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Conserved domains on  [gi|1827323766|gb|KAF3847163|]
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hypothetical protein F7725_020191 [Dissostichus mawsoni]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 92-193 1.35e-68

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: 223.03  E-value: 1.35e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  92 AWEKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKPERGKMRVHKINNVNKALDFIAGKGVKL 171
Cdd:cd21214     1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPERGKMRFHKIANVNKALDFIASKGVKL 80

                          90       100
                  ....*....|....*....|....*
gi 1827323766 172 VSIGAE---DGNAKMTLGMIWTIIL 193
Cdd:cd21214    81 VSIGAEeivDGNLKMTLGMIWTIIL 105
SAC6 super family cl26648
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
93-365 1.33e-53

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


The actual alignment was detected with superfamily member COG5069:

Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 197.86  E-value: 1.33e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  93 WEKQQRKTFTAWCNSHLRKSGT-QIENIEEDFRDGLKLMLLLETISGERLAKPERGK-MRVHKINNVNKALDFIAGKGVK 170
Cdd:COG5069     6 WQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPeTRIHVMENVSGRLEFIKGKGVK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 171 LVSIG---AEDGNAKMTLGMIWTIILRFAIQDISR--PLPRRVFS-LWCQRKTAPYKN-VNVQNFHISWKDGLAFNALIH 243
Cdd:COG5069    86 LFNIGpqdIVDGNPKLILGLIWSLISRLTIATINEegELTKHINLlLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIH 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 244 RHRPDLIDYDSLRKLLK----------ENNNIFNNECFVHGEETplkyIVNTARPDEKAIMTYVSSFYHAFSGAQKAETA 313
Cdd:COG5069   166 DSRPDTLDPNVLDLQKKnkalnnfqafENANKVIGIARLIGVED----IVNVSIPDERSIMTYVSWYIIRFGLLEKIDIA 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1827323766 314 ANRICKVLAVNQENEQMMEDYEKLASELLEWIRRTIPWLENRTQEKTVTDMQ 365
Cdd:COG5069   242 LHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGE 293
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 432-537 5.77e-25

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: 100.09  E-value: 5.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 432 HLAEKFHQKSKIHESWTDGKEAMLTQKDYEtCTLSEVKALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSASVN 511
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                          90       100
                  ....*....|....*....|....*.
gi 1827323766 512 ARCQKICDQWDSLGALTQNRKESLER 537
Cdd:pfam00435  80 ERLEELNERWEQLLELAAERKQKLEE 105
EFhand_Ca_insen super family cl24210
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 860-927 2.18e-20

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.


The actual alignment was detected with superfamily member pfam08726:

Pssm-ID: 430177  Cd Length: 69  Bit Score: 85.83  E-value: 2.18e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827323766 860 DTDTADQVIASFKILAADK-----VNLHHGrgaaegAPPDQAEYCIARMAPYTGP--DAAPGALDYMSFSTALYG 927
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKpyvteEDLRRE------LTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 788-855 6.61e-13

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: 64.11  E-value: 6.61e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827323766 788 EYRASFNHFDKDHSGALMAEEFKACLISLGYDvennkQGDSEFARIMSIVDPNNSGAVTFQAFIDFMS 855
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEG-----LSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 667-771 3.44e-06

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: 46.54  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 667 KFATQANTVGAYIQAKMEVMRISEIGRiSIEmngTLEDQLTNLRDYQTSIMSYMPEINTLEGSHQLIQEALIFDNQYTSY 746
Cdd:pfam00435   5 QFFRDADDLESWIEEKEALLSSEDYGK-DLE---SVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                          90       100
                  ....*....|....*....|....*
gi 1827323766 747 TMEHLRVGWEQLLTTIARTINEVEN 771
Cdd:pfam00435  81 RLEELNERWEQLLELAAERKQKLEE 105
 
Name Accession Description Interval E-value
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 92-193 1.35e-68

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: 223.03  E-value: 1.35e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  92 AWEKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKPERGKMRVHKINNVNKALDFIAGKGVKL 171
Cdd:cd21214     1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPERGKMRFHKIANVNKALDFIASKGVKL 80

                          90       100
                  ....*....|....*....|....*
gi 1827323766 172 VSIGAE---DGNAKMTLGMIWTIIL 193
Cdd:cd21214    81 VSIGAEeivDGNLKMTLGMIWTIIL 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
93-365 1.33e-53

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 197.86  E-value: 1.33e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  93 WEKQQRKTFTAWCNSHLRKSGT-QIENIEEDFRDGLKLMLLLETISGERLAKPERGK-MRVHKINNVNKALDFIAGKGVK 170
Cdd:COG5069     6 WQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPeTRIHVMENVSGRLEFIKGKGVK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 171 LVSIG---AEDGNAKMTLGMIWTIILRFAIQDISR--PLPRRVFS-LWCQRKTAPYKN-VNVQNFHISWKDGLAFNALIH 243
Cdd:COG5069    86 LFNIGpqdIVDGNPKLILGLIWSLISRLTIATINEegELTKHINLlLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIH 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 244 RHRPDLIDYDSLRKLLK----------ENNNIFNNECFVHGEETplkyIVNTARPDEKAIMTYVSSFYHAFSGAQKAETA 313
Cdd:COG5069   166 DSRPDTLDPNVLDLQKKnkalnnfqafENANKVIGIARLIGVED----IVNVSIPDERSIMTYVSWYIIRFGLLEKIDIA 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1827323766 314 ANRICKVLAVNQENEQMMEDYEKLASELLEWIRRTIPWLENRTQEKTVTDMQ 365
Cdd:COG5069   242 LHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGE 293
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 197-305 7.04e-46

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: 160.22  E-value: 7.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 197 IQDIS--RPLPRRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkeNNNIFN-NECFvh 273
Cdd:cd21216     1 IQDISveELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRK----DDPRENlNLAF-- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1827323766 274 geETPLKY-----------IVNTARPDEKAIMTYVSSFYHAFS 305
Cdd:cd21216    75 --DVAEKHldipkmldaedIVNTPRPDERSVMTYVSCYYHAFA 115
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 432-537 5.77e-25

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: 100.09  E-value: 5.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 432 HLAEKFHQKSKIHESWTDGKEAMLTQKDYEtCTLSEVKALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSASVN 511
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                          90       100
                  ....*....|....*....|....*.
gi 1827323766 512 ARCQKICDQWDSLGALTQNRKESLER 537
Cdd:pfam00435  80 ERLEELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 433-566 1.24e-22

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: 97.13  E-value: 1.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 433 LAEKFHQKSKIHESWTDGKEAMLTQKDYETcTLSEVKALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSASVNA 512
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1827323766 513 RCQKICDQWDSLGALTQNRKESLERTEKQLESIDELYLeyakraapFNNWMEEQ 566
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEK 125
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 95-197 2.41e-22

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 92.73  E-value: 2.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  95 KQQRKTFTAWCNSHLRKSG--TQIENIEEDFRDGLKLMLLLETISGERLAKPERGKMRVHKINNVNKALDFIAGK-GVKL 171
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKlGVPK 80

                          90       100
                  ....*....|....*....|....*....
gi 1827323766 172 VSIGAED---GNAKMTLGMIWTIILRFAI 197
Cdd:pfam00307  81 VLIEPEDlveGDNKSVLTYLASLFRRFQA 109
SPEC smart00150
Spectrin repeats;
435-536 6.37e-22

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 91.24  E-value: 6.37e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  435 EKFHQKSKIHESWTDGKEAMLTQKDYeTCTLSEVKALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSASVNARC 514
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                           90       100
                   ....*....|....*....|..
gi 1827323766  515 QKICDQWDSLGALTQNRKESLE 536
Cdd:smart00150  80 EELNERWEELKELAEERRQKLE 101
EFhand_Ca_insen pfam08726
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 860-927 2.18e-20

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: 85.83  E-value: 2.18e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827323766 860 DTDTADQVIASFKILAADK-----VNLHHGrgaaegAPPDQAEYCIARMAPYTGP--DAAPGALDYMSFSTALYG 927
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKpyvteEDLRRE------LTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 205-306 7.82e-19

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: 82.72  E-value: 7.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 205 PRRVFSLWCQRKTAPYK-NVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSL---RKLLKENNNIFNNECF----VHGEE 276
Cdd:pfam00307   3 LEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnksEFDKLENINLALDVAEkklgVPKVL 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1827323766 277 TPLKYIVNtarPDEKAIMTYVSSFYHAFSG 306
Cdd:pfam00307  83 IEPEDLVE---GDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 99-194 1.26e-18

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 81.98  E-value: 1.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766   99 KTFTAWCNSHLRKSGTQ-IENIEEDFRDGLKLMLLLETISGERL--AKPERGKMRVHKINNVNKALDFIAGKGVKLVSIG 175
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVdkKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|.
gi 1827323766  176 AED--GNAKMTLGMIWTIILR 194
Cdd:smart00033  81 PEDlvEGPKLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 207-300 4.67e-14

