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Conserved domains on  [gi|19115207|ref|NP_594295|]
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alpha-actinin [Schizosaccharomyces pombe]

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];
1-616 0e+00

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


:

Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 880.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   1 MQANQWQSVQNRTFTKWFNTKLSSRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIK 80
Cdd:COG5069   1 MEAKKWQKVQKKTFTKWTNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207  81 SKGMPLTNIGPADIVDGNLKLILGLIWTLILRFTIADINEEG-LTAKEGLLLWCQRKTANYHPEVDVQDFTRSWTNGLAF 159
Cdd:COG5069  81 GKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGeLTKHINLLLWCDEDTGGYKPEVDTFDFFRSWRDGLAF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 160 CALIHQHRPDLLDYNKLD--KKNHRANMQLAFDIAQKSIGIPRLIEVEDVCDVDRPDERSIMTYVAEYFHAFSTLDKVET 237
Cdd:COG5069 161 SALIHDSRPDTLDPNVLDlqKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRFGLLEKIDI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 238 AARRVERFTEVLMSTHDMKIDYESRMKRLLGSIARMQEYWHTVQFENNYTDVKSHSNNFAKFKATEKREWVkEKIDLESL 317
Cdd:COG5069 241 ALHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCSRAPL-ETTDLHSL 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 318 LGTIQTNLKTYQLRKYEPPAGLKIVDLERQWKDFLSEEAnQSKLINTHMREIKE-SMRIAFADRANSFSKMLSTISNEIT 396
Cdd:COG5069 320 AGQILQNAEKYDCRKYLPPAGNPKLDLAFVAHLFNTHPG-QEPLEEEEKPEIEEfDAEGEFEARVFTFWLNSLDVSPEIT 398

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 397 NLQGDWRDQLDHVEFLQEHLGPLEVELASVKVLYdncfQAGIEENDYTMFSYEDLEHEFGITANIIANKIKYLENELLER 476
Cdd:COG5069 399 NLFGDLRDQLILLQALSKKLMPMTVTHKLVKKQP----ASGIEENRFKAFENENYAVDLGITEGFSLVGIKGLEILDGIR 474

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 477 EKRTLSKQELDGITKVFRHFEKKKSNMLNEVEFYAALASLGLVYDTEEGTALFHRAANSEEGVTYERFTEIVMEELEDRD 556
Cdd:COG5069 475 LKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVFYLDVLKGIHSELVDYD 554

                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 557 SARQVLYAFCDVADGKSYVTSDDLLRSQVrpNIVKFLECNMNKHSEGLDYLTWIKQLLAE 616
Cdd:COG5069 555 LVTRGFTEFDDIADARSLAISSKILRSLG--AIIKFLPEDINGVRPRLDVLTFIESLMAD 612
 
Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-616 0e+00

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 880.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   1 MQANQWQSVQNRTFTKWFNTKLSSRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIK 80
Cdd:COG5069   1 MEAKKWQKVQKKTFTKWTNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207  81 SKGMPLTNIGPADIVDGNLKLILGLIWTLILRFTIADINEEG-LTAKEGLLLWCQRKTANYHPEVDVQDFTRSWTNGLAF 159
Cdd:COG5069  81 GKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGeLTKHINLLLWCDEDTGGYKPEVDTFDFFRSWRDGLAF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 160 CALIHQHRPDLLDYNKLD--KKNHRANMQLAFDIAQKSIGIPRLIEVEDVCDVDRPDERSIMTYVAEYFHAFSTLDKVET 237
Cdd:COG5069 161 SALIHDSRPDTLDPNVLDlqKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRFGLLEKIDI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 238 AARRVERFTEVLMSTHDMKIDYESRMKRLLGSIARMQEYWHTVQFENNYTDVKSHSNNFAKFKATEKREWVkEKIDLESL 317
Cdd:COG5069 241 ALHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCSRAPL-ETTDLHSL 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 318 LGTIQTNLKTYQLRKYEPPAGLKIVDLERQWKDFLSEEAnQSKLINTHMREIKE-SMRIAFADRANSFSKMLSTISNEIT 396
Cdd:COG5069 320 AGQILQNAEKYDCRKYLPPAGNPKLDLAFVAHLFNTHPG-QEPLEEEEKPEIEEfDAEGEFEARVFTFWLNSLDVSPEIT 398

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 397 NLQGDWRDQLDHVEFLQEHLGPLEVELASVKVLYdncfQAGIEENDYTMFSYEDLEHEFGITANIIANKIKYLENELLER 476
Cdd:COG5069 399 NLFGDLRDQLILLQALSKKLMPMTVTHKLVKKQP----ASGIEENRFKAFENENYAVDLGITEGFSLVGIKGLEILDGIR 474

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 477 EKRTLSKQELDGITKVFRHFEKKKSNMLNEVEFYAALASLGLVYDTEEGTALFHRAANSEEGVTYERFTEIVMEELEDRD 556
Cdd:COG5069 475 LKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVFYLDVLKGIHSELVDYD 554

                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 557 SARQVLYAFCDVADGKSYVTSDDLLRSQVrpNIVKFLECNMNKHSEGLDYLTWIKQLLAE 616
Cdd:COG5069 555 LVTRGFTEFDDIADARSLAISSKILRSLG--AIIKFLPEDINGVRPRLDVLTFIESLMAD 612
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 115-230 5.01e-79

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


Pssm-ID: 409140  Cd Length: 115  Bit Score: 245.52  E-value: 5.01e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 115 IADINEEGLTAKEGLLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQK 194
Cdd:cd21291   1 IADINEEGLTAKEGLLLWCQRKTAGYD-EVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASK 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19115207 195 SIGIPRLIEVEDVCDVDRPDERSIMTYVAEYFHAFS 230
Cdd:cd21291  80 EIGIPQLLDVEDVCDVAKPDERSIMTYVAYYFHAFS 115
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 123-231 4.81e-29

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: 111.22  E-value: 4.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   123 LTAKEGLLLWCQRKTANYHPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKK--NHRANMQLAFDIAQKSIGIPR 200
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 19115207   201 -LIEVEDVCDvdrPDERSIMTYVAEYFHAFST 231
Cdd:pfam00307  81 vLIEPEDLVE---GDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 12-112 4.39e-17

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 76.97  E-value: 4.39e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207     12 RTFTKWFNTKLSSRDLPSVFDLRKDLSDGIL-LIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMPLTNIG 90
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVAlCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 19115207     91 PADIVDGNlKLILGLIWTLILR 112
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101
 
Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-616 0e+00

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 880.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   1 MQANQWQSVQNRTFTKWFNTKLSSRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIK 80
Cdd:COG5069   1 MEAKKWQKVQKKTFTKWTNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207  81 SKGMPLTNIGPADIVDGNLKLILGLIWTLILRFTIADINEEG-LTAKEGLLLWCQRKTANYHPEVDVQDFTRSWTNGLAF 159
Cdd:COG5069  81 GKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGeLTKHINLLLWCDEDTGGYKPEVDTFDFFRSWRDGLAF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 160 CALIHQHRPDLLDYNKLD--KKNHRANMQLAFDIAQKSIGIPRLIEVEDVCDVDRPDERSIMTYVAEYFHAFSTLDKVET 237
Cdd:COG5069 161 SALIHDSRPDTLDPNVLDlqKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRFGLLEKIDI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 238 AARRVERFTEVLMSTHDMKIDYESRMKRLLGSIARMQEYWHTVQFENNYTDVKSHSNNFAKFKATEKREWVkEKIDLESL 317
Cdd:COG5069 241 ALHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCSRAPL-ETTDLHSL 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 318 LGTIQTNLKTYQLRKYEPPAGLKIVDLERQWKDFLSEEAnQSKLINTHMREIKE-SMRIAFADRANSFSKMLSTISNEIT 396
Cdd:COG5069 320 AGQILQNAEKYDCRKYLPPAGNPKLDLAFVAHLFNTHPG-QEPLEEEEKPEIEEfDAEGEFEARVFTFWLNSLDVSPEIT 398

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 397 NLQGDWRDQLDHVEFLQEHLGPLEVELASVKVLYdncfQAGIEENDYTMFSYEDLEHEFGITANIIANKIKYLENELLER 476
Cdd:COG5069 399 NLFGDLRDQLILLQALSKKLMPMTVTHKLVKKQP----ASGIEENRFKAFENENYAVDLGITEGFSLVGIKGLEILDGIR 474

