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Conserved domains on  [gi|119600537|gb|EAW80131|]
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growth arrest-specific 2 like 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_GAS2L1_2 cd21268
calponin homology (CH) domain found in GAS2-like protein 1 (GAS2L1), GAS2L2, and similar ...
 23-163 2.08e-83

calponin homology (CH) domain found in GAS2-like protein 1 (GAS2L1), GAS2L2, and similar proteins; This subfamily includes GAS2L1 (also called GAS2-related protein on chromosome 22 or growth arrest-specific protein 2-like 1) and GAS2L2 (also called GAS2-related protein on chromosome 17 or growth arrest-specific protein 2-like 2). They may be involved in the cross-linking of microtubules and microfilaments. Members of this subfamily contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409117  Cd Length: 142  Bit Score: 263.41  E-value: 2.08e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  23 PFKSSEQYLEAMKEDLAEWLRDLYGLDIDAANFLQVLETGLVLCQHANVVTDAALAFLAEAPAQAQKIP-MPRVGVSCNG 101
Cdd:cd21268    1 PFKSSEEYLYAMKEDLAEWLNTLYNLDITADNFFEKLETGVLLCKHANNVTRAAREFQAQHPERASPLKlPPREVIFYRP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119600537 102 AAQPGTFQARDNVSNFIQWCRKEMGIQEVLMFETEDLVLRKNVKNVVLCLLELGRRAWRFGV 163
Cdd:cd21268   81 SAKPGSFQARDNVSNFINWCRQLLGIPEVLLFETDDLVLRKNEKNFVLCLLEVARRGAKFGM 142
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
 206-274 1.57e-41

Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.


:

Pssm-ID: 460480  Cd Length: 69  Bit Score: 145.82  E-value: 1.57e-41
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119600537  206 LDQMVQSLVSHCTCPVQFSMVKVSEGKYRVGDSNTLIFIRILRNHVMVRVGGGWDTLGHYLDKHDPCRC 274
Cdd:pfam02187   1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 419-875 7.82e-09

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.95  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  419 SWVHEETDSWGTDAGNPTPQRLRAIEATTKGISARGPSPLPRSFGPAeclglrLPLRDEAKGAffqfrEPESVRSPTPVQ 498
Cdd:PHA03247 2535 TWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPA------VTSRARRPDA-----PPQSARPRAPVD 2603

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  499 GLTKIPIRLPPA-RPPTPGRSFPGATSGSPR--TELGRDPIPLRAVTVDLAGSTHGDCSVEVRQEDQQLDIQVMAEARES 575
Cdd:PHA03247 2604 DRGDPRGPAPPSpLPPDTHAPDPPPPSPSPAanEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP 2683

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  576 WDLGLQEQEGRYT----PLPLGGNKEQAIYCSLEEEILgnmkllevrSACPQGTRSGVIPRSGVYIPRLAGQWPE-PGGP 650
Cdd:PHA03247 2684 RRRAARPTVGSLTsladPPPPPPTPEPAPHALVSATPL---------PPGPAAARQASPALPAAPAPPAVPAGPAtPGGP 2754

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  651 YDKAIQELAQGSPSllkvdlEAWKAAPTGSPKPAVTPGPG-----SLKGKLGARQSGPRTKASLSAKGTHMRKVPPQGGQ 725
Cdd:PHA03247 2755 ARPARPPTTAGPPA------PAPPAAPAAGPPRRLTRPAVaslseSRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  726 DCSASTVSASPeaPTPSPLDPNSDKAKACLSKGRRTLRKPKRVPSIYKLKLRPRIRPRRDHRPekQPSRIPRPLAYVFLG 805
Cdd:PHA03247 2829 PPPTSAQPTAP--PPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARP--AVSRSTESFALPPDQ 2904

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  806 PARQPPKDrllravlgskggeasrvdgasvgeeeEEGKEEKEPAAPLESSPQPPEGLQPhwLNQAPLPPE 875
Cdd:PHA03247 2905 PERPPQPQ--------------------------APPPPQPQPQPPPPPQPQPPPPPPP--RPQPPLAPT 2946
 
