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Conserved domains on  [gi|87298845|ref|NP_033921|]
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abnormal spindle-like microcephaly-associated protein homolog [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 1081-1229 9.45e-67

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


:

Pssm-ID: 409073 [Multi-domain]  Cd Length: 138  Bit Score: 222.18  E-value: 9.45e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1081 VQLLMDWVNAVCAFYNKKVENFTVSFSDGRILCYLIHHYHPCYVPFDAICQRTSQSVACAQTGSVVLNSSSESeggcldl 1160
Cdd:cd21224    2 LSLLLKWCQAVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQTVDRAQDEAEDFWVAEFS------- 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 87298845 1161 slealDHESTPEMYKELLENEKKNFHLVRSAARDLGGIPAMIHHSDMSNTIPDEKVVITYLSFLCARLL 1229
Cdd:cd21224   75 -----PSTGDSGLSSELLANEKRNFKLVQQAVAELGGVPALLRASDMSNTIPDEKVVILFLSYLCARLL 138
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 908-1020 1.97e-54

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: 185.87  E-value: 1.97e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  908 LSRHLSFLGLPVSHVQTPLDEFDFAVTNLAVDLQCGVRLVRTVELLTQNWNLSDKLRIPAISRVQKMHNVDLVLQVLKSR 987
Cdd:cd21223    1 LTRHLGYLGYVLSHVQTPLDEFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQKLHNVEVALKALKEA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 87298845  988 GVpLTDEHGSAISSKDVVDRHREKTLGLLWKIA 1020
Cdd:cd21223   81 GV-LRGGDGGGITAKDIVDGHREKTLALLWRII 112
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 29-126 4.01e-38

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


:

Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 138.95  E-value: 4.01e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845     29 PVLLLSHFCGVPFLCFGDVRVGTSRTRSLVLHNPHEEPLQVELSLLRAAGQGFSVAPNRCELKPKEKLTISVTWTPLREG 108
Cdd:pfam15780    1 PVLLLAPFSRQPFVCFGDVPVGTSAERLLTVVNPSEEPAEVKVSKVPAPTKGFSVSPLEFTVQPGESQTLTVTWTPTEEG 80

                           90
                   ....*....|....*...
gi 87298845    109 GVREIVTFLVNDFLKHQA 126
Cdd:pfam15780   81 AVRETLQFTVNDVGKHQV 98
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
1236-1419 2.27e-09

Myosin heavy chain [General function prediction only];


The actual alignment was detected with superfamily member COG5022:

Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 63.56  E-value: 2.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1236 RAARLIQTTWRKYKLKRDLKHHQERDKAARVIQSvvlNFLSRRRLQ--KNVSAALVIQKCWR----------RVSAQRKL 1303
Cdd:COG5022  746 NIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQH---GFRLRRLVDyeLKWRLFIKLQPLLSllgsrkeyrsYLACIIKL 822

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1304 -RMLKNEKLA------KLQNKSAVLIQAYWRRYSTRKRFLRLKHYSVILQSRIRMKIALTSYKRYLWATVTIQRhwRAYL 1376
Cdd:COG5022  823 qKTIKREKKLreteevEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS--LKLV 900

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 87298845 1377 SRKRDQQIFRKLK--SSSLVIQFMFR-----RWKRRKLQLQTKAAVTLQR 1419
Cdd:COG5022  901 NLELESEIIELKKslSSDLIENLEFKteliaRLKKLLNNIDLEEGPSIEY 950
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
2103-2290 6.96e-08

Myosin heavy chain [General function prediction only];


The actual alignment was detected with superfamily member COG5022:

Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 58.94  E-value: 6.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2103 RYLKMRTAALIIQVRYRAYYLGKiqheKYLRTLKAIKTLQAGVRGARVRRtVRKMHF---AATLIQSHFRGHRQQTYFHR 2179
Cdd:COG5022  740 RDAKLDNIATRIQRAIRGRYLRR----RYLQALKRIKKIQVIQHGFRLRR-LVDYELkwrLFIKLQPLLSLLGSRKEYRS 814

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2180 LRKAATMVQqrYRAVKEgsaefqrysrlrrsvlliqaafRGLRTRRHLKAMHLAATLIQRRFRTFAMRRKFLSLRKTAIW 2259
Cdd:COG5022  815 YLACIIKLQ--KTIKRE----------------------KKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIY 870

                        170       180       190
                 ....*....|....*....|....*....|.
gi 87298845 2260 IQRQYRARLYAKYSRQqllLEKAVIKIQSSY 2290
Cdd:COG5022  871 LQSAQRVELAERQLQE---LKIDVKSISSLK 898
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
2225-2393 5.20e-07

Myosin heavy chain [General function prediction only];


The actual alignment was detected with superfamily member COG5022:

Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 55.85  E-value: 5.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2225 RHLKAMHLAATLIQRRFRTFAMRRKFLSLRKTAIWIQRQYRARLYAKYSRQQLLLeKAVIKIQSSYRGWVVRKRVQKMHR 2304
Cdd:COG5022  739 MRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKW-RLFIKLQPLLSLLGSRKEYRSYLA 817

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2305 AATVIQatfrmhgaYMRYQHLKRASVVIQVhtaaelqRQKHAAVILQAAVRGMKTRSHLKTMHSSATLIQSQFRAFIVRR 2384
Cdd:COG5022  818 CIIKLQ--------KTIKREKKLRETEEVE-------FSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAER 882


                 ....*....
gi 87298845 2385 RFIALRKAA 2393
Cdd:COG5022  883 QLQELKIDV 891
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
1593-1739 7.81e-05

Myosin heavy chain [General function prediction only];


The actual alignment was detected with superfamily member COG5022:

Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.54  E-value: 7.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1593 VLASYQKTRS-----SVIVLQSACRGMQARKAFRHALASVIKIQSYYRAYICRKTFQNFK--NATIKLQSIVKMKQSRKQ 1665
Cdd:COG5022  732 VLAALEDMRDakldnIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELkwRLFIKLQPLLSLLGSRKE 811

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 87298845 1666 YLQIRAAALFIQRWYRSQKLASQKRKEYIQVRESCIKlQSHFRGCLVRKQLRLQCKAAISLQSYFRMRTARQRY 1739
Cdd:COG5022  812 YRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLI-QKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL 884
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
1915-2046 6.18e-04

Myosin heavy chain [General function prediction only];


The actual alignment was detected with superfamily member COG5022:

Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.84  E-value: 6.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1915 LRHAALVFQAAWKGKMLRRQIARQHQCAALIQSY-----YRMHIQRRKWSimkTAALQIQLCYRAYkvgkEQRHLYLKTK 1989
Cdd:COG5022  744 LDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIqhgfrLRRLVDYELKW---RLFIKLQPLLSLL----GSRKEYRSYL 816

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1990 AAVVTLQ-SAYRGMKVRKRVAEC--HKAAVTIQSKFRAYRTQKKYTTYRTSAIVIQRWYR 2046
Cdd:COG5022  817 ACIIKLQkTIKREKKLRETEEVEfsLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQR 876
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
1696-1887 1.34e-03

Myosin heavy chain [General function prediction only];


The actual alignment was detected with superfamily member COG5022:

Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1696 VRESCIKLQSHFRGCLVRKQ-LRLQC--KAAISLQSYFRMRTARQRYLKMcKAALVIQSFYCAYraqiSQRKNFLQVKRA 1772
Cdd:COG5022  744 LDNIATRIQRAIRGRYLRRRyLQALKriKKIQVIQHGFRLRRLVDYELKW-RLFIKLQPLLSLL----GSRKEYRSYLAC 818