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 477 EKRTLSKQELDGITKVFRHFEKKKSNMLNEVEFYAALASLGLVYDTEEGTALFHRAANSEEGVTYERFTEIVMEELEDRD 556
Cdd:COG5069 475 LKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVFYLDVLKGIHSELVDYD 554

                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 557 SARQVLYAFCDVADGKSYVTSDDLLRSQVrpNIVKFLECNMNKHSEGLDYLTWIKQLLAE 616
Cdd:COG5069 555 LVTRGFTEFDDIADARSLAISSKILRSLG--AIIKFLPEDINGVRPRLDVLTFIESLMAD 612
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 115-230 5.01e-79

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


Pssm-ID: 409140  Cd Length: 115  Bit Score: 245.52  E-value: 5.01e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 115 IADINEEGLTAKEGLLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQK 194
Cdd:cd21291   1 IADINEEGLTAKEGLLLWCQRKTAGYD-EVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASK 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19115207 195 SIGIPRLIEVEDVCDVDRPDERSIMTYVAEYFHAFS 230
Cdd:cd21291  80 EIGIPQLLDVEDVCDVAKPDERSIMTYVAYYFHAFS 115
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 115-230 9.27e-71

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


Pssm-ID: 409065  Cd Length: 115  Bit Score: 223.78  E-value: 9.27e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 115 IADINEEGLTAKEGLLLWCQRKTANYHPeVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQK 194
Cdd:cd21216   1 IQDISVEELSAKEGLLLWCQRKTAPYKN-VNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEK 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19115207 195 SIGIPRLIEVEDVCDVDRPDERSIMTYVAEYFHAFS 230
Cdd:cd21216  80 HLDIPKMLDAEDIVNTPRPDERSVMTYVSCYYHAFA 115
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 124-229 6.85e-56

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


Pssm-ID: 409043  Cd Length: 105  Bit Score: 184.54  E-value: 6.85e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIE 203
Cdd:cd21194   2 SAKDALLLWCQRKTAGY-PGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLD 80

                        90       100
                ....*....|....*....|....*.
gi 19115207 204 VEDVcDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21194  81 AEDV-DVARPDEKSIMTYVASYYHYF 105
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 6-113 1.79e-55

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: 183.37  E-value: 1.79e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   6 WQSVQNRTFTKWFNTKLSSRDLPsVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMP 85
Cdd:cd21215   1 WVDVQKKTFTKWLNTKLSSRGLS-ITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVK 79

                        90       100
                ....*....|....*....|....*...
gi 19115207  86 LTNIGPADIVDGNLKLILGLIWTLILRF 113
Cdd:cd21215  80 LTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 124-229 6.35e-47

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


Pssm-ID: 409097  Cd Length: 105  Bit Score: 160.25  E-value: 6.35e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIE 203
Cdd:cd21248   2 SAKDALLLWCQMKTAGY-PNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLD 80

                        90       100
                ....*....|....*....|....*.
gi 19115207 204 VEDVcDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21248  81 PEDV-NVEQPDEKSIITYVVTYYHYF 105
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 123-230 1.96e-43

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


Pssm-ID: 409098  Cd Length: 109  Bit Score: 151.17  E-value: 1.96e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 123 LTAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLI 202
Cdd:cd21249   3 RSAKEALLIWCQRKTAGY-TNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLL 81

                        90       100
                ....*....|....*....|....*...
gi 19115207 203 EVEDVCdVDRPDERSIMTYVAEYFHAFS 230
Cdd:cd21249  82 DPEDVA-VPHPDERSIMTYVSLYYHYFS 108
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
 115-239 3.13e-42

second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It 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: 409137  Cd Length: 124  Bit Score: 148.30  E-value: 3.13e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 115 IADINEEGLTAKEGLLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQK 194
Cdd:cd21288   1 IQDISVEETSAKEGLLLWCQRKTAPYR-NVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 19115207 195 SIGIPRLIEVEDVCDVDRPDERSIMTYVAEYFHAFSTLDKVETAA 239
Cdd:cd21288  80 HLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAA 124
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 115-239 7.09e-42

second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It 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: 409138  Cd Length: 124  Bit Score: 147.56  E-value: 7.09e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 115 IADINEEGLTAKEGLLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQK 194
Cdd:cd21289   1 IQDISVEETSAKEGLLLWCQRKTAPYR-NVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 19115207 195 SIGIPRLIEVEDVCDVDRPDERSIMTYVAEYFHAFSTLDKVETAA 239
Cdd:cd21289  80 YLDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAA 124
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 124-229 4.11e-41

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


Pssm-ID: 409038  Cd Length: 105  Bit Score: 144.46  E-value: 4.11e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIE 203
Cdd:cd21189   1 SAKEALLLWARRTTEGY-PGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLD 79

                        90       100
                ....*....|....*....|....*.
gi 19115207 204 VEDVcDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21189  80 PEDV-DVPEPDEKSIITYVSSLYDVF 104
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
 115-230 9.56e-41

second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It 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: 409136  Cd Length: 124  Bit Score: 144.46  E-value: 9.56e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 115 IADINEEGLTAKEGLLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQK 194
Cdd:cd21287   1 IQDISVEETSAKEGLLLWCQRKTAPYK-NVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEK 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19115207 195 SIGIPRLIEVEDVCDVDRPDERSIMTYVAEYFHAFS 230
Cdd:cd21287  80 YLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFS 115
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
 120-232 2.02e-40

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


Pssm-ID: 409168  Cd Length: 112  Bit Score: 142.84  E-value: 2.02e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 120 EEGLTAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIP 199
Cdd:cd21319   1 RETRSAKDALLLWCQMKTAGY-PNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGIT 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 19115207 200 RLIEVEDVCdVDRPDERSIMTYVAEYFHAFSTL 232
Cdd:cd21319  80 KLLDPEDVF-TENPDEKSIITYVVAFYHYFSKM 111
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
 123-229 3.78e-40

second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409092  Cd Length: 109  Bit Score: 142.07  E-value: 3.78e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 123 LTAKEGLLLWCQRKTANyHPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLI 202
Cdd:cd21243   4 GGAKKALLKWVQNAAAK-RFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLL 82

                        90       100
                ....*....|....*....|....*..
gi 19115207 203 EVEDVcDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21243  83 DPEDV-DVDKPDEKSIMTYVAQFLKKY 108
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
 112-230 2.80e-39

second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 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. It 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: 409139  Cd Length: 125  Bit Score: 140.22  E-value: 2.80e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 112 RFTIADINEEGLTAKEGLLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDI 191
Cdd:cd21290   1 RFAIQDISVEETSAKEGLLLWCQRKTAPYK-NVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEV 79

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19115207 192 AQKSIGIPRLIEVEDVCDVDRPDERSIMTYVAEYFHAFS 230
Cdd:cd21290  80 AEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFS 118
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 120-232 1.17e-38

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


Pssm-ID: 409170  Cd Length: 119  Bit Score: 138.27  E-value: 1.17e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 120 EEGLTAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIP 199
Cdd:cd21321   1 KEKKSAKDALLLWCQMKTAGY-PNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLT 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 19115207 200 RLIEVEDVcDVDRPDERSIMTYVAEYFHAFSTL 232
Cdd:cd21321  80 KLLDPEDV-NVDQPDEKSIITYVATYYHYFSKM 111
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 119-232 9.99e-38

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


Pssm-ID: 409171  Cd Length: 130  Bit Score: 136.34  E-value: 9.99e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 119 NEEGLTAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGI 198
Cdd:cd21322  12 NRETRSAKDALLLWCQMKTAGY-PEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGL 90

                        90       100       110
                ....*....|....*....|....*....|....
gi 19115207 199 PRLIEVEDVcDVDRPDERSIMTYVAEYFHAFSTL 232
Cdd:cd21322  91 TKLLDPEDV-NMEAPDEKSIITYVVSFYHYFSKM 123
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 127-230 3.33e-37

calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409188  Cd Length: 105  Bit Score: 133.95  E-value: 3.33e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 127 EGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEVED 206
Cdd:cd22198   3 EELLSWCQEQTEGY-RGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQE 81