Name Accession Description Interval E-value
CH_GAS2L1_2 cd21268
calponin homology (CH) domain found in GAS2-like protein 1 (GAS2L1), GAS2L2, and similar ...
 23-163 2.08e-83

calponin homology (CH) domain found in GAS2-like protein 1 (GAS2L1), GAS2L2, and similar proteins; This subfamily includes GAS2L1 (also called GAS2-related protein on chromosome 22 or growth arrest-specific protein 2-like 1) and GAS2L2 (also called GAS2-related protein on chromosome 17 or growth arrest-specific protein 2-like 2). They may be involved in the cross-linking of microtubules and microfilaments. Members of this subfamily contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409117  Cd Length: 142  Bit Score: 263.41  E-value: 2.08e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  23 PFKSSEQYLEAMKEDLAEWLRDLYGLDIDAANFLQVLETGLVLCQHANVVTDAALAFLAEAPAQAQKIP-MPRVGVSCNG 101
Cdd:cd21268    1 PFKSSEEYLYAMKEDLAEWLNTLYNLDITADNFFEKLETGVLLCKHANNVTRAAREFQAQHPERASPLKlPPREVIFYRP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119600537 102 AAQPGTFQARDNVSNFIQWCRKEMGIQEVLMFETEDLVLRKNVKNVVLCLLELGRRAWRFGV 163
Cdd:cd21268   81 SAKPGSFQARDNVSNFINWCRQLLGIPEVLLFETDDLVLRKNEKNFVLCLLEVARRGAKFGM 142
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
 206-274 1.57e-41

Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.


Pssm-ID: 460480  Cd Length: 69  Bit Score: 145.82  E-value: 1.57e-41
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119600537  206 LDQMVQSLVSHCTCPVQFSMVKVSEGKYRVGDSNTLIFIRILRNHVMVRVGGGWDTLGHYLDKHDPCRC 274
Cdd:pfam02187   1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
 204-276 5.92e-33

Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain


Pssm-ID: 128539  Cd Length: 73  Bit Score: 121.79  E-value: 5.92e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600537   204 RNLDQMVQSLVSHCTCPVQFSMVKVSEGKYRVGDSNTLIFIRILRNHVMVRVGGGWDTLGHYLDKHDPCRCTS 276
Cdd:smart00243   1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 32-158 1.13e-12

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: 65.00  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537   32 EAMKEDLAEWLRDLYGLDIDA---ANFLQVLETGLVLCQHANVVtdaalaflaeapaQAQKIPMPRVGVScngaaqpgTF 108
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGvrvTNFTTDLRDGLALCALLNKL-------------APGLVDKKKLNKS--------EF 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 119600537  109 QARDNVSNFIQWCRKEMGIQEVLMfETEDLVLRKNvKNVVLCLLELGRRA 158
Cdd:pfam00307  60 DKLENINLALDVAEKKLGVPKVLI-EPEDLVEGDN-KSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 36-154 1.19e-09

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: 56.17  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537    36 EDLAEWLRDLYGLDIDAA--NFLQVLETGLVLCQHANVVtdaalaflaeapaQAQKIPMPRVgvscngAAQPGTFQARDN 113
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPvtNFSSDLKDGVALCALLNSL-------------SPGLVDKKKV------AASLSRFKKIEN 61

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 119600537   114 VSNFIQWCRKEMGIqeVLMFETEDLVL-RKNVKNVVLCLLEL 154
Cdd:smart00033  62 INLALSFAEKLGGK--VVLFEPEDLVEgPKLILGVIWTLISL 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
 419-875 7.82e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.95  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  419 SWVHEETDSWGTDAGNPTPQRLRAIEATTKGISARGPSPLPRSFGPAeclglrLPLRDEAKGAffqfrEPESVRSPTPVQ 498
Cdd:PHA03247 2535 TWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPA------VTSRARRPDA-----PPQSARPRAPVD 2603

