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Conserved domains on  [gi|4539245|emb|CAB39801|]
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fimbrin [Schizosaccharomyces pombe]

Protein Classification

fimbrin/plastin family actin filament-binding protein( domain architecture ID 11473718)

fimbrin/plastin family actin filament-binding protein similar to Saccharomyces cerevisiae fimbrin, which binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity

CATH:  1.10.418.10
Gene Ontology:  GO:0051015|GO:0051017|GO:0005509
PubMed:  32478077|12186940
SCOP:  4004022

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-614 0e+00

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


:

Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 831.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245    1 MLALKLQ----KKYPELTNEEILT-LTDQFNKLDVDGKGYLDQPTTIKAFEDSKKGSYDEVREAIREVNVDSSGRVEPED 75
Cdd:COG5069   1 MEAKKWQkvqkKTFTKWTNEKLISgGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245   76 FVG--IFNVLKKG-VEGTEVKKGRITIKGSSSSVSHTINEEErrEFIKHINSVLAGDPDVGSRVPiNTETFEFFDQCKDG 152
Cdd:COG5069  81 GKGvkLFNIGPQDiVDGNPKLILGLIWSLISRLTIATINEEG--ELTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  153 LILSKLINDSVPDTIDERVLNKQRNNKPLDNFKCIENNNVVINSAKAMGGISITNIGAGDileGREHLILgLVWQIIRRG 232
Cdd:COG5069 158 LAFSALIHDSRPDTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIPD---ERSIMTY-VSWYIIRFG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  233 LLGKIDITLHpELYRLLEEDETLDQfLRLPPEKILLRWFN-YHLKAANWPrtVSNFSKDVSDGENYTVLLNQLApELCSR 311
Cdd:COG5069 234 LLEKIDIALH-RVYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANWK--VVNFSKDVSDGENYTDLLNQLN-ALCSR 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  312 APLQTTDVLQRAEQVLQNAEKLDCRKYLTPtamvAGNPKLNLAFVAHLFNTHPGLEPLNEEEKPEIEPFDAEGEREARVF 391
Cdd:COG5069 309 APLETTDLHSLAGQILQNAEKYDCRKYLPP----AGNPKLDLAFVAHLFNTHPGQEPLEEEEKPEIEEFDAEGEFEARVF 384
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  392 TLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKIT-PNTVNWKKVNKAPASGDEMMRFKAVENCNYAVDLGKNQGFSLVGI 470
Cdd:COG5069 385 TFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLmPMTVTHKLVKKQPASGIEENRFKAFENENYAVDLGITEGFSLVGI 464
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  471 QGADITDGSRtLTLALVWQMMRMNITKTLHSLSRGGKTLSDSDMVAWANSMAAKGGKGSQIRSFRDPSIST-GVFVLDVL 549
Cdd:COG5069 465 KGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVsGVFYLDVL 543
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4539245  550 HGIKSEYVDYNLVTDGSTEELAIQNAR-LAIS--IARKLGAVIFILPEDIVAVRPRL-VLHFIGSLMAV 614
Cdd:COG5069 544 KGIHSELVDYDLVTRGFTEFDDIADARsLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLMAD 612
 
Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-614 0e+00

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 831.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245    1 MLALKLQ----KKYPELTNEEILT-LTDQFNKLDVDGKGYLDQPTTIKAFEDSKKGSYDEVREAIREVNVDSSGRVEPED 75
Cdd:COG5069   1 MEAKKWQkvqkKTFTKWTNEKLISgGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245   76 FVG--IFNVLKKG-VEGTEVKKGRITIKGSSSSVSHTINEEErrEFIKHINSVLAGDPDVGSRVPiNTETFEFFDQCKDG 152
Cdd:COG5069  81 GKGvkLFNIGPQDiVDGNPKLILGLIWSLISRLTIATINEEG--ELTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  153 LILSKLINDSVPDTIDERVLNKQRNNKPLDNFKCIENNNVVINSAKAMGGISITNIGAGDileGREHLILgLVWQIIRRG 232
Cdd:COG5069 158 LAFSALIHDSRPDTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIPD---ERSIMTY-VSWYIIRFG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  233 LLGKIDITLHpELYRLLEEDETLDQfLRLPPEKILLRWFN-YHLKAANWPrtVSNFSKDVSDGENYTVLLNQLApELCSR 311
Cdd:COG5069 234 LLEKIDIALH-RVYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANWK--VVNFSKDVSDGENYTDLLNQLN-ALCSR 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  312 APLQTTDVLQRAEQVLQNAEKLDCRKYLTPtamvAGNPKLNLAFVAHLFNTHPGLEPLNEEEKPEIEPFDAEGEREARVF 391
Cdd:COG5069 309 APLETTDLHSLAGQILQNAEKYDCRKYLPP----AGNPKLDLAFVAHLFNTHPGQEPLEEEEKPEIEEFDAEGEFEARVF 384
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  392 TLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKIT-PNTVNWKKVNKAPASGDEMMRFKAVENCNYAVDLGKNQGFSLVGI 470
Cdd:COG5069 385 TFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLmPMTVTHKLVKKQPASGIEENRFKAFENENYAVDLGITEGFSLVGI 464
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  471 QGADITDGSRtLTLALVWQMMRMNITKTLHSLSRGGKTLSDSDMVAWANSMAAKGGKGSQIRSFRDPSIST-GVFVLDVL 549
Cdd:COG5069 465 KGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVsGVFYLDVL 543
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4539245  550 HGIKSEYVDYNLVTDGSTEELAIQNAR-LAIS--IARKLGAVIFILPEDIVAVRPRL-VLHFIGSLMAV 614
Cdd:COG5069 544 KGIHSELVDYDLVTRGFTEFDDIADARsLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLMAD 612
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
253-361 1.53e-78

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


Pssm-ID: 409146  Cd Length: 109  Bit Score: 243.62  E-value: 1.53e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  253 ETLDQFLRLPPEKILLRWFNYHLKAANWPRTVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDVLQRAEQVLQNAEK 332
Cdd:cd21297   1 ETLEQFLRLPPEQILLRWFNYHLKAANWPRRVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDLLQRAEQVLQNAEK 80
                        90       100
                ....*....|....*....|....*....
gi 4539245  333 LDCRKYLTPTAMVAGNPKLNLAFVAHLFN 361
Cdd:cd21297  81 LDCRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
261-365 1.49e-21

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 90.04  E-value: 1.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245    261 LPPEKILLRWFNYHLKAANWPRTVSNFSKDVSDGENYTVLLNQLAPELC--SRAPLQTTDVLQRAEQVLQNAE-KLDCRK 337
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVdkKKLNKSEFDKLENINLALDVAEkKLGVPK 80
                          90       100
                  ....*....|....*....|....*....
gi 4539245    338 YL-TPTAMVAGNPKLNLAFVAHLFNTHPG 365
Cdd:pfam00307  81 VLiEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
116-231 9.03e-19

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 81.59  E-value: 9.03e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245     116 REFIKHINSVLAGDPDVGsrvpinteTFEFFDQCKDGLILSKLINDSVPDTIDERVLNKQRNnkpldNFKCIENNNVVIN 195
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPP--------VTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLS-----RFKKIENINLALS 67
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 4539245     196 SAKAMGGIsITNIGAGDILEGReHLILGLVWQIIRR 231
Cdd:smart00033  68 FAEKLGGK-VVLFEPEDLVEGP-KLILGVIWTLISL 101
PTZ00183 PTZ00183
centrin; Provisional
8-119 1.84e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.37  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245     8 KKYPELTNEEILTLTDQFNKLDVDGKGYLDqPTTIKA------FEdSKKgsyDEVREAIREVNVDSSGRVEPEDFVGIFN 81
Cdd:PTZ00183   6 SERPGLTEDQKKEIREAFDLFDTDGSGTID-PKELKVamrslgFE-PKK---EEIKQMIADVDKDGSGKIDFEEFLDIMT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4539245    82 V-LKKGVEGTEVKK----------GRITIKG---SSSSVSHTINEEERREFI 119
Cdd:PTZ00183  81 KkLGERDPREEILKafrlfdddktGKISLKNlkrVAKELGETITDEELQEMI 132
 
Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-614 0e+00

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 831.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245    1 MLALKLQ----KKYPELTNEEILT-LTDQFNKLDVDGKGYLDQPTTIKAFEDSKKGSYDEVREAIREVNVDSSGRVEPED 75
Cdd:COG5069   1 MEAKKWQkvqkKTFTKWTNEKLISgGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245   76 FVG--IFNVLKKG-VEGTEVKKGRITIKGSSSSVSHTINEEErrEFIKHINSVLAGDPDVGSRVPiNTETFEFFDQCKDG 152
Cdd:COG5069  81 GKGvkLFNIGPQDiVDGNPKLILGLIWSLISRLTIATINEEG--ELTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  153 LILSKLINDSVPDTIDERVLNKQRNNKPLDNFKCIENNNVVINSAKAMGGISITNIGAGDileGREHLILgLVWQIIRRG 232
Cdd:COG5069 158 LAFSALIHDSRPDTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIPD---ERSIMTY-VSWYIIRFG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  233 LLGKIDITLHpELYRLLEEDETLDQfLRLPPEKILLRWFN-YHLKAANWPrtVSNFSKDVSDGENYTVLLNQLApELCSR 311
Cdd:COG5069 234 LLEKIDIALH-RVYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANWK--VVNFSKDVSDGENYTDLLNQLN-ALCSR 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  312 APLQTTDVLQRAEQVLQNAEKLDCRKYLTPtamvAGNPKLNLAFVAHLFNTHPGLEPLNEEEKPEIEPFDAEGEREARVF 391
Cdd:COG5069 309 APLETTDLHSLAGQILQNAEKYDCRKYLPP----AGNPKLDLAFVAHLFNTHPGQEPLEEEEKPEIEEFDAEGEFEARVF 384
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  392 TLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKIT-PNTVNWKKVNKAPASGDEMMRFKAVENCNYAVDLGKNQGFSLVGI 470
Cdd:COG5069 385 TFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLmPMTVTHKLVKKQPASGIEENRFKAFENENYAVDLGITEGFSLVGI 464
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  471 QGADITDGSRtLTLALVWQMMRMNITKTLHSLSRGGKTLSDSDMVAWANSMAAKGGKGSQIRSFRDPSIST-GVFVLDVL 549
Cdd:COG5069 465 KGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVsGVFYLDVL 543
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4539245  550 HGIKSEYVDYNLVTDGSTEELAIQNAR-LAIS--IARKLGAVIFILPEDIVAVRPRL-VLHFIGSLMAV 614
Cdd:COG5069 544 KGIHSELVDYDLVTRGFTEFDDIADARsLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLMAD 612
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
253-361 1.53e-78

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


Pssm-ID: 409146  Cd Length: 109  Bit Score: 243.62  E-value: 1.53e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  253 ETLDQFLRLPPEKILLRWFNYHLKAANWPRTVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDVLQRAEQVLQNAEK 332
Cdd:cd21297   1 ETLEQFLRLPPEQILLRWFNYHLKAANWPRRVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDLLQRAEQVLQNAEK 80
                        90       100
                ....*....|....*....|....*....
gi 4539245  333 LDCRKYLTPTAMVAGNPKLNLAFVAHLFN 361
Cdd:cd21297  81 LDCRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
380-499 5.65e-78

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


Pssm-ID: 409149  Cd Length: 119  Bit Score: 242.71  E-value: 5.65e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  380 FDAEGEREARVFTLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKAPASgDEMMRFKAVENCNYAVDL 459
Cdd:cd21300   1 FDAEGEREARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPAS-AEISRFKAVENTNYAVEL 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4539245  460 GKNQGFSLVGIQGADITDGSRTLTLALVWQMMRMNITKTL 499
Cdd:cd21300  80 GKQLGFSLVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
108-232 4.13e-74

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 232.72  E-value: 4.13e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  108 HTINEEERREFIKHINSVLAGDPDVGSRVPINTETFEFFDQCKDGLILSKLINDSVPDTIDERVLNKQ-RNNKPLDNFKC 186
Cdd:cd21294   1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPpRKNKPLNNFQM 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4539245  187 IENNNVVINSAKAMGGiSITNIGAGDILEGREHLILGLVWQIIRRG 232
Cdd:cd21294  81 IENNNIVINSAKAIGC-SVVNIGAGDIIEGREHLILGLIWQIIRRG 125
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
506-613 3.61e-63

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


Pssm-ID: 409152  Cd Length: 108  Bit Score: 203.43  E-value: 3.61e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  506 GKTLSDSDMVAWANSMAAKGGKGSQIRSFRDPSISTGVFVLDVLHGIKSEYVDYNLVTDGSTEELAIQNARLAISIARKL 585
Cdd:cd21303   1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLVTPGNTEDEAYLNAKLAISIARKL 80
                        90       100
                ....*....|....*....|....*...
gi 4539245  586 GAVIFILPEDIVAVRPRLVLHFIGSLMA 613
Cdd:cd21303  81 GALIFLVPEDIVEVRPRLVLTFIGSLMA 108
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
383-499 3.72e-58