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 68.88  E-value: 4.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  207 RVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLLKENNNIFNNECFV---HGEETPLKYI- 282
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALsfaEKLGGKVVLFe 80

                           90       100
                   ....*....|....*....|.
gi 1827323766  283 ---VNTARPDEKAIMTYVSSF 300
Cdd:smart00033  81 pedLVEGPKLILGVIWTLISL 101
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 788-855 6.61e-13

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: 64.11  E-value: 6.61e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827323766 788 EYRASFNHFDKDHSGALMAEEFKACLISLGYDvennkQGDSEFARIMSIVDPNNSGAVTFQAFIDFMS 855
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEG-----LSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00184 PTZ00184
calmodulin; Provisional
 778-877 3.51e-11

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 62.09  E-value: 3.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 778 AKGISQEQLYEYRASFNHFDKDHSGALMAEEFKACLISLGydvENNKQGdsEFARIMSIVDPNNSGAVTFQAFIDFMSRE 857
Cdd:PTZ00184    2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLG---QNPTEA--ELQDMINEVDADGNGTIDFPEFLTLMARK 76

                          90       100
                  ....*....|....*....|
gi 1827323766 858 TTDTDTADQVIASFKILAAD 877
Cdd:PTZ00184   77 MKDTDSEEEIKEAFKVFDRD 96
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 667-771 3.44e-06

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: 46.54  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 667 KFATQANTVGAYIQAKMEVMRISEIGRiSIEmngTLEDQLTNLRDYQTSIMSYMPEINTLEGSHQLIQEALIFDNQYTSY 746
Cdd:pfam00435   5 QFFRDADDLESWIEEKEALLSSEDYGK-DLE---SVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                          90       100
                  ....*....|....*....|....*
gi 1827323766 747 TMEHLRVGWEQLLTTIARTINEVEN 771
Cdd:pfam00435  81 RLEELNERWEQLLELAAERKQKLEE 105
EF-hand_7 pfam13499
EF-hand domain pair;
790-855 3.09e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 3.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827323766 790 RASFNHFDKDHSGALMAEEFKACLISLGydvENNKQGDSEFARIMSIVDPNNSGAVTFQAFIDFMS 855
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLE---EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
788-854 1.18e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.86  E-value: 1.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827323766 788 EYRASFNHFDKDHSGALMAEEFKACLISLGYDVENNKQGdseFARImsivDPNNSGAVTFQAFIDFM 854
Cdd:COG5126    70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADEL---FARL----DTDGDGKISFEEFVAAV 129
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
465-554 2.80e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 41.21  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 465 LSEVKALLRKHEAFESDLAAHQDRveqiaaIAQELNELDYYDS--ASVNARCQKICDQWDSLG-ALTQNRKESLERTEKQ 541
Cdd:COG0497   305 LALLRRLARKYGVTVEELLAYAEE------LRAELAELENSDErlEELEAELAEAEAELLEAAeKLSAARKKAAKKLEKA 378

                          90
                  ....*....|....
gi 1827323766 542 L-ESIDELYLEYAK 554
Cdd:COG0497   379 VtAELADLGMPNAR 392
 
Name Accession Description Interval E-value
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 92-193 1.35e-68

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: 223.03  E-value: 1.35e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  92 AWEKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKPERGKMRVHKINNVNKALDFIAGKGVKL 171
Cdd:cd21214     1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPERGKMRFHKIANVNKALDFIASKGVKL 80

                          90       100
                  ....*....|....*....|....*
gi 1827323766 172 VSIGAE---DGNAKMTLGMIWTIIL 193
Cdd:cd21214    81 VSIGAEeivDGNLKMTLGMIWTIIL 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
93-365 1.33e-53

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 197.86  E-value: 1.33e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  93 WEKQQRKTFTAWCNSHLRKSGT-QIENIEEDFRDGLKLMLLLETISGERLAKPERGK-MRVHKINNVNKALDFIAGKGVK 170
Cdd:COG5069     6 WQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPeTRIHVMENVSGRLEFIKGKGVK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 171 LVSIG---AEDGNAKMTLGMIWTIILRFAIQDISR--PLPRRVFS-LWCQRKTAPYKN-VNVQNFHISWKDGLAFNALIH 243
Cdd:COG5069    86 LFNIGpqdIVDGNPKLILGLIWSLISRLTIATINEegELTKHINLlLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIH 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 244 RHRPDLIDYDSLRKLLK----------ENNNIFNNECFVHGEETplkyIVNTARPDEKAIMTYVSSFYHAFSGAQKAETA 313
Cdd:COG5069   166 DSRPDTLDPNVLDLQKKnkalnnfqafENANKVIGIARLIGVED----IVNVSIPDERSIMTYVSWYIIRFGLLEKIDIA 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1827323766 314 ANRICKVLAVNQENEQMMEDYEKLASELLEWIRRTIPWLENRTQEKTVTDMQ 365
Cdd:COG5069   242 LHRVYRLLEADETLIQLRLPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGE 293
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 197-305 7.04e-46

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: 160.22  E-value: 7.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 197 IQDIS--RPLPRRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkeNNNIFN-NECFvh 273
Cdd:cd21216     1 IQDISveELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRK----DDPRENlNLAF-- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1827323766 274 geETPLKY-----------IVNTARPDEKAIMTYVSSFYHAFS 305
Cdd:cd21216    75 --DVAEKHldipkmldaedIVNTPRPDERSVMTYVSCYYHAFA 115
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
 194-309 1.71e-43

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: 153.70  E-value: 1.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 194 RFAIQDIS--RPLPRRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRK--LLKENNNIFnne 269
Cdd:cd21290     1 RFAIQDISveETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKddPVTNLNNAF--- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1827323766 270 cfvhgeETPLKY-----------IVNTARPDEKAIMTYVSSFYHAFSGAQK 309
Cdd:cd21290    78 ------EVAEKYldipkmldaedIVNTARPDEKAIMTYVSSFYHAFSGAQK 122
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 97-194 1.43e-42

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: 150.52  E-value: 1.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  97 QRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKPERGKMRVHKINNVNKALDFIAGKgVKLVSIGA 176
Cdd:cd21193    17 QKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRGRLRVQKIENVNKALAFLKTK-VRLENIGA 95

                          90       100
                  ....*....|....*....|.
gi 1827323766 177 E---DGNAKMTLGMIWTIILR 194
Cdd:cd21193    96 EdivDGNPRLILGLIWTIILR 116
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 97-195 1.14e-40

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: 144.85  E-value: 1.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  97 QRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKpERGKMRVHKINNVNKALDFIAGKGVKLVSIGA 176
Cdd:cd21188     4 QKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPR-ERGRMRFHRLQNVQTALDFLKYRKIKLVNIRA 82

                          90       100
                  ....*....|....*....|..
gi 1827323766 177 E---DGNAKMTLGMIWTIILRF 195
Cdd:cd21188    83 EdivDGNPKLTLGLIWTIILHF 104
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 197-314 2.98e-39

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: 141.79  E-value: 2.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 197 IQDIS--RPLPRRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkeNNNIFN-NECFvh 273
Cdd:cd21289     1 IQDISveETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRK----DDPIGNlNTAF-- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1827323766 274 geETPLKY-----------IVNTARPDEKAIMTYVSSFYHAFSGAQKAETAA 314
Cdd:cd21289    75 --EVAEKYldipkmldaedIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAA 124
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 94-194 3.71e-39

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: 140.97  E-value: 3.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKPERGKMRVHKINNVNKALDFIAGKGVKLVS 173
Cdd:cd21246    14 EAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKMRIHCLENVDKALQFLKEQRVHLEN 93

                          90       100
                  ....*....|....*....|....
gi 1827323766 174 IGAE---DGNAKMTLGMIWTIILR 194
Cdd:cd21246    94 MGSHdivDGNHRLTLGLIWTIILR 117
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
 197-309 3.40e-38

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: 138.68  E-value: 3.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 197 IQDIS--RPLPRRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkeNNNIFN-NECFVH 273
Cdd:cd21287     1 IQDISveETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRK----DDPLTNlNTAFDV 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1827323766 274 GEE-------TPLKYIVNTARPDEKAIMTYVSSFYHAFSGAQK 309
Cdd:cd21287    77 AEKyldipkmLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQK 119
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 93-195 5.56e-38

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: 137.15  E-value: 5.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  93 WEKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAK-PERGKMRVHKINNVNKALDFIAGKGVKL 171
Cdd:cd21215     1 WVDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRyNKNPKMRVQKLENVNKALEFIKSRGVKL 80

