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Conserved domains on  [gi|215273935|sp|Q8IZT6|]
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RecName: Full=Abnormal spindle-like microcephaly-associated protein; AltName: Full=Abnormal spindle protein homolog; Short=Asp homolog

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 ...
 1112-1261 1.60e-70

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: 233.35  E-value: 1.60e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1112 NIKLLMDWVNAVCAFYNKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRTTQTVECTQTGSVvlnsssesddssLD 1191
Cdd:cd21224     1 VLSLLLKWCQAVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQTVDRAQDEAE------------DF 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1192 MSLKAFDHENTSELYKELLENEKKNFHLVRSAVRDLGGIPAMINHSDMSNTIPDEKVVITYLSFLCARLL 1261
Cdd:cd21224    69 WVAEFSPSTGDSGLSSELLANEKRNFKLVQQAVAELGGVPALLRASDMSNTIPDEKVVILFLSYLCARLL 138
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 940-1053 5.44e-55

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: 187.80  E-value: 5.44e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  940 LSRHLGLLGLPVNHVQTPFDEFDFAVTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRIPAISRLQKMHNVDIVLQVLKSR 1019
Cdd:cd21223     1 LTRHLGYLGYVLSHVQTPLDEFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQKLHNVEVALKALKEA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 215273935 1020 GIeLSDEHGNTILSKDIVDRHREKTLRLLWKIAF 1053
Cdd:cd21223    81 GV-LRGGDGGGITAKDIVDGHREKTLALLWRIIF 113
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 37-134 2.38e-39

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: 142.42  E-value: 2.38e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935    37 PVLSLSHFCRSPFLCFGDVLLGASRTLSLALDNPNEEVAEVKISHFPAADLGFSVSQRCFVLQPKEKIVISVNWTPLKEG 116
Cdd:pfam15780    1 PVLLLAPFSRQPFVCFGDVPVGTSAERLLTVVNPSEEPAEVKVSKVPAPTKGFSVSPLEFTVQPGESQTLTVTWTPTEEG 80

                           90
                   ....*....|....*...
gi 215273935   117 RVREIMTFLVNDVLKHQA 134
Cdd:pfam15780   81 AVRETLQFTVNDVGKHQV 98
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
2257-2433 9.26e-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: 55.08  E-value: 9.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2257 RHLKMMHIAATLIQRRFRTLMMRRRFLSLKK---TAILIQRKYRAHLCTKHHLQFlqvqNAVIKIQSSYRRWMIRKRMRE 2333
Cdd:COG5022   739 MRDAKLDNIATRIQRAIRGRYLRRRYLQALKrikKIQVIQHGFRLRRLVDYELKW----RLFIKLQPLLSLLGSRKEYRS 814

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2334 MHRAATFIQSTFRmhrlhmRYQALKQASVVIqqqyqanraaklqrqhylRQRHSAVILQAAFRGMKTRRHLKSMHSSATL 2413
Cdd:COG5022   815 YLACIIKLQKTIK------REKKLRETEEVE------------------FSLKAEVLIQKFGRSLKAKKRFSLLKKETIY 870

                         170       180
                  ....*....|....*....|
gi 215273935 2414 IQSRFRSLLVRRRFISLKKA 2433
Cdd:COG5022   871 LQSAQRVELAERQLQELKID 890
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
2138-2322 2.76e-06

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: 53.54  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2138 TMRKAAIVIQVRCRAYYQgkmqREKYLTILKAVKVLQASFRGVRVRRtLRKMQT---AATLIQSNYRRYRQQTYFNKLKK 2214
Cdd:COG5022   743 KLDNIATRIQRAIRGRYL----RRRYLQALKRIKKIQVIQHGFRLRR-LVDYELkwrLFIKLQPLLSLLGSRKEYRSYLA 817

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2215 ITKTVQQRywamkerniqfqrynklrhsvIYIQAIFRgkkARRHLKMMHIAATLIQRRFRTLMMRRRFLSLKKTAILIQR 2294
Cdd:COG5022   818 CIIKLQKT---------------------IKREKKLR---ETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS 873

                         170       180
                  ....*....|....*....|....*...
gi 215273935 2295 KYRAHLCTKhhlQFLQVQNAVIKIQSSY 2322
Cdd:COG5022   874 AQRVELAER---QLQELKIDVKSISSLK 898
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
1549-1705 1.32e-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: 51.23  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1549 RRLKAHNLCRQIRAAcviqsyWRMRQDRVRFLNLKKTIIKFQAHVRKHQQRQ--KYKKMKKAAVIIQTHFRAYIFAmkvl 1626
Cdd:COG5022   740 RDAKLDNIATRIQRA------IRGRYLRRRYLQALKRIKKIQVIQHGFRLRRlvDYELKWRLFIKLQPLLSLLGSR---- 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1627 ASYQKTRSAVIVLQ-SAYRGMQARKMY--IHILTSVIKIQSYYRAYVSKKEFLSLKNATIKLQSTVKMKQTRKQYLHLRA 1703
Cdd:COG5022   810 KEYRSYLACIIKLQkTIKREKKLRETEevEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKI 889


                  ..
gi 215273935 1704 AA 1705
Cdd:COG5022   890 DV 891
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
1809-1972 2.54e-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: 50.46  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1809 QAAYRGYKVRQLIKQQSIAAL-------------KIQSAFRGYNKRVKYQSVLQSIIKIQRWYRAYKTLHDTRtHFLKTK 1875
Cdd:COG5022   716 SSKYQIGNTKVFFKAGVLAALedmrdakldniatRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVD-YELKWR 794

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1876 AAvISLQSAYRGWKVRKQIRREHQAALKIQsafRMAKAQKQFRL-----FKTAALVIQQnfRAWTAGRKQCMeYIELRHA 1950
Cdd:COG5022   795 LF-IKLQPLLSLLGSRKEYRSYLACIIKLQ---KTIKREKKLREteeveFSLKAEVLIQ--KFGRSLKAKKR-FSLLKKE 867

                         170       180
                  ....*....|....*....|..
gi 215273935 1951 VLVLQSMWKGKTLRRQLQRQHK 1972
Cdd:COG5022   868 TIYLQSAQRVELAERQLQELKI 889
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
1268-1451 2.57e-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: 50.46  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1268 RAARLIQTTWRKYKLKTDLKRHQEREKAARIIQlavINFLAKQRLR--KRVNAALVIQKYWRrVLAQRKLLMLKKEKLEK 1345
Cdd:COG5022   746 NIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQ---HGFRLRRLVDyeLKWRLFIKLQPLLS-LLGSRKEYRSYLACIIK 821

