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Conserved domains on  [gi|442614868|ref|NP_001259166|]
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alpha actinin, isoform H [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 139-252 7.17e-86

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: 269.62  E-value: 7.17e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 139 IQDISVEEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKY 218
Cdd:cd21216    1 IQDISVEELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKH 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 442614868 219 LDIPRMLDPDDLINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21216   81 LDIPKMLDAEDIVNTPRPDERSVMTYVSCYYHAF 114
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 31-135 8.98e-75

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: 239.60  E-value: 8.98e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  31 AWEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASKGVHL 110
Cdd:cd21214    1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPERGKMRFHKIANVNKALDFIASKGVKL 80

                         90       100
                 ....*....|....*....|....*
gi 442614868 111 VSIGAEEIVDGNLKMTLGMIWTIIL 135
Cdd:cd21214   81 VSIGAEEIVDGNLKMTLGMIWTIIL 105
EFhand_Ca_insen pfam08726
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 847-913 1.35e-33

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: 123.19  E-value: 1.35e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442614868  847 DTDTAEQVIDSFRILAADKPYILPDELRRELPPDQAEYCIQRMPPYKGP--NGVPGALDYMSFSTALYG 913
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 420-647 7.89e-33

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 126.41  E-value: 7.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 420 LAQKFKHKADAHEDWTRGKEEMLQSQDFRQcKLNELKALKKKHEAFESDLAAHQDRVEQIAAIAQELNTLEYHDCVSVNA 499
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 500 RCQRICDQWDRLGALTQRRRTALDEAERILEKI-DILHLEfakraapfnNWLDGTREDLVDMFIVHTMEEIQGLIQAHDQ 578
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFrDADDLE---------QWLEEKEAALASEDLGKDLESVEELLKKHKE 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442614868 579 FKATLGEADKEFNLIVNLVREVESIVKQHqipgglENPYTTLTANDMTRKWSDVRQLVPQRDQTLANEL 647
Cdd:cd00176  151 LEEELEAHEPRLKSLNELAEELLEEGHPD------ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 302-525 6.98e-19

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 86.35  E-value: 6.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 302 EEYERLASDLLEWIRRTMPWLNSRQADNSLAGVQKKLEEYRTYRR--KHKPPRVEQkakletnFNTLQTKLRLSNRPAYL 379
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEA-------LNELGEQLIEEGHPDAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 380 PTEgKTVSDISNSWKGL-ELAEKafeewllaetmRLERLEHLAQKFKHKADAH--EDWTRGKEEMLQSQDFRQcKLNELK 456
Cdd:cd00176   76 EIQ-ERLEELNQRWEELrELAEE-----------RRQRLEEALDLQQFFRDADdlEQWLEEKEAALASEDLGK-DLESVE 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 457 ALKKKHEAFESDLAAHQDRVEQIAAIAQEL-NTLEYHDCVSVNARCQRICDQWDRLGALTQRRRTALDEA 525
Cdd:cd00176  143 ELLKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 538-760 5.48e-17

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.57  E-value: 5.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 538 EFAKRAAPFNNWLDGTREDLVDMFIVHTMEEIQGLIQAHDQFKATLGEADKEFNlivNLVREVESIVKQHQIpgglENPY 617
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVE---ALNELGEQLIEEGHP----DAEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 618 TTLTANDMTRKWSDVRQLVPQRDQTLANELRKQQNNEMLRRqfaekaniVGPWIERQMDAVTAIGMG-LQGSLEDQLHRL 696
Cdd:cd00176   77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGkDLESVEELLKKH 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442614868 697 KEYEQAVYAYKPNIEELEKIHQAVQESMIFEN-RYTNYTMETLRVGWEQLLTSINRNINEVENQI 760
Cdd:cd00176  149 KELEEELEAHEPRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 775-842 1.30e-12

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 63.34  E-value: 1.30e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442614868 775 EFRSSFNHFDKNRTGRLSPEEFKSCLVSLGysigkDRQGDLDFQRILAVVDPNNTGYVHFDAFLDFMT 842
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLG-----EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 139-252 7.17e-86

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: 269.62  E-value: 7.17e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 139 IQDISVEEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKY 218
Cdd:cd21216    1 IQDISVEELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKH 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 442614868 219 LDIPRMLDPDDLINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21216   81 LDIPKMLDAEDIVNTPRPDERSVMTYVSCYYHAF 114
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 31-135 8.98e-75

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: 239.60  E-value: 8.98e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  31 AWEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASKGVHL 110
Cdd:cd21214    1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPERGKMRFHKIANVNKALDFIASKGVKL 80

                         90       100
                 ....*....|....*....|....*
gi 442614868 111 VSIGAEEIVDGNLKMTLGMIWTIIL 135
Cdd:cd21214   81 VSIGAEEIVDGNLKMTLGMIWTIIL 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
32-394 3.99e-64

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 227.52  E-value: 3.99e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  32 WEKQQKKTFTAWCNSHLRKAGT-AIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGK-MRFHKIANVNKALDFIASKGVH 109
Cdd:COG5069    6 WQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPeTRIHVMENVSGRLEFIKGKGVK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 110 LVSIGAEEIVDGNLKMTLGMIWTIILRFAIQDISVE-EMTAKEGLLLWCQRKTAPYKN-VNVQNFHLSFKDGLAFCALIH 187
Cdd:COG5069   86 LFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEgELTKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIH 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 188 RHRPDLIDYAKLS--KDNPLENLNTAFDVAEKYLDIPRMLDPDDLINTPKPDERAIMTYVSCYYHAFQGAQQVgnvthvp 265
Cdd:COG5069  166 DSRPDTLDPNVLDlqKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRFGLLEKI------- 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 266 eptrqytyvpnnynaETAANRICKVLKVNQENERLMEEYERLASDLLEWIRRTMPWLNSRQADNSLAGVQKK---LEEYR 342
Cdd:COG5069  239 ---------------DIALHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYtdlLNQLN 303

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442614868 343 TYRRKhkppRVEQKAKLETNFNTLQTKLRLSNRPAYLPTEGKTVSDISNSWK 394
Cdd:COG5069  304 ALCSR----APLETTDLHSLAGQILQNAEKYDCRKYLPPAGNPKLDLAFVAH 351
EFhand_Ca_insen pfam08726
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 847-913 1.35e-33

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: 123.19  E-value: 1.35e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442614868  847 DTDTAEQVIDSFRILAADKPYILPDELRRELPPDQAEYCIQRMPPYKGP--NGVPGALDYMSFSTALYG 913
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 420-647 7.89e-33

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 126.41  E-value: 7.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 420 LAQKFKHKADAHEDWTRGKEEMLQSQDFRQcKLNELKALKKKHEAFESDLAAHQDRVEQIAAIAQELNTLEYHDCVSVNA 499
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 500 RCQRICDQWDRLGALTQRRRTALDEAERILEKI-DILHLEfakraapfnNWLDGTREDLVDMFIVHTMEEIQGLIQAHDQ 578
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFrDADDLE---------QWLEEKEAALASEDLGKDLESVEELLKKHKE 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442614868 579 FKATLGEADKEFNLIVNLVREVESIVKQHqipgglENPYTTLTANDMTRKWSDVRQLVPQRDQTLANEL 647
Cdd:cd00176  151 LEEELEAHEPRLKSLNELAEELLEEGHPD------ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 147-254 2.64e-31

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: 118.16  E-value: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  147 MTAKEGLLLWCQRKTAPYK-NVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKD--NPLENLNTAFDVAEKYLDIPR 223
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 442614868  224 ML-DPDDLINtpkPDERAIMTYVSCYYHAFQG 254
Cdd:pfam00307  81 VLiEPEDLVE---GDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 34-139 8.01e-25

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: 99.67  E-value: 8.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868   34 KQQKKTFTAWCNSHLRKAG--TAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASK-GVHL 110
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKlGVPK 80

                          90       100
                  ....*....|....*....|....*....
gi 442614868  111 VSIGAEEIVDGNLKMTLGMIWTIILRFAI 139
Cdd:pfam00307  81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 151-246 9.07e-23

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 93.53  E-value: 9.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868   151 EGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKD----NPLENLNTAFDVAEKYLDIPRMLD 226
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|
gi 442614868   227 PDDlINTPKPDERAIMTYVS 246
Cdd:smart00033  81 PED-LVEGPKLILGVIWTLI 99
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 419-524 1.72e-22

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 93.15  E-value: 1.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  419 HLAQKFKHKADAHEDWTRGKEEMLQSQDFRQcKLNELKALKKKHEAFESDLAAHQDRVEQIAAIAQELNTLEYHDCVSVN 498
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                          90       100
                  ....*....|....*....|....*.
gi 442614868  499 ARCQRICDQWDRLGALTQRRRTALDE 524
Cdd:pfam00435  80 ERLEELNERWEQLLELAAERKQKLEE 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 38-136 2.59e-22

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 92.38  E-value: 2.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868    38 KTFTAWCNSHLRKAG-TAIDNIEEDFRNGLKLMLLLEVISGETLPK--PDRGKMRFHKIANVNKALDFIASKGVHLVSIG 114
Cdd:smart00033   1 KTLLRWVNSLLAEYDkPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 442614868   115 AEEIVDGNlKMTLGMIWTIILR 136
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101
SPEC smart00150
Spectrin repeats;
422-523 3.69e-19

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 83.15  E-value: 3.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868   422 QKFKHKADAHEDWTRGKEEMLQSQDFrQCKLNELKALKKKHEAFESDLAAHQDRVEQIAAIAQELNTLEYHDCVSVNARC 501
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                           90       100
                   ....*....|....*....|..
gi 442614868   502 QRICDQWDRLGALTQRRRTALD 523
Cdd:smart00150  80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 302-525 6.98e-19