                          90       100
                  ....*....|....*....|....*..
gi 1827323766 172 VSIGAE---DGNAKMTLGMIWTIILRF 195
Cdd:cd21215    81 TNIGAEdivDGNLKLILGLLWTLILRF 107
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 211-304 8.51e-38

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: 136.77  E-value: 8.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkeNNNIFN-NECF-VHGEETPLKYI-----V 283
Cdd:cd21194     9 LWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDP----NDHLGNlNNAFdVAEQELGIAKLldaedV 84

                          90       100
                  ....*....|....*....|.
gi 1827323766 284 NTARPDEKAIMTYVSSFYHAF 304
Cdd:cd21194    85 DVARPDEKSIMTYVASYYHYF 105
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 97-198 2.54e-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: 135.59  E-value: 2.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  97 QRKTFTAWCNSHLRKSG-TQIENIEEDFRDGLKLMLLLETISGERLaKPERGKMRVHKINNVNKALDFIAGKGVKLVSIG 175
Cdd:cd21186     3 QKKTFTKWINSQLSKANkPPIKDLFEDLRDGTRLLALLEVLTGKKL-KPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81

                          90       100
                  ....*....|....*....|....*.
gi 1827323766 176 AED---GNAKMTLGMIWTIILRFAIQ 198
Cdd:cd21186    82 SNDivdGNPKLTLGLVWSIILHWQVK 107
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 211-304 3.80e-37

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: 134.83  E-value: 3.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkeNNNIFN-NECFVHGEE----TPL--KYIV 283
Cdd:cd21248     9 LWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSK----SNALYNlQNAFNVAEQklglTKLldPEDV 84

                          90       100
                  ....*....|....*....|.
gi 1827323766 284 NTARPDEKAIMTYVSSFYHAF 304
Cdd:cd21248    85 NVEQPDEKSIITYVVTYYHYF 105
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
 197-314 4.71e-37

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: 135.20  E-value: 4.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 197 IQDIS--RPLPRRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLLKENNNIFNNECFVHG 274
Cdd:cd21288     1 IQDISveETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1827323766 275 EETP----LKYIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAA 314
Cdd:cd21288    81 LDIPkmldAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAA 124
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 94-194 3.60e-32

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: 122.06  E-value: 3.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKPERGKMRVHKINNVNKALDFIAGKGVKLVS 173
Cdd:cd21318    36 EAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRMRIHSLENVDKALQFLKEQRVHLEN 115

                          90       100
                  ....*....|....*....|....
gi 1827323766 174 IGAE---DGNAKMTLGMIWTIILR 194
Cdd:cd21318   116 VGSHdivDGNHRLTLGLIWTIILR 139
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 93-197 6.57e-32

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: 120.08  E-value: 6.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  93 WEKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERL-AKPERGKMRVHKINNVNKALDFIAGKGVKL 171
Cdd:cd21227     1 WVEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLgRVIKKPLNQHQKLENVTLALKAMAEDGIKL 80

                          90       100
                  ....*....|....*....|....*....
gi 1827323766 172 VSIGAED---GNAKMTLGMIWTIILRFAI 197
Cdd:cd21227    81 VNIGNEDivnGNLKLILGLIWHLILRYQI 109
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
 211-305 7.91e-32

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: 120.11  E-value: 7.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkeNNNIFN-NECFVHGEE----TPL--KYIV 283
Cdd:cd21319    12 LWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKK----SNARHNlEHAFNVAERqlgiTKLldPEDV 87

                          90       100
                  ....*....|....*....|..
gi 1827323766 284 NTARPDEKAIMTYVSSFYHAFS 305
Cdd:cd21319    88 FTENPDEKSIITYVVAFYHYFS 109
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 211-305 9.05e-32

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: 119.58  E-value: 9.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRkllkENNNIFN--NECFVHGEETPLKYI-----V 283
Cdd:cd21249    11 IWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLR----PDRPLYNlaNAFLVAEQELGISQLldpedV 86

                          90       100
                  ....*....|....*....|..
gi 1827323766 284 NTARPDEKAIMTYVSSFYHAFS 305
Cdd:cd21249    87 AVPHPDERSIMTYVSLYYHYFS 108
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 94-198 9.72e-32

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


Pssm-ID: 409090  Cd Length: 113  Bit Score: 119.79  E-value: 9.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNSHLRKSG--TQIENIEEDFRDGLKLMLLLETISGERLAKpERGKM--RVHKINNVNKALDFIAGKGV 169
Cdd:cd21241     3 ERVQKKTFTNWINSYLAKRKppMKVEDLFEDIKDGTKLLALLEVLSGEKLPC-EKGRRlkRVHFLSNINTALKFLESKKI 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1827323766 170 KLVSIGAE---DGNAKMTLGMIWTIILRFAIQ 198
Cdd:cd21241    82 KLVNINPTdivDGKPSIVLGLIWTIILYFQIE 113
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 80-194 9.37e-31

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: 117.46  E-value: 9.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  80 ENDWDRD------------LLLDPAWEKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKPERG 147
Cdd:cd21317     3 DDDWDNDnssarlfersriKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1827323766 148 KMRVHKINNVNKALDFIAGKGVKLVSIGAE---DGNAKMTLGMIWTIILR 194
Cdd:cd21317    83 RMRIHCLENVDKALQFLKEQKVHLENMGSHdivDGNHRLTLGLIWTIILR 132
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 211-305 3.02e-30

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: 115.70  E-value: 3.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLLKENNNIFNNECFVHGEETP----LKYIVNTA 286
Cdd:cd21291    17 LWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPqlldVEDVCDVA 96

                          90
                  ....*....|....*....
gi 1827323766 287 RPDEKAIMTYVSSFYHAFS 305
Cdd:cd21291    97 KPDERSIMTYVAYYFHAFS 115
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 94-200 6.43e-30

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: 115.08  E-value: 6.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKpERGKMRVHKINNVNKALDFIAGKGVKLVS 173
Cdd:cd21236    15 DKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALDYLKRRQVKLVN 93

                          90       100       110
                  ....*....|....*....|....*....|
gi 1827323766 174 IGAE---DGNAKMTLGMIWTIILRFAIQDI 200
Cdd:cd21236    94 IRNDditDGNPKLTLGLIWTIILHFQISDI 123
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 211-305 6.55e-30

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: 114.77  E-value: 6.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLLKENN--NIFNnecfVHGEETPLKYI-----V 283
Cdd:cd21321    12 LWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNlqNAFN----VAEKELGLTKLldpedV 87

                          90       100
                  ....*....|....*....|..
gi 1827323766 284 NTARPDEKAIMTYVSSFYHAFS 305
Cdd:cd21321    88 NVDQPDEKSIITYVATYYHYFS 109
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 94-200 1.63e-28

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: 110.88  E-value: 1.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKpERGKMRVHKINNVNKALDFIAGKGVKLVS 173
Cdd:cd21235     4 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1827323766 174 IGAE---DGNAKMTLGMIWTIILRFAIQDI 200
Cdd:cd21235    83 IRNDdiaDGNPKLTLGLIWTIILHFQISDI 112
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 82-197 1.70e-28

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: 111.00  E-value: 1.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  82 DWDRDLLLDPAWEKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAK-PERGKMRVHKINNVNKA 160
Cdd:cd21311     1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKfNKRPTFRSQKLENVSVA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1827323766 161 LDFIAG-KGVKLVSIGAE---DGNAKMTLGMIWTIILRFAI 197
Cdd:cd21311    81 LKFLEEdEGIKIVNIDSSdivDGKLKLILGLIWTLILHYSI 121
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 94-198 1.08e-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: 108.09  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNSHLRKSGTQ-IENIEEDFRDGLKLMLLLETISGERLAKpERGKMRVHKINNVNKALDFIAGKGVKLV 172
Cdd:cd21231     4 EDVQKKTFTKWINAQFAKFGKPpIEDLFTDLQDGRRLLELLEGLTGQKLVK-EKGSTRVHALNNVNKALQVLQKNNVDLV 82

                          90       100
                  ....*....|....*....|....*....
gi 1827323766 173 SIGAE---DGNAKMTLGMIWTIILRFAIQ 198
Cdd:cd21231    83 NIGSAdivDGNHKLTLGLIWSIILHWQVK 111
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 211-305 1.78e-27

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: 108.22  E-value: 1.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkeNNNIFNNECFVHGEETPLKYI-------V 283
Cdd:cd21322    24 LWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTK----SNATYNLQQAFNTAEQHLGLTklldpedV 99

                          90       100
                  ....*....|....*....|..
gi 1827323766 284 NTARPDEKAIMTYVSSFYHAFS 305
Cdd:cd21322   100 NMEAPDEKSIITYVVSFYHYFS 121
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 211-304 4.39e-27

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: 105.94  E-value: 4.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLL-KEN-NNIFN---NECFVhgeeTPL--KYIV 283
Cdd:cd21189     8 LWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSnRENlENAFNvaeKEFGV----TRLldPEDV 83

