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Conserved domains on  [gi|398365759|ref|NP_010414|]
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fimbrin [Saccharomyces cerevisiae S288C]

Protein Classification

fimbrin/plastin family actin filament-binding protein( domain architecture ID 11473718)

fimbrin/plastin family actin filament-binding protein similar to Saccharomyces cerevisiae fimbrin, which binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity

CATH:  1.10.418.10
Gene Ontology:  GO:0051015|GO:0051017|GO:0005509
PubMed:  32478077|12186940
SCOP:  4004022

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-640 0e+00

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


:

Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 809.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   1 MNIVKLQ----RKFPILTQEDLFS-TIEKFRAIDLDDKGWVEKQQALEAVSKDGDATYDEARETLKHVGVDASGRVELDD 75
Cdd:COG5069    1 MEAKKWQkvqkKTFTKWTNEKLISgGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  76 YVGlvaklresktgaapQTTFNVAPNStpivstAATGLQHKGKGtqakIIVAGSQTGTTHTINEEErrEFTKHINSVLAG 155
Cdd:COG5069   81 GKG--------------VKLFNIGPQD------IVDGNPKLILG----LIWSLISRLTIATINEEG--ELTKHINLLLWC 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 156 DQDIGDLLPfPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNWPKKGKELNNFQASENANIVINSAKAIG-CVVVNV 234
Cdd:COG5069  135 DEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGvEDIVNV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 235 HSEDiieGREHLILgLIWQIIRRGLLSKIDIKLHpELYRLLEDDETLEQfLRLPPEQILLRWFN-YHLKQANWNrrVTNF 313
Cdd:COG5069  214 SIPD---ERSIMTY-VSWYIIRFGLLEKIDIALH-RVYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANWK--VVNF 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 314 SKDVSDGENYTILLNQLDpALCSKAPLQTTDLMERAEQVLQNAEKLDCRKYLTPsslvAGNPKLNLAFVAHLFNTHPGLE 393
Cdd:COG5069  286 SKDVSDGENYTDLLNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPP----AGNPKLDLAFVAHLFNTHPGQE 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 394 PIQEEEKPEIEEFDAEGEREARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKV-MPGAVDFKHVNKRPASGAEISR 472
Cdd:COG5069  361 PLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASGIEENR 440
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 473 FKALENTNYAVDLGRAKGFSLVGIEGSDIVDGNKlLTLGLVWQLMRRNISITMKTLSSSGRDMSDSQILKWAQDQVTKGG 552
Cdd:COG5069  441 FKAFENENYAVDLGITEGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGD 519
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 553 KNSTIRSFKDQALSN-AHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANAR-LAIS--IARKLGALIWLVPEDINEVRAR 628
Cdd:COG5069  520 KEEGIRSFGDPAGSVsGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADARsLAISskILRSLGAIIKFLPEDINGVRPR 599
                        650
                 ....*....|...
gi 398365759 629 L-IITFIASLMTL 640
Cdd:COG5069  600 LdVLTFIESLMAD 612
 
Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-640 0e+00

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 809.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   1 MNIVKLQ----RKFPILTQEDLFS-TIEKFRAIDLDDKGWVEKQQALEAVSKDGDATYDEARETLKHVGVDASGRVELDD 75
Cdd:COG5069    1 MEAKKWQkvqkKTFTKWTNEKLISgGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  76 YVGlvaklresktgaapQTTFNVAPNStpivstAATGLQHKGKGtqakIIVAGSQTGTTHTINEEErrEFTKHINSVLAG 155
Cdd:COG5069   81 GKG--------------VKLFNIGPQD------IVDGNPKLILG----LIWSLISRLTIATINEEG--ELTKHINLLLWC 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 156 DQDIGDLLPfPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNWPKKGKELNNFQASENANIVINSAKAIG-CVVVNV 234
Cdd:COG5069  135 DEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGvEDIVNV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 235 HSEDiieGREHLILgLIWQIIRRGLLSKIDIKLHpELYRLLEDDETLEQfLRLPPEQILLRWFN-YHLKQANWNrrVTNF 313
Cdd:COG5069  214 SIPD---ERSIMTY-VSWYIIRFGLLEKIDIALH-RVYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANWK--VVNF 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 314 SKDVSDGENYTILLNQLDpALCSKAPLQTTDLMERAEQVLQNAEKLDCRKYLTPsslvAGNPKLNLAFVAHLFNTHPGLE 393
Cdd:COG5069  286 SKDVSDGENYTDLLNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPP----AGNPKLDLAFVAHLFNTHPGQE 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 394 PIQEEEKPEIEEFDAEGEREARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKV-MPGAVDFKHVNKRPASGAEISR 472
Cdd:COG5069  361 PLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASGIEENR 440
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 473 FKALENTNYAVDLGRAKGFSLVGIEGSDIVDGNKlLTLGLVWQLMRRNISITMKTLSSSGRDMSDSQILKWAQDQVTKGG 552
Cdd:COG5069  441 FKAFENENYAVDLGITEGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGD 519
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 553 KNSTIRSFKDQALSN-AHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANAR-LAIS--IARKLGALIWLVPEDINEVRAR 628
Cdd:COG5069  520 KEEGIRSFGDPAGSVsGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADARsLAISskILRSLGAIIKFLPEDINGVRPR 599
                        650
                 ....*....|...
gi 398365759 629 L-IITFIASLMTL 640
Cdd:COG5069  600 LdVLTFIESLMAD 612
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
135-258 1.02e-77

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: 243.12  E-value: 1.02e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 135 HTINEEERREFTKHINSVLAGDQDIGDLLPFPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNWP-KKGKELNNFQA 213
Cdd:cd21294    1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPpRKNKPLNNFQM 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 398365759 214 SENANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRG 258
Cdd:cd21294   81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRRG 125
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
287-391 6.04e-23

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 93.89  E-value: 6.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  287 LPPEQILLRWFNYHLKQANWNRRVTNFSKDVSDGENYTILLNQLDPALCSKA--PLQTTDLMERAEQVLQNAE-KLDCRK 363
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKklNKSEFDKLENINLALDVAEkKLGVPK 80
                          90       100
                  ....*....|....*....|....*....
gi 398365759  364 YL-TPSSLVAGNPKLNLAFVAHLFNTHPG 391
Cdd:pfam00307  81 VLiEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
415-519 9.29e-23

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: 93.15  E-value: 9.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   415 RVFTLWLNSL---DVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNkrpasgAEISRFKALENTNYAVDLGRAKGF 491
Cdd:smart00033   1 KTLLRWVNSLlaeYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVA------ASLSRFKKIENINLALSFAEKLGG 74
                           90       100
                   ....*....|....*....|....*...
gi 398365759   492 SLVGIEGSDIVDGNKlLTLGLVWQLMRR 519
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
 
Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-640 0e+00

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 809.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   1 MNIVKLQ----RKFPILTQEDLFS-TIEKFRAIDLDDKGWVEKQQALEAVSKDGDATYDEARETLKHVGVDASGRVELDD 75
Cdd:COG5069    1 MEAKKWQkvqkKTFTKWTNEKLISgGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  76 YVGlvaklresktgaapQTTFNVAPNStpivstAATGLQHKGKGtqakIIVAGSQTGTTHTINEEErrEFTKHINSVLAG 155
Cdd:COG5069   81 GKG--------------VKLFNIGPQD------IVDGNPKLILG----LIWSLISRLTIATINEEG--ELTKHINLLLWC 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 156 DQDIGDLLPfPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNWPKKGKELNNFQASENANIVINSAKAIG-CVVVNV 234
Cdd:COG5069  135 DEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGvEDIVNV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 235 HSEDiieGREHLILgLIWQIIRRGLLSKIDIKLHpELYRLLEDDETLEQfLRLPPEQILLRWFN-YHLKQANWNrrVTNF 313
Cdd:COG5069  214 SIPD---ERSIMTY-VSWYIIRFGLLEKIDIALH-RVYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANWK--VVNF 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 314 SKDVSDGENYTILLNQLDpALCSKAPLQTTDLMERAEQVLQNAEKLDCRKYLTPsslvAGNPKLNLAFVAHLFNTHPGLE 393
Cdd:COG5069  286 SKDVSDGENYTDLLNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPP----AGNPKLDLAFVAHLFNTHPGQE 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 394 PIQEEEKPEIEEFDAEGEREARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKV-MPGAVDFKHVNKRPASGAEISR 472
Cdd:COG5069  361 PLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASGIEENR 440
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 473 FKALENTNYAVDLGRAKGFSLVGIEGSDIVDGNKlLTLGLVWQLMRRNISITMKTLSSSGRDMSDSQILKWAQDQVTKGG 552
Cdd:COG5069  441 FKAFENENYAVDLGITEGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGD 519
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 553 KNSTIRSFKDQALSN-AHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANAR-LAIS--IARKLGALIWLVPEDINEVRAR 628
Cdd:COG5069  520 KEEGIRSFGDPAGSVsGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADARsLAISskILRSLGAIIKFLPEDINGVRPR 599
                        650
                 ....*....|...
gi 398365759 629 L-IITFIASLMTL 640
Cdd:COG5069  600 LdVLTFIESLMAD 612
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
135-258 1.02e-77