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1346 VQN------------------KAASLIQGYWRRYSTRQRFLKLKYYSIILQSRIRMIIAVTSYKRYLWATVTIQrhwRAY 1407
Cdd:COG5022   822 LQKtikrekklreteevefslKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS---SLK 898

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 215273935 1408 LRRKQDQQRYEMLKSST---LIIQSMFR-----KWKQRKMQSQVKATVILQR 1451
Cdd:COG5022   899 LVNLELESEIIELKKSLssdLIENLEFKteliaRLKKLLNNIDLEEGPSIEY 950
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
1480-1609 1.54e-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: 47.77  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1480 ELRKYIYIRSCVVIIQKRFRCFQAQKLYKRRKESILTIQ------KYY---------------KAYLKGKIERTNYLQKR 1538
Cdd:COG5022   737 EDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQviqhgfRLRrlvdyelkwrlfiklQPLLSLLGSRKEYRSYL 816

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215273935 1539 AAAIQLQAAFRRLK----AHNLCRQIRAACVIQSYWRMRQDRVRFLNLKKTIIKFQAHVRKHQQRQKYKKMKKAA 1609
Cdd:COG5022   817 ACIIKLQKTIKREKklreTEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDV 891
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
2908-3083 4.05e-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: 43.14  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2908 QIRSSVIIIQARSKGFIQKRKFQEIKNSTIKIQAMWR-RYRAKKYLCKVKAACKIQAWYRCWRAHK--EYLAILKAVKII 2984
Cdd:COG5022   720 QIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRgRYLRRRYLQALKRIKKIQVIQHGFRLRRlvDYELKWRLFIKL 799

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2985 QGCFYTKLERTRFLNVRASAIIIQRKwraILPAKIAHEHFLMIKRHRAACLIQAHYRGYKGRQVFLRQKSAALIIQKYIR 3064
Cdd:COG5022   800 QPLLSLLGSRKEYRSYLACIIKLQKT---IKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQR 876

                         170
                  ....*....|....*....
gi 215273935 3065 AREAGKHERIKYIEFKKST 3083
Cdd:COG5022   877 VELAERQLQELKIDVKSIS 895
 
Name Accession Description Interval E-value
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 1112-1261 1.60e-70

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: 233.35  E-value: 1.60e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1112 NIKLLMDWVNAVCAFYNKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRTTQTVECTQTGSVvlnsssesddssLD 1191
Cdd:cd21224     1 VLSLLLKWCQAVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQTVDRAQDEAE------------DF 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1192 MSLKAFDHENTSELYKELLENEKKNFHLVRSAVRDLGGIPAMINHSDMSNTIPDEKVVITYLSFLCARLL 1261
Cdd:cd21224    69 WVAEFSPSTGDSGLSSELLANEKRNFKLVQQAVAELGGVPALLRASDMSNTIPDEKVVILFLSYLCARLL 138
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 940-1053 5.44e-55

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: 187.80  E-value: 5.44e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  940 LSRHLGLLGLPVNHVQTPFDEFDFAVTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRIPAISRLQKMHNVDIVLQVLKSR 1019
Cdd:cd21223     1 LTRHLGYLGYVLSHVQTPLDEFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQKLHNVEVALKALKEA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 215273935 1020 GIeLSDEHGNTILSKDIVDRHREKTLRLLWKIAF 1053
Cdd:cd21223    81 GV-LRGGDGGGITAKDIVDGHREKTLALLWRIIF 113
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 37-134 2.38e-39

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: 142.42  E-value: 2.38e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935    37 PVLSLSHFCRSPFLCFGDVLLGASRTLSLALDNPNEEVAEVKISHFPAADLGFSVSQRCFVLQPKEKIVISVNWTPLKEG 116
Cdd:pfam15780    1 PVLLLAPFSRQPFVCFGDVPVGTSAERLLTVVNPSEEPAEVKVSKVPAPTKGFSVSPLEFTVQPGESQTLTVTWTPTEEG 80

                           90
                   ....*....|....*...
gi 215273935   117 RVREIMTFLVNDVLKHQA 134
Cdd:pfam15780   81 AVRETLQFTVNDVGKHQV 98
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 1114-1170 1.34e-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: 1.34e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 215273935  1114 KLLMDWVNAVCAFY--NKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRTTQTVE 1170
Cdd:pfam00307    5 KELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLE 63
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2257-2433 9.26e-07

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 55.08  E-value: 9.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2257 RHLKMMHIAATLIQRRFRTLMMRRRFLSLKK---TAILIQRKYRAHLCTKHHLQFlqvqNAVIKIQSSYRRWMIRKRMRE 2333
Cdd:COG5022   739 MRDAKLDNIATRIQRAIRGRYLRRRYLQALKrikKIQVIQHGFRLRRLVDYELKW----RLFIKLQPLLSLLGSRKEYRS 814

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2334 MHRAATFIQSTFRmhrlhmRYQALKQASVVIqqqyqanraaklqrqhylRQRHSAVILQAAFRGMKTRRHLKSMHSSATL 2413
Cdd:COG5022   815 YLACIIKLQKTIK------REKKLRETEEVE------------------FSLKAEVLIQKFGRSLKAKKRFSLLKKETIY 870

                         170       180
                  ....*....|....*....|
gi 215273935 2414 IQSRFRSLLVRRRFISLKKA 2433
Cdd:COG5022   871 LQSAQRVELAERQLQELKID 890
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2138-2322 2.76e-06

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 53.54  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2138 TMRKAAIVIQVRCRAYYQgkmqREKYLTILKAVKVLQASFRGVRVRRtLRKMQT---AATLIQSNYRRYRQQTYFNKLKK 2214
Cdd:COG5022   743 KLDNIATRIQRAIRGRYL----RRRYLQALKRIKKIQVIQHGFRLRR-LVDYELkwrLFIKLQPLLSLLGSRKEYRSYLA 817

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2215 ITKTVQQRywamkerniqfqrynklrhsvIYIQAIFRgkkARRHLKMMHIAATLIQRRFRTLMMRRRFLSLKKTAILIQR 2294
Cdd:COG5022   818 CIIKLQKT---------------------IKREKKLR---ETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS 873

