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Conserved domains on  [gi|568960615|ref|XP_006510811|]
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plastin-1 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
21-165 4.15e-107

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).


The actual alignment was detected with superfamily member cd21323:

Pssm-ID: 469584  Cd Length: 145  Bit Score: 316.99  E-value: 4.15e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  21 EGITAIGGTSSISSEGTQHSYSEEEKVAFVNWINKALENDADCSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDE 100
Cdd:cd21323    1 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568960615 101 RAINKKKLTPFTVSENLNLALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKVGLFADIEI 165
Cdd:cd21323   81 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
313-430 2.45e-84

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).


The actual alignment was detected with superfamily member cd21329:

Pssm-ID: 469584  Cd Length: 118  Bit Score: 257.61  E-value: 2.45e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 313 LEGESKEERTFRNWMNSLGVNPYINHLYSDLADALVIFQLYEMIRVPVNWSQVNKPPYPALGGNMKKIENCNYAVELGKN 392
Cdd:cd21329    1 LEGESSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRVPVDWGHVNKPPYPALGGNMKKIENCNYAVELGKN 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 393 EAKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVL 430
Cdd:cd21329   81 KAKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
SAC6 super family cl26648
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
27-543 1.34e-82

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


The actual alignment was detected with superfamily member COG5069:

Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 269.50  E-value: 1.34e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  27 GGTSSISSEGTQHSYSEEEKvaFVNWINKALENDADCSHLLPmNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINK- 105
Cdd:COG5069  104 GLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLq 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 106 ---KKLTPFTVSENLNLALNSASAIG-CTVVNIGAQDLKEgkpHLVLgLLWQIIKVGLFADIEISRNEaLIALLKDGEDL 181
Cdd:COG5069  181 kknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERS---IMTY-VSWYIIRFGLLEKIDIALHR-VYRLLEADETL 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 182 EElMKLSPEELLLRWVN-YHLTNAGWRTInNFSQDIKDSKAYFHLLNQIAPKGDRddGPAVAIDLsgfnekndLKRAGFM 260
Cdd:COG5069  256 IQ-LRLPYEIILLRLLNlIHLKQANWKVV-NFSKDVSDGENYTDLLNQLNALCSR--APLETTDL--------HSLAGQI 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 261 LQEADKLGCRQFVTPAdvvsGNPKLNLAFVANLFNTYPCL------HKPDNNDIDlnlLEGEsKEERTFRNWMNSLGVNP 334
Cdd:COG5069  324 LQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQepleeeEKPEIEEFD---AEGE-FEARVFTFWLNSLDVSP 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 335 YINHLYSDLADALVIFQLYEMIRVP--VNWSQVNKPPYPALGGN-MKKIENCNYAVELGKNEAkFSLVGIAGQDLNEGNa 411
Cdd:COG5069  396 EITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVGIKGLEILDGI- 473
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 412 TLTLALVWQLMRRYTLKVLSDLGEGEKVTDDI-IIKWVNQTLKSANKSTSISSFKDKSISTSLP-VLDLIDAIAPNAVRQ 489
Cdd:COG5069  474 RLKLTLVWQVLRSNTALFNHVLKKDGCGLSDSdLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDVLKGIHSELVDY 553
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568960615 490 EMIKREHLTDEDKLNNAKYAIS--VARKIGARIYALPDDLVEVKPKM-VMTVFACLM 543
Cdd:COG5069  554 DLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
 
Name Accession Description Interval E-value
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
21-165 4.15e-107

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: 316.99  E-value: 4.15e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  21 EGITAIGGTSSISSEGTQHSYSEEEKVAFVNWINKALENDADCSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDE 100
Cdd:cd21323    1 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568960615 101 RAINKKKLTPFTVSENLNLALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKVGLFADIEI 165
Cdd:cd21323   81 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
313-430 2.45e-84

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: 257.61  E-value: 2.45e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 313 LEGESKEERTFRNWMNSLGVNPYINHLYSDLADALVIFQLYEMIRVPVNWSQVNKPPYPALGGNMKKIENCNYAVELGKN 392
Cdd:cd21329    1 LEGESSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRVPVDWGHVNKPPYPALGGNMKKIENCNYAVELGKN 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 393 EAKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVL 430
Cdd:cd21329   81 KAKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
27-543 1.34e-82

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 269.50  E-value: 1.34e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  27 GGTSSISSEGTQHSYSEEEKvaFVNWINKALENDADCSHLLPmNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINK- 105
Cdd:COG5069  104 GLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLq 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 106 ---KKLTPFTVSENLNLALNSASAIG-CTVVNIGAQDLKEgkpHLVLgLLWQIIKVGLFADIEISRNEaLIALLKDGEDL 181
Cdd:COG5069  181 kknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERS---IMTY-VSWYIIRFGLLEKIDIALHR-VYRLLEADETL 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 182 EElMKLSPEELLLRWVN-YHLTNAGWRTInNFSQDIKDSKAYFHLLNQIAPKGDRddGPAVAIDLsgfnekndLKRAGFM 260
Cdd:COG5069  256 IQ-LRLPYEIILLRLLNlIHLKQANWKVV-NFSKDVSDGENYTDLLNQLNALCSR--APLETTDL--------HSLAGQI 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 261 LQEADKLGCRQFVTPAdvvsGNPKLNLAFVANLFNTYPCL------HKPDNNDIDlnlLEGEsKEERTFRNWMNSLGVNP 334
Cdd:COG5069  324 LQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQepleeeEKPEIEEFD---AEGE-FEARVFTFWLNSLDVSP 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 335 YINHLYSDLADALVIFQLYEMIRVP--VNWSQVNKPPYPALGGN-MKKIENCNYAVELGKNEAkFSLVGIAGQDLNEGNa 411
Cdd:COG5069  396 EITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVGIKGLEILDGI- 473
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 412 TLTLALVWQLMRRYTLKVLSDLGEGEKVTDDI-IIKWVNQTLKSANKSTSISSFKDKSISTSLP-VLDLIDAIAPNAVRQ 489
Cdd:COG5069  474 RLKLTLVWQVLRSNTALFNHVLKKDGCGLSDSdLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDVLKGIHSELVDY 553
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568960615 490 EMIKREHLTDEDKLNNAKYAIS--VARKIGARIYALPDDLVEVKPKM-VMTVFACLM 543
Cdd:COG5069  554 DLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
177-298 2.96e-79

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: 244.41  E-value: 2.96e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 177 DGEDLEELMKLSPEELLLRWVNYHLTNAGWRTINNFSQDIKDSKAYFHLLNQIAPKGDrDDGPAVAIDLSGFNEKNDLKR 256
Cdd:cd21326    1 EGEELEELMKLSPEELLLRWVNYHLTNAGWQNISNFSQDIKDSRAYFHLLNQIAPKGD-VFDENIEIDFSGFNEKNDLKR 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568960615 257 AGFMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 298
Cdd:cd21326   80 AEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 121
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
43-158 3.34e-22

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 91.58  E-value: 3.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615   43 EEEKVAFVNWINKALENDADcshllpmNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINKKkltPFTVSENLNLALN 122
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGP-------GVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568960615  123 SAS-AIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKVG 158
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
187-298 1.81e-20

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: 86.57  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  187 LSPEELLLRWVNYHLTNAGWRT-INNFSQDIKDSKAYFHLLNQIAPKgdrddgpAVAIDLSGFNEKNDLKRAGFMLQEA- 264
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVrVTNFTTDLRDGLALCALLNKLAPG-------LVDKKKLNKSEFDKLENINLALDVAe 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568960615  265 DKLGCRQF-VTPADVVSGNPKLNLAFVANLFNTYP 298
Cdd:pfam00307  74 KKLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
48-155 5.89e-19

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 81.98  E-value: 5.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615    48 AFVNWINKALENDAdcshllpmNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINKKKlTPFTVSENLNLALNSASAI 127
Cdd:smart00033   2 TLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEKL 72
                           90       100
                   ....*....|....*....|....*...
gi 568960615   128 GCTVVNIGAQDLKEGkPHLVLGLLWQII 155
Cdd:smart00033  73 GGKVVLFEPEDLVEG-PKLILGVIWTLI 99
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
319-425 2.64e-17

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 77.71  E-value: 2.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  319 EERTFRNWMNSL----GVNPYINHLYSDLADALVIFQLYEMIRvP--VNWSQVNKPPypalggnMKKIENCNYAVELGKN 392
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 568960615  393 EAKFSLVGIAGQDLNEGNATLTLALVWQLMRRY 425
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
191-294 2.18e-15

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 71.96  E-value: 2.18e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615   191 ELLLRWVNYHLTNAGWRTINNFSQDIKDSKAYFHLLNQIAPKGDRDDGPAvaidlSGFNEKNDLKRAGFMLQEADKLGC- 269
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVA-----ASLSRFKKIENINLALSFAEKLGGk 75
                           90       100
                   ....*....|....*....|....*
gi 568960615   270 RQFVTPADVVSGnPKLNLAFVANLF 294
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLI 99
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
321-424 1.25e-14

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 69.65  E-value: 1.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615   321 RTFRNWMNSLGVN---PYINHLYSDLADALVIFQLYEMIRVP-VNWSQVNKPPYPalggnMKKIENCNYAVELGKnEAKF 396
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAE-KLGG 74
                           90       100
                   ....*....|....*....|....*...
gi 568960615   397 SLVGIAGQDLNEGNaTLTLALVWQLMRR 424
Cdd:smart00033  75 KVVLFEPEDLVEGP-KLILGVIWTLISL 101
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
310-517 1.63e-04