                        90       100
                ....*....|....*....|....
gi 19115207 207 VCDVDRPDERSIMTYVAEYFHAFS 230
Cdd:cd22198  82 MASLAVPDKLSMVSYLSQFYEAFK 105
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 124-229 4.87e-36

calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409102  Cd Length: 106  Bit Score: 130.54  E-value: 4.87e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIE 203
Cdd:cd21253   1 AGIKALQQWCRQQTEGY-RDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLD 79

                        90       100
                ....*....|....*....|....*.
gi 19115207 204 VEDVCDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21253  80 AEDMVALKVPDKLSILTYVSQYYNYF 105
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 125-229 1.40e-34

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


Pssm-ID: 409041  Cd Length: 107  Bit Score: 126.77  E-value: 1.40e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 125 AKEGLLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEV 204
Cdd:cd21192   4 AEKALLKWVQAEIGKYY-GIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEV 82

                        90       100
                ....*....|....*....|....*
gi 19115207 205 EDVcDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21192  83 EDV-LVDKPDERSIMTYVSQFLRMF 106
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 124-232 4.52e-34

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


Pssm-ID: 409169  Cd Length: 108  Bit Score: 125.21  E-value: 4.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIE 203
Cdd:cd21320   2 SAKDALLLWCQMKTAGY-PNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 80

                        90       100
                ....*....|....*....|....*....
gi 19115207 204 VEDVcDVDRPDERSIMTYVAEYFHAFSTL 232
Cdd:cd21320  81 PEDI-SVDHPDEKSIITYVVTYYHYFSKM 108
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 125-229 4.59e-34

calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409046  Cd Length: 105  Bit Score: 124.96  E-value: 4.59e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 125 AKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEV 204
Cdd:cd21197   1 KIQALLRWCRRQCEGY-PGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDA 79

                        90       100
                ....*....|....*....|....*
gi 19115207 205 EDVCDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21197  80 EDMVTMHVPDRLSIITYVSQYYNHF 104
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 124-230 6.23e-33

calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409049  Cd Length: 107  Bit Score: 122.07  E-value: 6.23e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIE 203
Cdd:cd21200   1 SIKQMLLEWCQAKTRGY-EHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLE 79

                        90       100
                ....*....|....*....|....*...
gi 19115207 204 VEDVCDV-DRPDERSIMTYVAEYFHAFS 230
Cdd:cd21200  80 VEDMVRMgNRPDWKCVFTYVQSLYRHLR 107
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 124-230 6.79e-32

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


Pssm-ID: 409094  Cd Length: 106  Bit Score: 119.13  E-value: 6.79e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTANYHpeVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIE 203
Cdd:cd21245   3 KAIKALLNWVQRRTRKYG--VAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                        90       100
                ....*....|....*....|....*..
gi 19115207 204 VEDVCdVDRPDERSIMTYVAEYFHAFS 230
Cdd:cd21245  81 PEDVM-VDSPDEQSIMTYVAQFLEHFP 106
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 124-222 1.39e-31

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


Pssm-ID: 409047  Cd Length: 105  Bit Score: 118.30  E-value: 1.39e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKsIGIPRLIE 203
Cdd:cd21198   1 SSGQDLLEWCQEVTKGY-RGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLD 78

                        90
                ....*....|....*....
gi 19115207 204 VEDVCDVDRPDERSIMTYV 222
Cdd:cd21198  79 PADMVLLSVPDKLSVMTYL 97
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 8-112 3.28e-31

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: 117.40  E-value: 3.28e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   8 SVQNRTFTKWFNTKLSSRDLpSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNpRMRVHRLENVNKALEYIKSKgMPLT 87
Cdd:cd21193  15 NIQKKTFTKWINSFLEKANL-EIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRG-RLRVQKIENVNKALAFLKTK-VRLE 91

                        90       100
                ....*....|....*....|....*
gi 19115207  88 NIGPADIVDGNLKLILGLIWTLILR 112
Cdd:cd21193  92 NIGAEDIVDGNPRLILGLIWTIILR 116
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
 125-230 5.23e-31

calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409101  Cd Length: 107  Bit Score: 116.51  E-value: 5.23e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 125 AKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEV 204
Cdd:cd21252   1 ARRALQAWCRRQCEGY-PGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDP 79

                        90       100
                ....*....|....*....|....*.
gi 19115207 205 EDVCDVDRPDERSIMTYVAEYFHAFS 230
Cdd:cd21252  80 EDMVSMKVPDCLSIMTYVSQYYNHFS 105
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
 123-225 3.13e-30

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


Pssm-ID: 409093  Cd Length: 109  Bit Score: 114.55  E-value: 3.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 123 LTAKEGLLLWCQRKTANYHPeVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLI 202
Cdd:cd21244   4 MSARKALLLWAQEQCAKVGS-ISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLL 82

                        90       100
                ....*....|....*....|...
gi 19115207 203 EVEDVcDVDRPDERSIMTYVAEY 225
Cdd:cd21244  83 EPEDV-DVVNPDEKSIMTYVAQF 104
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 6-115 3.25e-30

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: 114.31  E-value: 3.25e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   6 WQSVQNRTFTKWFNTKLSSRDLpSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMP 85
Cdd:cd21227   1 WVEIQKNTFTNWVNEQLKPTGM-SVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIK 79

                        90       100       110
                ....*....|....*....|....*....|
gi 19115207  86 LTNIGPADIVDGNLKLILGLIWTLILRFTI 115
Cdd:cd21227  80 LVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 129-226 1.12e-29

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


Pssm-ID: 409036  Cd Length: 104  Bit Score: 112.91  E-value: 1.12e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 129 LLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEVEDVc 208
Cdd:cd21187   5 LLAWCRQSTRGY-EQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDV- 82

                        90
                ....*....|....*...
gi 19115207 209 DVDRPDERSIMTYVAEYF 226
Cdd:cd21187  83 NVEQPDKKSILMYVTSLF 100
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 3-112 2.33e-29

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: 112.46  E-value: 2.33e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   3 ANQWQSVQNRTFTKWFNTKLSSRDLpSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNpRMRVHRLENVNKALEYIKSK 82
Cdd:cd21246  10 ADEREAVQKKTFTKWVNSHLARVGC-RINDLYTDLRDGRMLIKLLEVLSGERLPKPTKG-KMRIHCLENVDKALQFLKEQ 87

                        90       100       110
                ....*....|....*....|....*....|
gi 19115207  83 GMPLTNIGPADIVDGNLKLILGLIWTLILR 112
Cdd:cd21246  88 RVHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
 121-229 2.63e-29

calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409044 [Multi-domain]  Cd Length: 110  Bit Score: 112.06  E-value: 2.63e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 121 EGLTAKEGLLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPR 200
Cdd:cd21195   1 SGDIRPSKLLTWCQQQTEGYQ-HVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPP 79

                        90       100
                ....*....|....*....|....*....
gi 19115207 201 LIEVEDVCDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21195  80 VTTGKEMASAQEPDKLSMVMYLSKFYELF 108
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
 128-229 4.22e-29

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


Pssm-ID: 409048  Cd Length: 112  Bit Score: 111.30  E-value: 4.22e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 128 GLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQkSIGIPRLIEVEDV 207
Cdd:cd21199  12 ALLKWCQEKTQGY-KGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEM 89

                        90       100
                ....*....|....*....|..
gi 19115207 208 CDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21199  90 VSMERPDWQSVMSYVTAIYKHF 111
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 123-231 4.81e-29

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: 111.22  E-value: 4.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   123 LTAKEGLLLWCQRKTANYHPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKK--NHRANMQLAFDIAQKSIGIPR 200
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 19115207   201 -LIEVEDVCDvdrPDERSIMTYVAEYFHAFST 231
Cdd:pfam00307  81 vLIEPEDLVE---GDNKSVLTYLASLFRRFQA 109
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
 126-237 9.51e-29

calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409109  Cd Length: 116  Bit Score: 110.56  E-value: 9.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 126 KEGLLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEVE 205
Cdd:cd21260   3 KNMLLEWCRAKTRGYE-HVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVE 81

                        90       100       110
                ....*....|....*....|....*....|..
gi 19115207 206 DVCDVDRPDERSIMTYVAEYFHAFSTLDKVET 237
Cdd:cd21260  82 DMVRMSVPDSKCVYTYIQELYRSLVQKGLVKT 113
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
 121-229 2.16e-28

calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409100 [Multi-domain]  Cd Length: 111  Bit Score: 109.27  E-value: 2.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 121 EGLTAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPR 200
Cdd:cd21251   2 ESVARSSKLLGWCQRQTEGY-AGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80

