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Conserved domains on  [gi|13123944|sp|O88990|]
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RecName: Full=Alpha-actinin-3; AltName: Full=Alpha-actinin skeletal muscle isoform 3; AltName: Full=F-actin cross-linking protein

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 ...
 149-263 6.65e-87

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: 272.31  E-value: 6.65e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 149 IQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKY 228
Cdd:cd21216   1 IQDISVEELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKH 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 13123944 229 LDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFA 263
Cdd:cd21216  81 LDIPKMLDAEDIVNTPRPDERSVMTYVSCYYHAFA 115
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 41-145 1.81e-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: 241.14  E-value: 1.81e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  41 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKGVKL 120
Cdd:cd21214   1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPERGKMRFHKIANVNKALDFIASKGVKL 80

                        90       100
                ....*....|....*....|....*
gi 13123944 121 VSIGAEEIVDGNLKMTLGMIWTIIL 145
Cdd:cd21214  81 VSIGAEEIVDGNLKMTLGMIWTIIL 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 408-635 3.12e-32

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: 124.87  E-value: 3.12e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 408 LAEKFQQKASLHEAWTRGKEEMLNQHDYeSASLQEVRALLRRHEAFESDLAAHQDRVEHIAALAQELNELDYHEAASVNS 487
Cdd:cd00176   1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 488 RCQAICDQWDNLGTLTQKRRDALERMEKLLETIDQLQLefarraapFNNWLDGAIEDLQDVWLVHSVEETQSLLTAHEQF 567
Cdd:cd00176  80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGKDLESVEELLKKHKEL 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13123944 568 KATLPEADRERGAILGIQGEIQKicqtygLRPKSGNPYITLSSQDINNKWDTVRKLVPSRDQTLQEEL 635
Cdd:cd00176 152 EEELEAHEPRLKSLNELAEELLE------EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
EFhand_Ca_insen pfam08726
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 830-896 3.55e-30

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: 113.56  E-value: 3.55e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13123944   830 ETDTAEQVVASFKILAGDKNYITPEELRRELPAEQAEYCIRRMAPYKGS--GAPSGALDYVAFSSALYG 896
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 290-513 6.25e-13

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: 68.63  E-value: 6.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 290 EEYEKLASELLEWIRRTVPWLENRVGEPSMS---AMQRKLEDFRDYRRLHKPpRVQEkcqleinFNTLQTKLRLSHRPAf 366
Cdd:cd00176   3 QQFLRDADELEAWLSEKEELLSSTDYGDDLEsveALLKKHEALEAELAAHEE-RVEA-------LNELGEQLIEEGHPD- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 367 MPSEGKLVSDIANAWRGLEQvekgyedwlLSEIRRlQRLQHLAEKFQQKASLH--EAWTRGKEEMLNQHDYESaSLQEVR 444
Cdd:cd00176  74 AEEIQERLEELNQRWEELRE---------LAEERR-QRLEEALDLQQFFRDADdlEQWLEEKEAALASEDLGK-DLESVE 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 445 ALLRRHEAFESDLAAHQDRVEHIAALAQEL-NELDYHEAASVNSRCQAICDQWDNLGTLTQKRRDALERM 513
Cdd:cd00176 143 ELLKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
PTZ00184 super family cl33172
calmodulin; Provisional
 753-857 1.02e-11

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 63.63  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  753 AKGLSQEQLNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFIDFMTRETAETD 832
Cdd:PTZ00184   2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTD 81

                         90       100
                 ....*....|....*....|....*.
gi 13123944  833 TAEQVVASFKILAGDKN-YITPEELR 857
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNgFISAAELR 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 526-746 1.47e-11

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: 64.77  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 526 EFARRAAPFNNWLDGAIEDLQDVWLVHSVEETQSLLTAHEQFKATLpEADRERgaILGIQGEIQKICQTYGlrpkSGNPY 605
Cdd:cd00176   4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAEL-AAHEER--VEALNELGEQLIEEGH----PDAEE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 606 ITLSSQDINNKWDTVRKLVPSRDQTLQEELARQqvnerlrrQFAAQANAIGPWIQGKVEEVGRLAAG-LAGSLEEQMAGL 684
Cdd:cd00176  77 IQERLEELNQRWEELRELAEERRQRLEEALDLQ--------QFFRDADDLEQWLEEKEAALASEDLGkDLESVEELLKKH 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13123944 685 RQQEQNIINYKSNIDRLEGDHQLLQESLVFDNKHTVY-SMEHIRVGWEQLLTSIARTINEVEN 746
Cdd:cd00176 149 KELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEeKLEELNERWEELLELAEERQKKLEE 211
 
Name Accession Description Interval E-value
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 149-263 6.65e-87

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: 272.31  E-value: 6.65e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 149 IQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKY 228
Cdd:cd21216   1 IQDISVEELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKH 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 13123944 229 LDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFA 263
Cdd:cd21216  81 LDIPKMLDAEDIVNTPRPDERSVMTYVSCYYHAFA 115
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 41-145 1.81e-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: 241.14  E-value: 1.81e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  41 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKGVKL 120
Cdd:cd21214   1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPERGKMRFHKIANVNKALDFIASKGVKL 80

                        90       100
                ....*....|....*....|....*
gi 13123944 121 VSIGAEEIVDGNLKMTLGMIWTIIL 145
Cdd:cd21214  81 VSIGAEEIVDGNLKMTLGMIWTIIL 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
42-305 1.33e-67

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 237.15  E-value: 1.33e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  42 WEKQQRKTFTAWCNSHLRKAGT-QIENIEEDFRNGLKLMLLLEVISGERLPRPDKGK-MRFHKIANVNKALDFIASKGVK 119
Cdd:COG5069   6 WQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPeTRIHVMENVSGRLEFIKGKGVK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 120 LVSIGAEEIVDGNLKMTLGMIWTIILRFAIQDISVE-ETSAKEGLLLWCQRKTAPYRN-VNVQNFHTSWKDGLALCALIH 197
Cdd:COG5069  86 LFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEgELTKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIH 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 198 RHRPDLIDYAKL---RKDDPIgNLNTAFEVAEKYLDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAANR 274
Cdd:COG5069 166 DSRPDTLDPNVLdlqKKNKAL-NNFQAFENANKVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRFGLLEKIDIALHR 244

                       250       260       270
                ....*....|....*....|....*....|.
gi 13123944 275 ICKVLAVNQENEKLMEEYEKLASELLEWIRR 305
Cdd:COG5069 245 VYRLLEADETLIQLRLPYEIILLRLLNLIHL 275
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 158-262 4.31e-33

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: 123.17  E-value: 4.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944   158 SAKEGLLLWCQRKTAPY-RNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKD--DPIGNLNTAFEVAEKYLDIPKM 234
Cdd:pfam00307   2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPKV 81

                          90       100
                  ....*....|....*....|....*....
gi 13123944   235 L-DAEDIVNtpkPDEKAIMTYVSCFYHAF 262
Cdd:pfam00307  82 LiEPEDLVE---GDNKSVLTYLASLFRRF 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 408-635 3.12e-32

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: 124.87  E-value: 3.12e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 408 LAEKFQQKASLHEAWTRGKEEMLNQHDYeSASLQEVRALLRRHEAFESDLAAHQDRVEHIAALAQELNELDYHEAASVNS 487
Cdd:cd00176   1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 488 RCQAICDQWDNLGTLTQKRRDALERMEKLLETIDQLQLefarraapFNNWLDGAIEDLQDVWLVHSVEETQSLLTAHEQF 567
Cdd:cd00176  80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGKDLESVEELLKKHKEL 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13123944 568 KATLPEADRERGAILGIQGEIQKicqtygLRPKSGNPYITLSSQDINNKWDTVRKLVPSRDQTLQEEL 635
Cdd:cd00176 152 EEELEAHEPRLKSLNELAEELLE------EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
EFhand_Ca_insen pfam08726
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 830-896 3.55e-30

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: 113.56  E-value: 3.55e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13123944   830 ETDTAEQVVASFKILAGDKNYITPEELRRELPAEQAEYCIRRMAPYKGS--GAPSGALDYVAFSSALYG 896
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 161-256 2.09e-25

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: 101.24  E-value: 2.09e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944    161 EGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKD----DPIGNLNTAFEVAEKYLDIPKMLD 236
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|
gi 13123944    237 AEDIVnTPKPDEKAIMTYVS 256
Cdd:smart00033  81 PEDLV-EGPKLILGVIWTLI 99
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 44-149 2.49e-24

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: 98.51  E-value: 2.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944    44 KQQRKTFTAWCNSHLRKAG--TQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASK-GVKL 120
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKlGVPK 80

                          90       100
                  ....*....|....*....|....*....
gi 13123944   121 VSIGAEEIVDGNLKMTLGMIWTIILRFAI 149
Cdd:pfam00307  81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 407-512 2.23e-23

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: 95.46  E-value: 2.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944   407 HLAEKFQQKASLHEAWTRGKEEMLNQHDYESaSLQEVRALLRRHEAFESDLAAHQDRVEHIAALAQELNELDYHEAASVN 486
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                          90       100
                  ....*....|....*....|....*.
gi 13123944   487 SRCQAICDQWDNLGTLTQKRRDALER 512
Cdd:pfam00435  80 ERLEELNERWEQLLELAAERKQKLEE 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 48-146 8.56e-22

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 90.84  E-value: 8.56e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944     48 KTFTAWCNSHLRKAGTQ-IENIEEDFRNGLKLMLLLEVISGERLP--RPDKGKMRFHKIANVNKALDFIASKGVKLVSIG 124
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVDkkKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 13123944    125 AEEIVDGNlKMTLGMIWTIILR 146
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101
SPEC smart00150
Spectrin repeats;
410-511 8.19e-19

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 82.38  E-value: 8.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944    410 EKFQQKASLHEAWTRGKEEMLNQHDYeSASLQEVRALLRRHEAFESDLAAHQDRVEHIAALAQELNELDYHEAASVNSRC 489
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                           90       100
                   ....*....|....*....|..
gi 13123944    490 QAICDQWDNLGTLTQKRRDALE 511
Cdd:smart00150  80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 290-513 6.25e-13