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 190.57  E-value: 3.72e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  383 EGEREARVFTLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKAPAsgdeMMRFKAVENCNYAVDLGKN 462
Cdd:cd21219   1 EGSREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNKPKP----LNKFKKVENCNYAVDLAKK 76
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 4539245  463 QGFSLVGIQGADITDGSRTLTLALVWQMMRMNITKTL 499
Cdd:cd21219  77 LGFSLVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
251-361 2.42e-53

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


Pssm-ID: 409144  Cd Length: 113  Bit Score: 177.85  E-value: 2.42e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  251 EDETLDQFLRLPPEKILLRWFNYHLKAANWPRTVSNFSKDVSDGENYTVLLNQLAPELCSRAP--LQTTDVLQRAEQVLQ 328
Cdd:cd21295   1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRRIKNFSGDIKDSEAYTHLLKQIAPKDAGVDTsaLRESDLLQRAELMLQ 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 4539245  329 NAEKLDCRKYLTPTAMVAGNPKLNLAFVAHLFN 361
Cdd:cd21295  81 NADKIGCRKFVTPKDVVTGNPKLNLAFVANLFN 113
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
509-613 2.61e-51

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


Pssm-ID: 409069  Cd Length: 105  Bit Score: 172.07  E-value: 2.61e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  509 LSDSDMVAWANSMAAKGGKGSQIRSFRDPSISTGVFVLDVLHGIKSEYVDYNLVTDGSTEELAIQNARLAISIARKLGAV 588
Cdd:cd21220   1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLVTEGETDEEKEQNAKYAISLARKIGAV 80
                        90       100
                ....*....|....*....|....*
gi 4539245  589 IFILPEDIVAVRPRLVLHFIGSLMA 613
Cdd:cd21220  81 IFLLWEDIVEVKPKMILTFVASLMA 105
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
113-230 9.62e-51

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 170.83  E-value: 9.62e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  113 EERREFIKHINSVLAGDPDVGSRVPINTETFEFFDQCKDGLILSKLINDSVPDTIDERVLNKQrnnKPLDNFKCIENNNV 192
Cdd:cd21217   1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKK---KPKNIFEATENLNL 77
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4539245  193 VINSAKAMgGISITNIGAGDILEGREHLILGLVWQIIR 230
Cdd:cd21217  78 ALNAAKKI-GCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
383-499 5.05e-49

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 166.26  E-value: 5.05e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  383 EGE-REARVFTLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKAPASGDEMMrfKAVENCNYAVDLGK 461
Cdd:cd21298   2 IEEtREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGANM--KKIENCNYAVELGK 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4539245  462 NQGFSLVGIQGADITDGSRTLTLALVWQMMRMNITKTL 499
Cdd:cd21298  80 KLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLSIL 117
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
88-239 3.90e-46

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


Pssm-ID: 409141  Cd Length: 145  Bit Score: 159.75  E-value: 3.90e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245   88 EGTEVKKGriTIKGSSSSVSHTINEEERREFIKHINSVLAGDPDVGSRVPINTETFEFFDQCKDGLILSKLINDSVPDTI 167
Cdd:cd21292   1 EGIDAKGG--TSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTI 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4539245  168 DERVLNKqrnnKPLDNFKCIENNNVVINSAKAMgGISITNIGAGDILEGREHLILGLVWQIIRRGLLGKIDI 239
Cdd:cd21292  79 DERAINK----KKLTVFTIHENLTLALNSASAI-GCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
253-360 9.91e-46

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


Pssm-ID: 409145  Cd Length: 109  Bit Score: 157.29  E-value: 9.91e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  253 ETLDQFLRLPPEKILLRWFNYHLKAANWPRTVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDVLQRAEQVLQNAEK 332
Cdd:cd21296   1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKTVTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEK 80
                        90       100
                ....*....|....*....|....*...
gi 4539245  333 LDCRKYLTPTAMVAGNPKLNLAFVAHLF 360
Cdd:cd21296  81 MNCKRYLTAKDIVEGSANLNLAFVAQIF 108
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
253-361 5.96e-44