                        90       100
                ....*....|....*....|....*....
gi 19115207 201 LIEVEDVCDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21251  81 IMTGKEMASVGEPDKLSMVMYLTQFYEMF 109
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 5-111 3.32e-28

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: 108.63  E-value: 3.32e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   5 QWQSVQNRTFTKWFNTKLSSRDLpSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRnPRMRVHRLENVNKALEYIKSKGM 84
Cdd:cd21214   1 AWEKQQRKTFTAWCNSHLRKAGT-QIENIEEDFRDGLKLMLLLEVISGERLPKPER-GKMRFHKIANVNKALDFIASKGV 78

                        90       100
                ....*....|....*....|....*..
gi 19115207  85 PLTNIGPADIVDGNLKLILGLIWTLIL 111
Cdd:cd21214  79 KLVSIGAEEIVDGNLKMTLGMIWTIIL 105
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 123-229 8.80e-28

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


Pssm-ID: 409089  Cd Length: 107  Bit Score: 107.44  E-value: 8.80e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 123 LTAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQkSIGIPRLI 202
Cdd:cd21240   3 MSAKEKLLLWTQKVTAGY-TGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAE-RLGVTRLL 80

                        90       100
                ....*....|....*....|....*..
gi 19115207 203 EVEDVcDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21240  81 DAEDV-DVPSPDEKSVITYVSSIYDAF 106
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 8-113 8.85e-28

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: 107.49  E-value: 8.85e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   8 SVQNRTFTKWFNTKLSSRDLPsVFDLRKDLSDGILLIQLLEIIGDENLGRynRNPRMRVHRLENVNKALEYIKSKGMPLT 87
Cdd:cd21188   2 AVQKKTFTKWVNKHLIKARRR-VVDLFEDLRDGHNLISLLEVLSGESLPR--ERGRMRFHRLQNVQTALDFLKYRKIKLV 78

                        90       100
                ....*....|....*....|....*.
gi 19115207  88 NIGPADIVDGNLKLILGLIWTLILRF 113
Cdd:cd21188  79 NIRAEDIVDGNPKLTLGLIWTIILHF 104
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 124-229 1.06e-27

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


Pssm-ID: 409088  Cd Length: 104  Bit Score: 107.38  E-value: 1.06e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKsIGIPRLIE 203
Cdd:cd21239   1 SAKERLLLWSQQMTEGY-TGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLD 78

                        90       100
                ....*....|....*....|....*.
gi 19115207 204 VEDVcDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21239  79 PEDV-DVSSPDEKSVITYVSSLYDVF 103
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 120-229 1.14e-27

calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409106  Cd Length: 112  Bit Score: 107.42  E-value: 1.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 120 EEGLTAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQkSIGIP 199
Cdd:cd21257   4 EYGGSKRNALLKWCQKKTEGY-PNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIK 81

                        90       100       110
                ....*....|....*....|....*....|
gi 19115207 200 RLIEVEDVCDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21257  82 PSLELSEMMYTDRPDWQSVMQYVAQIYKYF 111
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 126-226 2.84e-27

calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409108  Cd Length: 112  Bit Score: 106.23  E-value: 2.84e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 126 KEGLLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEVE 205
Cdd:cd21259   3 KQMLLDWCRAKTRGYE-NVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVE 81

                        90       100
                ....*....|....*....|.
gi 19115207 206 DVCDVDRPDERSIMTYVAEYF 226
Cdd:cd21259  82 DMVRMREPDWKCVYTYIQEFY 102
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 124-224 6.36e-27

calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409104  Cd Length: 105  Bit Score: 104.87  E-value: 6.36e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDiAQKSIGIPRLIE 203
Cdd:cd21255   1 SSSQSLLEWCQEVTAGY-RGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFE-AFASLGVPRLLE 78

                        90       100
                ....*....|....*....|.
gi 19115207 204 VEDVCDVDRPDERSIMTYVAE 224
Cdd:cd21255  79 PADMVLLPIPDKLIVMTYLCQ 99
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 123-228 1.06e-26

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


Pssm-ID: 409087  Cd Length: 106  Bit Score: 104.33  E-value: 1.06e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 123 LTAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLI 202
Cdd:cd21238   1 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLL 79

                        90       100
                ....*....|....*....|....*.
gi 19115207 203 EVEDVcDVDRPDERSIMTYVAEYFHA 228
Cdd:cd21238  80 DPEDV-DVPQPDEKSIITYVSSLYDA 104
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
 126-227 1.55e-26

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


Pssm-ID: 409110  Cd Length: 107  Bit Score: 103.89  E-value: 1.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 126 KEGLLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEVE 205
Cdd:cd21261   3 KQILLEWCRSKTIGYK-NIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVE 81

                        90       100
                ....*....|....*....|...
gi 19115207 206 DVCDVDR-PDERSIMTYVAEYFH 227
Cdd:cd21261  82 DMMVMGRkPDPMCVFTYVQSLYN 104
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 6-113 2.60e-26

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: 103.33  E-value: 2.60e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   6 WQSVQNRTFTKWFNTKLSSRDLpSVFDLRKDLSDGILLIQLLEIIGDENLGR-YNRNPRMRVHRLENVNKALEYIKSKGM 84
Cdd:cd21183   1 WKRIQANTFTRWCNEHLKERGM-QIHDLATDFSDGLCLIALLENLSTRPLKRsYNRRPAFQQHYLENVSTALKFIEADHI 79

                        90       100
                ....*....|....*....|....*....
gi 19115207  85 PLTNIGPADIVDGNLKLILGLIWTLILRF 113
Cdd:cd21183  80 KLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 124-222 2.71e-26

calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409103  Cd Length: 107  Bit Score: 103.39  E-value: 2.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTANYHPeVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQkSIGIPRLIE 203
Cdd:cd21254   1 NASQSLLAWCKEVTKGYRG-VKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLE 78

                        90
                ....*....|....*....
gi 19115207 204 VEDVCDVDRPDERSIMTYV 222
Cdd:cd21254  79 PSDMVLLAVPDKLTVMTYL 97
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 3-112 4.31e-26

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: 103.95  E-value: 4.31e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   3 ANQWQSVQNRTFTKWFNTKLSSRDLpSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNpRMRVHRLENVNKALEYIKSK 82
Cdd:cd21318  32 ADEREAVQKKTFTKWVNSHLARVPC-RINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRG-RMRIHSLENVDKALQFLKEQ 109

                        90       100       110
                ....*....|....*....|....*....|
gi 19115207  83 GMPLTNIGPADIVDGNLKLILGLIWTLILR 112
Cdd:cd21318 110 RVHLENVGSHDIVDGNHRLTLGLIWTIILR 139
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 127-229 1.16e-25

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


Pssm-ID: 409075  Cd Length: 103  Bit Score: 101.39  E-value: 1.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 127 EGLLLWCqRKTANYHPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEVED 206
Cdd:cd21226   3 DGLLAWC-RQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAED 81

                        90       100
                ....*....|....*....|...
gi 19115207 207 VCDVDrPDERSIMTYVAEYFHAF 229
Cdd:cd21226  82 VMTGN-PDERSIVLYTSLFYHAF 103
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
 129-229 8.50e-25

calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409099 [Multi-domain]  Cd Length: 110  Bit Score: 99.18  E-value: 8.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 129 LLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEVEDVC 208
Cdd:cd21250   9 LLTWCQKQTEGYQ-NVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMA 87

                        90       100
                ....*....|....*....|.
gi 19115207 209 DVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21250  88 SAEEPDKLSMVMYLSKFYELF 108
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 9-113 1.45e-24

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: 98.61  E-value: 1.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   9 VQNRTFTKWFNTKLSSRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRynRNPRMRVHRLENVNKALEYIKSKGMPLTN 88
Cdd:cd21186   2 VQKKTFTKWINSQLSKANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKP--EKGRMRVHHLNNVNRALQVLEQNNVKLVN 79

                        90       100
                ....*....|....*....|....*
gi 19115207  89 IGPADIVDGNLKLILGLIWTLILRF 113
Cdd:cd21186  80 ISSNDIVDGNPKLTLGLVWSIILHW 104
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
 126-227 3.05e-24

calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409107  Cd Length: 111  Bit Score: 97.81  E-value: 3.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 126 KEGLLLWCQRKTANYHpEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEVE 205
Cdd:cd21258   3 KQMLLDWCRAKTRGYE-HVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVE 81

