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Conserved domains on  [gi|100816764|ref|NP_444385|]
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calmin isoform a [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
29-142 1.06e-74

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: 241.33  E-value: 1.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   29 ERENVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21191     1 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSN 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 100816764  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 142
Cdd:cd21191    81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
186-291 3.92e-65

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: 214.65  E-value: 3.92e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  186 QRKAIKTLLSWVQRKTRKYGVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLE 265
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80
                          90       100
                  ....*....|....*....|....*.
gi 100816764  266 PEDIMVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21245    81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106
 
Name Accession Description Interval E-value
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
29-142 1.06e-74

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: 241.33  E-value: 1.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   29 ERENVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21191     1 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSN 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 100816764  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 142
Cdd:cd21191    81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
186-291 3.92e-65

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: 214.65  E-value: 3.92e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  186 QRKAIKTLLSWVQRKTRKYGVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLE 265
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80
                          90       100
                  ....*....|....*....|....*.
gi 100816764  266 PEDIMVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21245    81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
26-297 1.81e-30

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 128.52  E-value: 1.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   26 LQVERENVQKRTFTRWINLHLEKCDPPlEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLE 105
Cdd:COG5069     2 EAKKWQKVQKKTFTKWTNEKLISGGQK-EFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  106 DSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKEltgnlsrsspssslspgsggtdsdssypptpttersvaVAVKD 185
Cdd:COG5069    81 GKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIAT--------------------------------------INEEG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  186 QRKAIKTLLSWVQRKTRKY--GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMK--QALEDSTRDNLEKAFSIAHDSLHIP 261
Cdd:COG5069   123 ELTKHINLLLWCDEDTGGYkpEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNvlDLQKKNKALNNFQAFENANKVIGIA 202
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 100816764  262 RLLEPEDIM-VDMPDEQSIVTYVAQFLERFPELEPED 297
Cdd:COG5069   203 RLIGVEDIVnVSIPDERSIMTYVSWYIIRFGLLEKID 239
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
32-140 1.05e-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: 93.89  E-value: 1.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764    32 NVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGrNLLHEYKSSSHRIFRLNNIAKALKFLEDS-NVK 110
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAP-GLVDKKKLNKSEFDKLENINLALDVAEKKlGVP 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 100816764   111 LVSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
191-291 2.64e-21

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: 90.04  E-value: 2.64e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   191 KTLLSWVQRKTRKYG--VAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQ--ALEDSTRDNLEKAFSIAHDSLHIPR-LLE 265
Cdd:pfam00307    5 KELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlnKSEFDKLENINLALDVAEKKLGVPKvLIE 84
                           90       100
                   ....*....|....*....|....*.
gi 100816764   266 PEDIMvdMPDEQSIVTYVAQFLERFP 291
Cdd:pfam00307   85 PEDLV--EGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
36-137 8.78e-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: 79.67  E-value: 8.78e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764     36 RTFTRWINLHLEKcDPPLEVTDLFVDIQDGKILMALLEVLSGR-NLLHEYKSSSHRIFRLNNIAKALKFLEDSNVKLVSI 114
Cdd:smart00033    1 KTLLRWVNSLLAE-YDKPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79
                            90       100
                    ....*....|....*....|...
gi 100816764    115 DAAEIADGNPsLVLGLIWNIILF 137
Cdd:smart00033   80 EPEDLVEGPK-LILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
191-286 7.88e-15

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: 71.19  E-value: 7.88e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764    191 KTLLSWVQRKTRKYG-VAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTR----DNLEKAFSIAHDSLHIPRLLE 265
Cdd:smart00033    1 KTLLRWVNSLLAEYDkPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 100816764    266 PEDIMVDMPDEQSIVTYVAQF 286
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
 
Name Accession Description Interval E-value
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
29-142 1.06e-74

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: 241.33  E-value: 1.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   29 ERENVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21191     1 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSN 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 100816764  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 142
Cdd:cd21191    81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
186-291 3.92e-65

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: 214.65  E-value: 3.92e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  186 QRKAIKTLLSWVQRKTRKYGVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLE 265
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80
                          90       100
                  ....*....|....*....|....*.
gi 100816764  266 PEDIMVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21245    81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
186-291 6.02e-54

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: 183.01  E-value: 6.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  186 QRKAIKTLLSWVQRKTRK-YGVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLL 264
Cdd:cd21192     1 QGSAEKALLKWVQAEIGKyYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLL 80
                          90       100
                  ....*....|....*....|....*..
gi 100816764  265 EPEDIMVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21192    81 EVEDVLVDKPDERSIMTYVSQFLRMFP 107
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
29-141 1.31e-47

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: 165.24  E-value: 1.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   29 ERENVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 100816764  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21241    81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
184-291 4.12e-42

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: 149.39  E-value: 4.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  184 KDQRKAIKTLLSWVQRK-TRKYGVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPR 262
Cdd:cd21243     1 KFKGGAKKALLKWVQNAaAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPR 80
                          90       100
                  ....*....|....*....|....*....
gi 100816764  263 LLEPEDIMVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21243    81 LLDPEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
29-141 1.99e-40

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: 144.64  E-value: 1.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   29 ERENVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRC 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 100816764  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21190    81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
22-136 3.00e-40

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: 144.36  E-value: 3.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   22 RVQNLQVERENVQKRTFTRWINLHLEKCDppLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21193     5 RIRALQEERINIQKKTFTKWINSFLEKAN--LEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRGRL-RVQKIENVNKAL 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 100816764  102 KFLEdSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21193    82 AFLK-TKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
32-141 1.04e-38

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: 139.44  E-value: 1.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   32 NVQKRTFTRWINLHLEKCDPPLeVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSshRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21186     1 DVQKKTFTKWINSQLSKANKPP-IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRM--RVHHLNNVNRALQVLEQNNVKL 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 100816764  112 VSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21186    78 VNISSNDIVDGNPKLTLGLVWSIILHWQVK 107
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
22-136 9.66e-38

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: 137.11  E-value: 9.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   22 RVQNLQVERENVQKRTFTRWINLHLEKCdpPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21246     5 RIKALADEREAVQKKTFTKWVNSHLARV--GCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKM-RIHCLENVDKAL 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 100816764  102 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21246    82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
189-288 1.08e-36

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: 133.81  E-value: 1.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  189 AIKTLLSWVQRKTRKYG-VAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPE 267
Cdd:cd21244     6 ARKALLLWAQEQCAKVGsISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEPE 85
                          90       100
                  ....*....|....*....|.
gi 100816764  268 DIMVDMPDEQSIVTYVAQFLE 288
Cdd:cd21244    86 DVDVVNPDEKSIMTYVAQFLQ 106
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
29-141 4.20e-36