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 44.55  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 310 LNLLEGESKEERTFRNWMN---SLGVNPYINHLYSDLADALVIFQLYEMIRvPVNWSQVNKPPYPalggNMKKIENCNYA 386
Cdd:COG5069    1 MEAKKWQKVQKKTFTKWTNeklISGGQKEFGDLDTDLKDGVKLAQLLEALQ-KDNAGEYNETPET----RIHVMENVSGR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 387 VELGKNEAKfSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVLSDlgEGEKVTDDIIIKWVNQTLKSANKSTSISSFKD 466
Cdd:COG5069   76 LEFIKGKGV-KLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINE--EGELTKHINLLLWCDEDTGGYKPEVDTFDFFR 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568960615 467 ---------KSISTSLPvldliDAIAPNAVRQEmiKREHLTDEDK-LNNAKYAISVARKIG 517
Cdd:COG5069  153 swrdglafsALIHDSRP-----DTLDPNVLDLQ--KKNKALNNFQaFENANKVIGIARLIG 206
 
Name Accession Description Interval E-value
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
21-165 4.15e-107

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: 316.99  E-value: 4.15e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  21 EGITAIGGTSSISSEGTQHSYSEEEKVAFVNWINKALENDADCSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDE 100
Cdd:cd21323    1 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568960615 101 RAINKKKLTPFTVSENLNLALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKVGLFADIEI 165
Cdd:cd21323   81 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
21-165 1.63e-100

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: 299.97  E-value: 1.63e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  21 EGITAIGGTSSISSEGTQHSYSEEEKVAFVNWINKALENDADCSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDE 100
Cdd:cd21292    1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568960615 101 RAINKKKLTPFTVSENLNLALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKVGLFADIEI 165
Cdd:cd21292   81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
313-430 2.45e-84

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: 257.61  E-value: 2.45e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 313 LEGESKEERTFRNWMNSLGVNPYINHLYSDLADALVIFQLYEMIRVPVNWSQVNKPPYPALGGNMKKIENCNYAVELGKN 392
Cdd:cd21329    1 LEGESSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRVPVDWGHVNKPPYPALGGNMKKIENCNYAVELGKN 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 393 EAKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVL 430
Cdd:cd21329   81 KAKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
21-168 4.10e-84

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: 258.06  E-value: 4.10e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  21 EGITAIGGTSSISSEGTQHSYSEEEKVAFVNWINKALENDADCSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDE 100
Cdd:cd21325    1 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960615 101 RAINKKKLTPFTVSENLNLALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKVGLFADIEISRN 168
Cdd:cd21325   81 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRN 148
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
297-430 1.19e-83

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: 256.08  E-value: 1.19e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 297 YPCLHKPDNNDIDLNLLEGESKEERTFRNWMNSLGVNPYINHLYSDLADALVIFQLYEMIRVPVNWSQVNKPPYPALGGN 376
Cdd:cd21331    1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568960615 377 MKKIENCNYAVELGKNEAKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVL 430
Cdd:cd21331   81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
27-543 1.34e-82

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 269.50  E-value: 1.34e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  27 GGTSSISSEGTQHSYSEEEKvaFVNWINKALENDADCSHLLPmNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINK- 105
Cdd:COG5069  104 GLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLq 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 106 ---KKLTPFTVSENLNLALNSASAIG-CTVVNIGAQDLKEgkpHLVLgLLWQIIKVGLFADIEISRNEaLIALLKDGEDL 181
Cdd:COG5069  181 kknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERS---IMTY-VSWYIIRFGLLEKIDIALHR-VYRLLEADETL 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 182 EElMKLSPEELLLRWVN-YHLTNAGWRTInNFSQDIKDSKAYFHLLNQIAPKGDRddGPAVAIDLsgfnekndLKRAGFM 260
Cdd:COG5069  256 IQ-LRLPYEIILLRLLNlIHLKQANWKVV-NFSKDVSDGENYTDLLNQLNALCSR--APLETTDL--------HSLAGQI 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 261 LQEADKLGCRQFVTPAdvvsGNPKLNLAFVANLFNTYPCL------HKPDNNDIDlnlLEGEsKEERTFRNWMNSLGVNP 334
Cdd:COG5069  324 LQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQepleeeEKPEIEEFD---AEGE-FEARVFTFWLNSLDVSP 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 335 YINHLYSDLADALVIFQLYEMIRVP--VNWSQVNKPPYPALGGN-MKKIENCNYAVELGKNEAkFSLVGIAGQDLNEGNa 411
Cdd:COG5069  396 EITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVGIKGLEILDGI- 473
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 412 TLTLALVWQLMRRYTLKVLSDLGEGEKVTDDI-IIKWVNQTLKSANKSTSISSFKDKSISTSLP-VLDLIDAIAPNAVRQ 489
Cdd:COG5069  474 RLKLTLVWQVLRSNTALFNHVLKKDGCGLSDSdLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDVLKGIHSELVDY 553
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568960615 490 EMIKREHLTDEDKLNNAKYAIS--VARKIGARIYALPDDLVEVKPKM-VMTVFACLM 543
Cdd:COG5069  554 DLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
177-298 2.96e-79

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: 244.41  E-value: 2.96e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 177 DGEDLEELMKLSPEELLLRWVNYHLTNAGWRTINNFSQDIKDSKAYFHLLNQIAPKGDrDDGPAVAIDLSGFNEKNDLKR 256
Cdd:cd21326    1 EGEELEELMKLSPEELLLRWVNYHLTNAGWQNISNFSQDIKDSRAYFHLLNQIAPKGD-VFDENIEIDFSGFNEKNDLKR 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568960615 257 AGFMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 298
Cdd:cd21326   80 AEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 121
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
21-165 3.04e-79

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: 245.30  E-value: 3.04e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  21 EGITAIGGTSSISSEGTQHSYSEEEKVAFVNWINKALENDADCSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDE 100
Cdd:cd21324    1 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568960615 101 RAINKKKLTPFTVSENLNLALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKVGLFADIEI 165
Cdd:cd21324   81 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
432-546 1.22e-75

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: 234.84  E-value: 1.22e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 432 DLGEGEKVTDDIIIKWVNQTLKSANKSTSISSFKDKSISTSLPVLDLIDAIAPNAVRQEMIKREHLTDEDKLNNAKYAIS 511
Cdd:cd21332    1 DLGEGEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDLSDADKLNNAKYAIS 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568960615 512 VARKIGARIYALPDDLVEVKPKMVMTVFACLMGKG 546
Cdd:cd21332   81 VARKIGARVYALPEDLVEVKPKMVMTVFACLMGKG 115
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
307-430 1.94e-75

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: 234.88  E-value: 1.94e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 307 DIDLNLLEGESKEERTFRNWMNSLGVNPYINHLYSDLADALVIFQLYEMIRVPVNWSQVNKPPYPALGGNMKKIENCNYA 386
Cdd:cd21330    2 DIDWSSIEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGENMKKLENCNYA 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568960615 387 VELGKNEAKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVL 430
Cdd:cd21330   82 VELGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 125
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
174-295 4.11e-75

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: 233.70  E-value: 4.11e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 174 LLKDGEDLEELMKLSPEELLLRWVNYHLTNAGWRTINNFSQDIKDSKAYFHLLNQIAPKGDRDDGPAVAIDLSGFNEKND 253
Cdd:cd21328    1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEPRIDINMSGFNEKDD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568960615 254 LKRAGFMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 295
Cdd:cd21328   81 LKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
313-430 6.80e-74

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: 230.20  E-value: 6.80e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 313 LEGESKEERTFRNWMNSLGVNPYINHLYSDLADALVIFQLYEMIRVPVNWSQVNKPPYPALGGNMKKIENCNYAVELGKN 392
Cdd:cd21298    1 VIEETREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGANMKKIENCNYAVELGKK 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 393 EaKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVL 430
Cdd:cd21298   81 L-KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLSIL 117
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
174-298 7.85e-71

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: 222.91  E-value: 7.85e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 174 LLKDGEDLEELMKLSPEELLLRWVNYHLTNAGWRTINNFSQDIKDSKAYFHLLNQIAPKGDRDDGPAVAIDLSGFNEKND 253
Cdd:cd21327    1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNKINNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAIVIDMSGLREKDD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568960615 254 LKRAGFMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 298
Cdd:cd21327   81 LKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
177-295 6.87e-68

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: 214.45  E-value: 6.87e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 177 DGEDLEELMKLSPEELLLRWVNYHLTNAGW-RTINNFSQDIKDSKAYFHLLNQIAPKGDRDDgpavaidLSGFNEKNDLK 255
Cdd:cd21295    1 DGETLEDLLKLSPEEILLRWVNYHLERAGCdRRIKNFSGDIKDSEAYTHLLKQIAPKDAGVD-------TSALRESDLLQ 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568960615 256 RAGFMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 295
Cdd:cd21295   74 RAELMLQNADKIGCRKFVTPKDVVTGNPKLNLAFVANLFN 113
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
434-547 5.19e-65

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: 207.15  E-value: 5.19e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 434 GEGEKVTDDIIIKWVNQTLKSANKSTSISSFKDKSISTSLPVLDLIDAIAPNAVRQEMIKREHLTDEDKLNNAKYAISVA 513
Cdd:cd21333    1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNNAKYAISMA 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568960615 514 RKIGARIYALPDDLVEVKPKMVMTVFACLMGKGL 547
Cdd:cd21333   81 RKIGARVYALPEDLVEVKPKMVMTVFACLMGRGM 114
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
439-550 4.27e-60