                        90       100
                ....*....|....*....|...
gi 19115207 206 DVCDV-DRPDERSIMTYVAEYFH 227
Cdd:cd21258  82 DMMIMgKKPDSKCVFTYVQSLYN 104
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 7-115 3.23e-24

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: 97.83  E-value: 3.23e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   7 QSVQNRTFTKWFNTKLSSRDLP-SVFDLRKDLSDGILLIQLLEIIGDENLgRYNRNPRM-RVHRLENVNKALEYIKSKGM 84
Cdd:cd21241   3 ERVQKKTFTNWINSYLAKRKPPmKVEDLFEDIKDGTKLLALLEVLSGEKL-PCEKGRRLkRVHFLSNINTALKFLESKKI 81

                        90       100       110
                ....*....|....*....|....*....|.
gi 19115207  85 PLTNIGPADIVDGNLKLILGLIWTLILRFTI 115
Cdd:cd21241  82 KLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
 120-231 3.66e-24

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


Pssm-ID: 409105  Cd Length: 119  Bit Score: 97.84  E-value: 3.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 120 EEGLTAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQkSIGIP 199
Cdd:cd21256  10 EYGGSKRNALLKWCQKKTEGY-QNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIK 87

                        90       100       110
                ....*....|....*....|....*....|..
gi 19115207 200 RLIEVEDVCDVDRPDERSIMTYVAEYFHAFST 231
Cdd:cd21256  88 STLDINEMVRTERPDWQSVMTYVTAIYKYFET 119
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 5-116 4.24e-24

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: 97.52  E-value: 4.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   5 QWQSVQNRTFTKWFNTKLSSRDlPSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKS-KG 83
Cdd:cd21311  11 QWKRIQQNTFTRWANEHLKTAN-KHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEG 89

                        90       100       110
                ....*....|....*....|....*....|...
gi 19115207  84 MPLTNIGPADIVDGNLKLILGLIWTLILRFTIA 116
Cdd:cd21311  90 IKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 3-112 4.46e-24

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: 97.82  E-value: 4.46e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   3 ANQWQSVQNRTFTKWFNTKLSsRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNpRMRVHRLENVNKALEYIKSK 82
Cdd:cd21317  25 ADEREAVQKKTFTKWVNSHLA-RVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKG-RMRIHCLENVDKALQFLKEQ 102

                        90       100       110
                ....*....|....*....|....*....|
gi 19115207  83 GMPLTNIGPADIVDGNLKLILGLIWTLILR 112
Cdd:cd21317 103 KVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 6-113 3.07e-23

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: 94.86  E-value: 3.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   6 WQSVQNRTFTKWFNTKLSSRDLpSVFDLRKDLSDGILLIQLLEIIGDENLGR-YNRNPRMRVHRLENVNKALEYIKSKGM 84
Cdd:cd21228   1 WKKIQQNTFTRWCNEHLKCVNK-RIYNLETDLSDGLRLIALLEVLSQKRMYKkYNKRPTFRQMKLENVSVALEFLERESI 79

                        90       100
                ....*....|....*....|....*....
gi 19115207  85 PLTNIGPADIVDGNLKLILGLIWTLILRF 113
Cdd:cd21228  80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 129-229 3.17e-23

second 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. The model corresponds to the second CH domain.


Pssm-ID: 409082  Cd Length: 111  Bit Score: 94.61  E-value: 3.17e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 129 LLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRAN-MQLAFDIAQKSIGIPRLIEVEDV 207
Cdd:cd21233   5 LLSWVRQSTRNY-PQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSATErLDHAFNIARQHLGIEKLLDPEDV 83

                        90       100
                ....*....|....*....|..
gi 19115207 208 cDVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21233  84 -ATAHPDKKSILMYVTSLFQVL 104
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 124-226 1.40e-21

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: 89.60  E-value: 1.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTANYHpevdVQDFTRSWTNGLAFCALIHQHRPDLLDYNK-LDKKNHRANMQLAFDIAQKSIGIPRLI 202
Cdd:cd21184   1 SGKSLLLEWVNSKIPEYK----VKNFTTDWNDGKALAALVDALKPGLIPDNEsLDKENPLENATKAMDIAEEELGIPKII 76

                        90       100
                ....*....|....*....|....
gi 19115207 203 EVEDVCDVDrPDERSIMTYVAeYF 226
Cdd:cd21184  77 TPEDMVSPN-VDELSVMTYLS-YF 98
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 3-118 1.41e-21

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: 90.81  E-value: 1.41e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   3 ANQWQSVQNRTFTKWFNTKLSsRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRynRNPRMRVHRLENVNKALEYIKSK 82
Cdd:cd21236  11 KDERDKVQKKTFTKWINQHLM-KVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHRLQNVQIALDYLKRR 87

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19115207  83 GMPLTNIGPADIVDGNLKLILGLIWTLILRFTIADI 118
Cdd:cd21236  88 QVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 129-226 4.51e-21

second 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 second CH domain.


Pssm-ID: 409083 [Multi-domain]  Cd Length: 104  Bit Score: 88.48  E-value: 4.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 129 LLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEVEDVC 208
Cdd:cd21234   5 LLSWVRQSTRPY-SQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVA 83

                        90
                ....*....|....*...
gi 19115207 209 dVDRPDERSIMTYVAEYF 226
Cdd:cd21234  84 -VQLPDKKSIIMYLTSLF 100
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 5-115 1.19e-20

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: 87.89  E-value: 1.19e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   5 QWQSVQNRTFTKWFNTKLSSRDLPSVF-DLRKDLSDGILLIQLLEIIGDENLGRYNRNpRMRVHRLENVNKALEYIKSKg 83
Cdd:cd21247  16 QRMTMQKKTFTKWMNNVFSKNGAKIEItDIYTELKDGIHLLRLLELISGEQLPRPSRG-KMRVHFLENNSKAITFLKTK- 93

                        90       100       110
                ....*....|....*....|....*....|..
gi 19115207  84 MPLTNIGPADIVDGNLKLILGLIWTLILRFTI 115
Cdd:cd21247  94 VPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 9-122 2.28e-20

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: 87.00  E-value: 2.28e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   9 VQNRTFTKWFNTKLSsRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRynRNPRMRVHRLENVNKALEYIKSKGMPLTN 88
Cdd:cd21235   6 VQKKTFTKWVNKHLI-KAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVN 82

                        90       100       110
                ....*....|....*....|....*....|....
gi 19115207  89 IGPADIVDGNLKLILGLIWTLILRFTIADINEEG 122
Cdd:cd21235  83 IRNDDIADGNPKLTLGLIWTIILHFQISDIQVSG 116
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 6-116 2.65e-20

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: 87.01  E-value: 2.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   6 WQSVQNRTFTKWFNTKLSSRDlPSVFDLRKDLSDGILLIQLLEIIGDENLGR-YNRNPRMRVHRLENVNKALEYIKSKGM 84
Cdd:cd21310  13 WKKIQQNTFTRWCNEHLKCVQ-KRLNDLQKDLSDGLRLIALLEVLSQKKMYRkYHPRPNFRQMKLENVSVALEFLDREHI 91

                        90       100       110
                ....*....|....*....|....*....|..
gi 19115207  85 PLTNIGPADIVDGNLKLILGLIWTLILRFTIA 116
Cdd:cd21310  92 KLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 7-115 6.58e-20

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: 85.31  E-value: 6.58e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   7 QSVQNRTFTKWFNTKLSSRDLPSVF-DLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMP 85
Cdd:cd21190   3 ERVQKKTFTNWINSHLAKLSQPIVInDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIK 82

                        90       100       110
                ....*....|....*....|....*....|
gi 19115207  86 LTNIGPADIVDGNLKLILGLIWTLILRFTI 115
Cdd:cd21190  83 LVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 7-115 1.55e-19

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: 84.20  E-value: 1.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   7 QSVQNRTFTKWFNTKLSSRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRynRNPRMRVHRLENVNKALEYIKSKGMPL 86
Cdd:cd21231   4 EDVQKKTFTKWINAQFAKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVK--EKGSTRVHALNNVNKALQVLQKNNVDL 81