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: 132.26  E-value: 4.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   29 ERENVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEyksSSHRIFRL-NNIAKALKFLEDS 107
Cdd:cd21242     1 EQEQTQKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPRE---KGHNVFQCrSNIETALSFLKNK 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 100816764  108 NVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21242    78 SIKLINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
33-139 1.04e-35

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: 130.98  E-value: 1.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   33 VQKRTFTRWINLHLEKCDPPleVTDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSNVKLV 112
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRE--RGRMRFHRLQNVQTALDFLKYRKIKLV 78
                          90       100
                  ....*....|....*....|....*..
gi 100816764  113 SIDAAEIADGNPSLVLGLIWNIILFFQ 139
Cdd:cd21188    79 NIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
29-141 1.60e-33

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: 125.04  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   29 ERENVQKRTFTRWINLHLEKC-DPPLEvtDLFVDIQDGKILMALLEVLSGRNLLHEYKSSshRIFRLNNIAKALKFLEDS 107
Cdd:cd21231     2 EREDVQKKTFTKWINAQFAKFgKPPIE--DLFTDLQDGRRLLELLEGLTGQKLVKEKGST--RVHALNNVNKALQVLQKN 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 100816764  108 NVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21231    78 NVDLVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
187-290 2.36e-31

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: 118.28  E-value: 2.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  187 RKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLE 265
Cdd:cd21194     1 KSAKDALLLWCQRKTAGYpGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLD 80
                          90       100
                  ....*....|....*....|....*
gi 100816764  266 PEDIMVDMPDEQSIVTYVAQFLERF 290
Cdd:cd21194    81 AEDVDVARPDEKSIMTYVASYYHYF 105
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
29-143 1.13e-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: 117.39  E-value: 1.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   29 ERENVQKRTFTRWINLHLEKCDPplEVTDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21236    13 ERDKVQKKTFTKWINQHLMKVRK--HVNDLYEDLRDGHNLISLLEVLSGDTLPRE--KGRMRFHRLQNVQIALDYLKRRQ 88
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 100816764  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKEL 143
Cdd:cd21236    89 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
31-136 1.21e-30

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: 116.33  E-value: 1.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   31 ENVQKRTFTRWINLHLEKCDPPLEvtDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKALKFLEDSNVK 110
Cdd:cd21214     3 EKQQRKTFTAWCNSHLRKAGTQIE--NIEEDFRDGLKLMLLLEVISGERLPKPERGKM-RFHKIANVNKALDFIASKGVK 79
                          90       100
                  ....*....|....*....|....*.
gi 100816764  111 LVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21214    80 LVSIGAEEIVDGNLKMTLGMIWTIIL 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
26-297 1.81e-30

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 128.52  E-value: 1.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   26 LQVERENVQKRTFTRWINLHLEKCDPPlEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLE 105
Cdd:COG5069     2 EAKKWQKVQKKTFTKWTNEKLISGGQK-EFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  106 DSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKEltgnlsrsspssslspgsggtdsdssypptpttersvaVAVKD 185
Cdd:COG5069    81 GKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIAT--------------------------------------INEEG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  186 QRKAIKTLLSWVQRKTRKY--GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMK--QALEDSTRDNLEKAFSIAHDSLHIP 261
Cdd:COG5069   123 ELTKHINLLLWCDEDTGGYkpEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNvlDLQKKNKALNNFQAFENANKVIGIA 202
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 100816764  262 RLLEPEDIM-VDMPDEQSIVTYVAQFLERFPELEPED 297
Cdd:COG5069   203 RLIGVEDIVnVSIPDERSIMTYVSWYIIRFGLLEKID 239
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
22-136 7.33e-30

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: 115.51  E-value: 7.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   22 RVQNLQVERENVQKRTFTRWINLHLEKCdpPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21318    27 RIKALADEREAVQKKTFTKWVNSHLARV--PCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRM-RIHSLENVDKAL 103
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 100816764  102 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21318   104 QFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
189-291 2.99e-29

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: 112.49  E-value: 2.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  189 AIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPE 267
Cdd:cd21189     2 AKEALLLWARRTTEGYpGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDPE 81
                          90       100
                  ....*....|....*....|....
gi 100816764  268 DIMVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21189    82 DVDVPEPDEKSIITYVSSLYDVFP 105
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
186-290 6.18e-29

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: 111.88  E-value: 6.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  186 QRKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLL 264
Cdd:cd21249     2 LRSAKEALLIWCQRKTAGYtNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLL 81
                          90       100
                  ....*....|....*....|....*.
gi 100816764  265 EPEDIMVDMPDEQSIVTYVAQFLERF 290
Cdd:cd21249    82 DPEDVAVPHPDERSIMTYVSLYYHYF 107
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
31-138 7.13e-29

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: 111.34  E-value: 7.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   31 ENVQKRTFTRWINLHLEKCDppLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSNVK 110
Cdd:cd21215     2 VDVQKKTFTKWLNTKLSSRG--LSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVK 79
                          90       100
                  ....*....|....*....|....*...
gi 100816764  111 LVSIDAAEIADGNPSLVLGLIWNIILFF 138
Cdd:cd21215    80 LTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
22-136 7.91e-29

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: 112.45  E-value: 7.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   22 RVQNLQVERENVQKRTFTRWINLHLEKCDppLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21317    20 RIKALADEREAVQKKTFTKWVNSHLARVT--CRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKGRM-RIHCLENVDKAL 96
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 100816764  102 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21317    97 QFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
29-143 8.38e-29

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: 111.66  E-value: 8.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   29 ERENVQKRTFTRWINLHLEKCDPplEVTDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21235     2 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 100816764  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKEL 143
Cdd:cd21235    78 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDI 112
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
33-138 1.56e-27

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: 107.57  E-value: 1.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   33 VQKRTFTRWINLHLEKCDppLEVTDLFVDIQDGKILMALLEVLSGRNLLHEY-KSSSHRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21228     4 IQQNTFTRWCNEHLKCVN--KRIYNLETDLSDGLRLIALLEVLSQKRMYKKYnKRPTFRQMKLENVSVALEFLERESIKL 81
                          90       100
                  ....*....|....*....|....*..
gi 100816764  112 VSIDAAEIADGNPSLVLGLIWNIILFF 138
Cdd:cd21228    82 VSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
33-140 2.69e-27

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: 107.54  E-value: 2.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   33 VQKRTFTRWINLHLEKCDPPLEvtDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLE-DSNVKL 111
Cdd:cd21311    15 IQQNTFTRWANEHLKTANKHIA--DLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEeDEGIKI 92
                          90       100
                  ....*....|....*....|....*....
gi 100816764  112 VSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21311    93 VNIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
32-141 3.19e-27