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: 194.34  E-value: 4.27e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 439 VTDDIIIKWVNQTLKSANKSTSISSFKDKSISTSLPVLDLIDAIAPNAVRQEMIKREHLTDEDKLNNAKYAISVARKIGA 518
Cdd:cd21334    1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568960615 519 RIYALPDDLVEVKPKMVMTVFACLMGKGLNRL 550
Cdd:cd21334   81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
439-546 8.06e-59

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: 190.57  E-value: 8.06e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 439 VTDDIIIKWVNQTLKSANKSTSISSFKDKSISTSLPVLDLIDAIAPNAVRQEMIkREHLTDEDKLNNAKYAISVARKIGA 518
Cdd:cd21301    1 ISDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLV-LEGNSEEDKLSNAKYAISMARKIGA 79
                         90       100
                 ....*....|....*....|....*...
gi 568960615 519 RIYALPDDLVEVKPKMVMTVFACLMGKG 546
Cdd:cd21301   80 RVYALPEDIVEVKPKMVMTVFACLMALD 107
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
44-156 7.40e-52

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: 172.76  E-value: 7.40e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  44 EEKVAFVNWINKALENDADCSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINKKK-LTPFTVSENLNLALN 122
Cdd:cd21217    1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKpKNIFEATENLNLALN 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568960615 123 SASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIK 156
Cdd:cd21217   81 AAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
315-430 5.52e-51

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: 170.15  E-value: 5.52e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 315 GESKEERTFRNWMNSLGVNPYINHLYSDLADALVIFQLYEMIRV-PVNWSQVNKPPypaLGGNMKKIENCNYAVELGKnE 393
Cdd:cd21219    1 EGSREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPgCVNWKKVNKPK---PLNKFKKVENCNYAVDLAK-K 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568960615 394 AKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVL 430
Cdd:cd21219   77 LGFSLVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
439-543 1.34e-44

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: 153.19  E-value: 1.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 439 VTDDIIIKWVNQTLKSANKSTSISSFKDKSISTSLPVLDLIDAIAPNAVRQEMIKrEHLTDEDKLNNAKYAISVARKIGA 518
Cdd:cd21220    1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLVT-EGETDEEKEQNAKYAISLARKIGA 79
                         90       100
                 ....*....|....*....|....*
gi 568960615 519 RIYALPDDLVEVKPKMVMTVFACLM 543
Cdd:cd21220   80 VIFLLWEDIVEVKPKMILTFVASLM 104
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
45-157 4.77e-42

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: 146.52  E-value: 4.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKALENDADCSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDERAIN-KKKLTPFTVSENLNLALNS 123
Cdd:cd21293    2 EKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINtKKVLNPWERNENHTLCLNS 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568960615 124 ASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKV 157
Cdd:cd21293   82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKI 115
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
39-158 7.86e-42

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 146.44  E-value: 7.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  39 HSYSEEEKVAFVNWINKALENDADCSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINK-----KKLTPFTV 113
Cdd:cd21294    1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKpprknKPLNNFQM 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568960615 114 SENLNLALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKVG 158
Cdd:cd21294   81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRRG 125
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
313-430 1.86e-41

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


Pssm-ID: 409149  Cd Length: 119  Bit Score: 145.26  E-value: 1.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 313 LEGEsKEERTFRNWMNSLGVNPYINHLYSDLADALVIFQLYEMIrVP--VNWSQVNKPPYPALGGNMKKIENCNYAVELG 390
Cdd:cd21300    3 AEGE-REARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKV-IPgsVNWKKVNKAPASAEISRFKAVENTNYAVELG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568960615 391 KNEaKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVL 430
Cdd:cd21300   81 KQL-GFSLVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
179-295 4.48e-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: 143.98  E-value: 4.48e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 179 EDLEELMKLSPEELLLRWVNYHLTNAGWR--TINNFSQDIKDSKAYFHLLNQIAPKGDRDDgpavaIDLSGFNEKNDLKR 256
Cdd:cd21218    1 ETLESLLYLPPEEILLRWVNYHLKKAGPTkkRVTNFSSDLKDGEVYALLLHSLAPELCDKE-----LVLEVLSEEDLEKR 75
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568960615 257 AGFMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 295
Cdd:cd21218   76 AEKVLQAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
179-295 3.99e-37

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


Pssm-ID: 409146  Cd Length: 109  Bit Score: 133.07  E-value: 3.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 179 EDLEELMKLSPEELLLRWVNYHLTNAGW-RTINNFSQDIKDSKAYFHLLNQIAPkGDRDDGPAVAIDLsgfnekndLKRA 257
Cdd:cd21297    1 ETLEQFLRLPPEQILLRWFNYHLKAANWpRRVSNFSKDVSDGENYTVLLNQLAP-ELCSRAPLQTTDL--------LQRA 71
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 258 GFMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 295
Cdd:cd21297   72 EQVLQNAEKLDCRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
179-294 7.18e-34

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: 124.17  E-value: 7.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 179 EDLEELMKLSPEELLLRWVNYHLTNAGW-RTINNFSQDIKDSKAYFHLLNQIAPKgdrddgpavAIDLSGFNEKNDLKRA 257
Cdd:cd21296    1 EDVEELLRLPPEKVLLKWMNFHLKKAGYkKTVTNFSSDVKDAEAYAYLLNVLAPE---------HCDPATLEAKDPLERA 71
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568960615 258 GFMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLF 294
Cdd:cd21296   72 KLVLEQAEKMNCKRYLTAKDIVEGSANLNLAFVAQIF 108
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
315-431 1.38e-33

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: 123.38  E-value: 1.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 315 GESKEERTFRNWMNSLGVNPYINHLYSDLADALVIFQ-LYEMIRVPVNWSQVNKPPypaLGGNMKKIENCNYAVELGKnE 393
Cdd:cd21299    1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEvLDKVSPGSVNWKHANKPP---IKMPFKKVENCNQVVKIGK-Q 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 394 AKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVLS 431
Cdd:cd21299   77 LKFSLVNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
436-543 6.12e-30

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: 113.29  E-value: 6.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 436 GEKVTDDIIIKWVNQTLKSANKSTSISSFKDKSISTSLPVLDLIDAIAPNAVRQEMIKREHlTDEDKLNNAKYAISVARK 515
Cdd:cd21303    1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLVTPGN-TEDEAYLNAKLAISIARK 79
                         90       100
                 ....*....|....*....|....*...
gi 568960615 516 IGARIYALPDDLVEVKPKMVMTVFACLM 543
Cdd:cd21303   80 LGALIFLVPEDIVEVRPRLVLTFIGSLM 107
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
439-543 2.78e-25

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: 100.32  E-value: 2.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 439 VTDDIIIKWVNQTLKSANKSTSISSFKDKSISTSLPVLDLIDAIAPNAVRQEMIKREHlTDEDKLNNAKYAISVARKIGA 518
Cdd:cd21302    2 MTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGE-TDEEKRLNATYIISVARKLGC 80
                         90       100
                 ....*....|....*....|....*
gi 568960615 519 RIYALPDDLVEVKPKMVMTVFACLM 543
Cdd:cd21302   81 SIFLLPEDIVEVNQKMILILTASIM 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
43-158 3.34e-22

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 91.58  E-value: 3.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615   43 EEEKVAFVNWINKALENDADcshllpmNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINKKkltPFTVSENLNLALN 122
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGP-------GVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568960615  123 SAS-AIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKVG 158
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
187-298 1.81e-20

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: 86.57  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  187 LSPEELLLRWVNYHLTNAGWRT-INNFSQDIKDSKAYFHLLNQIAPKgdrddgpAVAIDLSGFNEKNDLKRAGFMLQEA- 264
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVrVTNFTTDLRDGLALCALLNKLAPG-------LVDKKKLNKSEFDKLENINLALDVAe 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568960615  265 DKLGCRQF-VTPADVVSGNPKLNLAFVANLFNTYP 298
Cdd:pfam00307  74 KKLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
48-155 5.89e-19

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 81.98  E-value: 5.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615    48 AFVNWINKALENDAdcshllpmNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINKKKlTPFTVSENLNLALNSASAI 127
Cdd:smart00033   2 TLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEKL 72
                           90       100
                   ....*....|....*....|....*...
gi 568960615   128 GCTVVNIGAQDLKEGkPHLVLGLLWQII 155
Cdd:smart00033  73 GGKVVLFEPEDLVEG-PKLILGVIWTLI 99
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
319-425 2.64e-17

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 77.71  E-value: 2.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  319 EERTFRNWMNSL----GVNPYINHLYSDLADALVIFQLYEMIRvP--VNWSQVNKPPypalggnMKKIENCNYAVELGKN 392
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 568960615  393 EAKFSLVGIAGQDLNEGNATLTLALVWQLMRRY 425
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
438-546 5.48e-17

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 76.56  E-value: 5.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  438 KVTDDIIIKWVNQTLKSANKSTSISSFKdKSISTSLPVLDLIDAIAPNAVRQEMIKREHltdEDKLNNAKYAISVAR-KI 516
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKLNKSE---FDKLENINLALDVAEkKL 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 568960615  517 GARIYAL-PDDLVEVKPKMVMTVFACLMGKG 546
Cdd:pfam00307  77 GVPKVLIePEDLVEGDNKSVLTYLASLFRRF 107
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
48-156 1.14e-15

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 72.76  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  48 AFVNWINKALENDadcshllpMNPNDGSLFKSLADGILLCKMINLSEPDTIDEraINKKKLTPFTVSENLNLALNSASAI 127
Cdd:cd00014    3 ELLKWINEVLGEE--------LPVSITDLFESLRDGVLLCKLINKLSPGSIPK--INKKPKSPFKKRENINLFLNACKKL 72
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568960615 128 G-CTVVNIGAQDLKEGK-PHLVLGLLWQIIK 156
Cdd:cd00014   73 GlPELDLFEPEDLYEKGnLKKVLGTLWALAL 103
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
191-294 2.18e-15