                         170       180
                  ....*....|....*....|....*...
gi 215273935 2295 KYRAHLCTKhhlQFLQVQNAVIKIQSSY 2322
Cdd:COG5022   874 AQRVELAER---QLQELKIDVKSISSLK 898
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 1114-1161 7.84e-06

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: 46.93  E-value: 7.84e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 215273935   1114 KLLMDWVNAVCAFYNK-KVENFTVSFSDGRVLCYLIHHYHPCYVPFDAI 1161
Cdd:smart00033    1 KTLLRWVNSLLAEYDKpPVTNFSSDLKDGVALCALLNSLSPGLVDKKKV 49
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1549-1705 1.32e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 51.23  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1549 RRLKAHNLCRQIRAAcviqsyWRMRQDRVRFLNLKKTIIKFQAHVRKHQQRQ--KYKKMKKAAVIIQTHFRAYIFAmkvl 1626
Cdd:COG5022   740 RDAKLDNIATRIQRA------IRGRYLRRRYLQALKRIKKIQVIQHGFRLRRlvDYELKWRLFIKLQPLLSLLGSR---- 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1627 ASYQKTRSAVIVLQ-SAYRGMQARKMY--IHILTSVIKIQSYYRAYVSKKEFLSLKNATIKLQSTVKMKQTRKQYLHLRA 1703
Cdd:COG5022   810 KEYRSYLACIIKLQkTIKREKKLRETEevEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKI 889


                  ..
gi 215273935 1704 AA 1705
Cdd:COG5022   890 DV 891
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1809-1972 2.54e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 50.46  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1809 QAAYRGYKVRQLIKQQSIAAL-------------KIQSAFRGYNKRVKYQSVLQSIIKIQRWYRAYKTLHDTRtHFLKTK 1875
Cdd:COG5022   716 SSKYQIGNTKVFFKAGVLAALedmrdakldniatRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVD-YELKWR 794

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1876 AAvISLQSAYRGWKVRKQIRREHQAALKIQsafRMAKAQKQFRL-----FKTAALVIQQnfRAWTAGRKQCMeYIELRHA 1950
Cdd:COG5022   795 LF-IKLQPLLSLLGSRKEYRSYLACIIKLQ---KTIKREKKLREteeveFSLKAEVLIQ--KFGRSLKAKKR-FSLLKKE 867

                         170       180
                  ....*....|....*....|..
gi 215273935 1951 VLVLQSMWKGKTLRRQLQRQHK 1972
Cdd:COG5022   868 TIYLQSAQRVELAERQLQELKI 889
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1268-1451 2.57e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 50.46  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1268 RAARLIQTTWRKYKLKTDLKRHQEREKAARIIQlavINFLAKQRLR--KRVNAALVIQKYWRrVLAQRKLLMLKKEKLEK 1345
Cdd:COG5022   746 NIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQ---HGFRLRRLVDyeLKWRLFIKLQPLLS-LLGSRKEYRSYLACIIK 821

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1346 VQN------------------KAASLIQGYWRRYSTRQRFLKLKYYSIILQSRIRMIIAVTSYKRYLWATVTIQrhwRAY 1407
Cdd:COG5022   822 LQKtikrekklreteevefslKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS---SLK 898

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 215273935 1408 LRRKQDQQRYEMLKSST---LIIQSMFR-----KWKQRKMQSQVKATVILQR 1451
Cdd:COG5022   899 LVNLELESEIIELKKSLssdLIENLEFKteliaRLKKLLNNIDLEEGPSIEY 950
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1480-1609 1.54e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 47.77  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1480 ELRKYIYIRSCVVIIQKRFRCFQAQKLYKRRKESILTIQ------KYY---------------KAYLKGKIERTNYLQKR 1538
Cdd:COG5022   737 EDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQviqhgfRLRrlvdyelkwrlfiklQPLLSLLGSRKEYRSYL 816

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215273935 1539 AAAIQLQAAFRRLK----AHNLCRQIRAACVIQSYWRMRQDRVRFLNLKKTIIKFQAHVRKHQQRQKYKKMKKAA 1609
Cdd:COG5022   817 ACIIKLQKTIKREKklreTEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDV 891
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2908-3083 4.05e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.14  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2908 QIRSSVIIIQARSKGFIQKRKFQEIKNSTIKIQAMWR-RYRAKKYLCKVKAACKIQAWYRCWRAHK--EYLAILKAVKII 2984
Cdd:COG5022   720 QIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRgRYLRRRYLQALKRIKKIQVIQHGFRLRRlvDYELKWRLFIKL 799

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2985 QGCFYTKLERTRFLNVRASAIIIQRKwraILPAKIAHEHFLMIKRHRAACLIQAHYRGYKGRQVFLRQKSAALIIQKYIR 3064
Cdd:COG5022   800 QPLLSLLGSRKEYRSYLACIIKLQKT---IKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQR 876

                         170
                  ....*....|....*....
gi 215273935 3065 AREAGKHERIKYIEFKKST 3083
Cdd:COG5022   877 VELAERQLQELKIDVKSIS 895
 
Name Accession Description Interval E-value
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 1112-1261 1.60e-70

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: 233.35  E-value: 1.60e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1112 NIKLLMDWVNAVCAFYNKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRTTQTVECTQTGSVvlnsssesddssLD 1191
Cdd:cd21224     1 VLSLLLKWCQAVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQTVDRAQDEAE------------DF 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1192 MSLKAFDHENTSELYKELLENEKKNFHLVRSAVRDLGGIPAMINHSDMSNTIPDEKVVITYLSFLCARLL 1261
Cdd:cd21224    69 WVAEFSPSTGDSGLSSELLANEKRNFKLVQQAVAELGGVPALLRASDMSNTIPDEKVVILFLSYLCARLL 138
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 940-1053 5.44e-55

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: 187.80  E-value: 5.44e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  940 LSRHLGLLGLPVNHVQTPFDEFDFAVTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRIPAISRLQKMHNVDIVLQVLKSR 1019
Cdd:cd21223     1 LTRHLGYLGYVLSHVQTPLDEFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQKLHNVEVALKALKEA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 215273935 1020 GIeLSDEHGNTILSKDIVDRHREKTLRLLWKIAF 1053
Cdd:cd21223    81 GV-LRGGDGGGITAKDIVDGHREKTLALLWRIIF 113
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 37-134 2.38e-39