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 86.35  E-value: 6.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 302 EEYERLASDLLEWIRRTMPWLNSRQADNSLAGVQKKLEEYRTYRR--KHKPPRVEQkakletnFNTLQTKLRLSNRPAYL 379
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEA-------LNELGEQLIEEGHPDAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 380 PTEgKTVSDISNSWKGL-ELAEKafeewllaetmRLERLEHLAQKFKHKADAH--EDWTRGKEEMLQSQDFRQcKLNELK 456
Cdd:cd00176   76 EIQ-ERLEELNQRWEELrELAEE-----------RRQRLEEALDLQQFFRDADdlEQWLEEKEAALASEDLGK-DLESVE 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 457 ALKKKHEAFESDLAAHQDRVEQIAAIAQEL-NTLEYHDCVSVNARCQRICDQWDRLGALTQRRRTALDEA 525
Cdd:cd00176  143 ELLKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 538-760 5.48e-17

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.57  E-value: 5.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 538 EFAKRAAPFNNWLDGTREDLVDMFIVHTMEEIQGLIQAHDQFKATLGEADKEFNlivNLVREVESIVKQHQIpgglENPY 617
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVE---ALNELGEQLIEEGHP----DAEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 618 TTLTANDMTRKWSDVRQLVPQRDQTLANELRKQQNNEMLRRqfaekaniVGPWIERQMDAVTAIGMG-LQGSLEDQLHRL 696
Cdd:cd00176   77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGkDLESVEELLKKH 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442614868 697 KEYEQAVYAYKPNIEELEKIHQAVQESMIFEN-RYTNYTMETLRVGWEQLLTSINRNINEVENQI 760
Cdd:cd00176  149 KELEEELEAHEPRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 775-842 1.30e-12

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 63.34  E-value: 1.30e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442614868 775 EFRSSFNHFDKNRTGRLSPEEFKSCLVSLGysigkDRQGDLDFQRILAVVDPNNTGYVHFDAFLDFMT 842
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLG-----EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00184 PTZ00184
calmodulin; Provisional
 768-874 6.28e-12

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 64.40  E-value: 6.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 768 ISQEQLNEFRSSFNHFDKNRTGRLSPEEFKSCLVSLGYSigkDRQGDLdfQRILAVVDPNNTGYVHFDAFLDFMTRESTD 847
Cdd:PTZ00184   5 LTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQN---PTEAEL--QDMINEVDADGNGTIDFPEFLTLMARKMKD 79

                         90       100
                 ....*....|....*....|....*...
gi 442614868 848 TDTAEQVIDSFRILAAD-KPYILPDELR 874
Cdd:PTZ00184  80 TDSEEEIKEAFKVFDRDgNGFISAAELR 107
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 656-758 9.68e-09

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 53.86  E-value: 9.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  656 LRRQFAEKANIVGPWIERQMDAVTAIGMGLQ-GSLEDQLHRLKEYEQAVYAYKPNIEELEKIHQAVQESMIFENRYTNYT 734
Cdd:pfam00435   2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDlESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQER 81

                          90       100
                  ....*....|....*....|....
gi 442614868  735 METLRVGWEQLLTSINRNINEVEN 758
Cdd:pfam00435  82 LEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 299-409 2.74e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 52.32  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  299 RLMEEYERLASDLLEWIRRTMPWLNSRQADNSLAGVQKKLEEyrtYRRKHKPPRVeQKAKLEtNFNTLQTKLrLSNRPAY 378
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKK---HKALEAELAA-HQDRVE-ALNELAEKL-IDEGHYA 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 442614868  379 LPTEGKTVSDISNSWKGLELAEKAFEEWLLA 409
Cdd:pfam00435  75 SEEIQERLEELNERWEQLLELAAERKQKLEE 105
EF-hand_7 pfam13499
EF-hand domain pair;
774-842 1.13e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.78  E-value: 1.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442614868  774 NEFRSSFNHFDKNRTGRLSPEEFKSCLVSLGYSIGKDRQgdlDFQRILAVVDPNNTGYVHFDAFLDFMT 842
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDE---EVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
774-842 4.18e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.32  E-value: 4.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442614868 774 NEFRSSFNHFDKNRTGRLSPEEFKSCLVSLGYSigkdrqgDLDFQRILAVVDPNNTGYVHFDAFLDFMT 842
Cdd:COG5126   69 PFARAAFDLLDTDGDGKISADEFRRLLTALGVS-------EEEADELFARLDTDGDGKISFEEFVAAVR 130
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 775-803 1.81e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 36.59  E-value: 1.81e-03
                           10        20
                   ....*....|....*....|....*....
gi 442614868   775 EFRSSFNHFDKNRTGRLSPEEFKSCLVSL 803
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
40-131 3.92e-03

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 41.08  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  40 FTAWCNSHLrkAGTAIDNIEEDFRNGLKLMLLLEVISGE---------TLPKPDRGKMRFHKIANVNKALDFIASKGVHL 110
Cdd:COG5069  384 FTFWLNSLD--VSPEITNLFGDLRDQLILLQALSKKLMPmtvthklvkKQPASGIEENRFKAFENENYAVDLGITEGFSL 461

                         90       100
                 ....*....|....*....|.
gi 442614868 111 VSIGAEEIVDGNlKMTLGMIW 131
Cdd:COG5069  462 VGIKGLEILDGI-RLKLTLVW 481
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
413-533 1.00e-02

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 1.00e-02
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 413 RLERLEHLAQKFKHKADAHEDWTRGKEEMLQSQDFRQcklnELKALKKKHEAFESDLAAHQDRVEQIAAIAQELNTLEYH 492
Cdd:COG4717  110 ELEELREELEKLEKLLQLLPLYQELEALEAELAELPE----RLEELEERLEELRELEEELEELEAELAELQEELEELLEQ 185

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 442614868 493 DCVSVNARCQRICDQWDRLGALTQRRRTALDEAERILEKID 533
Cdd:COG4717  186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
 
Name Accession Description Interval E-value
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 139-252 7.17e-86

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: 269.62  E-value: 7.17e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 139 IQDISVEEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKY 218
Cdd:cd21216    1 IQDISVEELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKH 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 442614868 219 LDIPRMLDPDDLINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21216   81 LDIPKMLDAEDIVNTPRPDERSVMTYVSCYYHAF 114
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 31-135 8.98e-75

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: 239.60  E-value: 8.98e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  31 AWEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASKGVHL 110
Cdd:cd21214    1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPERGKMRFHKIANVNKALDFIASKGVKL 80

                         90       100
                 ....*....|....*....|....*
gi 442614868 111 VSIGAEEIVDGNLKMTLGMIWTIIL 135
Cdd:cd21214   81 VSIGAEEIVDGNLKMTLGMIWTIIL 105
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 139-257 7.44e-68

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: 221.52  E-value: 7.44e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 139 IQDISVEEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKY 218
Cdd:cd21289    1 IQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKY 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442614868 219 LDIPRMLDPDDLINTPKPDERAIMTYVSCYYHAFQGAQQ 257
Cdd:cd21289   81 LDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQ 119
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
 139-257 6.96e-66

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: 216.11  E-value: 6.96e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 139 IQDISVEEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKY 218
Cdd:cd21287    1 IQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKY 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442614868 219 LDIPRMLDPDDLINTPKPDERAIMTYVSCYYHAFQGAQQ 257
Cdd:cd21287   81 LDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQK 119
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
 139-257 8.34e-66

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: 216.09  E-value: 8.34e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 139 IQDISVEEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKY 218
Cdd:cd21288    1 IQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKH 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442614868 219 LDIPRMLDPDDLINTPKPDERAIMTYVSCYYHAFQGAQQ 257
Cdd:cd21288   81 LDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQ 119
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
32-394 3.99e-64

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 227.52  E-value: 3.99e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  32 WEKQQKKTFTAWCNSHLRKAGT-AIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGK-MRFHKIANVNKALDFIASKGVH 109
Cdd:COG5069    6 WQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPeTRIHVMENVSGRLEFIKGKGVK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 110 LVSIGAEEIVDGNLKMTLGMIWTIILRFAIQDISVE-EMTAKEGLLLWCQRKTAPYKN-VNVQNFHLSFKDGLAFCALIH 187
Cdd:COG5069   86 LFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEgELTKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIH 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 188 RHRPDLIDYAKLS--KDNPLENLNTAFDVAEKYLDIPRMLDPDDLINTPKPDERAIMTYVSCYYHAFQGAQQVgnvthvp 265
Cdd:COG5069  166 DSRPDTLDPNVLDlqKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRFGLLEKI------- 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 266 eptrqytyvpnnynaETAANRICKVLKVNQENERLMEEYERLASDLLEWIRRTMPWLNSRQADNSLAGVQKK---LEEYR 342
Cdd:COG5069  239 ---------------DIALHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYtdlLNQLN 303

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442614868 343 TYRRKhkppRVEQKAKLETNFNTLQTKLRLSNRPAYLPTEGKTVSDISNSWK 394
Cdd:COG5069  304 ALCSR----APLETTDLHSLAGQILQNAEKYDCRKYLPPAGNPKLDLAFVAH 351
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
 136-257 7.00e-64

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: 210.71  E-value: 7.00e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 136 RFAIQDISVEEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVA 215
Cdd:cd21290    1 RFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 442614868 216 EKYLDIPRMLDPDDLINTPKPDERAIMTYVSCYYHAFQGAQQ 257
Cdd:cd21290   81 EKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQK 122
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 148-252 1.36e-53

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: 181.46  E-value: 1.36e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDP 227
Cdd:cd21194    2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81

                         90       100
                 ....*....|....*....|....*
gi 442614868 228 DDlINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21194   82 ED-VDVARPDEKSIMTYVASYYHYF 105
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 139-252 4.38e-53

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: 180.42  E-value: 4.38e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 139 IQDISVEEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKY 218
Cdd:cd21291    1 IADINEEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKE 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 442614868 219 LDIPRMLDPDDLINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21291   81 IGIPQLLDVEDVCDVAKPDERSIMTYVAYYFHAF 114
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 148-252 5.38e-52