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1773 AICLQaayrgCKVRRQIKQQSTAAVtiqrvfrghsqrmkyQTMLQSAVKIQRWYRAQKVaydmRIQFLKTREAVVCLQSA 1852
Cdd:COG5022  819 IIKLQ-----KTIKREKKLRETEEV---------------EFSLKAEVLIQKFGRSLKA----KKRFSLLKKETIYLQSA 874

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 87298845 1853 YRGWQVRQQLRRQHEAAVKIQStfrmaVAQQQYKL 1887
Cdd:COG5022  875 QRVELAERQLQELKIDVKSISS-----LKLVNLEL 904
 
Name Accession Description Interval E-value
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 1081-1229 9.45e-67

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


Pssm-ID: 409073 [Multi-domain]  Cd Length: 138  Bit Score: 222.18  E-value: 9.45e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1081 VQLLMDWVNAVCAFYNKKVENFTVSFSDGRILCYLIHHYHPCYVPFDAICQRTSQSVACAQTGSVVLNSSSESeggcldl 1160
Cdd:cd21224    2 LSLLLKWCQAVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQTVDRAQDEAEDFWVAEFS------- 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 87298845 1161 slealDHESTPEMYKELLENEKKNFHLVRSAARDLGGIPAMIHHSDMSNTIPDEKVVITYLSFLCARLL 1229
Cdd:cd21224   75 -----PSTGDSGLSSELLANEKRNFKLVQQAVAELGGVPALLRASDMSNTIPDEKVVILFLSYLCARLL 138
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 908-1020 1.97e-54

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: 185.87  E-value: 1.97e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  908 LSRHLSFLGLPVSHVQTPLDEFDFAVTNLAVDLQCGVRLVRTVELLTQNWNLSDKLRIPAISRVQKMHNVDLVLQVLKSR 987
Cdd:cd21223    1 LTRHLGYLGYVLSHVQTPLDEFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQKLHNVEVALKALKEA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 87298845  988 GVpLTDEHGSAISSKDVVDRHREKTLGLLWKIA 1020
Cdd:cd21223   81 GV-LRGGDGGGITAKDIVDGHREKTLALLWRII 112
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 29-126 4.01e-38

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 138.95  E-value: 4.01e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845     29 PVLLLSHFCGVPFLCFGDVRVGTSRTRSLVLHNPHEEPLQVELSLLRAAGQGFSVAPNRCELKPKEKLTISVTWTPLREG 108
Cdd:pfam15780    1 PVLLLAPFSRQPFVCFGDVPVGTSAERLLTVVNPSEEPAEVKVSKVPAPTKGFSVSPLEFTVQPGESQTLTVTWTPTEEG 80

                           90
                   ....*....|....*...
gi 87298845    109 GVREIVTFLVNDFLKHQA 126
Cdd:pfam15780   81 AVRETLQFTVNDVGKHQV 98
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1236-1419 2.27e-09

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 63.56  E-value: 2.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1236 RAARLIQTTWRKYKLKRDLKHHQERDKAARVIQSvvlNFLSRRRLQ--KNVSAALVIQKCWR----------RVSAQRKL 1303
Cdd:COG5022  746 NIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQH---GFRLRRLVDyeLKWRLFIKLQPLLSllgsrkeyrsYLACIIKL 822

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1304 -RMLKNEKLA------KLQNKSAVLIQAYWRRYSTRKRFLRLKHYSVILQSRIRMKIALTSYKRYLWATVTIQRhwRAYL 1376
Cdd:COG5022  823 qKTIKREKKLreteevEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS--LKLV 900

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 87298845 1377 SRKRDQQIFRKLK--SSSLVIQFMFR-----RWKRRKLQLQTKAAVTLQR 1419
Cdd:COG5022  901 NLELESEIIELKKslSSDLIENLEFKteliaRLKKLLNNIDLEEGPSIEY 950
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2103-2290 6.96e-08

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 58.94  E-value: 6.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2103 RYLKMRTAALIIQVRYRAYYLGKiqheKYLRTLKAIKTLQAGVRGARVRRtVRKMHF---AATLIQSHFRGHRQQTYFHR 2179
Cdd:COG5022  740 RDAKLDNIATRIQRAIRGRYLRR----RYLQALKRIKKIQVIQHGFRLRR-LVDYELkwrLFIKLQPLLSLLGSRKEYRS 814

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2180 LRKAATMVQqrYRAVKEgsaefqrysrlrrsvlliqaafRGLRTRRHLKAMHLAATLIQRRFRTFAMRRKFLSLRKTAIW 2259
Cdd:COG5022  815 YLACIIKLQ--KTIKRE----------------------KKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIY 870

                        170       180       190
                 ....*....|....*....|....*....|.
gi 87298845 2260 IQRQYRARLYAKYSRQqllLEKAVIKIQSSY 2290
Cdd:COG5022  871 LQSAQRVELAERQLQE---LKIDVKSISSLK 898
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 1082-1132 1.24e-07

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: 52.29  E-value: 1.24e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 87298845   1082 QLLMDWVNAVCAFY--NKKVENFTVSFSDGRILCYLIHHYHPCYVPFDAICQR 1132
Cdd:pfam00307    5 KELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS 57
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 1084-1224 2.54e-07

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: 51.16  E-value: 2.54e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845    1084 LMDWVNAVCAFYNK-KVENFTVSFSDGRILCYLIHHYHPCYVPFDAICQRTSQsvacaqtgsvvlnssseseggcldlsl 1162
Cdd:smart00033    3 LLRWVNSLLAEYDKpPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSR--------------------------- 55

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 87298845    1163 ealdhestpemykellENEKKNFHLVRSAARDLGGIPAMIHHSDMSNTIPDEKVVITYLSFL 1224
Cdd:smart00033   56 ----------------FKKIENINLALSFAEKLGGKVVLFEPEDLVEGPKLILGVIWTLISL 101
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2225-2393 5.20e-07

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 55.85  E-value: 5.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2225 RHLKAMHLAATLIQRRFRTFAMRRKFLSLRKTAIWIQRQYRARLYAKYSRQQLLLeKAVIKIQSSYRGWVVRKRVQKMHR 2304
Cdd:COG5022  739 MRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKW-RLFIKLQPLLSLLGSRKEYRSYLA 817

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2305 AATVIQatfrmhgaYMRYQHLKRASVVIQVhtaaelqRQKHAAVILQAAVRGMKTRSHLKTMHSSATLIQSQFRAFIVRR 2384
Cdd:COG5022  818 CIIKLQ--------KTIKREKKLRETEEVE-------FSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAER 882


                 ....*....
gi 87298845 2385 RFIALRKAA 2393
Cdd:COG5022  883 QLQELKIDV 891
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
933-1121 5.89e-05

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 48.78  E-value: 5.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLtQNWNLSDKLRIPAiSRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHREKT 1012
Cdd:COG5069   30 FGDLDTDLKDGVKLAQLLEAL-QKDNAGEYNETPE-TRIHVMENVSGRLEFIKGKGVKLFN-----IGPQDIVDGNPKLI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1013 LGLLWKIALafqvdiSLNLDQLKEEIDFLKHTHSIkramsaLTCpsqaitnkqrdKRISGNFerygdsvqllmdwVNAVc 1092
Cdd:COG5069  103 LGLIWSLIS------RLTIATINEEGELTKHINLL------LWC-----------DEDTGGY-------------KPEV- 145

