 423
Cdd:COG5069 335 YLPPA----GNPKLDLAFVAHLFNTHPGQEPLEE-EEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLI 409

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 424 LLEVLDKV-SPGSVNWKHANKPPIK----MPFKKVENCNEVIKIGKELRFSLVNVAGNDIVQGNkKLLLAFLWQLMRYTM 498
Cdd:COG5069 410 LLQALSKKlMPMTVTHKLVKKQPASgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNT 488

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 499 LQLLRNLRshSQGKEITDADILNWANRKVKRGGRTSQADSFRDKNLS-SGMFFLELLSAVEPRVVNWSLVTNGETEEDKK 577
Cdd:COG5069 489 ALFNHVLK--KDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSvSGVFYLDVLKGIHSELVDYDLVTRGFTEFDDI 566

                       490       500       510
                ....*....|....*....|....*....|....*..
gi 15027847 578 LNA-TYIIS--VARKLGCSIFLLPEDIIEVNQKMMLI 611
Cdd:COG5069 567 ADArSLAISskILRSLGAIIKFLPEDINGVRPRLDVL 603

CH_AtFIM_like_rpt2

cd21296

second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

259-367

1.75e-68

Pssm-ID: 409145 Cd Length: 109 Bit Score: 219.31 E-value: 1.75e-68

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 259 QDAEELMGLAPEKVLLKWMNFHLKKAGYEKQVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEK 338
Cdd:cd21296   1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKTVTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEK 80

                        90       100
                ....*....|....*....|....*....
gi 15027847 339 LDCKRYLSPKDIVDGSANLNLAFVAQIFQ 367
Cdd:cd21296  81 MNCKRYLTAKDIVEGSANLNLAFVAQIFH 109

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...

267-371

3.82e-23

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: 94.66 E-value: 3.82e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847   267 LAPEKVLLKWMNFHLKKAGYEKQVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETK--DPTERAKKVLEQAE-KLDCKR 343
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEkKLGVPK 80

                          90       100
                  ....*....|....*....|....*....
gi 15027847   344 YLS-PKDIVDGSANLNLAFVAQIFQHRNG 371
Cdd:pfam00307  81 VLIePEDLVEGDNKSVLTYLASLFRRFQA 109

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...

398-496

3.53e-20

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

Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.83 E-value: 3.53e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847    398 FRLWINSLG---TATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpiKMPFKKVENCNEVIKIGKELRFSLVNVA 474
Cdd:smart00033   3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 15027847    475 GNDIVQGnKKLLLAFLWQLMRY 496
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLISL 101

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...

394-496

2.16e-17

Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 78.10 E-value: 2.16e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847   394 EERCFRLWINSL----GTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpikmPFKKVENCNEVIKIG-KELRF 468
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLALDVAeKKLGV 78

                          90       100
                  ....*....|....*....|....*...
gi 15027847   469 SLVNVAGNDIVQGNKKLLLAFLWQLMRY 496
Cdd:pfam00307  79 PKVLIEPEDLVEGDNKSVLTYLASLFRR 106

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...

148-237

5.77e-17

Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 76.59 E-value: 5.77e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847    148 IDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKtlNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPyLV 227
Cdd:smart00033  15 DKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL--SRFKKIENINLALSFAEKLGGKVVLFEPEDLVEGPK-LI 91

                           90
                   ....*....|
gi 15027847    228 LGLISQIIKI 237
Cdd:smart00033  92 LGVIWTLISL 101

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...

142-236

9.94e-16

Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 73.47 E-value: 9.94e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847   142 LKSYLPIDPATNaFFDLVKDGVLLCKLINVAVPGTIDERAINTKktlnPWERNENLTLGLNSA-KAIGCTVVNIGTQDIA 220
Cdd:pfam00307  15 LAEYGPGVRVTN-FTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLALDVAeKKLGVPKVLIEPEDLV 89

                          90
                  ....*....|....*.
gi 15027847   221 EGRPYLVLGLISQIIK 236
Cdd:pfam00307  90 EGDNKSVLTYLASLFR 105

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...

271-368

1.86e-15

Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 72.35 E-value: 1.86e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847    271 KVLLKWMNFHLKKAGYEKqVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETK----DPTERAKKVLEQAEKLDCKR-YL 345
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVvLF 79

                           90       100
                   ....*....|....*....|...
gi 15027847    346 SPKDIVDGSaNLNLAFVAQIFQH 368
Cdd:smart00033  80 EPEDLVEGP-KLILGVIWTLISL 101

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...

513-617

3.95e-15

Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 71.55 E-value: 3.95e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847   513 EITDADILNWANRKVKRGGRTSQADSFRdKNLSSGMFFLELLSAVEPRVVNWSLVTNgeTEEDKKLNATYIISVAR-KLG 591
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKLNK--SEFDKLENINLALDVAEkKLG 77

                          90       100
                  ....*....|....*....|....*..
gi 15027847   592 CSIFLL-PEDIIEVNQKMMLILAASIM 617
Cdd:pfam00307  78 VPKVLIePEDLVEGDNKSVLTYLASLF 104

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...

518-619

2.09e-12

Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 63.87 E-value: 2.09e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847    518 DILNWANRKVKrgGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGCSIFLL 597
Cdd:smart00033   2 TLLRWVNSLLA--EYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79

                           90       100
                   ....*....|....*....|...
gi 15027847    598 -PEDIIEVNqKMMLILAASIMYW 619
Cdd:smart00033  80 ePEDLVEGP-KLILGVIWTLISL 101

Name

Accession

Description

Interval

E-value

CH_AtFIM_like_rpt3

third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

390-503

1.12e-81

Pssm-ID: 409148 Cd Length: 114 Bit Score: 253.96 E-value: 1.12e-81

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 390 ETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNEVIKIGKELRFS 469
Cdd:cd21299   1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFS 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 15027847 470 LVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLLR 503
Cdd:cd21299  81 LVNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114

CH_AtFIM_like_rpt1

first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

123-238

1.09e-79

Pssm-ID: 409142 Cd Length: 116 Bit Score: 248.98 E-value: 1.09e-79

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 123 SEKASYVSHVNNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLN 202
Cdd:cd21293   1 SEKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWERNENHTLCLN 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15027847 203 SAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQ 238
Cdd:cd21293  81 SAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKIQ 116

CH_AtFIM_like_rpt4

fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

513-621

5.72e-72

Pssm-ID: 409151 Cd Length: 109 Bit Score: 228.21 E-value: 5.72e-72

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 513 EITDADILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGC 592
Cdd:cd21302   1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80

                        90       100
                ....*....|....*....|....*....
gi 15027847 593 SIFLLPEDIIEVNQKMMLILAASIMYWSL 621
Cdd:cd21302  81 SIFLLPEDIVEVNQKMILILTASIMYWSL 109

SAC6

COG5069

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

110-611

4.85e-71

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

Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 242.54 E-value: 4.85e-71

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 110 KTSTTTVHHAINESEKasYVSHVNNYLRDDPFLKSYLPiDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKT-- 187
Cdd:COG5069 108 SLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKnk 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 188 -LNPWERNENLTLGLNSAKAIG-CTVVNIGTQDiaeGRPYLVLgLISQIIKIQMLA--DLNFKKTPSLFQLVDDTQDaee 263
Cdd:COG5069 185 aLNNFQAFENANKVIGIARLIGvEDIVNVSIPD---ERSIMTY-VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ--- 257

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 264 lMGLAPEKVLLKWMNFHLKKAGYEKqVTNFSSDLKDGEAYAYLLNALAPEHSTHVaLETKDPTERAKKVLEQAEKLDCKR 343
Cdd:COG5069 258 -LRLPYEIILLRLLNLIHLKQANWK-VVNFSKDVSDGENYTDLLNQLNALCSRAP-LETTDLHSLAGQILQNAEKYDCRK 334

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 344 YLSPKdivdGSANLNLAFVAQIFQHRNGLTVDDSkTSFAEMMTDDVETSREERCFRLWINSLGTATYVNNVFEDLRNGWV 423
Cdd:COG5069 335 YLPPA----GNPKLDLAFVAHLFNTHPGQEPLEE-EEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLI 409

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 424 LLEVLDKV-SPGSVNWKHANKPPIK----MPFKKVENCNEVIKIGKELRFSLVNVAGNDIVQGNkKLLLAFLWQLMRYTM 498
Cdd:COG5069 410 LLQALSKKlMPMTVTHKLVKKQPASgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNT 488

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 499 LQLLRNLRshSQGKEITDADILNWANRKVKRGGRTSQADSFRDKNLS-SGMFFLELLSAVEPRVVNWSLVTNGETEEDKK 577
Cdd:COG5069 489 ALFNHVLK--KDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSvSGVFYLDVLKGIHSELVDYDLVTRGFTEFDDI 566

                       490       500       510
                ....*....|....*....|....*....|....*..
gi 15027847 578 LNA-TYIIS--VARKLGCSIFLLPEDIIEVNQKMMLI 611
Cdd:COG5069 567 ADArSLAISskILRSLGAIIKFLPEDINGVRPRLDVL 603

CH_AtFIM_like_rpt2

cd21296

second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

259-367

1.75e-68

Pssm-ID: 409145 Cd Length: 109 Bit Score: 219.31 E-value: 1.75e-68

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 259 QDAEELMGLAPEKVLLKWMNFHLKKAGYEKQVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEK 338
Cdd:cd21296   1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKTVTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEK 80

                        90       100
                ....*....|....*....|....*....
gi 15027847 339 LDCKRYLSPKDIVDGSANLNLAFVAQIFQ 367
Cdd:cd21296  81 MNCKRYLTAKDIVEGSANLNLAFVAQIFH 109

CH_PLS_FIM_rpt3

cd21219

third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...