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: 106.63  E-value: 3.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   32 NVQKRTFTRWINLHLEKCDPPlEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSshRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKP-PIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGST--RVHALNNVNRVLQVLHQNNVEL 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 100816764  112 VSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21232    78 VNIGGTDIVDGNHKLTLGLLWSIILHWQVK 107
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
187-290 3.68e-27

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: 106.33  E-value: 3.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  187 RKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLE 265
Cdd:cd21248     1 RSAKDALLLWCQMKTAGYpNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLD 80
                          90       100
                  ....*....|....*....|....*
gi 100816764  266 PEDIMVDMPDEQSIVTYVAQFLERF 290
Cdd:cd21248    81 PEDVNVEQPDEKSIITYVVTYYHYF 105
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
191-291 5.15e-27

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: 105.97  E-value: 5.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  191 KTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDI 269
Cdd:cd21187     3 KTLLAWCRQSTRGYeQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDV 82
                          90       100
                  ....*....|....*....|..
gi 100816764  270 MVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21187    83 NVEQPDKKSILMYVTSLFQVLP 104
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
193-290 5.99e-27

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: 106.29  E-value: 5.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDIM- 270
Cdd:cd21216    15 LLLWCQRKTAPYkNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDAEDIVn 94
                          90       100
                  ....*....|....*....|
gi 100816764  271 VDMPDEQSIVTYVAQFLERF 290
Cdd:cd21216    95 TPRPDERSVMTYVSCYYHAF 114
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
29-143 1.11e-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: 105.50  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   29 ERENVQKRTFTRWINLHLEKCDPplEVTDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21237     2 ERDRVQKKTFTKWVNKHLMKVRK--HINDLYEDLRDGHNLISLLEVLSGVKLPRE--KGRMRFHRLQNVQIALDFLKQRQ 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 100816764  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKEL 143
Cdd:cd21237    78 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 112
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
193-290 1.66e-25

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: 102.22  E-value: 1.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDIM- 270
Cdd:cd21291    15 LLLWCQRKTAGYdEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVEDVCd 94
                          90       100
                  ....*....|....*....|
gi 100816764  271 VDMPDEQSIVTYVAQFLERF 290
Cdd:cd21291    95 VAKPDERSIMTYVAYYFHAF 114
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
33-138 2.40e-25

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: 101.40  E-value: 2.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   33 VQKRTFTRWINLHLEKCDppLEVTDLFVDIQDGKILMALLEVLSGRNLLHEY-KSSSHRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21183     4 IQANTFTRWCNEHLKERG--MQIHDLATDFSDGLCLIALLENLSTRPLKRSYnRRPAFQQHYLENVSTALKFIEADHIKL 81
                          90       100
                  ....*....|....*....|....*..
gi 100816764  112 VSIDAAEIADGNPSLVLGLIWNIILFF 138
Cdd:cd21183    82 VNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
33-140 3.00e-25

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: 101.21  E-value: 3.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   33 VQKRTFTRWINLHLEKCDppLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSNVKLV 112
Cdd:cd21227     4 IQKNTFTNWVNEQLKPTG--MSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLV 81
                          90       100
                  ....*....|....*....|....*...
gi 100816764  113 SIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21227    82 NIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
184-294 5.58e-25

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: 100.46  E-value: 5.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  184 KDQRKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPR 262
Cdd:cd21319     1 RETRSAKDALLLWCQMKTAGYpNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 100816764  263 LLEPEDIMVDMPDEQSIVTYVAQFLERFPELE 294
Cdd:cd21319    81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKMK 112
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
22-136 1.05e-24

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: 101.27  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   22 RVQNLQVERENVQKRTFTRWINLHLEKCDppLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21316    42 RIKALADEREAVQKKTFTKWVNSHLARVS--CRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRM-RIHCLENVDKAL 118
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 100816764  102 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21316   119 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
16-140 1.62e-24

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: 99.83  E-value: 1.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   16 GQISDIRVQNLQVERENVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLlheyKSSSHRIFR-- 93
Cdd:cd21247     3 TEYEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQL----PRPSRGKMRvh 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 100816764   94 -LNNIAKALKFLEdSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21247    79 fLENNSKAITFLK-TKVPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
31-140 1.16e-23

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: 97.41  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   31 ENVQKRTFTRWINLHLeKCDPPlEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSH-RIFRLNNIAKALKFLEDSNV 109
Cdd:cd21310    14 KKIQQNTFTRWCNEHL-KCVQK-RLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNfRQMKLENVSVALEFLDREHI 91
                          90       100       110
                  ....*....|....*....|....*....|.
gi 100816764  110 KLVSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21310    92 KLVSIDSKAIVDGNLKLILGLIWTLILHYSI 122
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
184-294 1.20e-23

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: 97.05  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  184 KDQRKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPR 262
Cdd:cd21321     1 KEKKSAKDALLLWCQMKTAGYpNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 100816764  263 LLEPEDIMVDMPDEQSIVTYVAQFLERFPELE 294
Cdd:cd21321    81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMK 112
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
188-290 3.39e-23

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: 95.11  E-value: 3.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  188 KAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEP 266
Cdd:cd21253     1 AGIKALQQWCRQQTEGYrDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80
                          90       100
                  ....*....|....*....|....*.
gi 100816764  267 EDiMVDM--PDEQSIVTYVAQFLERF 290
Cdd:cd21253    81 ED-MVALkvPDKLSILTYVSQYYNYF 105
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
189-291 3.71e-23

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: 95.05  E-value: 3.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  189 AIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAhDSLHIPRLLEPE 267
Cdd:cd21239     2 AKERLLLWSQQMTEGYtGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVA-EKLGVTRLLDPE 80
                          90       100
                  ....*....|....*....|....
gi 100816764  268 DIMVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21239    81 DVDVSSPDEKSVITYVSSLYDVFP 104
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
32-140 1.05e-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: 93.89  E-value: 1.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764    32 NVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGrNLLHEYKSSSHRIFRLNNIAKALKFLEDS-NVK 110
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAP-GLVDKKKLNKSEFDKLENINLALDVAEKKlGVP 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 100816764   111 LVSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
189-291 1.01e-21

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: 90.85  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  189 AIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPE 267
Cdd:cd21238     3 AKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 82
                          90       100
                  ....*....|....*....|....
gi 100816764  268 DIMVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21238    83 DVDVPQPDEKSIITYVSSLYDAMP 106
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
184-294 1.10e-21

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: 91.65  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  184 KDQRKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPR 262
Cdd:cd21322    13 RETRSAKDALLLWCQMKTAGYpEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLTK 92
                          90       100       110
                  ....*....|....*....|....*....|..
gi 100816764  263 LLEPEDIMVDMPDEQSIVTYVAQFLERFPELE 294
Cdd:cd21322    93 LLDPEDVNMEAPDEKSIITYVVSFYHYFSKMK 124
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
191-291 2.64e-21

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: 90.04  E-value: 2.64e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   191 KTLLSWVQRKTRKYG--VAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQ--ALEDSTRDNLEKAFSIAHDSLHIPR-LLE 265
Cdd:pfam00307    5 KELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlnKSEFDKLENINLALDVAEKKLGVPKvLIE 84
                           90       100
                   ....*....|....*....|....*.
gi 100816764   266 PEDIMvdMPDEQSIVTYVAQFLERFP 291
Cdd:pfam00307   85 PEDLV--EGDNKSVLTYLASLFRRFQ 108
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
189-290 2.83e-21

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: 89.65  E-value: 2.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  189 AIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPE 267
Cdd:cd22198     1 RPEELLSWCQEQTEGYrGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQ 80
                          90       100
                  ....*....|....*....|....
gi 100816764  268 DIM-VDMPDEQSIVTYVAQFLERF 290
Cdd:cd22198    81 EMAsLAVPDKLSMVSYLSQFYEAF 104
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
191-291 3.09e-21

second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.