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 71.96  E-value: 2.18e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615   191 ELLLRWVNYHLTNAGWRTINNFSQDIKDSKAYFHLLNQIAPKGDRDDGPAvaidlSGFNEKNDLKRAGFMLQEADKLGC- 269
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVA-----ASLSRFKKIENINLALSFAEKLGGk 75
                           90       100
                   ....*....|....*....|....*
gi 568960615   270 RQFVTPADVVSGnPKLNLAFVANLF 294
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLI 99
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
321-424 1.25e-14

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 69.65  E-value: 1.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615   321 RTFRNWMNSLGVN---PYINHLYSDLADALVIFQLYEMIRVP-VNWSQVNKPPYPalggnMKKIENCNYAVELGKnEAKF 396
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAE-KLGG 74
                           90       100
                   ....*....|....*....|....*...
gi 568960615   397 SLVGIAGQDLNEGNaTLTLALVWQLMRR 424
Cdd:smart00033  75 KVVLFEPEDLVEGP-KLILGVIWTLISL 101
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
42-156 3.46e-14

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 68.85  E-value: 3.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  42 SEEEKvAFVNWINKalendadcshlLPMNPNDGSLFKSLADGILLCKMINLSEPDTID-ERAINKKKLTPFTVSENLNLA 120
Cdd:cd21219    3 SREER-AFRMWLNS-----------LGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNwKKVNKPKPLNKFKKVENCNYA 70
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568960615 121 LNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIK 156
Cdd:cd21219   71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMR 106
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
49-155 7.48e-11

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: 59.22  E-value: 7.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  49 FVNWINKalendadcsHLLPMNPNDGSLFKSLADGILLCKMInlsepDTIDER---AINKKKLTPFTVSENLNLALNSAS 125
Cdd:cd21227    9 FTNWVNE---------QLKPTGMSVEDLATDLEDGVKLIALV-----EILQGRklgRVIKKPLNQHQKLENVTLALKAMA 74
                         90       100       110
                 ....*....|....*....|....*....|
gi 568960615 126 AIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21227   75 EDGIKLVNIGNEDIVNGNLKLILGLIWHLI 104
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
442-543 1.19e-10

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: 58.48  E-value: 1.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615   442 DIIIKWVNQTLKSANKSTsISSFkDKSISTSLPVLDLIDAIAPNAVRQEMIKREhLTDEDKLNNAKYAISVARKIG-ARI 520
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPP-VTNF-SSDLKDGVALCALLNSLSPGLVDKKKVAAS-LSRFKKIENINLALSFAEKLGgKVV 77
                           90       100
                   ....*....|....*....|...
gi 568960615   521 YALPDDLVEvKPKMVMTVFACLM 543
Cdd:smart00033  78 LFEPEDLVE-GPKLILGVIWTLI 99
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
42-156 1.71e-10

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: 58.40  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  42 SEEEKVaFVNWINKalendadcshlLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINK---KKLTPFTVSENLN 118
Cdd:cd21298    5 TREEKT-YRNWMNS-----------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKpfkKLGANMKKIENCN 72
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 119 LALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIK 156
Cdd:cd21298   73 YAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMR 110
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
314-424 3.88e-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: 58.11  E-value: 3.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMIrvpvNWSQVNKPPYpalgGNMK--KIENCNYAVEL 389
Cdd:cd21318   34 EREAVQKKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLEVL----SGEQLPKPTR----GRMRihSLENVDKALQF 105
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568960615 390 GKnEAKFSLVGIAGQDLNEGNATLTLALVWQLMRR 424
Cdd:cd21318  106 LK-EQRVHLENVGSHDIVDGNHRLTLGLIWTIILR 139
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
43-156 7.16e-10

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: 56.66  E-value: 7.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  43 EEEKVAFVNWINKalendadcshlLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINKKK----LTPFTVSENLN 118
Cdd:cd21300    6 EREARVFTLWLNS-----------LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaeISRFKAVENTN 74
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 119 LALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIK 156
Cdd:cd21300   75 YAVELGKQLGFSLVGIQGADITDGSRTLTLALVWQLMR 112
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
314-424 8.84e-10

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


Pssm-ID: 409042  Cd Length: 116  Bit Score: 56.54  E-value: 8.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNSL--GVNPYINHLYSDLADALVIFQLYEMIrvpvnwsQVNKPPYPALGG-NMKKIENCNYAVELG 390
Cdd:cd21193   12 ERINIQKKTFTKWINSFleKANLEIGDLFTDLSDGKLLLKLLEII-------SGEKLGKPNRGRlRVQKIENVNKALAFL 84
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568960615 391 KneAKFSLVGIAGQDLNEGNATLTLALVWQLMRR 424
Cdd:cd21193   85 K--TKVRLENIGAEDIVDGNPRLILGLIWTIILR 116
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
43-164 9.36e-10

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: 56.23  E-value: 9.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  43 EEEKV---AFVNWINKALendadCSHLLPMNPNDgsLFKSLADGILLCKMIN-LSEPDTIDERAINKKKltPFTVSeNLN 118
Cdd:cd21241    1 EQERVqkkTFTNWINSYL-----AKRKPPMKVED--LFEDIKDGTKLLALLEvLSGEKLPCEKGRRLKR--VHFLS-NIN 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568960615 119 LALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIkvgLFADIE 164
Cdd:cd21241   71 TALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTII---LYFQIE 113
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
45-156 1.20e-09

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


Pssm-ID: 409064  Cd Length: 107  Bit Score: 55.87  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKALEndadcSHLLPMNpndgSLFKSLADGILLCKMINLSEPDTIDERAINKK----KLtpftvsENLNLA 120
Cdd:cd21215    5 QKKTFTKWLNTKLS-----SRGLSIT----DLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKmrvqKL------ENVNKA 69
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568960615 121 LNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIK 156
Cdd:cd21215   70 LEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLIL 105
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
45-155 1.69e-09

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


Pssm-ID: 409042  Cd Length: 116  Bit Score: 55.77  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINkalendadcSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDEraINKKKLTPFTVsENLNLALNSA 124
Cdd:cd21193   17 QKKTFTKWIN---------SFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGK--PNRGRLRVQKI-ENVNKALAFL 84
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568960615 125 SAiGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21193   85 KT-KVRLENIGAEDIVDGNPRLILGLIWTII 114
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
45-155 2.32e-09

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: 55.22  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKALENdadcsHLLPMNPNDgsLFKSLADGILLCKMIN-LSEPDTIDERAINkkkltPFTVSENLNLALNS 123
Cdd:cd21242    6 QKRTFTNWINSQLAK-----HSPPSVVSD--LFTDIQDGHRLLDLLEvLSGQQLPREKGHN-----VFQCRSNIETALSF 73
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568960615 124 ASAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21242   74 LKNKSIKLINIHVPDIIEGKPSIILGLIWTII 105
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
441-536 2.62e-09

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 55.00  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 441 DDIIIKWVNQTLKSAN-KSTSISSFkDKSISTSLPVLDLIDAIAPNAVRQEMIKrEHLTDEDKLNNAKYAISVARKIGAR 519
Cdd:cd21218   12 EEILLRWVNYHLKKAGpTKKRVTNF-SSDLKDGEVYALLLHSLAPELCDKELVL-EVLSEEDLEKRAEKVLQAAEKLGCK 89
                         90
                 ....*....|....*..
gi 568960615 520 IYALPDDLVEVKPKMVM 536
Cdd:cd21218   90 YFLTPEDIVSGNPRLNL 106
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
319-425 2.89e-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: 54.71  E-value: 2.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 319 EERTFRNWMNS-LGVNPY-INHLYSDLADALVIFQLYEMIrvpvnwSQVNKPPY---PALggNMKKIENCNYAVELGKNE 393
Cdd:cd21215    5 QKKTFTKWLNTkLSSRGLsITDLVTDLSDGVRLIQLLEII------GDESLGRYnknPKM--RVQKLENVNKALEFIKSR 76
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568960615 394 aKFSLVGIAGQDLNEGNATLTLALVWQLMRRY 425
Cdd:cd21215   77 -GVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
314-424 9.84e-09

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: 53.90  E-value: 9.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNS-LG-VNPYINHLYSDLADALVIFQLYEMIrvpvNWSQVNKPPypalGGNMKK--IENCNYAVEL 389
Cdd:cd21317   27 EREAVQKKTFTKWVNShLArVTCRIGDLYTDLRDGRMLIRLLEVL----SGEQLPKPT----KGRMRIhcLENVDKALQF 98
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568960615 390 GKnEAKFSLVGIAGQDLNEGNATLTLALVWQLMRR 424
Cdd:cd21317   99 LK-EQKVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
314-424 7.62e-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: 50.83  E-value: 7.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMI---RVPvnwsqvnKPPYpalgGNMK--KIENCNYA 386
Cdd:cd21246   12 EREAVQKKTFTKWVNShlARVGCRINDLYTDLRDGRMLIKLLEVLsgeRLP-------KPTK----GKMRihCLENVDKA 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 387 VELGKNEaKFSLVGIAGQDLNEGNATLTLALVWQLMRR 424
Cdd:cd21246   81 LQFLKEQ-RVHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
188-283 1.39e-07