390-502

1.41e-60

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

Pssm-ID: 409068 Cd Length: 113 Bit Score: 198.27 E-value: 1.41e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 390 ETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNEVIKIGKELRFS 469
Cdd:cd21219   1 EGSREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKPLNKFKKVENCNYAVDLAKKLGFS 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 15027847 470 LVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLL 502
Cdd:cd21219  81 LVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113

CH_PLS_rpt1

cd21292

first calponin homology (CH) domain found in the plastin family; The plastin family includes ...

95-244

1.76e-58

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

Pssm-ID: 409141 Cd Length: 145 Bit Score: 194.04 E-value: 1.76e-58

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847  95 GVEKSGGSKGASSflkTSTTtvhHAINESEKASYVSHVNNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVP 174
Cdd:cd21292   2 GIDAKGGTSEASS---EGTT---HSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVP 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 175 GTIDERAINTKKtLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQMLADLN 244
Cdd:cd21292  76 DTIDERAINKKK-LTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIE 144

CH_PLS_FIM_rpt1

cd21217

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...

123-236

5.09e-55

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

Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 183.54 E-value: 5.09e-55

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 123 SEKASYVSHVNNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLN 202
Cdd:cd21217   1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKNIFEATENLNLALN 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 15027847 203 SAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIK 236
Cdd:cd21217  81 AAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114

CH_PLS_FIM_rpt4

cd21220

fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...

514-618

3.61e-50

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: 170.14 E-value: 3.61e-50

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 514 ITDADILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGCS 593
Cdd:cd21220   1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLVTEGETDEEKEQNAKYAISLARKIGAV 80

                        90       100
                ....*....|....*....|....*
gi 15027847 594 IFLLPEDIIEVNQKMMLILAASIMY 618
Cdd:cd21220  81 IFLLWEDIVEVKPKMILTFVASLMA 105

CH_PLS1_rpt1

cd21323

first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...

104-243

1.00e-47

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: 164.83 E-value: 1.00e-47

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 104 GASSFLKTSTTtvHHAINESEKASYVSHVNNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAIN 183
Cdd:cd21323   7 GGTSAISSEGT--QHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDERAIN 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 184 TKKtLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQMLADL 243
Cdd:cd21323  85 KKK-LTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADI 143

CH_PLS_rpt3

cd21298

third calponin homology (CH) domain found in the plastin family; The plastin family includes ...

390-502

2.51e-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: 157.40 E-value: 2.51e-45

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 390 ETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMP--FKKVENCNEVIKIGKELR 467
Cdd:cd21298   3 EETREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGanMKKIENCNYAVELGKKLK 82

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15027847 468 FSLVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLL 502
Cdd:cd21298  83 FSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLSIL 117

CH_FIMB_rpt3

cd21300

third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...

388-502

4.55e-43

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

Pssm-ID: 409149 Cd Length: 119 Bit Score: 151.04 E-value: 4.55e-43

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 388 DVETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPP---IKMPFKKVENCNEVIKIGK 464
Cdd:cd21300   2 DAEGEREARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaEISRFKAVENTNYAVELGK 81

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15027847 465 ELRFSLVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLL 502
Cdd:cd21300  82 QLGFSLVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119

CH_PLS_rpt2

cd21295

second calponin homology (CH) domain found in the family of plastin; The plastin family ...

257-366

1.70e-41

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

Pssm-ID: 409144 Cd Length: 113 Bit Score: 146.65 E-value: 1.70e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 257 DTQDAEELMGLAPEKVLLKWMNFHLKKAGYEKQVTNFSSDLKDGEAYAYLLNALAPEHST--HVALETKDPTERAKKVLE 334
Cdd:cd21295   1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRRIKNFSGDIKDSEAYTHLLKQIAPKDAGvdTSALRESDLLQRAELMLQ 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 15027847 335 QAEKLDCKRYLSPKDIVDGSANLNLAFVAQIF 366
Cdd:cd21295  81 NADKIGCRKFVTPKDVVTGNPKLNLAFVANLF 112

CH_PLS_FIM_rpt2

cd21218

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...

259-367

2.87e-41

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

Pssm-ID: 409067 Cd Length: 114 Bit Score: 145.90 E-value: 2.87e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 259 QDAEELMGLAPEKVLLKWMNFHLKKAGYEK-QVTNFSSDLKDGEAYAYLLNALAPEHSTHV----ALETKDPTERAKKVL 333
Cdd:cd21218   1 ETLESLLYLPPEEILLRWVNYHLKKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELCDKElvleVLSEEDLEKRAEKVL 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 15027847 334 EQAEKLDCKRYLSPKDIVDGSANLNLAFVAQIFQ 367
Cdd:cd21218  81 QAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114

CH_FIMB_rpt1

cd21294

first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...

118-236

9.20e-41

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

Pssm-ID: 409143 Cd Length: 125 Bit Score: 144.90 E-value: 9.20e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 118 HAINESEKASYVSHVNNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTK----KTLNPWER 193
Cdd:cd21294   1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPprknKPLNNFQM 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15027847 194 NENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIK 236
Cdd:cd21294  81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIR 123

CH_PLS2_rpt1

cd21324

first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...

110-243

1.22e-39

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: 142.46 E-value: 1.22e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 110 KTSTTTVHHAINESEKASYVSHVNNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKtLN 189
Cdd:cd21324  11 EQSSAGTQHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKK-LT 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15027847 190 PWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQMLADL 243
Cdd:cd21324  90 PFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADI 143

CH_FIMB_rpt4

cd21303

fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...

511-617

3.44e-39

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

Pssm-ID: 409152 Cd Length: 108 Bit Score: 139.87 E-value: 3.44e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 511 GKEITDADILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKL 590
Cdd:cd21303   1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLVTPGNTEDEAYLNAKLAISIARKL 80

                        90       100
                ....*....|....*....|....*..
gi 15027847 591 GCSIFLLPEDIIEVNQKMMLILAASIM 617
Cdd:cd21303  81 GALIFLVPEDIVEVRPRLVLTFIGSLM 107

CH_PLS3_rpt1

cd21325

first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...

104-247

5.15e-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: 140.96 E-value: 5.15e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 104 GASSFLKTSTTtvHHAINESEKASYVSHVNNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAIN 183
Cdd:cd21325   7 GGTSELSSEGT--QHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAIN 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15027847 184 tKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQMLADLNFKK 247
Cdd:cd21325  85 -KKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSR 147

CH_FIMB_rpt2

cd21297

second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...

262-366

5.08e-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: 133.84 E-value: 5.08e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 262 EELMGLAPEKVLLKWMNFHLKKAGYEKQVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDC 341
Cdd:cd21297   4 EQFLRLPPEQILLRWFNYHLKAANWPRRVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDLLQRAEQVLQNAEKLDC 83

                        90       100
                ....*....|....*....|....*
gi 15027847 342 KRYLSPKDIVDGSANLNLAFVAQIF 366
Cdd:cd21297  84 RKFLTPTSLVAGNPKLNLAFVANLF 108

CH_PLS_rpt4

cd21301

fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...

514-617

3.38e-36

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

Pssm-ID: 409150 Cd Length: 107 Bit Score: 131.63 E-value: 3.38e-36

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 514 ITDADILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGCS 593
Cdd:cd21301   1 ISDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLVLEGNSEEDKLSNAKYAISMARKIGAR 80

                        90       100
                ....*....|....*....|....
gi 15027847 594 IFLLPEDIIEVNQKMMLILAASIM 617
Cdd:cd21301  81 VYALPEDIVEVKPKMVMTVFACLM 104

CH_PLS3_rpt2

cd21328

second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...