Pssm-ID: 409083 [Multi-domain]  Cd Length: 104  Bit Score: 89.63  E-value: 3.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  191 KTLLSWVQRKTRKYG-VAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDI 269
Cdd:cd21234     3 KILLSWVRQSTRPYSqVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDV 82
                          90       100
                  ....*....|....*....|..
gi 100816764  270 MVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21234    83 AVQLPDKKSIIMYLTSLFEVLP 104
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
189-291 4.82e-21

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: 89.33  E-value: 4.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  189 AIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAhDSLHIPRLLEPE 267
Cdd:cd21240     5 AKEKLLLWTQKVTAGYtGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVA-ERLGVTRLLDAE 83
                          90       100
                  ....*....|....*....|....
gi 100816764  268 DIMVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21240    84 DVDVPSPDEKSVITYVSSIYDAFP 107
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
31-140 5.93e-21

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: 89.75  E-value: 5.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   31 ENVQKRTFTRWINLHLEKCDPplEVTDLFVDIQDGKILMALLEVLSGRNLLHEY-KSSSHRIFRLNNIAKALKFLEDSNV 109
Cdd:cd21309    15 KKIQQNTFTRWCNEHLKCVNK--RIGNLQTDLSDGLRLIALLEVLSQKRMYRKYhQRPTFRQMQLENVSVALEFLDRESI 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 100816764  110 KLVSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21309    93 KLVSIDSKAIVDGNLKLILGLVWTLILHYSI 123
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
31-140 7.69e-21

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: 89.37  E-value: 7.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   31 ENVQKRTFTRWINLHLEKCDPplEVTDLFVDIQDGKILMALLEVLSGRNLLHEY-KSSSHRIFRLNNIAKALKFLEDSNV 109
Cdd:cd21308    18 KKIQQNTFTRWCNEHLKCVSK--RIANLQTDLSDGLRLIALLEVLSQKKMHRKHnQRPTFRQMQLENVSVALEFLDRESI 95
                          90       100       110
                  ....*....|....*....|....*....|.
gi 100816764  110 KLVSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21308    96 KLVSIDSKAIVDGNLKLILGLIWTLILHYSI 126
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
188-285 8.49e-21

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: 88.25  E-value: 8.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  188 KAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAhDSLHIPRLLEP 266
Cdd:cd21198     1 SSGQDLLEWCQEVTKGYrGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAA-AKLGIPRLLDP 79
                          90       100
                  ....*....|....*....|
gi 100816764  267 ED-IMVDMPDEQSIVTYVAQ 285
Cdd:cd21198    80 ADmVLLSVPDKLSVMTYLHQ 99
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
189-290 1.69e-20

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: 87.59  E-value: 1.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  189 AIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPE 267
Cdd:cd21197     1 KIQALLRWCRRQCEGYpGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80
                          90       100
                  ....*....|....*....|....*
gi 100816764  268 DiMVDM--PDEQSIVTYVAQFLERF 290
Cdd:cd21197    81 D-MVTMhvPDRLSIITYVSQYYNHF 104
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
187-293 4.55e-20

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: 86.31  E-value: 4.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  187 RKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLE 265
Cdd:cd21320     1 KSAKDALLLWCQMKTAGYpNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 80
                          90       100
                  ....*....|....*....|....*...
gi 100816764  266 PEDIMVDMPDEQSIVTYVAQFLERFPEL 293
Cdd:cd21320    81 PEDISVDHPDEKSIITYVVTYYHYFSKM 108
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
191-290 1.15e-19

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: 85.21  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  191 KTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDI 269
Cdd:cd21226     3 DGLLAWCRQTTEGYdGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
                          90       100
                  ....*....|....*....|.
gi 100816764  270 MVDMPDEQSIVTYVAQFLERF 290
Cdd:cd21226    83 MTGNPDERSIVLYTSLFYHAF 103
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
191-292 1.26e-18

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: 82.28  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  191 KTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQAL-EDSTRDNLEKAFSIAHDSLHIPRLLEPED 268
Cdd:cd21233     3 KILLSWVRQSTRNYpQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVsQQSATERLDHAFNIARQHLGIEKLLDPED 82
                          90       100
                  ....*....|....*....|....
gi 100816764  269 IMVDMPDEQSIVTYVAQFLERFPE 292
Cdd:cd21233    83 VATAHPDKKSILMYVTSLFQVLPQ 106
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
193-288 2.97e-18

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: 81.13  E-value: 2.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKYgvAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTR-DNLEKAFSIAHDSLHIPRLLEPEDIMV 271
Cdd:cd21184     6 LLEWVNSKIPEY--KVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPlENATKAMDIAEEELGIPKIITPEDMVS 83
                          90
                  ....*....|....*..
gi 100816764  272 DMPDEQSIVTYVAQFLE 288
Cdd:cd21184    84 PNVDELSVMTYLSYFRN 100
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
35-136 3.85e-18

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 80.85  E-value: 3.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   35 KRTFTRWINLHLEKcDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSNV-KLVS 113
Cdd:cd00014     1 EEELLKWINEVLGE-ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLpELDL 79
                          90       100
                  ....*....|....*....|....
gi 100816764  114 IDAAEI-ADGNPSLVLGLIWNIIL 136
Cdd:cd00014    80 FEPEDLyEKGNLKKVLGTLWALAL 103
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
189-290 6.81e-18