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  499 GLTKIPIRLPPA-RPPTPGRSFPGATSGSPR--TELGRDPIPLRAVTVDLAGSTHGDCSVEVRQEDQQLDIQVMAEARES 575
Cdd:PHA03247 2604 DRGDPRGPAPPSpLPPDTHAPDPPPPSPSPAanEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP 2683

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  576 WDLGLQEQEGRYT----PLPLGGNKEQAIYCSLEEEILgnmkllevrSACPQGTRSGVIPRSGVYIPRLAGQWPE-PGGP 650
Cdd:PHA03247 2684 RRRAARPTVGSLTsladPPPPPPTPEPAPHALVSATPL---------PPGPAAARQASPALPAAPAPPAVPAGPAtPGGP 2754

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  651 YDKAIQELAQGSPSllkvdlEAWKAAPTGSPKPAVTPGPG-----SLKGKLGARQSGPRTKASLSAKGTHMRKVPPQGGQ 725
Cdd:PHA03247 2755 ARPARPPTTAGPPA------PAPPAAPAAGPPRRLTRPAVaslseSRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  726 DCSASTVSASPeaPTPSPLDPNSDKAKACLSKGRRTLRKPKRVPSIYKLKLRPRIRPRRDHRPekQPSRIPRPLAYVFLG 805
Cdd:PHA03247 2829 PPPTSAQPTAP--PPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARP--AVSRSTESFALPPDQ 2904

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  806 PARQPPKDrllravlgskggeasrvdgasvgeeeEEGKEEKEPAAPLESSPQPPEGLQPhwLNQAPLPPE 875
Cdd:PHA03247 2905 PERPPQPQ--------------------------APPPPQPQPQPPPPPQPQPPPPPPP--RPQPPLAPT 2946
SCP1 COG5199
Calponin [Cytoskeleton];
32-158 1.67e-05

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 46.45  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  32 EAMKEdLAEWLRDLYGLDIDAA-NFLQVLETGLVLCQhanvvtdaalaFLAEA-PAQaqkipmprvgVSCNGAAQPgtFQ 109
Cdd:COG5199   13 KQQKE-VTLWIETVLGEKFEPPgDLLSLLKDGVRLCR-----------ILNEAsPLD----------IKYKESKMP--FV 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 119600537 110 ARDNVSNFIQWCRKeMGIQEVLMFETEDLVLRKNVKNVVLCLLELGRRA 158
Cdd:COG5199   69 QMENISSFINGLKK-LRVPEYELFQTNDLFEAKDLRQVVICLYSLSRYA 116
 
Name Accession Description Interval E-value
CH_GAS2L1_2 cd21268
calponin homology (CH) domain found in GAS2-like protein 1 (GAS2L1), GAS2L2, and similar ...
 23-163 2.08e-83

calponin homology (CH) domain found in GAS2-like protein 1 (GAS2L1), GAS2L2, and similar proteins; This subfamily includes GAS2L1 (also called GAS2-related protein on chromosome 22 or growth arrest-specific protein 2-like 1) and GAS2L2 (also called GAS2-related protein on chromosome 17 or growth arrest-specific protein 2-like 2). They may be involved in the cross-linking of microtubules and microfilaments. Members of this subfamily contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409117  Cd Length: 142  Bit Score: 263.41  E-value: 2.08e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  23 PFKSSEQYLEAMKEDLAEWLRDLYGLDIDAANFLQVLETGLVLCQHANVVTDAALAFLAEAPAQAQKIP-MPRVGVSCNG 101
Cdd:cd21268    1 PFKSSEEYLYAMKEDLAEWLNTLYNLDITADNFFEKLETGVLLCKHANNVTRAAREFQAQHPERASPLKlPPREVIFYRP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119600537 102 AAQPGTFQARDNVSNFIQWCRKEMGIQEVLMFETEDLVLRKNVKNVVLCLLELGRRAWRFGV 163
Cdd:cd21268   81 SAKPGSFQARDNVSNFINWCRQLLGIPEVLLFETDDLVLRKNEKNFVLCLLEVARRGAKFGM 142
CH_GAS2-like cd21204
calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth ...
 28-162 2.61e-54

calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth arrest-specific protein 2 (GAS-2) family includes GAS-2, and GAS-2 like proteins, GAS2L1-3. GAS-2 may play a role in apoptosis by acting as a cell death substrate for caspases. GAS2L1 (also called GAS2-related protein on chromosome 22 or growth arrest-specific protein 2-like 1) and GAS2L2 (also called GAS2-related protein on chromosome 17 or growth arrest-specific protein 2-like 2) may be involved in the cross-linking of microtubules and microfilaments. GAS2L3, also called GAS2-like protein 3, is a cytoskeletal linker protein that may promote and stabilize the formation of the actin and microtubule network. Members of this family contain a single copy of the CH domain at the N-terminal region. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409053  Cd Length: 131  Bit Score: 184.39  E-value: 2.61e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  28 EQYLEAMKEDLAEWLRDLYGLDIDAANFLQVLETGLVLCQHANVVTDAALAFLAeapAQAQKIPMPRVGVSCNGAAQPGT 107
Cdd:cd21204    1 EEALLPMKEDLAEWLNDLLGDDLTPDNFLDELRNGVVLCQLAQKIQEAAEKARE---AGKKNGPPPSYKLKCNENAKPGS 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119600537 108 FQARDNVSNFIQWCRKEmGIQEVLMFETEDLVLRKNVKNVVLCLLELGRRAWRFG 162
Cdd:cd21204   78 FFARDNVANFLRWCRKL-GVDEVLLFESEDLVLHKNPRQVLLCLLELARIAARYG 131
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
 206-274 1.57e-41

Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.


Pssm-ID: 460480  Cd Length: 69  Bit Score: 145.82  E-value: 1.57e-41
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119600537  206 LDQMVQSLVSHCTCPVQFSMVKVSEGKYRVGDSNTLIFIRILRNHVMVRVGGGWDTLGHYLDKHDPCRC 274
Cdd:pfam02187   1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
 204-276 5.92e-33

Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain


Pssm-ID: 128539  Cd Length: 73  Bit Score: 121.79  E-value: 5.92e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600537   204 RNLDQMVQSLVSHCTCPVQFSMVKVSEGKYRVGDSNTLIFIRILRNHVMVRVGGGWDTLGHYLDKHDPCRCTS 276
Cdd:smart00243   1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
CH_GAS2 cd21267
calponin homology (CH) domain found in growth arrest-specific protein 2; Growth ...
 28-163 1.50e-31

calponin homology (CH) domain found in growth arrest-specific protein 2; Growth arrest-specific protein 2 (GAS-2) may play a role in apoptosis by acting as a cell death substrate for caspases. It contains a single copy of the CH domain at the N-terminal region. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409116  Cd Length: 136  Bit Score: 120.05  E-value: 1.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  28 EQYLEAMKEDLAEWLRDLYGLDIDAANFLQVLETGLVLCQHANVVTDAALAFLAEAPAQAQKIPMPRVgvSCNGAAQPGT 107
Cdd:cd21267    2 EASLLPMKEDLALWLTNLLGKEITAESFMEKLDNGALLCQLAETLQEKFKENSADANKPGKSLPVRKI--PCRANAPSGS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119600537 108 FQARDNVSNFIQWCRkEMGIQEVLMFETEDLVLRKNVKNVVLCLLELGRRAWRFGV 163
Cdd:cd21267   80 FFARDNTANFLSWCR-DVGVGDTCLFESEGLVLHKQPREVCLCLLELGRIAARFGV 134
CH_GAS2L3 cd21269
calponin homology (CH) domain found in growth arrest-specific protein 2-like 3; Growth ...
 28-162 9.74e-29