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: 142.42  E-value: 2.38e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935    37 PVLSLSHFCRSPFLCFGDVLLGASRTLSLALDNPNEEVAEVKISHFPAADLGFSVSQRCFVLQPKEKIVISVNWTPLKEG 116
Cdd:pfam15780    1 PVLLLAPFSRQPFVCFGDVPVGTSAERLLTVVNPSEEPAEVKVSKVPAPTKGFSVSPLEFTVQPGESQTLTVTWTPTEEG 80

                           90
                   ....*....|....*...
gi 215273935   117 RVREIMTFLVNDVLKHQA 134
Cdd:pfam15780   81 AVRETLQFTVNDVGKHQV 98
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 1113-1254 3.01e-09

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: 56.97  E-value: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1113 IKLLMDWVNAVCAFYNK-KVENFTVSFSDGRVLCYLIHHYHPCYVPFDAicqrttqtvectqtgsvvlnsssesddssld 1191
Cdd:cd21253     3 IKALQQWCRQQTEGYRDvKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDS------------------------------- 51

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215273935 1192 mslkafdhentseLYKE-LLENEKKNFhlvRSAVRDLgGIPAMINHSDM-SNTIPDEKVVITYLS 1254
Cdd:cd21253    52 -------------LSKEnVYENNKLAF---TVAEKEL-GIPALLDAEDMvALKVPDKLSILTYVS 99
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 962-1055 3.23e-08

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: 53.94  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  962 DFAVTNLAVDLQCGVRLVRTMELLTQNwDLSKKLRIPAIsRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHR 1041
Cdd:cd21215    21 GLSITDLVTDLSDGVRLIQLLEIIGDE-SLGRYNKNPKM-RVQKLENVNKALEFIKSRGVKLTN-----IGAEDIVDGNL 93

                          90
                  ....*....|....
gi 215273935 1042 EKTLRLLWKIAFAF 1055
Cdd:cd21215    94 KLILGLLWTLILRF 107
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 965-1057 5.43e-08

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: 53.54  E-value: 5.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRipaiSRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHREKT 1044
Cdd:cd21186    23 IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGR----MRVHHLNNVNRALQVLEQNNVKLVN-----ISSNDIVDGNPKLT 93

                          90
                  ....*....|...
gi 215273935 1045 LRLLWKIAFAFQV 1057
Cdd:cd21186    94 LGLVWSIILHWQV 106
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 1114-1254 6.77e-08

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


Pssm-ID: 409033  Cd Length: 103  Bit Score: 53.01  E-value: 6.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1114 KLLMDWVNAVCAfyNKKVENFTVSFSDGRVLCYLIHHYHPCYVPfdaicqrttqtvectqtgsvvlnsssesddssldms 1193
Cdd:cd21184     4 SLLLEWVNSKIP--EYKVKNFTTDWNDGKALAALVDALKPGLIP------------------------------------ 45

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215273935 1194 lkafdhENTSELYKELLENEKKNFhlvrSAVRDLGGIPAMINHSDMSNTIPDEKVVITYLS 1254
Cdd:cd21184    46 ------DNESLDKENPLENATKAM----DIAEEELGIPKIITPEDMVSPNVDELSVMTYLS 96
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 1114-1170 1.34e-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: 1.34e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 215273935  1114 KLLMDWVNAVCAFY--NKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRTTQTVE 1170
Cdd:pfam00307    5 KELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLE 63
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 1116-1256 1.44e-07

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: 52.10  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1116 LMDWVNAVCAFYNK-KVENFTVSFSDGRVLCYLIHHYHPCYVPFDAIcqrttqtvectqtgsvvlnsssesddssldmsl 1194
Cdd:cd21255     6 LLEWCQEVTAGYRGvRVTNFTTSWRNGLAFCAILHHFHPDLVDYESL--------------------------------- 52

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215273935 1195 KAFDhentselykeLLENEKKNFHLVRSAvrdlgGIPAMINHSDMS-NTIPDEKVVITYLSFL 1256
Cdd:cd21255    53 DPLD----------IKENNKKAFEAFASL-----GVPRLLEPADMVlLPIPDKLIVMTYLCQL 100
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 1113-1260 2.42e-07

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: 51.57  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1113 IK-LLMDWVNAVCAFY-NKKVENFTVSFSDGRVLCYLIHHYHPcyvpfdaicqrttqtvectqtgsvvlnsssesddssl 1190
Cdd:cd21200     2 IKqMLLEWCQAKTRGYeHVDITNFSSSWSDGMAFCALIHHFFP------------------------------------- 44

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215273935 1191 dmslKAFDHENTSElykellENEKKNFHLVRSAVRDLGGIPAMINHSDM--SNTIPDEKVVITYLSFLCARL 1260
Cdd:cd21200    45 ----DAFDYSSLDP------KNRRKNFELAFSTAEELADIAPLLEVEDMvrMGNRPDWKCVFTYVQSLYRHL 106
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2257-2433 9.26e-07

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 55.08  E-value: 9.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2257 RHLKMMHIAATLIQRRFRTLMMRRRFLSLKK---TAILIQRKYRAHLCTKHHLQFlqvqNAVIKIQSSYRRWMIRKRMRE 2333
Cdd:COG5022   739 MRDAKLDNIATRIQRAIRGRYLRRRYLQALKrikKIQVIQHGFRLRRLVDYELKW----RLFIKLQPLLSLLGSRKEYRS 814

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2334 MHRAATFIQSTFRmhrlhmRYQALKQASVVIqqqyqanraaklqrqhylRQRHSAVILQAAFRGMKTRRHLKSMHSSATL 2413
Cdd:COG5022   815 YLACIIKLQKTIK------REKKLRETEEVE------------------FSLKAEVLIQKFGRSLKAKKRFSLLKKETIY 870

                         170       180
                  ....*....|....*....|
gi 215273935 2414 IQSRFRSLLVRRRFISLKKA 2433
Cdd:COG5022   871 LQSAQRVELAERQLQELKID 890
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 1113-1254 2.57e-06

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: 48.69  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1113 IKLLMDWVNAVCAFY-NKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAIcqrttqtvectqtgsvvlnsssesddssld 1191
Cdd:cd21197     2 IQALLRWCRRQCEGYpGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSL------------------------------ 51

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215273935 1192 mslkafDHENtselykeLLENEKKNFHLVRSAVrdlgGIPAMINHSDM-SNTIPDEKVVITYLS 1254
Cdd:cd21197    52 ------KKDN-------WLENNRLAFRVAETSL----GIPALLDAEDMvTMHVPDRLSIITYVS 98
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2138-2322 2.76e-06