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: 80.22  E-value: 6.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  189 AIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHdSLHIPRLLEPE 267
Cdd:cd21255     2 SSQSLLEWCQEVTAGYrGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEPA 80
                          90       100
                  ....*....|....*....|....
gi 100816764  268 D-IMVDMPDEQSIVTYVAQFLERF 290
Cdd:cd21255    81 DmVLLPIPDKLIVMTYLCQLRAHF 104
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
36-137 8.78e-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: 79.67  E-value: 8.78e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764     36 RTFTRWINLHLEKcDPPLEVTDLFVDIQDGKILMALLEVLSGR-NLLHEYKSSSHRIFRLNNIAKALKFLEDSNVKLVSI 114
Cdd:smart00033    1 KTLLRWVNSLLAE-YDKPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79
                            90       100
                    ....*....|....*....|...
gi 100816764    115 DAAEIADGNPsLVLGLIWNIILF 137
Cdd:smart00033   80 EPEDLVEGPK-LILGVIWTLISL 101
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
31-132 1.12e-17

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: 79.50  E-value: 1.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   31 ENVQKRTFTRWINLHLEKCDPPlEVTDLFVDIQDGKILMALLEVLSGRNLLHEYK-SSSHRIFRLNNIAKALKFLE-DSN 108
Cdd:cd21225     2 EKVQIKAFTAWVNSVLEKRGIP-KISDLATDLSDGVRLIFFLELVSGKKFPKKFDlEPKNRIQMIQNLHLAMLFIEeDLK 80
                          90       100
                  ....*....|....*....|....
gi 100816764  109 VKLVSIDAAEIADGNPSLVLGLIW 132
Cdd:cd21225    81 IRVQGIGAEDFVDNNKKLILGLLW 104
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
189-290 1.38e-17

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: 79.13  E-value: 1.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  189 AIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAhDSLHIPRLLEPE 267
Cdd:cd21254     2 ASQSLLAWCKEVTKGYrGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGF-ASLGISRLLEPS 80
                          90       100
                  ....*....|....*....|....
gi 100816764  268 D-IMVDMPDEQSIVTYVAQFLERF 290
Cdd:cd21254    81 DmVLLAVPDKLTVMTYLYQIRAHF 104
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
185-301 1.41e-17

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: 79.74  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  185 DQRKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRL 263
Cdd:cd21287     7 EETSAKEGLLLWCQRKTAPYkNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKM 86
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 100816764  264 LEPEDIM-VDMPDEQSIVTYVAQFLERFPelEPEDFVNP 301
Cdd:cd21287    87 LDAEDIVgTARPDEKAIMTYVSSFYHAFS--GAQKAETA 123
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
185-290 3.53e-17

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: 78.59  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  185 DQRKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRL 263
Cdd:cd21290    10 EETSAKEGLLLWCQRKTAPYkNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKM 89
                          90       100
                  ....*....|....*....|....*...
gi 100816764  264 LEPEDIM-VDMPDEQSIVTYVAQFLERF 290
Cdd:cd21290    90 LDAEDIVnTARPDEKAIMTYVSSFYHAF 117
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
193-290 4.97e-17

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: 77.77  E-value: 4.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDIM- 270
Cdd:cd21195     9 LLTWCQQQTEGYqHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMAs 88
                          90       100
                  ....*....|....*....|
gi 100816764  271 VDMPDEQSIVTYVAQFLERF 290
Cdd:cd21195    89 AQEPDKLSMVMYLSKFYELF 108
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
189-290 8.10e-17

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: 77.00  E-value: 8.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  189 AIKT-LLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEP 266
Cdd:cd21200     1 SIKQmLLEWCQAKTRGYeHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                          90       100
                  ....*....|....*....|....*..
gi 100816764  267 EDiMVDM---PDEQSIVTYVAQFLERF 290
Cdd:cd21200    81 ED-MVRMgnrPDWKCVFTYVQSLYRHL 106
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
38-138 8.23e-17

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: 76.85  E-value: 8.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   38 FTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSNVKLVSIDAA 117
Cdd:cd21212     5 YTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQGITAE 84
                          90       100
                  ....*....|....*....|.
gi 100816764  118 EIADGNPSLVLGLIWNIILFF 138
Cdd:cd21212    85 DIVDGNLKAILGLFFSLSRYK 105
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
185-294 9.73e-17

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: 77.46  E-value: 9.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  185 DQRKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRL 263
Cdd:cd21289     7 EETSAKEGLLLWCQRKTAPYrNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKM 86
                          90       100       110
                  ....*....|....*....|....*....|..
gi 100816764  264 LEPEDIM-VDMPDEQSIVTYVAQFLERFPELE 294
Cdd:cd21289    87 LDAEDIVnTPKPDEKAIMTYVSCFYHAFAGAE 118
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
189-290 8.14e-16

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: 74.14  E-value: 8.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  189 AIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPE 267
Cdd:cd21252     1 ARRALQAWCRRQCEGYpGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
                          90       100
                  ....*....|....*....|....*
gi 100816764  268 DiMVDM--PDEQSIVTYVAQFLERF 290
Cdd:cd21252    81 D-MVSMkvPDCLSIMTYVSQYYNHF 104
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
193-292 1.75e-15

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: 73.44  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHI-PRLLEPEDIM 270
Cdd:cd21251    10 LLGWCQRQTEGYaGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGIsPIMTGKEMAS 89
                          90       100
                  ....*....|....*....|..
gi 100816764  271 VDMPDEQSIVTYVAQFLERFPE 292
Cdd:cd21251    90 VGEPDKLSMVMYLTQFYEMFKD 111
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
191-286 2.25e-15

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: 73.10  E-value: 2.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  191 KTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDi 269
Cdd:cd21259     4 QMLLDWCRAKTRGYeNVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED- 82
                          90
                  ....*....|....*....
gi 100816764  270 MVDM--PDEQSIVTYVAQF 286
Cdd:cd21259    83 MVRMrePDWKCVYTYIQEF 101
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
185-294 3.15e-15

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: 73.18  E-value: 3.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  185 DQRKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRL 263
Cdd:cd21288     7 EETSAKEGLLLWCQRKTAPYrNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKM 86
                          90       100       110
                  ....*....|....*....|....*....|..
gi 100816764  264 LEPEDIM-VDMPDEQSIVTYVAQFLERFPELE 294
Cdd:cd21288    87 LDAEDIVnTPKPDERAIMTYVSCFYHAFAGAE 118
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
191-286 7.88e-15

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: 71.19  E-value: 7.88e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764    191 KTLLSWVQRKTRKYG-VAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTR----DNLEKAFSIAHDSLHIPRLLE 265
Cdd:smart00033    1 KTLLRWVNSLLAEYDkPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 100816764    266 PEDIMVDMPDEQSIVTYVAQF 286
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
193-290 2.19e-14

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: 70.47  E-value: 2.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAhDSLHIPRLLEPEDiMV 271
Cdd:cd21199    13 LLKWCQEKTQGYkGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAA-ESVGIPTTLTIDE-MV 90
                          90       100
                  ....*....|....*....|.
gi 100816764  272 DM--PDEQSIVTYVAQFLERF 290
Cdd:cd21199    91 SMerPDWQSVMSYVTAIYKHF 111
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
193-286 5.86e-14