                          90       100
                  ....*....|....*....|.
gi 1827323766 284 NTARPDEKAIMTYVSSFYHAF 304
Cdd:cd21189    84 DVPEPDEKSIITYVSSLYDVF 104
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 97-197 9.45e-27

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: 106.00  E-value: 9.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  97 QRKTFTAWCNSHLRKSGTQIE--NIEEDFRDGLKLMLLLETISGERLAKPERGKMRVHKINNVNKALDFIAGKgVKLVSI 174
Cdd:cd21247    21 QKKTFTKWMNNVFSKNGAKIEitDIYTELKDGIHLLRLLELISGEQLPRPSRGKMRVHFLENNSKAITFLKTK-VPVKLI 99

                          90       100
                  ....*....|....*....|....*.
gi 1827323766 175 GAE---DGNAKMTLGMIWTIILRFAI 197
Cdd:cd21247   100 GPEnivDGDRTLILGLIWIIILRFQI 125
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 93-195 1.55e-26

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 104.49  E-value: 1.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  93 WEKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKP--ERGKMRVHKINNVNKALDFIAGKGVK 170
Cdd:cd21183     1 WKRIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSynRRPAFQQHYLENVSTALKFIEADHIK 80

                          90       100
                  ....*....|....*....|....*...
gi 1827323766 171 LVSIGAED---GNAKMTLGMIWTIILRF 195
Cdd:cd21183    81 LVNIGSGDivnGNIKLILGLIWTLILHY 108
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 94-200 1.57e-26

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: 105.11  E-value: 1.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKpERGKMRVHKINNVNKALDFIAGKGVKLVS 173
Cdd:cd21237     4 DRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPR-EKGRMRFHRLQNVQIALDFLKQRQVKLVN 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1827323766 174 IGAE---DGNAKMTLGMIWTIILRFAIQDI 200
Cdd:cd21237    83 IRNDditDGNPKLTLGLIWTIILHFQISDI 112
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 84-197 4.36e-26

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


Pssm-ID: 409159  Cd Length: 125  Bit Score: 103.96  E-value: 4.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  84 DRDLLLDPAWEKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKP--ERGKMRVHKINNVNKAL 161
Cdd:cd21310     4 EKDLAEDAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhPRPNFRQMKLENVSVAL 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1827323766 162 DFIAGKGVKLVSIGAE---DGNAKMTLGMIWTIILRFAI 197
Cdd:cd21310    84 EFLDREHIKLVSIDSKaivDGNLKLILGLIWTLILHYSI 122
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 94-194 8.23e-26

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: 104.36  E-value: 8.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKPERGKMRVHKINNVNKALDFIAGKGVKLVS 173
Cdd:cd21316    51 EAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLEN 130

                          90       100
                  ....*....|....*....|....
gi 1827323766 174 IGAE---DGNAKMTLGMIWTIILR 194
Cdd:cd21316   131 MGSHdivDGNHRLTLGLIWTIILR 154
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 93-195 1.54e-25

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: 101.80  E-value: 1.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  93 WEKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKP--ERGKMRVHKINNVNKALDFIAGKGVK 170
Cdd:cd21228     1 WKKIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKynKRPTFRQMKLENVSVALEFLERESIK 80

                          90       100
                  ....*....|....*....|....*...
gi 1827323766 171 LVSIGAE---DGNAKMTLGMIWTIILRF 195
Cdd:cd21228    81 LVSIDSSaivDGNLKLILGLIWTLILHY 108
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 211-304 1.60e-25

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: 101.65  E-value: 1.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkenNNIF-NNE-CFVHGEE---TPL----KY 281
Cdd:cd21253     8 QWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSK-----ENVYeNNKlAFTVAEKelgIPAlldaED 82

                          90       100
                  ....*....|....*....|...
gi 1827323766 282 IVNTARPDEKAIMTYVSSFYHAF 304
Cdd:cd21253    83 MVALKVPDKLSILTYVSQYYNYF 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 432-537 5.77e-25

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: 100.09  E-value: 5.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 432 HLAEKFHQKSKIHESWTDGKEAMLTQKDYEtCTLSEVKALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSASVN 511
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79

                          90       100
                  ....*....|....*....|....*.
gi 1827323766 512 ARCQKICDQWDSLGALTQNRKESLER 537
Cdd:pfam00435  80 ERLEELNERWEQLLELAAERKQKLEE 105
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 212-305 1.22e-24

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: 99.28  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSlrklLKENNNIFNNE-CFVHGEE----TPL---KYIV 283
Cdd:cd22198     8 WCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSS----LDPENIAENNQlAFDVAEQelgiPPVmtgQEMA 83

                          90       100
                  ....*....|....*....|..
gi 1827323766 284 NTARPDEKAIMTYVSSFYHAFS 305
Cdd:cd22198    84 SLAVPDKLSMVSYLSQFYEAFK 105
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 97-198 2.75e-24

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: 98.16  E-value: 2.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  97 QRKTFTAWCNSHLRKSGT-QIENIEEDFRDGLKLMLLLETISGERLAKpERGKMRVHKINNVNKALDFIAGKGVKLVSIG 175
Cdd:cd21232     3 QKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPK-ERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81

                          90       100
                  ....*....|....*....|....*.
gi 1827323766 176 AE---DGNAKMTLGMIWTIILRFAIQ 198
Cdd:cd21232    82 GTdivDGNHKLTLGLLWSIILHWQVK 107
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 211-305 3.77e-24

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: 97.86  E-value: 3.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkeNNNIFNNECFVHGEETPLKYI-------V 283
Cdd:cd21320     9 LWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKK----SNAHYNLQNAFNLAEQHLGLTklldpedI 84

                          90       100
                  ....*....|....*....|..
gi 1827323766 284 NTARPDEKAIMTYVSSFYHAFS 305
Cdd:cd21320    85 SVDHPDEKSIITYVVTYYHYFS 106
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 84-197 7.62e-24

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


Pssm-ID: 409158  Cd Length: 131  Bit Score: 97.84  E-value: 7.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  84 DRDLLLDPAWEKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKP--ERGKMRVHKINNVNKAL 161
Cdd:cd21309     5 EKDLAEDAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKyhQRPTFRQMQLENVSVAL 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1827323766 162 DFIAGKGVKLVSIGAE---DGNAKMTLGMIWTIILRFAI 197
Cdd:cd21309    85 EFLDRESIKLVSIDSKaivDGNLKLILGLVWTLILHYSI 123
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 94-198 1.47e-23

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: 96.49  E-value: 1.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNSHL--RKSGTQIENIEEDFRDGLKLMLLLETISGERLA--KPERGKmRVHKINNVNKALDFIAGKGV 169
Cdd:cd21190     3 ERVQKKTFTNWINSHLakLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPieSGRVLQ-RAHKLSNIRNALDFLTKRCI 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1827323766 170 KLVSIGAE---DGNAKMTLGMIWTIILRFAIQ 198
Cdd:cd21190    82 KLVNINSTdivDGKPSIVLGLIWTIILYFQIE 113
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 84-197 2.84e-23

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


Pssm-ID: 409157  Cd Length: 129  Bit Score: 96.31  E-value: 2.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  84 DRDLLLDPAWEKQQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERLAKP--ERGKMRVHKINNVNKAL 161
Cdd:cd21308     8 EKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKhnQRPTFRQMQLENVSVAL 87

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1827323766 162 DFIAGKGVKLVSIGAE---DGNAKMTLGMIWTIILRFAI 197
Cdd:cd21308    88 EFLDRESIKLVSIDSKaivDGNLKLILGLIWTLILHYSI 126
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
 205-305 4.73e-23

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: 94.55  E-value: 4.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 205 PRRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkeNNNIFNNECFVHGEETPL----- 279
Cdd:cd21252     1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSK----DNVYENNRLAFEVAERELgipal 76

                          90       100
                  ....*....|....*....|....*....
gi 1827323766 280 ---KYIVNTARPDEKAIMTYVSSFYHAFS 305
Cdd:cd21252    77 ldpEDMVSMKVPDCLSIMTYVSQYYNHFS 105
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 212-301 8.12e-23

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: 94.03  E-value: 8.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSlrkLLKENNNIFNNECF-VHGEETPLKYI-----VNT 285
Cdd:cd21187     8 WCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDS---LVKDSPESRLEHAFtVAHEHLGIEKLldpedVNV 84

                          90
                  ....*....|....*.
gi 1827323766 286 ARPDEKAIMTYVSSFY 301
Cdd:cd21187    85 EQPDKKSILMYVTSLF 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 433-566 1.24e-22

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: 97.13  E-value: 1.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 433 LAEKFHQKSKIHESWTDGKEAMLTQKDYETcTLSEVKALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSASVNA 512
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1827323766 513 RCQKICDQWDSLGALTQNRKESLERTEKQLESIDELYLeyakraapFNNWMEEQ 566
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD--------LEQWLEEK 125
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 95-197 2.41e-22