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: 243.12  E-value: 1.02e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 135 HTINEEERREFTKHINSVLAGDQDIGDLLPFPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNWP-KKGKELNNFQA 213
Cdd:cd21294    1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPpRKNKPLNNFQM 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 398365759 214 SENANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRG 258
Cdd:cd21294   81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRRG 125
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
279-387 7.22e-77

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: 240.16  E-value: 7.22e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 279 ETLEQFLRLPPEQILLRWFNYHLKQANWNRRVTNFSKDVSDGENYTILLNQLDPALCSKAPLQTTDLMERAEQVLQNAEK 358
Cdd:cd21297    1 ETLEQFLRLPPEQILLRWFNYHLKAANWPRRVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDLLQRAEQVLQNAEK 80
                         90       100
                 ....*....|....*....|....*....
gi 398365759 359 LDCRKYLTPSSLVAGNPKLNLAFVAHLFN 387
Cdd:cd21297   81 LDCRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
406-525 1.43e-73

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: 231.93  E-value: 1.43e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 406 FDAEGEREARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRPASgAEISRFKALENTNYAVDL 485
Cdd:cd21300    1 FDAEGEREARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPAS-AEISRFKAVENTNYAVEL 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 398365759 486 GRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMRRNISITM 525
Cdd:cd21300   80 GKQLGFSLVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
532-639 1.04e-64

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: 208.05  E-value: 1.04e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 532 GRDMSDSQILKWAQDQVTKGGKNSTIRSFKDQALSNAHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANARLAISIARKL 611
Cdd:cd21303    1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLVTPGNTEDEAYLNAKLAISIARKL 80
                         90       100
                 ....*....|....*....|....*...
gi 398365759 612 GALIWLVPEDINEVRARLIITFIASLMT 639
Cdd:cd21303   81 GALIFLVPEDIVEVRPRLVLTFIGSLMA 108
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
277-387 4.11e-53

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: 177.47  E-value: 4.11e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 277 DDETLEQFLRLPPEQILLRWFNYHLKQANWNRRVTNFSKDVSDGENYTILLNQLDPALCSKAP--LQTTDLMERAEQVLQ 354
Cdd:cd21295    1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRRIKNFSGDIKDSEAYTHLLKQIAPKDAGVDTsaLRESDLLQRAELMLQ 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 398365759 355 NAEKLDCRKYLTPSSLVAGNPKLNLAFVAHLFN 387
Cdd:cd21295   81 NADKIGCRKFVTPKDVVTGNPKLNLAFVANLFN 113
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
112-265 4.63e-51

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: 173.23  E-value: 4.63e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 112 GLQHKGkGTqakiiVAGSQTGTTHTINEEERREFTKHINSVLAGDQDIGDLLPFPTDTFQLFDECRDGLVLSKLINDSVP 191
Cdd:cd21292    2 GIDAKG-GT-----SEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVP 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365759 192 DTIDTRVLNwpkKGKeLNNFQASENANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRGLLSKIDI 265
Cdd:cd21292   76 DTIDERAIN---KKK-LTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
140-256 9.00e-51

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: 171.22  E-value: 9.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 140 EERREFTKHINSVLAGDQDIGDLLPFPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNwpkKGKELNNFQASENANI 219
Cdd:cd21217    1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLN---KKKPKNIFEATENLNL 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 398365759 220 VINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIR 256
Cdd:cd21217   78 ALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
409-521 3.43e-49

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: 167.07  E-value: 3.43e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 409 EGEREARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRPASGaeisRFKALENTNYAVDLGRA 488
Cdd:cd21219    1 EGSREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKPLN----KFKKVENCNYAVDLAKK 76
                         90       100       110
                 ....*....|....*....|....*....|...
gi 398365759 489 KGFSLVGIEGSDIVDGNKLLTLGLVWQLMRRNI 521
Cdd:cd21219   77 LGFSLVGIGGKDIADGNRKLTLALVWQLMRYHV 109
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
279-387 2.23e-44

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: 153.99  E-value: 2.23e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 279 ETLEQFLRLPPEQILLRWFNYHLKQANWNR-RVTNFSKDVSDGENYTILLNQLDPALCSKA----PLQTTDLMERAEQVL 353
Cdd:cd21218    1 ETLESLLYLPPEEILLRWVNYHLKKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELCDKElvleVLSEEDLEKRAEKVL 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 398365759 354 QNAEKLDCRKYLTPSSLVAGNPKLNLAFVAHLFN 387
Cdd:cd21218   81 QAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
279-386 1.08e-43

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: 151.90  E-value: 1.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 279 ETLEQFLRLPPEQILLRWFNYHLKQANWNRRVTNFSKDVSDGENYTILLNQLDPALCSKAPLQTTDLMERAEQVLQNAEK 358
Cdd:cd21296    1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKTVTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEK 80
                         90       100
                 ....*....|....*....|....*...
gi 398365759 359 LDCRKYLTPSSLVAGNPKLNLAFVAHLF 386
Cdd:cd21296   81 MNCKRYLTAKDIVEGSANLNLAFVAQIF 108
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
535-639 8.07e-43

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: 149.34  E-value: 8.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 535 MSDSQILKWAQDQVTKGGKNSTIRSFKDQALSNAHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANARLAISIARKLGAL 614
Cdd:cd21220    1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLVTEGETDEEKEQNAKYAISLARKIGAV 80
                         90       100
                 ....*....|....*....|....*
gi 398365759 615 IWLVPEDINEVRARLIITFIASLMT 639
Cdd:cd21220   81 IFLLWEDIVEVKPKMILTFVASLMA 105
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
409-519 1.16e-42

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: 149.31  E-value: 1.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 409 EGE-REARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRP-ASGAEisrFKALENTNYAVDLG 486
Cdd:cd21298    2 IEEtREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFkKLGAN---MKKIENCNYAVELG 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 398365759 487 RAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21298   79 KKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRA 111
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
129-265 1.88e-39

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: 141.72  E-value: 1.88e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 129 SQTGTTHTINEEERREFTKHINSVLAGDQDIGDLLPF-PTDTfQLFDECRDGLVLSKLINDSVPDTIDTRVLNwpkkGKE 207
Cdd:cd21323   13 SSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMnPTDE-SLFKSLADGILLCKMINLSQPDTIDERAIN----KKK 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 398365759 208 LNNFQASENANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRGLLSKIDI 265
Cdd:cd21323   88 LTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
274-387 2.39e-35

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: 129.32  E-value: 2.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 274 LLEDDETLEQFLRLPPEQILLRWFNYHLKQANWNRrVTNFSKDVSDGENYTILLNQLDPA---------LCSKAPLQTTD 344
Cdd:cd21328    1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQK-INNFSSDIKDSRAYFHLLNQIAPKgqkegepriDINMSGFNEKD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 398365759 345 LMERAEQVLQNAEKLDCRKYLTPSSLVAGNPKLNLAFVAHLFN 387
Cdd:cd21328   80 DLKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
279-390 4.00e-35

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: 128.85  E-value: 4.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 279 ETLEQFLRLPPEQILLRWFNYHLKQANWnRRVTNFSKDVSDGENYTILLNQLDPALCSKAPLQTTDL--------MERAE 350
Cdd:cd21326    3 EELEELMKLSPEELLLRWVNYHLTNAGW-QNISNFSQDIKDSRAYFHLLNQIAPKGDVFDENIEIDFsgfnekndLKRAE 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 398365759 351 QVLQNAEKLDCRKYLTPSSLVAGNPKLNLAFVAHLFNTHP 390
Cdd:cd21326   82 YMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 121
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
141-256 4.92e-34

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: 125.72  E-value: 4.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVLAGDQDIGDLLPFPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNwpkKGKELNNFQASENANIV 220
Cdd:cd21293    2 EKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAIN---TKKVLNPWERNENHTLC 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 398365759 221 INSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIR 256
Cdd:cd21293   79 LNSAKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIK 114
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
274-390 7.01e-34

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: 125.46  E-value: 7.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 274 LLEDDETLEQFLRLPPEQILLRWFNYHLKQANWNRrVTNFSKDVSDGENYTILLNQLDPA---------LCSKAPLQTTD 344
Cdd:cd21327    1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNK-INNFSSDIKDSKAYYHLLNQVAPKgdeegipaiVIDMSGLREKD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 398365759 345 LMERAEQVLQNAEKLDCRKYLTPSSLVAGNPKLNLAFVAHLFNTHP 390
Cdd:cd21327   80 DLKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
536-640 7.38e-34