254-366

2.09e-30

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

Pssm-ID: 409177 [Multi-domain] Cd Length: 122 Bit Score: 115.83 E-value: 2.09e-30

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 254 LVDDTQDAEELMGLAPEKVLLKWMNFHLKKAGYEKqVTNFSSDLKDGEAYAYLLNALAPEHSTH---------VALETKD 324
Cdd:cd21328   1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQK-INNFSSDIKDSRAYFHLLNQIAPKGQKEgepridinmSGFNEKD 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15027847 325 PTERAKKVLEQAEKLDCKRYLSPKDIVDGSANLNLAFVAQIF 366
Cdd:cd21328  80 DLKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLF 121

CH_PLS1_rpt3

cd21329

third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...

392-502

9.16e-30

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

Pssm-ID: 409178 Cd Length: 118 Bit Score: 113.93 E-value: 9.16e-30

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 392 SREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPgSVNWKHANKPPIKM---PFKKVENCNEVIKIGK-ELR 467
Cdd:cd21329   5 SSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRV-PVDWGHVNKPPYPAlggNMKKIENCNYAVELGKnKAK 83

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15027847 468 FSLVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLL 502
Cdd:cd21329  84 FSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118

CH_PLS1_rpt2

cd21326

second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...

259-366

3.93e-29

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

Pssm-ID: 409175 Cd Length: 121 Bit Score: 112.28 E-value: 3.93e-29

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 259 QDAEELMGLAPEKVLLKWMNFHLKKAGYEKqVTNFSSDLKDGEAYAYLLNALAPEHSTHV--------ALETKDPTERAK 330
Cdd:cd21326   3 EELEELMKLSPEELLLRWVNYHLTNAGWQN-ISNFSQDIKDSRAYFHLLNQIAPKGDVFDenieidfsGFNEKNDLKRAE 81

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15027847 331 KVLEQAEKLDCKRYLSPKDIVDGSANLNLAFVAQIF 366
Cdd:cd21326  82 YMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLF 117

CH_PLS2_rpt2

cd21327

second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...

254-366

7.24e-29

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

Pssm-ID: 409176 Cd Length: 125 Bit Score: 111.59 E-value: 7.24e-29

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 254 LVDDTQDAEELMGLAPEKVLLKWMNFHLKKAGYEKqVTNFSSDLKDGEAYAYLLNALAPEHSTH---------VALETKD 324
Cdd:cd21327   1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNK-INNFSSDIKDSKAYYHLLNQVAPKGDEEgipaividmSGLREKD 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15027847 325 PTERAKKVLEQAEKLDCKRYLSPKDIVDGSANLNLAFVAQIF 366
Cdd:cd21327  80 DLKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLF 121

CH_PLS3_rpt3

cd21331

third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...

392-502

8.35e-27

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

Pssm-ID: 409180 Cd Length: 134 Bit Score: 105.85 E-value: 8.35e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 392 SREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPgSVNWKHANKPP---IKMPFKKVENCNEVIKIGKE-LR 467
Cdd:cd21331  21 TREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKV-PVDWNKVNKPPypkLGANMKKLENCNYAVELGKHpAK 99

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15027847 468 FSLVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLL 502
Cdd:cd21331 100 FSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134

CH_PLS2_rpt3

cd21330

third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...

392-502

9.02e-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: 9.02e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 392 SREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPgSVNWKHANKPP---IKMPFKKVENCNEVIKIGK-ELR 467
Cdd:cd21330  12 TREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKV-PVDWNRVNKPPypkLGENMKKLENCNYAVELGKnKAK 90

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15027847 468 FSLVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLL 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 ...

514-617

1.36e-24

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

Pssm-ID: 409183 Cd Length: 112 Bit Score: 98.81 E-value: 1.36e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 514 ITDADILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGE-TEEDKKLNATYIISVARKLGC 592
Cdd:cd21334   1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNlTDDDKLDNAKYAVSMARKIGA 80

                        90       100
                ....*....|....*....|....*
gi 15027847 593 SIFLLPEDIIEVNQKMMLILAASIM 617
Cdd:cd21334  81 RVYALPEDLVEVKPKMVMTVFACLM 105

CH_PLS2_rpt4

cd21333

fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...

509-617

1.39e-24

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

Pssm-ID: 409182 Cd Length: 115 Bit Score: 98.91 E-value: 1.39e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 509 SQGKEITDADILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKL-NATYIISVA 587
Cdd:cd21333   1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLnNAKYAISMA 80

                        90       100       110
                ....*....|....*....|....*....|
gi 15027847 588 RKLGCSIFLLPEDIIEVNQKMMLILAASIM 617
Cdd:cd21333  81 RKIGARVYALPEDLVEVKPKMVMTVFACLM 110

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...

267-371

3.82e-23

Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 94.66 E-value: 3.82e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847   267 LAPEKVLLKWMNFHLKKAGYEKQVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETK--DPTERAKKVLEQAE-KLDCKR 343
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEkKLGVPK 80

                          90       100
                  ....*....|....*....|....*....
gi 15027847   344 YLS-PKDIVDGSANLNLAFVAQIFQHRNG 371
Cdd:pfam00307  81 VLIePEDLVEGDNKSVLTYLASLFRRFQA 109

CH_PLS1_rpt4

cd21332

fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...

510-617

1.15e-20

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

Pssm-ID: 409181 Cd Length: 115 Bit Score: 87.70 E-value: 1.15e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 510 QGKEITDADILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGE-TEEDKKLNATYIISVAR 588
Cdd:cd21332   4 EGEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDlSDADKLNNAKYAISVAR 83

                        90       100
                ....*....|....*....|....*....
gi 15027847 589 KLGCSIFLLPEDIIEVNQKMMLILAASIM 617
Cdd:cd21332  84 KIGARVYALPEDLVEVKPKMVMTVFACLM 112

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...

398-496

3.53e-20

Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.83 E-value: 3.53e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847    398 FRLWINSLG---TATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpiKMPFKKVENCNEVIKIGKELRFSLVNVA 474
Cdd:smart00033   3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 15027847    475 GNDIVQGnKKLLLAFLWQLMRY 496
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLISL 101

CH_PLS_FIM_rpt1

cd21217

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...

394-495

1.17e-17

Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 79.15 E-value: 1.17e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS-----------LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNEVIKI 462
Cdd:cd21217   2 EKEAFVEHINSlladdpdlkhlLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKNIFEATENLNLALNA 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 15027847 463 GKELRFSLVNVAGNDIVQGNKKLLLAFLWQLMR 495
Cdd:cd21217  82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...

394-496

2.16e-17

Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 78.10 E-value: 2.16e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847   394 EERCFRLWINSL----GTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpikmPFKKVENCNEVIKIG-KELRF 468
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLALDVAeKKLGV 78

                          90       100
                  ....*....|....*....|....*...
gi 15027847   469 SLVNVAGNDIVQGNKKLLLAFLWQLMRY 496
Cdd:pfam00307  79 PKVLIEPEDLVEGDNKSVLTYLASLFRR 106

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...

148-237

5.77e-17

Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 76.59 E-value: 5.77e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847    148 IDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKtlNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPyLV 227
Cdd:smart00033  15 DKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL--SRFKKIENINLALSFAEKLGGKVVLFEPEDLVEGPK-LI 91

                           90
                   ....*....|
gi 15027847    228 LGLISQIIKI 237
Cdd:smart00033  92 LGVIWTLISL 101

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...

142-236

9.94e-16

Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 73.47 E-value: 9.94e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847   142 LKSYLPIDPATNaFFDLVKDGVLLCKLINVAVPGTIDERAINTKktlnPWERNENLTLGLNSA-KAIGCTVVNIGTQDIA 220
Cdd:pfam00307  15 LAEYGPGVRVTN-FTTDLRDGLALCALLNKLAPGLVDKKKLNKS----EFDKLENINLALDVAeKKLGVPKVLIEPEDLV 89

                          90
                  ....*....|....*.
gi 15027847   221 EGRPYLVLGLISQIIK 236
Cdd:pfam00307  90 EGDNKSVLTYLASLFR 105

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...

271-368

1.86e-15

Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 72.35 E-value: 1.86e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847    271 KVLLKWMNFHLKKAGYEKqVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETK----DPTERAKKVLEQAEKLDCKR-YL 345
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVvLF 79

                           90       100
                   ....*....|....*....|...
gi 15027847    346 SPKDIVDGSaNLNLAFVAQIFQH 368
Cdd:smart00033  80 EPEDLVEGP-KLILGVIWTLISL 101

CH_PLS_FIM_rpt3

cd21219

third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...