                        170       180
                 ....*....|....*....|....*....
gi 87298845 1093 afynkKVENFTVSFSDGRILCYLIHHYHP 1121
Cdd:COG5069  146 -----DTFDFFRSWRDGLAFSALIHDSRP 169
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1593-1739 7.81e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.54  E-value: 7.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1593 VLASYQKTRS-----SVIVLQSACRGMQARKAFRHALASVIKIQSYYRAYICRKTFQNFK--NATIKLQSIVKMKQSRKQ 1665
Cdd:COG5022  732 VLAALEDMRDakldnIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELkwRLFIKLQPLLSLLGSRKE 811

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 87298845 1666 YLQIRAAALFIQRWYRSQKLASQKRKEYIQVRESCIKlQSHFRGCLVRKQLRLQCKAAISLQSYFRMRTARQRY 1739
Cdd:COG5022  812 YRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLI-QKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL 884
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 933-1024 1.95e-04

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: 43.04  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845    933 VTNLAVDLQCGVRLVRTVELLTQNwnlSDKLRIPAISRVQKMHNVDLVLQVL-KSRGVPLTDehgsaISSKDVVDRHREK 1011
Cdd:pfam00307   24 VTNFTTDLRDGLALCALLNKLAPG---LVDKKKLNKSEFDKLENINLALDVAeKKLGVPKVL-----IEPEDLVEGDNKS 95

                           90
                   ....*....|...
gi 87298845   1012 TLGLLWKIALAFQ 1024
Cdd:pfam00307   96 VLTYLASLFRRFQ 108
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1915-2046 6.18e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.84  E-value: 6.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1915 LRHAALVFQAAWKGKMLRRQIARQHQCAALIQSY-----YRMHIQRRKWSimkTAALQIQLCYRAYkvgkEQRHLYLKTK 1989
Cdd:COG5022  744 LDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIqhgfrLRRLVDYELKW---RLFIKLQPLLSLL----GSRKEYRSYL 816

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1990 AAVVTLQ-SAYRGMKVRKRVAEC--HKAAVTIQSKFRAYRTQKKYTTYRTSAIVIQRWYR 2046
Cdd:COG5022  817 ACIIKLQkTIKREKKLRETEEVEfsLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQR 876
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1696-1887 1.34e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1696 VRESCIKLQSHFRGCLVRKQ-LRLQC--KAAISLQSYFRMRTARQRYLKMcKAALVIQSFYCAYraqiSQRKNFLQVKRA 1772
Cdd:COG5022  744 LDNIATRIQRAIRGRYLRRRyLQALKriKKIQVIQHGFRLRRLVDYELKW-RLFIKLQPLLSLL----GSRKEYRSYLAC 818

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1773 AICLQaayrgCKVRRQIKQQSTAAVtiqrvfrghsqrmkyQTMLQSAVKIQRWYRAQKVaydmRIQFLKTREAVVCLQSA 1852
Cdd:COG5022  819 IIKLQ-----KTIKREKKLRETEEV---------------EFSLKAEVLIQKFGRSLKA----KKRFSLLKKETIYLQSA 874

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 87298845 1853 YRGWQVRQQLRRQHEAAVKIQStfrmaVAQQQYKL 1887
Cdd:COG5022  875 QRVELAERQLQELKIDVKSISS-----LKLVNLEL 904
 
Name Accession Description Interval E-value
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 1081-1229 9.45e-67

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


Pssm-ID: 409073 [Multi-domain]  Cd Length: 138  Bit Score: 222.18  E-value: 9.45e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1081 VQLLMDWVNAVCAFYNKKVENFTVSFSDGRILCYLIHHYHPCYVPFDAICQRTSQSVACAQTGSVVLNSSSESeggcldl 1160
Cdd:cd21224    2 LSLLLKWCQAVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQTVDRAQDEAEDFWVAEFS------- 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 87298845 1161 slealDHESTPEMYKELLENEKKNFHLVRSAARDLGGIPAMIHHSDMSNTIPDEKVVITYLSFLCARLL 1229
Cdd:cd21224   75 -----PSTGDSGLSSELLANEKRNFKLVQQAVAELGGVPALLRASDMSNTIPDEKVVILFLSYLCARLL 138
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 908-1020 1.97e-54

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: 185.87  E-value: 1.97e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  908 LSRHLSFLGLPVSHVQTPLDEFDFAVTNLAVDLQCGVRLVRTVELLTQNWNLSDKLRIPAISRVQKMHNVDLVLQVLKSR 987
Cdd:cd21223    1 LTRHLGYLGYVLSHVQTPLDEFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQKLHNVEVALKALKEA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 87298845  988 GVpLTDEHGSAISSKDVVDRHREKTLGLLWKIA 1020
Cdd:cd21223   81 GV-LRGGDGGGITAKDIVDGHREKTLALLWRII 112
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 29-126 4.01e-38

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 138.95  E-value: 4.01e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845     29 PVLLLSHFCGVPFLCFGDVRVGTSRTRSLVLHNPHEEPLQVELSLLRAAGQGFSVAPNRCELKPKEKLTISVTWTPLREG 108
Cdd:pfam15780    1 PVLLLAPFSRQPFVCFGDVPVGTSAERLLTVVNPSEEPAEVKVSKVPAPTKGFSVSPLEFTVQPGESQTLTVTWTPTEEG 80

                           90
                   ....*....|....*...
gi 87298845    109 GVREIVTFLVNDFLKHQA 126
Cdd:pfam15780   81 AVRETLQFTVNDVGKHQV 98
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 922-1023 2.63e-12

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: 65.50  E-value: 2.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  922 VQTPLDEFDFAVTNLAVDLQCGVRLVRTVELLTQN----WNLSDKLRipaisrVQKMHNVDLVLQVLKSRGVPLTDehgs 997
Cdd:cd21215   13 LNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDEslgrYNKNPKMR------VQKLENVNKALEFIKSRGVKLTN---- 82

                         90       100
                 ....*....|....*....|....*.
gi 87298845  998 aISSKDVVDRHREKTLGLLWKIALAF 1023
Cdd:cd21215   83 -IGAEDIVDGNLKLILGLLWTLILRF 107
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 933-1025 3.93e-12

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: 65.10  E-value: 3.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQNWNLSDKLRipaiSRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHREKT 1012
Cdd:cd21186   23 IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGR----MRVHHLNNVNRALQVLEQNNVKLVN-----ISSNDIVDGNPKLT 93

                         90
                 ....*....|...
gi 87298845 1013 LGLLWKIALAFQV 1025
Cdd:cd21186   94 LGLVWSIILHWQV 106
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 926-1021 9.32e-10

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: 58.46  E-value: 9.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  926 LDEFDFAVTNLAVDLQCGVRLVRTVELLTqnwnlSDKLRIPA--ISRVQKMHNVDLVLQVLKSRgVPLtdehgSAISSKD 1003
Cdd:cd21193   29 LEKANLEIGDLFTDLSDGKLLLKLLEIIS-----GEKLGKPNrgRLRVQKIENVNKALAFLKTK-VRL-----ENIGAED 97

                         90
                 ....*....|....*...
gi 87298845 1004 VVDRHREKTLGLLWKIAL 1021
Cdd:cd21193   98 IVDGNPRLILGLIWTIIL 115
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1236-1419 2.27e-09