calponin homology (CH) domain found in growth arrest-specific protein 2-like 3; Growth arrest-specific protein 2-like 3 (GAS2L3), also called GAS2-like protein 3, is a cytoskeletal linker protein that may promote and stabilize the formation of the actin and microtubule network. It contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409118  Cd Length: 130  Bit Score: 111.85  E-value: 9.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  28 EQYLEAMKEDLAEWLRDLYGLDIDAANFLQVLETGLVLCQHANVVTDAalafLAEAPAQAQKIPMPRVGVSCNGAAQPGT 107
Cdd:cd21269    1 EATLVPMQEDLSIWLSGMLGKEVKAERFMEELDNGVLLCQLIGVLQSK----IKECCSTEELKHFPMRKVPCKKDAPSGS 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119600537 108 FQARDNVSNFIQWCRkEMGIQEVLMFETEDLVLRKNVKNVVLCLLELGRRAWRFG 162
Cdd:cd21269   77 FFARDNTANFLSWCR-AIGVDETYLFESEGLVLHKDPRQVCLCLLEIGRIVSRYG 130
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 35-156 3.46e-13

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: 66.21  E-value: 3.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  35 KEDLAEWLRDLYG--LDIDAANFLQVLETGLVLCQHANVVTDAALAFLAEAPAQAqkipmprvgvscngaaqpgtFQARD 112
Cdd:cd00014    1 EEELLKWINEVLGeeLPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSP--------------------FKKRE 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119600537 113 NVSNFIQWCRKeMGIQEVLMFETEDLVLRKNVKNVVLCLLELGR 156
Cdd:cd00014   61 NINLFLNACKK-LGLPELDLFEPEDLYEKGNLKKVLGTLWALAL 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 32-158 1.13e-12

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: 65.00  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537   32 EAMKEDLAEWLRDLYGLDIDA---ANFLQVLETGLVLCQHANVVtdaalaflaeapaQAQKIPMPRVGVScngaaqpgTF 108
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGvrvTNFTTDLRDGLALCALLNKL-------------APGLVDKKKLNKS--------EF 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 119600537  109 QARDNVSNFIQWCRKEMGIQEVLMfETEDLVLRKNvKNVVLCLLELGRRA 158
Cdd:pfam00307  60 DKLENINLALDVAEKKLGVPKVLI-EPEDLVEGDN-KSVLTYLASLFRRF 107
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
 34-156 2.75e-11

calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar proteins; The family includes transgelins from Saccharomyces cerevisiae and Schizosaccharomyces pombe, which are also called SCP1 and STG1, respectively. Transgelin, also called calponin homolog 1, has actin-binding and actin-bundling activity. It stabilizes actin filaments against disassembly. Transgelin contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409059 [Multi-domain]  Cd Length: 101  Bit Score: 60.84  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  34 MKEDLAEWLRDLYGLDIDAANFLQVLETGLVLCQHANVVTdaalaflaeaPAQAQKIpmprvgvscNGAAQPgtFQARDN 113
Cdd:cd21210    1 AEQEAREWIEEVLGEKLAQGDLLDALKDGVVLCKLANRIL----------PADIRKY---------KESKMP--FVQMEN 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 119600537 114 VSNFIQWCRKeMGIQEVLMFETEDLVLRKNVKNVVLCLLELGR 156
Cdd:cd21210   60 ISAFLNAARK-LGVPENDLFQTVDLFERKNPAQVLQCLHALSR 101
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
 40-156 4.76e-10

calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 (dMP20) and similar domains; This subfamily contains Drosophila melanogaster muscle-specific protein 20 (dMP20), Echinococcus granulosus myophilin, Dictyostelium discoideum Rac guanine nucleotide exchange factor B (also called Trix), and similar proteins. dMP20 is present only in the synchronous muscles of D. melanogaster. It may be involved in the system linking the nerve impulse with the contraction or the relaxation process. Trix is involved in the regulation of the late steps of the endocytic pathway. dMP20 contains a single copy of the CH domain, while Trix (triple CH-domain array exchange factor) contains three, two type 3 CH domains which are included in this model, and one type 1 CH domain that is not included in this subfamily, but is part of the superfamily. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409056 [Multi-domain]  Cd Length: 107  Bit Score: 57.32  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  40 EWLRDLYGLDIDAA-NFLQVLETGLVLCQHANVVtdaalaflaeAPAQAQKIpmprvgvscNGAAQPgtFQARDNVSNFI 118
Cdd:cd21207   12 DWIEAVTGEKLDDGkDYEDVLKDGVILCKLINIL----------KPGSVKKI---------NTSKMA--FKLMENIENFL 70