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: 49.54  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 188 SPEELLLRWVNYHLTNagwRTINNFSQDIKDSKAYFHLLNQIAPkGDRDDGpavaidlSGFNEKNDLKRAGFMLQEA-DK 266
Cdd:cd21184    1 SGKSLLLEWVNSKIPE---YKVKNFTTDWNDGKALAALVDALKP-GLIPDN-------ESLDKENPLENATKAMDIAeEE 69
                         90
                 ....*....|....*..
gi 568960615 267 LGCRQFVTPADVVSGNP 283
Cdd:cd21184   70 LGIPKIITPEDMVSPNV 86
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
45-155 2.56e-07

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


Pssm-ID: 409037  Cd Length: 105  Bit Score: 48.94  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKalendadcsHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTID-ERAINKkkltpFTVSENLNLALNS 123
Cdd:cd21188    4 QKKTFTKWVNK---------HLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPrERGRMR-----FHRLQNVQTALDF 69
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568960615 124 ASAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21188   70 LKYRKIKLVNIRAEDIVDGNPKLTLGLIWTII 101
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
177-286 2.90e-07

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


Pssm-ID: 409164  Cd Length: 118  Bit Score: 49.39  E-value: 2.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 177 DGEDLEELMKLSPEELLLRWVNYHLTNagwRTINNFSQDIKDSKAYFHLLNQIApkgdrddgPAVAIDLSGFNEKNDLKR 256
Cdd:cd21315    5 EDDGPDDGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALA--------PGLCPDWEDWDPKDAVKN 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568960615 257 AGFMLQEADK-LGCRQFVTPADVVsgNPKLN 286
Cdd:cd21315   74 AKEAMDLAEDwLDVPQLIKPEEMV--NPKVD 102
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
49-155 3.10e-07

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 49.02  E-value: 3.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  49 FVNWINKalendadcsHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIdERAINKKKLTPFTVSENLNLALNSASAIG 128
Cdd:cd21183    9 FTRWCNE---------HLKERGMQIHDLATDFSDGLCLIALLENLSTRPL-KRSYNRRPAFQQHYLENVSTALKFIEADH 78
                         90       100
                 ....*....|....*....|....*..
gi 568960615 129 CTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21183   79 IKLVNIGSGDIVNGNIKLILGLIWTLI 105
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
41-155 3.44e-07

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: 49.21  E-value: 3.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  41 YSEEEKV---AFVNWINKalendadcsHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDErainKKKLTPFTVSENL 117
Cdd:cd21236   11 KDERDKVqkkTFTKWINQ---------HLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHRLQNV 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 118 NLALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21236   78 QIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTII 115
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
314-427 3.51e-07

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: 49.21  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMIrvpvnwsqvNKPPYPALGGNMK--KIENCNYAVE- 388
Cdd:cd21236   13 ERDKVQKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVL---------SGDTLPREKGRMRfhRLQNVQIALDy 83
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568960615 389 LGKNEAKfsLVGIAGQDLNEGNATLTLALVWQLMRRYTL 427
Cdd:cd21236   84 LKRRQVK--LVNIRNDDITDGNPKLTLGLIWTIILHFQI 120
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
45-155 4.41e-07

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


Pssm-ID: 409039  Cd Length: 113  Bit Score: 48.72  E-value: 4.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKALENdadcsHLLPMNPNDgsLFKSLADGIllcKMINLSEPDTIDERAINK-KKLTPFTVSENLNLALNS 123
Cdd:cd21190    6 QKKTFTNWINSHLAK-----LSQPIVIND--LFVDIKDGT---ALLRLLEVLSGQKLPIESgRVLQRAHKLSNIRNALDF 75
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568960615 124 ASAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21190   76 LTKRCIKLVNINSTDIVDGKPSIVLGLIWTII 107
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
42-156 7.51e-07

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: 48.06  E-value: 7.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  42 SEEEKvAFVNWINKalendadcshlLPMNPNDGSLFKSLADGILLCKMINLSEPdTIDERAINKKkltPFTV-------S 114
Cdd:cd21329    5 SSEER-TFRNWMNS-----------LGVNPYVNHLYSDLCDALVIFQLYEMTRV-PVDWGHVNKP---PYPAlggnmkkI 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568960615 115 ENLNLALN-SASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIK 156
Cdd:cd21329   69 ENCNYAVElGKNKAKFSLVGIAGSDLNEGNKTLTLALIWQLMR 111
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
42-156 9.90e-07

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


Pssm-ID: 409148  Cd Length: 114  Bit Score: 47.50  E-value: 9.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  42 SEEEKvAFVNWINkALENDADCSHLlpmnpndgslFKSLADGILLCKMINLSEPDTIDERAINKKKLT-PFTVSENLNLA 120
Cdd:cd21299    3 SREER-CFRLWIN-SLGIDTYVNNV----------FEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKmPFKKVENCNQV 70
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568960615 121 LNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIK 156
Cdd:cd21299   71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMR 106
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
319-428 1.49e-06

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: 46.99  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 319 EERTFRNWMNSLGVN---PYINHLYSDLADALVIFQLYEMIrvpvnwSQVNKPPYPalgGNMK--KIENCNYAVE-LGKN 392
Cdd:cd21186    3 QKKTFTKWINSQLSKankPPIKDLFEDLRDGTRLLALLEVL------TGKKLKPEK---GRMRvhHLNNVNRALQvLEQN 73
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568960615 393 EAKfsLVGIAGQDLNEGNATLTLALVWQLMRRYTLK 428
Cdd:cd21186   74 NVK--LVNISSNDIVDGNPKLTLGLVWSIILHWQVK 107
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
316-422 1.69e-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: 46.61  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 316 ESKEERTFRNWMNSL--GVNPYINHLYSDLADALVIFQLYEMIRvpvnwsqvNKPPYPALGGNMK--KIENCNYAveLGK 391
Cdd:cd21214    3 EKQQRKTFTAWCNSHlrKAGTQIENIEEDFRDGLKLMLLLEVIS--------GERLPKPERGKMRfhKIANVNKA--LDF 72
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568960615 392 NEAK-FSLVGIAGQDLNEGNATLTLALVWQLM 422
Cdd:cd21214   73 IASKgVKLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
319-425 1.81e-06

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


Pssm-ID: 409077  Cd Length: 108  Bit Score: 46.71  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 319 EERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMIRVPVNWSQVNKPPypalGGNMKKIENCNYAVELGKNEaKF 396
Cdd:cd21228    5 QQNTFTRWCNEhlKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRP----TFRQMKLENVSVALEFLERE-SI 79
                         90       100
                 ....*....|....*....|....*....
gi 568960615 397 SLVGIAGQDLNEGNATLTLALVWQLMRRY 425
Cdd:cd21228   80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
316-425 1.84e-06

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: 46.76  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 316 ESKEERTFRNWMNSL----GVNPyINHLYSDLADALVIFQLYEMIRVPVNWSQVNKPPypalGGNMKKIENCNYAVELGK 391
Cdd:cd21225    2 EKVQIKAFTAWVNSVlekrGIPK-ISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEP----KNRIQMIQNLHLAMLFIE 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568960615 392 NEAKFSLVGIAGQDLNEGNATLTLALVWQLMRRY 425
Cdd:cd21225   77 EDLKIRVQGIGAEDFVDNNKKLILGLLWTLYRKY 110
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
319-425 2.32e-06

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


Pssm-ID: 409076  Cd Length: 109  Bit Score: 46.51  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 319 EERTFRNWMN-SLGVNPY-INHLYSDLADALVIFQLYEMIRVPVNWSQVNKPPYPAlggnmKKIENCNYAVELGKNEAkF 396
Cdd:cd21227    5 QKNTFTNWVNeQLKPTGMsVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQH-----QKLENVTLALKAMAEDG-I 78
                         90       100
                 ....*....|....*....|....*....
gi 568960615 397 SLVGIAGQDLNEGNATLTLALVWQLMRRY 425
Cdd:cd21227   79 KLVNIGNEDIVNGNLKLILGLIWHLILRY 107
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
179-298 3.45e-06

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


Pssm-ID: 409163  Cd Length: 115  Bit Score: 46.22  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 179 EDLEELMKLSPEELLLRWVNYHLTNAgwrTINNFSQDIKDSKAYFHLLNQIApkgdrddgPAVAIDLSGFNEKNDLKRAG 258
Cdd:cd21314    2 EDEEDARKQTPKQRLLGWIQNKVPQL---PITNFNRDWQDGKALGALVDNCA--------PGLCPDWESWDPNQPVQNAR 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568960615 259 FMLQEADK-LGCRQFVTPADVVsgNPKLNLAFVANLFNTYP 298
Cdd:cd21314   71 EAMQQADDwLGVPQVIAPEEIV--DPNVDEHSVMTYLSQFP 109
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
45-166 5.04e-06

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: 45.79  E-value: 5.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKalendadcsHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDErainKKKLTPFTVSENLNLALNSA 124
Cdd:cd21235    7 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568960615 125 SAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKVGLFADIEIS 166
Cdd:cd21235   74 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 115
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
314-437 5.44e-06

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: 45.79  E-value: 5.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMIrvpvnwsqvNKPPYPALGGNMK--KIENCNYAVEL 389
Cdd:cd21235    2 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568960615 390 GKNEaKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVLSDLGEGE 437
Cdd:cd21235   73 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
319-425 5.50e-06

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 45.16  E-value: 5.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 319 EERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMIRV-PVNWSQVNKPPYPAlggnmKKIENCNYAVELGKNEaK 395
Cdd:cd21183    5 QANTFTRWCNEhlKERGMQIHDLATDFSDGLCLIALLENLSTrPLKRSYNRRPAFQQ-----HYLENVSTALKFIEAD-H 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 568960615 396 FSLVGIAGQDLNEGNATLTLALVWQLMRRY 425
Cdd:cd21183   79 IKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
314-435 5.61e-06