                        90       100
                ....*....|....*....|....*....
gi 19115207  87 TNIGPADIVDGNLKLILGLIWTLILRFTI 115
Cdd:cd21231  82 VNIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 3-112 3.20e-19

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: 84.71  E-value: 3.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   3 ANQWQSVQNRTFTKWFNTKLSsRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNpRMRVHRLENVNKALEYIKSK 82
Cdd:cd21316  47 ADEREAVQKKTFTKWVNSHLA-RVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKG-RMRIHCLENVDKALQFLKEQ 124

                        90       100       110
                ....*....|....*....|....*....|
gi 19115207  83 GMPLTNIGPADIVDGNLKLILGLIWTLILR 112
Cdd:cd21316 125 RVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 6-116 6.86e-19

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: 83.21  E-value: 6.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   6 WQSVQNRTFTKWFNTKLSSRDlPSVFDLRKDLSDGILLIQLLEIIGDENLGR-YNRNPRMRVHRLENVNKALEYIKSKGM 84
Cdd:cd21308  17 WKKIQQNTFTRWCNEHLKCVS-KRIANLQTDLSDGLRLIALLEVLSQKKMHRkHNQRPTFRQMQLENVSVALEFLDRESI 95

                        90       100       110
                ....*....|....*....|....*....|..
gi 19115207  85 PLTNIGPADIVDGNLKLILGLIWTLILRFTIA 116
Cdd:cd21308  96 KLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 7-115 8.78e-19

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: 82.19  E-value: 8.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   7 QSVQNRTFTKWFNTKLSSRDLPSVF-DLRKDLSDGILLIQLLEIIGDENLgrynrnPRMRVHRL----ENVNKALEYIKS 81
Cdd:cd21242   3 EQTQKRTFTNWINSQLAKHSPPSVVsDLFTDIQDGHRLLDLLEVLSGQQL------PREKGHNVfqcrSNIETALSFLKN 76

                        90       100       110
                ....*....|....*....|....*....|....
gi 19115207  82 KGMPLTNIGPADIVDGNLKLILGLIWTLILRFTI 115
Cdd:cd21242  77 KSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 14-113 1.09e-18

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: 81.47  E-value: 1.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207  14 FTKWFNTKLSSR-DLPSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMPLTNIGPA 92
Cdd:cd21212   5 YTDWANHYLEKGgHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQGITAE 84

                        90       100
                ....*....|....*....|.
gi 19115207  93 DIVDGNLKLILGLIWTLILRF 113
Cdd:cd21212  85 DIVDGNLKAILGLFFSLSRYK 105
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 8-115 1.11e-18

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: 81.59  E-value: 1.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   8 SVQNRTFTKWFNTKLSSRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRynRNPRMRVHRLENVNKALEYIKSKGMPLT 87
Cdd:cd21232   1 DVQKKTFTKWINARFSKSGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPK--ERGSTRVHALNNVNRVLQVLHQNNVELV 78

                        90       100
                ....*....|....*....|....*...
gi 19115207  88 NIGPADIVDGNLKLILGLIWTLILRFTI 115
Cdd:cd21232  79 NIGGTDIVDGNHKLTLGLLWSIILHWQV 106
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 6-116 1.88e-18

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: 82.05  E-value: 1.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   6 WQSVQNRTFTKWFNTKLSSRDlPSVFDLRKDLSDGILLIQLLEIIGDENLGR-YNRNPRMRVHRLENVNKALEYIKSKGM 84
Cdd:cd21309  14 WKKIQQNTFTRWCNEHLKCVN-KRIGNLQTDLSDGLRLIALLEVLSQKRMYRkYHQRPTFRQMQLENVSVALEFLDRESI 92

                        90       100       110
                ....*....|....*....|....*....|..
gi 19115207  85 PLTNIGPADIVDGNLKLILGLIWTLILRFTIA 116
Cdd:cd21309  93 KLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 7-115 4.43e-18

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: 80.32  E-value: 4.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   7 QSVQNRTFTKWFNTKLSSRDLP-SVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMP 85
Cdd:cd21191   3 ENVQKRTFTRWINLHLEKCNPPlEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSNVK 82

                        90       100       110
                ....*....|....*....|....*....|
gi 19115207  86 LTNIGPADIVDGNLKLILGLIWTLILRFTI 115
Cdd:cd21191  83 LVSIDAAEIADGNPSLVLGLIWNIILFFQI 112
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 9-122 2.15e-17

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: 78.54  E-value: 2.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   9 VQNRTFTKWFNTKLSsRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRynRNPRMRVHRLENVNKALEYIKSKGMPLTN 88
Cdd:cd21237   6 VQKKTFTKWVNKHLM-KVRKHINDLYEDLRDGHNLISLLEVLSGVKLPR--EKGRMRFHRLQNVQIALDFLKQRQVKLVN 82

                        90       100       110
                ....*....|....*....|....*....|....
gi 19115207  89 IGPADIVDGNLKLILGLIWTLILRFTIADINEEG 122
Cdd:cd21237  83 IRNDDITDGNPKLTLGLIWTIILHFQISDIYISG 116
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 12-112 4.39e-17

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 76.97  E-value: 4.39e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207     12 RTFTKWFNTKLSSRDLPSVFDLRKDLSDGIL-LIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMPLTNIG 90
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVAlCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 19115207     91 PADIVDGNlKLILGLIWTLILR 112
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 127-222 1.14e-16

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 75.82  E-value: 1.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207    127 EGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKK----NHRANMQLAFDIAQKSIGIPRLI 202
Cdd:smart00033   1 KTLLRWVNSLLAEY-DKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVVLF 79

                           90       100
                   ....*....|....*....|
gi 19115207    203 EVEDVCDVdRPDERSIMTYV 222
Cdd:smart00033  80 EPEDLVEG-PKLILGVIWTL 98
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 6-109 4.98e-16

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: 74.10  E-value: 4.98e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   6 WQSVQNRTFTKWFNTKLSSRDLPSVFDLRKDLSDGILLIQLLEIIGDENLG-RYNRNPRMRVHRLENVNKALEYI-KSKG 83
Cdd:cd21225   1 WEKVQIKAFTAWVNSVLEKRGIPKISDLATDLSDGVRLIFFLELVSGKKFPkKFDLEPKNRIQMIQNLHLAMLFIeEDLK 80

                        90       100
                ....*....|....*....|....*.
gi 19115207  84 MPLTNIGPADIVDGNLKLILGLIWTL 109
Cdd:cd21225  81 IRVQGIGAEDFVDNNKKLILGLLWTL 106
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 124-225 5.39e-16

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: 73.96  E-value: 5.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTanyhPEVDVQDFTRSWTNGLAFCALIHQHRPDLL-DYNKLDKKNHRANMQLAFDIAQKSIGIPRLI 202
Cdd:cd21230   1 TPKQRLLGWIQNKI----PQLPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLI 76

                        90       100
                ....*....|....*....|...
gi 19115207 203 EVEDVCDvDRPDERSIMTYVAEY 225
Cdd:cd21230  77 TPEEIIN-PNVDEMSVMTYLSQF 98
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
 122-229 4.95e-15

calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409045  Cd Length: 106  Bit Score: 71.23  E-value: 4.95e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 122 GLTAKEGLLLWCQRKTANYhPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRL 201
Cdd:cd21196   1 SSGTQEELLRWCQEQTAGY-PGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPV 79

                        90       100
                ....*....|....*....|....*...
gi 19115207 202 IEVEDVcdVDRPDERSIMTYVAEYFHAF 229
Cdd:cd21196  80 VSAQAV--VAGSDPLGLIAYLSHFHSAF 105
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 117-225 5.55e-15

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: 71.35  E-value: 5.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 117 DINEEGLTAKEGLLLWCQRKTanyhPEVDVQDFTRSWTNGLAFCALIHQHRPDLL-DYNKLDKKNHRANMQLAFDIAQKS 195
Cdd:cd21315   9 PDDGKGPTPKQRLLGWIQSKV----PDLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDW 84

                        90       100       110
                ....*....|....*....|....*....|
gi 19115207 196 IGIPRLIEVEDVCDvDRPDERSIMTYVAEY 225
Cdd:cd21315  85 LDVPQLIKPEEMVN-PKVDELSMMTYLSQF 113
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 126-226 6.58e-15