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: 68.63  E-value: 6.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 290 EEYEKLASELLEWIRRTVPWLENRVGEPSMS---AMQRKLEDFRDYRRLHKPpRVQEkcqleinFNTLQTKLRLSHRPAf 366
Cdd:cd00176   3 QQFLRDADELEAWLSEKEELLSSTDYGDDLEsveALLKKHEALEAELAAHEE-RVEA-------LNELGEQLIEEGHPD- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 367 MPSEGKLVSDIANAWRGLEQvekgyedwlLSEIRRlQRLQHLAEKFQQKASLH--EAWTRGKEEMLNQHDYESaSLQEVR 444
Cdd:cd00176  74 AEEIQERLEELNQRWEELRE---------LAEERR-QRLEEALDLQQFFRDADdlEQWLEEKEAALASEDLGK-DLESVE 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 445 ALLRRHEAFESDLAAHQDRVEHIAALAQEL-NELDYHEAASVNSRCQAICDQWDNLGTLTQKRRDALERM 513
Cdd:cd00176 143 ELLKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
PTZ00184 PTZ00184
calmodulin; Provisional
 753-857 1.02e-11

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 63.63  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  753 AKGLSQEQLNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFIDFMTRETAETD 832
Cdd:PTZ00184   2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTD 81

                         90       100
                 ....*....|....*....|....*.
gi 13123944  833 TAEQVVASFKILAGDKN-YITPEELR 857
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNgFISAAELR 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 526-746 1.47e-11

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: 64.77  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 526 EFARRAAPFNNWLDGAIEDLQDVWLVHSVEETQSLLTAHEQFKATLpEADRERgaILGIQGEIQKICQTYGlrpkSGNPY 605
Cdd:cd00176   4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAEL-AAHEER--VEALNELGEQLIEEGH----PDAEE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 606 ITLSSQDINNKWDTVRKLVPSRDQTLQEELARQqvnerlrrQFAAQANAIGPWIQGKVEEVGRLAAG-LAGSLEEQMAGL 684
Cdd:cd00176  77 IQERLEELNQRWEELRELAEERRQRLEEALDLQ--------QFFRDADDLEQWLEEKEAALASEDLGkDLESVEELLKKH 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13123944 685 RQQEQNIINYKSNIDRLEGDHQLLQESLVFDNKHTVY-SMEHIRVGWEQLLTSIARTINEVEN 746
Cdd:cd00176 149 KELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEeKLEELNERWEELLELAEERQKKLEE 211
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 763-825 3.37e-11

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: 59.48  E-value: 3.37e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13123944 763 EFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFIDFMT 825
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 643-746 5.24e-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: 54.63  E-value: 5.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944   643 RLRRQFAAQANAIGPWIQGKVEEVG-RLAAGLAGSLEEQMAGLRQQEQNIINYKSNIDRLEGDHQLLQESLVFDNKHTVY 721
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSsEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                          90       100
                  ....*....|....*....|....*
gi 13123944   722 SMEHIRVGWEQLLTSIARTINEVEN 746
Cdd:pfam00435  81 RLEELNERWEQLLELAAERKQKLEE 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
502-862 8.28e-09

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 59.18  E-value: 8.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 502 LTQKRRDALERMEKLLE---TIDQLQLEFARRAApfnNWLdGAIEDLQDVWLVHSVEETQSLLTAH----EQFKATLPEA 574
Cdd:COG5069 234 LLEKIDIALHRVYRLLEadeTLIQLRLPYEIILL---RLL-NLIHLKQANWKVVNFSKDVSDGENYtdllNQLNALCSRA 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 575 DRERGAILGIQGEIQKICQTYGLR---PKSGNPYITLSSQdinnkwdtvRKLVPSRD--QTLQEELARQQVNERLRRQFA 649
Cdd:COG5069 310 PLETTDLHSLAGQILQNAEKYDCRkylPPAGNPKLDLAFV---------AHLFNTHPgqEPLEEEEKPEIEEFDAEGEFE 380

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 650 AQANAIgpWIqgkveevgrLAAGLAGSLEEQMAGLRQQEQNIINYKSNIDRLEGDHQL---LQESLVFDNKHTVYSMEHI 726
Cdd:COG5069 381 ARVFTF--WL---------NSLDVSPEITNLFGDLRDQLILLQALSKKLMPMTVTHKLvkkQPASGIEENRFKAFENENY 449

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 727 RVGWEQLLTSIARTINEVENQVLTRDAKGLSQEQLNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTm 806
Cdd:COG5069 450 AVDLGITEGFSLVGIKGLEILDGIRLKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFG- 528

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 807 vdpNAAGVVTFQAFIDFmTRETAET----DTAEQVVASFKILAGDKNYITPEELRRELPA 862
Cdd:COG5069 529 ---DPAGSVSGVFYLDV-LKGIHSElvdyDLVTRGFTEFDDIADARSLAISSKILRSLGA 584
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 287-396 1.99e-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: 52.71  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944   287 KLMEEYEKLASELLEWIRRTVPWLENRVGEPSMSAMQRKLedfRDYRRLHKPPRVQEKCQLEInfNTLQTKLrLSHRPAF 366
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALL---KKHKALEAELAAHQDRVEAL--NELAEKL-IDEGHYA 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 13123944   367 MPSEGKLVSDIANAWRGLEQVEKGYEDWLL 396
Cdd:pfam00435  75 SEEIQERLEELNERWEQLLELAAERKQKLE 104
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
359-529 4.67e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 4.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 359 RLSHrpafmpSEgKLVSDIANAWRGLEQVEKGYEDWLLSEIRRLQRLQHLAEKFQQ-KASLHEAW------TRGKEEMLN 431
Cdd:COG0497 217 RLSN------AE-KLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAElAERLESALieleeaASELRRYLD 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 432 QHDYESASLQEV-------RALLRRH-----------EAFESDLAAHQDRVEHIAALAQELNEL--DYHEAASvnsrcqa 491
Cdd:COG0497 290 SLEFDPERLEEVeerlallRRLARKYgvtveellayaEELRAELAELENSDERLEELEAELAEAeaELLEAAE------- 362

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 13123944 492 icdqwdnlgTLTQKRRDALERMEKLLET-IDQLQLEFAR 529
Cdd:COG0497 363 ---------KLSAARKKAAKKLEKAVTAeLADLGMPNAR 392
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
759-872 7.56e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 7.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 759 EQLNEFRASFNHFDRKRNGMMEPDDFRAclismgydLGEVEFARIMTMVDPNAAGVVTFQAFIDFMTRETAETDtAEQVV 838
Cdd:COG5126   2 LQRRKLDRRFDLLDADGDGVLERDDFEA--------LFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFAR 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13123944 839 ASFKILagDKN---YITPEELRR-----ELPAEQAEYCIRRM 872
Cdd:COG5126  73 AAFDLL--DTDgdgKISADEFRRlltalGVSEEEADELFARL 112
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
50-141 1.74e-03

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 41.85  E-value: 1.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  50 FTAWCNSHLrkAGTQIENIEEDFRNGLKLMLLLEVISGE---------RLPRPDKGKMRFHKIANVNKALDFIASKGVKL 120
Cdd:COG5069 384 FTFWLNSLD--VSPEITNLFGDLRDQLILLQALSKKLMPmtvthklvkKQPASGIEENRFKAFENENYAVDLGITEGFSL 461

                        90       100
                ....*....|....*....|.
gi 13123944 121 VSIGAEEIVDGNlKMTLGMIW 141
Cdd:COG5069 462 VGIKGLEILDGI-RLKLTLVW 481
EF-hand_6 pfam13405
EF-hand domain;
763-792 6.51e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 6.51e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 13123944   763 EFRASFNHFDRKRNGMMEPDDFRACLISMG 792
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
 
Name Accession Description Interval E-value
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 149-263 6.65e-87

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: 272.31  E-value: 6.65e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 149 IQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKY 228
Cdd:cd21216   1 IQDISVEELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKH 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 13123944 229 LDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFA 263
Cdd:cd21216  81 LDIPKMLDAEDIVNTPRPDERSVMTYVSCYYHAFA 115
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 149-272 8.72e-83

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: 261.58  E-value: 8.72e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 149 IQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKY 228
Cdd:cd21289   1 IQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKY 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 13123944 229 LDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAA 272
Cdd:cd21289  81 LDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAA 124
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
 149-272 1.24e-77

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: 248.06  E-value: 1.24e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 149 IQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKY 228
Cdd:cd21288   1 IQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKH 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 13123944 229 LDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAA 272
Cdd:cd21288  81 LDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAA 124
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 41-145 1.81e-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: 241.14  E-value: 1.81e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  41 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKGVKL 120
Cdd:cd21214   1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPERGKMRFHKIANVNKALDFIASKGVKL 80

                        90       100
                ....*....|....*....|....*
gi 13123944 121 VSIGAEEIVDGNLKMTLGMIWTIIL 145
Cdd:cd21214  81 VSIGAEEIVDGNLKMTLGMIWTIIL 105
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
 149-267 1.45e-70

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: 228.82  E-value: 1.45e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 149 IQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKY 228
Cdd:cd21287   1 IQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKY 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 13123944 229 LDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQ 267
Cdd:cd21287  81 LDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQK 119
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
 146-267 4.21e-70

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: 227.66  E-value: 4.21e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 146 RFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVA 225
Cdd:cd21290   1 RFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13123944 226 EKYLDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQ 267
Cdd:cd21290  81 EKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQK 122
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
42-305 1.33e-67