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: 176.82  E-value: 5.38e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDP 227
Cdd:cd21248    2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81

                         90       100
                 ....*....|....*....|....*
gi 442614868 228 DDlINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21248   82 ED-VNVEQPDEKSIITYVVTYYHYF 105
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 147-252 8.96e-47

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: 162.34  E-value: 8.96e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 147 MTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLD 226
Cdd:cd21249    3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82

                         90       100
                 ....*....|....*....|....*.
gi 442614868 227 PDDLInTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21249   83 PEDVA-VPHPDERSIMTYVSLYYHYF 107
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 36-136 2.89e-46

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: 161.31  E-value: 2.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  36 QKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASKgVHLVSIGA 115
Cdd:cd21193   17 QKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRGRLRVQKIENVNKALAFLKTK-VRLENIGA 95

                         90       100
                 ....*....|....*....|.
gi 442614868 116 EEIVDGNLKMTLGMIWTIILR 136
Cdd:cd21193   96 EDIVDGNPRLILGLIWTIILR 116
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
 145-252 1.50e-44

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: 156.32  E-value: 1.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 145 EEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRM 224
Cdd:cd21319    2 ETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKL 81

                         90       100
                 ....*....|....*....|....*...
gi 442614868 225 LDPDDLInTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21319   82 LDPEDVF-TENPDEKSIITYVVAFYHYF 108
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 36-137 7.25e-44

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: 154.10  E-value: 7.25e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  36 QKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKpDRGKMRFHKIANVNKALDFIASKGVHLVSIGA 115
Cdd:cd21188    4 QKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPR-ERGRMRFHRLQNVQTALDFLKYRKIKLVNIRA 82

                         90       100
                 ....*....|....*....|..
gi 442614868 116 EEIVDGNLKMTLGMIWTIILRF 137
Cdd:cd21188   83 EDIVDGNPKLTLGLIWTIILHF 104
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 148-252 1.95e-43

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: 152.55  E-value: 1.95e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDP 227
Cdd:cd21189    1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80

                         90       100
                 ....*....|....*....|....*
gi 442614868 228 DDlINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21189   81 ED-VDVPEPDEKSIITYVSSLYDVF 104
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 33-136 6.36e-43

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: 151.75  E-value: 6.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASKGVHLVS 112
Cdd:cd21246   14 EAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKMRIHCLENVDKALQFLKEQRVHLEN 93

                         90       100
                 ....*....|....*....|....
gi 442614868 113 IGAEEIVDGNLKMTLGMIWTIILR 136
Cdd:cd21246   94 MGSHDIVDGNHRLTLGLIWTIILR 117
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 148-252 1.88e-42

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: 149.80  E-value: 1.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDP 227
Cdd:cd21253    1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80

                         90       100
                 ....*....|....*....|....*
gi 442614868 228 DDLINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21253   81 EDMVALKVPDKLSILTYVSQYYNYF 105
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 32-137 1.93e-41

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: 147.16  E-value: 1.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  32 WEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPD-RGKMRFHKIANVNKALDFIASKGVHL 110
Cdd:cd21215    1 WVDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYNkNPKMRVQKLENVNKALEFIKSRGVKL 80

                         90       100
                 ....*....|....*....|....*..
gi 442614868 111 VSIGAEEIVDGNLKMTLGMIWTIILRF 137
Cdd:cd21215   81 TNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 145-252 3.76e-39

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: 140.96  E-value: 3.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 145 EEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRM 224
Cdd:cd21321    2 EKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKL 81

                         90       100
                 ....*....|....*....|....*...
gi 442614868 225 LDPDDlINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21321   82 LDPED-VNVDQPDEKSIITYVATYYHYF 108
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
 149-252 4.23e-38

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: 137.69  E-value: 4.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 149 AKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPD 228
Cdd:cd21252    1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80

                         90       100
                 ....*....|....*....|....
gi 442614868 229 DLINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21252   81 DMVSMKVPDCLSIMTYVSQYYNHF 104
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 145-252 9.46e-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: 137.49  E-value: 9.46e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 145 EEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRM 224
Cdd:cd21322   14 ETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLTKL 93

                         90       100
                 ....*....|....*....|....*...
gi 442614868 225 LDPDDlINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21322   94 LDPED-VNMEAPDEKSIITYVVSFYHYF 120
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 149-252 1.11e-37

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: 136.51  E-value: 1.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 149 AKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPD 228
Cdd:cd21197    1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80

                         90       100
                 ....*....|....*....|....
gi 442614868 229 DLINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21197   81 DMVTMHVPDRLSIITYVSQYYNHF 104
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 33-136 1.18e-37

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: 137.46  E-value: 1.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASKGVHLVS 112
Cdd:cd21318   36 EAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRMRIHSLENVDKALQFLKEQRVHLEN 115

                         90       100
                 ....*....|....*....|....
gi 442614868 113 IGAEEIVDGNLKMTLGMIWTIILR 136
Cdd:cd21318  116 VGSHDIVDGNHRLTLGLIWTIILR 139
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 151-252 1.70e-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: 135.88  E-value: 1.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 151 EGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDDL 230
Cdd:cd22198    3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEM 82

                         90       100
                 ....*....|....*....|..
gi 442614868 231 INTPKPDERAIMTYVSCYYHAF 252
Cdd:cd22198   83 ASLAVPDKLSMVSYLSQFYEAF 104
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 33-136 9.43e-36

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: 131.71  E-value: 9.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASKGVHLVS 112
Cdd:cd21317   29 EAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKGRMRIHCLENVDKALQFLKEQKVHLEN 108

                         90       100
                 ....*....|....*....|....
gi 442614868 113 IGAEEIVDGNLKMTLGMIWTIILR 136
Cdd:cd21317  109 MGSHDIVDGNHRLTLGLIWTIILR 132
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
 147-252 2.28e-35

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: 129.75  E-value: 2.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 147 MTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLD 226
Cdd:cd21243    4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83

                         90       100
                 ....*....|....*....|....*.
gi 442614868 227 PDDlINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21243   84 PED-VDVDKPDEKSIMTYVAQFLKKY 108
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 36-140 4.00e-35

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: 129.04  E-value: 4.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  36 QKKTFTAWCNSHLRKAG-TAIDNIEEDFRNGLKLMLLLEVISGETLpKPDRGKMRFHKIANVNKALDFIASKGVHLVSIG 114
Cdd:cd21186    3 QKKTFTKWINSQLSKANkPPIKDLFEDLRDGTRLLALLEVLTGKKL-KPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81

                         90       100
                 ....*....|....*....|....*.
gi 442614868 115 AEEIVDGNLKMTLGMIWTIILRFAIQ 140
Cdd:cd21186   82 SNDIVDGNPKLTLGLVWSIILHWQVK 107
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 148-252 1.71e-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: 127.52  E-value: 1.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDP 227
Cdd:cd21320    2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81

                         90       100
                 ....*....|....*....|....*
gi 442614868 228 DDlINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21320   82 ED-ISVDHPDEKSIITYVVTYYHYF 105
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 153-249 3.71e-34

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: 126.39  E-value: 3.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 153 LLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDDlIN 232
Cdd:cd21187    5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED-VN 83

                         90
                 ....*....|....*..
gi 442614868 233 TPKPDERAIMTYVSCYY 249
Cdd:cd21187   84 VEQPDKKSILMYVTSLF 100
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 33-144 5.14e-34

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: 126.64  E-value: 5.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKpDRGKMRFHKIANVNKALDFIASKGVHLVS 112
Cdd:cd21236   15 DKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALDYLKRRQVKLVN 93

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442614868 113 IGAEEIVDGNLKMTLGMIWTIILRFAIQDISV 144
Cdd:cd21236   94 IRNDDITDGNPKLTLGLIWTIILHFQISDIHV 125
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 146-246 8.95e-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: 125.23  E-value: 8.95e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 146 EMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRML 225
Cdd:cd21192    1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLL 80

                         90       100
                 ....*....|....*....|.
gi 442614868 226 DPDDlINTPKPDERAIMTYVS 246
Cdd:cd21192   81 EVED-VLVDKPDERSIMTYVS 100
EFhand_Ca_insen pfam08726
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 847-913 1.35e-33

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: 123.19  E-value: 1.35e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442614868  847 DTDTAEQVIDSFRILAADKPYILPDELRRELPPDQAEYCIQRMPPYKGP--NGVPGALDYMSFSTALYG 913
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 33-144 1.69e-33

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: 125.14  E-value: 1.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKpDRGKMRFHKIANVNKALDFIASKGVHLVS 112
Cdd:cd21235    4 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442614868 113 IGAEEIVDGNLKMTLGMIWTIILRFAIQDISV 144
Cdd:cd21235   83 IRNDDIADGNPKLTLGLIWTIILHFQISDIQV 114
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 32-139 7.57e-33

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: 122.78  E-value: 7.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  32 WEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKP-DRGKMRFHKIANVNKALDFIASKGVHL 110
Cdd:cd21227    1 WVEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRViKKPLNQHQKLENVTLALKAMAEDGIKL 80

                         90       100
                 ....*....|....*....|....*....
gi 442614868 111 VSIGAEEIVDGNLKMTLGMIWTIILRFAI 139
Cdd:cd21227   81 VNIGNEDIVNGNLKLILGLIWHLILRYQI 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 420-647 7.89e-33