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: 124.70  E-value: 7.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 536 SDSQILKWAQDQVTKGGKNSTIRSFKDQALSNAHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANARLAISIARKLGALI 615
Cdd:cd21301    2 SDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLVLEGNSEEDKLSNAKYAISMARKIGARV 81
                         90       100
                 ....*....|....*....|....*
gi 398365759 616 WLVPEDINEVRARLIITFIASLMTL 640
Cdd:cd21301   82 YALPEDIVEVKPKMVMTVFACLMAL 106
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
409-521 8.30e-34

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: 124.92  E-value: 8.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 409 EGEREARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRPASgaeiSRFKALENTNYAVDLGRA 488
Cdd:cd21299    1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIK----MPFKKVENCNQVVKIGKQ 76
                         90       100       110
                 ....*....|....*....|....*....|...
gi 398365759 489 KGFSLVGIEGSDIVDGNKLLTLGLVWQLMRRNI 521
Cdd:cd21299   77 LKFSLVNVAGNDIVQGNKKLILALLWQLMRYHM 109
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
129-265 2.60e-33

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: 124.79  E-value: 2.60e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 129 SQTGTTHTINEEERREFTKHINSVLAGDQDIGDLLPFPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNwpkkGKEL 208
Cdd:cd21325   13 SSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAIN----KKKL 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 398365759 209 NNFQASENANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRGLLSKIDI 265
Cdd:cd21325   89 TPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIEL 145
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
129-265 7.00e-33

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: 123.58  E-value: 7.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 129 SQTGTTHTINEEERREFTKHINSVLAGDQDIGDLLPFPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNwpkkGKEL 208
Cdd:cd21324   13 SSAGTQHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTIN----KKKL 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 398365759 209 NNFQASENANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRGLLSKIDI 265
Cdd:cd21324   89 TPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
409-519 9.42e-33

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: 122.02  E-value: 9.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 409 EGE-REARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKVMPgAVDFKHVNKRPASgAEISRFKALENTNYAVDLGR 487
Cdd:cd21329    2 EGEsSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRV-PVDWGHVNKPPYP-ALGGNMKKIENCNYAVELGK 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 398365759 488 AKG-FSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21329   80 NKAkFSLVGIAGSDLNEGNKTLTLALIWQLMRR 112
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
409-519 2.42e-31

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: 118.56  E-value: 2.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 409 EGE-REARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKV-MPgaVDFKHVNKRPAS--GAEIsrfKALENTNYAVD 484
Cdd:cd21331   18 EGEtREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIkVP--VDWNKVNKPPYPklGANM---KKLENCNYAVE 92
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 398365759 485 LGRAKG-FSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21331   93 LGKHPAkFSLVGIGGQDLNDGNPTLTLALVWQLMRR 128
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
534-638 1.33e-30

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: 115.73  E-value: 1.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 534 DMSDSQILKWAQDQVTKGGKNSTIRSFKDQALSNAHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANARLAISIARKLGA 613
Cdd:cd21302    1 EMTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGC 80
                         90       100
                 ....*....|....*....|....*
gi 398365759 614 LIWLVPEDINEVRARLIITFIASLM 638
Cdd:cd21302   81 SIFLLPEDIVEVNQKMILILTASIM 105
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
409-519 2.35e-28

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: 110.08  E-value: 2.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 409 EGE-REARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKV-MPgaVDFKHVNKRPASGAEiSRFKALENTNYAVDLG 486
Cdd:cd21330    9 EGEtREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIkVP--VDWNRVNKPPYPKLG-ENMKKLENCNYAVELG 85
                         90       100       110
                 ....*....|....*....|....*....|....
gi 398365759 487 RAKG-FSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21330   86 KNKAkFSLVGIAGQDLNEGNRTLTLALIWQLMRR 119
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
530-638 2.45e-26

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


Pssm-ID: 409182  Cd Length: 115  Bit Score: 103.92  E-value: 2.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 530 SSGRDMSDSQILKWAQDQVTKGGKNSTIRSFKDQALSNAHFLLDVLNGIAPGYVDYDLVTPGN-TEEERYANARLAISIA 608
Cdd:cd21333    1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDlNDEEKLNNAKYAISMA 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 398365759 609 RKLGALIWLVPEDINEVRARLIITFIASLM 638
Cdd:cd21333   81 RKIGARVYALPEDLVEVKPKMVMTVFACLM 110
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
536-638 5.43e-25

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


Pssm-ID: 409183  Cd Length: 112  Bit Score: 99.96  E-value: 5.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 536 SDSQILKWAQDQVTKGGKNSTIRSFKDQALSNAHFLLDVLNGIAPGYVDYDLVTPGN-TEEERYANARLAISIARKLGAL 614
Cdd:cd21334    2 NDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNlTDDDKLDNAKYAVSMARKIGAR 81
                         90       100
                 ....*....|....*....|....
gi 398365759 615 IWLVPEDINEVRARLIITFIASLM 638
Cdd:cd21334   82 VYALPEDLVEVKPKMVMTVFACLM 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
287-391 6.04e-23

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 93.89  E-value: 6.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  287 LPPEQILLRWFNYHLKQANWNRRVTNFSKDVSDGENYTILLNQLDPALCSKA--PLQTTDLMERAEQVLQNAE-KLDCRK 363
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKklNKSEFDKLENINLALDVAEkKLGVPK 80
                          90       100
                  ....*....|....*....|....*....
gi 398365759  364 YL-TPSSLVAGNPKLNLAFVAHLFNTHPG 391
Cdd:pfam00307  81 VLiEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
415-519 9.29e-23

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: 93.15  E-value: 9.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   415 RVFTLWLNSL---DVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNkrpasgAEISRFKALENTNYAVDLGRAKGF 491
Cdd:smart00033   1 KTLLRWVNSLlaeYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVA------ASLSRFKKIENINLALSFAEKLGG 74
                           90       100
                   ....*....|....*....|....*...
gi 398365759   492 SLVGIEGSDIVDGNKlLTLGLVWQLMRR 519
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
411-520 2.24e-22

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 92.35  E-value: 2.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  411 EREARVFTLWLNS---LDVDPPVI-SLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRPasgaeisrFKALENTNYAVDLG 486
Cdd:pfam00307   1 LELEKELLRWINShlaEYGPGVRVtNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE--------FDKLENINLALDVA 72
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 398365759  487 RAK-GFSLVGIEGSDIVDGNKLLTLGLVWQLMRRN 520
Cdd:pfam00307  73 EKKlGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
143-257 8.97e-22

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: 90.45  E-value: 8.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   143 REFTKHINSVLAGDQdigdllpfPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNwpkkgKELNNFQASENANIVIN 222
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVA-----ASLSRFKKIENINLALS 67
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 398365759   223 SAKAIGCVVVNVHSEDIIEGReHLILGLIWQIIRR 257
Cdd:smart00033  68 FAEKLGGKVVLFEPEDLVEGP-KLILGVIWTLISL 101
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
139-263 5.60e-21

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: 88.49  E-value: 5.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 139 EEERREFTKHINSVlagdqDIGDLLPfptdtfQLFDECRDGLVLSKLIndsvpDTIDTRVLNWPKKGK--ELNNFQASEN 216
Cdd:cd21219    3 SREERAFRMWLNSL-----GLDPLIN------NLYEDLRDGLVLLQVL-----DKIQPGCVNWKKVNKpkPLNKFKKVEN 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 398365759 217 ANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRGLLSKI 263
Cdd:cd21219   67 CNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
532-638 2.17e-20

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


Pssm-ID: 409181  Cd Length: 115  Bit Score: 86.93  E-value: 2.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 532 GRDMSDSQILKWAQDQVTKGGKNSTIRSFKDQALSNAHFLLDVLNGIAPGYVDYDLVTPGN-TEEERYANARLAISIARK 610
Cdd:cd21332    5 GEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDlSDADKLNNAKYAISVARK 84
                         90       100
                 ....*....|....*....|....*...
gi 398365759 611 LGALIWLVPEDINEVRARLIITFIASLM 638
Cdd:cd21332   85 IGARVYALPEDLVEVKPKMVMTVFACLM 112
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
413-518 2.59e-19

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: 83.78  E-value: 2.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 413 EARVFTLWLNS-----------LDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRPAsgaeISRFKALENTNY 481
Cdd:cd21217    2 EKEAFVEHINSlladdpdlkhlLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKP----KNIFEATENLNL 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 398365759 482 AVDLGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMR 518
Cdd:cd21217   78 ALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
139-258 7.37e-18

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 79.25  E-value: 7.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  139 EEERREFTKHINSVLAGDQDigdllpfPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNWpkkgkelNNFQASENAN 218
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGP-------GVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNK-------SEFDKLENIN 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 398365759  219 IVINSA-KAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRG 258
Cdd:pfam00307  67 LALDVAeKKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
411-519 1.58e-17