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 237.15  E-value: 1.33e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  42 WEKQQRKTFTAWCNSHLRKAGT-QIENIEEDFRNGLKLMLLLEVISGERLPRPDKGK-MRFHKIANVNKALDFIASKGVK 119
Cdd:COG5069   6 WQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPeTRIHVMENVSGRLEFIKGKGVK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 120 LVSIGAEEIVDGNLKMTLGMIWTIILRFAIQDISVE-ETSAKEGLLLWCQRKTAPYRN-VNVQNFHTSWKDGLALCALIH 197
Cdd:COG5069  86 LFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEgELTKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIH 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 198 RHRPDLIDYAKL---RKDDPIgNLNTAFEVAEKYLDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAANR 274
Cdd:COG5069 166 DSRPDTLDPNVLdlqKKNKAL-NNFQAFENANKVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRFGLLEKIDIALHR 244

                       250       260       270
                ....*....|....*....|....*....|.
gi 13123944 275 ICKVLAVNQENEKLMEEYEKLASELLEWIRR 305
Cdd:COG5069 245 VYRLLEADETLIQLRLPYEIILLRLLNLIHL 275
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 158-262 1.53e-57

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: 192.24  E-value: 1.53e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 237
Cdd:cd21194   2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81

                        90       100
                ....*....|....*....|....*
gi 13123944 238 EDiVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21194  82 ED-VDVARPDEKSIMTYVASYYHYF 105
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 158-262 1.70e-54

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: 183.75  E-value: 1.70e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 237
Cdd:cd21248   2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81

                        90       100
                ....*....|....*....|....*
gi 13123944 238 EDiVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21248  82 ED-VNVEQPDEKSIITYVVTYYHYF 105
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 149-263 1.95e-54

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: 184.27  E-value: 1.95e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 149 IQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKY 228
Cdd:cd21291   1 IADINEEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKE 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 13123944 229 LDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFA 263
Cdd:cd21291  81 IGIPQLLDVEDVCDVAKPDERSIMTYVAYYFHAFS 115
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 158-263 1.48e-48

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: 167.35  E-value: 1.48e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 237
Cdd:cd21249   4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLDP 83

                        90       100
                ....*....|....*....|....*.
gi 13123944 238 EDIVnTPKPDEKAIMTYVSCFYHAFA 263
Cdd:cd21249  84 EDVA-VPHPDERSIMTYVSLYYHYFS 108
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
 155-263 1.06e-46

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: 162.10  E-value: 1.06e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 155 EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKM 234
Cdd:cd21319   2 ETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKL 81

                        90       100
                ....*....|....*....|....*....
gi 13123944 235 LDAEDiVNTPKPDEKAIMTYVSCFYHAFA 263
Cdd:cd21319  82 LDPED-VFTENPDEKSIITYVVAFYHYFS 109
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 46-147 1.13e-45

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: 159.10  E-value: 1.13e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  46 QRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRpDKGKMRFHKIANVNKALDFIASKGVKLVSIGA 125
Cdd:cd21188   4 QKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPR-ERGRMRFHRLQNVQTALDFLKYRKIKLVNIRA 82

                        90       100
                ....*....|....*....|..
gi 13123944 126 EEIVDGNLKMTLGMIWTIILRF 147
Cdd:cd21188  83 EDIVDGNPKLTLGLIWTIILHF 104
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 46-146 5.53e-45

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: 157.46  E-value: 5.53e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  46 QRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKgVKLVSIGA 125
Cdd:cd21193  17 QKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRGRLRVQKIENVNKALAFLKTK-VRLENIGA 95

                        90       100
                ....*....|....*....|.
gi 13123944 126 EEIVDGNLKMTLGMIWTIILR 146
Cdd:cd21193  96 EDIVDGNPRLILGLIWTIILR 116
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 158-262 3.61e-44

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: 154.86  E-value: 3.61e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 237
Cdd:cd21189   1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80

                        90       100
                ....*....|....*....|....*
gi 13123944 238 EDiVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21189  81 ED-VDVPEPDEKSIITYVSSLYDVF 104
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 158-262 1.27e-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: 150.58  E-value: 1.27e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 237
Cdd:cd21253   1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80

                        90       100
                ....*....|....*....|....*
gi 13123944 238 EDIVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21253  81 EDMVALKVPDKLSILTYVSQYYNYF 105
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 42-147 2.73e-42

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: 149.47  E-value: 2.73e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  42 WEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKG-KMRFHKIANVNKALDFIASKGVKL 120
Cdd:cd21215   1 WVDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNpKMRVQKLENVNKALEFIKSRGVKL 80

                        90       100
                ....*....|....*....|....*..
gi 13123944 121 VSIGAEEIVDGNLKMTLGMIWTIILRF 147
Cdd:cd21215  81 TNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 43-146 2.74e-42

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: 149.82  E-value: 2.74e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKGVKLVS 122
Cdd:cd21246  14 EAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKMRIHCLENVDKALQFLKEQRVHLEN 93

                        90       100
                ....*....|....*....|....
gi 13123944 123 IGAEEIVDGNLKMTLGMIWTIILR 146
Cdd:cd21246  94 MGSHDIVDGNHRLTLGLIWTIILR 117
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 155-263 1.68e-41

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: 147.90  E-value: 1.68e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 155 EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKM 234
Cdd:cd21321   2 EKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKL 81

                        90       100
                ....*....|....*....|....*....
gi 13123944 235 LDAEDiVNTPKPDEKAIMTYVSCFYHAFA 263
Cdd:cd21321  82 LDPED-VNVDQPDEKSIITYVATYYHYFS 109
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 161-262 2.04e-39

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: 141.27  E-value: 2.04e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 161 EGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDI 240
Cdd:cd22198   3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEM 82

                        90       100
                ....*....|....*....|..
gi 13123944 241 VNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd22198  83 ASLAVPDKLSMVSYLSQFYEAF 104
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 155-263 3.86e-39

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: 141.34  E-value: 3.86e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 155 EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKM 234
Cdd:cd21322  14 ETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLTKL 93

                        90       100
                ....*....|....*....|....*....
gi 13123944 235 LDAEDiVNTPKPDEKAIMTYVSCFYHAFA 263
Cdd:cd21322  94 LDPED-VNMEAPDEKSIITYVVSFYHYFS 121
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 163-259 2.62e-37

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: 135.25  E-value: 2.62e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 163 LLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDiVN 242
Cdd:cd21187   5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED-VN 83

                        90
                ....*....|....*..
gi 13123944 243 TPKPDEKAIMTYVSCFY 259
Cdd:cd21187  84 VEQPDKKSILMYVTSLF 100
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 46-150 3.97e-37

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: 134.82  E-value: 3.97e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  46 QRKTFTAWCNSHLRKAG-TQIENIEEDFRNGLKLMLLLEVISGERLPrPDKGKMRFHKIANVNKALDFIASKGVKLVSIG 124
Cdd:cd21186   3 QKKTFTKWINSQLSKANkPPIKDLFEDLRDGTRLLALLEVLTGKKLK-PEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81

                        90       100
                ....*....|....*....|....*.
gi 13123944 125 AEEIVDGNLKMTLGMIWTIILRFAIQ 150
Cdd:cd21186  82 SNDIVDGNPKLTLGLVWSIILHWQVK 107
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 158-263 3.46e-36

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: 132.15  E-value: 3.46e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 237
Cdd:cd21320   2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81

                        90       100
                ....*....|....*....|....*.
gi 13123944 238 EDiVNTPKPDEKAIMTYVSCFYHAFA 263
Cdd:cd21320  82 ED-ISVDHPDEKSIITYVVTYYHYFS 106
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
 157-262 1.39e-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: 130.52  E-value: 1.39e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 157 TSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLD 236
Cdd:cd21243   4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83

                        90       100
                ....*....|....*....|....*.
gi 13123944 237 AEDiVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21243  84 PED-VDVDKPDEKSIMTYVAQFLKKY 108
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 42-149 1.46e-35

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: 130.49  E-value: 1.46e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  42 WEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRP-DKGKMRFHKIANVNKALDFIASKGVKL 120
Cdd:cd21227   1 WVEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRViKKPLNQHQKLENVTLALKAMAEDGIKL 80

                        90       100
                ....*....|....*....|....*....
gi 13123944 121 VSIGAEEIVDGNLKMTLGMIWTIILRFAI 149
Cdd:cd21227  81 VNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 159-262 1.96e-35

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: 129.96  E-value: 1.96e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 159 AKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAE 238
Cdd:cd21197   1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80

                        90       100
                ....*....|....*....|....
gi 13123944 239 DIVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21197  81 DMVTMHVPDRLSIITYVSQYYNHF 104
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 43-146 1.97e-35

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: 131.30  E-value: 1.97e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKGVKLVS 122
Cdd:cd21318  36 EAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRMRIHSLENVDKALQFLKEQRVHLEN 115

                        90       100
                ....*....|....*....|....
gi 13123944 123 IGAEEIVDGNLKMTLGMIWTIILR 146
Cdd:cd21318 116 VGSHDIVDGNHRLTLGLIWTIILR 139
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 43-154 3.40e-35

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: 130.10  E-value: 3.40e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRpDKGKMRFHKIANVNKALDFIASKGVKLVS 122
Cdd:cd21236  15 DKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALDYLKRRQVKLVN 93

                        90       100       110
                ....*....|....*....|....*....|..
gi 13123944 123 IGAEEIVDGNLKMTLGMIWTIILRFAIQDISV 154
Cdd:cd21236  94 IRNDDITDGNPKLTLGLIWTIILHFQISDIHV 125
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
 159-262 3.70e-35

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: 129.22  E-value: 3.70e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 159 AKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAE 238
Cdd:cd21252   1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80

                        90       100
                ....*....|....*....|....
gi 13123944 239 DIVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21252  81 DMVSMKVPDCLSIMTYVSQYYNHF 104
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 29-146 1.34e-34

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: 128.63  E-value: 1.34e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  29 EEDWDRD------------LLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKG 96
Cdd:cd21317   3 DDDWDNDnssarlfersriKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKG 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 13123944  97 KMRFHKIANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILR 146
Cdd:cd21317  83 RMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 43-150 4.68e-34