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: 45.79  E-value: 5.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMIrvpvnwsqvNKPPYPALGGNMK--KIENCNYAVEL 389
Cdd:cd21237    2 ERDRVQKKTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLEVL---------SGVKLPREKGRMRfhRLQNVQIALDF 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568960615 390 GKnEAKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVLSDLGE 435
Cdd:cd21237   73 LK-QRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGE 117
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
177-298 8.42e-06

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


Pssm-ID: 409161  Cd Length: 114  Bit Score: 45.18  E-value: 8.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 177 DGEDLEELMKLSPEELLLRWVNYHLTNAgwrTINNFSQDIKDSKAYFHLLNQIApkgdrddgPAVAIDLSGFNEKNDLKR 256
Cdd:cd21312    1 DEEEDEEAKKQTPKQRLLGWIQNKLPQL---PITNFSRDWQSGRALGALVDSCA--------PGLCPDWDSWDASKPVTN 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568960615 257 AGFMLQEADK-LGCRQFVTPADVVsgNPKLNLAFVANLFNTYP 298
Cdd:cd21312   70 AREAMQQADDwLGIPQVITPEEIV--DPNVDEHSVMTYLSQFP 110
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
319-425 8.49e-06

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) 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. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 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: 409096  Cd Length: 125  Bit Score: 45.13  E-value: 8.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 319 EERTFRNWMNSL----GVNPYINHLYSDLADALVIFQLYEMIrvpvnwsQVNKPPYPALGG-NMKKIENCNYAVELGKNE 393
Cdd:cd21247   21 QKKTFTKWMNNVfsknGAKIEITDIYTELKDGIHLLRLLELI-------SGEQLPRPSRGKmRVHFLENNSKAITFLKTK 93
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568960615 394 AKFSLVGiaGQDLNEGNATLTLALVWQLMRRY 425
Cdd:cd21247   94 VPVKLIG--PENIVDGDRTLILGLIWIIILRF 123
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
314-424 1.24e-05

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


Pssm-ID: 409165  Cd Length: 154  Bit Score: 45.42  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMIrvpvnwsQVNKPPYPALGG-NMKKIENCNYAVELG 390
Cdd:cd21316   49 EREAVQKKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLEVL-------SGERLPKPTKGRmRIHCLENVDKALQFL 121
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568960615 391 KnEAKFSLVGIAGQDLNEGNATLTLALVWQLMRR 424
Cdd:cd21316  122 K-EQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
190-294 1.33e-05

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


Pssm-ID: 409069  Cd Length: 105  Bit Score: 44.18  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 190 EELLLRWVNYHLTNAGWRT-INNFS-QDIKDSKAYFHLLNQIAPKGDRDDgpavaIDLSGFNEKNDLKRAGFMLQEADKL 267
Cdd:cd21220    3 DADILAWANSKVREAGKSSpISSFKdPSLSTGLFLLDLLAAIDPGAVDYD-----LVTEGETDEEKEQNAKYAISLARKI 77
                         90       100
                 ....*....|....*....|....*..
gi 568960615 268 GCRQFVTPADVVSGNPKLNLAFVANLF 294
Cdd:cd21220   78 GAVIFLLWEDIVEVKPKMILTFVASLM 104
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
45-156 1.51e-05

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: 44.61  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKalendadcshlLPMNPNDGSLFKSLADGILLCKMIN-LSEPdtIDERAINKKKLTPFTVS----ENLNL 119
Cdd:cd21331   23 EERTFRNWMNS-----------LGVNPHVNHLYGDLQDALVILQLYEkIKVP--VDWNKVNKPPYPKLGANmkklENCNY 89
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 120 ALN-SASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIK 156
Cdd:cd21331   90 AVElGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMR 127
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
319-427 1.51e-05

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


Pssm-ID: 409160  Cd Length: 124  Bit Score: 44.36  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 319 EERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMI---RVPvnwsQVNKPPypalggNMK--KIENCNYAVELGK 391
Cdd:cd21311   16 QQNTFTRWANEhlKTANKHIADLETDLSDGLRLIALVEVLsgkKFP----KFNKRP------TFRsqKLENVSVALKFLE 85
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568960615 392 NEAKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTL 427
Cdd:cd21311   86 EDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
319-419 1.55e-05

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


Pssm-ID: 409037  Cd Length: 105  Bit Score: 43.93  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 319 EERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMIrvpvnwSQVNkppYPALGGNMK--KIENCNYAVELGKNEa 394
Cdd:cd21188    4 QKKTFTKWVNKhlIKARRRVVDLFEDLRDGHNLISLLEVL------SGES---LPRERGRMRfhRLQNVQTALDFLKYR- 73
                         90       100
                 ....*....|....*....|....*
gi 568960615 395 KFSLVGIAGQDLNEGNATLTLALVW 419
Cdd:cd21188   74 KIKLVNIRAEDIVDGNPKLTLGLIW 98
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
190-293 2.03e-05

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: 43.83  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 190 EELLLRWVNYHLTNAG-WRTINNFSQ-DIKDSKAYFHLLNQIAPKGDRDDgpavAIDLSGFNEKNDLKRAGFMLQEADKL 267
Cdd:cd21333    8 DETIVNWVNETLTEAGkSSSISSFKDgKISTSMPVLDLIDAIQPGSINYD----LLKTEDLNDEEKLNNAKYAISMARKI 83
                         90       100
                 ....*....|....*....|....*.
gi 568960615 268 GCRQFVTPADVVSGNPKLNLAFVANL 293
Cdd:cd21333   84 GARVYALPEDLVEVKPKMVMTVFACL 109
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
317-423 2.09e-05

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 44.65  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 317 SKEER-TFRNWMNS-----------LGVNPYINHLYSDLADALVIFQLyemirvpVNWSQVNKPPYPALggNMKKI---- 380
Cdd:cd21323   22 SEEEKvAFVNWINKalegdpdckhvVPMNPTDESLFKSLADGILLCKM-------INLSQPDTIDERAI--NKKKLtpft 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568960615 381 --ENCNYAVelgkNEAKF---SLVGIAGQDLNEGNATLTLALVWQLMR 423
Cdd:cd21323   93 isENLNLAL----NSASAigcTVVNIGSLDLKEGKPHLVLGLLWQIIK 136
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
42-155 2.19e-05

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: 43.89  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  42 SEEEKV---AFVNWINkalendadcSHLLPMNPNDGSLFKSLADGILLCKMIN-LSepdtiDER--AINKKKLTPFTVsE 115
Cdd:cd21246   11 DEREAVqkkTFTKWVN---------SHLARVGCRINDLYTDLRDGRMLIKLLEvLS-----GERlpKPTKGKMRIHCL-E 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568960615 116 NLNLALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21246   76 NVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTII 115
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
319-429 2.27e-05

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


Pssm-ID: 409158  Cd Length: 131  Bit Score: 44.30  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 319 EERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMIRVPVNWSQVNKPPypalGGNMKKIENCNYAVELGKNEAkF 396
Cdd:cd21309   18 QQNTFTRWCNEhlKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRP----TFRQMQLENVSVALEFLDRES-I 92
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568960615 397 SLVGIAGQDLNEGNATLTLALVWQLMRRYTLKV 429
Cdd:cd21309   93 KLVSIDSKAIVDGNLKLILGLVWTLILHYSISM 125
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
193-293 2.51e-05

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: 43.42  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 193 LLRWVNYHLTNAGWRT-INNFS-QDIKDSKAYFHLLNQIAPKG-DRDdgpavaIDLSGFNEKNDLKRAGFMLQEADKLGC 269
Cdd:cd21301    6 IVEWANEKLKSAGKSTsISSFKdPSISTSLPILDLIDAIKPGSvDYS------LVLEGNSEEDKLSNAKYAISMARKIGA 79
                         90       100
                 ....*....|....*....|....
gi 568960615 270 RQFVTPADVVSGNPKLNLAFVANL 293
Cdd:cd21301   80 RVYALPEDIVEVKPKMVMTVFACL 103
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
45-155 2.74e-05

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: 44.25  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINkalendadcSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINKKKLTPFtvsENLNLALNSA 124
Cdd:cd21318   39 QKKTFTKWVN---------SHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRMRIHSL---ENVDKALQFL 106
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568960615 125 SAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21318  107 KEQRVHLENVGSHDIVDGNHRLTLGLIWTII 137
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
378-423 2.74e-05

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: 43.33  E-value: 2.74e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568960615 378 KKIENCNYAVElGKNEAKFSLVGIAGQDLNEGNATLTLALVWQLMR 423
Cdd:cd21217   70 EATENLNLALN-AAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
180-293 2.82e-05

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: 43.40  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 180 DLEELMKLSpEELLLRWVNYHLTNAGWRT-INNFS-QDIKDSKAYFHLLNQIAPKGDRDDgpavAIDLSGFNEKNDLKRA 257
Cdd:cd21332    1 DLGEGEKVN-DEIIIKWVNQTLANANKTTsITSFKdKSISTSLPVLDLIDAIAPNAIREE----MVKREDLSDADKLNNA 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568960615 258 GFMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANL 293
Cdd:cd21332   76 KYAISVARKIGARVYALPEDLVEVKPKMVMTVFACL 111
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
319-429 3.08e-05

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


Pssm-ID: 409157  Cd Length: 129  Bit Score: 43.92  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 319 EERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMIRVPVNWSQVNKPPypalGGNMKKIENCNYAVELGKNEAkF 396
Cdd:cd21308   21 QQNTFTRWCNEhlKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRP----TFRQMQLENVSVALEFLDRES-I 95
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568960615 397 SLVGIAGQDLNEGNATLTLALVWQLMRRYTLKV 429
Cdd:cd21308   96 KLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 128
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
182-298 3.69e-05