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 63.56  E-value: 2.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1236 RAARLIQTTWRKYKLKRDLKHHQERDKAARVIQSvvlNFLSRRRLQ--KNVSAALVIQKCWR----------RVSAQRKL 1303
Cdd:COG5022  746 NIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQH---GFRLRRLVDyeLKWRLFIKLQPLLSllgsrkeyrsYLACIIKL 822

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1304 -RMLKNEKLA------KLQNKSAVLIQAYWRRYSTRKRFLRLKHYSVILQSRIRMKIALTSYKRYLWATVTIQRhwRAYL 1376
Cdd:COG5022  823 qKTIKREKKLreteevEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS--LKLV 900

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 87298845 1377 SRKRDQQIFRKLK--SSSLVIQFMFR-----RWKRRKLQLQTKAAVTLQR 1419
Cdd:COG5022  901 NLELESEIIELKKslSSDLIENLEFKteliaRLKKLLNNIDLEEGPSIEY 950
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 926-1025 6.96e-09

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: 55.76  E-value: 6.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  926 LDEFDFAVTNLAVDLQCGVRLVRTVELLtQNWNLSDKLRIPaISRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVV 1005
Cdd:cd21227   17 LKPTGMSVEDLATDLEDGVKLIALVEIL-QGRKLGRVIKKP-LNQHQKLENVTLALKAMAEDGIKLVN-----IGNEDIV 89

                         90       100
                 ....*....|....*....|
gi 87298845 1006 DRHREKTLGLLWKIALAFQV 1025
Cdd:cd21227   90 NGNLKLILGLIWHLILRYQI 109
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 1080-1222 1.41e-08

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: 55.05  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1080 SVQLLMDWVNAVCAFYNK-KVENFTVSFSDGRILCYLIHHYHPCYVPFDAicqrtsqsvacaqtgsvvlnssseseggcl 1158
Cdd:cd21253    2 GIKALQQWCRQQTEGYRDvKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDS------------------------------ 51

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 87298845 1159 dLSLEaldhestpemykELLENEKKNFhlvRSAARDLgGIPAMIHHSDM-SNTIPDEKVVITYLS 1222
Cdd:cd21253   52 -LSKE------------NVYENNKLAF---TVAEKEL-GIPALLDAEDMvALKVPDKLSILTYVS 99
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 1080-1224 2.04e-08

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: 54.41  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1080 SVQLLMDWVNAVCAFYNK-KVENFTVSFSDGRILCYLIHHYHPCYVPFDaicqrtsqsvacaqtgsvvlnssseseggcl 1158
Cdd:cd21255    2 SSQSLLEWCQEVTAGYRGvRVTNFTTSWRNGLAFCAILHHFHPDLVDYE------------------------------- 50

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 87298845 1159 dlSLEALDHEstpemykellENEKKNFhlvrSAARDLgGIPAMIHHSDMS-NTIPDEKVVITYLSFL 1224
Cdd:cd21255   51 --SLDPLDIK----------ENNKKAF----EAFASL-GVPRLLEPADMVlLPIPDKLIVMTYLCQL 100
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1303-1451 3.03e-08

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 60.09  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1303 LRMLKNEKLAKLQNkSAVLIQAYWRRYSTRKRFLRLKHYSVILQSRIRMKIALTSYKRYLW--ATVTIQRHWRAYLSRKR 1380
Cdd:COG5022  733 LAALEDMRDAKLDN-IATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKwrLFIKLQPLLSLLGSRKE 811

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1381 dqqiFRKLKSSSLVIQFMFRRWKRRKLQLQT----KAAVTLQRAFREWHLRKQIR--ERSAVVIQSWYRM---HRELQKY 1451
Cdd:COG5022  812 ----YRSYLACIIKLQKTIKREKKLRETEEVefslKAEVLIQKFGRSLKAKKRFSllKKETIYLQSAQRVelaERQLQEL 887
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 1082-1228 6.31e-08

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: 53.12  E-value: 6.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1082 QLLMDWVNAVCAFY-NKKVENFTVSFSDGRILCYLIHHYHPcyvpfdaicqrtsqsvacaqtgsvvlnssseseggcldl 1160
Cdd:cd21200    4 QMLLEWCQAKTRGYeHVDITNFSSSWSDGMAFCALIHHFFP--------------------------------------- 44

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 87298845 1161 slEALDHES-TPemykellENEKKNFHLVRSAARDLGGIPAMIHHSDM--SNTIPDEKVVITYLSFLCARL 1228
Cdd:cd21200   45 --DAFDYSSlDP-------KNRRKNFELAFSTAEELADIAPLLEVEDMvrMGNRPDWKCVFTYVQSLYRHL 106
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2103-2290 6.96e-08

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 58.94  E-value: 6.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2103 RYLKMRTAALIIQVRYRAYYLGKiqheKYLRTLKAIKTLQAGVRGARVRRtVRKMHF---AATLIQSHFRGHRQQTYFHR 2179
Cdd:COG5022  740 RDAKLDNIATRIQRAIRGRYLRR----RYLQALKRIKKIQVIQHGFRLRR-LVDYELkwrLFIKLQPLLSLLGSRKEYRS 814

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2180 LRKAATMVQqrYRAVKEgsaefqrysrlrrsvlliqaafRGLRTRRHLKAMHLAATLIQRRFRTFAMRRKFLSLRKTAIW 2259
Cdd:COG5022  815 YLACIIKLQ--KTIKRE----------------------KKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIY 870

                        170       180       190
                 ....*....|....*....|....*....|.
gi 87298845 2260 IQRQYRARLYAKYSRQqllLEKAVIKIQSSY 2290
Cdd:COG5022  871 LQSAQRVELAERQLQE---LKIDVKSISSLK 898
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 1082-1222 1.04e-07

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


Pssm-ID: 409033  Cd Length: 103  Bit Score: 52.24  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1082 QLLMDWVNAVCAfyNKKVENFTVSFSDGRILCYLIHHYHPcyvpfdaicqrtsqsvacaqtGSVVLNSSSEseggcldls 1161
Cdd:cd21184    4 SLLLEWVNSKIP--EYKVKNFTTDWNDGKALAALVDALKP---------------------GLIPDNESLD--------- 51

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 87298845 1162 lealdhESTPemykelLENEKKNFhlvrSAARDLGGIPAMIHHSDMSNTIPDEKVVITYLS 1222
Cdd:cd21184   52 ------KENP------LENATKAM----DIAEEELGIPKIITPEDMVSPNVDELSVMTYLS 96
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 1082-1132 1.24e-07

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: 52.29  E-value: 1.24e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 87298845   1082 QLLMDWVNAVCAFY--NKKVENFTVSFSDGRILCYLIHHYHPCYVPFDAICQR 1132
Cdd:pfam00307    5 KELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS 57
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 933-1025 2.37e-07

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: 51.46  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQNWNLSDKlripAISRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHREKT 1012
Cdd:cd21231   27 IEDLFTDLQDGRRLLELLEGLTGQKLVKEK----GSTRVHALNNVNKALQVLQKNNVDLVN-----IGSADIVDGNHKLT 97

                         90
                 ....*....|...
gi 87298845 1013 LGLLWKIALAFQV 1025
Cdd:cd21231   98 LGLIWSIILHWQV 110
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 1084-1224 2.54e-07

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: 51.16  E-value: 2.54e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845    1084 LMDWVNAVCAFYNK-KVENFTVSFSDGRILCYLIHHYHPCYVPFDAICQRTSQsvacaqtgsvvlnssseseggcldlsl 1162
Cdd:smart00033    3 LLRWVNSLLAEYDKpPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSR--------------------------- 55