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: 70.88  E-value: 6.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 126 KEGLLLWCQRKTanyhPEVDVQDFTRSWTNGLAFCALIHQHRPDLL-DYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEV 204
Cdd:cd21229   5 KKLMLAWLQAVL----PELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSP 80

                        90       100
                ....*....|....*....|..
gi 19115207 205 EDVCDVDRpDERSIMTYVAeYF 226
Cdd:cd21229  81 EDLSSPHL-DELSGMTYLS-YF 100
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 10-109 6.64e-15

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 70.79  E-value: 6.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207  10 QNRTFTKWFNTKLSSR-DLPSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMPLTN 88
Cdd:cd21213   1 QLQAYVAWVNSQLKKRpGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80

                        90       100
                ....*....|....*....|.
gi 19115207  89 IGPADIVDGNLKLILGLIWTL 109
Cdd:cd21213  81 TSAKDIVDGNLKAIMRLILAL 101
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 12-115 5.45e-14

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: 68.60  E-value: 5.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207  12 RTFTKWfntkLSSRDL-PSVFDLRKDLSDGIL--LIQLLEIIGDENLGRYNRNPR----MRVHRLENVNKALEYIKSKGM 84
Cdd:cd21300  10 RVFTLW----LNSLDVePAVNDLFEDLRDGLIllQAYDKVIPGSVNWKKVNKAPAsaeiSRFKAVENTNYAVELGKQLGF 85

                        90       100       110
                ....*....|....*....|....*....|.
gi 19115207  85 PLTNIGPADIVDGNLKLILGLIWTLiLRFTI 115
Cdd:cd21300  86 SLVGIQGADITDGSRTLTLALVWQL-MRFHI 115
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 126-227 7.70e-14

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 67.75  E-value: 7.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 126 KEGLLLWCQRKTANYHPeVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKN---HRANMQLAFDIAqKSIGIPR-- 200
Cdd:cd00014   1 EEELLKWINEVLGEELP-VSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSpfkKRENINLFLNAC-KKLGLPEld 78

                        90       100
                ....*....|....*....|....*..
gi 19115207 201 LIEVEDVcdVDRPDERSIMTYVAEYFH 227
Cdd:cd00014  79 LFEPEDL--YEKGNLKKVLGTLWALAL 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 9-115 6.24e-13

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: 65.39  E-value: 6.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207     9 VQNRTFTKWFNTKL-SSRDLPSVFDLRKDLSDGILLIQLLEIIgDENLGRYNRNPRMRVHRLENVNKALEYIKSK-GMPL 86
Cdd:pfam00307   2 ELEKELLRWINSHLaEYGPGVRVTNFTTDLRDGLALCALLNKL-APGLVDKKKLNKSEFDKLENINLALDVAEKKlGVPK 80

                          90       100
                  ....*....|....*....|....*....
gi 19115207    87 TNIGPADIVDGNLKLILGLIWTLILRFTI 115
Cdd:pfam00307  81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 129-223 6.78e-13

second 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 CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409073 [Multi-domain]  Cd Length: 138  Bit Score: 66.17  E-value: 6.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 129 LLLWCQRKTANYhpEVDVQDFTRSWTNGLAFCALIHQHRPDLL------------------------------------D 172
Cdd:cd21224   5 LLKWCQAVCAHY--GVKVENFTVSFADGRALCYLIHHYLPSLLpldairqpttqtvdraqdeaedfwvaefspstgdsgL 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19115207 173 YNKLdKKNHRANMQLAFDIAQKSIGIPRLIEVEDVCDvDRPDERSIMTYVA 223
Cdd:cd21224  83 SSEL-LANEKRNFKLVQQAVAELGGVPALLRASDMSN-TIPDEKVVILFLS 131
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 142-227 1.11e-12

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


Pssm-ID: 409034  Cd Length: 98  Bit Score: 64.25  E-value: 1.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 142 PEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDiAQKSIGIPRLIEVEDVCDVDrPDERSIMTY 221
Cdd:cd21185  15 PDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPE-VEHLGIMAY 92


                ....*.
gi 19115207 222 VAEYFH 227
Cdd:cd21185  93 AAQLQK 98
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 12-110 5.04e-12

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: 62.68  E-value: 5.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207  12 RTFTKWFNtklsSRDL-PSVFDLRKDLSDGIL--LIQLLEIIGDENLGRYNRN-PRMRVHRLENVNKALEYIKSKGMPLT 87
Cdd:cd21219   7 RAFRMWLN----SLGLdPLINNLYEDLRDGLVllQVLDKIQPGCVNWKKVNKPkPLNKFKKVENCNYAVDLAKKLGFSLV 82

                        90       100
                ....*....|....*....|...
gi 19115207  88 NIGPADIVDGNLKLILGLIWTLI 110
Cdd:cd21219  83 GIGGKDIADGNRKLTLALVWQLM 105
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 117-225 5.44e-12

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: 62.78  E-value: 5.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 117 DINEEGL---TAKEGLLLWCQRKTanyhPEVDVQDFTRSWTNGLAFCALIHQHRPDLL-DYNKLDKKNHRANMQLAFDIA 192
Cdd:cd21314   1 DEDEEDArkqTPKQRLLGWIQNKV----PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQA 76

                        90       100       110
                ....*....|....*....|....*....|...
gi 19115207 193 QKSIGIPRLIEVEDVCDVDrPDERSIMTYVAEY 225
Cdd:cd21314  77 DDWLGVPQVIAPEEIVDPN-VDEHSVMTYLSQF 108
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 12-111 1.31e-11

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 61.20  E-value: 1.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207  12 RTFTKWFNTKLSSRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMP-LTNIG 90
Cdd:cd00014   2 EELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLPeLDLFE 81

                        90       100
                ....*....|....*....|..
gi 19115207  91 PADIV-DGNLKLILGLIWTLIL 111
Cdd:cd00014  82 PEDLYeKGNLKKVLGTLWALAL 103
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 124-225 9.00e-11

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


Pssm-ID: 409161  Cd Length: 114  Bit Score: 59.43  E-value: 9.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTanyhPEVDVQDFTRSWTNGLAFCALIHQHRPDLL-DYNKLDKKNHRANMQLAFDIAQKSIGIPRLI 202
Cdd:cd21312  12 TPKQRLLGWIQNKL----PQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVI 87

                        90       100
                ....*....|....*....|...
gi 19115207 203 EVEDVCDVDrPDERSIMTYVAEY 225
Cdd:cd21312  88 TPEEIVDPN-VDEHSVMTYLSQF 109
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 12-116 2.67e-10

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 58.02  E-value: 2.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207  12 RTFTKWFNTKLSSrdlPSVFDLRKDLSDGIL--LIQLLEIIGDENLGRYNRNP-RMRVH--RLENVNKALEYIKSKGMPL 86
Cdd:cd21298   9 KTYRNWMNSLGVN---PFVNHLYSDLRDGLVllQLYDKIKPGVVDWSRVNKPFkKLGANmkKIENCNYAVELGKKLKFSL 85

                        90       100       110
                ....*....|....*....|....*....|
gi 19115207  87 TNIGPADIVDGNLKLILGLIWTLILRFTIA 116
Cdd:cd21298  86 VGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 67-110 4.95e-10

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: 57.20  E-value: 4.95e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19115207  67 HRLENVNKALEYIKSKGMPLTNIGPADIVDGNLKLILGLIWTLI 110
Cdd:cd21217  70 EATENLNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
 124-225 3.47e-09

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


Pssm-ID: 409162  Cd Length: 110  Bit Score: 54.71  E-value: 3.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 124 TAKEGLLLWCQRKTanyhPEVDVQDFTRSWTNGLAFCALIHQHRPDLL-DYNKLDKKNHRANMQLAFDIAQKSIGIPRLI 202
Cdd:cd21313   8 TPKQRLLGWIQNKI----PYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGVPQVI 83

                        90       100
                ....*....|....*....|...
gi 19115207 203 EVEDVCDVDrPDERSIMTYVAEY 225
Cdd:cd21313  84 TPEEIIHPD-VDEHSVMTYLSQF 105
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 12-109 3.60e-09

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (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. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409135  Cd Length: 105  Bit Score: 54.65  E-value: 3.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207  12 RTFTKWFNTKLSSRDLPSVF-DLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMPLTNIG 90
Cdd:cd21286   3 KIYTDWANHYLAKSGHKRLIkDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 82