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: 79.03  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 411 EREARVFTLWLNS-----------LDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRPASGAEISRFKALENT 479
Cdd:cd21294    5 EDERREFTKHINAvlagdpdvgsrLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPPRKNKPLNNFQMIENN 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 398365759 480 NYAVDLGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21294   85 NIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRR 124
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
139-261 1.90e-16

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: 75.92  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 139 EEERREFTKHINSVlagdqdigDLLPFPTDtfqLFDECRDGLVLSKLINDSVPDTIDTRVLNWPKKGKELNNFQASENAN 218
Cdd:cd21300    6 EREARVFTLWLNSL--------DVEPAVND---LFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPASAEISRFKAVENTN 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 398365759 219 IVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRGLLS 261
Cdd:cd21300   75 YAVELGKQLGFSLVGIQGADITDGSRTLTLALVWQLMRFHITK 117
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
292-386 7.94e-16

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 73.50  E-value: 7.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   292 ILLRWFNYHLKQANwNRRVTNFSKDVSDGENYTILLNQLDPALCSK----APLQTTDLMERAEQVLQNAEKL-DCRKYLT 366
Cdd:smart00033   2 TLLRWVNSLLAEYD-KPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLgGKVVLFE 80
                           90       100
                   ....*....|....*....|
gi 398365759   367 PSSLVAGnPKLNLAFVAHLF 386
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLI 99
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
534-642 4.82e-15

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 71.55  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  534 DMSDSQILKWAQDQVTKGGKNSTIRSFKDQaLSNAHFLLDVLNGIAPGYVDYDLVTPgnTEEERYANARLAISIAR-KLG 612
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTD-LRDGLALCALLNKLAPGLVDKKKLNK--SEFDKLENINLALDVAEkKLG 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 398365759  613 ALIWLV-PEDINEVRARLIITFIASLMTLNK 642
Cdd:pfam00307  78 VPKVLIePEDLVEGDNKSVLTYLASLFRRFQ 108
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
415-519 4.88e-15

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: 71.28  E-value: 4.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 415 RVFTLWLNS-LDV-DPPVISLFDDLKDGLILLQAYEkVMPGAVDFKHvNKRPASgaeisRFKALENTNYAVDLGRAKGFS 492
Cdd:cd21215    7 KTFTKWLNTkLSSrGLSITDLVTDLSDGVRLIQLLE-IIGDESLGRY-NKNPKM-----RVQKLENVNKALEFIKSRGVK 79
                         90       100
                 ....*....|....*....|....*..
gi 398365759 493 LVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21215   80 LTNIGAEDIVDGNLKLILGLLWTLILR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
539-640 2.15e-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: 69.27  E-value: 2.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   539 QILKWAQDQVTKGGKnsTIRSFKDQALSNAHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANARLAISIARKLG-ALIWL 617
Cdd:smart00033   2 TLLRWVNSLLAEYDK--PPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGgKVVLF 79
                           90       100
                   ....*....|....*....|...
gi 398365759   618 VPEDINEVRaRLIITFIASLMTL 640
Cdd:smart00033  80 EPEDLVEGP-KLILGVIWTLISL 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
142-256 3.12e-13

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 66.21  E-value: 3.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 142 RREFTKHINSVLAGDqdigdllpFPTDTFQLFDECRDGLVLSKLINDSVPDTIDtrvlnwPKKGKELNNFQASENANIVI 221
Cdd:cd00014    1 EEELLKWINEVLGEE--------LPVSITDLFESLRDGVLLCKLINKLSPGSIP------KINKKPKSPFKKRENINLFL 66
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 398365759 222 NSAKAIG-CVVVNVHSEDIIEGR-EHLILGLIWQIIR 256
Cdd:cd00014   67 NACKKLGlPELDLFEPEDLYEKGnLKKVLGTLWALAL 103
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
415-514 4.33e-13

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: 65.87  E-value: 4.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 415 RVFTLWLNSLDVD---PPVISLFDDLKDGLILLQAYEkVMPGAvdfkhvNKRPASGAeiSRFKALENTNYAVDLGRAKGF 491
Cdd:cd21186    5 KTFTKWINSQLSKankPPIKDLFEDLRDGTRLLALLE-VLTGK------KLKPEKGR--MRVHHLNNVNRALQVLEQNNV 75
                         90       100
                 ....*....|....*....|...
gi 398365759 492 SLVGIEGSDIVDGNKLLTLGLVW 514
Cdd:cd21186   76 KLVNISSNDIVDGNPKLTLGLVW 98
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
415-514 5.50e-12

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: 62.42  E-value: 5.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 415 RVFTLWLNS--LDVDPPVISLFDDLKDGLILLQAYEKVmpgavdfkhvnkrpaSGAEISR------FKALENTNYAVDLG 486
Cdd:cd21188    6 KTFTKWVNKhlIKARRRVVDLFEDLRDGHNLISLLEVL---------------SGESLPRergrmrFHRLQNVQTALDFL 70
                         90       100
                 ....*....|....*....|....*...
gi 398365759 487 RAKGFSLVGIEGSDIVDGNKLLTLGLVW 514
Cdd:cd21188   71 KYRKIKLVNIRAEDIVDGNPKLTLGLIW 98
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
409-514 9.49e-12

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: 62.01  E-value: 9.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 409 EGER-EARVFTLWLNS--LDVDPP--VISLFDDLKDGLILLQAYEkVMPGavdfkhvNKRPA-SGAEISRFKALENTNYA 482
Cdd:cd21241    1 EQERvQKKTFTNWINSylAKRKPPmkVEDLFEDIKDGTKLLALLE-VLSG-------EKLPCeKGRRLKRVHFLSNINTA 72
                         90       100       110
                 ....*....|....*....|....*....|..
gi 398365759 483 VDLGRAKGFSLVGIEGSDIVDGNKLLTLGLVW 514
Cdd:cd21241   73 LKFLESKKIKLVNINPTDIVDGKPSIVLGLIW 104
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
172-261 9.72e-12

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: 62.25  E-value: 9.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 172 LFDECRDGLVLSKLINDSVPDTIDTRVLNWPKKgKELNNFQASENANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLI 251
Cdd:cd21298   27 LYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFK-KLGANMKKIENCNYAVELGKKLKFSLVGIGGKDIYDGNRTLTLALV 105
                         90
                 ....*....|
gi 398365759 252 WQIIRRGLLS 261
Cdd:cd21298  106 WQLMRAYTLS 115
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
411-517 1.98e-11

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: 61.09  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 411 ERE---ARVFTLWLNSLDVD---PPVISLFDDLKDGLILLQAYEkvmpGAVDFKHVNKRPASgaeisRFKALENTNYAVD 484
Cdd:cd21231    2 EREdvqKKTFTKWINAQFAKfgkPPIEDLFTDLQDGRRLLELLE----GLTGQKLVKEKGST-----RVHALNNVNKALQ 72
                         90       100       110
                 ....*....|....*....|....*....|...
gi 398365759 485 LGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLM 517
Cdd:cd21231   73 VLQKNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
410-519 2.10e-11

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: 61.23  E-value: 2.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 410 GEREA---RVFTLWLNS--LDVDPPVISLFDDLKDGLILLQAYEkVMPGavdfKHVnKRPASGAeiSRFKALENTNYAVD 484
Cdd:cd21246   11 DEREAvqkKTFTKWVNShlARVGCRINDLYTDLRDGRMLIKLLE-VLSG----ERL-PKPTKGK--MRIHCLENVDKALQ 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 398365759 485 LGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21246   83 FLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
415-518 2.79e-11

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 60.43  E-value: 2.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 415 RVFTLWLNSL---DVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRpasgaeiSRFKALENTNYAVDLGRAKGF 491
Cdd:cd00014    2 EELLKWINEVlgeELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPK-------SPFKKRENINLFLNACKKLGL 74
                         90       100
                 ....*....|....*....|....*....
gi 398365759 492 -SLVGIEGSDIV-DGNKLLTLGLVWQLMR 518
Cdd:cd00014   75 pELDLFEPEDLYeKGNLKKVLGTLWALAL 103
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
141-260 3.28e-11

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: 60.59  E-value: 3.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSvlagdqdigdllpFPTDTF--QLFDECRDGLVLSKLIndsvpDTIDTRVLNWPKKGKE--LNNFQASEN 216
Cdd:cd21299    5 EERCFRLWINS-------------LGIDTYvnNVFEDVRDGWVLLEVL-----DKVSPGSVNWKHANKPpiKMPFKKVEN 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 398365759 217 ANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRGLL 260
Cdd:cd21299   67 CNQVVKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRYHML 110
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
411-518 4.26e-11