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: 69.34  E-value: 5.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDiMV 271
Cdd:cd21260     6 LLEWCRAKTRGYeHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED-MV 84
                          90
                  ....*....|....*..
gi 100816764  272 DM--PDEQSIVTYVAQF 286
Cdd:cd21260    85 RMsvPDSKCVYTYIQEL 101
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
191-283 1.44e-13

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: 68.15  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  191 KTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDI 269
Cdd:cd21258     4 QMLLDWCRAKTRGYeHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVEDM 83
                          90
                  ....*....|....*.
gi 100816764  270 MV--DMPDEQSIVTYV 283
Cdd:cd21258    84 MImgKKPDSKCVFTYV 99
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
193-290 2.35e-13

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: 67.21  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLE-PEDIM 270
Cdd:cd21250     9 LLTWCQKQTEGYqNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMAS 88
                          90       100
                  ....*....|....*....|
gi 100816764  271 VDMPDEQSIVTYVAQFLERF 290
Cdd:cd21250    89 AEEPDKLSMVMYLSKFYELF 108
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
193-286 2.72e-13

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


Pssm-ID: 409079  Cd Length: 103  Bit Score: 67.02  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRkyGVAVQDFAGSWRSGLAFLAVIKAIDPSLV------DMKQALEdstrdNLEKAFSIAHDSLHIPRLLEP 266
Cdd:cd21230     6 LLGWIQNKIP--QLPITNFTTDWNDGRALGALVDSCAPGLCpdwetwDPNDALE-----NATEAMQLAEDWLGVPQLITP 78
                          90       100
                  ....*....|....*....|
gi 100816764  267 EDIMVDMPDEQSIVTYVAQF 286
Cdd:cd21230    79 EEIINPNVDEMSVMTYLSQF 98
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
191-283 6.62e-13

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: 65.76  E-value: 6.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  191 KTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDI 269
Cdd:cd21261     4 QILLEWCRSKTIGYkNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVEDM 83
                          90
                  ....*....|....*.
gi 100816764  270 MV--DMPDEQSIVTYV 283
Cdd:cd21261    84 MVmgRKPDPMCVFTYV 99
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
193-290 3.08e-12

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: 64.28  E-value: 3.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAhDSLHIPRLLEPEDIM- 270
Cdd:cd21257    13 LLKWCQKKTEGYpNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAA-ESVGIKPSLELSEMMy 91
                          90       100
                  ....*....|....*....|
gi 100816764  271 VDMPDEQSIVTYVAQFLERF 290
Cdd:cd21257    92 TDRPDWQSVMQYVAQIYKYF 111
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
190-286 6.56e-12

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: 62.74  E-value: 6.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  190 IKTLLSWVQRKTRKYG-VAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDST---RDNLEKAFSIAHD-SLHIPRLL 264
Cdd:cd00014     1 EEELLKWINEVLGEELpVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
                          90       100
                  ....*....|....*....|..
gi 100816764  265 EPEDImVDMPDEQSIVTYVAQF 286
Cdd:cd00014    81 EPEDL-YEKGNLKKVLGTLWAL 101
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
42-135 1.06e-11

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


Pssm-ID: 409072  Cd Length: 113  Bit Score: 62.61  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   42 INLHLEKCD-------PPLE-----VTDLFVDIQDGKILMALLEVLSGRNLLHeykSSSH-----RIFRLNNIAKALKFL 104
Cdd:cd21223     1 LTRHLGYLGyvlshvqTPLDefdfaVTNLAVDLRDGVRLCRLVELLTGDWSLL---SKLRvpaisRLQKLHNVEVALKAL 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 100816764  105 EDSNV----KLVSIDAAEIADGNPSLVLGLIWNII 135
Cdd:cd21223    78 KEAGVlrggDGGGITAKDIVDGHREKTLALLWRII 112
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
35-135 2.06e-09

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: 56.04  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   35 KRTFTRWINLHLEKcDP--------PLEVTDLFVDIQDGKILMALLE-------VLSGRNllheyKSSSHRIFRLN-NIA 98
Cdd:cd21217     3 KEAFVEHINSLLAD-DPdlkhllpiDPDGDDLFEALRDGVLLCKLINkivpgtiDERKLN-----KKKPKNIFEATeNLN 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 100816764   99 KALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNII 135
Cdd:cd21217    77 LALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
193-290 6.81e-09

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: 54.69  E-value: 6.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAhDSLHIPRLLEPEDIM- 270
Cdd:cd21256    19 LLKWCQKKTEGYqNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAA-ESVGIKSTLDINEMVr 97
                          90       100
                  ....*....|....*....|
gi 100816764  271 VDMPDEQSIVTYVAQFLERF 290
Cdd:cd21256    98 TERPDWQSVMTYVTAIYKYF 117
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
193-286 8.06e-09

second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409164  Cd Length: 118  Bit Score: 54.79  E-value: 8.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKygVAVQDFAGSWRSGLAFLAVIKAIDPSLV------DMKQALEdstrdNLEKAFSIAHDSLHIPRLLEP 266
Cdd:cd21315    21 LLGWIQSKVPD--LPITNFTNDWNDGKAIGALVDALAPGLCpdwedwDPKDAVK-----NAKEAMDLAEDWLDVPQLIKP 93
                          90       100
                  ....*....|....*....|
gi 100816764  267 EDIMVDMPDEQSIVTYVAQF 286
Cdd:cd21315    94 EEMVNPKVDELSMMTYLSQF 113
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
34-131 1.55e-08

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: 53.46  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   34 QKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNL--LHEYKSSSHRifRLNNIAKALKFLEDSNVKL 111
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgIDWNPTTDAE--RKENVEKVLQFMASKRIRM 78
                          90       100
                  ....*....|....*....|
gi 100816764  112 VSIDAAEIADGNPSLVLGLI 131
Cdd:cd21213    79 HQTSAKDIVDGNLKAIMRLI 98
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
193-286 1.87e-08

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


Pssm-ID: 409162  Cd Length: 110  Bit Score: 53.17  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKygVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALE-DSTRDNLEKAFSIAHDSLHIPRLLEPEDIMV 271
Cdd:cd21313    13 LLGWIQNKIPY--LPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDpQKPVDNAREAMQQADDWLGVPQVITPEEIIH 90
                          90
                  ....*....|....*
gi 100816764  272 DMPDEQSIVTYVAQF 286
Cdd:cd21313    91 PDVDEHSVMTYLSQF 105
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
191-287 5.11e-08