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 119600537 119 QWCrKEMGIQEVLMFETEDLVLRKNVKNVVLCLLELGR 156
Cdd:cd21207   71 TAC-KGYGVPKTDLFQTVDLYEKKNIPQVTNCLFALGR 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 36-154 1.19e-09

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: 56.17  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537    36 EDLAEWLRDLYGLDIDAA--NFLQVLETGLVLCQHANVVtdaalaflaeapaQAQKIPMPRVgvscngAAQPGTFQARDN 113
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPvtNFSSDLKDGVALCALLNSL-------------SPGLVDKKKV------AASLSRFKKIEN 61

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 119600537   114 VSNFIQWCRKEMGIqeVLMFETEDLVL-RKNVKNVVLCLLEL 154
Cdd:smart00033  62 INLALSFAEKLGGK--VVLFEPEDLVEgPKLILGVIWTLISL 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
 419-875 7.82e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.95  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  419 SWVHEETDSWGTDAGNPTPQRLRAIEATTKGISARGPSPLPRSFGPAeclglrLPLRDEAKGAffqfrEPESVRSPTPVQ 498
Cdd:PHA03247 2535 TWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPA------VTSRARRPDA-----PPQSARPRAPVD 2603

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  499 GLTKIPIRLPPA-RPPTPGRSFPGATSGSPR--TELGRDPIPLRAVTVDLAGSTHGDCSVEVRQEDQQLDIQVMAEARES 575
Cdd:PHA03247 2604 DRGDPRGPAPPSpLPPDTHAPDPPPPSPSPAanEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP 2683

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  576 WDLGLQEQEGRYT----PLPLGGNKEQAIYCSLEEEILgnmkllevrSACPQGTRSGVIPRSGVYIPRLAGQWPE-PGGP 650
Cdd:PHA03247 2684 RRRAARPTVGSLTsladPPPPPPTPEPAPHALVSATPL---------PPGPAAARQASPALPAAPAPPAVPAGPAtPGGP 2754

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  651 YDKAIQELAQGSPSllkvdlEAWKAAPTGSPKPAVTPGPG-----SLKGKLGARQSGPRTKASLSAKGTHMRKVPPQGGQ 725
Cdd:PHA03247 2755 ARPARPPTTAGPPA------PAPPAAPAAGPPRRLTRPAVaslseSRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  726 DCSASTVSASPeaPTPSPLDPNSDKAKACLSKGRRTLRKPKRVPSIYKLKLRPRIRPRRDHRPekQPSRIPRPLAYVFLG 805
Cdd:PHA03247 2829 PPPTSAQPTAP--PPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARP--AVSRSTESFALPPDQ 2904

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  806 PARQPPKDrllravlgskggeasrvdgasvgeeeEEGKEEKEPAAPLESSPQPPEGLQPhwLNQAPLPPE 875
Cdd:PHA03247 2905 PERPPQPQ--------------------------APPPPQPQPQPPPPPQPQPPPPPPP--RPQPPLAPT 2946
SCP1 COG5199
Calponin [Cytoskeleton];
32-158 1.67e-05

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 46.45  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  32 EAMKEdLAEWLRDLYGLDIDAA-NFLQVLETGLVLCQhanvvtdaalaFLAEA-PAQaqkipmprvgVSCNGAAQPgtFQ 109
Cdd:COG5199   13 KQQKE-VTLWIETVLGEKFEPPgDLLSLLKDGVRLCR-----------ILNEAsPLD----------IKYKESKMP--FV 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 119600537 110 ARDNVSNFIQWCRKeMGIQEVLMFETEDLVLRKNVKNVVLCLLELGRRA 158
Cdd:COG5199   69 QMENISSFINGLKK-LRVPEYELFQTNDLFEAKDLRQVVICLYSLSRYA 116
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
 40-151 5.55e-05

calponin homology (CH) domain found in the IQ motif containing GTPase activating protein family; Members of the IQ motif containing GTPase activating protein (IQGAP) family are associated with the Ras GTP-binding protein and act as essential regulators of cytoskeletal function. There are three known IQGAP family members: IQGAP1, IQGAP2, and IQGAP3. They are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity. It lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3 regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton.