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: 61.21  E-value: 4.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 411 EREARVFTLWLNS-----------LDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRpasgaEISRFKALENT 479
Cdd:cd21323   23 EEEKVAFVNWINKalegdpdckhvVPMNPTDESLFKSLADGILLCKMINLSQPDTIDERAINKK-----KLTPFTISENL 97
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 398365759 480 NYAVDLGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMR 518
Cdd:cd21323   98 NLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIK 136
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
411-519 1.21e-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: 59.65  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 411 EREA---RVFTLWLNS--LDVDPPVISLFDDLKDGLILLQAYEkVMPGavdfkHVNKRPASGAeiSRFKALENTNYAVDL 485
Cdd:cd21318   34 EREAvqkKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLE-VLSG-----EQLPKPTRGR--MRIHSLENVDKALQF 105
                         90       100       110
                 ....*....|....*....|....*....|....
gi 398365759 486 GRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21318  106 LKEQRVHLENVGSHDIVDGNHRLTLGLIWTIILR 139
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
415-517 1.22e-10

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: 58.55  E-value: 1.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 415 RVFTLWLNSL--DVDPPVISLFDDLKDGLILLQAYEkVMPGavdfKHVNKrPASGAeiSRFKALENTNYAVDLGRAKGFS 492
Cdd:cd21214    8 KTFTAWCNSHlrKAGTQIENIEEDFRDGLKLMLLLE-VISG----ERLPK-PERGK--MRFHKIANVNKALDFIASKGVK 79
                         90       100
                 ....*....|....*....|....*
gi 398365759 493 LVGIEGSDIVDGNKLLTLGLVWQLM 517
Cdd:cd21214   80 LVSIGAEEIVDGNLKMTLGMIWTII 104
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
411-519 1.40e-10

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: 59.60  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 411 EREARVFTLWLNS-----------LDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRPasgaeISRFKALENT 479
Cdd:cd21292   23 EEEKVAFVNWINKnlgddpdckhlLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDERAINKKK-----LTVFTIHENL 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 398365759 480 NYAVDLGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21292   98 TLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRI 137
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
413-517 1.44e-10

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: 58.48  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 413 EARVFTLWLN---SLDVDPPVISLFDDLKDGLILLQAYEKVMPgavdfKHVNKRPASgaeiSRFKALENTNYAVDLGRAK 489
Cdd:cd21232    3 QKKTFTKWINarfSKSGKPPIKDMFTDLRDGRKLLDLLEGLTG-----KSLPKERGS----TRVHALNNVNRVLQVLHQN 73
                         90       100
                 ....*....|....*....|....*...
gi 398365759 490 GFSLVGIEGSDIVDGNKLLTLGLVWQLM 517
Cdd:cd21232   74 NVELVNIGGTDIVDGNHKLTLGLLWSII 101
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
413-517 2.17e-10

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: 58.35  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 413 EARVFTLWLNS---LDVDPPVIS-LFDDLKDGLILLQAYEkVMPGavdfkhvNKRPA-SGAEISRFKALENTNYAVDLGR 487
Cdd:cd21190    6 QKKTFTNWINShlaKLSQPIVINdLFVDIKDGTALLRLLE-VLSG-------QKLPIeSGRVLQRAHKLSNIRNALDFLT 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 398365759 488 AKGFSLVGIEGSDIVDGNKLLTLGLVWQLM 517
Cdd:cd21190   78 KRCIKLVNINSTDIVDGKPSIVLGLIWTII 107
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
411-519 2.60e-10

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: 58.53  E-value: 2.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 411 EREA---RVFTLWLNS--LDVDPPVISLFDDLKDGLILLQAYEkVMPGavdfkHVNKRPASGAeiSRFKALENTNYAVDL 485
Cdd:cd21317   27 EREAvqkKTFTKWVNShlARVTCRIGDLYTDLRDGRMLIRLLE-VLSG-----EQLPKPTKGR--MRIHCLENVDKALQF 98
                         90       100       110
                 ....*....|....*....|....*....|....
gi 398365759 486 GRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21317   99 LKEQKVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
407-525 3.92e-10

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: 57.85  E-value: 3.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 407 DAEGER-EARVFTLWLNS--LDVDPPVISLFDDLKDGLILLqAYEKVMPGAvDFKHVNKRPASgaeisRFKALENTNYAV 483
Cdd:cd21311    9 DAQWKRiQQNTFTRWANEhlKTANKHIADLETDLSDGLRLI-ALVEVLSGK-KFPKFNKRPTF-----RSQKLENVSVAL 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 398365759 484 D-LGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMrRNISITM 525
Cdd:cd21311   82 KfLEEDEGIKIVNIDSSDIVDGKLKLILGLIWTLI-LHYSISM 123
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
411-519 8.06e-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: 8.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 411 EREA---RVFTLWLNSL--DVDPPVISLFDDLKDGLILLQAYEKVMPGAVdfkhvnKRPASGaeISRFKALENTNYAVDL 485
Cdd:cd21193   12 ERINiqkKTFTKWINSFleKANLEIGDLFTDLSDGKLLLKLLEIISGEKL------GKPNRG--RLRVQKIENVNKALAF 83
                         90       100       110
                 ....*....|....*....|....*....|....
gi 398365759 486 GRAKgFSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21193   84 LKTK-VRLENIGAEDIVDGNPRLILGLIWTIILR 116
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
411-519 9.58e-10

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: 56.14  E-value: 9.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 411 EREARVFTLWLN-SLDV-DPPVISLFDDLKDGLILLQAYEKVMpgAVDFKHVNKRPasgaeISRFKALENTNYAVDLGRA 488
Cdd:cd21227    3 EIQKNTFTNWVNeQLKPtGMSVEDLATDLEDGVKLIALVEILQ--GRKLGRVIKKP-----LNQHQKLENVTLALKAMAE 75
                         90       100       110
                 ....*....|....*....|....*....|.
gi 398365759 489 KGFSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21227   76 DGIKLVNIGNEDIVNGNLKLILGLIWHLILR 106
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
407-517 1.52e-09

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


Pssm-ID: 409085  Cd Length: 128  Bit Score: 56.15  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 407 DAEGEREARVFTLWLNS--LDVDPPVISLFDDLKDGLILLQAYEkVMPGavdfkhvNKRPASGAEIsRFKALENTNYAVD 484
Cdd:cd21236   12 DERDKVQKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLE-VLSG-------DTLPREKGRM-RFHRLQNVQIALD 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 398365759 485 LGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLM 517
Cdd:cd21236   83 YLKRRQVKLVNIRNDDITDGNPKLTLGLIWTII 115
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
177-257 7.60e-09

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: 53.83  E-value: 7.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 177 RDGLVLSKLIndsvpDTIDTRVLNwPKKGKELNNFQASENANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIR 256
Cdd:cd21227   32 EDGVKLIALV-----EILQGRKLG-RVIKKPLNQHQKLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLIL 105

                 .
gi 398365759 257 R 257
Cdd:cd21227  106 R 106
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
141-255 8.55e-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: 53.68  E-value: 8.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVLAGDQDigdllpfPTDTFQLFDECRDGLVLSKLIndsvpDTIDTRVLnwpKKGKELNNFQASENANIV 220
Cdd:cd21242    6 QKRTFTNWINSQLAKHSP-------PSVVSDLFTDIQDGHRLLDLL-----EVLSGQQL---PREKGHNVFQCRSNIETA 70
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 398365759 221 INSAKAIGCVVVNVHSEDIIEGREHLILGLIWQII 255
Cdd:cd21242   71 LSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTII 105
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
130-257 1.91e-08

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


Pssm-ID: 409042  Cd Length: 116  Bit Score: 52.68  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 130 QTGTTHTINEE----ERREFTKHINSVLA-GDQDIGDLlpfptdtfqlFDECRDGLVLSKLIndsvpDTIDTRVLNWPKK 204
Cdd:cd21193    2 EKGRIRALQEEriniQKKTFTKWINSFLEkANLEIGDL----------FTDLSDGKLLLKLL-----EIISGEKLGKPNR 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 398365759 205 GKElnNFQASENANIVINSAKAiGCVVVNVHSEDIIEGREHLILGLIWQIIRR 257
Cdd:cd21193   67 GRL--RVQKIENVNKALAFLKT-KVRLENIGAEDIVDGNPRLILGLIWTIILR 116
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
417-517 2.24e-08

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: 52.49  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 417 FTLWLNS--LDVDPPVISLFDDLKDGLILLqAYEKVMPGAVDFKHVNKRPASgaeisRFKALENTNYAVDLGRAKGFSLV 494
Cdd:cd21228    9 FTRWCNEhlKCVNKRIYNLETDLSDGLRLI-ALLEVLSQKRMYKKYNKRPTF-----RQMKLENVSVALEFLERESIKLV 82
                         90       100
                 ....*....|....*....|...
gi 398365759 495 GIEGSDIVDGNKLLTLGLVWQLM 517
Cdd:cd21228   83 SIDSSAIVDGNLKLILGLIWTLI 105
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
541-637 2.62e-08

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 52.30  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 541 LKWAQDQVTK-GGKNSTIRSFKDQaLSNAHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANARLAISIARKLGALIWLVP 619
Cdd:cd21218   16 LRWVNYHLKKaGPTKKRVTNFSSD-LKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYFLTP 94
                         90
                 ....*....|....*...
gi 398365759 620 EDINEVRARLIITFIASL 637
Cdd:cd21218   95 EDIVSGNPRLNLAFVATL 112
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
139-255 3.22e-08