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 87298845    1163 ealdhestpemykellENEKKNFHLVRSAARDLGGIPAMIHHSDMSNTIPDEKVVITYLSFL 1224
Cdd:smart00033   56 ----------------FKKIENINLALSFAEKLGGKVVLFEPEDLVEGPKLILGVIWTLISL 101
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 933-1024 3.28e-07

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: 50.86  E-value: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQnwnlsDKL-RIPAISRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHREK 1011
Cdd:cd21188   23 VVDLFEDLRDGHNLISLLEVLSG-----ESLpRERGRMRFHRLQNVQTALDFLKYRKIKLVN-----IRAEDIVDGNPKL 92

                         90
                 ....*....|...
gi 87298845 1012 TLGLLWKIALAFQ 1024
Cdd:cd21188   93 TLGLIWTIILHFQ 105
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2225-2393 5.20e-07

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 55.85  E-value: 5.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2225 RHLKAMHLAATLIQRRFRTFAMRRKFLSLRKTAIWIQRQYRARLYAKYSRQQLLLeKAVIKIQSSYRGWVVRKRVQKMHR 2304
Cdd:COG5022  739 MRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKW-RLFIKLQPLLSLLGSRKEYRSYLA 817

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2305 AATVIQatfrmhgaYMRYQHLKRASVVIQVhtaaelqRQKHAAVILQAAVRGMKTRSHLKTMHSSATLIQSQFRAFIVRR 2384
Cdd:COG5022  818 CIIKLQ--------KTIKREKKLRETEEVE-------FSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAER 882


                 ....*....
gi 87298845 2385 RFIALRKAA 2393
Cdd:COG5022  883 QLQELKIDV 891
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 1080-1221 9.06e-07

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: 49.73  E-value: 9.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1080 SVQLLMDWVNAVCAFY-NKKVENFTVSFSDGRILCYLIHHYHPCYVPFDaicqrtsqsvacaqtgsvvlnssseseggcl 1158
Cdd:cd21198    2 SGQDLLEWCQEVTKGYrGVKITNLTTSWRNGLAFCAILHHFRPDLIDFS------------------------------- 50

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 87298845 1159 dlSLEALDhestpemykeLLENEKKNFhlvrSAARDLgGIPAMIHHSDM-SNTIPDEKVVITYL 1221
Cdd:cd21198   51 --SLSPHD----------IKENCKLAF----DAAAKL-GIPRLLDPADMvLLSVPDKLSVMTYL 97
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 933-1021 1.74e-06

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: 49.29  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTqnwnlSDKLRIPAIS--RVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHRE 1010
Cdd:cd21246   36 INDLYTDLRDGRMLIKLLEVLS-----GERLPKPTKGkmRIHCLENVDKALQFLKEQRVHLEN-----MGSHDIVDGNHR 105

                         90
                 ....*....|.
gi 87298845 1011 KTLGLLWKIAL 1021
Cdd:cd21246  106 LTLGLIWTIIL 116
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 932-1025 2.08e-06

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: 49.11  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  932 AVTNLAVDLQCGVRLVRTVELLTqNWNLSDKLRiPAISRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHREK 1011
Cdd:cd21191   26 EVKDLFVDIQDGKILMALLEVLS-GQNLLQEYK-PSSHRIFRLNNIAKALKFLEDSNVKLVS-----IDAAEIADGNPSL 98

                         90
                 ....*....|....
gi 87298845 1012 TLGLLWKIALAFQV 1025
Cdd:cd21191   99 VLGLIWNIILFFQI 112
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 933-1025 2.50e-06

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: 48.47  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQNWNLSDKlripAISRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHREKT 1012
Cdd:cd21232   23 IKDMFTDLRDGRKLLDLLEGLTGKSLPKER----GSTRVHALNNVNRVLQVLHQNNVELVN-----IGGTDIVDGNHKLT 93

                         90
                 ....*....|...
gi 87298845 1013 LGLLWKIALAFQV 1025
Cdd:cd21232   94 LGLLWSIILHWQV 106
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 1084-1222 3.87e-06

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: 48.13  E-value: 3.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1084 LMDWVNAVCAFY-NKKVENFTVSFSDGRILCYLIHHYHPcyvpfdaicqrtsqsvacaqtgsvvlnssseseggclDLsl 1162
Cdd:cd21216   15 LLLWCQRKTAPYkNVNVQNFHTSWKDGLAFCALIHRHRP-------------------------------------DL-- 55

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 87298845 1163 eaLDHESTPEmykellENEKKNFHLVRSAARDLGGIPAMIHHSDMSNTI-PDEKVVITYLS 1222
Cdd:cd21216   56 --LDYDKLRK------DDPRENLNLAFDVAEKHLDIPKMLDAEDIVNTPrPDERSVMTYVS 108
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 1084-1222 4.13e-06

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: 47.67  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1084 LMDWVNAVCAFY-NKKVENFTVSFSDGRILCYLIHHYHPCYVPFDaicqrtsqsvacaqtgsvvlnssseseggcldlsl 1162
Cdd:cd22198    5 LLSWCQEQTEGYrGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFS----------------------------------- 49

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 87298845 1163 eALDHEstpemykELLENEKKNFHLvrsAARDLgGIPAMIHHSDMSN-TIPDEKVVITYLS 1222
Cdd:cd22198   50 -SLDPE-------NIAENNQLAFDV---AEQEL-GIPPVMTGQEMASlAVPDKLSMVSYLS 98
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 933-1016 4.99e-06

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: 47.58  E-value: 4.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTqNWNLSDKLRIPAIsRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHREKT 1012
Cdd:cd21212   22 ITDLQKDLGDGLTLVNLIEAVA-GEKVPGIHSRPKT-RAQKLENIQACLQFLAALGVDVQG-----ITAEDIVDGNLKAI 94


                 ....
gi 87298845 1013 LGLL 1016
Cdd:cd21212   95 LGLF 98
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 932-1021 8.21e-06

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: 47.00  E-value: 8.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  932 AVTNLAVDLQCGVRLVRTVELLT-QNWNLSDKLRIpaisRVQKMHNVDLVLQVLKSRGVPLtdehgSAISSKDVVDRHRE 1010
Cdd:cd21214   24 QIENIEEDFRDGLKLMLLLEVISgERLPKPERGKM----RFHKIANVNKALDFIASKGVKL-----VSIGAEEIVDGNLK 94

                         90
                 ....*....|.
gi 87298845 1011 KTLGLLWKIAL 1021
Cdd:cd21214   95 MTLGMIWTIIL 105
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 1084-1224 9.83e-06

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: 46.56  E-value: 9.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1084 LMDWVNAVCAFYNK-KVENFTVSFSDGRILCYLIHHYHPCYVPFDAICQRTSqsvacaqtgsvvlnssseseggcldlsl 1162
Cdd:cd00014    4 LLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSP---------------------------- 55

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87298845 1163 ealdhestpemykellENEKKNFHLVRSAARDLG-GIPAMIHHSDMSNTiPDEKVVITYLSFL 1224
Cdd:cd00014   56 ----------------FKKRENINLFLNACKKLGlPELDLFEPEDLYEK-GNLKKVLGTLWAL 101
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 922-1021 1.15e-05