Pssm-ID: 409055 [Multi-domain]  Cd Length: 118  Bit Score: 43.37  E-value: 5.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  40 EWLRDLYGLDI-DAANFLQVLETGLVLCQHANVVtdaalaflaeAPAQAQKIPMPRVGVScngaaqpgtFQARDNVSNFI 118
Cdd:cd21206   15 QWIEACLNEELpPTTEFEEELRNGVVLAKLANKF----------APKLVPLKKIYDVGLQ---------FRHTDNINHFL 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 119600537 119 QWCrKEMGIQEVLMFETEDLVLRKNVKNVVLCL 151
Cdd:cd21206   76 RAL-KKIGLPKIFHFETTDLYEKKNIPKVIYCL 107
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 35-154 1.44e-04

calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. This family includes a group of kinesin-like proteins belonging to KIN-14 protein family. They all contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409052 [Multi-domain]  Cd Length: 112  Bit Score: 42.02  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  35 KEDLAEWLRDLYGLDIDA----ANFLQVLETGLVLCQHANVVtdaalafLAEApaqaqkipMPRVGVSCNGAAQP--GTF 108
Cdd:cd21203    2 RYEAAEWIQNVLGVLVLPdpseEEFRLCLRDGVVLCKLLNKL-------QPGA--------VPKVVESPDDPDGAagSAF 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 119600537 109 QARDNVSNFIQWCrKEMGIQevlMFETEDL--VLRKNVKNVVLCLLEL 154
Cdd:cd21203   67 QYFENVRNFLVAI-EEMGLP---TFEASDLeqGGGGSRPRVVDCILAL 110
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
 39-154 9.15e-04

calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV proteins.


Pssm-ID: 409050  Cd Length: 117  Bit Score: 39.93  E-value: 9.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  39 AEWLRDLYGL---------DIDAANFLQVLETGLVLCQHANVVTDAALAFLAEAPAQaqkipmprvgvscngaaQPGTFQ 109
Cdd:cd21201    7 ADWLIRCGVLppdhratqpNATVFDLAQALRDGVLLCQLLNRLSPGSVDDREINLRP-----------------QMSQFL 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119600537 110 ARDNVSNFIQWCRKEMGIQEVLMFETEDLVLRKNVKNVVLCLLEL 154
Cdd:cd21201   70 CLKNIRTFLQACRTVFGLRSADLFEPEDLYDVTNFGKVIRTLSKL 114
CH_LRCH4 cd21273
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 57-154 2.04e-03

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 4; Leucine-rich repeat and calponin homology domain-containing protein 4 (LRCH4), also called leucine-rich repeat neuronal protein 4, or leucine-rich neuronal protein, acts as a novel Toll-like receptor (TLR) accessory protein that regulates the innate immune response. LRCH4 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409122  Cd Length: 109  Bit Score: 38.73  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  57 QVLETGLVLCQHANVVTDAALAFLaeapaqaqKIPMPRVgvscngaAQPGTFQARDNVSNFIQWCRKeMGIQEVLMFETE 136
Cdd:cd21273   27 EALSNGAVLCQLANQLRPRSVSII--------HVPSPAV-------PKLSKAKCRKNVENFIEACRK-MGVPEVDLCSPS 90