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 126.41  E-value: 7.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 420 LAQKFKHKADAHEDWTRGKEEMLQSQDFRQcKLNELKALKKKHEAFESDLAAHQDRVEQIAAIAQELNTLEYHDCVSVNA 499
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 500 RCQRICDQWDRLGALTQRRRTALDEAERILEKI-DILHLEfakraapfnNWLDGTREDLVDMFIVHTMEEIQGLIQAHDQ 578
Cdd:cd00176   80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFrDADDLE---------QWLEEKEAALASEDLGKDLESVEELLKKHKE 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442614868 579 FKATLGEADKEFNLIVNLVREVESIVKQHqipgglENPYTTLTANDMTRKWSDVRQLVPQRDQTLANEL 647
Cdd:cd00176  151 LEEELEAHEPRLKSLNELAEELLEEGHPD------ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 151-252 2.66e-32

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: 121.03  E-value: 2.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 151 EGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDDL 230
Cdd:cd21226    3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82

                         90       100
                 ....*....|....*....|..
gi 442614868 231 iNTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21226   83 -MTGNPDERSIVLYTSLFYHAF 103
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 148-245 2.85e-32

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: 120.99  E-value: 2.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKyLDIPRMLDP 227
Cdd:cd21198    1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79

                         90
                 ....*....|....*...
gi 442614868 228 DDLINTPKPDERAIMTYV 245
Cdd:cd21198   80 ADMVLLSVPDKLSVMTYL 97
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 148-253 3.24e-32

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: 120.91  E-value: 3.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDP 227
Cdd:cd21200    1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80

                         90       100
                 ....*....|....*....|....*..
gi 442614868 228 DDLIN-TPKPDERAIMTYVSCYYHAFQ 253
Cdd:cd21200   81 EDMVRmGNRPDWKCVFTYVQSLYRHLR 107
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 33-140 3.84e-32

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: 120.94  E-value: 3.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHL--RKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKM-RFHKIANVNKALDFIASKGVH 109
Cdd:cd21241    3 ERVQKKTFTNWINSYLakRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLkRVHFLSNINTALKFLESKKIK 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 442614868 110 LVSIGAEEIVDGNLKMTLGMIWTIILRFAIQ 140
Cdd:cd21241   83 LVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
 152-253 1.30e-31

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: 119.39  E-value: 1.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 152 GLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYlDIPRMLDPDDLI 231
Cdd:cd21199   12 ALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESV-GIPTTLTIDEMV 90

                         90       100
                 ....*....|....*....|..
gi 442614868 232 NTPKPDERAIMTYVSCYYHAFQ 253
Cdd:cd21199   91 SMERPDWQSVMSYVTAIYKHFE 112
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 147-254 2.64e-31

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: 118.16  E-value: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  147 MTAKEGLLLWCQRKTAPYK-NVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKD--NPLENLNTAFDVAEKYLDIPR 223
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 442614868  224 ML-DPDDLINtpkPDERAIMTYVSCYYHAFQG 254
Cdd:pfam00307  81 VLiEPEDLVE---GDNKSVLTYLASLFRRFQA 109
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 147-251 1.13e-30

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: 116.27  E-value: 1.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 147 MTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLD 226
Cdd:cd21238    1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80

                         90       100
                 ....*....|....*....|....*
gi 442614868 227 PDDlINTPKPDERAIMTYVSCYYHA 251
Cdd:cd21238   81 PED-VDVPQPDEKSIITYVSSLYDA 104
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 29-139 7.02e-30

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: 114.86  E-value: 7.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  29 DPAWEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPD-RGKMRFHKIANVNKALDFIAS-K 106
Cdd:cd21311    9 DAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNkRPTFRSQKLENVSVALKFLEEdE 88

                         90       100       110
                 ....*....|....*....|....*....|...
gi 442614868 107 GVHLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 139
Cdd:cd21311   89 GIKIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 33-136 9.07e-30

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: 115.53  E-value: 9.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASKGVHLVS 112
Cdd:cd21316   51 EAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLEN 130

                         90       100
                 ....*....|....*....|....
gi 442614868 113 IGAEEIVDGNLKMTLGMIWTIILR 136
Cdd:cd21316  131 MGSHDIVDGNHRLTLGLIWTIILR 154
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 148-252 2.00e-29

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: 112.77  E-value: 2.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKyLDIPRMLDP 227
Cdd:cd21239    1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79

                         90       100
                 ....*....|....*....|....*
gi 442614868 228 DDlINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21239   80 ED-VDVSSPDEKSVITYVSSLYDVF 103
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 33-144 3.00e-29

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: 112.82  E-value: 3.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKpDRGKMRFHKIANVNKALDFIASKGVHLVS 112
Cdd:cd21237    4 DRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPR-EKGRMRFHRLQNVQIALDFLKQRQVKLVN 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442614868 113 IGAEEIVDGNLKMTLGMIWTIILRFAIQDISV 144
Cdd:cd21237   83 IRNDDITDGNPKLTLGLIWTIILHFQISDIYI 114
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 36-139 4.53e-29

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: 112.54  E-value: 4.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  36 QKKTFTAWCNSHLRK--AGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASKgVHLVSI 113
Cdd:cd21247   21 QKKTFTKWMNNVFSKngAKIEITDIYTELKDGIHLLRLLELISGEQLPRPSRGKMRVHFLENNSKAITFLKTK-VPVKLI 99

                         90       100
                 ....*....|....*....|....*.
gi 442614868 114 GAEEIVDGNLKMTLGMIWTIILRFAI 139
Cdd:cd21247  100 GPENIVDGDRTLILGLIWIIILRFQI 125
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 32-137 5.10e-29

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: 111.80  E-value: 5.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  32 WEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRF--HKIANVNKALDFIASKGVH 109
Cdd:cd21183    1 WKRIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYNRRPAFqqHYLENVSTALKFIEADHIK 80

                         90       100
                 ....*....|....*....|....*...
gi 442614868 110 LVSIGAEEIVDGNLKMTLGMIWTIILRF 137
Cdd:cd21183   81 LVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 148-246 6.74e-29

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: 111.42  E-value: 6.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKyLDIPRMLDP 227
Cdd:cd21255    1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79

                         90
                 ....*....|....*....
gi 442614868 228 DDLINTPKPDERAIMTYVS 246
Cdd:cd21255   80 ADMVLLPIPDKLIVMTYLC 98
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 150-249 2.23e-28

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: 110.08  E-value: 2.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 150 KEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDD 229
Cdd:cd21259    3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82

                         90       100
                 ....*....|....*....|
gi 442614868 230 LINTPKPDERAIMTYVSCYY 249
Cdd:cd21259   83 MVRMREPDWKCVYTYIQEFY 102
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 32-137 2.31e-28

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: 109.89  E-value: 2.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  32 WEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKP--DRGKMRFHKIANVNKALDFIASKGVH 109
Cdd:cd21228    1 WKKIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKynKRPTFRQMKLENVSVALEFLERESIK 80

                         90       100
                 ....*....|....*....|....*...
gi 442614868 110 LVSIGAEEIVDGNLKMTLGMIWTIILRF 137
Cdd:cd21228   81 LVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 146-252 2.60e-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: 109.75  E-value: 2.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 146 EMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKyLDIPRML 225
Cdd:cd21240    2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80

                         90       100
                 ....*....|....*....|....*..
gi 442614868 226 DPDDlINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21240   81 DAED-VDVPSPDEKSVITYVSSIYDAF 106
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
 153-254 2.90e-28

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: 109.75  E-value: 2.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 153 LLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDDLIN 232
Cdd:cd21195    9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMAS 88

                         90       100
                 ....*....|....*....|..
gi 442614868 233 TPKPDERAIMTYVSCYYHAFQG 254
Cdd:cd21195   89 AQEPDKLSMVMYLSKFYELFRG 110
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
 146-246 6.29e-28

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: 108.77  E-value: 6.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 146 EMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRML 225
Cdd:cd21244    3 KMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLL 82

                         90       100
                 ....*....|....*....|.
gi 442614868 226 DPDDlINTPKPDERAIMTYVS 246
Cdd:cd21244   83 EPED-VDVVNPDEKSIMTYVA 102
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 33-140 2.60e-27

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: 106.89  E-value: 2.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHL--RKAGTAIDNIEEDFRNGLKLMLLLEVISGETLP--KPDRGKmRFHKIANVNKALDFIASKGV 108
Cdd:cd21190    3 ERVQKKTFTNWINSHLakLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPieSGRVLQ-RAHKLSNIRNALDFLTKRCI 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442614868 109 HLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQ 140
Cdd:cd21190   82 KLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 33-140 4.17e-27

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: 106.55  E-value: 4.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHLRKAG-TAIDNIEEDFRNGLKLMLLLEVISGETLPKpDRGKMRFHKIANVNKALDFIASKGVHLV 111
Cdd:cd21231    4 EDVQKKTFTKWINAQFAKFGkPPIEDLFTDLQDGRRLLELLEGLTGQKLVK-EKGSTRVHALNNVNKALQVLQKNNVDLV 82

                         90       100
                 ....*....|....*....|....*....
gi 442614868 112 SIGAEEIVDGNLKMTLGMIWTIILRFAIQ 140
Cdd:cd21231   83 NIGSADIVDGNHKLTLGLIWSIILHWQVK 111
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
 153-254 1.32e-26

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: 104.96  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 153 LLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDDLIN 232
Cdd:cd21250    9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMAS 88

                         90       100
                 ....*....|....*....|..
gi 442614868 233 TPKPDERAIMTYVSCYYHAFQG 254
Cdd:cd21250   89 AEEPDKLSMVMYLSKFYELFRG 110
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 29-139 2.37e-26

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: 104.73  E-value: 2.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  29 DPAWEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETL-----PKPDRGKMRFHkiaNVNKALDFI 103
Cdd:cd21310   10 DAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMyrkyhPRPNFRQMKLE---NVSVALEFL 86

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 442614868 104 ASKGVHLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 139
Cdd:cd21310   87 DREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 122
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 153-249 8.00e-26

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: 102.34  E-value: 8.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 153 LLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDDlIN 232
Cdd:cd21234    5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED-VA 83