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: 152.45  E-value: 5.96e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  253 ETLDQFLRLPPEKILLRWFNYHLKAANWPR-TVSNFSKDVSDGENYTVLLNQLAPELCS----RAPLQTTDVLQRAEQVL 327
Cdd:cd21218   1 ETLESLLYLPPEEILLRWVNYHLKKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVL 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 4539245  328 QNAEKLDCRKYLTPTAMVAGNPKLNLAFVAHLFN 361
Cdd:cd21218  81 QAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
97-239 2.51e-38

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 138.25  E-value: 2.51e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245   97 ITIKGSSSSVS-----HTINEEERREFIKHINSVLAGDPDVGSRVPINTETFEFFDQCKDGLILSKLINDSVPDTIDERV 171
Cdd:cd21323   3 ITAIGGTSAISsegtqHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDERA 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4539245  172 LNKqrnnKPLDNFKCIENNNVVINSAKAMgGISITNIGAGDILEGREHLILGLVWQIIRRGLLGKIDI 239
Cdd:cd21323  83 INK----KKLTPFTISENLNLALNSASAI-GCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
383-499 3.88e-37

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


Pssm-ID: 409148  Cd Length: 114  Bit Score: 133.78  E-value: 3.88e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  383 EGEREARVFTLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKAPASgdemMRFKAVENCNYAVDLGKN 462
Cdd:cd21299   1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIK----MPFKKVENCNQVVKIGKQ 76
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 4539245  463 QGFSLVGIQGADITDGSRTLTLALVWQMMRMNITKTL 499
Cdd:cd21299  77 LKFSLVNVAGNDIVQGNKKLILALLWQLMRYHMLQLL 113
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
251-364 5.71e-36

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


Pssm-ID: 409175  Cd Length: 121  Bit Score: 131.16  E-value: 5.71e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  251 EDETLDQFLRLPPEKILLRWFNYHLKAANWpRTVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDV--------LQR 322
Cdd:cd21326   1 EGEELEELMKLSPEELLLRWVNYHLTNAGW-QNISNFSQDIKDSRAYFHLLNQIAPKGDVFDENIEIDFsgfnekndLKR 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4539245  323 AEQVLQNAEKLDCRKYLTPTAMVAGNPKLNLAFVAHLFNTHP 364
Cdd:cd21326  80 AEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 121
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
509-614 5.93e-35

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


Pssm-ID: 409150  Cd Length: 107  Bit Score: 127.78  E-value: 5.93e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  509 LSDSDMVAWANSMAAKGGKGSQIRSFRDPSISTGVFVLDVLHGIKSEYVDYNLVTDGSTEELAIQNARLAISIARKLGAV 588
Cdd:cd21301   1 ISDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLVLEGNSEEDKLSNAKYAISMARKIGAR 80
                        90       100
                ....*....|....*....|....*.
gi 4539245  589 IFILPEDIVAVRPRLVLHFIGSLMAV 614
Cdd:cd21301  81 VYALPEDIVEVKPKMVMTVFACLMAL 106
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
248-364 5.97e-35

second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contaisn 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: 409176  Cd Length: 125  Bit Score: 128.15  E-value: 5.97e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  248 LLEEDETLDQFLRLPPEKILLRWFNYHLKAANWPRtVSNFSKDVSDGENYTVLLNQLAPE---------LCSRAPLQTTD 318
Cdd:cd21327   1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNK-INNFSSDIKDSKAYYHLLNQVAPKgdeegipaiVIDMSGLREKD 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4539245  319 VLQRAEQVLQNAEKLDCRKYLTPTAMVAGNPKLNLAFVAHLFNTHP 364
Cdd:cd21327  80 DLKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
248-361 1.23e-34

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


Pssm-ID: 409177 [Multi-domain]  Cd Length: 122  Bit Score: 127.39  E-value: 1.23e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  248 LLEEDETLDQFLRLPPEKILLRWFNYHLKAANWPRtVSNFSKDVSDGENYTVLLNQLAPE---------LCSRAPLQTTD 318
Cdd:cd21328   1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQK-INNFSSDIKDSRAYFHLLNQIAPKgqkegepriDINMSGFNEKD 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 4539245  319 VLQRAEQVLQNAEKLDCRKYLTPTAMVAGNPKLNLAFVAHLFN 361
Cdd:cd21328  80 DLKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
383-492 1.31e-33