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


Pssm-ID: 409162  Cd Length: 110  Bit Score: 43.16  E-value: 3.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 182 EELMKLSPEELLLRWVNYHLTnagWRTINNFSQDIKDSKAYFHLLNQIApkgdrddgPAVAIDLSGFNEKNDLKRAGFML 261
Cdd:cd21313    2 DDAKKQTPKQRLLGWIQNKIP---YLPITNFNQNWQDGKALGALVDSCA--------PGLCPDWESWDPQKPVDNAREAM 70
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 262 QEADK-LGCRQFVTPADVVsgNPKLNLAFVANLFNTYP 298
Cdd:cd21313   71 QQADDwLGVPQVITPEEII--HPDVDEHSVMTYLSQFP 106
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
319-429 3.92e-05

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


Pssm-ID: 409159  Cd Length: 125  Bit Score: 43.48  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 319 EERTFRNWMNS--LGVNPYINHLYSDLADALVIFQLYEMIrvpvNWSQVNKPPYPALGGNMKKIENCNYAVELGKNEaKF 396
Cdd:cd21310   17 QQNTFTRWCNEhlKCVQKRLNDLQKDLSDGLRLIALLEVL----SQKKMYRKYHPRPNFRQMKLENVSVALEFLDRE-HI 91
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568960615 397 SLVGIAGQDLNEGNATLTLALVWQLMRRYTLKV 429
Cdd:cd21310   92 KLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 124
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
45-166 5.51e-05

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: 42.71  E-value: 5.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKalendadcsHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDErainKKKLTPFTVSENLNLALNSA 124
Cdd:cd21237    7 QKKTFTKWVNK---------HLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPR----EKGRMRFHRLQNVQIALDFL 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568960615 125 SAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKVGLFADIEIS 166
Cdd:cd21237   74 KQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYIS 115
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
435-542 6.07e-05

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: 42.56  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 435 EGEKVTD-------DIIIKWVNQTLKSANKSTsISSFKdKSISTSLPVLDLIDAIAP-NAVRQEMIKREH--LTDEDKLN 504
Cdd:cd21326    1 EGEELEElmklspeELLLRWVNYHLTNAGWQN-ISNFS-QDIKDSRAYFHLLNQIAPkGDVFDENIEIDFsgFNEKNDLK 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568960615 505 NAKYAISVARKIGARIYALPDDLVEVKPKMVMTVFACL 542
Cdd:cd21326   79 RAEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANL 116
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
48-100 7.40e-05

calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. This family includes a group of kinesin-like proteins belonging to KIN-14 protein family. They all contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409052 [Multi-domain]  Cd Length: 112  Bit Score: 42.40  E-value: 7.40e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568960615  48 AFVNWINKALENDadcshlLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDE 100
Cdd:cd21203    4 EAAEWIQNVLGVL------VLPDPSEEEFRLCLRDGVVLCKLLNKLQPGAVPK 50
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
78-128 7.87e-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: 42.33  E-value: 7.87e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568960615  78 KSLADGILLCKMINLSEPDTIdeRAINKKKlTPFTVSENLNLALNSASAIG 128
Cdd:cd21208   24 ESLEDGILLCELINAIKPGSI--KKINRLP-TPIAGLDNLNLFLKACEDLG 71
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
44-155 9.75e-05

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


Pssm-ID: 409063  Cd Length: 105  Bit Score: 41.61  E-value: 9.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  44 EEKVAFVNWINkalendadcSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDERaiNKKKLTpFTVSENLNLALNS 123
Cdd:cd21214    5 QQRKTFTAWCN---------SHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKP--ERGKMR-FHKIANVNKALDF 72
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568960615 124 ASAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21214   73 IASKGVKLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
45-155 1.31e-04

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: 41.96  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINkalendadcSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINKKKLTPFtvsENLNLALNSA 124
Cdd:cd21317   32 QKKTFTKWVN---------SHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKGRMRIHCL---ENVDKALQFL 99
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568960615 125 SAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21317  100 KEQKVHLENMGSHDIVDGNHRLTLGLIWTII 130
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
188-284 1.47e-04

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: 41.21  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 188 SPEELLLRWVNYHLTNagwRTINNFSQDIKDSKAYFHLLNQIApkgdrddgPAVAIDLSGFNEKNDLKRAGFMLQEADK- 266
Cdd:cd21230    1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCA--------PGLCPDWETWDPNDALENATEAMQLAEDw 69
                         90
                 ....*....|....*...
gi 568960615 267 LGCRQFVTPADVVsgNPK 284
Cdd:cd21230   70 LGVPQLITPEEII--NPN 85
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
314-428 1.50e-04

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


Pssm-ID: 409091  Cd Length: 111  Bit Score: 41.35  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNS-LGVNP---YINHLYSDLADALVIFQLYEMIrvpvnwsQVNKPPYPALGGNMKKIENCNYAVEL 389
Cdd:cd21242    1 EQEQTQKRTFTNWINSqLAKHSppsVVSDLFTDIQDGHRLLDLLEVL-------SGQQLPREKGHNVFQCRSNIETALSF 73
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568960615 390 GKNEAkFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLK 428
Cdd:cd21242   74 LKNKS-IKLINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
433-542 1.51e-04

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


Pssm-ID: 409177 [Multi-domain]  Cd Length: 122  Bit Score: 41.49  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 433 LGEGEKVTD-------DIIIKWVNQTLKSA--NKSTSISSfkdkSISTSLPVLDLIDAIAPNAVRQEM----IKREHLTD 499
Cdd:cd21328    2 LRDGETLEDlmklspeELLLRWANFHLENAgwQKINNFSS----DIKDSRAYFHLLNQIAPKGQKEGEpridINMSGFNE 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568960615 500 EDKLNNAKYAISVARKIGARIYALPDDLVEVKPKMVMTVFACL 542
Cdd:cd21328   78 KDDLKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANL 120
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
310-517 1.63e-04

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 44.55  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 310 LNLLEGESKEERTFRNWMN---SLGVNPYINHLYSDLADALVIFQLYEMIRvPVNWSQVNKPPYPalggNMKKIENCNYA 386
Cdd:COG5069    1 MEAKKWQKVQKKTFTKWTNeklISGGQKEFGDLDTDLKDGVKLAQLLEALQ-KDNAGEYNETPET----RIHVMENVSGR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 387 VELGKNEAKfSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVLSDlgEGEKVTDDIIIKWVNQTLKSANKSTSISSFKD 466
Cdd:COG5069   76 LEFIKGKGV-KLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINE--EGELTKHINLLLWCDEDTGGYKPEVDTFDFFR 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568960615 467 ---------KSISTSLPvldliDAIAPNAVRQEmiKREHLTDEDK-LNNAKYAISVARKIG 517
Cdd:COG5069  153 swrdglafsALIHDSRP-----DTLDPNVLDLQ--KKNKALNNFQaFENANKVIGIARLIG 206
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
190-293 1.64e-04

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: 41.41  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 190 EELLLRWVNYHLTNAGWRT-INNFS-QDIKDSKAYFHLLNQIAPKGDRDDgpavAIDLSGFNEKNDLKRAGFMLQEADKL 267
Cdd:cd21334    3 DDIIVNWVNRTLSEAGKSTsIQNFKdKTISSSLAVVDLIDAIQPGCINYD----LVKTGNLTDDDKLDNAKYAVSMARKI 78
                         90       100
                 ....*....|....*....|....*.
gi 568960615 268 GCRQFVTPADVVSGNPKLNLAFVANL 293
Cdd:cd21334   79 GARVYALPEDLVEVKPKMVMTVFACL 104
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
314-428 1.83e-04

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: 41.06  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNSLGVN---PYINHLYSDLADALVIFQLYEMIrvpvnwsQVNKPPYPALGGNMKKIENCNYAVE-L 389
Cdd:cd21231    2 EREDVQKKTFTKWINAQFAKfgkPPIEDLFTDLQDGRRLLELLEGL-------TGQKLVKEKGSTRVHALNNVNKALQvL 74
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568960615 390 GKNEAkfSLVGIAGQDLNEGNATLTLALVWQLMRRYTLK 428
Cdd:cd21231   75 QKNNV--DLVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
45-155 2.22e-04

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: 41.03  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKALENdadCSHllPMNPNDgsLFKSLADG-ILLCKMINLSEPDTIDERAINKKKLtpFTVSeNLNLALNS 123
Cdd:cd21191    6 QKRTFTRWINLHLEK---CNP--PLEVKD--LFVDIQDGkILMALLEVLSGQNLLQEYKPSSHRI--FRLN-NIAKALKF 75
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568960615 124 ASAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21191   76 LEDSNVKLVSIDAAEIADGNPSLVLGLIWNII 107
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
319-428 2.58e-04

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: 40.76  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 319 EERTFRNWMN---SLGVNPYINHLYSDLADALVIFQLYEmirvpvnwsQVNKPPYPALGGNMK--KIENCNYAVELgKNE 393
Cdd:cd21232    3 QKKTFTKWINarfSKSGKPPIKDMFTDLRDGRKLLDLLE---------GLTGKSLPKERGSTRvhALNNVNRVLQV-LHQ 72
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568960615 394 AKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLK 428
Cdd:cd21232   73 NNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQVK 107
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
49-155 3.24e-04

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: 40.16  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  49 FVNWINKalendadcsHLLPMNPNDGSLFKSLADGILLCKMIN-LSEPDTidERAINKKKLTPFTVSENLNLALNSASAI 127
Cdd:cd21228    9 FTRWCNE---------HLKCVNKRIYNLETDLSDGLRLIALLEvLSQKRM--YKKYNKRPTFRQMKLENVSVALEFLERE 77
                         90       100
                 ....*....|....*....|....*...
gi 568960615 128 GCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21228   78 SIKLVSIDSSAIVDGNLKLILGLIWTLI 105
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
314-428 3.57e-04