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: 47.71  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  922 VQTPLDEFDFAVTNLAVDLQCGVRLVRTVELLTqnwnlSDKLRIPAISR--VQKMHNVDLVLQVLKSRGVpltdeHGSAI 999
Cdd:cd21318   47 VNSHLARVPCRINDLYTDLRDGYVLTRLLEVLS-----GEQLPKPTRGRmrIHSLENVDKALQFLKEQRV-----HLENV 116

                         90       100
                 ....*....|....*....|..
gi 87298845 1000 SSKDVVDRHREKTLGLLWKIAL 1021
Cdd:cd21318  117 GSHDIVDGNHRLTLGLIWTIIL 138
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 933-1026 1.21e-05

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: 46.60  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTqnwnlSDKLRIPAISRVQKMH---NVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHR 1009
Cdd:cd21241   27 VEDLFEDIKDGTKLLALLEVLS-----GEKLPCEKGRRLKRVHflsNINTALKFLESKKIKLVN-----INPTDIVDGKP 96

                         90
                 ....*....|....*..
gi 87298845 1010 EKTLGLLWKIALAFQVD 1026
Cdd:cd21241   97 SIVLGLIWTIILYFQIE 113
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 927-1021 1.27e-05

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: 46.56  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  927 DEFDFAVTNLAVDLQCGVRLVRTVELLTQNwnLSDKLRIPAISRVQKMHNVDLVLQVLKSRGVPLTDehgsAISSKDVVD 1006
Cdd:cd00014   14 EELPVSITDLFESLRDGVLLCKLINKLSPG--SIPKINKKPKSPFKKRENINLFLNACKKLGLPELD----LFEPEDLYE 87

                         90
                 ....*....|....*.
gi 87298845 1007 RHREK-TLGLLWKIAL 1021
Cdd:cd00014   88 KGNLKkVLGTLWALAL 103
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 1080-1222 1.33e-05

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: 46.38  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1080 SVQLLMDWVNAVCAFY-NKKVENFTVSFSDGRILCYLIHHYHPCYVPFDaicqrtsqsvacaqtgsvvlnssseseggcl 1158
Cdd:cd21197    1 KIQALLRWCRRQCEGYpGVNITNLTSSFRDGLAFCAILHRHRPELIDFH------------------------------- 49

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 87298845 1159 dlsleALDHEStpemykeLLENEKKNFhlvRSAARDLgGIPAMIHHSDM-SNTIPDEKVVITYLS 1222
Cdd:cd21197   50 -----SLKKDN-------WLENNRLAF---RVAETSL-GIPALLDAEDMvTMHVPDRLSIITYVS 98
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 933-1021 1.47e-05

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: 46.97  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTqnwnlSDKLRIPAISR--VQKMHNVDLVLQVLKSRGVpltdeHGSAISSKDVVDRHRE 1010
Cdd:cd21317   51 IGDLYTDLRDGRMLIRLLEVLS-----GEQLPKPTKGRmrIHCLENVDKALQFLKEQKV-----HLENMGSHDIVDGNHR 120

                         90
                 ....*....|.
gi 87298845 1011 KTLGLLWKIAL 1021
Cdd:cd21317  121 LTLGLIWTIIL 131
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 933-1025 1.70e-05

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: 46.90  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQNWNLSDKLRIpaisRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHREKT 1012
Cdd:cd21236   37 VNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM----RFHRLQNVQIALDYLKRRQVKLVN-----IRNDDITDGNPKLT 107

                         90
                 ....*....|...
gi 87298845 1013 LGLLWKIALAFQV 1025
Cdd:cd21236  108 LGLIWTIILHFQI 120
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 1082-1221 1.86e-05

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: 46.14  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1082 QLLMDWVNAVCAFY-NKKVENFTVSFSDGRILCYLIHHYHPcyvpfdaicqrtsqsvacaqtgsvvlnssseseggcldl 1160
Cdd:cd21259    4 QMLLDWCRAKTRGYeNVDIQNFSSSWSDGMAFCALVHNFFP--------------------------------------- 44

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87298845 1161 slEALDHES-TPemykellENEKKNFHLVRSAARDLGGIPAMIHHSDMSNTI-PDEKVVITYL 1221
Cdd:cd21259   45 --EAFDYSQlSP-------QNRRHNFEVAFSSAEKHADCPQLLDVEDMVRMRePDWKCVYTYI 98
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 933-1025 1.94e-05

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: 46.56  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQNWNLSDKLRIpaisRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHREKT 1012
Cdd:cd21235   26 ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQVKLVN-----IRNDDIADGNPKLT 96

                         90
                 ....*....|...
gi 87298845 1013 LGLLWKIALAFQV 1025
Cdd:cd21235   97 LGLIWTIILHFQI 109
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 1099-1138 2.39e-05

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 44.98  E-value: 2.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 87298845   1099 VENFTVSFSDGRILCYLIHHYHPCYVPFDAICQRTSQSVA 1138
Cdd:pfam11971   13 VEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLA 52
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 933-1026 2.43e-05

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: 46.02  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTqnwnlSDKLRIPAISRVQKMH---NVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHR 1009
Cdd:cd21190   27 INDLFVDIKDGTALLRLLEVLS-----GQKLPIESGRVLQRAHklsNIRNALDFLTKRCIKLVN-----INSTDIVDGKP 96

                         90
                 ....*....|....*..
gi 87298845 1010 EKTLGLLWKIALAFQVD 1026
Cdd:cd21190   97 SIVLGLIWTIILYFQIE 113
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
 1082-1224 4.03e-05

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: 45.42  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1082 QLLMDWVNAVCAFY-NKKVENFTVSFSDGRILCYLIHHYHPcyvpfdaicqrtsqsvacaqtgsvvlnssseseggcldl 1160
Cdd:cd21258    4 QMLLDWCRAKTRGYeHVDIQNFSSSWSDGMAFCALVHNFFP--------------------------------------- 44

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 87298845 1161 slEALDHES-TPemykellENEKKNFHLVRSAARDLGGIPAMIHHSDM--SNTIPDEKVVITYLSFL 1224
Cdd:cd21258   45 --DAFDYSQlSP-------QNRRQNFEVAFSAAEMLADCVPLVEVEDMmiMGKKPDSKCVFTYVQSL 102
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 933-1025 5.48e-05

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: 45.14  E-value: 5.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQNwnlsdklRIPAIS-----RVQKMHNVDLVLQVLKS-RGVPLTDehgsaISSKDVVD 1006
Cdd:cd21311   35 IADLETDLSDGLRLIALVEVLSGK-------KFPKFNkrptfRSQKLENVSVALKFLEEdEGIKIVN-----IDSSDIVD 102

                         90
                 ....*....|....*....
gi 87298845 1007 RHREKTLGLLWKIALAFQV 1025
Cdd:cd21311  103 GKLKLILGLIWTLILHYSI 121
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
933-1121 5.89e-05

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 48.78  E-value: 5.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLtQNWNLSDKLRIPAiSRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHREKT 1012
Cdd:COG5069   30 FGDLDTDLKDGVKLAQLLEAL-QKDNAGEYNETPE-TRIHVMENVSGRLEFIKGKGVKLFN-----IGPQDIVDGNPKLI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1013 LGLLWKIALafqvdiSLNLDQLKEEIDFLKHTHSIkramsaLTCpsqaitnkqrdKRISGNFerygdsvqllmdwVNAVc 1092
Cdd:COG5069  103 LGLIWSLIS------RLTIATINEEGELTKHINLL------LWC-----------DEDTGGY-------------KPEV- 145