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 124.33  E-value: 1.31e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  383 EGE-REARVFTLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKiTPNTVNWKKVNKAP--ASGDEMmrfKAVENCNYAVDL 459
Cdd:cd21329   2 EGEsSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEM-TRVPVDWGHVNKPPypALGGNM---KKIENCNYAVEL 77
                        90       100       110
                ....*....|....*....|....*....|....
gi 4539245  460 GKNQG-FSLVGIQGADITDGSRTLTLALVWQMMR 492
Cdd:cd21329  78 GKNKAkFSLVGIAGSDLNEGNKTLTLALIWQLMR 111
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
373-492 1.60e-33

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 124.73  E-value: 1.60e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  373 EKPEIEPFD---AEGE-REARVFTLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKI-TPntVNWKKVNKAPAS--GDEMm 445
Cdd:cd21331   5 TKPENQDIDwtlLEGEtREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIkVP--VDWNKVNKPPYPklGANM- 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 4539245  446 rfKAVENCNYAVDLGKNQG-FSLVGIQGADITDGSRTLTLALVWQMMR 492
Cdd:cd21331  82 --KKLENCNYAVELGKHPAkFSLVGIGGQDLNDGNPTLTLALVWQLMR 127
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
114-230 2.35e-32

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


Pssm-ID: 409142  Cd Length: 116  Bit Score: 120.71  E-value: 2.35e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  114 ERREFIKHINSVLAGDPDVGSRVPINTETFEFFDQCKDGLILSKLINDSVPDTIDERVLNKQRNNKPLDNfkcIENNNVV 193
Cdd:cd21293   2 EKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKKVLNPWER---NENHTLC 78
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 4539245  194 INSAKAMgGISITNIGAGDILEGREHLILGLVWQIIR 230
Cdd:cd21293  79 LNSAKAI-GCSVVNIGTQDLAEGRPHLVLGLISQIIK 114
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
102-240 5.40e-32

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


Pssm-ID: 409174  Cd Length: 148  Bit Score: 120.93  E-value: 5.40e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  102 SSSSVSHTINEEERREFIKHINSVLAGDPDVGSRVPINTETFEFFDQCKDGLILSKLINDSVPDTIDERVLNKqrnnKPL 181
Cdd:cd21325  13 SSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINK----KKL 88
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4539245  182 DNFKCIENNNVVINSAKAMgGISITNIGAGDILEGREHLILGLVWQIIRRGLLGKIDIT 240
Cdd:cd21325  89 TPFIIQENLNLALNSASAI-GCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
98-239 8.31e-32

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


Pssm-ID: 409173  Cd Length: 145  Bit Score: 120.11  E-value: 8.31e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245   98 TIKGSSSSVSHTINEEERREFIKHINSVLAGDPDVGSRVPINTETFEFFDQCKDGLILSKLINDSVPDTIDERVLNKqrn 177
Cdd:cd21324   9 TSEQSSAGTQHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINK--- 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4539245  178 nKPLDNFKCIENNNVVINSAKAMgGISITNIGAGDILEGREHLILGLVWQIIRRGLLGKIDI 239
Cdd:cd21324  86 -KKLTPFTIQENLNLALNSASAI-GCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
383-492 1.56e-31

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 118.94  E-value: 1.56e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  383 EGE-REARVFTLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKITPnTVNWKKVNKAPAS--GDEMmrfKAVENCNYAVDL 459
Cdd:cd21330   9 EGEtREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKV-PVDWNRVNKPPYPklGENM---KKLENCNYAVEL 84
                        90       100       110
                ....*....|....*....|....*....|....
gi 4539245  460 GKNQG-FSLVGIQGADITDGSRTLTLALVWQMMR 492
Cdd:cd21330  85 GKNKAkFSLVGIAGQDLNEGNRTLTLALIWQLMR 118
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
509-612 8.65e-30

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


Pssm-ID: 409151  Cd Length: 109  Bit Score: 113.42  E-value: 8.65e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  509 LSDSDMVAWANSMAAKGGKGSQIRSFRDPSISTGVFVLDVLHGIKSEYVDYNLVTDGSTEELAIQNARLAISIARKLGAV 588
Cdd:cd21302   2 MTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGETDEEKRLNATYIISVARKLGCS 81
                        90       100
                ....*....|....*....|....
gi 4539245  589 IFILPEDIVAVRPRLVLHFIGSLM 612
Cdd:cd21302  82 IFLLPEDIVEVNQKMILILTASIM 105
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
505-613 1.21e-25