                         90
                 ....*....|....*..
gi 442614868 233 TPKPDERAIMTYVSCYY 249
Cdd:cd21234   84 VQLPDKKSIIMYLTSLF 100
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 148-245 9.23e-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: 102.24  E-value: 9.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKyLDIPRMLDP 227
Cdd:cd21254    1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79

                         90
                 ....*....|....*...
gi 442614868 228 DDLINTPKPDERAIMTYV 245
Cdd:cd21254   80 SDMVLLAVPDKLTVMTYL 97
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 148-251 1.84e-25

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: 101.54  E-value: 1.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYknvNVQNFHLSFKDGLAFCALIHRHRPDLI-DYAKLSKDNPLENLNTAFDVAEKYLDIPRMLD 226
Cdd:cd21184    1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIIT 77

                         90       100
                 ....*....|....*....|....*
gi 442614868 227 PDDLINtPKPDERAIMTYVSCYYHA 251
Cdd:cd21184   78 PEDMVS-PNVDELSVMTYLSYFRNA 101
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
 145-253 3.27e-25

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: 101.18  E-value: 3.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 145 EEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRM 224
Cdd:cd21251    2 ESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPI 81

                         90       100
                 ....*....|....*....|....*....
gi 442614868 225 LDPDDLINTPKPDERAIMTYVSCYYHAFQ 253
Cdd:cd21251   82 MTGKEMASVGEPDKLSMVMYLTQFYEMFK 110
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 153-258 4.03e-25

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: 100.77  E-value: 4.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 153 LLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDY-AKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDDlI 231
Cdd:cd21233    5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWnSVVSQQSATERLDHAFNIARQHLGIEKLLDPED-V 83

                         90       100
                 ....*....|....*....|....*..
gi 442614868 232 NTPKPDERAIMTYVSCYYHAFqgAQQV 258
Cdd:cd21233   84 ATAHPDKKSILMYVTSLFQVL--PQQV 108
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 36-140 6.30e-25

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: 100.08  E-value: 6.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  36 QKKTFTAWCNSHLRKAGT-AIDNIEEDFRNGLKLMLLLEVISGETLPKpDRGKMRFHKIANVNKALDFIASKGVHLVSIG 114
Cdd:cd21232    3 QKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPK-ERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81

                         90       100
                 ....*....|....*....|....*.
gi 442614868 115 AEEIVDGNLKMTLGMIWTIILRFAIQ 140
Cdd:cd21232   82 GTDIVDGNHKLTLGLLWSIILHWQVK 107
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
 150-252 7.87e-25

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: 100.16  E-value: 7.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 150 KEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDD 229
Cdd:cd21260    3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82

                         90       100
                 ....*....|....*....|...
gi 442614868 230 LINTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21260   83 MVRMSVPDSKCVYTYIQELYRSL 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 34-139 8.01e-25

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: 99.67  E-value: 8.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868   34 KQQKKTFTAWCNSHLRKAG--TAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASK-GVHL 110
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKlGVPK 80

                          90       100
                  ....*....|....*....|....*....
gi 442614868  111 VSIGAEEIVDGNLKMTLGMIWTIILRFAI 139
Cdd:pfam00307  81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
 150-250 8.30e-25

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: 99.74  E-value: 8.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 150 KEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDD 229
Cdd:cd21258    3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82

                         90       100
                 ....*....|....*....|..
gi 442614868 230 -LINTPKPDERAIMTYVSCYYH 250
Cdd:cd21258   83 mMIMGKKPDSKCVFTYVQSLYN 104
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 148-253 1.07e-24

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: 99.72  E-value: 1.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKyLDIPRMLDP 227
Cdd:cd21257    8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLEL 86

                         90       100
                 ....*....|....*....|....*.
gi 442614868 228 DDLINTPKPDERAIMTYVSCYYHAFQ 253
Cdd:cd21257   87 SEMMYTDRPDWQSVMQYVAQIYKYFE 112
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 33-140 3.34e-24

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: 97.98  E-value: 3.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHLRKAGT--AIDNIEEDFRNGLKLMLLLEVISGETLPKpDRGKMRFHKIANVNKALDFIASKGVHL 110
Cdd:cd21242    3 EQTQKRTFTNWINSQLAKHSPpsVVSDLFTDIQDGHRLLDLLEVLSGQQLPR-EKGHNVFQCRSNIETALSFLKNKSIKL 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 442614868 111 VSIGAEEIVDGNLKMTLGMIWTIILRFAIQ 140
Cdd:cd21242   82 INIHVPDIIEGKPSIILGLIWTIILHFHIE 111
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 148-252 5.11e-24

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: 97.55  E-value: 5.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYkNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDP 227
Cdd:cd21245    3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81

                         90       100
                 ....*....|....*....|....*
gi 442614868 228 DDLInTPKPDERAIMTYVSCYYHAF 252
Cdd:cd21245   82 EDVM-VDSPDEQSIMTYVAQFLEHF 105
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 29-139 8.67e-24

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: 97.84  E-value: 8.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  29 DPAWEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKP--DRGKMRFHKIANVNKALDFIASK 106
Cdd:cd21309   11 DAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKyhQRPTFRQMQLENVSVALEFLDRE 90

                         90       100       110
                 ....*....|....*....|....*....|...
gi 442614868 107 GVHLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 139
Cdd:cd21309   91 SIKLVSIDSKAIVDGNLKLILGLVWTLILHYSI 123
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 29-139 1.58e-23

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: 96.69  E-value: 1.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  29 DPAWEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKP--DRGKMRFHKIANVNKALDFIASK 106
Cdd:cd21308   14 DAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKhnQRPTFRQMQLENVSVALEFLDRE 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 442614868 107 GVHLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 139
Cdd:cd21308   94 SIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 126
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 36-137 6.30e-23

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: 94.19  E-value: 6.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  36 QKKTFTAWCNSHLRKAGTA--IDNIEEDFRNGLKLMLLLEVISGETLPKP-DRGKMRFHKIANVNKALDFIASKGVHLVS 112
Cdd:cd21212    1 EIEIYTDWANHYLEKGGHKriITDLQKDLGDGLTLVNLIEAVAGEKVPGIhSRPKTRAQKLENIQACLQFLAALGVDVQG 80

                         90       100
                 ....*....|....*....|....*
gi 442614868 113 IGAEEIVDGNLKMTLGMIWTIILRF 137
Cdd:cd21212   81 ITAEDIVDGNLKAILGLFFSLSRYK 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 151-246 9.07e-23

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 93.53  E-value: 9.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868   151 EGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKD----NPLENLNTAFDVAEKYLDIPRMLD 226
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|
gi 442614868   227 PDDlINTPKPDERAIMTYVS 246
Cdd:smart00033  81 PED-LVEGPKLILGVIWTLI 99
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
 150-250 1.67e-22

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: 93.11  E-value: 1.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 150 KEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDD 229
Cdd:cd21261    3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82

                         90       100
                 ....*....|....*....|...
gi 442614868 230 -LINTPKPDERAIMTYV-SCYYH 250
Cdd:cd21261   83 mMVMGRKPDPMCVFTYVqSLYNH 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 419-524 1.72e-22

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 93.15  E-value: 1.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  419 HLAQKFKHKADAHEDWTRGKEEMLQSQDFRQcKLNELKALKKKHEAFESDLAAHQDRVEQIAAIAQELNTLEYHDCVSVN 498
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                          90       100
                  ....*....|....*....|....*.
gi 442614868  499 ARCQRICDQWDRLGALTQRRRTALDE 524
Cdd:pfam00435  80 ERLEELNERWEQLLELAAERKQKLEE 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 38-136 2.59e-22

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 92.38  E-value: 2.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868    38 KTFTAWCNSHLRKAG-TAIDNIEEDFRNGLKLMLLLEVISGETLPK--PDRGKMRFHKIANVNKALDFIASKGVHLVSIG 114
Cdd:smart00033   1 KTLLRWVNSLLAEYDkPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 442614868   115 AEEIVDGNlKMTLGMIWTIILR 136
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
 148-253 4.99e-22

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: 92.06  E-value: 4.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKyLDIPRMLDP 227
Cdd:cd21256   14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDI 92

                         90       100
                 ....*....|....*....|....*.
gi 442614868 228 DDLINTPKPDERAIMTYVSCYYHAFQ 253
Cdd:cd21256   93 NEMVRTERPDWQSVMTYVTAIYKYFE 118
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 32-133 8.03e-20

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: 85.66  E-value: 8.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  32 WEKQQKKTFTAWCNSHLRKAG-TAIDNIEEDFRNGLKLMLLLEVISGETLPKP--DRGKMRFHKIANVNKALDFIASK-G 107
Cdd:cd21225    1 WEKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdLEPKNRIQMIQNLHLAMLFIEEDlK 80

                         90       100
                 ....*....|....*....|....*.
gi 442614868 108 VHLVSIGAEEIVDGNLKMTLGMIWTI 133
Cdd:cd21225   81 IRVQGIGAEDFVDNNKKLILGLLWTL 106
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 33-141 9.42e-20

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: 85.32  E-value: 9.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHLRKAGT--AIDNIEEDFRNGLKLMLLLEVISGETLPKPDR-GKMRFHKIANVNKALDFIASKGVH 109
Cdd:cd21191    3 ENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKpSSHRIFRLNNIAKALKFLEDSNVK 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442614868 110 LVSIGAEEIVDGNLKMTLGMIWTIILRFAIQD 141
Cdd:cd21191   83 LVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
SPEC smart00150
Spectrin repeats;
422-523 3.69e-19

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 83.15  E-value: 3.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868   422 QKFKHKADAHEDWTRGKEEMLQSQDFrQCKLNELKALKKKHEAFESDLAAHQDRVEQIAAIAQELNTLEYHDCVSVNARC 501
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                           90       100
                   ....*....|....*....|..
gi 442614868   502 QRICDQWDRLGALTQRRRTALD 523
Cdd:smart00150  80 EELNERWEELKELAEERRQKLE 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 150-250 4.16e-19