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: 51.99  E-value: 3.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 139 EEER---REFTKHINSVLAGDQDigdllpfPTDTFQLFDECRDGLVLSKLIndsvpdtidtRVLNWPK----KGKELNNF 211
Cdd:cd21241    1 EQERvqkKTFTNWINSYLAKRKP-------PMKVEDLFEDIKDGTKLLALL----------EVLSGEKlpceKGRRLKRV 63
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 398365759 212 QASENANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQII 255
Cdd:cd21241   64 HFLSNINTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTII 107
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
288-375 3.48e-08

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: 51.47  E-value: 3.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 288 PPEQILLRWFNYHLKqanwNRRVTNFSKDVSDGENYTILLNQLDPALCS-KAPLQTTDLMERAEQVLQNAE-KLDCRKYL 365
Cdd:cd21184    1 SGKSLLLEWVNSKIP----EYKVKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEeELGIPKII 76
                         90
                 ....*....|
gi 398365759 366 TPSSLVAGNP 375
Cdd:cd21184   77 TPEDMVSPNV 86
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
411-518 3.94e-08

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: 52.70  E-value: 3.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 411 EREARVFTLWLNS-----------LDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRpasgaEISRFKALENT 479
Cdd:cd21324   23 EEEKYAFVNWINKalendpdckhvIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKK-----KLTPFTIQENL 97
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 398365759 480 NYAVDLGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMR 518
Cdd:cd21324   98 NLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 136
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
415-517 4.73e-08

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: 51.37  E-value: 4.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 415 RVFTLWLNSL---DVDPPVIS-LFDDLKDGLILLQAYEkVMpgavdfkhvnkrpaSGAEISR------FKALENTNYAVD 484
Cdd:cd21242    8 RTFTNWINSQlakHSPPSVVSdLFTDIQDGHRLLDLLE-VL--------------SGQQLPRekghnvFQCRSNIETALS 72
                         90       100       110
                 ....*....|....*....|....*....|...
gi 398365759 485 LGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLM 517
Cdd:cd21242   73 FLKNKSIKLINIHVPDIIEGKPSIILGLIWTII 105
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
411-517 4.79e-08

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: 51.81  E-value: 4.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 411 EREA---RVFTLWLNSL--DVDPP--VISLFDDLKDGLILLQAYEKVMPGAVDFKHvnkRPASgaeiSRFKALENTNYAV 483
Cdd:cd21191    1 ERENvqkRTFTRWINLHleKCNPPleVKDLFVDIQDGKILMALLEVLSGQNLLQEY---KPSS----HRIFRLNNIAKAL 73
                         90       100       110
                 ....*....|....*....|....*....|....
gi 398365759 484 DLGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLM 517
Cdd:cd21191   74 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNII 107
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
407-517 5.19e-08

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


Pssm-ID: 409086  Cd Length: 118  Bit Score: 51.57  E-value: 5.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 407 DAEGEREARVFTLWLNS--LDVDPPVISLFDDLKDGLILLQAYEkVMPGAvdfkhvnKRPASGAEIsRFKALENTNYAVD 484
Cdd:cd21237    1 DERDRVQKKTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLE-VLSGV-------KLPREKGRM-RFHRLQNVQIALD 71
                         90       100       110
                 ....*....|....*....|....*....|...
gi 398365759 485 LGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLM 517
Cdd:cd21237   72 FLKQRQVKLVNIRNDDITDGNPKLTLGLIWTII 104
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
141-255 7.50e-08

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: 51.03  E-value: 7.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVLAGdqdigdlLPFPTDTFQLFDECRDGLVLSKLIndsvpdtidtRVLNWPK----KGKELNNFQASEN 216
Cdd:cd21190    6 QKKTFTNWINSHLAK-------LSQPIVINDLFVDIKDGTALLRLL----------EVLSGQKlpieSGRVLQRAHKLSN 68
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 398365759 217 ANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQII 255
Cdd:cd21190   69 IRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTII 107
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
411-518 1.18e-07

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: 51.60  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 411 EREARVFTLWLNS-----------LDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRpasgaEISRFKALENT 479
Cdd:cd21325   23 EEEKYAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKK-----KLTPFIIQENL 97
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 398365759 480 NYAVDLGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMR 518
Cdd:cd21325   98 NLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 136
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
407-517 1.28e-07

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


Pssm-ID: 409084  Cd Length: 119  Bit Score: 50.41  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 407 DAEGEREARVFTLWLNS--LDVDPPVISLFDDLKDGLILLQAYEkVMPGavdfkhvNKRPASGAEIsRFKALENTNYAVD 484
Cdd:cd21235    1 DERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLE-VLSG-------DSLPREKGRM-RFHKLQNVQIALD 71
                         90       100       110
                 ....*....|....*....|....*....|...
gi 398365759 485 LGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLM 517
Cdd:cd21235   72 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 104
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
141-257 1.38e-07

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: 51.18  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVLAgdqdigdllPFPTDTFQLFDECRDGLVLSKLIndsvpDTIDTRVLNWPKKGKElnNFQASENANIV 220
Cdd:cd21318   39 QKKTFTKWVNSHLA---------RVPCRINDLYTDLRDGYVLTRLL-----EVLSGEQLPKPTRGRM--RIHSLENVDKA 102
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 398365759 221 INSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRR 257
Cdd:cd21318  103 LQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIILR 139
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
411-519 1.55e-07

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: 51.20  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 411 EREA---RVFTLWLNS--LDVDPPVISLFDDLKDGLILLQAYEkVMPGavdfkhvNKRPASGAEISRFKALENTNYAVDL 485
Cdd:cd21316   49 EREAvqkKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLE-VLSG-------ERLPKPTKGRMRIHCLENVDKALQF 120
                         90       100       110
                 ....*....|....*....|....*....|....
gi 398365759 486 GRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21316  121 LKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
413-519 2.30e-07

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 49.40  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 413 EARVFTLWLNS--LDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHvNKRPASgaeisRFKALENTNYAVDLGRAKG 490
Cdd:cd21183    5 QANTFTRWCNEhlKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSY-NRRPAF-----QQHYLENVSTALKFIEADH 78
                         90       100
                 ....*....|....*....|....*....
gi 398365759 491 FSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21183   79 IKLVNIGSGDIVNGNIKLILGLIWTLILH 107
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
424-518 3.45e-07

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: 49.06  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 424 LDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRpasgAEISRFKALENTNYAVDLGRAKGFSLVGIEGSDIVD 503
Cdd:cd21293   24 LPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTK----KVLNPWERNENHTLCLNSAKAIGCSVVNIGTQDLAE 99
                         90
                 ....*....|....*
gi 398365759 504 GNKLLTLGLVWQLMR 518
Cdd:cd21293  100 GRPHLVLGLISQIIK 114
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
417-519 6.23e-07

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


Pssm-ID: 409074  Cd Length: 111  Bit Score: 48.30  E-value: 6.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 417 FTLWLNSL---DVDPPVISLFDDLKDGLILLQAYEKVMPGAVDfKHVNKRPASgaeisRFKALENTNYAVD-LGRAKGFS 492
Cdd:cd21225    9 FTAWVNSVlekRGIPKISDLATDLSDGVRLIFFLELVSGKKFP-KKFDLEPKN-----RIQMIQNLHLAMLfIEEDLKIR 82
                         90       100
                 ....*....|....*....|....*..
gi 398365759 493 LVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21225   83 VQGIGAEDFVDNNKKLILGLLWTLYRK 109
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
141-257 6.59e-07

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


Pssm-ID: 409064  Cd Length: 107  Bit Score: 48.17  E-value: 6.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVLAG-DQDIGDLLpfpTDTfqlfdecRDGLVLSKLInDSVPDTIDTRVLNWPKKgkelnNFQASENANI 219
Cdd:cd21215    5 QKKTFTKWLNTKLSSrGLSITDLV---TDL-------SDGVRLIQLL-EIIGDESLGRYNKNPKM-----RVQKLENVNK 68
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 398365759 220 VINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRR 257
Cdd:cd21215   69 ALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILR 106
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
422-517 1.09e-06

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


Pssm-ID: 409072  Cd Length: 113  Bit Score: 47.59  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 422 NSLD-VDPPVISLFDDLKDGLILLQAYEkVMPGAVDFKHVNKRPAsgaeISRFKALENTNYAV----DLGRAKGFSLVGI 496
Cdd:cd21223   17 TPLDeFDFAVTNLAVDLRDGVRLCRLVE-LLTGDWSLLSKLRVPA----ISRLQKLHNVEVALkalkEAGVLRGGDGGGI 91
                         90       100
                 ....*....|....*....|.
gi 398365759 497 EGSDIVDGNKLLTLGLVWQLM 517
Cdd:cd21223   92 TAKDIVDGHREKTLALLWRII 112
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
141-255 1.27e-06