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 92.73  E-value: 2.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  95 KQQRKTFTAWCNSHLRKSG--TQIENIEEDFRDGLKLMLLLETISGERLAKPERGKMRVHKINNVNKALDFIAGK-GVKL 171
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKlGVPK 80

                          90       100
                  ....*....|....*....|....*....
gi 1827323766 172 VSIGAED---GNAKMTLGMIWTIILRFAI 197
Cdd:pfam00307  81 VLIEPEDlveGDNKSVLTYLASLFRRFQA 109
SPEC smart00150
Spectrin repeats;
435-536 6.37e-22

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 91.24  E-value: 6.37e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  435 EKFHQKSKIHESWTDGKEAMLTQKDYeTCTLSEVKALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSASVNARC 514
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79

                           90       100
                   ....*....|....*....|..
gi 1827323766  515 QKICDQWDSLGALTQNRKESLE 536
Cdd:smart00150  80 EELNERWEELKELAEERRQKLE 101
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
 212-304 3.07e-21

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: 89.68  E-value: 3.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkeNNNIFNNECFVHGEETPLKYI-------VN 284
Cdd:cd21243    13 WVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKR----RSNRENLETAFTVAEKELGIPrlldpedVD 88

                          90       100
                  ....*....|....*....|
gi 1827323766 285 TARPDEKAIMTYVSSFYHAF 304
Cdd:cd21243    89 VDKPDEKSIMTYVAQFLKKY 108
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 205-304 3.43e-21

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: 89.13  E-value: 3.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 205 PRRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkenNNIF-NNECFVHGEETPL---- 279
Cdd:cd21197     1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKK-----DNWLeNNRLAFRVAETSLgipa 75

                          90       100
                  ....*....|....*....|....*....
gi 1827323766 280 ----KYIVNTARPDEKAIMTYVSSFYHAF 304
Cdd:cd21197    76 lldaEDMVTMHVPDRLSIITYVSQYYNHF 104
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
 206-304 6.29e-21

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: 88.96  E-value: 6.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 206 RRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLLKENNNIFnneCFVHGEETPLKYIVN- 284
Cdd:cd21199    10 RNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTL---AFKAAESVGIPTTLTi 86

                          90       100
                  ....*....|....*....|....*
gi 1827323766 285 -----TARPDEKAIMTYVSSFYHAF 304
Cdd:cd21199    87 demvsMERPDWQSVMSYVTAIYKHF 111
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 94-198 1.19e-20

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: 87.96  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNSHLRK--SGTQIENIEEDFRDGLKLMLLLETISGERLAKpERGKMRVHKINNVNKALDFIAGKGVKL 171
Cdd:cd21242     3 EQTQKRTFTNWINSQLAKhsPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPR-EKGHNVFQCRSNIETALSFLKNKSIKL 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1827323766 172 VSIGAED---GNAKMTLGMIWTIILRFAIQ 198
Cdd:cd21242    82 INIHVPDiieGKPSIILGLIWTIILHFHIE 111
EFhand_Ca_insen pfam08726
Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the ...
 860-927 2.18e-20

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: 85.83  E-value: 2.18e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827323766 860 DTDTADQVIASFKILAADK-----VNLHHGrgaaegAPPDQAEYCIARMAPYTGP--DAAPGALDYMSFSTALYG 927
Cdd:pfam08726   1 DTDTAEQVEASFRALAGGKpyvteEDLRRE------LTPDQAEYCIARMPPYSGPdgDSVPGAYDYVSFSEALFG 69
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 94-199 7.22e-20

first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409040  Cd Length: 114  Bit Score: 85.71  E-value: 7.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNSHLRKSGT--QIENIEEDFRDGLKLMLLLETISGERLAKPER-GKMRVHKINNVNKALDFIAGKGVK 170
Cdd:cd21191     3 ENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKpSSHRIFRLNNIAKALKFLEDSNVK 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1827323766 171 LVSIGAE---DGNAKMTLGMIWTIILRFAIQD 199
Cdd:cd21191    83 LVSIDAAeiaDGNPSLVLGLIWNIILFFQIKE 114
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
 212-306 7.52e-20

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: 85.86  E-value: 7.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSlrklLKENNNIFNNECFVHGEETPL--------KYIV 283
Cdd:cd21195    12 WCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDS----LNEDDAVENNQLAFDVAEREFgippvttgKEMA 87

                          90       100
                  ....*....|....*....|...
gi 1827323766 284 NTARPDEKAIMTYVSSFYHAFSG 306
Cdd:cd21195    88 SAQEPDKLSMVMYLSKFYELFRG 110
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 212-305 1.18e-19

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: 84.78  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKL-LKENNNIFNNECFVHGEETPLK--YIVNTARP 288
Cdd:cd21198     9 WCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHdIKENCKLAFDAAAKLGIPRLLDpaDMVLLSVP 88

                          90
                  ....*....|....*..
gi 1827323766 289 DEKAIMTYVSSFYHAFS 305
Cdd:cd21198    89 DKLSVMTYLHQIRAHFT 105
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 206-300 1.39e-19

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: 84.78  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 206 RRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSlrklLKENNNIFN-NECFVHGEE----TPLK 280
Cdd:cd21192     5 EKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKT----VKNRSPRDNlELAFRIAEQhlniPRLL 80

                          90       100
                  ....*....|....*....|..
gi 1827323766 281 YI--VNTARPDEKAIMTYVSSF 300
Cdd:cd21192    81 EVedVLVDKPDERSIMTYVSQF 102
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
 212-304 3.31e-19

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: 83.84  E-value: 3.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLLKENNN-----IFNNECFVhgeeTPL---KYIV 283
Cdd:cd21251    13 WCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNqlafdIAEKEFGI----SPImtgKEMA 88

                          90       100
                  ....*....|....*....|.
gi 1827323766 284 NTARPDEKAIMTYVSSFYHAF 304
Cdd:cd21251    89 SVGEPDKLSMVMYLTQFYEMF 109
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 212-305 3.53e-19

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: 83.55  E-value: 3.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSlrklLKENNNIFNNE-CFVHGEE----TPL----KYI 282
Cdd:cd21200     9 WCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSS----LDPKNRRKNFElAFSTAEEladiAPLleveDMV 84

                          90       100
                  ....*....|....*....|...
gi 1827323766 283 VNTARPDEKAIMTYVSSFYHAFS 305
Cdd:cd21200    85 RMGNRPDWKCVFTYVQSLYRHLR 107
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
 211-306 3.98e-19

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: 83.78  E-value: 3.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSlrklLKENNNIFNNE-CFVHGEE-------TPLKYI 282
Cdd:cd21250    11 TWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDS----LNEDDAVKNNQlAFDVAERefgippvTTGKEM 86

                          90       100
                  ....*....|....*....|....
gi 1827323766 283 VNTARPDEKAIMTYVSSFYHAFSG 306
Cdd:cd21250    87 ASAEEPDKLSMVMYLSKFYELFRG 110
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 97-195 4.07e-19

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: 83.40  E-value: 4.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  97 QRKTFTAWCNSHLRKSGTQ--IENIEEDFRDGLKLMLLLETISGERLAKP-ERGKMRVHKINNVNKALDFIAGKGVKLVS 173
Cdd:cd21212     1 EIEIYTDWANHYLEKGGHKriITDLQKDLGDGLTLVNLIEAVAGEKVPGIhSRPKTRAQKLENIQACLQFLAALGVDVQG 80

                          90       100
                  ....*....|....*....|....*
gi 1827323766 174 IGAED---GNAKMTLGMIWTIILRF 195
Cdd:cd21212    81 ITAEDivdGNLKAILGLFFSLSRYK 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 205-306 7.82e-19

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: 82.72  E-value: 7.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 205 PRRVFSLWCQRKTAPYK-NVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSL---RKLLKENNNIFNNECF----VHGEE 276
Cdd:pfam00307   3 LEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnksEFDKLENINLALDVAEkklgVPKVL 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1827323766 277 TPLKYIVNtarPDEKAIMTYVSSFYHAFSG 306
Cdd:pfam00307  83 IEPEDLVE---GDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 99-194 1.26e-18

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 81.98  E-value: 1.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766   99 KTFTAWCNSHLRKSGTQ-IENIEEDFRDGLKLMLLLETISGERL--AKPERGKMRVHKINNVNKALDFIAGKGVKLVSIG 175
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVdkKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|.
gi 1827323766  176 AED--GNAKMTLGMIWTIILR 194
Cdd:smart00033  81 PEDlvEGPKLILGVIWTLISL 101
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 211-304 1.76e-18

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: 81.57  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSlrklLKENNNIFNNE-CFVHGEETPLKYI-----VN 284
Cdd:cd21239     8 LWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNT----VAVQSNLANLEhAFYVAEKLGVTRLldpedVD 83