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: 83.16  E-value: 4.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 150 KEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDY---AKLSKDNPLENLNTAFDVAEKY-LDIPRML 225
Cdd:cd00014    1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinkKPKSPFKKRENINLFLNACKKLgLPELDLF 80

                         90       100
                 ....*....|....*....|....*
gi 442614868 226 DPDDLINtpKPDERAIMTYVSCYYH 250
Cdd:cd00014   81 EPEDLYE--KGNLKKVLGTLWALAL 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 302-525 6.98e-19

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 86.35  E-value: 6.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 302 EEYERLASDLLEWIRRTMPWLNSRQADNSLAGVQKKLEEYRTYRR--KHKPPRVEQkakletnFNTLQTKLRLSNRPAYL 379
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEA-------LNELGEQLIEEGHPDAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 380 PTEgKTVSDISNSWKGL-ELAEKafeewllaetmRLERLEHLAQKFKHKADAH--EDWTRGKEEMLQSQDFRQcKLNELK 456
Cdd:cd00176   76 EIQ-ERLEELNQRWEELrELAEE-----------RRQRLEEALDLQQFFRDADdlEQWLEEKEAALASEDLGK-DLESVE 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 457 ALKKKHEAFESDLAAHQDRVEQIAAIAQEL-NTLEYHDCVSVNARCQRICDQWDRLGALTQRRRTALDEA 525
Cdd:cd00176  143 ELLKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 148-248 2.34e-18

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: 81.27  E-value: 2.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTaPYKNVNvqNFHLSFKDGLAFCALIHRHRPDLI-DYAKLSKDNPLENLNTAFDVAEKYLDIPRMLD 226
Cdd:cd21230    1 TPKQRLLGWIQNKI-PQLPIT--NFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77

                         90       100
                 ....*....|....*....|..
gi 442614868 227 PDDLINtPKPDERAIMTYVSCY 248
Cdd:cd21230   78 PEEIIN-PNVDEMSVMTYLSQF 98
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 37-135 5.26e-18

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: 80.08  E-value: 5.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  37 KKTFTAWCNSHLRKAGTA-IDNIEEDFRNGLKLMLLLEVISGETLPKPDR-GKMRFHKIANVNKALDFIASKGVH-LVSI 113
Cdd:cd00014    1 EEELLKWINEVLGEELPVsITDLFESLRDGVLLCKLINKLSPGSIPKINKkPKSPFKKRENINLFLNACKKLGLPeLDLF 80

                         90       100
                 ....*....|....*....|...
gi 442614868 114 GAEEIV-DGNLKMTLGMIWTIIL 135
Cdd:cd00014   81 EPEDLYeKGNLKKVLGTLWALAL 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 538-760 5.48e-17

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.57  E-value: 5.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 538 EFAKRAAPFNNWLDGTREDLVDMFIVHTMEEIQGLIQAHDQFKATLGEADKEFNlivNLVREVESIVKQHQIpgglENPY 617
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVE---ALNELGEQLIEEGHP----DAEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 618 TTLTANDMTRKWSDVRQLVPQRDQTLANELRKQQNNEMLRRqfaekaniVGPWIERQMDAVTAIGMG-LQGSLEDQLHRL 696
Cdd:cd00176   77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGkDLESVEELLKKH 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442614868 697 KEYEQAVYAYKPNIEELEKIHQAVQESMIFEN-RYTNYTMETLRVGWEQLLTSINRNINEVENQI 760
Cdd:cd00176  149 KELEEELEAHEPRLKSLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 36-130 1.02e-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: 73.87  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  36 QKKTFTAWCNSHLRKAGTA--IDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFH-KIANVNKALDFIASKGVHLVS 112
Cdd:cd21213    1 QLQAYVAWVNSQLKKRPGIrpVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAeRKENVEKVLQFMASKRIRMHQ 80

                         90
                 ....*....|....*...
gi 442614868 113 IGAEEIVDGNLKMTLGMI 130
Cdd:cd21213   81 TSAKDIVDGNLKAIMRLI 98
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
 150-253 8.46e-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: 8.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 150 KEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDD 229
Cdd:cd21196    5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84

                         90       100
                 ....*....|....*....|....
gi 442614868 230 LINTPKPdeRAIMTYVSCYYHAFQ 253
Cdd:cd21196   85 VVAGSDP--LGLIAYLSHFHSAFK 106
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 150-249 6.41e-14

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: 68.57  E-value: 6.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 150 KEGLLLWCQrktAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLI-DYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPD 228
Cdd:cd21229    5 KKLMLAWLQ---AVLPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81

                         90       100
                 ....*....|....*....|.
gi 442614868 229 DLINtPKPDERAIMTYVScYY 249
Cdd:cd21229   82 DLSS-PHLDELSGMTYLS-YF 100
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 33-131 1.01e-13

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 68.08  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNSHLRkaGTAIDNIEEDFRNGLKLMLLLEVISGETL-------PKPdrgKMRFHKIANVNKALDFIAS 105
Cdd:cd21219    2 GSREERAFRMWLNSLGL--DPLINNLYEDLRDGLVLLQVLDKIQPGCVnwkkvnkPKP---LNKFKKVENCNYAVDLAKK 76

                         90       100
                 ....*....|....*....|....*.
gi 442614868 106 KGVHLVSIGAEEIVDGNLKMTLGMIW 131
Cdd:cd21219   77 LGFSLVGIGGKDIADGNRKLTLALVW 102
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 148-251 1.07e-13

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: 68.27  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 148 TAKEGLLLWCQRKTApykNVNVQNFHLSFKDGLAFCALIHRHRPDLI-DYAKLSKDNPLENLNTAFDVAEKYLDIPRMLD 226
Cdd:cd21315   16 TPKQRLLGWIQSKVP---DLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92

                         90       100
                 ....*....|....*....|....*
gi 442614868 227 PDDLINtPKPDERAIMTYVSCYYHA 251
Cdd:cd21315   93 PEEMVN-PKVDELSMMTYLSQFPNA 116
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 27-137 3.55e-13

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: 66.84  E-value: 3.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  27 LLDPAWEK--QQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLP------KPDRGKmrfHKIANVNK 98
Cdd:cd21222    6 LFDEAPEKlaEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyhlTPSTDD---EKLHNVKL 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442614868  99 ALDFIASKGVHLVSIGAEEIVDGNLKMTLGMIWTIILRF 137
Cdd:cd21222   83 ALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 775-842 1.30e-12

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 63.34  E-value: 1.30e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442614868 775 EFRSSFNHFDKNRTGRLSPEEFKSCLVSLGysigkDRQGDLDFQRILAVVDPNNTGYVHFDAFLDFMT 842
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLG-----EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 38-139 1.86e-12

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: 64.75  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  38 KTFTAWCNShlRKAGTAIDNIEEDFRNGLKLMLLLE-VISGE------TLPKPDRGKMRFHKIANVNKALDFIASKGVHL 110
Cdd:cd21300   10 RVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSvnwkkvNKAPASAEISRFKAVENTNYAVELGKQLGFSL 87

                         90       100
                 ....*....|....*....|....*....
gi 442614868 111 VSIGAEEIVDGNLKMTLGMIWTiILRFAI 139
Cdd:cd21300   88 VGIQGADITDGSRTLTLALVWQ-LMRFHI 115
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 153-246 1.87e-12

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: 65.40  E-value: 1.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 153 LLLWCQRKTAPYkNVNVQNFHLSFKDGLAFCALIHRHRPDLI------------------------------------DY 196
Cdd:cd21224    5 LLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLpldairqpttqtvdraqdeaedfwvaefspstgdsgLS 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 442614868 197 AKLSKdNPLENLNTAFDVAEKYLDIPRMLDPDDLINTPkPDERAIMTYVS 246
Cdd:cd21224   84 SELLA-NEKRNFKLVQQAVAELGGVPALLRASDMSNTI-PDEKVVILFLS 131
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 145-251 3.82e-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: 63.94  E-value: 3.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 145 EEMTAKEGLLLWCQRKTApykNVNVQNFHLSFKDGLAFCALIHRHRPDLI-DYAKLSKDNPLENLNTAFDVAEKYLDIPR 223
Cdd:cd21314    8 RKQTPKQRLLGWIQNKVP---QLPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQ 84

                         90       100
                 ....*....|....*....|....*...
gi 442614868 224 MLDPDDLINtPKPDERAIMTYVSCYYHA 251
Cdd:cd21314   85 VIAPEEIVD-PNVDEHSVMTYLSQFPKA 111
PTZ00184 PTZ00184
calmodulin; Provisional
 768-874 6.28e-12

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 64.40  E-value: 6.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 768 ISQEQLNEFRSSFNHFDKNRTGRLSPEEFKSCLVSLGYSigkDRQGDLdfQRILAVVDPNNTGYVHFDAFLDFMTRESTD 847
Cdd:PTZ00184   5 LTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQN---PTEAEL--QDMINEVDADGNGTIDFPEFLTLMARKMKD 79

                         90       100
                 ....*....|....*....|....*...
gi 442614868 848 TDTAEQVIDSFRILAAD-KPYILPDELR 874
Cdd:PTZ00184  80 TDSEEEIKEAFKVFDRDgNGFISAAELR 107
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 54-134 8.93e-12

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: 62.61  E-value: 8.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  54 AIDNIEEDFRNGLKLMLLLEVISGetlPKPDRGKMRF------HKIANVNKALDFIASKGV----HLVSIGAEEIVDGNL 123
Cdd:cd21223   25 AVTNLAVDLRDGVRLCRLVELLTG---DWSLLSKLRVpaisrlQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHR 101

                         90
                 ....*....|.
gi 442614868 124 KMTLGMIWTII 134
Cdd:cd21223  102 EKTLALLWRII 112
PTZ00183 PTZ00183
centrin; Provisional
 767-865 2.19e-11