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 53.54  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2138 TMRKAAIVIQVRCRAYYQgkmqREKYLTILKAVKVLQASFRGVRVRRtLRKMQT---AATLIQSNYRRYRQQTYFNKLKK 2214
Cdd:COG5022   743 KLDNIATRIQRAIRGRYL----RRRYLQALKRIKKIQVIQHGFRLRR-LVDYELkwrLFIKLQPLLSLLGSRKEYRSYLA 817

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2215 ITKTVQQRywamkerniqfqrynklrhsvIYIQAIFRgkkARRHLKMMHIAATLIQRRFRTLMMRRRFLSLKKTAILIQR 2294
Cdd:COG5022   818 CIIKLQKT---------------------IKREKKLR---ETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS 873

                         170       180
                  ....*....|....*....|....*...
gi 215273935 2295 KYRAHLCTKhhlQFLQVQNAVIKIQSSY 2322
Cdd:COG5022   874 AQRVELAER---QLQELKIDVKSISSLK 898
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 965-1056 4.87e-06

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: 47.78  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRIpaisRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHREKT 1044
Cdd:cd21188    23 VVDLFEDLRDGHNLISLLEVLSGESLPRERGRM----RFHRLQNVQTALDFLKYRKIKLVN-----IRAEDIVDGNPKLT 93

                          90
                  ....*....|..
gi 215273935 1045 LRLLWKIAFAFQ 1056
Cdd:cd21188    94 LGLIWTIILHFQ 105
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 962-1057 6.73e-06

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: 47.67  E-value: 6.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  962 DFAVTNLAVDLQCGVRLVRTMELLtQNWDLSKKLRIPaISRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHR 1041
Cdd:cd21227    21 GMSVEDLATDLEDGVKLIALVEIL-QGRKLGRVIKKP-LNQHQKLENVTLALKAMAEDGIKLVN-----IGNEDIVNGNL 93

                          90
                  ....*....|....*.
gi 215273935 1042 EKTLRLLWKIAFAFQV 1057
Cdd:cd21227    94 KLILGLIWHLILRYQI 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 1114-1161 7.84e-06

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: 46.93  E-value: 7.84e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 215273935   1114 KLLMDWVNAVCAFYNK-KVENFTVSFSDGRVLCYLIHHYHPCYVPFDAI 1161
Cdd:smart00033    1 KTLLRWVNSLLAEYDKpPVTNFSSDLKDGVALCALLNSLSPGLVDKKKV 49
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 1105-1254 8.86e-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: 47.36  E-value: 8.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1105 SFEQYSENIKLLMdWVNAVCAFY-NKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDaicqrttqtvectqtgsvvlnsss 1183
Cdd:cd21216     5 SVEELSAKEGLLL-WCQRKTAPYkNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYD------------------------ 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215273935 1184 esddssldmslkafdhentsELYKellENEKKNFHLVRS-AVRDLgGIPAMINHSDMSNTI-PDEKVVITYLS 1254
Cdd:cd21216    60 --------------------KLRK---DDPRENLNLAFDvAEKHL-DIPKMLDAEDIVNTPrPDERSVMTYVS 108
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1549-1705 1.32e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 51.23  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1549 RRLKAHNLCRQIRAAcviqsyWRMRQDRVRFLNLKKTIIKFQAHVRKHQQRQ--KYKKMKKAAVIIQTHFRAYIFAmkvl 1626
Cdd:COG5022   740 RDAKLDNIATRIQRA------IRGRYLRRRYLQALKRIKKIQVIQHGFRLRRlvDYELKWRLFIKLQPLLSLLGSR---- 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1627 ASYQKTRSAVIVLQ-SAYRGMQARKMY--IHILTSVIKIQSYYRAYVSKKEFLSLKNATIKLQSTVKMKQTRKQYLHLRA 1703
Cdd:COG5022   810 KEYRSYLACIIKLQkTIKREKKLRETEevEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKI 889


                  ..
gi 215273935 1704 AA 1705
Cdd:COG5022   890 DV 891
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 1116-1254 1.50e-05

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: 46.51  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1116 LMDWVNAVCAFY-NKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAIcqrttqtvectqtgsvvlnsssesddssldmsl 1194
Cdd:cd22198     5 LLSWCQEQTEGYrGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSL--------------------------------- 51

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215273935 1195 kafDHENTselykelLENEKKNFHLvrsAVRDLgGIPAMINHSDMSN-TIPDEKVVITYLS 1254
Cdd:cd22198    52 ---DPENI-------AENNQLAFDV---AEQEL-GIPPVMTGQEMASlAVPDKLSMVSYLS 98
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1809-1972 2.54e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 50.46  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1809 QAAYRGYKVRQLIKQQSIAAL-------------KIQSAFRGYNKRVKYQSVLQSIIKIQRWYRAYKTLHDTRtHFLKTK 1875
Cdd:COG5022   716 SSKYQIGNTKVFFKAGVLAALedmrdakldniatRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVD-YELKWR 794

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1876 AAvISLQSAYRGWKVRKQIRREHQAALKIQsafRMAKAQKQFRL-----FKTAALVIQQnfRAWTAGRKQCMeYIELRHA 1950
Cdd:COG5022   795 LF-IKLQPLLSLLGSRKEYRSYLACIIKLQ---KTIKREKKLREteeveFSLKAEVLIQ--KFGRSLKAKKR-FSLLKKE 867

                         170       180
                  ....*....|....*....|..
gi 215273935 1951 VLVLQSMWKGKTLRRQLQRQHK 1972
Cdd:COG5022   868 TIYLQSAQRVELAERQLQELKI 889
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1268-1451 2.57e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 50.46  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1268 RAARLIQTTWRKYKLKTDLKRHQEREKAARIIQlavINFLAKQRLR--KRVNAALVIQKYWRrVLAQRKLLMLKKEKLEK 1345
Cdd:COG5022   746 NIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQ---HGFRLRRLVDyeLKWRLFIKLQPLLS-LLGSRKEYRSYLACIIK 821

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1346 VQN------------------KAASLIQGYWRRYSTRQRFLKLKYYSIILQSRIRMIIAVTSYKRYLWATVTIQrhwRAY 1407
Cdd:COG5022   822 LQKtikrekklreteevefslKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS---SLK 898