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


Pssm-ID: 409078  Cd Length: 105  Bit Score: 52.00  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  191 KTLLSWVQRKTRKYGVavQDFAGSWRSGLAFLAVIKAIDPSLV-DMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDI 269
Cdd:cd21229     6 KLMLAWLQAVLPELKI--TNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPEDL 83
                          90
                  ....*....|....*...
gi 100816764  270 MVDMPDEQSIVTYVAQFL 287
Cdd:cd21229    84 SSPHLDELSGMTYLSYFM 101
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
193-286 1.08e-07

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


Pssm-ID: 409163  Cd Length: 115  Bit Score: 51.22  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKygVAVQDFAGSWRSGLAFLAVIKAIDPSLV------DMKQALEdstrdNLEKAFSIAHDSLHIPRLLEP 266
Cdd:cd21314    16 LLGWIQNKVPQ--LPITNFNRDWQDGKALGALVDNCAPGLCpdweswDPNQPVQ-----NAREAMQQADDWLGVPQVIAP 88
                          90       100
                  ....*....|....*....|
gi 100816764  267 EDIMVDMPDEQSIVTYVAQF 286
Cdd:cd21314    89 EEIVDPNVDEHSVMTYLSQF 108
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
15-141 2.39e-07

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 51.20  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   15 IGQISDIRVQNLQVERENVQKRTFTRWINLHLEKcDP------PLEVTD--LFVDIQDGKILMALLEvLSGRNLLHEYKS 86
Cdd:cd21323     6 IGGTSAISSEGTQHSYSEEEKVAFVNWINKALEG-DPdckhvvPMNPTDesLFKSLADGILLCKMIN-LSQPDTIDERAI 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 100816764   87 SSHRI--FRLN-NIAKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNII---LFFQIK 141
Cdd:cd21323    84 NKKKLtpFTISeNLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIkvgLFADIE 144
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
26-132 4.42e-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: 49.73  E-value: 4.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   26 LQVEREnvqKRTFTRWINlhleKCDPPLEVTDLFVDIQDGKILM-ALLEVLSGR-NLLHEYKSSSH----RIFRLNNIAK 99
Cdd:cd21300     3 AEGERE---ARVFTLWLN----SLDVEPAVNDLFEDLRDGLILLqAYDKVIPGSvNWKKVNKAPASaeisRFKAVENTNY 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 100816764  100 ALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIW 132
Cdd:cd21300    76 AVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
29-135 6.25e-07

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: 49.20  E-value: 6.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   29 EREnvqKRTFTRWINlhleKCDPPLEVTDLFVDIQDGKILMALLEVLSG----------RNLLHEYKssshrifRLNN-- 96
Cdd:cd21219     3 SRE---ERAFRMWLN----SLGLDPLINNLYEDLRDGLVLLQVLDKIQPgcvnwkkvnkPKPLNKFK-------KVENcn 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 100816764   97 ----IAKALKFledsnvKLVSIDAAEIADGNPSLVLGLIWNII 135
Cdd:cd21219    69 yavdLAKKLGF------SLVGIGGKDIADGNRKLTLALVWQLM 105
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
193-290 6.83e-07

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: 48.89  E-value: 6.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQ-----ALEDSTRdnlekAFSIAHDSLHIPRLLEP 266
Cdd:cd21196     8 LLRWCQEQTAGYpGVHVSDLSSSWADGLALCALVYRLQPGLLEPSElqglgALEATAW-----ALKVAENELGITPVVSA 82
                          90       100
                  ....*....|....*....|....
gi 100816764  267 EDIMVDmPDEQSIVTYVAQFLERF 290
Cdd:cd21196    83 QAVVAG-SDPLGLIAYLSHFHSAF 105
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
191-286 7.40e-07

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


Pssm-ID: 409161  Cd Length: 114  Bit Score: 49.03  E-value: 7.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  191 KTLLSWVQRKTRKygVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTR-DNLEKAFSIAHDSLHIPRLLEPEDI 269
Cdd:cd21312    15 QRLLGWIQNKLPQ--LPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPvTNAREAMQQADDWLGIPQVITPEEI 92
                          90
                  ....*....|....*..
gi 100816764  270 MVDMPDEQSIVTYVAQF 286
Cdd:cd21312    93 VDPNVDEHSVMTYLSQF 109
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
12-140 1.01e-06

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


Pssm-ID: 409141  Cd Length: 145  Bit Score: 49.20  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   12 EELIGQISDIRVQNLQVERENVQKRTFTRWINLHLEKcDP------PLEVT--DLFVDIQDGKILMALLEvLSGRNLLHE 83
Cdd:cd21292     3 IDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGD-DPdckhllPMDPNtdDLFEKVKDGILLCKMIN-LSVPDTIDE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 100816764   84 ykssshrifRLNNIAKALKFLEDSNVKL------------VSIDAAEIADGNPSLVLGLIWNII---LFFQI 140
Cdd:cd21292    81 ---------RAINKKKLTVFTIHENLTLalnsasaigcnvVNIGAEDLKEGKPHLVLGLLWQIIrigLFADI 143
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
40-134 3.39e-06

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 46.91  E-value: 3.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   40 RWINLHLEKCDPPL-EVTDLFVDIQDGKILMALLEVLSGRN----LLHEYKSSSHrifRLNNIAKALKFLEDSNVKLVsI 114
Cdd:cd21218    17 RWVNYHLKKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELcdkeLVLEVLSEED---LEKRAEKVLQAAEKLGCKYF-L 92
                          90       100
                  ....*....|....*....|
gi 100816764  115 DAAEIADGNPSLVLGLIWNI 134
Cdd:cd21218    93 TPEDIVSGNPRLNLAFVATL 112
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
34-139 1.04e-05

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: 45.72  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   34 QKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSNVKLVS 113
Cdd:cd21285    11 DKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAKGINIQG 90
                          90       100
                  ....*....|....*....|....*.
gi 100816764  114 IDAAEIADGNPSLVLGLIWNIILFFQ 139
Cdd:cd21285    91 LSAEEIRNGNLKAILGLFFSLSRYKQ 116
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
28-135 1.16e-05

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 46.15  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   28 VERENVQKRTFTRWINLhlEKCDPplEVTDLFVDIQDGKILMALLE---VLSGRNLLHE--YKSSSHRIFRLNNIAKALK 102
Cdd:cd21331    17 LEGETREERTFRNWMNS--LGVNP--HVNHLYGDLQDALVILQLYEkikVPVDWNKVNKppYPKLGANMKKLENCNYAVE 92
                          90       100       110
                  ....*....|....*....|....*....|....
gi 100816764  103 FLEDS-NVKLVSIDAAEIADGNPSLVLGLIWNII 135
Cdd:cd21331    93 LGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLM 126
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
36-134 1.59e-05

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: 45.02  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   36 RTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEY---KSSSHRIfrlNNIAKALKFLEDSNVKLV 112
Cdd:cd21286     3 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINgcpRSQSQMI---ENVDVCLSFLAARGVNVQ 79
                          90       100
                  ....*....|....*....|..
gi 100816764  113 SIDAAEIADGNPSLVLGLIWNI 134
Cdd:cd21286    80 GLSAEEIRNGNLKAILGLFFSL 101
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
15-146 3.04e-05