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 62.78  E-value: 2.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 767 GISQEQLNEFRSSFNHFDKNRTGRLSPEEFKSCLVSLGYSIGKDrqgdlDFQRILAVVDPNNTGYVHFDAFLDFMTREST 846
Cdd:PTZ00183  10 GLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKE-----EIKQMIADVDKDGSGKIDFEEFLDIMTKKLG 84

                         90
                 ....*....|....*....
gi 442614868 847 DTDTAEQVIDSFRILAADK 865
Cdd:PTZ00183  85 ERDPREEILKAFRLFDDDK 103
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 38-133 2.52e-11

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: 61.20  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  38 KTFTAWCNSHLRKAGTA--IDNIEEDFRNGLKLMLLLEVISGETLPK-PDRGKMRFHKIANVNKALDFIASKGVHLVSIG 114
Cdd:cd21286    3 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVEDiNGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 82

                         90
                 ....*....|....*....
gi 442614868 115 AEEIVDGNLKMTLGMIWTI 133
Cdd:cd21286   83 AEEIRNGNLKAILGLFFSL 101
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 36-133 5.59e-11

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: 60.75  E-value: 5.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  36 QKKTFTAWCNSHLRKAGTA--IDNIEEDFRNGLKLMLLLEVISGETL------PKpDRGKMrfhkIANVNKALDFIASKG 107
Cdd:cd21285   11 DKQIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKIedingcPK-NRSQM----IENIDACLSFLAAKG 85

                         90       100
                 ....*....|....*....|....*.
gi 442614868 108 VHLVSIGAEEIVDGNLKMTLGMIWTI 133
Cdd:cd21285   86 INIQGLSAEEIRNGNLKAILGLFFSL 111
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
 145-251 7.26e-11

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: 60.11  E-value: 7.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 145 EEMTAKEGLLLWCQRKTaPYknVNVQNFHLSFKDGLAFCALIHRHRPDLI-DYAKLSKDNPLENLNTAFDVAEKYLDIPR 223
Cdd:cd21313    5 KKQTPKQRLLGWIQNKI-PY--LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGVPQ 81

                         90       100
                 ....*....|....*....|....*...
gi 442614868 224 MLDPDDLINtPKPDERAIMTYVSCYYHA 251
Cdd:cd21313   82 VITPEEIIH-PDVDEHSVMTYLSQFPKA 108
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 33-140 3.26e-10

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 58.40  E-value: 3.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNShlrkAGTA--IDNIEEDFRNGLKLMLLLEVI------SGETLPKPDRGKMRFHKIANVNKALDFIA 104
Cdd:cd21298    4 ETREEKTYRNWMNS----LGVNpfVNHLYSDLRDGLVLLQLYDKIkpgvvdWSRVNKPFKKLGANMKKIENCNYAVELGK 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 442614868 105 SKGVHLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQ 140
Cdd:cd21298   80 KLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 535-645 6.05e-10

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 57.33  E-value: 6.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  535 LHLEFAKRAAPFNNWLDGTREDLVDMFIVHTMEEIQGLIQAHDQFKATLGEADKEFNLIVNLVREVESIvkqhqipGGLE 614
Cdd:pfam00435   2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-------GHYA 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 442614868  615 NPYTTLTANDMTRKWSDVRQLVPQRDQTLAN 645
Cdd:pfam00435  75 SEEIQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 656-758 9.68e-09

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 53.86  E-value: 9.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  656 LRRQFAEKANIVGPWIERQMDAVTAIGMGLQ-GSLEDQLHRLKEYEQAVYAYKPNIEELEKIHQAVQESMIFENRYTNYT 734
Cdd:pfam00435   2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDlESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQER 81

                          90       100
                  ....*....|....*....|....
gi 442614868  735 METLRVGWEQLLTSINRNINEVEN 758
Cdd:pfam00435  82 LEELNERWEQLLELAAERKQKLEE 105
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 140-251 1.17e-08

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: 54.04  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 140 QDISVEEMTAKEGLLLWCQRKTApykNVNVQNFHLSFKDGLAFCALIHRHRPDLI-DYAKLSKDNPLENLNTAFDVAEKY 218
Cdd:cd21312    4 EDEEAKKQTPKQRLLGWIQNKLP---QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDW 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 442614868 219 LDIPRMLDPDDLINtPKPDERAIMTYVSCYYHA 251
Cdd:cd21312   81 LGIPQVITPEEIVD-PNVDEHSVMTYLSQFPKA 112
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 159-245 1.39e-08

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: 53.08  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 159 RKTAPykNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKyLDIPRMLDPDDLINtPKPDE 238
Cdd:cd21185   11 RQLLP--DVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMAD-PEVEH 86


                 ....*..
gi 442614868 239 RAIMTYV 245
Cdd:cd21185   87 LGIMAYA 93
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 299-409 2.74e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 52.32  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  299 RLMEEYERLASDLLEWIRRTMPWLNSRQADNSLAGVQKKLEEyrtYRRKHKPPRVeQKAKLEtNFNTLQTKLrLSNRPAY 378
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKK---HKALEAELAA-HQDRVE-ALNELAEKL-IDEGHYA 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 442614868  379 LPTEGKTVSDISNSWKGLELAEKAFEEWLLA 409
Cdd:pfam00435  75 SEEIQERLEELNERWEQLLELAAERKQKLEE 105
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 35-139 7.66e-08

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: 51.35  E-value: 7.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  35 QQKKTFTAWCNShlRKAGTAIDNIEEDFRNGLKLMLLLE-----VISGETLPKPDRgKMRFHKIANVNKALDFIASKGVH 109
Cdd:cd21299    4 REERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDkvspgSVNWKHANKPPI-KMPFKKVENCNQVVKIGKQLKFS 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 442614868 110 LVSIGAEEIVDGNLKMTLGMIWTiILRFAI 139
Cdd:cd21299   81 LVNVAGNDIVQGNKKLILALLWQ-LMRYHM 109
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 158-231 1.18e-06

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


Pssm-ID: 432229  Cd Length: 85  Bit Score: 47.29  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  158 QRKTAPYkNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAK------LSKDNPLENLNTAFDVAEKYLDI-PRMLDPDDL 230
Cdd:pfam11971   3 SQRSLPL-SPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDiclkesMSLADSLYNIQLLQEFCQRHLGNrCCHLTLEDL 81


                  .
gi 442614868  231 I 231
Cdd:pfam11971  82 L 82
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 37-134 1.36e-06

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: 47.95  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  37 KKTFTAWCNSHLRK---------AGTAIDNIEEDFRNGLKLMLLLEVISGETLP--KPDRGKMR--FHKIANVNKALDFI 103
Cdd:cd21217    3 KEAFVEHINSLLADdpdlkhllpIDPDGDDLFEALRDGVLLCKLINKIVPGTIDerKLNKKKPKniFEATENLNLALNAA 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 442614868 104 ASKGVHLVSIGAEEIVDGNLKMTLGMIWTII 134
Cdd:cd21217   83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 143-245 4.71e-06

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: 46.52  E-value: 4.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 143 SVEEMTAKEGLLLWCQR--KTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLID----YAKLSKDNPLENLNTAFDVAE 216
Cdd:cd21218    5 SLLYLPPEEILLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAE 84

                         90       100
                 ....*....|....*....|....*....
gi 442614868 217 KyLDIPRMLDPDDLINtpkPDERAIMTYV 245
Cdd:cd21218   85 K-LGCKYFLTPEDIVS---GNPRLNLAFV 109
SPEC smart00150
Spectrin repeats;
538-643 4.82e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 4.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868   538 EFAKRAAPFNNWLDGTREDLVDMFIVHTMEEIQGLIQAHDQFKATLGEADKEFNLIVNLVREVesIVKQHQipgglENPY 617
Cdd:smart00150   2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQL--IEEGHP-----DAEE 74

                           90       100
                   ....*....|....*....|....*.
gi 442614868   618 TTLTANDMTRKWSDVRQLVPQRDQTL 643
Cdd:smart00150  75 IEERLEELNERWEELKELAEERRQKL 100
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 27-137 9.23e-06

second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-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. 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: 409155  Cd Length: 121  Bit Score: 45.87  E-value: 9.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  27 LLDPAWEKQQ--KKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLP------KPDRGKmrfHKIANVNK 98
Cdd:cd21306    6 LFDHAPDKLNvvKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPlhsfhlTPTSFE---QKVHNVQF 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442614868  99 ALDFIASKGVHLVSIGAEEIVDGNLKMTLGMIWTIILRF 137
Cdd:cd21306   83 AFELMQDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
EF-hand_7 pfam13499
EF-hand domain pair;
774-842 1.13e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.78  E-value: 1.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442614868  774 NEFRSSFNHFDKNRTGRLSPEEFKSCLVSLGYSIGKDRQgdlDFQRILAVVDPNNTGYVHFDAFLDFMT 842
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDE---EVEELFKEFDLDKDGRISFEEFLELYS 67
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
 37-137 1.22e-05

second calponin homology (CH) domain found in alpha-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. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin 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: 409186  Cd Length: 129  Bit Score: 45.76  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  37 KKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLP------KPDRGKmrfHKIANVNKALDFIASKGVHL 110
Cdd:cd21337   22 KKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPlhsfflTPDSFE---QKVLNVSFAFELMQDGGLEK 98

                         90       100
                 ....*....|....*....|....*..
gi 442614868 111 VSIGAEEIVDGNLKMTLGMIWTIILRF 137
Cdd:cd21337   99 PKPRPEDIVNCDLKSTLRVLYNLFTKY 125
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 33-139 3.92e-05

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 44.22  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNShlRKAGTAIDNIEEDFRNGLKLMLLLEVIS----GETLPKPDRGKM--RFHKIANVNKALDFIASK 106
Cdd:cd21331   20 ETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIKvpvdWNKVNKPPYPKLgaNMKKLENCNYAVELGKHP 97