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: 126.34  E-value: 4.68e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNSHL--RKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRpDKGKM--RFHKIANVNKALDFIASKGV 118
Cdd:cd21241   3 ERVQKKTFTNWINSYLakRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPC-EKGRRlkRVHFLSNINTALKFLESKKI 81

                        90       100       110
                ....*....|....*....|....*....|..
gi 13123944 119 KLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQ 150
Cdd:cd21241  82 KLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 43-154 1.06e-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: 125.52  E-value: 1.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRpDKGKMRFHKIANVNKALDFIASKGVKLVS 122
Cdd:cd21235   4 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 82

                        90       100       110
                ....*....|....*....|....*....|..
gi 13123944 123 IGAEEIVDGNLKMTLGMIWTIILRFAIQDISV 154
Cdd:cd21235  83 IRNDDIADGNPKLTLGLIWTIILHFQISDIQV 114
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 31-149 2.37e-33

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: 124.49  E-value: 2.37e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  31 DWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKG-KMRFHKIANVNKA 109
Cdd:cd21311   1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRpTFRSQKLENVSVA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13123944 110 LDFIAS-KGVKLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 149
Cdd:cd21311  81 LKFLEEdEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
 158-262 3.52e-33

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: 123.63  E-value: 3.52e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYlDIPKMLDA 237
Cdd:cd21199   8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESV-GIPTTLTI 86

                        90       100
                ....*....|....*....|....*
gi 13123944 238 EDIVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21199  87 DEMVSMERPDWQSVMSYVTAIYKHF 111
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 158-262 4.31e-33

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: 123.17  E-value: 4.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944   158 SAKEGLLLWCQRKTAPY-RNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKD--DPIGNLNTAFEVAEKYLDIPKM 234
Cdd:pfam00307   2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPKV 81

                          90       100
                  ....*....|....*....|....*....
gi 13123944   235 L-DAEDIVNtpkPDEKAIMTYVSCFYHAF 262
Cdd:pfam00307  82 LiEPEDLVE---GDNKSVLTYLASLFRRF 107
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 156-263 8.18e-33

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: 122.53  E-value: 8.18e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 156 ETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKML 235
Cdd:cd21192   1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLL 80

                        90       100
                ....*....|....*....|....*...
gi 13123944 236 DAEDiVNTPKPDEKAIMTYVSCFYHAFA 263
Cdd:cd21192  81 EVED-VLVDKPDERSIMTYVSQFLRMFP 107
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 161-262 2.17e-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: 2.17e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 161 EGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDi 240
Cdd:cd21226   3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAED- 81

                        90       100
                ....*....|....*....|..
gi 13123944 241 VNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21226  82 VMTGNPDERSIVLYTSLFYHAF 103
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 158-262 2.52e-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: 2.52e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 237
Cdd:cd21200   1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80

                        90       100
                ....*....|....*....|....*.
gi 13123944 238 EDIVN-TPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21200  81 EDMVRmGNRPDWKCVFTYVQSLYRHL 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 408-635 3.12e-32

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: 124.87  E-value: 3.12e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 408 LAEKFQQKASLHEAWTRGKEEMLNQHDYeSASLQEVRALLRRHEAFESDLAAHQDRVEHIAALAQELNELDYHEAASVNS 487
Cdd:cd00176   1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 488 RCQAICDQWDNLGTLTQKRRDALERMEKLLETIDQLQLefarraapFNNWLDGAIEDLQDVWLVHSVEETQSLLTAHEQF 567
Cdd:cd00176  80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEKEAALASEDLGKDLESVEELLKKHKEL 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13123944 568 KATLPEADRERGAILGIQGEIQKicqtygLRPKSGNPYITLSSQDINNKWDTVRKLVPSRDQTLQEEL 635
Cdd:cd00176 152 EEELEAHEPRLKSLNELAEELLE------EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 158-255 2.13e-31

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


Pssm-ID: 409047  Cd Length: 105  Bit Score: 118.30  E-value: 2.13e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 237
Cdd:cd21198   1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79

                        90
                ....*....|....*...
gi 13123944 238 EDIVNTPKPDEKAIMTYV 255
Cdd:cd21198  80 ADMVLLSVPDKLSVMTYL 97
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 43-158 2.64e-31

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: 118.60  E-value: 2.64e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRpDKGKMRFHKIANVNKALDFIASKGVKLVS 122
Cdd:cd21237   4 DRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPR-EKGRMRFHRLQNVQIALDFLKQRQVKLVN 82

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 13123944 123 IGAEEIVDGNLKMTLGMIWTIILRFAIQDISVEETS 158
Cdd:cd21237  83 IRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 42-147 5.11e-31

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: 117.58  E-value: 5.11e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  42 WEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRF--HKIANVNKALDFIASKGVK 119
Cdd:cd21183   1 WKRIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYNRRPAFqqHYLENVSTALKFIEADHIK 80

                        90       100
                ....*....|....*....|....*...
gi 13123944 120 LVSIGAEEIVDGNLKMTLGMIWTIILRF 147
Cdd:cd21183  81 LVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
 163-264 1.06e-30

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: 116.52  E-value: 1.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 163 LLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDIVN 242
Cdd:cd21250   9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMAS 88

                        90       100
                ....*....|....*....|..
gi 13123944 243 TPKPDEKAIMTYVSCFYHAFAG 264
Cdd:cd21250  89 AEEPDKLSMVMYLSKFYELFRG 110
EFhand_Ca_insen pfam08726
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 830-896 3.55e-30

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: 113.56  E-value: 3.55e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13123944   830 ETDTAEQVVASFKILAGDKNYITPEELRRELPAEQAEYCIRRMAPYKGS--GAPSGALDYVAFSSALYG 896
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKPYVTEEDLRRELTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
 163-264 3.82e-30

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: 115.14  E-value: 3.82e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 163 LLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDIVN 242
Cdd:cd21195   9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMAS 88

                        90       100
                ....*....|....*....|..
gi 13123944 243 TPKPDEKAIMTYVSCFYHAFAG 264
Cdd:cd21195  89 AQEPDKLSMVMYLSKFYELFRG 110
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 158-262 3.98e-30

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: 114.70  E-value: 3.98e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 237
Cdd:cd21239   1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79

                        90       100
                ....*....|....*....|....*
gi 13123944 238 EDiVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21239  80 ED-VDVSSPDEKSVITYVSSLYDVF 103
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 33-149 5.12e-30

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: 115.13  E-value: 5.12e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  33 DRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERL-----PRPDKGKMRFHkiaNVN 107
Cdd:cd21310   4 EKDLAEDAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMyrkyhPRPNFRQMKLE---NVS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13123944 108 KALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 149
Cdd:cd21310  81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 122
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 158-259 5.73e-30

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: 114.70  E-value: 5.73e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 237
Cdd:cd21259   1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80

                        90       100
                ....*....|....*....|..
gi 13123944 238 EDIVNTPKPDEKAIMTYVSCFY 259
Cdd:cd21259  81 EDMVRMREPDWKCVYTYIQEFY 102
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 26-149 1.13e-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: 114.08  E-value: 1.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  26 MEQEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRK--AGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKI 103
Cdd:cd21247   1 MDTEYEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKngAKIEITDIYTELKDGIHLLRLLELISGEQLPRPSRGKMRVHFL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 13123944 104 ANVNKALDFIASKgVKLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 149
Cdd:cd21247  81 ENNSKAITFLKTK-VPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 42-147 1.83e-29

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: 112.97  E-value: 1.83e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  42 WEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRP--DKGKMRFHKIANVNKALDFIASKGVK 119
Cdd:cd21228   1 WKKIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKynKRPTFRQMKLENVSVALEFLERESIK 80

                        90       100
                ....*....|....*....|....*...
gi 13123944 120 LVSIGAEEIVDGNLKMTLGMIWTIILRF 147
Cdd:cd21228  81 LVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 43-146 1.96e-29

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: 114.76  E-value: 1.96e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKGVKLVS 122
Cdd:cd21316  51 EAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLEN 130

                        90       100
                ....*....|....*....|....
gi 13123944 123 IGAEEIVDGNLKMTLGMIWTIILR 146
Cdd:cd21316 131 MGSHDIVDGNHRLTLGLIWTIILR 154
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 156-262 2.25e-29

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: 112.83  E-value: 2.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 156 ETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKML 235
Cdd:cd21240   2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80

                        90       100
                ....*....|....*....|....*..
gi 13123944 236 DAEDiVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21240  81 DAED-VDVPSPDEKSVITYVSSIYDAF 106
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 158-256 2.29e-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: 112.57  E-value: 2.29e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 237
Cdd:cd21255   1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79

                        90
                ....*....|....*....
gi 13123944 238 EDIVNTPKPDEKAIMTYVS 256
Cdd:cd21255  80 ADMVLLPIPDKLIVMTYLC 98
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 158-261 8.21e-29

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: 110.79  E-value: 8.21e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYrnvNVQNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLD 236
Cdd:cd21184   1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIIT 77

                        90       100
                ....*....|....*....|....*
gi 13123944 237 AEDIVNtPKPDEKAIMTYVSCFYHA 261
Cdd:cd21184  78 PEDMVS-PNVDELSVMTYLSYFRNA 101
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
 158-258 1.27e-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: 110.69  E-value: 1.27e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 237
Cdd:cd21244   5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEP 84

                        90       100
                ....*....|....*....|.
gi 13123944 238 EDiVNTPKPDEKAIMTYVSCF 258
Cdd:cd21244  85 ED-VDVVNPDEKSIMTYVAQF 104
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 158-261 1.53e-28

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: 110.11  E-value: 1.53e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 237
Cdd:cd21238   2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 81

                        90       100
                ....*....|....*....|....
gi 13123944 238 EDiVNTPKPDEKAIMTYVSCFYHA 261
Cdd:cd21238  82 ED-VDVPQPDEKSIITYVSSLYDA 104
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 43-150 3.29e-28