                        170       180
                 ....*....|....*....|....*....
gi 87298845 1093 afynkKVENFTVSFSDGRILCYLIHHYHP 1121
Cdd:COG5069  146 -----DTFDFFRSWRDGLAFSALIHDSRP 169
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1593-1739 7.81e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.54  E-value: 7.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1593 VLASYQKTRS-----SVIVLQSACRGMQARKAFRHALASVIKIQSYYRAYICRKTFQNFK--NATIKLQSIVKMKQSRKQ 1665
Cdd:COG5022  732 VLAALEDMRDakldnIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELkwRLFIKLQPLLSLLGSRKE 811

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 87298845 1666 YLQIRAAALFIQRWYRSQKLASQKRKEYIQVRESCIKlQSHFRGCLVRKQLRLQCKAAISLQSYFRMRTARQRY 1739
Cdd:COG5022  812 YRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLI-QKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL 884
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 1082-1121 8.72e-05

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 44.21  E-value: 8.72e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 87298845 1082 QLLMDWVNAVCAFYN---KKVENFTVSFSDGRILCYLIHHYHP 1121
Cdd:cd21218   13 EILLRWVNYHLKKAGptkKRVTNFSSDLKDGEVYALLLHSLAP 55
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 933-1023 1.30e-04

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: 43.63  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQNWNLSDKLRIPAIsRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHREKT 1012
Cdd:cd21228   24 IYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRPTF-RQMKLENVSVALEFLERESIKLVS-----IDSSAIVDGNLKLI 97

                         90
                 ....*....|.
gi 87298845 1013 LGLLWKIALAF 1023
Cdd:cd21228   98 LGLIWTLILHY 108
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 933-1024 1.95e-04

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: 43.04  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845    933 VTNLAVDLQCGVRLVRTVELLTQNwnlSDKLRIPAISRVQKMHNVDLVLQVL-KSRGVPLTDehgsaISSKDVVDRHREK 1011
Cdd:pfam00307   24 VTNFTTDLRDGLALCALLNKLAPG---LVDKKKLNKSEFDKLENINLALDVAeKKLGVPKVL-----IEPEDLVEGDNKS 95

                           90
                   ....*....|...
gi 87298845   1012 TLGLLWKIALAFQ 1024
Cdd:pfam00307   96 VLTYLASLFRRFQ 108
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 1082-1221 2.28e-04

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: 42.92  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1082 QLLMDWVNAVCAFYNK-KVENFTVSFSDGRILCYLIHHYHPCYVPFDAIcqrtsqsvacaqtgsvvlnssseseggcldl 1160
Cdd:cd21254    4 QSLLAWCKEVTKGYRGvKITNFTTSWRNGLAFCAILHHFRPDLIDYKSL------------------------------- 52

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 87298845 1161 slealdhesTPEMYKellENEKKNFHLVRSAardlgGIPAMIHHSDMSN-TIPDEKVVITYL 1221
Cdd:cd21254   53 ---------NPHDIK---ENNKKAYDGFASL-----GISRLLEPSDMVLlAVPDKLTVMTYL 97
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 926-1023 3.45e-04

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: 42.47  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  926 LDEFDFAVTNLAVDLQCGVRLVRTVELLTQ-----NWNlsdklRIPAIsRVQKMHNVDLVLQVLKSRGVPLTDehgsaIS 1000
Cdd:cd21183   17 LKERGMQIHDLATDFSDGLCLIALLENLSTrplkrSYN-----RRPAF-QQHYLENVSTALKFIEADHIKLVN-----IG 85

                         90       100
                 ....*....|....*....|...
gi 87298845 1001 SKDVVDRHREKTLGLLWKIALAF 1023
Cdd:cd21183   86 SGDIVNGNIKLILGLIWTLILHY 108
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2200-2521 4.03e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 46.22  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2200 EFQRYSRLRRSVLLIQAAFRGLRTR-RHLKAMHL--AATLIQRRFRTFAMRRKFLSLRKtAIWIQRQYRARLYAKYSRQq 2276
Cdd:COG5022  737 EDMRDAKLDNIATRIQRAIRGRYLRrRYLQALKRikKIQVIQHGFRLRRLVDYELKWRL-FIKLQPLLSLLGSRKEYRS- 814

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2277 llLEKAVIKIQ-SSYRGWVVRKRVQK--MHRAATVIQATFRMHGAYMRYQHLKRASVVIQvhTAAELQRQKHAAVILQAA 2353
Cdd:COG5022  815 --YLACIIKLQkTIKREKKLRETEEVefSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQ--SAQRVELAERQLQELKID 890

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2354 VRgmktrshlKTMHSSATLIQSQFRAFIVRRRFialrKAAIFVQRKFRATLYAKHKLHqflqLRKAAITIQSS--YRRLM 2431
Cdd:COG5022  891 VK--------SISSLKLVNLELESEIIELKKSL----SSDLIENLEFKTELIARLKKL----LNNIDLEEGPSieYVKLP 954

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 2432 VQKKLQE----MHRAAALIQATFRMHRTYVAFHIWKCASIRI-QQCYRTYRTIK--LQKE-KLIREEQHSAAVLIQSTYR 2503
Cdd:COG5022  955 ELNKLHEveskLKETSEEYEDLLKKSTILVREGNKANSELKNfKKELAELSKQYgaLQEStKQLKELPVEVAELQSASKI 1034

                        330
                 ....*....|....*...
gi 87298845 2504 MYRQRCFYQQRRWAAKVI 2521
Cdd:COG5022 1035 ISSESTELSILKPLQKLK 1052
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1580-1717 6.03e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.84  E-value: 6.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1580 IQTHFRASISARRvlasYQKTRSSVIVLQSACRGMQARKAFRHALAS--VIKIQSYYRAYICRKTFQNFKNATIKLQ-SI 1656
Cdd:COG5022  751 IQRAIRGRYLRRR----YLQALKRIKKIQVIQHGFRLRRLVDYELKWrlFIKLQPLLSLLGSRKEYRSYLACIIKLQkTI 826

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87298845 1657 VKMKQSRKQYLQIRA--AALFIQRWYRSqklaSQKRKEYIQVRESCIKLQSHFRGCLVRKQLR 1717
Cdd:COG5022  827 KREKKLRETEEVEFSlkAEVLIQKFGRS----LKAKKRFSLLKKETIYLQSAQRVELAERQLQ 885
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1915-2046 6.18e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.84  E-value: 6.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1915 LRHAALVFQAAWKGKMLRRQIARQHQCAALIQSY-----YRMHIQRRKWSimkTAALQIQLCYRAYkvgkEQRHLYLKTK 1989
Cdd:COG5022  744 LDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIqhgfrLRRLVDYELKW---RLFIKLQPLLSLL----GSRKEYRSYL 816

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1990 AAVVTLQ-SAYRGMKVRKRVAEC--HKAAVTIQSKFRAYRTQKKYTTYRTSAIVIQRWYR 2046
Cdd:COG5022  817 ACIIKLQkTIKREKKLRETEEVEfsLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQR 876
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 933-1033 1.17e-03

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: 41.60  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQNWNLSDKLRIPAISRVQkMHNVDLVLQVLKSRGVPLTdehgsAISSKDVVDRHREKT 1012
Cdd:cd21309   37 IGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFRQMQ-LENVSVALEFLDRESIKLV-----SIDSKAIVDGNLKLI 110

                         90       100
                 ....*....|....*....|.
gi 87298845 1013 LGLLWKIALAFQVDISLNLDQ 1033
Cdd:cd21309  111 LGLVWTLILHYSISMPVWEDE 131
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 933-1027 1.18e-03