                         90       100       110
                 ....*....|....*....|....*....|....
gi 442614868 107 G-VHLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 139
Cdd:cd21331   98 AkFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 777-842 4.05e-05

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 44.83  E-value: 4.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 777 RSSFNHFDKNRTGRLSPEEFKSCLVSLGYSI------------GKDRQGDL---DFQRILAVV----------DPNNTGY 831
Cdd:cd16180   70 RRLFRRFDRDRSGSIDFNELQNALSSFGYRLspqfvqllvrkfDRRRRGSIsfdDFVEACVTLkrltdafrkyDTNRTGY 149

                         90
                 ....*....|.
gi 442614868 832 VHFDaFLDFMT 842
Cdd:cd16180  150 ATIS-YEDFLT 159
EF-hand_6 pfam13405
EF-hand domain;
775-804 7.88e-05

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 40.24  E-value: 7.88e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 442614868  775 EFRSSFNHFDKNRTGRLSPEEFKSCLVSLG 804
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 43-133 9.50e-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: 42.67  E-value: 9.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  43 WCNSHLRKAGTA---IDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKM--RFHKIANVNKALDFIASKGVHLVsIGAEE 117
Cdd:cd21218   18 WVNYHLKKAGPTkkrVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVlsEEDLEKRAEKVLQAAEKLGCKYF-LTPED 96

                         90
                 ....*....|....*.
gi 442614868 118 IVDGNLKMTLGMIWTI 133
Cdd:cd21218   97 IVSGNPRLNLAFVATL 112
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 37-137 1.69e-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: 41.95  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  37 KKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLP------KPDRGKMRFHkiaNVNKALDFIASKGVHL 110
Cdd:cd21307   18 KKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHlsefflTPSSTSEMLH---NVTLALELLKEGGLLN 94

                         90       100
                 ....*....|....*....|....*..
gi 442614868 111 VSIGAEEIVDGNLKMTLGMIWTIILRF 137
Cdd:cd21307   95 FPVNPEDIVNGDSKATIRVLYCLFSKY 121
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 53-136 3.33e-04

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: 41.28  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  53 TAIDNIEEDFRNGLKLMLLLEVISGETL--------PKPDRGKMRFHKIANVNKALDFIASKGVHLVSIGAEEIVDGNLK 124
Cdd:cd21294   33 TDTFQLFDECKDGLVLSKLINDSVPDTIdervlnkpPRKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREH 112

                         90
                 ....*....|..
gi 442614868 125 MTLGMIWTIILR 136
Cdd:cd21294  113 LILGLIWQIIRR 124
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 33-139 3.49e-04

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: 41.12  E-value: 3.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNShlRKAGTAIDNIEEDFRNGLKLMLLLEV----ISGETLPKPDR----GKMRfhKIANVNKALDFIA 104
Cdd:cd21329    4 ESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpVDWGHVNKPPYpalgGNMK--KIENCNYAVELGK 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 442614868 105 SKG-VHLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 139
Cdd:cd21329   80 NKAkFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTL 115
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 31-134 3.71e-04

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: 41.97  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  31 AWEKQQKKTFTAWCNS---------HLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKI---ANVNK 98
Cdd:cd21325   20 SYSEEEKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFiiqENLNL 99

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 442614868  99 ALDFIASKGVHLVSIGAEEIVDGNLKMTLGMIWTII 134
Cdd:cd21325  100 ALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
774-842 4.18e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.32  E-value: 4.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442614868 774 NEFRSSFNHFDKNRTGRLSPEEFKSCLVSLGYSigkdrqgDLDFQRILAVVDPNNTGYVHFDAFLDFMT 842
Cdd:COG5126   69 PFARAAFDLLDTDGDGKISADEFRRLLTALGVS-------EEEADELFARLDTDGDGKISFEEFVAAVR 130
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 37-103 5.55e-04

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


Pssm-ID: 409070  Cd Length: 106  Bit Score: 40.33  E-value: 5.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442614868  37 KKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPD-----RGKMrfHKIANVNKALDFI 103
Cdd:cd21221    3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqseEGQK--QKLAVVLACVNFL 72
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 776-914 7.76e-04

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 40.73  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 776 FRSSFNHFDKNRTGRLSPEEFKSCLVSLGYSIGKDrqgdlDFQRILAVVDPNNTGYVHFDAFLDFMtRESTDTDTAEQVI 855
Cdd:cd15898    2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEK-----ELKKLFKEVDTNGDGTLTFDEFEELY-KSLTERPELEPIF 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442614868 856 DsfRILAADKPYILPDELRR--------ELPPDQAEYCIQRMppykGPNGVPGALDYMSFSTALYGE 914
Cdd:cd15898   76 K--KYAGTNRDYMTLEEFIRflreeqgeNVSEEECEELIEKY----EPERENRQLSFEGFTNFLLSP 136
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 31-134 1.72e-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: 39.61  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  31 AWEKQQKKTFTAWCNSHLRK---------AGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMR---FHKIANVNK 98
Cdd:cd21324   20 SYSEEEKYAFVNWINKALENdpdckhvipMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKKltpFTIQENLNL 99

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 442614868  99 ALDFIASKGVHLVSIGAEEIVDGNLKMTLGMIWTII 134
Cdd:cd21324  100 ALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 767-866 1.74e-03

EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar proteins; This family represents a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this family is protein Plc1p (also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1) encoded by PLC1 genes from Saccharomyces cerevisiae. ScPlc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that ScPlc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like SCPlc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 39.54  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 767 GISQEQLnefRSSFNHFDKNRTGRLSPEEFKSCLVSLgysigKDRQgdlDFQRILAVVDPNNTGYVHFDAFLDFMT---R 843
Cdd:cd16207   34 NCSESYL---RELFDKADTDKKGYLNFEEFQEFVKLL-----KRRK---DIKAIFKQLTKPGSDGLTLEEFLKFLRdvqK 102

                         90       100
                 ....*....|....*....|...
gi 442614868 844 ESTDTDTAEQVIDSFRILAADKP 866
Cdd:cd16207  103 EDVDRETWEKIFEKFARRIDDSD 125
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 775-803 1.81e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 36.59  E-value: 1.81e-03
                           10        20
                   ....*....|....*....|....*....
gi 442614868   775 EFRSSFNHFDKNRTGRLSPEEFKSCLVSL 803
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
 27-137 2.17e-03

second calponin homology (CH) domain found in beta-parvin; 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. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin 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: 409187  Cd Length: 130  Bit Score: 39.18  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  27 LLDPAWEKQQ--KKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLP------KPDRGKMRFHkiaNVNK 98
Cdd:cd21338   11 LFDHAPDKLSvvKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPlhnfylTPESFDQKVH---NVSF 87

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442614868  99 ALDFIASKGVHLVSIGAEEIVDGNLKMTLGMIWTIILRF 137
Cdd:cd21338   88 AFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKY 126
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 33-139 3.52e-03

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 38.43  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  33 EKQQKKTFTAWCNShlRKAGTAIDNIEEDFRNGLKLMLLLEVIS----GETLPKPDRGKM--RFHKIANVNKALDFIASK 106
Cdd:cd21330   11 ETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLgeNMKKLENCNYAVELGKNK 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 442614868 107 G-VHLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 139
Cdd:cd21330   89 AkFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTL 122
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 771-840 3.59e-03

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 39.12  E-value: 3.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442614868 771 EQLNEF----RSSFNHFDKNRTGRLSPEEFKSCLVSLGYSIgkdrqGDLDFQRILAVVDPNNTGYVHFDAFLDF 840
Cdd:cd16185   59 AALHQFlsnmQNGFEQRDTSRSGRLDANEVHEALAASGFQL-----DPPAFQALFRKFDPDRGGSLGFDDYIEL 127
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
40-131 3.92e-03

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 41.08  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868  40 FTAWCNSHLrkAGTAIDNIEEDFRNGLKLMLLLEVISGE---------TLPKPDRGKMRFHKIANVNKALDFIASKGVHL 110
Cdd:COG5069  384 FTFWLNSLD--VSPEITNLFGDLRDQLILLQALSKKLMPmtvthklvkKQPASGIEENRFKAFENENYAVDLGITEGFSL 461

                         90       100
                 ....*....|....*....|.
gi 442614868 111 VSIGAEEIVDGNlKMTLGMIW 131
Cdd:COG5069  462 VGIKGLEILDGI-RLKLTLVW 481
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 775-803 4.16e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 35.45  E-value: 4.16e-03
                          10        20
                  ....*....|....*....|....*....
gi 442614868  775 EFRSSFNHFDKNRTGRLSPEEFKSCLVSL 803
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 144-231 4.88e-03

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


Pssm-ID: 409145  Cd Length: 109  Bit Score: 37.50  E-value: 4.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 144 VEE---MTAKEGLLLWC--QRKTAPYKNVnVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKy 218
Cdd:cd21296    3 VEEllrLPPEKVLLKWMnfHLKKAGYKKT-VTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEK- 80

                         90
                 ....*....|...
gi 442614868 219 LDIPRMLDPDDLI 231
Cdd:cd21296   81 MNCKRYLTAKDIV 93
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 163-217 9.51e-03

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: 36.78  E-value: 9.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442614868 163 PYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPL------ENLNTAFDVAEK 217
Cdd:cd21217   24 LPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKnifeatENLNLALNAAKK 84
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
413-533 1.00e-02

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 1.00e-02
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614868 413 RLERLEHLAQKFKHKADAHEDWTRGKEEMLQSQDFRQcklnELKALKKKHEAFESDLAAHQDRVEQIAAIAQELNTLEYH 492
Cdd:COG4717  110 ELEELREELEKLEKLLQLLPLYQELEALEAELAELPE----RLEELEERLEELRELEEELEELEAELAELQEELEELLEQ 185

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 442614868 493 DCVSVNARCQRICDQWDRLGALTQRRRTALDEAERILEKID 533
Cdd:COG4717  186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
 
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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