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 215273935 1408 LRRKQDQQRYEMLKSST---LIIQSMFR-----KWKQRKMQSQVKATVILQR 1451
Cdd:COG5022   899 LVNLELESEIIELKKSLssdLIENLEFKteliaRLKKLLNNIDLEEGPSIEY 950
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 958-1051 3.32e-05

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: 45.75  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  958 FDEFDFAVTNLAVDLQCGVRLVRTMELLTqnwdlSKKLRIPA--ISRLQKMHNVDIVLQVLKSRgielsdEHGNTILSKD 1035
Cdd:cd21193    29 LEKANLEIGDLFTDLSDGKLLLKLLEIIS-----GEKLGKPNrgRLRVQKIENVNKALAFLKTK------VRLENIGAED 97

                          90
                  ....*....|....*.
gi 215273935 1036 IVDRHREKTLRLLWKI 1051
Cdd:cd21193    98 IVDGNPRLILGLIWTI 113
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 1113-1159 4.00e-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: 45.02  E-value: 4.00e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 215273935 1113 IKLLMDWVNAVCAFYNK-KVENFTVSFSDGRVLCYLIHHYHPCYVPFD 1159
Cdd:cd00014     1 EEELLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIPKI 48
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 1116-1253 5.24e-05

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: 44.72  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1116 LMDWVNAVCAFY-NKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAIcqrttqtvectqtgsvvlnsssesddssldmsl 1194
Cdd:cd21198     6 LLEWCQEVTKGYrGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSL--------------------------------- 52

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1195 kafDHENTSelykellENEKKNFHLVRSAvrdlgGIPAMINHSDM-SNTIPDEKVVITYL 1253
Cdd:cd21198    53 ---SPHDIK-------ENCKLAFDAAAKL-----GIPRLLDPADMvLLSVPDKLSVMTYL 97
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1947-2253 5.61e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 49.31  E-value: 5.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1947 LRHAVLVLQSMWKGKTLRRQ----LQRQHKCAIIIQSY-YRMHVQQKKWKimkKAALLIQKYYRAYSIgREQnhlYLKTK 2021
Cdd:COG5022   744 LDNIATRIQRAIRGRYLRRRylqaLKRIKKIQVIQHGFrLRRLVDYELKW---RLFIKLQPLLSLLGS-RKE---YRSYL 816

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2022 AAVVTLQ-SAYRGMKVRKRIKDCN--KAAVTIQSKYRAYKTKKKYATYRASAIIIQRWYRGIKItnhqHKEYLNLKKTAI 2098
Cdd:COG5022   817 ACIIKLQkTIKREKKLRETEEVEFslKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELA----ERQLQELKIDVK 892

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2099 KIQSVY--------RGIRVRRHIQHMHRAATFIK----AMFKMH--------QSRISYHTMRKAAIVIQVRCR------- 2151
Cdd:COG5022   893 SISSLKlvnlelesEIIELKKSLSSDLIENLEFKteliARLKKLlnnidleeGPSIEYVKLPELNKLHEVESKlketsee 972

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2152 ---AYYQGKMQREKYLTI---LKAVKVLQASFRGVRVR-----RTLRKMQTAATLIQSNYRRYRQQTY----FNKLKKIT 2216
Cdd:COG5022   973 yedLLKKSTILVREGNKAnseLKNFKKELAELSKQYGAlqestKQLKELPVEVAELQSASKIISSESTelsiLKPLQKLK 1052

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 215273935 2217 K--TVQQRYWAMKERNIQFQRYNKLRHSV-IYIQAIFRGK 2253
Cdd:COG5022  1053 GllLLENNQLQARYKALKLRRENSLLDDKqLYQLESTENL 1092
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 1114-1153 5.71e-05

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 44.98  E-value: 5.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 215273935 1114 KLLMDWVNAVCAFYN---KKVENFTVSFSDGRVLCYLIHHYHP 1153
Cdd:cd21218    13 EILLRWVNYHLKKAGptkKRVTNFSSDLKDGEVYALLLHSLAP 55
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 1114-1253 6.40e-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: 44.98  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1114 KLLMDWVNAVCAFY-NKKVENFTVSFSDGRVLCYLIHHYHPcyvpfdaicqrttqtvectqtgsvvlnsssesddssldm 1192
Cdd:cd21259     4 QMLLDWCRAKTRGYeNVDIQNFSSSWSDGMAFCALVHNFFP--------------------------------------- 44

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215273935 1193 slKAFDHENTSElykellENEKKNFHLVRSAVRDLGGIPAMINHSDMSNTI-PDEKVVITYL 1253
Cdd:cd21259    45 --EAFDYSQLSP------QNRRHNFEVAFSSAEKHADCPQLLDVEDMVRMRePDWKCVYTYI 98
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 965-1057 8.36e-05

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: 44.53  E-value: 8.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTqNWDLSKKlriPAISRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHREKT 1044
Cdd:cd21231    27 IEDLFTDLQDGRRLLELLEGLT-GQKLVKE---KGSTRVHALNNVNKALQVLQKNNVDLVN-----IGSADIVDGNHKLT 97

                          90
                  ....*....|...
gi 215273935 1045 LRLLWKIAFAFQV 1057
Cdd:cd21231    98 LGLIWSIILHWQV 110
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1726-1906 9.29e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.54  E-value: 9.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1726 MQMRESCIKLQAFVRGYLVRKQM--RLQR-KAVISLQSYFRMRKARQYYLKmYKAIIVIQNYYHAYkaqvNQRKNFLQVK 1802
Cdd:COG5022   742 AKLDNIATRIQRAIRGRYLRRRYlqALKRiKKIQVIQHGFRLRRLVDYELK-WRLFIKLQPLLSLL----GSRKEYRSYL 816

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1803 KAATCLQ-AAYRGYKVRQLIKQqsiaALKIQSAfrgynkrvkyqsvlqsiIKIQRWYRAYKTlhdtRTHFLKTKAAVISL 1881
Cdd:COG5022   817 ACIIKLQkTIKREKKLRETEEV----EFSLKAE-----------------VLIQKFGRSLKA----KKRFSLLKKETIYL 871

                         170       180
                  ....*....|....*....|....*
gi 215273935 1882 QSAYRGWKVRKQIRREHQAALKIQS 1906
Cdd:COG5022   872 QSAQRVELAERQLQELKIDVKSISS 896
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1480-1609 1.54e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 47.77  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1480 ELRKYIYIRSCVVIIQKRFRCFQAQKLYKRRKESILTIQ------KYY---------------KAYLKGKIERTNYLQKR 1538
Cdd:COG5022   737 EDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQviqhgfRLRrlvdyelkwrlfiklQPLLSLLGSRKEYRSYL 816