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: 40.26  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNSL--GVNP--YINHLYSDLADALVIFQLYEMIRvPVNWSQVNKPpypaLGGNMKKIENCNYAVEL 389
Cdd:cd21191    1 ERENVQKRTFTRWINLHleKCNPplEVKDLFVDIQDGKILMALLEVLS-GQNLLQEYKP----SSHRIFRLNNIAKALKF 75
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568960615 390 GKnEAKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLK 428
Cdd:cd21191   76 LE-DSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 113
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
45-156 5.18e-04

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: 39.97  E-value: 5.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKalendadcshlLPMNPNDGSLFKSLADGILLCKMI-NLSEPdtIDERAINK----------KKLtpftv 113
Cdd:cd21330   14 EERTFRNWMNS-----------LGVNPRVNHLYSDLSDALVIFQLYeKIKVP--VDWNRVNKppypklgenmKKL----- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568960615 114 sENLNLALN-SASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIK 156
Cdd:cd21330   76 -ENCNYAVElGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMR 118
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
441-542 5.25e-04

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: 39.85  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 441 DDIIIKWVNQTLKSANKSTSISSF-KDKSISTSLPVLdlIDAIAPnavrqEMIKREHLTDEDKLNNAKYAISVARKIGAR 519
Cdd:cd21297   12 EQILLRWFNYHLKAANWPRRVSNFsKDVSDGENYTVL--LNQLAP-----ELCSRAPLQTTDLLQRAEQVLQNAEKLDCR 84
                         90       100
                 ....*....|....*....|...
gi 568960615 520 IYALPDDLVEVKPKMVMTVFACL 542
Cdd:cd21297   85 KFLTPTSLVAGNPKLNLAFVANL 107
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
435-542 5.73e-04

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: 39.56  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 435 EGEKVTD-------DIIIKWVNQTLKSANKSTSISSFKdKSISTSLPVLDLIDAIAPNavrQEMIKREHLTDEDKLNNAK 507
Cdd:cd21295    1 DGETLEDllklspeEILLRWVNYHLERAGCDRRIKNFS-GDIKDSEAYTHLLKQIAPK---DAGVDTSALRESDLLQRAE 76
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568960615 508 YAISVARKIGARIYALPDDLVEVKPKMVMTVFACL 542
Cdd:cd21295   77 LMLQNADKIGCRKFVTPKDVVTGNPKLNLAFVANL 111
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
45-155 1.12e-03

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


Pssm-ID: 409035  Cd Length: 107  Bit Score: 38.90  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKALeNDADCSHLlpmnpNDgsLFKSLADGILLckminLSEPDTIDERAINKKK-LTPFTVSENLNLALNS 123
Cdd:cd21186    3 QKKTFTKWINSQL-SKANKPPI-----KD--LFEDLRDGTRL-----LALLEVLTGKKLKPEKgRMRVHHLNNVNRALQV 69
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568960615 124 ASAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21186   70 LEQNNVKLVNISSNDIVDGNPKLTLGLVWSII 101
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
45-155 1.43e-03

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: 38.37  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKALENDAdcshllpmNPNDGSLFKSLADGILLCKMINlsepDTIDERAINKKKLTPFTVSENLNLALNSA 124
Cdd:cd21231    7 QKKTFTKWINAQFAKFG--------KPPIEDLFTDLQDGRRLLELLE----GLTGQKLVKEKGSTRVHALNNVNKALQVL 74
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568960615 125 SAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21231   75 QKNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
314-425 3.30e-03

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


Pssm-ID: 409090  Cd Length: 113  Bit Score: 37.35  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNS--LGVNP--YINHLYSDLADALVIFQLYEMI---RVPVNwsqvnkppypaLGGNMKKIE---NC 383
Cdd:cd21241    1 EQERVQKKTFTNWINSylAKRKPpmKVEDLFEDIKDGTKLLALLEVLsgeKLPCE-----------KGRRLKRVHflsNI 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568960615 384 NYAVEL--GKneaKFSLVGIAGQDLNEGNATLTLALVWQLMRRY 425
Cdd:cd21241   70 NTALKFleSK---KIKLVNINPTDIVDGKPSIVLGLIWTIILYF 110
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
433-545 3.49e-03

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: 37.63  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 433 LGEGEKVTD-------DIIIKWVNQTLKSA--NKSTSISSfkdkSISTSLPVLDLIDAIAPNAVRQEM----IKREHLTD 499
Cdd:cd21327    2 LRDGESLEDlmklspeELLLRWANYHLENAgcNKINNFSS----DIKDSKAYYHLLNQVAPKGDEEGIpaivIDMSGLRE 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568960615 500 EDKLNNAKYAISVARKIGARIYALPDDLVEVKPKMVMTVFACLMGK 545
Cdd:cd21327   78 KDDLKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNK 123
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
190-295 3.67e-03

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: 37.32  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 190 EELLLRWVNYHLTNAGWRTINNFSQDIKDSKAYFHLLNQIAPKgdrddgpavAIDLSGFNEKNDLKRA---GFMLQEADK 266
Cdd:cd00014    1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPG---------SIPKINKKPKSPFKKReniNLFLNACKK 71
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568960615 267 LGC--RQFVTPADVVS-GNPKLNLAFVANLFN 295
Cdd:cd00014   72 LGLpeLDLFEPEDLYEkGNLKKVLGTLWALAL 103
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
71-143 3.91e-03

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: 37.29  E-value: 3.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568960615  71 PNDGSLFKSLADGILLCKMINLSEPDTIdeRAINKKKLtPFTVSENLNLALNSASAIGCTVVNI-GAQDLKEGK 143
Cdd:cd21207   23 DDGKDYEDVLKDGVILCKLINILKPGSV--KKINTSKM-AFKLMENIENFLTACKGYGVPKTDLfQTVDLYEKK 93
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
45-155 4.65e-03

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: 38.10  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINkalendadcSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINKKKLTPFtvsENLNLALNSA 124
Cdd:cd21316   54 QKKTFTKWVN---------SHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCL---ENVDKALQFL 121
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568960615 125 SAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21316  122 KEQRVHLENMGSHDIVDGNHRLTLGLIWTII 152
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
45-155 4.82e-03

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


Pssm-ID: 409160  Cd Length: 124  Bit Score: 37.43  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615  45 EKVAFVNWINKalendadcsHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIdeRAINKKKLTPFTVSENLNLALNS- 123
Cdd:cd21311   16 QQNTFTRWANE---------HLKTANKHIADLETDLSDGLRLIALVEVLSGKKF--PKFNKRPTFRSQKLENVSVALKFl 84
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568960615 124 ASAIGCTVVNIGAQDLKEGKPHLVLGLLWQII 155
Cdd:cd21311   85 EEDEGIKIVNIDSSDIVDGKLKLILGLIWTLI 116
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
317-424 6.02e-03

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: 37.26  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 317 SKEERT-FRNWMNS-----------LGVNPYINHLYSDLADALVifqLYEMIrvpvNWSQVNKPPYPALggNMKKI---- 380
Cdd:cd21292   22 SEEEKVaFVNWINKnlgddpdckhlLPMDPNTDDLFEKVKDGIL---LCKMI----NLSVPDTIDERAI--NKKKLtvft 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568960615 381 --ENCNYAVelgkNEAKF---SLVGIAGQDLNEGNATLTLALVWQLMRR 424
Cdd:cd21292   93 ihENLTLAL----NSASAigcNVVNIGAEDLKEGKPHLVLGLLWQIIRI 137
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
339-424 6.25e-03

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: 37.04  E-value: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 339 LYSDLADALVIFQLYEMIrVP--VNWSQVNKPPYPALGGN-MKKIENCNYAVELGKnEAKFSLVGIAGQDLNEGNATLTL 415
Cdd:cd21294   38 LFDECKDGLVLSKLINDS-VPdtIDERVLNKPPRKNKPLNnFQMIENNNIVINSAK-AIGCSVVNIGAGDIIEGREHLIL 115

                 ....*....
gi 568960615 416 ALVWQLMRR 424
Cdd:cd21294  116 GLIWQIIRR 124
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
314-422 7.36e-03

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: 36.39  E-value: 7.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 314 EGESKEERTFRNWMNS----LGVNPYINHLYSDLADALVIFQLYEMI---RVPVNWSQVNKppypalggNMKKIENCNYA 386
Cdd:cd21190    1 EQERVQKKTFTNWINShlakLSQPIVINDLFVDIKDGTALLRLLEVLsgqKLPIESGRVLQ--------RAHKLSNIRNA 72
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568960615 387 VELGKNEaKFSLVGIAGQDLNEGNATLTLALVWQLM 422
Cdd:cd21190   73 LDFLTKR-CIKLVNINSTDIVDGKPSIVLGLIWTII 107
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
443-529 8.50e-03

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


Pssm-ID: 409145  Cd Length: 109  Bit Score: 36.34  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960615 443 IIIKWVNQTLKSANKSTSISSF----KDKSISTSLpvldlIDAIAPnavrqEMIKREHLTDEDKLNNAKYAISVARKIGA 518
Cdd:cd21296   14 VLLKWMNFHLKKAGYKKTVTNFssdvKDAEAYAYL-----LNVLAP-----EHCDPATLEAKDPLERAKLVLEQAEKMNC 83
                         90
                 ....*....|.
gi 568960615 519 RIYALPDDLVE 529
Cdd:cd21296   84 KRYLTAKDIVE 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
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