146-240

3.02e-15

Pssm-ID: 409068 Cd Length: 113 Bit Score: 72.31 E-value: 3.02e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 146 LPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPY 225
Cdd:cd21219  16 LGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKPLNKFKKVENCNYAVDLAKKLGFSLVGIGGKDIADGNRK 95

                        90
                ....*....|....*
gi 15027847 226 LVLGLISQIIKIQML 240
Cdd:cd21219  96 LTLALVWQLMRYHVL 110

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...

513-617

3.95e-15

Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 71.55 E-value: 3.95e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847   513 EITDADILNWANRKVKRGGRTSQADSFRdKNLSSGMFFLELLSAVEPRVVNWSLVTNgeTEEDKKLNATYIISVAR-KLG 591
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKLNK--SEFDKLENINLALDVAEkKLG 77

                          90       100
                  ....*....|....*....|....*..
gi 15027847   592 CSIFLL-PEDIIEVNQKMMLILAASIM 617
Cdd:pfam00307  78 VPKVLIePEDLVEGDNKSVLTYLASLF 104

CH_SF

cd00014

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...

142-236

1.47e-13

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

Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 66.98 E-value: 1.47e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 142 LKSYLPIDPatNAFFDLVKDGVLLCKLINVAVPGTIDERAintKKTLNPWERNENLTLGLNSAKAIG-CTVVNIGTQDIA 220
Cdd:cd00014  12 LGEELPVSI--TDLFESLRDGVLLCKLINKLSPGSIPKIN---KKPKSPFKKRENINLFLNACKKLGlPELDLFEPEDLY 86

                        90
                ....*....|....*..
gi 15027847 221 EGR-PYLVLGLISQIIK 236
Cdd:cd00014  87 EKGnLKKVLGTLWALAL 103

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...

518-619

2.09e-12

Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 63.87 E-value: 2.09e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847    518 DILNWANRKVKrgGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGCSIFLL 597
Cdd:smart00033   2 TLLRWVNSLLA--EYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79

                           90       100
                   ....*....|....*....|...
gi 15027847    598 -PEDIIEVNqKMMLILAASIMYW 619
Cdd:smart00033  80 ePEDLVEGP-KLILGVIWTLISL 101

CH_SF

cd00014

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...

395-495

1.19e-11

Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 61.59 E-value: 1.19e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 395 ERCFRLWINSLgTATY----VNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKppiKMPFKKVENCNEVIKIGKELRF-S 469
Cdd:cd00014   1 EEELLKWINEV-LGEElpvsITDLFESLRDGVLLCKLINKLSPGSIPKINKKP---KSPFKKRENINLFLNACKKLGLpE 76

                        90       100
                ....*....|....*....|....*..
gi 15027847 470 LVNVAGNDIVQ-GNKKLLLAFLWQLMR 495
Cdd:cd00014  77 LDLFEPEDLYEkGNLKKVLGTLWALAL 103

CH_PLS_FIM_rpt2

cd21218

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...

520-616

3.28e-11

Pssm-ID: 409067 Cd Length: 114 Bit Score: 60.78 E-value: 3.28e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 520 LNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGCSIFLLPE 599
Cdd:cd21218  16 LRWVNYHLKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYFLTPE 95

                        90
                ....*....|....*..
gi 15027847 600 DIIEVNQKMMLILAASI 616
Cdd:cd21218  96 DIVSGNPRLNLAFVATL 112

CH_FLN-like_rpt2

cd21184

second calponin homology (CH) domain found in the filamin family; The filamin family includes ...

269-354

1.40e-10

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

Pssm-ID: 409033 Cd Length: 103 Bit Score: 58.40 E-value: 1.40e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 269 PEKVLLKWMNFHLKkagyEKQVTNFSSDLKDGEAYAYLLNALAPE-HSTHVALETKDPTERAKKVLEQAE-KLDCKRYLS 346
Cdd:cd21184   2 GKSLLLEWVNSKIP----EYKVKNFTTDWNDGKALAALVDALKPGlIPDNESLDKENPLENATKAMDIAEeELGIPKIIT 77


                ....*...
gi 15027847 347 PKDIVDGS 354
Cdd:cd21184  78 PEDMVSPN 85

CH_SPTBN4_rpt1

cd21318

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...

388-494

3.81e-10

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: 58.50 E-value: 3.81e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 388 DVETSREERCFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPgsvnwKHANKPPI-KMPFKKVENCNEVIKIGK 464
Cdd:cd21318  33 DEREAVQKKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLEVLSG-----EQLPKPTRgRMRIHSLENVDKALQFLK 107

                        90       100       110
                ....*....|....*....|....*....|
gi 15027847 465 ELRFSLVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21318 108 EQRVHLENVGSHDIVDGNHRLTLGLIWTII 137

CH_DMD-like_rpt1

cd21186

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...

394-491

7.00e-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: 7.00e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS-LGTA--TYVNNVFEDLRNGWVLLEVLDKVSPgsvnwKHANKPPIKMPFKKVENCNEVIKIGKELRFSL 470
Cdd:cd21186   3 QKKTFTKWINSqLSKAnkPPIKDLFEDLRDGTRLLALLEVLTG-----KKLKPEKGRMRVHHLNNVNRALQVLEQNNVKL 77

                        90       100
                ....*....|....*....|.
gi 15027847 471 VNVAGNDIVQGNKKLLLAFLW 491
Cdd:cd21186  78 VNISSNDIVDGNPKLTLGLVW 98

CH_DYST_rpt1

cd21236

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...

383-494

1.99e-09

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

Pssm-ID: 409085 Cd Length: 128 Bit Score: 56.15 E-value: 1.99e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 383 EMMTDDVETSREER------CFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVE 454
Cdd:cd21236   1 QAYENVLERYKDERdkvqkkTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKG-----RMRFHRLQ 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15027847 455 NCNEVIKIGKELRFSLVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21236  76 NVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTII 115

CH_FIMB_rpt1

cd21294

first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...

414-495

5.88e-09

Pssm-ID: 409143 Cd Length: 125 Bit Score: 54.76 E-value: 5.88e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 414 VFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKM----PFKKVENCNEVIKIGKELRFSLVNVAGNDIVQGNKKLLLAF 489
Cdd:cd21294  38 LFDECKDGLVLSKLINDSVPDTIDERVLNKPPRKNkplnNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGL 117


                ....*.
gi 15027847 490 LWQLMR 495
Cdd:cd21294 118 IWQIIR 123

CH_SpAIN1-like_rpt1

cd21215

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...

394-494

9.92e-09

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

Pssm-ID: 409064 Cd Length: 107 Bit Score: 53.56 E-value: 9.92e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS-LGTATY-VNNVFEDLRNGWVLLEVLDKVSPGSVNwKHANKPpiKMPFKKVENCNEVIKIGKELRFSLV 471
Cdd:cd21215   5 QKKTFTKWLNTkLSSRGLsITDLVTDLSDGVRLIQLLEIIGDESLG-RYNKNP--KMRVQKLENVNKALEFIKSRGVKLT 81

                        90       100
                ....*....|....*....|...
gi 15027847 472 NVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21215  82 NIGAEDIVDGNLKLILGLLWTLI 104

CH_SPTB-like_rpt1

cd21246

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...

394-491

1.43e-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: 1.43e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS-LGTAT-YVNNVFEDLRNGWVLLEVLDKVSPgsvnwKHANKP-PIKMPFKKVENCNEVIKIGKELRFSL 470
Cdd:cd21246  17 QKKTFTKWVNShLARVGcRINDLYTDLRDGRMLIKLLEVLSG-----ERLPKPtKGKMRIHCLENVDKALQFLKEQRVHL 91

                        90       100
                ....*....|....*....|.
gi 15027847 471 VNVAGNDIVQGNKKLLLAFLW 491
Cdd:cd21246  92 ENMGSHDIVDGNHRLTLGLIW 112

CH_CTX_rpt1

cd21225

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...

394-495

1.76e-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: 52.92 E-value: 1.76e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINSL---GTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpiKMPFKKVENCNEVIK-IGKELRFS 469
Cdd:cd21225   5 QIKAFTAWVNSVlekRGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEP--KNRIQMIQNLHLAMLfIEEDLKIR 82

                        90       100
                ....*....|....*....|....*.
gi 15027847 470 LVNVAGNDIVQGNKKLLLAFLWQLMR 495
Cdd:cd21225  83 VQGIGAEDFVDNNKKLILGLLWTLYR 108

CH_SF

cd00014

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...

270-353

3.32e-08

Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 51.96 E-value: 3.32e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 270 EKVLLKWMNFHLKKAGYEKqVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDP---TERAKKVLEQAEKL--DCKRY 344
Cdd:cd00014   1 EEELLKWINEVLGEELPVS-ITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLglPELDL 79


                ....*....
gi 15027847 345 LSPKDIVDG 353
Cdd:cd00014  80 FEPEDLYEK 88

CH_FLN-like_rpt1

cd21183

first calponin homology (CH) domain found in the filamin family; The filamin family includes ...