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: 109.58  E-value: 3.29e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNSHL--RKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRpDKGKM--RFHKIANVNKALDFIASKGV 118
Cdd:cd21190   3 ERVQKKTFTNWINSHLakLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPI-ESGRVlqRAHKLSNIRNALDFLTKRCI 81

                        90       100       110
                ....*....|....*....|....*....|..
gi 13123944 119 KLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQ 150
Cdd:cd21190  82 KLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 43-150 1.25e-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: 107.70  E-value: 1.25e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNSHLRKAGTQ-IENIEEDFRNGLKLMLLLEVISGERLPRpDKGKMRFHKIANVNKALDFIASKGVKLV 121
Cdd:cd21231   4 EDVQKKTFTKWINAQFAKFGKPpIEDLFTDLQDGRRLLELLEGLTGQKLVK-EKGSTRVHALNNVNKALQVLQKNNVDLV 82

                        90       100
                ....*....|....*....|....*....
gi 13123944 122 SIGAEEIVDGNLKMTLGMIWTIILRFAIQ 150
Cdd:cd21231  83 NIGSADIVDGNHKLTLGLIWSIILHWQVK 111
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
 163-262 4.39e-27

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: 106.19  E-value: 4.39e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 163 LLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDIVN 242
Cdd:cd21251  10 LLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEMAS 89

                        90       100
                ....*....|....*....|
gi 13123944 243 TPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21251  90 VGEPDKLSMVMYLTQFYEMF 109
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 163-259 6.34e-27

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: 105.42  E-value: 6.34e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 163 LLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDIVn 242
Cdd:cd21234   5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVA- 83

                        90
                ....*....|....*..
gi 13123944 243 TPKPDEKAIMTYVSCFY 259
Cdd:cd21234  84 VQLPDKKSIIMYLTSLF 100
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 158-264 1.10e-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: 104.93  E-value: 1.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 237
Cdd:cd21254   1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79

                        90       100
                ....*....|....*....|....*..
gi 13123944 238 EDIVNTPKPDEKAIMTYVSCFYHAFAG 264
Cdd:cd21254  80 SDMVLLAVPDKLTVMTYLYQIRAHFSG 106
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 33-149 1.25e-26

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: 105.93  E-value: 1.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  33 DRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRP--DKGKMRFHKIANVNKAL 110
Cdd:cd21309   5 EKDLAEDAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKyhQRPTFRQMQLENVSVAL 84

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 13123944 111 DFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 149
Cdd:cd21309  85 EFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSI 123
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 33-149 3.89e-26

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: 104.40  E-value: 3.89e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  33 DRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRP--DKGKMRFHKIANVNKAL 110
Cdd:cd21308   8 EKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKhnQRPTFRQMQLENVSVAL 87

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 13123944 111 DFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 149
Cdd:cd21308  88 EFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 126
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 158-262 6.73e-26

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: 102.80  E-value: 6.73e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 237
Cdd:cd21257   8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLEL 86

                        90       100
                ....*....|....*....|....*
gi 13123944 238 EDIVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21257  87 SEMMYTDRPDWQSVMQYVAQIYKYF 111
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
 160-262 8.77e-26

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: 102.86  E-value: 8.77e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 160 KEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAED 239
Cdd:cd21260   3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82

                        90       100
                ....*....|....*....|...
gi 13123944 240 IVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21260  83 MVRMSVPDSKCVYTYIQELYRSL 105
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 43-150 1.10e-25

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: 102.22  E-value: 1.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNSHLRKAGTQ--IENIEEDFRNGLKLMLLLEVISGERLPRpDKGKMRFHKIANVNKALDFIASKGVKL 120
Cdd:cd21242   3 EQTQKRTFTNWINSQLAKHSPPsvVSDLFTDIQDGHRLLDLLEVLSGQQLPR-EKGHNVFQCRSNIETALSFLKNKSIKL 81

                        90       100       110
                ....*....|....*....|....*....|
gi 13123944 121 VSIGAEEIVDGNLKMTLGMIWTIILRFAIQ 150
Cdd:cd21242  82 INIHVPDIIEGKPSIILGLIWTIILHFHIE 111
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 161-256 2.09e-25

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: 101.24  E-value: 2.09e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944    161 EGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKD----DPIGNLNTAFEVAEKYLDIPKMLD 236
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|
gi 13123944    237 AEDIVnTPKPDEKAIMTYVS 256
Cdd:smart00033  81 PEDLV-EGPKLILGVIWTLI 99
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
 158-260 2.96e-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: 101.28  E-value: 2.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 237
Cdd:cd21258   1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80

                        90       100
                ....*....|....*....|....
gi 13123944 238 ED-IVNTPKPDEKAIMTYVSCFYH 260
Cdd:cd21258  81 EDmMIMGKKPDSKCVFTYVQSLYN 104
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 163-262 1.73e-24

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: 98.85  E-value: 1.73e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 163 LLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDY-AKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDiV 241
Cdd:cd21233   5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWnSVVSQQSATERLDHAFNIARQHLGIEKLLDPED-V 83

                        90       100
                ....*....|....*....|.
gi 13123944 242 NTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21233  84 ATAHPDKKSILMYVTSLFQVL 104
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 44-149 2.49e-24

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: 98.51  E-value: 2.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944    44 KQQRKTFTAWCNSHLRKAG--TQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASK-GVKL 120
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKlGVPK 80

                          90       100
                  ....*....|....*....|....*....
gi 13123944   121 VSIGAEEIVDGNLKMTLGMIWTIILRFAI 149
Cdd:pfam00307  81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
 158-262 3.43e-24

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


Pssm-ID: 409105  Cd Length: 119  Bit Score: 98.22  E-value: 3.43e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 237
Cdd:cd21256  14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDI 92

                        90       100
                ....*....|....*....|....*
gi 13123944 238 EDIVNTPKPDEKAIMTYVSCFYHAF 262
Cdd:cd21256  93 NEMVRTERPDWQSVMTYVTAIYKYF 117
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 46-147 1.11e-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: 96.50  E-value: 1.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  46 QRKTFTAWCNSHLRKAGTQ--IENIEEDFRNGLKLMLLLEVISGERLPRP-DKGKMRFHKIANVNKALDFIASKGVKLVS 122
Cdd:cd21212   1 EIEIYTDWANHYLEKGGHKriITDLQKDLGDGLTLVNLIEAVAGEKVPGIhSRPKTRAQKLENIQACLQFLAALGVDVQG 80

                        90       100
                ....*....|....*....|....*
gi 13123944 123 IGAEEIVDGNLKMTLGMIWTIILRF 147
Cdd:cd21212  81 ITAEDIVDGNLKAILGLFFSLSRYK 105
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 46-150 1.21e-23

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: 96.23  E-value: 1.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  46 QRKTFTAWCNSHLRKAGT-QIENIEEDFRNGLKLMLLLEVISGERLPRpDKGKMRFHKIANVNKALDFIASKGVKLVSIG 124
Cdd:cd21232   3 QKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPK-ERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81

                        90       100
                ....*....|....*....|....*.
gi 13123944 125 AEEIVDGNLKMTLGMIWTIILRFAIQ 150
Cdd:cd21232  82 GTDIVDGNHKLTLGLLWSIILHWQVK 107
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 407-512 2.23e-23

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: 95.46  E-value: 2.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944   407 HLAEKFQQKASLHEAWTRGKEEMLNQHDYESaSLQEVRALLRRHEAFESDLAAHQDRVEHIAALAQELNELDYHEAASVN 486
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                          90       100
                  ....*....|....*....|....*.
gi 13123944   487 SRCQAICDQWDNLGTLTQKRRDALER 512
Cdd:pfam00435  80 ERLEELNERWEQLLELAAERKQKLEE 105
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
 158-260 2.02e-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: 92.72  E-value: 2.02e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 237
Cdd:cd21261   1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80

                        90       100
                ....*....|....*....|....
gi 13123944 238 ED-IVNTPKPDEKAIMTYVSCFYH 260
Cdd:cd21261  81 EDmMVMGRKPDPMCVFTYVQSLYN 104
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 159-262 3.08e-22

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: 92.16  E-value: 3.08e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 159 AKEGLLLWCQRKTAPYrNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAE 238
Cdd:cd21245   4 AIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82

                        90       100
                ....*....|....*....|....*
gi 13123944 239 DI-VNTpkPDEKAIMTYVSCFYHAF 262
Cdd:cd21245  83 DVmVDS--PDEQSIMTYVAQFLEHF 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 48-146 8.56e-22

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 90.84  E-value: 8.56e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944     48 KTFTAWCNSHLRKAGTQ-IENIEEDFRNGLKLMLLLEVISGERLP--RPDKGKMRFHKIANVNKALDFIASKGVKLVSIG 124
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVDkkKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 13123944    125 AEEIVDGNlKMTLGMIWTIILR 146
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 43-151 1.21e-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: 88.02  E-value: 1.21e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNSHLRKAGT--QIENIEEDFRNGLKLMLLLEVISGERLPRPDK-GKMRFHKIANVNKALDFIASKGVK 119
Cdd:cd21191   3 ENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKpSSHRIFRLNNIAKALKFLEDSNVK 82

                        90       100       110
                ....*....|....*....|....*....|..
gi 13123944 120 LVSIGAEEIVDGNLKMTLGMIWTIILRFAIQD 151
Cdd:cd21191  83 LVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 160-260 1.94e-20

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: 87.01  E-value: 1.94e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 160 KEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDP---IGNLNTAFEVAEKY-LDIPKML 235
Cdd:cd00014   1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLgLPELDLF 80

                        90       100
                ....*....|....*....|....*
gi 13123944 236 DAEDIVNtpKPDEKAIMTYVSCFYH 260
Cdd:cd00014  81 EPEDLYE--KGNLKKVLGTLWALAL 103
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 158-258 2.68e-20

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: 86.67  E-value: 2.68e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTaPYRNVNvqNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLD 236
Cdd:cd21230   1 TPKQRLLGWIQNKI-PQLPIT--NFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77