                          90       100
                  ....*....|....*....|
gi 1827323766 285 TARPDEKAIMTYVSSFYHAF 304
Cdd:cd21239    84 VSSPDEKSVITYVSSLYDVF 103
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 93-191 9.26e-18

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: 79.88  E-value: 9.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  93 WEKQQRKTFTAWCNSHL-RKSGTQIENIEEDFRDGLKLMLLLETISGERLAKP--ERGKMRVHKINNVNKALDFIAGK-G 168
Cdd:cd21225     1 WEKVQIKAFTAWVNSVLeKRGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdLEPKNRIQMIQNLHLAMLFIEEDlK 80

                          90       100
                  ....*....|....*....|....*.
gi 1827323766 169 VKLVSIGAE---DGNAKMTLGMIWTI 191
Cdd:cd21225    81 IRVQGIGAEdfvDNNKKLILGLLWTL 106
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 212-301 3.84e-17

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: 77.69  E-value: 3.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKL-----LKENNNIFNNECFVHGEETPLKYIVNTa 286
Cdd:cd21234     8 WVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMspverLEHAFSKAKNHLGIEKLLDPEDVAVQL- 86

                          90
                  ....*....|....*
gi 1827323766 287 rPDEKAIMTYVSSFY 301
Cdd:cd21234    87 -PDKKSIIMYLTSLF 100
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 211-304 5.07e-17

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: 77.39  E-value: 5.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDydsLRKLLKENNNIFNNECFVHGEETPLKYI-----VNT 285
Cdd:cd21240    11 LWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVD---MERVQIQSNRENLEQAFEVAERLGVTRLldaedVDV 87

                          90
                  ....*....|....*....
gi 1827323766 286 ARPDEKAIMTYVSSFYHAF 304
Cdd:cd21240    88 PSPDEKSVITYVSSIYDAF 106
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 212-298 1.29e-16

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: 76.36  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKL-LKENNNifnnECFVHGEETPLKYIVNTAR--- 287
Cdd:cd21255     9 WCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLdIKENNK----KAFEAFASLGVPRLLEPADmvl 84

                          90
                  ....*....|....
gi 1827323766 288 ---PDEKAIMTYVS 298
Cdd:cd21255    85 lpiPDKLIVMTYLC 98
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 212-306 1.51e-16

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: 76.04  E-value: 1.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLLKENNNIFNNECFVH-GEETPLK--YIVNTARP 288
Cdd:cd21254     9 WCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASlGISRLLEpsDMVLLAVP 88

                          90
                  ....*....|....*...
gi 1827323766 289 DEKAIMTYVSSFYHAFSG 306
Cdd:cd21254    89 DKLTVMTYLYQIRAHFSG 106
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 212-304 1.92e-16

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: 76.22  E-value: 1.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLLKENNNIFnneCFVHGEETPLK------YIVNT 285
Cdd:cd21257    16 WCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLL---AFQAAESVGIKpslelsEMMYT 92

                          90
                  ....*....|....*....
gi 1827323766 286 ARPDEKAIMTYVSSFYHAF 304
Cdd:cd21257    93 DRPDWQSVMQYVAQIYKYF 111
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 212-304 4.33e-16

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: 74.96  E-value: 4.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRK---LLKENNNIFNNECFVHGEETPLK-YIVNTAR 287
Cdd:cd21233     8 WVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSqqsATERLDHAFNIARQHLGIEKLLDpEDVATAH 87

                          90
                  ....*....|....*..
gi 1827323766 288 PDEKAIMTYVSSFYHAF 304
Cdd:cd21233    88 PDKKSILMYVTSLFQVL 104
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 211-303 8.89e-16

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: 73.90  E-value: 8.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKllkeNNNIFNNECFVHGEETPLKYI-------V 283
Cdd:cd21238     9 LWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYR----QTNLENLDQAFSVAERDLGVTrlldpedV 84

                          90       100
                  ....*....|....*....|
gi 1827323766 284 NTARPDEKAIMTYVSSFYHA 303
Cdd:cd21238    85 DVPQPDEKSIITYVSSLYDA 104
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
 212-302 1.37e-15

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: 73.54  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSlrklLKENNNIFNNECFVHGEET-----PL----KYI 282
Cdd:cd21258     9 WCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQ----LSPQNRRQNFEVAFSAAEMladcvPLveveDMM 84

                          90       100
                  ....*....|....*....|
gi 1827323766 283 VNTARPDEKAIMTYVSSFYH 302
Cdd:cd21258    85 IMGKKPDSKCVFTYVQSLYN 104
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
 206-304 1.39e-15

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: 73.95  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 206 RRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLLKENNNIFnneCFVHGEETPLKY---- 281
Cdd:cd21256    16 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTL---AFQAAESVGIKStldi 92

                          90       100
                  ....*....|....*....|....*
gi 1827323766 282 --IVNTARPDEKAIMTYVSSFYHAF 304
Cdd:cd21256    93 neMVRTERPDWQSVMTYVTAIYKYF 117
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
 212-304 2.56e-15

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: 72.81  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLR-KLLKENNNIFNNECFVHGEETPL---KYIVNTAR 287
Cdd:cd21260     9 WCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDpANRRHNFTLAFSTAEKHADCAPLlevEDMVRMSV 88

                          90
                  ....*....|....*..
gi 1827323766 288 PDEKAIMTYVSSFYHAF 304
Cdd:cd21260    89 PDSKCVYTYIQELYRSL 105
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
 206-300 6.58e-15

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: 71.40  E-value: 6.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 206 RRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSlrklLKENNNIFNNECFVHGEETPLKYI--- 282
Cdd:cd21244     7 RKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEK----LKGRSNRENLEEAFRIAEQELKIPrll 82

                          90       100
                  ....*....|....*....|..
gi 1827323766 283 ----VNTARPDEKAIMTYVSSF 300
Cdd:cd21244    83 epedVDVVNPDEKSIMTYVAQF 104
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
 212-302 7.76e-15

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: 71.15  E-value: 7.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLLKENN---------NIFNNECFVHGEETplkyI 282
Cdd:cd21261     9 WCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNfelafsmaeKLANCDRLIEVEDM----M 84

                          90       100
                  ....*....|....*....|
gi 1827323766 283 VNTARPDEKAIMTYVSSFYH 302
Cdd:cd21261    85 VMGRKPDPMCVFTYVQSLYN 104
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 98-193 9.02e-15

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 70.83  E-value: 9.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  98 RKTFTAWCNSHLRKSGTQ-IENIEEDFRDGLKLMLLLETISGERLAK-PERGKMRVHKINNVNKALDFIAGKGV-KLVSI 174
Cdd:cd00014     1 EEELLKWINEVLGEELPVsITDLFESLRDGVLLCKLINKLSPGSIPKiNKKPKSPFKKRENINLFLNACKKLGLpELDLF 80

                          90       100
                  ....*....|....*....|...
gi 1827323766 175 GAED----GNAKMTLGMIWTIIL 193
Cdd:cd00014    81 EPEDlyekGNLKKVLGTLWALAL 103
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 211-304 3.59e-14

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: 69.03  E-value: 3.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 211 LWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKL--LKENNNIFNnecFVHGEETPLKYI----VN 284
Cdd:cd21226     7 AWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMdaEARLNLAFD---FAEKKLGIPKLLeaedVM 83

                          90       100
                  ....*....|....*....|
gi 1827323766 285 TARPDEKAIMTYVSSFYHAF 304
Cdd:cd21226    84 TGNPDERSIVLYTSLFYHAF 103
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 212-301 3.76e-14

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: 69.63  E-value: 3.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSlrklLKENNNIFNNECFVHGEET--------PLKYIV 283
Cdd:cd21259     9 WCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQ----LSPQNRRHNFEVAFSSAEKhadcpqllDVEDMV 84

                          90
                  ....*....|....*...
gi 1827323766 284 NTARPDEKAIMTYVSSFY 301
Cdd:cd21259    85 RMREPDWKCVYTYIQEFY 102
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 207-300 4.67e-14

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 68.88  E-value: 4.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  207 RVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLLKENNNIFNNECFV---HGEETPLKYI- 282
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALsfaEKLGGKVVLFe 80

                           90       100
                   ....*....|....*....|.
gi 1827323766  283 ---VNTARPDEKAIMTYVSSF 300
Cdd:smart00033  81 pedLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 332-536 1.05e-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: 70.94  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 332 EDYEKLASELLEWIRRTIPWLENRTQEKTVTDMQAKQEDFRDYR---CVHKPPKTKL-RLSNRpafMPSEGRMDINGAWY 407
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEaelAAHEERVEALnELGEQ---LIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 408 TLEGAEKGYE---EWILSEIRRLERLEHLAEKFHQKSKIhESWTDGKEAMLTQKDYETcTLSEVKALLRKHEAFESDLAA 484
Cdd:cd00176    80 RLEELNQRWEelrELAEERRQRLEEALDLQQFFRDADDL-EQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1827323766 485 HQDRVEQIAAIAQEL-NELDYYDSASVNARCQKICDQWDSLGALTQNRKESLE 536
Cdd:cd00176   158 HEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 788-855 6.61e-13