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215273935 1539 AAAIQLQAAFRRLK----AHNLCRQIRAACVIQSYWRMRQDRVRFLNLKKTIIKFQAHVRKHQQRQKYKKMKKAA 1609
Cdd:COG5022   817 ACIIKLQKTIKREKklreTEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDV 891
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 965-1058 1.87e-04

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: 43.52  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTqnwdlSKKLRIPAISRLQKMH---NVDIVLQVLKSRGIELSDehgntILSKDIVDRHR 1041
Cdd:cd21241    27 VEDLFEDIKDGTKLLALLEVLS-----GEKLPCEKGRRLKRVHflsNINTALKFLESKKIKLVN-----INPTDIVDGKP 96

                          90
                  ....*....|....*..
gi 215273935 1042 EKTLRLLWKIAFAFQVD 1058
Cdd:cd21241    97 SIVLGLIWTIILYFQIE 113
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 959-1052 1.97e-04

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: 43.10  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  959 DEFDFAVTNLAVDLQCGVRLVRTMELLTQnwDLSKKLRIPAISRLQKMHNVDIVLQVLKSRGIELSDehgnTILSKDIVD 1038
Cdd:cd00014    14 EELPVSITDLFESLRDGVLLCKLINKLSP--GSIPKINKKPKSPFKKRENINLFLNACKKLGLPELD----LFEPEDLYE 87

                          90
                  ....*....|....*
gi 215273935 1039 RHREK-TLRLLWKIA 1052
Cdd:cd00014    88 KGNLKkVLGTLWALA 102
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 965-1057 2.17e-04

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: 43.07  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTQNwDLSKKlriPAISRLQKMHNVDIVLQVLKSRGIELSDEHGNtilskDIVDRHREKT 1044
Cdd:cd21232    23 IKDMFTDLRDGRKLLDLLEGLTGK-SLPKE---RGSTRVHALNNVNRVLQVLHQNNVELVNIGGT-----DIVDGNHKLT 93

                          90
                  ....*....|...
gi 215273935 1045 LRLLWKIAFAFQV 1057
Cdd:cd21232    94 LGLLWSIILHWQV 106
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 1131-1170 2.36e-04

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 42.29  E-value: 2.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 215273935  1131 VENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRTTQTVE 1170
Cdd:pfam11971   13 VEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLA 52
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 965-1051 2.68e-04

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: 43.86  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTQNwDLSKKLRipAISRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHREKT 1044
Cdd:cd21318    58 INDLYTDLRDGYVLTRLLEVLSGE-QLPKPTR--GRMRIHSLENVDKALQFLKEQRVHLEN-----VGSHDIVDGNHRLT 129


                  ....*..
gi 215273935 1045 LRLLWKI 1051
Cdd:cd21318   130 LGLIWTI 136
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 965-1049 4.23e-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: 42.48  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTQNwDLSKKLRIPAISRLQKMHNVDIVLQVLKSRGIELSdehgnTILSKDIVDRHREKT 1044
Cdd:cd21228    24 IYNLETDLSDGLRLIALLEVLSQK-RMYKKYNKRPTFRQMKLENVSVALEFLERESIKLV-----SIDSSAIVDGNLKLI 97


                  ....*
gi 215273935 1045 LRLLW 1049
Cdd:cd21228    98 LGLIW 102
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 965-1057 4.34e-04

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: 42.70  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRIpaisRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHREKT 1044
Cdd:cd21235    26 ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQVKLVN-----IRNDDIADGNPKLT 96

                          90
                  ....*....|...
gi 215273935 1045 LRLLWKIAFAFQV 1057
Cdd:cd21235    97 LGLIWTIILHFQI 109
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 965-1051 4.81e-04

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: 42.73  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTqnwdlSKKLRIPAISRLQK--MHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHRE 1042
Cdd:cd21317    51 IGDLYTDLRDGRMLIRLLEVLS-----GEQLPKPTKGRMRIhcLENVDKALQFLKEQKVHLEN-----MGSHDIVDGNHR 120


                  ....*....
gi 215273935 1043 KTLRLLWKI 1051
Cdd:cd21317   121 LTLGLIWTI 129
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 965-1057 5.33e-04

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: 42.66  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRIpaisRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHREKT 1044
Cdd:cd21236    37 VNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM----RFHRLQNVQIALDYLKRRQVKLVN-----IRNDDITDGNPKLT 107

                          90
                  ....*....|...
gi 215273935 1045 LRLLWKIAFAFQV 1057
Cdd:cd21236   108 LGLIWTIILHFQI 120
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 964-1057 8.52e-04

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: 41.80  E-value: 8.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  964 AVTNLAVDLQCGVRLVRTMELLTqNWDLSKKLRiPAISRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHREK 1043
Cdd:cd21191    26 EVKDLFVDIQDGKILMALLEVLS-GQNLLQEYK-PSSHRIFRLNNIAKALKFLEDSNVKLVS-----IDAAEIADGNPSL 98

                          90
                  ....*....|....
gi 215273935 1044 TLRLLWKIAFAFQV 1057
Cdd:cd21191    99 VLGLIWNIILFFQI 112
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 1116-1253 9.90e-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: 41.38  E-value: 9.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1116 LMDWVNAVCAFYNK-KVENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRttqtvectqtgsvvlnsssesddssldmsl 1194
Cdd:cd21254     6 LLAWCKEVTKGYRGvKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPH------------------------------ 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1195 kafdhentselykELLENEKKNFHLVRSAvrdlgGIPAMINHSDMSN-TIPDEKVVITYL 1253
Cdd:cd21254    56 -------------DIKENNKKAYDGFASL-----GISRLLEPSDMVLlAVPDKLTVMTYL 97
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 905-1051 1.10e-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: 41.42  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  905 LIDHDPclfckdAEFKASKEILLAFsrdflsgegdLSRHLGLLGLPVNHVQTPFDEfdfavtnlavdlqcGVRLVRTMEL 984
Cdd:cd21222     6 LFDEAP------EKLAEVKELLLQF----------VNKHLAKLNIEVTDLATQFHD--------------GVYLILLIGL 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215273935  985 LTQNWDLSKKLRIPAISRLQKMHNVDIVLQVLKSRGIELsdehgNTILSKDIVDRHREKTLRLLWKI 1051
Cdd:cd21222    56 LEGFFVPLHEYHLTPSTDDEKLHNVKLALELMEDAGIST-----PKIRPEDIVNGDLKSILRVLYSL 117
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2184-2371 1.38e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2184 RTLRKMQTAATLIQSNYRRYRQQTyfnklkkitktvqqrywamkerniqfqRYNKLRHSVIYIQAIFRGKKARRHLKMMH 2263
Cdd:COG5022   739 MRDAKLDNIATRIQRAIRGRYLRR---------------------------RYLQALKRIKKIQVIQHGFRLRRLVDYEL 791