                        90       100
                ....*....|....*....|..
gi 13123944 237 AEDIVNtPKPDEKAIMTYVSCF 258
Cdd:cd21230  78 PEEIIN-PNVDEMSVMTYLSQF 98
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 42-143 1.18e-19

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: 85.28  E-value: 1.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  42 WEKQQRKTFTAWCNSHLRKAG-TQIENIEEDFRNGLKLMLLLEVISGERLPRPDK--GKMRFHKIANVNKALDFIASK-G 117
Cdd:cd21225   1 WEKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDlePKNRIQMIQNLHLAMLFIEEDlK 80

                        90       100
                ....*....|....*....|....*.
gi 13123944 118 VKLVSIGAEEIVDGNLKMTLGMIWTI 143
Cdd:cd21225  81 IRVQGIGAEDFVDNNKKLILGLLWTL 106
SPEC smart00150
Spectrin repeats;
410-511 8.19e-19

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 82.38  E-value: 8.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944    410 EKFQQKASLHEAWTRGKEEMLNQHDYeSASLQEVRALLRRHEAFESDLAAHQDRVEHIAALAQELNELDYHEAASVNSRC 489
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                           90       100
                   ....*....|....*....|..
gi 13123944    490 QAICDQWDNLGTLTQKRRDALE 511
Cdd:smart00150  80 EELNERWEELKELAEERRQKLE 101
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
 157-262 3.41e-18

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: 80.86  E-value: 3.41e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 157 TSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLD 236
Cdd:cd21196   2 SGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVS 81

                        90       100
                ....*....|....*....|....*.
gi 13123944 237 AEDIVNTPKPdeKAIMTYVSCFYHAF 262
Cdd:cd21196  82 AQAVVAGSDP--LGLIAYLSHFHSAF 105
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 47-145 6.33e-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: 79.69  E-value: 6.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  47 RKTFTAWCNSHLRKAGTQ-IENIEEDFRNGLKLMLLLEVISGERLP-RPDKGKMRFHKIANVNKALDFIASKGV-KLVSI 123
Cdd:cd00014   1 EEELLKWINEVLGEELPVsITDLFESLRDGVLLCKLINKLSPGSIPkINKKPKSPFKKRENINLFLNACKKLGLpELDLF 80

                        90       100
                ....*....|....*....|...
gi 13123944 124 GAEEIV-DGNLKMTLGMIWTIIL 145
Cdd:cd00014  81 EPEDLYeKGNLKKVLGTLWALAL 103
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 46-140 4.24e-16

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: 74.64  E-value: 4.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  46 QRKTFTAWCNSHLRK-AGTQ-IENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFH-KIANVNKALDFIASKGVKLVS 122
Cdd:cd21213   1 QLQAYVAWVNSQLKKrPGIRpVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAeRKENVEKVLQFMASKRIRMHQ 80

                        90
                ....*....|....*...
gi 13123944 123 IGAEEIVDGNLKMTLGMI 140
Cdd:cd21213  81 TSAKDIVDGNLKAIMRLI 98
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 160-258 6.58e-15

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


Pssm-ID: 409078  Cd Length: 105  Bit Score: 71.26  E-value: 6.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 160 KEGLLLWCQrktAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAE 238
Cdd:cd21229   5 KKLMLAWLQ---AVLPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81

                        90       100
                ....*....|....*....|
gi 13123944 239 DIVNtPKPDEKAIMTYVSCF 258
Cdd:cd21229  82 DLSS-PHLDELSGMTYLSYF 100
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 158-261 2.80e-14

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: 69.81  E-value: 2.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTApyrNVNVQNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLD 236
Cdd:cd21315  16 TPKQRLLGWIQSKVP---DLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92

                        90       100
                ....*....|....*....|....*
gi 13123944 237 AEDIVNtPKPDEKAIMTYVSCFYHA 261
Cdd:cd21315  93 PEEMVN-PKVDELSMMTYLSQFPNA 116
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 155-261 9.62e-14

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: 68.56  E-value: 9.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 155 EETSAKEGLLLWCQRKTAPYRnvnVQNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKYLDIPK 233
Cdd:cd21314   8 RKQTPKQRLLGWIQNKVPQLP---ITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQ 84

                        90       100
                ....*....|....*....|....*...
gi 13123944 234 MLDAEDIVNtPKPDEKAIMTYVSCFYHA 261
Cdd:cd21314  85 VIAPEEIVD-PNVDEHSVMTYLSQFPKA 111
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 522-633 1.06e-13

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: 67.73  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944   522 QLQLEFARRAAPFNNWLDGAIEDLQDVWLVHSVEETQSLLTAHEQFKATLPEADRERGAILgiqgEIQKICQTYGlrpKS 601
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALN----ELAEKLIDEG---HY 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 13123944   602 GNPYITLSSQDINNKWDTVRKLVPSRDQTLQE 633
Cdd:pfam00435  74 ASEEIQERLEELNERWEQLLELAAERKQKLEE 105
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 43-141 1.61e-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: 67.69  E-value: 1.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNSHLRkaGTQIENIEEDFRNGLKLMLLLEVISG-----ERLPRPDKgKMRFHKIANVNKALDFIASKG 117
Cdd:cd21219   2 GSREERAFRMWLNSLGL--DPLINNLYEDLRDGLVLLQVLDKIQPgcvnwKKVNKPKP-LNKFKKVENCNYAVDLAKKLG 78

                        90       100
                ....*....|....*....|....
gi 13123944 118 VKLVSIGAEEIVDGNLKMTLGMIW 141
Cdd:cd21219  79 FSLVGIGGKDIADGNRKLTLALVW 102
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 35-147 2.78e-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: 67.23  E-value: 2.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  35 DLLLDPAWEK--QQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLP------RPDKgkmRFHKIANV 106
Cdd:cd21222   4 DDLFDEAPEKlaEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyhlTPST---DDEKLHNV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13123944 107 NKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRF 147
Cdd:cd21222  81 KLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 290-513 6.25e-13

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: 68.63  E-value: 6.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 290 EEYEKLASELLEWIRRTVPWLENRVGEPSMS---AMQRKLEDFRDYRRLHKPpRVQEkcqleinFNTLQTKLRLSHRPAf 366
Cdd:cd00176   3 QQFLRDADELEAWLSEKEELLSSTDYGDDLEsveALLKKHEALEAELAAHEE-RVEA-------LNELGEQLIEEGHPD- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 367 MPSEGKLVSDIANAWRGLEQvekgyedwlLSEIRRlQRLQHLAEKFQQKASLH--EAWTRGKEEMLNQHDYESaSLQEVR 444
Cdd:cd00176  74 AEEIQERLEELNQRWEELRE---------LAEERR-QRLEEALDLQQFFRDADdlEQWLEEKEAALASEDLGK-DLESVE 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 445 ALLRRHEAFESDLAAHQDRVEHIAALAQEL-NELDYHEAASVNSRCQAICDQWDNLGTLTQKRRDALERM 513
Cdd:cd00176 143 ELLKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 169-260 6.33e-13

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: 65.40  E-value: 6.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 169 RKTAPyrNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDAEDIVNtPKPDE 248
Cdd:cd21185  11 RQLLP--DVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMAD-PEVEH 86

                        90
                ....*....|..
gi 13123944 249 KAIMTYVSCFYH 260
Cdd:cd21185  87 LGIMAYAAQLQK 98
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 163-256 1.55e-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: 65.79  E-value: 1.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 163 LLLWCQRKTAPYrNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDD-----------------PIGNLNTAFEVA 225
Cdd:cd21224   5 LLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTtqtvdraqdeaedfwvaEFSPSTGDSGLS 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 13123944 226 EKYL------------------DIPKMLDAEDIVNTPkPDEKAIMTYVS 256
Cdd:cd21224  84 SELLanekrnfklvqqavaelgGVPALLRASDMSNTI-PDEKVVILFLS 131
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
 158-261 1.82e-12

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: 64.73  E-value: 1.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 158 SAKEGLLLWCQRKTaPYrnVNVQNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLD 236
Cdd:cd21313   8 TPKQRLLGWIQNKI-PY--LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGVPQVIT 84

                        90       100
                ....*....|....*....|....*
gi 13123944 237 AEDIVNtPKPDEKAIMTYVSCFYHA 261
Cdd:cd21313  85 PEEIIH-PDVDEHSVMTYLSQFPKA 108
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 48-143 4.86e-12

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: 63.13  E-value: 4.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  48 KTFTAWCNSHLRKAGTQ--IENIEEDFRNGLKLMLLLEVISGERLPR-PDKGKMRFHKIANVNKALDFIASKGVKLVSIG 124
Cdd:cd21286   3 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVEDiNGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 82

                        90
                ....*....|....*....
gi 13123944 125 AEEIVDGNLKMTLGMIWTI 143
Cdd:cd21286  83 AEEIRNGNLKAILGLFFSL 101
PTZ00184 PTZ00184
calmodulin; Provisional
 753-857 1.02e-11

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 63.63  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  753 AKGLSQEQLNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFIDFMTRETAETD 832
Cdd:PTZ00184   2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTD 81

                         90       100
                 ....*....|....*....|....*.
gi 13123944  833 TAEQVVASFKILAGDKN-YITPEELR 857
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNgFISAAELR 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 526-746 1.47e-11

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: 64.77  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 526 EFARRAAPFNNWLDGAIEDLQDVWLVHSVEETQSLLTAHEQFKATLpEADRERgaILGIQGEIQKICQTYGlrpkSGNPY 605
Cdd:cd00176   4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAEL-AAHEER--VEALNELGEQLIEEGH----PDAEE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 606 ITLSSQDINNKWDTVRKLVPSRDQTLQEELARQqvnerlrrQFAAQANAIGPWIQGKVEEVGRLAAG-LAGSLEEQMAGL 684
Cdd:cd00176  77 IQERLEELNQRWEELRELAEERRQRLEEALDLQ--------QFFRDADDLEQWLEEKEAALASEDLGkDLESVEELLKKH 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13123944 685 RQQEQNIINYKSNIDRLEGDHQLLQESLVFDNKHTVY-SMEHIRVGWEQLLTSIARTINEVEN 746
Cdd:cd00176 149 KELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEeKLEELNERWEELLELAEERQKKLEE 211
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 763-825 3.37e-11