394-494

4.02e-08

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

Pssm-ID: 409032 Cd Length: 108 Bit Score: 51.71 E-value: 4.02e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpiKMPFKKVENCNEVIKIGKELRFSLV 471
Cdd:cd21183   5 QANTFTRWCNEhlKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYNRRP--AFQQHYLENVSTALKFIEADHIKLV 82

                        90       100
                ....*....|....*....|...
gi 15027847 472 NVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21183  83 NIGSGDIVNGNIKLILGLIWTLI 105

CH_PLEC-like_rpt1

cd21188

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...

394-491

4.89e-08

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

Pssm-ID: 409037 Cd Length: 105 Bit Score: 51.25 E-value: 4.89e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNEVIKIGKELRFSLV 471
Cdd:cd21188   4 QKKTFTKWVNKhlIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERG-----RMRFHRLQNVQTALDFLKYRKIKLV 78

                        90       100
                ....*....|....*....|
gi 15027847 472 NVAGNDIVQGNKKLLLAFLW 491
Cdd:cd21188  79 NIRAEDIVDGNPKLTLGLIW 98

CH_FIMB_rpt3

cd21300

third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...

146-243

6.78e-08

Pssm-ID: 409149 Cd Length: 119 Bit Score: 51.27 E-value: 6.78e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 146 LPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKK---TLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEG 222
Cdd:cd21300  19 LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaEISRFKAVENTNYAVELGKQLGFSLVGIQGADITDG 98

                        90       100
                ....*....|....*....|.
gi 15027847 223 RPYLVLGLISQIIKIQMLADL 243
Cdd:cd21300  99 SRTLTLALVWQLMRFHITKTL 119

CH_jitterbug-like_rpt1

cd21227

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...

161-235

8.43e-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: 8.43e-08

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15027847 161 DGVLLCKLINVavpgtIDERAIN--TKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQII 235
Cdd:cd21227  33 DGVKLIALVEI-----LQGRKLGrvIKKPLNQHQKLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLI 104

CH_PLEC_rpt1

cd21235

first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...

394-494

8.81e-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: 51.18 E-value: 8.81e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNEVIKIGKELRFSLV 471
Cdd:cd21235   7 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 81

                        90       100
                ....*....|....*....|...
gi 15027847 472 NVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21235  82 NIRNDDIADGNPKLTLGLIWTII 104

CH_UTRN_rpt1

cd21232

first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...

394-494

9.52e-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: 50.78 E-value: 9.52e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINSLGTAT---YVNNVFEDLRNGWVLLEVLDKVSpGSVNWKHANKPPIKmpfkKVENCNEVIKIGKELRFSL 470
Cdd:cd21232   3 QKKTFTKWINARFSKSgkpPIKDMFTDLRDGRKLLDLLEGLT-GKSLPKERGSTRVH----ALNNVNRVLQVLHQNNVEL 77

                        90       100
                ....*....|....*....|....
gi 15027847 471 VNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21232  78 VNIGGTDIVDGNHKLTLGLLWSII 101

CH_SPTBN2_rpt1

cd21317

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...

388-494

1.07e-07

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

Pssm-ID: 409166 Cd Length: 132 Bit Score: 51.21 E-value: 1.07e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 388 DVETSREERCFRLWINS-LGTAT-YVNNVFEDLRNGWVLLEVLDKVSPgsvnwKHANKPPI-KMPFKKVENCNEVIKIGK 464
Cdd:cd21317  26 DEREAVQKKTFTKWVNShLARVTcRIGDLYTDLRDGRMLIRLLEVLSG-----EQLPKPTKgRMRIHCLENVDKALQFLK 100

                        90       100       110
                ....*....|....*....|....*....|
gi 15027847 465 ELRFSLVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21317 101 EQKVHLENMGSHDIVDGNHRLTLGLIWTII 130

CH_jitterbug-like_rpt1

cd21227

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...

398-496

1.96e-07

Pssm-ID: 409076 Cd Length: 109 Bit Score: 49.59 E-value: 1.96e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 398 FRLWIN-SL-GTATYVNNVFEDLRNGWVL---LEVLDKVSPGSVNwkhaNKPpiKMPFKKVENCNEVIKIGKELRFSLVN 472
Cdd:cd21227   9 FTNWVNeQLkPTGMSVEDLATDLEDGVKLialVEILQGRKLGRVI----KKP--LNQHQKLENVTLALKAMAEDGIKLVN 82

                        90       100
                ....*....|....*....|....*
gi 15027847 473 VAGNDIVQGNKKLLLAFLWQL-MRY 496
Cdd:cd21227  83 IGNEDIVNGNLKLILGLIWHLiLRY 107

CH_SYNE-like_rpt1

cd21190

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...

394-496

3.24e-07

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

Pssm-ID: 409039 Cd Length: 113 Bit Score: 49.49 E-value: 3.24e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS----LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVnwkHANKPPIKMPFKKVENCNEVIKIGKELRFS 469
Cdd:cd21190   6 QKKTFTNWINShlakLSQPIVINDLFVDIKDGTALLRLLEVLSGQKL---PIESGRVLQRAHKLSNIRNALDFLTKRCIK 82

                        90       100
                ....*....|....*....|....*..
gi 15027847 470 LVNVAGNDIVQGNKKLLLAFLWQLMRY 496
Cdd:cd21190  83 LVNINSTDIVDGKPSIVLGLIWTIILY 109

CH_AtFIM_like_rpt3

third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

146-244

3.87e-07

Pssm-ID: 409148 Cd Length: 114 Bit Score: 49.04 E-value: 3.87e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 146 LPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPY 225
Cdd:cd21299  16 LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVVKIGKQLKFSLVNVAGNDIVQGNKK 95

                        90
                ....*....|....*....
gi 15027847 226 LVLGLISQIIKIQMLADLN 244
Cdd:cd21299  96 LILALLWQLMRYHMLQLLK 114

CH_MACF1_rpt1

cd21237

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...

394-494

4.53e-07

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

Pssm-ID: 409086 Cd Length: 118 Bit Score: 48.88 E-value: 4.53e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNEVIKIGKELRFSLV 471
Cdd:cd21237   7 QKKTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKG-----RMRFHRLQNVQIALDFLKQRQVKLV 81

                        90       100
                ....*....|....*....|...
gi 15027847 472 NVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21237  82 NIRNDDITDGNPKLTLGLIWTII 104

CH_FLN_rpt1

cd21228

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...

394-494

5.31e-07

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

Pssm-ID: 409077 Cd Length: 108 Bit Score: 48.64 E-value: 5.31e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS-LGTAT-YVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMpfKKVENCNEVIKIGKELRFSLV 471
Cdd:cd21228   5 QQNTFTRWCNEhLKCVNkRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRPTFRQ--MKLENVSVALEFLERESIKLV 82

                        90       100
                ....*....|....*....|...
gi 15027847 472 NVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21228  83 SIDSSAIVDGNLKLILGLIWTLI 105

CH_DMD_rpt1

cd21231

first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...

394-494

1.18e-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: 47.61 E-value: 1.18e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINSLGTAT---YVNNVFEDLRNGWVLLEVLDKVSpgsvnwkhANKPPIKMPFKKVE---NCNEVIKIGKELR 467
Cdd:cd21231   7 QKKTFTKWINAQFAKFgkpPIEDLFTDLQDGRRLLELLEGLT--------GQKLVKEKGSTRVHalnNVNKALQVLQKNN 78

                        90       100
                ....*....|....*....|....*..
gi 15027847 468 FSLVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21231  79 VDLVNIGSADIVDGNHKLTLGLIWSII 105

CH_FLN_rpt2

cd21230

second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...

269-352

1.23e-06

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

Pssm-ID: 409079 Cd Length: 103 Bit Score: 47.38 E-value: 1.23e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 269 PEKVLLKWMNFHLKkagyEKQVTNFSSDLKDGEAYAYLLNALAP----EHSTHVAletKDPTERAKKVLEQAEK-LDCKR 343
Cdd:cd21230   2 PKQRLLGWIQNKIP----QLPITNFTTDWNDGRALGALVDSCAPglcpDWETWDP---NDALENATEAMQLAEDwLGVPQ 74


                ....*....
gi 15027847 344 YLSPKDIVD 352
Cdd:cd21230  75 LITPEEIIN 83

CH_ACTN_rpt1

cd21214

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...