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: 64.11  E-value: 6.61e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827323766 788 EYRASFNHFDKDHSGALMAEEFKACLISLGYDvennkQGDSEFARIMSIVDPNNSGAVTFQAFIDFMS 855
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEG-----LSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 212-305 1.17e-12

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: 65.20  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYkNVNVQNFHISWKDGLAFNALIHRHRPDLIDydsLRKLLKENNNIFNNECFVHGEET--------PLKYIV 283
Cdd:cd21245    11 WVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVD---MRQALEKSPRENLEDAFRIAQESlgippllePEDVMV 86

                          90       100
                  ....*....|....*....|..
gi 1827323766 284 NTarPDEKAIMTYVSSFYHAFS 305
Cdd:cd21245    87 DS--PDEQSIMTYVAQFLEHFP 106
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 97-188 2.10e-11

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: 61.54  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  97 QRKTFTAWCNSHLRKSGT--QIENIEEDFRDGLKLMLLLETISGERLA----KPERGKMRvhkINNVNKALDFIAGKGVK 170
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGirPVQDLRRDLRDGVALAQLIEILAGEKLPgidwNPTTDAER---KENVEKVLQFMASKRIR 77

                          90       100
                  ....*....|....*....|.
gi 1827323766 171 LVSIGAED---GNAKMTLGMI 188
Cdd:cd21213    78 MHQTSAKDivdGNLKAIMRLI 98
PTZ00184 PTZ00184
calmodulin; Provisional
 778-877 3.51e-11

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 62.09  E-value: 3.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 778 AKGISQEQLYEYRASFNHFDKDHSGALMAEEFKACLISLGydvENNKQGdsEFARIMSIVDPNNSGAVTFQAFIDFMSRE 857
Cdd:PTZ00184    2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLG---QNPTEA--ELQDMINEVDADGNGTIDFPEFLTLMARK 76

                          90       100
                  ....*....|....*....|
gi 1827323766 858 TTDTDTADQVIASFKILAAD 877
Cdd:PTZ00184   77 MKDTDSEEEIKEAFKVFDRD 96
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 94-189 9.58e-11

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: 59.60  E-value: 9.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNSHLRksGTQIENIEEDFRDGLKLMLLLETISG-----ERLAKPERgKMRVHKINNVNKALDFIAGKG 168
Cdd:cd21219     2 GSREERAFRMWLNSLGL--DPLINNLYEDLRDGLVLLQVLDKIQPgcvnwKKVNKPKP-LNKFKKVENCNYAVDLAKKLG 78

                          90       100
                  ....*....|....*....|....
gi 1827323766 169 VKLVSIGAED---GNAKMTLGMIW 189
Cdd:cd21219    79 FSLVGIGGKDiadGNRKLTLALVW 102
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 206-302 1.25e-10

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: 59.27  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 206 RRVFSLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKLLK----ENNNIFNNECFVHGEETPLKY 281
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkrENINLFLNACKKLGLPELDLF 80

                          90       100
                  ....*....|....*....|...
gi 1827323766 282 IVN--TARPDEKAIMTYVSSFYH 302
Cdd:cd00014    81 EPEdlYEKGNLKKVLGTLWALAL 103
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 86-195 3.75e-10

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: 58.37  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  86 DLLLDPAWEK--QQRKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISG------ERLAKPERgkmRVHKINNV 157
Cdd:cd21222     4 DDLFDEAPEKlaEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGffvplhEYHLTPST---DDEKLHNV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1827323766 158 NKALDFIAGKGVKLVSIGAED---GNAKMTLGMIWTIILRF 195
Cdd:cd21222    81 KLALELMEDAGISTPKIRPEDivnGDLKSILRVLYSLFSKY 121
PTZ00183 PTZ00183
centrin; Provisional
 780-878 1.48e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 57.78  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 780 GISQEQLYEYRASFNHFDKDHSGALMAEEFKACLISLGYDVENnkqgdSEFARIMSIVDPNNSGAVTFQAFIDFMSRETT 859
Cdd:PTZ00183   10 GLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKK-----EEIKQMIADVDKDGSGKIDFEEFLDIMTKKLG 84

                          90
                  ....*....|....*....
gi 1827323766 860 DTDTADQVIASFKILAADK 878
Cdd:PTZ00183   85 ERDPREEILKAFRLFDDDK 103
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
 212-304 9.72e-09

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: 53.90  E-value: 9.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRKL--LKENN---NIFNNECFVhgeeTP-LKYIVNT 285
Cdd:cd21196    11 WCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLgaLEATAwalKVAENELGI----TPvVSAQAVV 86

                          90
                  ....*....|....*....
gi 1827323766 286 ARPDEKAIMTYVSSFYHAF 304
Cdd:cd21196    87 AGSDPLGLIAYLSHFHSAF 105
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 99-191 1.02e-08

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: 53.88  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  99 KTFTAWCNSHLRKSGTQ--IENIEEDFRDGLKLMLLLETISGERLAKPER-GKMRVHKINNVNKALDFIAGKGVKLVSIG 175
Cdd:cd21286     3 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVEDINGcPRSQSQMIENVDVCLSFLAARGVNVQGLS 82

                          90
                  ....*....|....*....
gi 1827323766 176 AE---DGNAKMTLGMIWTI 191
Cdd:cd21286    83 AEeirNGNLKAILGLFFSL 101
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 212-303 2.35e-08

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


Pssm-ID: 409033  Cd Length: 103  Bit Score: 52.62  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYknvNVQNFHISWKDGLAFNALIHRHRPDLI-DYDSLRKLLKENNnifNNECFVHGEE--------TPlKYI 282
Cdd:cd21184     9 WVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLEN---ATKAMDIAEEelgipkiiTP-EDM 81

                          90       100
                  ....*....|....*....|.
gi 1827323766 283 VNTaRPDEKAIMTYVSSFYHA 303
Cdd:cd21184    82 VSP-NVDELSVMTYLSYFRNA 101
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 97-191 5.28e-08

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: 52.27  E-value: 5.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  97 QRKTFTAWCNSHLRKSGTQ--IENIEEDFRDGLKLMLLLETISGERLAKPER-GKMRVHKINNVNKALDFIAGKGVKLVS 173
Cdd:cd21285    11 DKQIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcPKNRSQMIENIDACLSFLAAKGINIQG 90

                          90       100
                  ....*....|....*....|.
gi 1827323766 174 IGAED---GNAKMTLGMIWTI 191
Cdd:cd21285    91 LSAEEirnGNLKAILGLFFSL 111
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 94-198 2.14e-07

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: 50.31  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNShlrkSGTQ--IENIEEDFRDGLKLMLLLETIS-----GERLAKP---ERGKMRvhKINNVNKALDF 163
Cdd:cd21298     4 ETREEKTYRNWMNS----LGVNpfVNHLYSDLRDGLVLLQLYDKIKpgvvdWSRVNKPfkkLGANMK--KIENCNYAVEL 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1827323766 164 IAGKGVKLVSIGAED---GNAKMTLGMIWTIILRFAIQ 198
Cdd:cd21298    78 GKKLKFSLVGIGGKDiydGNRTLTLALVWQLMRAYTLS 115
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 99-197 5.83e-07

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: 48.96  E-value: 5.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  99 KTFTAWCNShlRKSGTQIENIEEDFRDGLKLMLLLETIS-GE----RLAKPERGK--MRVHKINNVNKALDFIAGKGVKL 171
Cdd:cd21300    10 RVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIpGSvnwkKVNKAPASAeiSRFKAVENTNYAVELGKQLGFSL 87

                          90       100
                  ....*....|....*....|....*....
gi 1827323766 172 VSI-GA--EDGNAKMTLGMIWTiILRFAI 197
Cdd:cd21300    88 VGIqGAdiTDGSRTLTLALVWQ-LMRFHI 115
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 115-192 2.41e-06

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


Pssm-ID: 409072  Cd Length: 113  Bit Score: 47.20  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 115 QIENIEEDFRDGLKLMLLLETISGERlakPERGKMRV------HKINNVNKALDFIAGKGVKLVSIGAE-------DGNA 181
Cdd:cd21223    25 AVTNLAVDLRDGVRLCRLVELLTGDW---SLLSKLRVpaisrlQKLHNVEVALKALKEAGVLRGGDGGGitakdivDGHR 101

                          90
                  ....*....|.
gi 1827323766 182 KMTLGMIWTII 192
Cdd:cd21223   102 EKTLALLWRII 112
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 667-771 3.44e-06