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


Pssm-ID: 409174  Cd Length: 148  Bit Score: 45.05  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   15 IGQISDIRVQNLQVERENVQKRTFTRWINLHLEKcDP------PLE--VTDLFVDIQDGKILMALLEvLSGRNLLHEYKS 86
Cdd:cd21325     6 LGGTSELSSEGTQHSYSEEEKYAFVNWINKALEN-DPdcrhviPMNpnTDDLFKAVGDGIVLCKMIN-LSVPDTIDERAI 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 100816764   87 SSHRIFRL---NNIAKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNII---LFFQIkELTGN 146
Cdd:cd21325    84 NKKKLTPFiiqENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIkigLFADI-ELSRN 148
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
34-143 2.31e-04

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: 41.72  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   34 QKRTFTRWINlhleKCDPPLEVTDLFVDIQDGKILMALLEVLSGR--NLLHEYKSSSHRIFR-LNN------IAKALKFl 104
Cdd:cd21299     5 EERCFRLWIN----SLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGsvNWKHANKPPIKMPFKkVENcnqvvkIGKQLKF- 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 100816764  105 edsnvKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKEL 143
Cdd:cd21299    80 -----SLVNVAGNDIVQGNKKLILALLWQLMRYHMLQLL 113
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
29-134 3.51e-04

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: 41.42  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   29 ERENVQKRTFTRWINLHLEKCDppLEVTDLFVDIQDGKILMALLEVLSGRNL-LHEYKSS-SHRIFRLNNIAKALKFLED 106
Cdd:cd21222    12 EKLAEVKELLLQFVNKHLAKLN--IEVTDLATQFHDGVYLILLIGLLEGFFVpLHEYHLTpSTDDEKLHNVKLALELMED 89
                          90       100
                  ....*....|....*....|....*...
gi 100816764  107 SNVKLVSIDAAEIADGNPSLVLGLIWNI 134
Cdd:cd21222    90 AGISTPKIRPEDIVNGDLKSILRVLYSL 117
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
34-135 5.80e-04

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


Pssm-ID: 409173  Cd Length: 145  Bit Score: 41.53  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   34 QKRTFTRWINLHLEKcDP------PL--EVTDLFVDIQDGKILMALLEvLSGRNLLHEYKSSSHRIFRLN---NIAKALK 102
Cdd:cd21324    25 EKYAFVNWINKALEN-DPdckhviPMnpNTDDLFKAVGDGIVLCKMIN-FSVPDTIDERTINKKKLTPFTiqeNLNLALN 102
                          90       100       110
                  ....*....|....*....|....*....|...
gi 100816764  103 FLEDSNVKLVSIDAAEIADGNPSLVLGLIWNII 135
Cdd:cd21324   103 SASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
34-135 8.07e-04

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


Pssm-ID: 409142  Cd Length: 116  Bit Score: 40.20  E-value: 8.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   34 QKRTFTRWINLHLEKcDPPLE--------VTDLFVDIQDGKILMALLEV----------LSGRNLLHEYKSSSHRIFRLN 95
Cdd:cd21293     2 EKGSYVDHINRYLGD-DPFLKqflpidpsTNDLFDLVKDGVLLCKLINVavpgtideraINTKKVLNPWERNENHTLCLN 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 100816764   96 NiAKALkfledsNVKLVSIDAAEIADGNPSLVLGLIWNII 135
Cdd:cd21293    81 S-AKAI------GCSVVNIGTQDLAEGRPHLVLGLISQII 113
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
34-135 1.01e-03

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 40.12  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   34 QKRTFTRWINLHLEKcDP--------PLEVTDLFVDIQDGKILMALL-----EVLSGRNLLHEYKS----SSHRIFRLNN 96
Cdd:cd21294     7 ERREFTKHINAVLAG-DPdvgsrlpfPTDTFQLFDECKDGLVLSKLIndsvpDTIDERVLNKPPRKnkplNNFQMIENNN 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 100816764   97 I----AKALkfledsNVKLVSIDAAEIADGNPSLVLGLIWNII 135
Cdd:cd21294    86 IvinsAKAI------GCSVVNIGAGDIIEGREHLILGLIWQII 122
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
32-134 1.56e-03

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: 39.71  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764   32 NVQKRTFTRWINLHLEKCDppLEVTDLFVDIQDGKILMALLEVLSGRNL-LHEY----KSSSHRIfrlNNIAKALKFLED 106
Cdd:cd21306    15 NVVKKSLITFVNKHLNKLN--LEVTDLDTQFHDGVYLVLLMGLLEGYFVpLHSFhltpTSFEQKV---HNVQFAFELMQD 89
                          90       100
                  ....*....|....*....|....*...
gi 100816764  107 SNVKLVSIDAAEIADGNPSLVLGLIWNI 134
Cdd:cd21306    90 AGLPKPKARPEDIVNLDLKSTLRVLYNL 117
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
193-285 1.62e-03

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 39.20  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKYGVA---VQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEK-AFSIAH--DSLHIPRLLEP 266
Cdd:cd21218    15 LLRWVNYHLKKAGPTkkrVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKrAEKVLQaaEKLGCKYFLTP 94
                          90
                  ....*....|....*....
gi 100816764  267 EDImVDmPDEQSIVTYVAQ 285
Cdd:cd21218    95 EDI-VS-GNPRLNLAFVAT 111
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
194-286 3.84e-03

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


Pssm-ID: 409034  Cd Length: 98  Bit Score: 37.67  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  194 LSWVQRKTRKygVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHdSLHIPRLLEPEDiMVDm 273
Cdd:cd21185     7 LRWVRQLLPD--VDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGK-SLGVEPVLTAEE-MAD- 81
                          90
                  ....*....|....*
gi 100816764  274 PDEQS--IVTYVAQF 286
Cdd:cd21185    82 PEVEHlgIMAYAAQL 96
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
193-288 5.18e-03

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


Pssm-ID: 409069  Cd Length: 105  Bit Score: 37.63  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816764  193 LLSWVQRKTRKYGVA--VQDFAG-SWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEK----AFSIAHdSLHIPRLLE 265
Cdd:cd21220     6 ILAWANSKVREAGKSspISSFKDpSLSTGLFLLDLLAAIDPGAVDYDLVTEGETDEEKEQnakyAISLAR-KIGAVIFLL 84
                          90       100
                  ....*....|....*....|...
gi 100816764  266 PEDImVDMpDEQSIVTYVAQFLE 288
Cdd:cd21220    85 WEDI-VEV-KPKMILTFVASLMA 105
 
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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