394-494

1.43e-06

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

Pssm-ID: 409063 Cd Length: 105 Bit Score: 47.38 E-value: 1.43e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS----LGTAtyVNNVFEDLRNGWVLLEVLDKVSPGSVnwKHANKPpiKMPFKKVENCNEVIKIGKELRFS 469
Cdd:cd21214   6 QRKTFTAWCNShlrkAGTQ--IENIEEDFRDGLKLMLLLEVISGERL--PKPERG--KMRFHKIANVNKALDFIASKGVK 79

                        90       100
                ....*....|....*....|....*
gi 15027847 470 LVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21214  80 LVSIGAEEIVDGNLKMTLGMIWTII 104

CH_ASPM_rpt1

cd21223

first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...

411-494

3.14e-06

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

Pssm-ID: 409072 Cd Length: 113 Bit Score: 46.43 E-value: 3.14e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 411 VNNVFEDLRNG---WVLLEVLDKVSPGSvnwKHANKPPIKMPfKKVENCNEVIKI----GKELRFSLVNVAGNDIVQGNK 483
Cdd:cd21223  26 VTNLAVDLRDGvrlCRLVELLTGDWSLL---SKLRVPAISRL-QKLHNVEVALKAlkeaGVLRGGDGGGITAKDIVDGHR 101

                        90
                ....*....|.
gi 15027847 484 KLLLAFLWQLM 494
Cdd:cd21223 102 EKTLALLWRII 112

CH_SYNE2_rpt1

cd21242

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...

394-494

3.62e-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: 46.36 E-value: 3.62e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINSL----GTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPpikmpFKKVENCNEVIKIGKELRFS 469
Cdd:cd21242   6 QKRTFTNWINSQlakhSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNV-----FQCRSNIETALSFLKNKSIK 80

                        90       100
                ....*....|....*....|....*
gi 15027847 470 LVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21242  81 LINIHVPDIIEGKPSIILGLIWTII 105

CH_dMP20-like

cd21207

calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...

150-223

3.68e-06

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

Pssm-ID: 409056 [Multi-domain] Cd Length: 107 Bit Score: 46.15 E-value: 3.68e-06

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15027847 150 PATNAFFDLVKDGVLLCKLINVAVPGTIdeRAINTKKTlnPWERNENLTLGLNSAKAIGCTVVNI-GTQDIAEGR 223
Cdd:cd21207  23 DDGKDYEDVLKDGVILCKLINILKPGSV--KKINTSKM--AFKLMENIENFLTACKGYGVPKTDLfQTVDLYEKK 93

CH_SpAIN1-like_rpt1

cd21215

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...

150-236

4.59e-06

Pssm-ID: 409064 Cd Length: 107 Bit Score: 45.85 E-value: 4.59e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 150 PATNAFFDLvKDGVLLCKLINVAVPGTIDERAINTKKTLnpwERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLG 229
Cdd:cd21215  23 SITDLVTDL-SDGVRLIQLLEIIGDESLGRYNKNPKMRV---QKLENVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILG 98


                ....*..
gi 15027847 230 LISQIIK 236
Cdd:cd21215  99 LLWTLIL 105

CH_PLS_rpt3

cd21298

third calponin homology (CH) domain found in the plastin family; The plastin family includes ...

146-243

5.73e-06

Pssm-ID: 409147 Cd Length: 117 Bit Score: 45.69 E-value: 5.73e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 146 LPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINtkKTLNPWERN----ENLTLGLNSAKAIGCTVVNIGTQDIAE 221
Cdd:cd21298  18 LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVN--KPFKKLGANmkkiENCNYAVELGKKLKFSLVGIGGKDIYD 95

                        90       100
                ....*....|....*....|..
gi 15027847 222 GRPYLVLGLISQIIKIQMLADL 243
Cdd:cd21298  96 GNRTLTLALVWQLMRAYTLSIL 117

CH_dFLNA-like_rpt2

cd21315

second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...

256-352

6.64e-06

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

Pssm-ID: 409164 Cd Length: 118 Bit Score: 45.54 E-value: 6.64e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 256 DDTQDAEELMGLAPEKVLLKWMNFHLKkagyEKQVTNFSSDLKDGEAYAYLLNALAPEHSTHVAL-ETKDPTERAKKVLE 334
Cdd:cd21315   4 GEDDGPDDGKGPTPKQRLLGWIQSKVP----DLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDwDPKDAVKNAKEAMD 79

                        90
                ....*....|....*....
gi 15027847 335 QAEK-LDCKRYLSPKDIVD 352
Cdd:cd21315  80 LAEDwLDVPQLIKPEEMVN 98

CH_PLEC-like_rpt1

cd21188

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...

271-368

6.71e-06

Pssm-ID: 409037 Cd Length: 105 Bit Score: 45.47 E-value: 6.71e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 271 KVLLKWMNFHLKKAGyeKQVTNFSSDLKDGEAYAYLLNALAPEHSthvaletkdPTERAK----KVLEQAEKLDCKRY-- 344
Cdd:cd21188   6 KTFTKWVNKHLIKAR--RRVVDLFEDLRDGHNLISLLEVLSGESL---------PRERGRmrfhRLQNVQTALDFLKYrk 74

                        90       100
                ....*....|....*....|....*....
gi 15027847 345 -----LSPKDIVDGSANLNLAFVAQIFQH 368
Cdd:cd21188  75 iklvnIRAEDIVDGNPKLTLGLIWTIILH 103

CH_SPTBN1_rpt1

cd21316

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...

388-494

7.32e-06

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

Pssm-ID: 409165 Cd Length: 154 Bit Score: 46.58 E-value: 7.32e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 388 DVETSREERCFRLWINS--LGTATYVNNVFEDLRNGWVLLEVLDKVSPgsvnwKHANKPPI-KMPFKKVENCNEVIKIGK 464
Cdd:cd21316  48 DEREAVQKKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLEVLSG-----ERLPKPTKgRMRIHCLENVDKALQFLK 122

                        90       100       110
                ....*....|....*....|....*....|
gi 15027847 465 ELRFSLVNVAGNDIVQGNKKLLLAFLWQLM 494
Cdd:cd21316 123 EQRVHLENMGSHDIVDGNHRLTLGLIWTII 152

CH_FLNC_rpt2

cd21314

second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...

259-352

7.42e-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: 45.45 E-value: 7.42e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 259 QDAEELMGLAPEKVLLKWMNFHLKKAgyekQVTNFSSDLKDGEAYAYLLNALAPEHSTH-VALETKDPTERAKKVLEQAE 337
Cdd:cd21314   2 EDEEDARKQTPKQRLLGWIQNKVPQL----PITNFNRDWQDGKALGALVDNCAPGLCPDwESWDPNQPVQNAREAMQQAD 77

                        90
                ....*....|....*.
gi 15027847 338 K-LDCKRYLSPKDIVD 352
Cdd:cd21314  78 DwLGVPQVIAPEEIVD 93

CH_NAV2-like

cd21212

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...

275-353

8.45e-06

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

Pssm-ID: 409061 Cd Length: 105 Bit Score: 44.88 E-value: 8.45e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 275 KWMNFHLKKAGYEKQVTNFSSDLKDGEAYAYLLNALAPEHSTHValeTKDPTERAKKVleqaEKLD-CKRYL-------- 345
Cdd:cd21212   7 DWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGI---HSRPKTRAQKL----ENIQaCLQFLaalgvdvq 79

                        90
                ....*....|
gi 15027847 346 --SPKDIVDG 353
Cdd:cd21212  80 giTAEDIVDG 89

CH_CLMN_rpt1

cd21191

first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...

394-496

1.00e-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: 45.26 E-value: 1.00e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWIN----SLGTATYVNNVFEDLRNGWVLLEVLDKVSpgSVNWKHANKPPIKMPFKkVENCNEVIKIGKELRFS 469
Cdd:cd21191   6 QKRTFTRWINlhleKCNPPLEVKDLFVDIQDGKILMALLEVLS--GQNLLQEYKPSSHRIFR-LNNIAKALKFLEDSNVK 82

                        90       100
                ....*....|....*....|....*..
gi 15027847 470 LVNVAGNDIVQGNKKLLLAFLWQLMRY 496
Cdd:cd21191  83 LVSIDAAEIADGNPSLVLGLIWNIILF 109

CH_DIXDC1

cd21213

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...

276-353

1.05e-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: 44.98 E-value: 1.05e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 276 WMNFHLKKAGYEKQVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDCKR----YLSPKDIV 351
Cdd:cd21213   8 WVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRirmhQTSAKDIV 87


                ..
gi 15027847 352 DG 353
Cdd:cd21213  88 DG 89

CH_PLS1_rpt1

cd21323

first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...