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: 59.48  E-value: 3.37e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13123944 763 EFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFIDFMT 825
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 43-150 3.70e-11

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: 61.10  E-value: 3.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNShlrkAGTQ--IENIEEDFRNGLKLMLLLEVI------SGERLPRPDKGKMRFHKIANVNKALDFIA 114
Cdd:cd21298   4 ETREEKTYRNWMNS----LGVNpfVNHLYSDLRDGLVLLQLYDKIkpgvvdWSRVNKPFKKLGANMKKIENCNYAVELGK 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 13123944 115 SKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQ 150
Cdd:cd21298  80 KLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 46-143 3.87e-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: 61.13  E-value: 3.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  46 QRKTFTAWCNSHLRKAGTQ--IENIEEDFRNGLKLMLLLEVISGERLPRPDK-GKMRFHKIANVNKALDFIASKGVKLVS 122
Cdd:cd21285  11 DKQIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcPKNRSQMIENIDACLSFLAAKGINIQG 90

                        90       100
                ....*....|....*....|.
gi 13123944 123 IGAEEIVDGNLKMTLGMIWTI 143
Cdd:cd21285  91 LSAEEIRNGNLKAILGLFFSL 111
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 64-144 9.64e-11

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: 59.53  E-value: 9.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  64 QIENIEEDFRNGLKLMLLLEVISGerlPRPDKGKMRF------HKIANVNKALDFIASKGV----KLVSIGAEEIVDGNL 133
Cdd:cd21223  25 AVTNLAVDLRDGVRLCRLVELLTG---DWSLLSKLRVpaisrlQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHR 101

                        90
                ....*....|.
gi 13123944 134 KMTLGMIWTII 144
Cdd:cd21223 102 EKTLALLWRII 112
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 150-261 1.63e-10

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


Pssm-ID: 409161  Cd Length: 114  Bit Score: 59.05  E-value: 1.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 150 QDISVEETSAKEGLLLWCQRKTApyrNVNVQNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKY 228
Cdd:cd21312   4 EDEEAKKQTPKQRLLGWIQNKLP---QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDW 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 13123944 229 LDIPKMLDAEDIVNtPKPDEKAIMTYVSCFYHA 261
Cdd:cd21312  81 LGIPQVITPEEIVD-PNVDEHSVMTYLSQFPKA 112
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 48-149 3.65e-10

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


Pssm-ID: 409149  Cd Length: 119  Bit Score: 58.20  E-value: 3.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  48 KTFTAWCNShlRKAGTQIENIEEDFRNGLKLMLLLE-VISGE------RLPRPDKGKMRFHKIANVNKALDFIASKGVKL 120
Cdd:cd21300  10 RVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSvnwkkvNKAPASAEISRFKAVENTNYAVELGKQLGFSL 87

                        90       100
                ....*....|....*....|....*....
gi 13123944 121 VSIGAEEIVDGNLKMTLGMIWTiILRFAI 149
Cdd:cd21300  88 VGIQGADITDGSRTLTLALVWQ-LMRFHI 115
PTZ00183 PTZ00183
centrin; Provisional
 755-858 3.78e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 56.62  E-value: 3.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  755 GLSQEQLNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFIDFMTRETAETDTA 834
Cdd:PTZ00183  10 GLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKKLGERDPR 89

                         90       100
                 ....*....|....*....|....*
gi 13123944  835 EQVVASFKILAGDKN-YITPEELRR 858
Cdd:PTZ00183  90 EEILKAFRLFDDDKTgKISLKNLKR 114
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 167-240 4.11e-09

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 54.23  E-value: 4.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944   167 CQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRK------DDPIGNLNTAFEVAEKYLDI-PKMLDAED 239
Cdd:pfam11971   1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLkesmslADSLYNIQLLQEFCQRHLGNrCCHLTLED 80


                  .
gi 13123944   240 I 240
Cdd:pfam11971  81 L 81
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 643-746 5.24e-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: 54.63  E-value: 5.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944   643 RLRRQFAAQANAIGPWIQGKVEEVG-RLAAGLAGSLEEQMAGLRQQEQNIINYKSNIDRLEGDHQLLQESLVFDNKHTVY 721
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSsEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                          90       100
                  ....*....|....*....|....*
gi 13123944   722 SMEHIRVGWEQLLTSIARTINEVEN 746
Cdd:pfam00435  81 RLEELNERWEQLLELAAERKQKLEE 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
502-862 8.28e-09

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 59.18  E-value: 8.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 502 LTQKRRDALERMEKLLE---TIDQLQLEFARRAApfnNWLdGAIEDLQDVWLVHSVEETQSLLTAH----EQFKATLPEA 574
Cdd:COG5069 234 LLEKIDIALHRVYRLLEadeTLIQLRLPYEIILL---RLL-NLIHLKQANWKVVNFSKDVSDGENYtdllNQLNALCSRA 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 575 DRERGAILGIQGEIQKICQTYGLR---PKSGNPYITLSSQdinnkwdtvRKLVPSRD--QTLQEELARQQVNERLRRQFA 649
Cdd:COG5069 310 PLETTDLHSLAGQILQNAEKYDCRkylPPAGNPKLDLAFV---------AHLFNTHPgqEPLEEEEKPEIEEFDAEGEFE 380

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 650 AQANAIgpWIqgkveevgrLAAGLAGSLEEQMAGLRQQEQNIINYKSNIDRLEGDHQL---LQESLVFDNKHTVYSMEHI 726
Cdd:COG5069 381 ARVFTF--WL---------NSLDVSPEITNLFGDLRDQLILLQALSKKLMPMTVTHKLvkkQPASGIEENRFKAFENENY 449

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 727 RVGWEQLLTSIARTINEVENQVLTRDAKGLSQEQLNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTm 806
Cdd:COG5069 450 AVDLGITEGFSLVGIKGLEILDGIRLKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFG- 528

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 807 vdpNAAGVVTFQAFIDFmTRETAET----DTAEQVVASFKILAGDKNYITPEELRRELPA 862
Cdd:COG5069 529 ---DPAGSVSGVFYLDV-LKGIHSElvdyDLVTRGFTEFDDIADARSLAISSKILRSLGA 584
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 287-396 1.99e-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: 52.71  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944   287 KLMEEYEKLASELLEWIRRTVPWLENRVGEPSMSAMQRKLedfRDYRRLHKPPRVQEKCQLEInfNTLQTKLrLSHRPAF 366
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALL---KKHKALEAELAAHQDRVEAL--NELAEKL-IDEGHYA 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 13123944   367 MPSEGKLVSDIANAWRGLEQVEKGYEDWLL 396
Cdd:pfam00435  75 SEEIQERLEELNERWEQLLELAAERKQKLE 104
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 45-149 2.08e-07

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


Pssm-ID: 409148  Cd Length: 114  Bit Score: 50.19  E-value: 2.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  45 QQRKTFTAWCNShlRKAGTQIENIEEDFRNGLKLMLLLE-----VISGERLPRPDKgKMRFHKIANVNKALDFIASKGVK 119
Cdd:cd21299   4 REERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDkvspgSVNWKHANKPPI-KMPFKKVENCNQVVKIGKQLKFS 80

                        90       100       110
                ....*....|....*....|....*....|
gi 13123944 120 LVSIGAEEIVDGNLKMTLGMIWTiILRFAI 149
Cdd:cd21299  81 LVNVAGNDIVQGNKKLILALLWQ-LMRYHM 109
EFh_PEF_Group_II_sorcin_like cd16181
Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The ...
 761-841 4.79e-07

Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The family corresponds to the second group of penta-EF hand (PEF) proteins that includes sorcin, grancalcin, and similar proteins. Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. It contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH. Grancalcin (GCA) is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It can strongly interact with sorcin to form a heterodimer and further modulate the function of sorcin. GCA exists as homodimers in solution. It contains five EF-hand motifs attached to an N-terminal region of an approximately 50 residue-long segment rich in glycines and prolines. In contrast with sorcin, GCA binds two Ca2+ ions through its EF1 and EF3 hands.


Pssm-ID: 320056 [Multi-domain]  Cd Length: 165  Bit Score: 50.45  E-value: 4.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 761 LNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVdpNAAGVVTFQAFIDFMTRETAET------DTA 834
Cdd:cd16181  69 LNQWKTTFMQYDRDRSGTVEPQELQQAIRSFGYNLSPQALNVIVKRY--SKNGRITFDDFVACAVRLRALTdrfrrrDTQ 146


                ....*..
gi 13123944 835 EQVVASF 841
Cdd:cd16181 147 QNGTATF 153
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 35-147 5.85e-07

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: 49.34  E-value: 5.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  35 DLLLDPAWEKQQ--RKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLP------RPDKGKmrfHKIANV 106
Cdd:cd21306   4 DTLFDHAPDKLNvvKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPlhsfhlTPTSFE---QKVHNV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13123944 107 NKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRF 147
Cdd:cd21306  81 QFAFELMQDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
 35-147 7.52e-07

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: 49.22  E-value: 7.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  35 DLLLDPAWEKQQ--RKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLP------RPDKGKmrfHKIANV 106
Cdd:cd21337   8 DTLFDHAPDKLNvvKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPlhsfflTPDSFE---QKVLNV 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13123944 107 NKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRF 147
Cdd:cd21337  85 SFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKY 125
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 28-149 1.78e-06

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 48.07  E-value: 1.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  28 QEEDWDrdlLLDPawEKQQRKTFTAWCNShlRKAGTQIENIEEDFRNGLKLMLLLEVIS----GERLPRPDKGKM--RFH 101
Cdd:cd21331  10 QDIDWT---LLEG--ETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIKvpvdWNKVNKPPYPKLgaNMK 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 13123944 102 KIANVNKALDFIASKG-VKLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 149
Cdd:cd21331  83 KLENCNYAVELGKHPAkFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 100-144 2.65e-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: 47.18  E-value: 2.65e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 13123944 100 FHKIANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTII 144
Cdd:cd21217  69 FEATENLNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 161-255 1.63e-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: 44.98  E-value: 1.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 161 EGLLL-WCQR--KTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLID----YAKLRKDDPIGNLNTAFEVAEKyLDIPK 233
Cdd:cd21218  12 EEILLrWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEK-LGCKY 90