                         90
                 ....*....|....*...
gi 119600537 137 DlVLRKNVKNVVLCLLEL 154
Cdd:cd21273   91 D-VLLQGPAAVLRTVLAL 107
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
 54-159 2.60e-03

calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This family includes LIM domain only protein 7 (LMO-7) and LIM and calponin homology domains-containing protein 1 (LIMCH1), and similar proteins. LMO-7, also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. LIMCH1 acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409057 [Multi-domain]  Cd Length: 119  Bit Score: 38.47  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  54 NFLQVLETGLVLCQHANVVTdaalaflaeaPAQAQKIPMPRVGVSCngaaqpgtfqaRDNVSNFIQWCRkEMGIQEVLMF 133
Cdd:cd21208   21 DFRESLEDGILLCELINAIK----------PGSIKKINRLPTPIAG-----------LDNLNLFLKACE-DLGLKDSQLF 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 119600537 134 ETEDLV---------------LRKNVKNVVLCLLELGRRAW 159
Cdd:cd21208   79 DPTDLQdlsnrriathvrkkeDERRLKNVAITLYWLGRAAR 119
CH_LRCH cd21205
calponin homology (CH) domain found in the leucine-rich repeat and calponin homology ...
 31-154 3.50e-03

calponin homology (CH) domain found in the leucine-rich repeat and calponin homology domain-containing protein family; The leucine-rich repeat and calponin homology domain-containing protein (LRCH) family includes LRCH1-4. LRCH1, also called calponin homology domain-containing protein 1, or neuronal protein 81 (NP81), acts as a negative regulator of GTPase Cdc42 by sequestering Cdc42-guanine exchange factor DOCK8. LRCH2 may play a role in the organization of the cytoskeleton. LRCH3 is part of the DISP complex and may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. LRCH4, also called leucine-rich repeat neuronal protein 4, or leucine-rich neuronal protein, acts as a novel Toll-like receptor (TLR) accessory protein that regulates the innate immune response. Members of this family contain a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409054 [Multi-domain]  Cd Length: 107  Bit Score: 38.05  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  31 LEAMKEDLAEWLRDLYGLDIDAAnflqvLETGLVLCQHANVVTDAALAFLAEAPAQAQKIPMPRVgvscngaaqpgtfqa 110
Cdd:cd21205    3 IEQLRKSIESRLKVTLPDDLGEA-----LMDGVVLCHLANHVRPRSVPSIHVPSPAVPKLSMAKC--------------- 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119600537 111 RDNVSNFIQWCRKeMGIQEVLMFETEDLVLRKNVKNVVLCLLEL 154
Cdd:cd21205   63 RRNVENFLEACRK-LGVPEERLCSPGDILEEKGLVRVAVTVQAL 105
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
 35-158 5.37e-03

calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), also called basic calponin, or smooth muscle calponin H1, is a thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C, and tropomyosin. Calponin-1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409131 [Multi-domain]  Cd Length: 108  Bit Score: 37.55  E-value: 5.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  35 KEDLAEWLRDLYGLDIdAANFLQVLETGLVLCQHANVVTdaalaflaeaPAQAQKIpmprvgvscNGAAQpgTFQARDNV 114
Cdd:cd21282    5 EEELRVWIEGVTGRRI-GDNFMDGLKDGVILCELINKLQ----------PGSVRKI---------NESTQ--NWHKLENI 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119600537 115 SNFIQwCRKEMGIQEVLMFETEDLVLRKNVKNVVLCLLELGRRA 158
Cdd:cd21282   63 GNFIK-AIMHYGVKPHDIFEANDLFENTNHTQVQSTLIALASMA 105
CH_LMO7 cd21277
calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 ...
 41-158 7.54e-03

calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 (LMO-7), also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. It contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409126 [Multi-domain]  Cd Length: 116  Bit Score: 37.12  E-value: 7.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600537  41 WLRDLYGLDIDAANFLQVLETGLVLCQHANVVTdaalaflaeaPAQAQKIpmprvgvscNGAAQPgtFQARDNVSNFIQW 120
Cdd:cd21277    8 WIEAVTGKNFGNKDFRSALENGVLLCDLINKIK----------PGIIKKI---------NRLSTP--IAGLDNINVFLKA 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 119600537 121 CrKEMGIQEVLMF---ETEDLVLR---------KNVKNVVLCLLELGRRA 158
Cdd:cd21277   67 C-EKLGLKEAQLFhpgDLQDLSTRvtvkqeetdRRLKNVLITLYWLGRKA 115
 
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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