371-495

2.40e-05

Pssm-ID: 409172 Cd Length: 145 Bit Score: 44.65 E-value: 2.40e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 371 GLTVDDSKTSFAEMMTDDVETSREERCFRLWINS-----------LGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWK 439
Cdd:cd21323   2 GITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKalegdpdckhvVPMNPTDESLFKSLADGILLCKMINLSQPDTIDER 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15027847 440 HANKPPIKmPFKKVENCNEVIKIGKELRFSLVNVAGNDIVQGNKKLLLAFLWQLMR 495
Cdd:cd21323  82 AINKKKLT-PFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIK 136

CH_DMD-like_rpt1

cd21186

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...

271-368

3.47e-05

Pssm-ID: 409035 Cd Length: 107 Bit Score: 43.14 E-value: 3.47e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 271 KVLLKWMNFHLKKAGYEkQVTNFSSDLKDGEAYAYLLNAL-----APEH-STHV-ALETKDpteRAKKVLEQAE-KLdck 342
Cdd:cd21186   5 KTFTKWINSQLSKANKP-PIKDLFEDLRDGTRLLALLEVLtgkklKPEKgRMRVhHLNNVN---RALQVLEQNNvKL--- 77

                        90       100
                ....*....|....*....|....*.
gi 15027847 343 RYLSPKDIVDGSANLNLAFVAQIFQH 368
Cdd:cd21186  78 VNISSNDIVDGNPKLTLGLVWSIILH 103

CH_PLS_rpt1

cd21292

first calponin homology (CH) domain found in the plastin family; The plastin family includes ...

394-495

3.66e-05

Pssm-ID: 409141 Cd Length: 145 Bit Score: 44.19 E-value: 3.66e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS-LGT----ATYV------NNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKmPFKKVENCNEVIKI 462
Cdd:cd21292  25 EKVAFVNWINKnLGDdpdcKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTIDERAINKKKLT-VFTIHENLTLALNS 103

                        90       100       110
                ....*....|....*....|....*....|...
gi 15027847 463 GKELRFSLVNVAGNDIVQGNKKLLLAFLWQLMR 495
Cdd:cd21292 104 ASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIR 136

CH_LMO7-like

cd21208

calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...

155-208

3.97e-05

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

Pssm-ID: 409057 [Multi-domain] Cd Length: 119 Bit Score: 43.48 E-value: 3.97e-05

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15027847 155 FFDLVKDGVLLCKLINVAVPGTIdeRAINTKKTlnPWERNENLTLGLNSAKAIG 208
Cdd:cd21208  22 FRESLEDGILLCELINAIKPGSI--KKINRLPT--PIAGLDNLNLFLKACEDLG 71

CH_CYTS

cd21199

calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...

265-368

4.92e-05

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

Pssm-ID: 409048 Cd Length: 112 Bit Score: 43.12 E-value: 4.92e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 265 MGLAPEKVLLKWMnfHLKKAGYEK-QVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDCKR 343
Cdd:cd21199   5 YGGSKRNALLKWC--QEKTQGYKGiDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGIPT 82

                        90       100
                ....*....|....*....|....*...
gi 15027847 344 YLSPKDIVDGSA---NLNLAFVAQIFQH 368
Cdd:cd21199  83 TLTIDEMVSMERpdwQSVMSYVTAIYKH 110

CH_FLNA_rpt2

cd21312

second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...

257-352

7.54e-05

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

Pssm-ID: 409161 Cd Length: 114 Bit Score: 42.49 E-value: 7.54e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 257 DTQDAEELMGLAPEKVLLKWMNFHLKKAgyekQVTNFSSDLKDGEAYAYLLNALAPEHSTHV-ALETKDPTERAKKVLEQ 335
Cdd:cd21312   1 DEEEDEEAKKQTPKQRLLGWIQNKLPQL----PITNFSRDWQSGRALGALVDSCAPGLCPDWdSWDASKPVTNAREAMQQ 76

                        90
                ....*....|....*...
gi 15027847 336 AEK-LDCKRYLSPKDIVD 352
Cdd:cd21312  77 ADDwLGIPQVITPEEIVD 94

CH_jitterbug-like_rpt3

cd21185

third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...

274-354

7.69e-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: 41.90 E-value: 7.69e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 274 LKWMNFHLKkagyEKQVTNFSSDLKDGEAYAYLLNAL-----APEHSTHvaletKDPTERAKKVLEQAEKLDCKRYLSPK 348
Cdd:cd21185   7 LRWVRQLLP----DVDVNNFTTDWNDGRLLCGLVNALggsvpGWPNLDP-----EESENNIQRGLEAGKSLGVEPVLTAE 77


                ....*.
gi 15027847 349 DIVDGS 354
Cdd:cd21185  78 EMADPE 83

CH_FLN-like_rpt1

cd21183

first calponin homology (CH) domain found in the filamin family; The filamin family includes ...

161-235

8.26e-05

Pssm-ID: 409032 Cd Length: 108 Bit Score: 42.47 E-value: 8.26e-05

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15027847 161 DGVLLCKLINVaVPGTIDERAINtKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQII 235
Cdd:cd21183  33 DGLCLIALLEN-LSTRPLKRSYN-RRPAFQQHYLENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTLI 105

CH_SYNE2_rpt2

cd21244

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...

267-370

8.67e-05

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

Pssm-ID: 409093 Cd Length: 109 Bit Score: 42.13 E-value: 8.67e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 267 LAPEKVLLKWMNFHLKKAGyEKQVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEK-LDCKRYL 345
Cdd:cd21244   4 MSARKALLLWAQEQCAKVG-SISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQeLKIPRLL 82

                        90       100
                ....*....|....*....|....*..
gi 15027847 346 SPKD--IVDGSANLNLAFVAQIFQHRN 370
Cdd:cd21244  83 EPEDvdVVNPDEKSIMTYVAQFLQYSK 109

CH_CYTSB

cd21257

calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...

266-368

9.80e-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: 42.32 E-value: 9.80e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 266 GLAPEKVLLKWMnfHLKKAGYEK-QVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDCKRY 344
Cdd:cd21257   6 GGSKRNALLKWC--QKKTEGYPNiDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGIKPS 83

                        90       100
                ....*....|....*....|....*..
gi 15027847 345 LSPKDIVDGSA---NLNLAFVAQIFQH 368
Cdd:cd21257  84 LELSEMMYTDRpdwQSVMQYVAQIYKY 110

CH_SYNE-like_rpt2

cd21192

second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...

270-350

1.06e-04

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

Pssm-ID: 409041 Cd Length: 107 Bit Score: 42.03 E-value: 1.06e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 270 EKVLLKWMNfhlKKAG--YEKQVTNFSSDLKDGEAYAYLLNALAPEhstHVALET------KDPTERAKKVLEQAekLDC 341
Cdd:cd21192   5 EKALLKWVQ---AEIGkyYGIRVTDFDKSWRDGVAFLALIHAIRPD---LVDMKTvknrspRDNLELAFRIAEQH--LNI 76


                ....*....
gi 15027847 342 KRYLSPKDI 350
Cdd:cd21192  77 PRLLEVEDV 85

SAC6

COG5069

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

392-627

1.18e-04

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

Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 45.32 E-value: 1.18e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 392 SREERCFRLWIN---SLGTATYVNNVFEDLRnGWV----LLEVLDKVSPGSVNwkhankPPIKMPFKKVENCNEVIKIGK 464
Cdd:COG5069   8 KVQKKTFTKWTNeklISGGQKEFGDLDTDLK-DGVklaqLLEALQKDNAGEYN------ETPETRIHVMENVSGRLEFIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 465 ELRFSLVNVAGNDIVQGNKKLLLAFLWqlmryTMLQLLRNLRSHSQGKEITDADILNWANRKVkrGGRTSQADSFR-DKN 543
Cdd:COG5069  81 GKGVKLFNIGPQDIVDGNPKLILGLIW-----SLISRLTIATINEEGELTKHINLLLWCDEDT--GGYKPEVDTFDfFRS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 544 LSSGMFFLELLS-----AVEPRVVNWSlvtngetEEDKKLNATYIISVARK-LGCSIFLLPEDIIEVN----QKMMLILA 613
Cdd:COG5069 154 WRDGLAFSALIHdsrpdTLDPNVLDLQ-------KKNKALNNFQAFENANKvIGIARLIGVEDIVNVSipdeRSIMTYVS 226

                       250
                ....*....|....
gi 15027847 614 ASIMYWSLQQQSDT 627
Cdd:COG5069 227 WYIIRFGLLEKIDI 240

CH_NAV2-like

cd21212

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...