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2264 I--AATLIQRRFRTLMMRRRFLSLKKTAILIQRKYRAH--LCTKHHLQFLqvQNAVIKIQSSYRRWMIRKRMREMHRAAT 2339
Cdd:COG5022   792 KwrLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREkkLRETEEVEFS--LKAEVLIQKFGRSLKAKKRFSLLKKETI 869

                         170       180       190
                  ....*....|....*....|....*....|..
gi 215273935 2340 FIQSTFRMHRLHMRYQALKQASVVIQQQYQAN 2371
Cdd:COG5022   870 YLQSAQRVELAERQLQELKIDVKSISSLKLVN 901
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 965-1051 1.66e-03

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: 40.81  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTqnwdlSKKLRIPAIS--RLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHRE 1042
Cdd:cd21246    36 INDLYTDLRDGRMLIKLLEVLS-----GERLPKPTKGkmRIHCLENVDKALQFLKEQRVHLEN-----MGSHDIVDGNHR 105


                  ....*....
gi 215273935 1043 KTLRLLWKI 1051
Cdd:cd21246   106 LTLGLIWTI 114
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1303-1619 2.75e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.91  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1303 VINFLAKQRLRKRVNAALVIQKYWRRVLAQRKLLMLKKEKlekvqnKAASLIQGYWRRYSTRQRFLKLKYYsIILQSRIR 1382
Cdd:COG5022   732 VLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRI------KKIQVIQHGFRLRRLVDYELKWRLF-IKLQPLLS 804

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1383 MIIAVTSYKRYLWATVTIQRHWRAYLRRKQDQQRYEMLKsSTLIIQSMFRKWKQRKMQSQ-VKATVILQRAFREWHLRKQ 1461
Cdd:COG5022   805 LLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLK-AEVLIQKFGRSLKAKKRFSLlKKETIYLQSAQRVELAERQ 883

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1462 AKEENSAI-IIQSWYRMHKELRKYIYIRSCVVIIQKRFRCFQAQKLYKRRKESILTIQKyykaylkgKIERTNYLQKRAA 1540
Cdd:COG5022   884 LQELKIDVkSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDL--------EEGPSIEYVKLPE 955

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 1541 AIQLQAAFRRLKahNLCRQIRAAcVIQSYWRMRQDRVRFLNLKKTIIKFQAHVRKHQQRQ-KYKKMKKAAVIIQTHFRAY 1619
Cdd:COG5022   956 LNKLHEVESKLK--ETSEEYEDL-LKKSTILVREGNKANSELKNFKKELAELSKQYGALQeSTKQLKELPVEVAELQSAS 1032
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 965-1038 3.41e-03

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: 39.49  E-value: 3.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTqnwdlskKLRIPAI-----SRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVD 1038
Cdd:cd21212    22 ITDLQKDLGDGLTLVNLIEAVA-------GEKVPGIhsrpkTRAQKLENIQACLQFLAALGVDVQG-----ITAEDIVD 88
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 965-1058 3.45e-03

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: 39.86  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTqnwdlSKKLRIPAISRLQKMH---NVDIVLQVLKSRGIELSDEHgntilSKDIVDRHR 1041
Cdd:cd21190    27 INDLFVDIKDGTALLRLLEVLS-----GQKLPIESGRVLQRAHklsNIRNALDFLTKRCIKLVNIN-----STDIVDGKP 96

                          90
                  ....*....|....*..
gi 215273935 1042 EKTLRLLWKIAFAFQVD 1058
Cdd:cd21190    97 SIVLGLIWTIILYFQIE 113
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 1116-1158 3.94e-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: 39.63  E-value: 3.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 215273935 1116 LMDWVNAVCAFY-NKKVENFTVSFSDGRVLCYLIHHYHPCYVPF 1158
Cdd:cd21257    13 LLKWCQKKTEGYpNIDITNFSSSWSDGLAFCALLHTYLPAHIPY 56
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 965-1065 4.05e-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: 40.06  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRIPAISRLQkMHNVDIVLQVLKSRGIELSdehgnTILSKDIVDRHREKT 1044
Cdd:cd21309    37 IGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFRQMQ-LENVSVALEFLDRESIKLV-----SIDSKAIVDGNLKLI 110

                          90       100
                  ....*....|....*....|.
gi 215273935 1045 LRLLWKIAFAFQVDISLNLDQ 1065
Cdd:cd21309   111 LGLVWTLILHYSISMPVWEDE 131
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2908-3083 4.05e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.14  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2908 QIRSSVIIIQARSKGFIQKRKFQEIKNSTIKIQAMWR-RYRAKKYLCKVKAACKIQAWYRCWRAHK--EYLAILKAVKII 2984
Cdd:COG5022   720 QIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRgRYLRRRYLQALKRIKKIQVIQHGFRLRRlvDYELKWRLFIKL 799

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935 2985 QGCFYTKLERTRFLNVRASAIIIQRKwraILPAKIAHEHFLMIKRHRAACLIQAHYRGYKGRQVFLRQKSAALIIQKYIR 3064
Cdd:COG5022   800 QPLLSLLGSRKEYRSYLACIIKLQKT---IKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQR 876

                         170
                  ....*....|....*....
gi 215273935 3065 AREAGKHERIKYIEFKKST 3083
Cdd:COG5022   877 VELAERQLQELKIDVKSIS 895
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 965-1059 5.03e-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: 39.68  E-value: 5.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273935  965 VTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRIPAISRLQkMHNVDIVLQVLKSRGIELSdehgnTILSKDIVDRHREKT 1044
Cdd:cd21308    40 IANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQ-LENVSVALEFLDRESIKLV-----SIDSKAIVDGNLKLI 113

                          90
                  ....*....|....*
gi 215273935 1045 LRLLWKIAFAFQVDI 1059
Cdd:cd21308   114 LGLIWTLILHYSISM 128
 
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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