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


Pssm-ID: 409182  Cd Length: 115  Bit Score: 101.61  E-value: 1.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  505 GGKTLSDSDMVAWANSMAAKGGKGSQIRSFRDPSISTGVFVLDVLHGIKSEYVDYNLV-TDGSTEELAIQNARLAISIAR 583
Cdd:cd21333   2 GGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLkTEDLNDEEKLNNAKYAISMAR 81
                        90       100       110
                ....*....|....*....|....*....|
gi 4539245  584 KLGAVIFILPEDIVAVRPRLVLHFIGSLMA 613
Cdd:cd21333  82 KIGARVYALPEDLVEVKPKMVMTVFACLMG 111
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
510-612 1.11e-22

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


Pssm-ID: 409183  Cd Length: 112  Bit Score: 93.41  E-value: 1.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  510 SDSDMVAWANSMAAKGGKGSQIRSFRDPSISTGVFVLDVLHGIKSEYVDYNLVTDGS-TEELAIQNARLAISIARKLGAV 588
Cdd:cd21334   2 NDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNlTDDDKLDNAKYAVSMARKIGAR 81
                        90       100
                ....*....|....*....|....
gi 4539245  589 IFILPEDIVAVRPRLVLHFIGSLM 612
Cdd:cd21334  82 VYALPEDLVEVKPKMVMTVFACLM 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
261-365 1.49e-21

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 90.04  E-value: 1.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245    261 LPPEKILLRWFNYHLKAANWPRTVSNFSKDVSDGENYTVLLNQLAPELC--SRAPLQTTDVLQRAEQVLQNAE-KLDCRK 337
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVdkKKLNKSEFDKLENINLALDVAEkKLGVPK 80
                          90       100
                  ....*....|....*....|....*....
gi 4539245    338 YL-TPTAMVAGNPKLNLAFVAHLFNTHPG 365
Cdd:pfam00307  81 VLiEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
385-496 2.52e-20

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: 86.57  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245    385 EREARVFTLWLNSL----DVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKAPasgdemmrFKAVENCNYAVDLG 460
Cdd:pfam00307   1 LELEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE--------FDKLENINLALDVA 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 4539245    461 KNQ-GFSLVGIQGADITDGSRTLTLALVWQMMRMNIT 496
Cdd:pfam00307  73 EKKlGVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
112-232 7.21e-20

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: 85.03  E-value: 7.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245    112 EEERREFIKHINSVLAGDpdvGSRVPINtetfEFFDQCKDGLILSKLINDSVPDTIDERVLNKQRnnkpldnFKCIENNN 191
Cdd:pfam00307   1 LELEKELLRWINSHLAEY---GPGVRVT----NFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE-------FDKLENIN 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 4539245    192 VVINSAKAMGGISITNIGAGDILEGREHLILGLVWQIIRRG 232
Cdd:pfam00307  67 LALDVAEKKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
505-612 1.11e-19

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


Pssm-ID: 409181  Cd Length: 115  Bit Score: 85.00  E-value: 1.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  505 GGKTLSDSDMVAWANSMAAKGGKGSQIRSFRDPSISTGVFVLDVLHGIKSEYVDYNLVT-DGSTEELAIQNARLAISIAR 583
Cdd:cd21332   4 EGEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKrEDLSDADKLNNAKYAISVAR 83
                        90       100
                ....*....|....*....|....*....
gi 4539245  584 KLGAVIFILPEDIVAVRPRLVLHFIGSLM 612
Cdd:cd21332  84 KIGARVYALPEDLVEVKPKMVMTVFACLM 112
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
116-231 9.03e-19

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 81.59  E-value: 9.03e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245     116 REFIKHINSVLAGDPDVGsrvpinteTFEFFDQCKDGLILSKLINDSVPDTIDERVLNKQRNnkpldNFKCIENNNVVIN 195
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPP--------VTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLS-----RFKKIENINLALS 67
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 4539245     196 SAKAMGGIsITNIGAGDILEGReHLILGLVWQIIRR 231
Cdd:smart00033  68 FAEKLGGK-VVLFEPEDLVEGP-KLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
389-493 3.23e-18

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 80.05  E-value: 3.23e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245     389 RVFTLWLNSL---DVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKAPasgdemMRFKAVENCNYAVDLGKNQGF 465
Cdd:smart00033   1 KTLLRWVNSLlaeYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL------SRFKKIENINLALSFAEKLGG 74
                           90       100
                   ....*....|....*....|....*...
gi 4539245     466 SLVGIQGADITDGSRtLTLALVWQMMRM 493
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
112-237 1.37e-17