401-508

1.38e-04

Pssm-ID: 409061 Cd Length: 105 Bit Score: 41.41 E-value: 1.38e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 401 WINSL----GTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANkppIKMPFKKVENCNEVIKIGKELRFSLVNVAGN 476
Cdd:cd21212   8 WANHYlekgGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSR---PKTRAQKLENIQACLQFLAALGVDVQGITAE 84

                        90       100       110
                ....*....|....*....|....*....|..
gi 15027847 477 DIVQGNKKlllaflwqlmryTMLQLLRNLRSH 508
Cdd:cd21212  85 DIVDGNLK------------AILGLFFSLSRY 104

CH_SYNE1_rpt1

cd21241

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...

124-235

2.24e-04

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

Pssm-ID: 409090 Cd Length: 113 Bit Score: 41.21 E-value: 2.24e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 124 EKASYVSHVNNYL-RDDPFLKsylpidpaTNAFFDLVKDGVLLCKLINV----AVPGtidERAINTKKTlnPWERNENLT 198
Cdd:cd21241   6 QKKTFTNWINSYLaKRKPPMK--------VEDLFEDIKDGTKLLALLEVlsgeKLPC---EKGRRLKRV--HFLSNINTA 72

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15027847 199 LGLNSAKAIgcTVVNIGTQDIAEGRPYLVLGLISQII 235
Cdd:cd21241  73 LKFLESKKI--KLVNINPTDIVDGKPSIVLGLIWTII 107

CH_SYNE1_rpt1

cd21241

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...

394-496

2.88e-04

Pssm-ID: 409090 Cd Length: 113 Bit Score: 40.82 E-value: 2.88e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 394 EERCFRLWINS-LGTAT---YVNNVFEDLRNGWVLLEVLDKVSpGSvnwkhankppiKMPFKK---------VENCNEVI 460
Cdd:cd21241   6 QKKTFTNWINSyLAKRKppmKVEDLFEDIKDGTKLLALLEVLS-GE-----------KLPCEKgrrlkrvhfLSNINTAL 73

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15027847 461 KIGKELRFSLVNVAGNDIVQGNKKLLLAFLWQLMRY 496
Cdd:cd21241  74 KFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILY 109

CH_AtFIM_like_rpt4

fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...

273-365

2.89e-04

Pssm-ID: 409151 Cd Length: 109 Bit Score: 40.61 E-value: 2.89e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 273 LLKWMNFHLKKAGYEKQVTNF-SSDLKDGEAYAYLLNALAPEhSTHVALETKDPTERAKK-----VLEQAEKLDCKRYLS 346
Cdd:cd21302   7 ILSWANRKVRTMGRKSQIESFkDKSLSSGLFFLELLWAVEPR-VVNWNLVTKGETDEEKRlnatyIISVARKLGCSIFLL 85

                        90
                ....*....|....*....
gi 15027847 347 PKDIVDGSANLNLAFVAQI 365
Cdd:cd21302  86 PEDIVEVNQKMILILTASI 104

CH_PLS3_rpt1

cd21325

first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...

412-504

3.16e-04

Pssm-ID: 409174 Cd Length: 148 Bit Score: 41.58 E-value: 3.16e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 412 NNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIkMPFKKVENCNEVIKIGKELRFSLVNVAGNDIVQGNKKLLLAFLW 491
Cdd:cd21325  54 DDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKL-TPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLW 132

                        90
                ....*....|....*.
gi 15027847 492 QLMR---YTMLQLLRN 504
Cdd:cd21325 133 QIIKiglFADIELSRN 148

CH_SPTB_rpt2

cd21319

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...

273-350

3.48e-04

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

Pssm-ID: 409168 Cd Length: 112 Bit Score: 40.76 E-value: 3.48e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 273 LLKWMnfHLKKAGYEK-QVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAE-KLDCKRYLSPKDI 350
Cdd:cd21319  10 LLLWC--QMKTAGYPNvNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGITKLLDPEDV 87

CH_CTX_rpt2

cd21226

second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...

269-368

3.91e-04

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

Pssm-ID: 409075 Cd Length: 103 Bit Score: 40.14 E-value: 3.91e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 269 PEKVLLKWMNFHLKkaGYEKQ-VTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEK-LDCKRYLS 346
Cdd:cd21226   1 SEDGLLAWCRQTTE--GYDGVnITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLE 78

                        90       100
                ....*....|....*....|...
gi 15027847 347 PKDIVDGSA-NLNLAFVAQIFQH 368
Cdd:cd21226  79 AEDVMTGNPdERSIVLYTSLFYH 101

CH_CNN1

cd21282

calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...

153-208

4.56e-04

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

Pssm-ID: 409131 [Multi-domain] Cd Length: 108 Bit Score: 40.24 E-value: 4.56e-04

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15027847 153 NAFFDLVKDGVLLCKLINVAVPGTIdeRAINtKKTLNpWERNENLTlglNSAKAIG 208
Cdd:cd21282  22 DNFMDGLKDGVILCELINKLQPGSV--RKIN-ESTQN-WHKLENIG---NFIKAIM 70

CH_CYTSA

cd21256

calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...

266-351

4.92e-04

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

Pssm-ID: 409105 Cd Length: 119 Bit Score: 40.44 E-value: 4.92e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 266 GLAPEKVLLKWMnfHLKKAGYEK-QVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDCKRY 344
Cdd:cd21256  12 GGSKRNALLKWC--QKKTEGYQNiDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAESVGIKST 89


                ....*..
gi 15027847 345 LSPKDIV 351
Cdd:cd21256  90 LDINEMV 96

CH_SYNE2_rpt1

cd21242

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...

151-235

5.90e-04

Pssm-ID: 409091 Cd Length: 111 Bit Score: 39.81 E-value: 5.90e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 151 ATNAFFDLVKDGVLLCKLINVavpgtIDERAINTKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGL 230
Cdd:cd21242  26 VVSDLFTDIQDGHRLLDLLEV-----LSGQQLPREKGHNVFQCRSNIETALSFLKNKSIKLINIHVPDIIEGKPSIILGL 100


                ....*
gi 15027847 231 ISQII 235
Cdd:cd21242 101 IWTII 105

CH_EHBP

cd21198

calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...

269-373

6.69e-04

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

Pssm-ID: 409047 Cd Length: 105 Bit Score: 39.72 E-value: 6.69e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 269 PEKVLLKWMNFHLKkaGYEK-QVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDCKRYLSP 347
Cdd:cd21198   2 SGQDLLEWCQEVTK--GYRGvKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDP 79

                        90       100
                ....*....|....*....|....*.
gi 15027847 348 KDIVDGSANLNLAFVAQIFQHRNGLT 373
Cdd:cd21198  80 ADMVLLSVPDKLSVMTYLHQIRAHFT 105

CH_SYNE-like_rpt1

cd21190

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...

153-235

7.65e-04

Pssm-ID: 409039 Cd Length: 113 Bit Score: 39.86 E-value: 7.65e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 153 NAFFDLVKDGVLLCKLINVAvpgTIDERAINTKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLIS 232
Cdd:cd21190  28 NDLFVDIKDGTALLRLLEVL---SGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIW 104


                ...
gi 15027847 233 QII 235
Cdd:cd21190 105 TII 107

CH_CNN1

cd21282

calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...

395-461

8.82e-04

Pssm-ID: 409131 [Multi-domain] Cd Length: 108 Bit Score: 39.47 E-value: 8.82e-04

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15027847 395 ERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVnwKHANKPpiKMPFKKVENCNEVIK 461
Cdd:cd21282   5 EEELRVWIEGVTGRRIGDNFMDGLKDGVILCELINKLQPGSV--RKINES--TQNWHKLENIGNFIK 67

CH_PLS2_rpt1

cd21324

first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...

412-495

9.23e-04

Pssm-ID: 409173 Cd Length: 145 Bit Score: 39.99 E-value: 9.23e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 412 NNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKmPFKKVENCNEVIKIGKELRFSLVNVAGNDIVQGNKKLLLAFLW 491
Cdd:cd21324  54 DDLFKAVGDGIVLCKMINFSVPDTIDERTINKKKLT-PFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLW 132


                ....
gi 15027847 492 QLMR 495
Cdd:cd21324 133 QVIK 136

CH_SpAIN1-like_rpt1

cd21215

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...

270-362

1.30e-03

Pssm-ID: 409064 Cd Length: 107 Bit Score: 38.92 E-value: 1.30e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15027847 270 EKVLLKWMNFHLKKAGYEkqVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETK---DPTERAKKVLEQAEKLDCKRY-L 345
Cdd:cd21215   6 KKTFTKWLNTKLSSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKmrvQKLENVNKALEFIKSRGVKLTnI 83

                        90
                ....*....|....*..
gi 15027847 346 SPKDIVDGSANLNLAFV 362
Cdd:cd21215  84 GAEDIVDGNLKLILGLL 100

CH_AtFIM_like_rpt1