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: 46.54  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 667 KFATQANTVGAYIQAKMEVMRISEIGRiSIEmngTLEDQLTNLRDYQTSIMSYMPEINTLEGSHQLIQEALIFDNQYTSY 746
Cdd:pfam00435   5 QFFRDADDLESWIEEKEALLSSEDYGK-DLE---SVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQE 80

                          90       100
                  ....*....|....*....|....*
gi 1827323766 747 TMEHLRVGWEQLLTTIARTINEVEN 771
Cdd:pfam00435  81 RLEELNERWEQLLELAAERKQKLEE 105
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 79-197 6.34e-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: 46.53  E-value: 6.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  79 QENDWDrdlLLDPawEKQQRKTFTAWCNShlRKSGTQIENIEEDFRDGLKLMLLLETIS----GERLAKPERGKM--RVH 152
Cdd:cd21331    10 QDIDWT---LLEG--ETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIKvpvdWNKVNKPPYPKLgaNMK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1827323766 153 KINNVNKALDFiaGK---GVKLVSIGAED---GNAKMTLGMIWTIILRFAI 197
Cdd:cd21331    83 KLENCNYAVEL--GKhpaKFSLVGIGGQDlndGNPTLTLALVWQLMRRYTL 131
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 96-197 1.62e-05

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: 44.80  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  96 QQRKTFTAWCNShlRKSGTQIENIEEDFRDGLKLMLLLETISG-----ERLAKPERgKMRVHKINNVNKALDFiaGKGVK 170
Cdd:cd21299     4 REERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPgsvnwKHANKPPI-KMPFKKVENCNQVVKI--GKQLK 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1827323766 171 --LVSIGAED---GNAKMTLGMIWTiILRFAI 197
Cdd:cd21299    79 fsLVNVAGNDivqGNKKLILALLWQ-LMRYHM 109
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 98-167 2.88e-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: 43.80  E-value: 2.88e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827323766  98 RKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISGERL-----AKPERGKMrvHKINNVNKALDFIAGK 167
Cdd:cd21221     3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLevpevAQSEEGQK--QKLAVVLACVNFLLGL 75
EF-hand_7 pfam13499
EF-hand domain pair;
790-855 3.09e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 3.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827323766 790 RASFNHFDKDHSGALMAEEFKACLISLGydvENNKQGDSEFARIMSIVDPNNSGAVTFQAFIDFMS 855
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLE---EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 786-851 5.79e-05

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 44.44  E-value: 5.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827323766 786 LYEYRASFNHFDKDHSGALMAEEFKACLISLGYDVEnnkqgDSEFARIMSIVDPNNSGAVTFQAFI 851
Cdd:cd16180    66 IQDWRRLFRRFDRDRSGSIDFNELQNALSSFGYRLS-----PQFVQLLVRKFDRRRRGSISFDDFV 126
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 101-192 8.93e-05

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 42.56  E-value: 8.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 101 FTAWCNSHLRKS---------GTQIENIEEDFRDGLKLMLLLE-----TISGERLAKPerGKMRVHKIN-NVNKALDFIA 165
Cdd:cd21217     6 FVEHINSLLADDpdlkhllpiDPDGDDLFEALRDGVLLCKLINkivpgTIDERKLNKK--KPKNIFEATeNLNLALNAAK 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1827323766 166 GKGVKLVSIGAED---GNAKMTLGMIWTII 192
Cdd:cd21217    84 KIGCKVVNIGPQDildGNPHLVLGLLWQII 113
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
788-854 1.18e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.86  E-value: 1.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827323766 788 EYRASFNHFDKDHSGALMAEEFKACLISLGYDVENNKQGdseFARImsivDPNNSGAVTFQAFIDFM 854
Cdd:COG5126    70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADEL---FARL----DTDGDGKISFEEFVAAV 129
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 94-197 1.97e-04

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 41.89  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNShlRKSGTQIENIEEDFRDGLKLMLLLE----TISGERLAKPER----GKMRvhKINNVNKALDFIA 165
Cdd:cd21329     4 ESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEmtrvPVDWGHVNKPPYpalgGNMK--KIENCNYAVELGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1827323766 166 GKG-VKLVSIGAED---GNAKMTLGMIWTIILRFAI 197
Cdd:cd21329    80 NKAkFSLVGIAGSDlneGNKTLTLALIWQLMRRYTL 115
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 94-197 4.84e-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: 41.13  E-value: 4.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  94 EKQQRKTFTAWCNShlRKSGTQIENIEEDFRDGLKLMLLLETIS----GERLAKPERGKM--RVHKINNVNKALDFIAGK 167
Cdd:cd21330    11 ETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLgeNMKKLENCNYAVELGKNK 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1827323766 168 G-VKLVSIGAED---GNAKMTLGMIWTIILRFAI 197
Cdd:cd21330    89 AkFSLVGIAGQDlneGNRTLTLALIWQLMRRYTL 122
EF-hand_6 pfam13405
EF-hand domain;
788-817 5.43e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 37.93  E-value: 5.43e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1827323766 788 EYRASFNHFDKDHSGALMAEEFKACLISLG 817
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 86-195 6.64e-04

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: 40.48  E-value: 6.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766  86 DLLLDPAWEKQQ--RKTFTAWCNSHLRKSGTQIENIEEDFRDGLKLMLLLETISG------ERLAKPERGKMRVHkinNV 157
Cdd:cd21306     4 DTLFDHAPDKLNvvKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGyfvplhSFHLTPTSFEQKVH---NV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1827323766 158 NKALDFIAGKGVKLVSIGAED---GNAKMTLGMIWTIILRF 195
Cdd:cd21306    81 QFAFELMQDAGLPKPKARPEDivnLDLKSTLRVLYNLFTKY 121
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 784-851 1.02e-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: 40.71  E-value: 1.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827323766 784 EQLYEY----RASFNHFDKDHSGALMAEEFKACLISLGYDVEnnkqgdSEFAR-IMSIVDPNNSGAVTFQAFI 851
Cdd:cd16184    60 QALWNYiqqwKQVFQQFDRDRSGSIDENELHQALSQMGYRLS------PQFVQfLVSKYDPRARRSLTLDQFI 126
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 212-298 1.45e-03

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: 39.98  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 212 WCQRKTAPYkNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRK--------LLKENNNIFNNECFVHGEETPL--KY 281
Cdd:cd21224     8 WCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQpttqtvdrAQDEAEDFWVAEFSPSTGDSGLssEL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1827323766 282 IVNTAR----------------------------PDEKAIMTYVS 298
Cdd:cd21224    87 LANEKRnfklvqqavaelggvpallrasdmsntiPDEKVVILFLS 131
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 784-853 2.48e-03

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


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 39.51  E-value: 2.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827323766 784 EQLYEY----RASFNHFDKDHSGALMAEEFKACLISLGYDVennkqGDSEFARIMSIVDPNNSGAVTFQAFIDF 853
Cdd:cd16185    59 AALHQFlsnmQNGFEQRDTSRSGRLDANEVHEALAASGFQL-----DPPAFQALFRKFDPDRGGSLGFDDYIEL 127
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
465-554 2.80e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 41.21  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827323766 465 LSEVKALLRKHEAFESDLAAHQDRveqiaaIAQELNELDYYDS--ASVNARCQKICDQWDSLG-ALTQNRKESLERTEKQ 541
Cdd:COG0497   305 LALLRRLARKYGVTVEELLAYAEE------LRAELAELENSDErlEELEAELAEAEAELLEAAeKLSAARKKAAKKLEKA 378

                          90
                  ....*....|....
gi 1827323766 542 L-ESIDELYLEYAK 554
Cdd:COG0497   379 VtAELADLGMPNAR 392
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 790-852 3.16e-03

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: 39.43  E-value: 3.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827323766 790 RASFNHFDKDHSGALMAEEFKACLISlgydvennkqGDSEFARI------MSIVDPNNSGAVTFQAFID 852
Cdd:cd16180     3 RRIFQAVDRDRSGRISAKELQRALSN----------GDWTPFSIetvrlmINMFDRDRSGTINFDEFVG 61
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 786-823 3.79e-03

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 39.13  E-value: 3.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1827323766 786 LYEYRASFNHFDKDHSGALMAEEFKACLISLGYDVENN 823
Cdd:cd16182    71 LKKWQAIFKKFDTDRSGTLSSYELRKALESAGFHLSNK 108
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 214-273 6.75e-03

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 36.51  E-value: 6.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827323766 214 QRKTAPYkNVNVQNFHISWKDGLAFNALIHRHRPDLIDYDSLRklLKE---------NNNIFNNECFVH 273
Cdd:pfam11971   3 SQRSLPL-SPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDIC--LKEsmsladslyNIQLLQEFCQRH 68
 
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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