                        90       100
                ....*....|....*....|..
gi 13123944 234 MLDAEDIVNtpkPDEKAIMTYV 255
Cdd:cd21218  91 FLTPEDIVS---GNPRLNLAFV 109
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 53-143 1.81e-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: 44.60  E-value: 1.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  53 WCNSHLRKAGTQ---IENIEEDFRNGLKLMLLLEVISGERLPRPDKGKM--RFHKIANVNKALDFIASKGVKLVsIGAEE 127
Cdd:cd21218  18 WVNYHLKKAGPTkkrVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVlsEEDLEKRAEKVLQAAEKLGCKYF-LTPED 96

                        90
                ....*....|....*.
gi 13123944 128 IVDGNLKMTLGMIWTI 143
Cdd:cd21218  97 IVSGNPRLNLAFVATL 112
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
 35-147 5.17e-05

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: 43.81  E-value: 5.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  35 DLLLDPAWEKQQ--RKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLP------RPDKGKMRFHkiaNV 106
Cdd:cd21338   9 DTLFDHAPDKLSvvKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPlhnfylTPESFDQKVH---NV 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13123944 107 NKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRF 147
Cdd:cd21338  86 SFAFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKY 126
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 47-113 8.93e-05

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: 42.65  E-value: 8.93e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  47 RKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDK---GKMRFHKIANVNKALDFI 113
Cdd:cd21221   3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEVaqsEEGQKQKLAVVLACVNFL 72
SPEC smart00150
Spectrin repeats;
526-632 9.31e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 42.32  E-value: 9.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944    526 EFARRAAPFNNWLDGAIEDLQDVWLVHSVEETQSLLTAHEQFKAtlpEADRERGAILGIQGEIQKICQTYGlrpkSGNPY 605
Cdd:smart00150   2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEA---ELEAHEERVEALNELGEQLIEEGH----PDAEE 74

                           90       100
                   ....*....|....*....|....*..
gi 13123944    606 ITLSSQDINNKWDTVRKLVPSRDQTLQ 632
Cdd:smart00150  75 IEERLEELNERWEELKELAEERRQKLE 101
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 89-146 1.10e-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: 42.82  E-value: 1.10e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13123944  89 RLPRPDKGKMRFHKIANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILR 146
Cdd:cd21294  67 KPPRKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRR 124
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 43-149 1.28e-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: 42.28  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNShlRKAGTQIENIEEDFRNGLKLMLLLEVIsgeRLP----RPDK-------GKMRfhKIANVNKALD 111
Cdd:cd21329   4 ESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMT---RVPvdwgHVNKppypalgGNMK--KIENCNYAVE 76

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 13123944 112 FIASKG-VKLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 149
Cdd:cd21329  77 LGKNKAkFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTL 115
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 55-147 1.59e-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: 42.34  E-value: 1.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  55 NSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLP------RPDKGKMRFHkiaNVNKALDFIASKGVKLVSIGAEEI 128
Cdd:cd21307  26 NKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHlsefflTPSSTSEMLH---NVTLALELLKEGGLLNFPVNPEDI 102

                        90
                ....*....|....*....
gi 13123944 129 VDGNLKMTLGMIWTIILRF 147
Cdd:cd21307 103 VNGDSKATIRVLYCLFSKY 121
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
359-529 4.67e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 4.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 359 RLSHrpafmpSEgKLVSDIANAWRGLEQVEKGYEDWLLSEIRRLQRLQHLAEKFQQ-KASLHEAW------TRGKEEMLN 431
Cdd:COG0497 217 RLSN------AE-KLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAElAERLESALieleeaASELRRYLD 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 432 QHDYESASLQEV-------RALLRRH-----------EAFESDLAAHQDRVEHIAALAQELNEL--DYHEAASvnsrcqa 491
Cdd:COG0497 290 SLEFDPERLEEVeerlallRRLARKYgvtveellayaEELRAELAELENSDERLEELEAELAEAeaELLEAAE------- 362

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 13123944 492 icdqwdnlgTLTQKRRDALERMEKLLET-IDQLQLEFAR 529
Cdd:COG0497 363 ---------KLSAARKKAAKKLEKAVTAeLADLGMPNAR 392
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
759-872 7.56e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 7.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 759 EQLNEFRASFNHFDRKRNGMMEPDDFRAclismgydLGEVEFARIMTMVDPNAAGVVTFQAFIDFMTRETAETDtAEQVV 838
Cdd:COG5126   2 LQRRKLDRRFDLLDADGDGVLERDDFEA--------LFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFAR 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13123944 839 ASFKILagDKN---YITPEELRR-----ELPAEQAEYCIRRM 872
Cdd:COG5126  73 AAFDLL--DTDgdgKISADEFRRlltalGVSEEEADELFARL 112
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 765-821 7.85e-04

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: 40.97  E-value: 7.85e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13123944 765 RASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFI 821
Cdd:cd16180  70 RRLFRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFV 126
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 43-149 9.60e-04

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 39.97  E-value: 9.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  43 EKQQRKTFTAWCNShlRKAGTQIENIEEDFRNGLKLMLLLEVIS----GERLPRPDKGKM--RFHKIANVNKALDFIASK 116
Cdd:cd21330  11 ETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLgeNMKKLENCNYAVELGKNK 88

                        90       100       110
                ....*....|....*....|....*....|....
gi 13123944 117 G-VKLVSIGAEEIVDGNLKMTLGMIWTIILRFAI 149
Cdd:cd21330  89 AkFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTL 122
EFh_PEF_sorcin cd16187
Penta-EF hand, calcium binding motifs, found in sorcin; Sorcin, also termed 22 kDa Ca2 ...
 761-842 1.29e-03

Penta-EF hand, calcium binding motifs, found in sorcin; Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. The up-regulation of sorcin is correlated with a number of cancer types, including colorectal, gastric and breast cancer. It may represent a therapeutic target for reversing tumor multidrug resistance (MDR). Sorcin participates in the regulation of calcium homeostasis in cells and is necessary for the activation of mitosis and cytokinesis. It enhances metastasis and promotes epithelial-to-mesenchymal transition of colorectal cancer. Moreover, sorcin has been implicated in the regulation of intracellular Ca2+ cycling and cardiac excitation-contraction coupling. It displays the anti-apoptotic properties via the modulation of mitochondrial Ca2+ handling in cardiac myocytes. It can target and activate the sarcolemmal Na+/Ca2+ exchanger (NCX1) in cardiac muscle. Meanwhile, sorcin modulates cardiac L-type Ca2+ current by functional interaction with the alpha1C subunit. It also associates with calcium/calmodulin-dependent protein kinase IIdeltaC (CaMKIIdelta(C)) and further modulates ryanodine receptor (RyR) function in cardiac myocytes. Furthermore, sorcin may act as a Ca2+ sensor for glucose-induced nuclear translocation and the activation of carbohydrate-responsive element-binding protein (ChREBP)-dependent genes. As a mitochondrial chaperone TRAP1 interactor, sorcin involves in mitochondrial metabolism through the TRAP1 pathway. In addition, sorcin may regulate the inhibition of type I interferon response in cells through interacting with foot-and-mouth disease virus (FMDV) VP1. Sorcin contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH.


Pssm-ID: 320062 [Multi-domain]  Cd Length: 165  Bit Score: 40.66  E-value: 1.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 761 LNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVdpNAAGVVTFQAFIDFMTRETAET------DTA 834
Cdd:cd16187  69 LNGWRQHFISFDSDRSGTVDPQELQKALTTMGFRLSPQAVNSIAKRY--STNGKITFDDYIACCVKLRALTdsfrrrDTS 146


                ....*...
gi 13123944 835 EQVVASFK 842
Cdd:cd16187 147 QQGVVNFP 154
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
50-141 1.74e-03

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 41.85  E-value: 1.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944  50 FTAWCNSHLrkAGTQIENIEEDFRNGLKLMLLLEVISGE---------RLPRPDKGKMRFHKIANVNKALDFIASKGVKL 120
Cdd:COG5069 384 FTFWLNSLD--VSPEITNLFGDLRDQLILLQALSKKLMPmtvthklvkKQPASGIEENRFKAFENENYAVDLGITEGFSL 461

                        90       100
                ....*....|....*....|.
gi 13123944 121 VSIGAEEIVDGNlKMTLGMIW 141
Cdd:COG5069 462 VGIKGLEILDGI-RLKLTLVW 481
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
746-858 3.26e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.62  E-value: 3.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13123944 746 NQVLTRDAkgLSQEQLNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFIDFMT 825
Cdd:COG5126  19 DGVLERDD--FEALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT 96

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 13123944 826 RETAETDTAEQVVASFkilagDKN---YITPEELRR 858
Cdd:COG5126  97 ALGVSEEEADELFARL-----DTDgdgKISFEEFVA 127
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 759-823 6.00e-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: 38.35  E-value: 6.00e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13123944 759 EQLNEF----RASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFIDF 823
Cdd:cd16185  59 AALHQFlsnmQNGFEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDYIEL 127
EF-hand_6 pfam13405
EF-hand domain;
763-792 6.51e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 6.51e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 13123944   763 EFRASFNHFDRKRNGMMEPDDFRACLISMG 792
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 761-821 6.60e-03

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, 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+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 38.40  E-value: 6.60e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13123944 761 LNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEvEFAR-IMTMVDPNAAGVVTFQAFI 821
Cdd:cd16184  66 IQQWKQVFQQFDRDRSGSIDENELHQALSQMGYRLSP-QFVQfLVSKYDPRARRSLTLDQFI 126
 
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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