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: 47.40  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVL-AGDQDIGDLlpfptdtfqlFDECRDGLVLSKLINDSVPDTIdtrvlnwPK-KGKelNNFQASENAN 218
Cdd:cd21188    4 QKKTFTKWVNKHLiKARRRVVDL----------FEDLRDGHNLISLLEVLSGESL-------PReRGR--MRFHRLQNVQ 64
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 398365759 219 IVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQII 255
Cdd:cd21188   65 TALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTII 101
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
141-255 1.96e-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: 46.61  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVL--AGDQDIGDLlpfptdtfqlFDECRDGLVLSKLIndsvpDTIDTRVLNwPKKGK----ELNN---- 210
Cdd:cd21186    3 QKKTFTKWINSQLskANKPPIKDL----------FEDLRDGTRLLALL-----EVLTGKKLK-PEKGRmrvhHLNNvnra 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 398365759 211 FQASENANIVInsakaigcvvVNVHSEDIIEGREHLILGLIWQII 255
Cdd:cd21186   67 LQVLEQNNVKL----------VNISSNDIVDGNPKLTLGLVWSII 101
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
413-525 5.75e-06

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: 46.23  E-value: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 413 EARVFTLWLNS--LDVDPPVISLFDDLKDGLILLQAYEkVMPGAVDFKHVNKRPASgaeisRFKALENTNYAVDLGRAKG 490
Cdd:cd21308   21 QQNTFTRWCNEhlKCVSKRIANLQTDLSDGLRLIALLE-VLSQKKMHRKHNQRPTF-----RQMQLENVSVALEFLDRES 94
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 398365759 491 FSLVGIEGSDIVDGNKLLTLGLVWQLMrRNISITM 525
Cdd:cd21308   95 IKLVSIDSKAIVDGNLKLILGLIWTLI-LHYSISM 128
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
141-257 6.68e-06

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


Pssm-ID: 409166  Cd Length: 132  Bit Score: 45.82  E-value: 6.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVLAGDQ-DIGDLlpfptdtfqlFDECRDGLVLSKLIndsvpDTIDTRVLNWPKKGKElnNFQASENANI 219
Cdd:cd21317   32 QKKTFTKWVNSHLARVTcRIGDL----------YTDLRDGRMLIRLL-----EVLSGEQLPKPTKGRM--RIHCLENVDK 94
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 398365759 220 VINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRR 257
Cdd:cd21317   95 ALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
288-376 1.02e-05

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


Pssm-ID: 409079  Cd Length: 103  Bit Score: 44.68  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 288 PPEQILLRWFNYHLKQANwnrrVTNFSKDVSDGENYTILLNQLDPALCSKAPL-QTTDLMERAEQVLQNAEK-LDCRKYL 365
Cdd:cd21230    1 TPKQRLLGWIQNKIPQLP----ITNFTTDWNDGRALGALVDSCAPGLCPDWETwDPNDALENATEAMQLAEDwLGVPQLI 76
                         90
                 ....*....|.
gi 398365759 366 TPSSLVagNPK 376
Cdd:cd21230   77 TPEEII--NPN 85
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
413-525 1.04e-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: 45.46  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 413 EARVFTLWLNS--LDVDPPVISLFDDLKDGLILLQAYEkVMPGAVDFKHVNKRPASgaeisRFKALENTNYAVDLGRAKG 490
Cdd:cd21309   18 QQNTFTRWCNEhlKCVNKRIGNLQTDLSDGLRLIALLE-VLSQKRMYRKYHQRPTF-----RQMQLENVSVALEFLDRES 91
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 398365759 491 FSLVGIEGSDIVDGNKLLTLGLVWQLMrRNISITM 525
Cdd:cd21309   92 IKLVSIDSKAIVDGNLKLILGLVWTLI-LHYSISM 125
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
415-519 1.50e-05

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: 44.75  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 415 RVFTLWLNSL----DVDPPVISLFDDLKDGLILLQAYEKVMPGAVdfkhvnKRPASGAeiSRFKALENTNYAVDLGRAK- 489
Cdd:cd21247   23 KTFTKWMNNVfsknGAKIEITDIYTELKDGIHLLRLLELISGEQL------PRPSRGK--MRVHFLENNSKAITFLKTKv 94
                         90       100       110
                 ....*....|....*....|....*....|
gi 398365759 490 GFSLVGIEgsDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21247   95 PVKLIGPE--NIVDGDRTLILGLIWIIILR 122
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
413-519 1.83e-05

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


Pssm-ID: 409061  Cd Length: 105  Bit Score: 44.11  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 413 EARVFTLWLNSL----DVDPPVISLFDDLKDGLILLQAYEKVMPGAVDfkHVNKRPASgaeisRFKALENTNYAVDLGRA 488
Cdd:cd21212    1 EIEIYTDWANHYlekgGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVP--GIHSRPKT-----RAQKLENIQACLQFLAA 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 398365759 489 KGFSLVGIEGSDIVDGNKLLTLGLVWQLMRR 519
Cdd:cd21212   74 LGVDVQGITAEDIVDGNLKAILGLFFSLSRY 104
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
278-374 3.04e-05

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


Pssm-ID: 409163  Cd Length: 115  Bit Score: 43.52  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 278 DETLEQFLRLPPEQILLRWFNYHLKQAnwnrRVTNFSKDVSDGENYTILLNQLDPALC----SKAPLQTtdlMERAEQVL 353
Cdd:cd21314    1 DEDEEDARKQTPKQRLLGWIQNKVPQL----PITNFNRDWQDGKALGALVDNCAPGLCpdweSWDPNQP---VQNAREAM 73
                         90       100
                 ....*....|....*....|..
gi 398365759 354 QNAEK-LDCRKYLTPSSLVAGN 374
Cdd:cd21314   74 QQADDwLGVPQVIAPEEIVDPN 95
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
413-525 3.87e-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: 3.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 413 EARVFTLWLNS--LDVDPPVISLFDDLKDGLILLQAYEkVMPGAVDFKHVNKRPASgaeisRFKALENTNYAVDLGRAKG 490
Cdd:cd21310   17 QQNTFTRWCNEhlKCVQKRLNDLQKDLSDGLRLIALLE-VLSQKKMYRKYHPRPNF-----RQMKLENVSVALEFLDREH 90
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 398365759 491 FSLVGIEGSDIVDGNKLLTLGLVWQLMrRNISITM 525
Cdd:cd21310   91 IKLVSIDSKAIVDGNLKLILGLIWTLI-LHYSISM 124
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
141-268 4.08e-05

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: 43.43  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSvlagdqdigDLLPFPTDTFQLFDECRDGLVLSKLINDSVPDTIdtrvlnwPKKGKELNnFQASENANIV 220
Cdd:cd21236   18 QKKTFTKWINQ---------HLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTL-------PREKGRMR-FHRLQNVQIA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 398365759 221 INSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRGLLSKIDIKLH 268
Cdd:cd21236   81 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
141-257 4.25e-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: 43.12  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVLAG-DQDIGDLlpfptdtfqlFDECRDGLVLSKLIndsvpDTIDTRVLNWPKKGKElnNFQASENANI 219
Cdd:cd21246   17 QKKTFTKWVNSHLARvGCRINDL----------YTDLRDGRMLIKLL-----EVLSGERLPKPTKGKM--RIHCLENVDK 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 398365759 220 VINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRR 257
Cdd:cd21246   80 ALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
276-378 8.91e-05

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: 42.46  E-value: 8.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 276 EDDETLEQFLRLP-PEQILLRWFNYHLKqanwNRRVTNFSKDVSDGENYTILLNQLDPALCSK-APLQTTDLMERAEQVL 353
Cdd:cd21315    3 EGEDDGPDDGKGPtPKQRLLGWIQSKVP----DLPITNFTNDWNDGKAIGALVDALAPGLCPDwEDWDPKDAVKNAKEAM 78
                         90       100
                 ....*....|....*....|....*.
gi 398365759 354 QNAEK-LDCRKYLTPSSLVagNPKLN 378
Cdd:cd21315   79 DLAEDwLDVPQLIKPEEMV--NPKVD 102
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
172-257 1.05e-04

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 42.08  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 172 LFDECRDGLVLSKLIndsvpDTIDTRVLNWPKKGKELNNFQASENANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLI 251
Cdd:cd21183   27 LATDFSDGLCLIALL-----ENLSTRPLKRSYNRRPAFQQHYLENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLI 101

                 ....*.
gi 398365759 252 WQIIRR 257
Cdd:cd21183  102 WTLILH 107
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
141-255 1.05e-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: 41.83  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVLA--GDQDIGDLlpfptdtfqlFDECRDGLVLSKLINDSVPDTIdtrvlnwpKKGKELNNFQASENAN 218
Cdd:cd21231    7 QKKTFTKWINAQFAkfGKPPIEDL----------FTDLQDGRRLLELLEGLTGQKL--------VKEKGSTRVHALNNVN 68
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 398365759 219 IVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQII 255
Cdd:cd21231   69 KALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
140-255 1.28e-04