                        90
                ....*....|....*....
gi 19115207  91 PADIVDGNLKLILGLIWTL 109
Cdd:cd21286  83 AEEIRNGNLKAILGLFFSL 101
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 10-109 1.03e-07

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (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. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409134  Cd Length: 121  Bit Score: 50.73  E-value: 1.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207  10 QNRTFTKWFNTKLS-SRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMPLTN 88
Cdd:cd21285  11 DKQIYTDWANHYLAkSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAKGINIQG 90

                        90       100
                ....*....|....*....|.
gi 19115207  89 IGPADIVDGNLKLILGLIWTL 109
Cdd:cd21285  91 LSAEEIRNGNLKAILGLFFSL 111
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 7-115 5.88e-07

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 48.44  E-value: 5.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   7 QSVQNRTFTKWFNTKLSSrdlPSVFDLRKDLSDGILLIQLLEIIG-DENLGRYNRNPRM----RVHRLENVNKALEYIKS 81
Cdd:cd21329   4 ESSEERTFRNWMNSLGVN---PYVNHLYSDLCDALVIFQLYEMTRvPVDWGHVNKPPYPalggNMKKIENCNYAVELGKN 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 19115207  82 KG-MPLTNIGPADIVDGNLKLILGLIWTLILRFTI 115
Cdd:cd21329  81 KAkFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTL 115
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 8-115 5.90e-07

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


Pssm-ID: 409148  Cd Length: 114  Bit Score: 48.27  E-value: 5.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   8 SVQNRTFTKWFNTKLSSRDLPSVFDlrkDLSDG--ILLIQLLEIIGDENLGRYNRNP-RMRVHRLENVNKALEYIKSKGM 84
Cdd:cd21299   3 SREERCFRLWINSLGIDTYVNNVFE---DVRDGwvLLEVLDKVSPGSVNWKHANKPPiKMPFKKVENCNQVVKIGKQLKF 79

                        90       100       110
                ....*....|....*....|....*....|.
gi 19115207  85 PLTNIGPADIVDGNLKLILGLIWTLiLRFTI 115
Cdd:cd21299  80 SLVNVAGNDIVQGNKKLILALLWQL-MRYHM 109
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 55-113 1.00e-06

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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: 409071  Cd Length: 121  Bit Score: 47.97  E-value: 1.00e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19115207  55 LGRYNRNPRMRVHRLENVNKALEYIKSKGMPLTNIGPADIVDGNLKLILGLIWTLILRF 113
Cdd:cd21222  63 LHEYHLTPSTDDEKLHNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 7-115 1.24e-06

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: 48.07  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   7 QSVQNRTFTKWFNTKLSSrdlPSVFDLRKDLSDGILLIQLLEIIG-DENLGRYNRNPRMRV----HRLENVNKALEYIKS 81
Cdd:cd21331  20 ETREERTFRNWMNSLGVN---PHVNHLYGDLQDALVILQLYEKIKvPVDWNKVNKPPYPKLganmKKLENCNYAVELGKH 96

                        90       100       110
                ....*....|....*....|....*....|....*
gi 19115207  82 KG-MPLTNIGPADIVDGNLKLILGLIWTLILRFTI 115
Cdd:cd21331  97 PAkFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 54-112 2.83e-06

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: 46.67  E-value: 2.83e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19115207  54 NLGRYNRNPRMRVHRLENVNKALEYIKSKGMPLTNIGPADIVDGNLKLILGLIWTLILR 112
Cdd:cd21294  66 NKPPRKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRR 124
EFhand_Ca_insen pfam08726
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 554-615 4.62e-06

Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the regulation of many cellular processes. EF hands usually bind to Ca2+ ions which causes a major conformational change that allows the protein to interact with its designated targets. This domain corresponds to an EF hand which has partially or entirely lost its calcium-binding properties. The calcium insensitive EF hand is still able to mediate protein-protein recognition.


Pssm-ID: 430177  Cd Length: 69  Bit Score: 44.61  E-value: 4.62e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   554 DRDSARQVLYAFCDVADGKSYVTSDDLLRSQVrPNIVKFLECNMNKHSE--------GLDYLTWIKQLLA 615
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELT-PDQAEYCIARMPPYSGpdgdsvpgAYDYVSFSEALFG 69
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 123-227 4.44e-05

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: 43.06  E-value: 4.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 123 LTAKEGLLLWCqrktaNYH------PEVDVQDFTRSWTNGLAFCALIHQHRPDL----LDYNKLDKKN--HRANMQLAfd 190
Cdd:cd21218   9 LPPEEILLRWV-----NYHlkkagpTKKRVTNFSSDLKDGEVYALLLHSLAPELcdkeLVLEVLSEEDleKRAEKVLQ-- 81

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19115207 191 iAQKSIGIPRLIEVEDVCDvdrPDERSIMTYVAEYFH 227
Cdd:cd21218  82 -AAEKLGCKYFLTPEDIVS---GNPRLNLAFVATLFN 114
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 63-110 4.86e-05

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: 42.96  E-value: 4.86e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 19115207  63 RMRvhRLENVNKALEYIKSKGMPLTNIG----PADIVDGNLKLILGLIWTLI 110
Cdd:cd21223  63 RLQ--KLHNVEVALKALKEAGVLRGGDGggitAKDIVDGHREKTLALLWRII 112
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 70-119 7.07e-05

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


Pssm-ID: 409141  Cd Length: 145  Bit Score: 43.04  E-value: 7.07e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 19115207  70 ENVNKALEYIKSKGMPLTNIGPADIVDGNLKLILGLIWTLILRFTIADIN 119
Cdd:cd21292  95 ENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIE 144
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 7-115 8.22e-05

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: 42.67  E-value: 8.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207   7 QSVQNRTFTKWFNTKLSSrdlPSVFDLRKDLSDGILLIQLLEIIG-DENLGRYNRNPRMRV----HRLENVNKALEYIKS 81
Cdd:cd21330  11 ETREERTFRNWMNSLGVN---PRVNHLYSDLSDALVIFQLYEKIKvPVDWNRVNKPPYPKLgenmKKLENCNYAVELGKN 87

                        90       100       110
                ....*....|....*....|....*....|....*
gi 19115207  82 KG-MPLTNIGPADIVDGNLKLILGLIWTLILRFTI 115
Cdd:cd21330  88 KAkFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTL 122
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 70-118 2.77e-04

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: 41.57  E-value: 2.77e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 19115207  70 ENVNKALEYIKSKGMPLTNIGPADIVDGNLKLILGLIWTLILRFTIADI 118
Cdd:cd21323  95 ENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADI 143
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 54-114 2.79e-04

second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It 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: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 40.80  E-value: 2.79e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115207  54 NLGRYNRNPRMRVHRLENVNKALEYIKSKGMPLTNIGPADIVDGNLKLILGLIWTLILRFT 114
Cdd:cd21307  62 HLSEFFLTPSSTSEMLHNVTLALELLKEGGLLNFPVNPEDIVNGDSKATIRVLYCLFSKYK 122
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 129-223 1.43e-03

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


Pssm-ID: 409069  Cd Length: 105  Bit Score: 38.41  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115207 129 LLLWCQRKTANYHPEVDVQDFT-RSWTNGLAFCALIHQHRPDLLDYNKL------DKKnhRANMQLAFDIAQKsIGIPRL 201
Cdd:cd21220   6 ILAWANSKVREAGKSSPISSFKdPSLSTGLFLLDLLAAIDPGAVDYDLVtegetdEEK--EQNAKYAISLARK-IGAVIF 82

                        90       100
                ....*....|....*....|..
gi 19115207 202 IEVEDVCDVdRPdeRSIMTYVA 223
Cdd:cd21220  83 LLWEDIVEV-KP--KMILTFVA 101
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 70-118 5.11e-03

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: 38.12  E-value: 5.11e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 19115207  70 ENVNKALEYIKSKGMPLTNIGPADIVDGNLKLILGLIWTLILRFTIADI 118
Cdd:cd21325  95 ENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADI 143
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 70-118 9.29e-03

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


Pssm-ID: 409173  Cd Length: 145  Bit Score: 37.30  E-value: 9.29e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 19115207  70 ENVNKALEYIKSKGMPLTNIGPADIVDGNLKLILGLIWTLILRFTIADI 118
Cdd:cd21324  95 ENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADI 143
 
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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