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: 41.61  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQNWNLSDKLRIPAISRVQkMHNVDLVLQVLKSRGVPLTdehgsAISSKDVVDRHREKT 1012
Cdd:cd21308   40 IANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQ-LENVSVALEFLDRESIKLV-----SIDSKAIVDGNLKLI 113

                         90
                 ....*....|....*
gi 87298845 1013 LGLLWKIALAFQVDI 1027
Cdd:cd21308  114 LGLIWTLILHYSISM 128
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1696-1887 1.34e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1696 VRESCIKLQSHFRGCLVRKQ-LRLQC--KAAISLQSYFRMRTARQRYLKMcKAALVIQSFYCAYraqiSQRKNFLQVKRA 1772
Cdd:COG5022  744 LDNIATRIQRAIRGRYLRRRyLQALKriKKIQVIQHGFRLRRLVDYELKW-RLFIKLQPLLSLL----GSRKEYRSYLAC 818

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1773 AICLQaayrgCKVRRQIKQQSTAAVtiqrvfrghsqrmkyQTMLQSAVKIQRWYRAQKVaydmRIQFLKTREAVVCLQSA 1852
Cdd:COG5022  819 IIKLQ-----KTIKREKKLRETEEV---------------EFSLKAEVLIQKFGRSLKA----KKRFSLLKKETIYLQSA 874

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 87298845 1853 YRGWQVRQQLRRQHEAAVKIQStfrmaVAQQQYKL 1887
Cdd:COG5022  875 QRVELAERQLQELKIDVKSISS-----LKLVNLEL 904
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1267-1416 1.40e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1267 IQSVVLNFLSRRRLQKNVSAALVIQKCWRR----------VSAQRKLRMLKN----EKLAKLQNKS--AVLIQAYWRRYS 1330
Cdd:COG5022  728 FKAGVLAALEDMRDAKLDNIATRIQRAIRGrylrrrylqaLKRIKKIQVIQHgfrlRRLVDYELKWrlFIKLQPLLSLLG 807

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1331 TRKRFLRLKHYSVILQSRIRMKIALTSY---KRYLWATVTIQRHWRAYLSRKRdqqiFRKLKSSSLVIQFMFRRWKRRKL 1407
Cdd:COG5022  808 SRKEYRSYLACIIKLQKTIKREKKLRETeevEFSLKAEVLIQKFGRSLKAKKR----FSLLKKETIYLQSAQRVELAERQ 883


                 ....*....
gi 87298845 1408 QLQTKAAVT 1416
Cdd:COG5022  884 LQELKIDVK 892
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 933-1025 1.90e-03

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: 40.79  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQNWNLSDKLRIpaisRVQKMHNVDLVLQVLKSRGVPLTDehgsaISSKDVVDRHREKT 1012
Cdd:cd21237   26 INDLYEDLRDGHNLISLLEVLSGVKLPREKGRM----RFHRLQNVQIALDFLKQRQVKLVN-----IRNDDITDGNPKLT 96

                         90
                 ....*....|...
gi 87298845 1013 LGLLWKIALAFQV 1025
Cdd:cd21237   97 LGLIWTIILHFQI 109
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 933-1017 2.11e-03

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: 40.21  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQNwNLSDKLRIPAISRVQKMHNVDLVLQV----LKSRGVpltdehgsAISSKDVVDRH 1008
Cdd:cd21225   25 ISDLATDLSDGVRLIFFLELVSGK-KFPKKFDLEPKNRIQMIQNLHLAMLFieedLKIRVQ--------GIGAEDFVDNN 95


                 ....*....
gi 87298845 1009 REKTLGLLW 1017
Cdd:cd21225   96 KKLILGLLW 104
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 1077-1126 2.75e-03

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: 40.01  E-value: 2.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 87298845 1077 YGDSVQ-LLMDWVNAVCAFY-NKKVENFTVSFSDGRILCYLIHHYHPCYVPF 1126
Cdd:cd21257    5 YGGSKRnALLKWCQKKTEGYpNIDITNFSSSWSDGLAFCALLHTYLPAHIPY 56
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 933-1021 3.17e-03

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: 40.80  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTqnwnlSDKLRIPAISR--VQKMHNVDLVLQVLKSRGVpltdeHGSAISSKDVVDRHRE 1010
Cdd:cd21316   73 ITDLYMDLRDGRMLIKLLEVLS-----GERLPKPTKGRmrIHCLENVDKALQFLKEQRV-----HLENMGSHDIVDGNHR 142

                         90
                 ....*....|.
gi 87298845 1011 KTLGLLWKIAL 1021
Cdd:cd21316  143 LTLGLIWTIIL 153
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 873-1019 3.36e-03

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: 39.88  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  873 LIDHDPclfckdAEFKASKELLLAFsrdflsgegdLSRHLSFLGLPVshvqtpldefdfavTNLAVDLQCGVRLVRTVEL 952
Cdd:cd21222    6 LFDEAP------EKLAEVKELLLQF----------VNKHLAKLNIEV--------------TDLATQFHDGVYLILLIGL 55

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87298845  953 L------TQNWNLSdklripAISRVQKMHNVDLVLQVLKSRGVPLTdehgsAISSKDVVDRHREKTLGLLWKI 1019
Cdd:cd21222   56 LegffvpLHEYHLT------PSTDDEKLHNVKLALELMEDAGISTP-----KIRPEDIVNGDLKSILRVLYSL 117
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1761-1908 4.35e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.14  E-value: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845 1761 SQRKNFLQvkRAAICLQAAYRGCKVRRQIKQQSTAAVTIQRVFRG--HSQRMKYQTMLQSAVKIQR-----WYRAQKVAY 1833
Cdd:COG5022  738 DMRDAKLD--NIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGfrLRRLVDYELKWRLFIKLQPllsllGSRKEYRSY 815

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 87298845 1834 DMRIQFLKtreavvclQSAYRGWQVRQQLR--RQHEAAVKIQSTFRMAVAQQQYKLLRAAAAVIQQHVRARAAGKRQ 1908
Cdd:COG5022  816 LACIIKLQ--------KTIKREKKLRETEEveFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL 884
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 933-1025 4.95e-03

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: 39.74  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTqnwnlSDKLRIPAIS--RVQKMHNVDLVLQVLKSR-GVPLtdehgsaISSKDVVDRHR 1009
Cdd:cd21247   42 ITDIYTELKDGIHLLRLLELIS-----GEQLPRPSRGkmRVHFLENNSKAITFLKTKvPVKL-------IGPENIVDGDR 109

                         90
                 ....*....|....*.
gi 87298845 1010 EKTLGLLWKIALAFQV 1025
Cdd:cd21247  110 TLILGLIWIIILRFQI 125
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 933-1027 7.51e-03

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: 39.24  E-value: 7.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87298845  933 VTNLAVDLQCGVRLVRTVELLTQNwNLSDKLRIPAISRVQKMHNVDLVLQVLKSRGVPLTdehgsAISSKDVVDRHREKT 1012
Cdd:cd21310   36 LNDLQKDLSDGLRLIALLEVLSQK-KMYRKYHPRPNFRQMKLENVSVALEFLDREHIKLV-----SIDSKAIVDGNLKLI 109

                         90
                 ....*....|....*
gi 87298845 1013 LGLLWKIALAFQVDI 1027
Cdd:cd21310  110 LGLIWTLILHYSISM 124
 
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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