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: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 140 EERREFTKHINSVL--AGDQdIGDLlpfPTDTfqlfdecRDGLVLSKLIndsvpDTIDTRVLNWPKKGKElnNFQASENA 217
Cdd:cd21214    5 QQRKTFTAWCNSHLrkAGTQ-IENI---EEDF-------RDGLKLMLLL-----EVISGERLPKPERGKM--RFHKIANV 66
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 398365759 218 NIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQII 255
Cdd:cd21214   67 NKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
141-257 3.80e-04

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


Pssm-ID: 409061  Cd Length: 105  Bit Score: 40.26  E-value: 3.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVLA--GDQD-IGDLlpfPTDtfqlfdeCRDGLVLSKLINDSVPDTIDtrvlnwPKKGKELNNFQASENA 217
Cdd:cd21212    1 EIEIYTDWANHYLEkgGHKRiITDL---QKD-------LGDGLTLVNLIEAVAGEKVP------GIHSRPKTRAQKLENI 64
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 398365759 218 NIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRR 257
Cdd:cd21212   65 QACLQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRY 104
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
177-254 7.42e-04

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 39.59  E-value: 7.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365759 177 RDGLVLSKLINDSVPDTIDTRvlnwpKKGKELNNFQASENANIVINSAKAIGCVVVnVHSEDIIEGREHLILGLIWQI 254
Cdd:cd21218   41 KDGEVYALLLHSLAPELCDKE-----LVLEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPEDIVSGNPRLNLAFVATL 112
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
171-257 1.31e-03

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: 39.60  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 171 QLFDECRDGLVLSKLIND-SVPdtIDTRVLNWPKKGKELNNFQASENANIVINSAK-AIGCVVVNVHSEDIIEGREHLIL 248
Cdd:cd21331   42 HLYGDLQDALVILQLYEKiKVP--VDWNKVNKPPYPKLGANMKKLENCNYAVELGKhPAKFSLVGIGGQDLNDGNPTLTL 119

                 ....*....
gi 398365759 249 GLIWQIIRR 257
Cdd:cd21331  120 ALVWQLMRR 128
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
141-255 1.45e-03

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: 38.85  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINS-VLAGDQDIGDLlpfptdtfqlFDECRDGLVLSKLINDSVPDTIdtrvlnwPKKGKELNnFQASENANI 219
Cdd:cd21235    7 QKKTFTKWVNKhLIKAQRHISDL----------YEDLRDGHNLISLLEVLSGDSL-------PREKGRMR-FHKLQNVQI 68
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 398365759 220 VINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQII 255
Cdd:cd21235   69 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 104
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
141-257 2.33e-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: 39.26  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVLAgdqdigdllPFPTDTFQLFDECRDGLVLSKLIndsvpDTIDTRVLNWPKKGKElnNFQASENANIV 220
Cdd:cd21316   54 QKKTFTKWVNSHLA---------RVSCRITDLYMDLRDGRMLIKLL-----EVLSGERLPKPTKGRM--RIHCLENVDKA 117
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 398365759 221 INSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRR 257
Cdd:cd21316  118 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
286-336 2.56e-03

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


Pssm-ID: 409078  Cd Length: 105  Bit Score: 37.75  E-value: 2.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398365759 286 RLPPEQILLRWFNYHLKQANwnrrVTNFSKDVSDGENYTILLNQLDPALCS 336
Cdd:cd21229    1 KIPPKKLMLAWLQAVLPELK----ITNFSTDWNDGIALSALLDYCKPGLCP 47
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
171-257 2.71e-03

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: 38.04  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 171 QLFDECRDGLVLSKLInDSVPDTIDTRVLNWPKKGKELNNFQASENANIVINSAK-AIGCVVVNVHSEDIIEGREHLILG 249
Cdd:cd21329   26 HLYSDLCDALVIFQLY-EMTRVPVDWGHVNKPPYPALGGNMKKIENCNYAVELGKnKAKFSLVGIAGSDLNEGNKTLTLA 104

                 ....*...
gi 398365759 250 LIWQIIRR 257
Cdd:cd21329  105 LIWQLMRR 112
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
177-251 3.00e-03

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


Pssm-ID: 409069  Cd Length: 105  Bit Score: 37.63  E-value: 3.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365759 177 RDGLVLSKLIndsvpDTIDTRVLNWPKKGKELNNFQASENANIVINSAKAIGCVVvNVHSEDIIEGREHLILGLI 251
Cdd:cd21220   32 STGLFLLDLL-----AAIDPGAVDYDLVTEGETDEEKEQNAKYAISLARKIGAVI-FLLWEDIVEVKPKMILTFV 100
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
540-637 4.08e-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: 37.50  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 540 ILKWAQDQVTKGGKNSTIRSFK-DQALSNAHFLLdvLNGIAPGYVDYDLVTpgntEEERYANARLAISIARKLGALIWLV 618
Cdd:cd21296   15 LLKWMNFHLKKAGYKKTVTNFSsDVKDAEAYAYL--LNVLAPEHCDPATLE----AKDPLERAKLVLEQAEKMNCKRYLT 88
                         90
                 ....*....|....*....
gi 398365759 619 PEDINEVRARLIITFIASL 637
Cdd:cd21296   89 AKDIVEGSANLNLAFVAQI 107
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
141-257 4.20e-03

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: 37.82  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 141 ERREFTKHINSVLAGDQDIGDLlpfpTDtfqLFDECRDGLVLSKLIndsvpDTIDTRVLNWPKKGKELNNFqasenaniV 220
Cdd:cd21247   21 QKKTFTKWMNNVFSKNGAKIEI----TD---IYTELKDGIHLLRLL-----ELISGEQLPRPSRGKMRVHF--------L 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 398365759 221 INSAKAIGCVVVNVH-----SEDIIEGREHLILGLIWQIIRR 257
Cdd:cd21247   81 ENNSKAITFLKTKVPvkligPENIVDGDRTLILGLIWIIILR 122
CH_VAV1 cd21262
calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the ...
420-478 4.96e-03

calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV1 protein.


Pssm-ID: 409111  Cd Length: 120  Bit Score: 37.61  E-value: 4.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365759 420 WLNSLDVDPP----------VISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRPasgaEISRFKALEN 478
Cdd:cd21262    9 WLIQCRVLPPnhrvtwdsaqVCDLAQALRDGVLLCQLLNNLLPHAVNLREINLRP----QMSQFLCLKN 73
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
171-261 5.20e-03

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: 37.66  E-value: 5.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 171 QLFDECRDGLVLSKLIND-SVPdtIDTRVLNWPKKGKELNNFQASENANIVINSAK-AIGCVVVNVHSEDIIEGREHLIL 248
Cdd:cd21330   33 HLYSDLSDALVIFQLYEKiKVP--VDWNRVNKPPYPKLGENMKKLENCNYAVELGKnKAKFSLVGIAGQDLNEGNRTLTL 110
                         90
                 ....*....|...
gi 398365759 249 GLIWQIIRRGLLS 261
Cdd:cd21330  111 ALIWQLMRRYTLN 123
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
295-382 6.83e-03

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: 36.70  E-value: 6.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 295 RWFNYHLKQANwnRRVTNFSKDVSDGENYTILLNQLD----PALCSKAPLQTTDLMERAEQVLqnaEKLDCRKY----LT 366
Cdd:cd21228   11 RWCNEHLKCVN--KRIYNLETDLSDGLRLIALLEVLSqkrmYKKYNKRPTFRQMKLENVSVAL---EFLERESIklvsID 85
                         90
                 ....*....|....*.
gi 398365759 367 PSSLVAGNPKLNLAFV 382
Cdd:cd21228   86 SSAIVDGNLKLILGLI 101
EF-hand_7 pfam13499
EF-hand domain pair;
23-80 7.09e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 35.69  E-value: 7.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365759   23 EKFRAIDLDDKGWVEK---QQALEAVSKDGDATYDEARETLKHVGVDASGRVELDDYVGLV 80
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVeelKKLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
290-385 7.55e-03

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: 36.79  E-value: 7.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 290 EQILLRWFNYHLKQANWNRRVTNF-SKDVSDGENYTILLNQLDPA-----LCSKAPLQTTDLMERAEQVLQNAEKLDCRK 363
Cdd:cd21334    3 DDIIVNWVNRTLSEAGKSTSIQNFkDKTISSSLAVVDLIDAIQPGcinydLVKTGNLTDDDKLDNAKYAVSMARKIGARV 82
                         90       100
                 ....*....|....*....|..
gi 398365759 364 YLTPSSLVAGNPKLNLAFVAHL 385
Cdd:cd21334   83 YALPEDLVEVKPKMVMTVFACL 104
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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