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 78.86  E-value: 1.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  112 EEERREFIKHINSVlagdpDVGSRVPIntetfeFFDQCKDGLILSKLINDSVPDTIDERVLNKqrnNKPLDNFKCIENNN 191
Cdd:cd21219   3 SREERAFRMWLNSL-----GLDPLINN------LYEDLRDGLVLLQVLDKIQPGCVNWKKVNK---PKPLNKFKKVENCN 68
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4539245  192 VVINSAKAMGgISITNIGAGDILEGREHLILGLVWQIIRRGLLGKI 237
Cdd:cd21219  69 YAVDLAKKLG-FSLVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
387-492 5.00e-17

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 77.23  E-value: 5.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  387 EARVFTLWLNS-----------LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKAPASGDemmrFKAVENCNY 455
Cdd:cd21217   2 EKEAFVEHINSlladdpdlkhlLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKNI----FEATENLNL 77
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 4539245  456 AVDLGKNQGFSLVGIQGADITDGSRTLTLALVWQMMR 492
Cdd:cd21217  78 ALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
112-234 2.03e-16

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


Pssm-ID: 409149  Cd Length: 119  Bit Score: 75.54  E-value: 2.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  112 EEERREFIKHINSvLAGDPDVGSrvpintetfeFFDQCKDGLILSKLINDSVPDTIDERVLNKQRNNKPLDNFKCIENNN 191
Cdd:cd21300   6 EREARVFTLWLNS-LDVEPAVND----------LFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPASAEISRFKAVENTN 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 4539245  192 VVINSAKAMgGISITNIGAGDILEGREHLILGLVWQIIRRGLL 234
Cdd:cd21300  75 YAVELGKQL-GFSLVGIQGADITDGSRTLTLALVWQLMRFHIT 116
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
265-360 3.22e-15

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 71.58  E-value: 3.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245     265 KILLRWFNYHLKAANWPrTVSNFSKDVSDGENYTVLLNQLAPELCS----RAPLQTTDVLQRAEQVLQNAEKL-DCRKYL 339
Cdd:smart00033   1 KTLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVDkkkvAASLSRFKKIENINLALSFAEKLgGKVVLF 79
                           90       100
                   ....*....|....*....|.
gi 4539245     340 TPTAMVAGnPKLNLAFVAHLF 360
Cdd:smart00033  80 EPEDLVEG-PKLILGVIWTLI 99
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
115-230 4.99e-15

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 71.22  E-value: 4.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  115 RREFIKHINSVLAGDPDVGSRvpintetfEFFDQCKDGLILSKLINDSVPDTIDErvlnkqRNNKPLDNFKCIENNNVVI 194
Cdd:cd00014   1 EEELLKWINEVLGEELPVSIT--------DLFESLRDGVLLCKLINKLSPGSIPK------INKKPKSPFKKRENINLFL 66
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 4539245  195 NSAKAMGGISITNIGAGDILEGR-EHLILGLVWQIIR 230
Cdd:cd00014  67 NACKKLGLPELDLFEPEDLYEKGnLKKVLGTLWALAL 103
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
151-231 2.38e-14

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 69.57  E-value: 2.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  151 DGLILSKLIndsvpDTIDERVLNKQRNNKPLD----NFKCIENNNVVINSAKAMGgISITNIGAGDILEGREHLILGLVW 226
Cdd:cd21298  33 DGLVLLQLY-----DKIKPGVVDWSRVNKPFKklgaNMKKIENCNYAVELGKKLK-FSLVGIGGKDIYDGNRTLTLALVW 106

                ....*
gi 4539245  227 QIIRR 231
Cdd:cd21298 107 QLMRA 111
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
513-614 1.45e-13

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: 66.93  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245    513 DMVAWANSMAAKGGKGSQIRSFRDpSISTGVFVLDVLHGIKSEYVDYNLVTDgsTEELAIQNARLAISIAR-KLGA-VIF 590
Cdd:pfam00307   6 ELLRWINSHLAEYGPGVRVTNFTT-DLRDGLALCALLNKLAPGLVDKKKLNK--SEFDKLENINLALDVAEkKLGVpKVL 82
                          90       100
                  ....*....|....*....|....
gi 4539245    591 ILPEDIVAVRPRLVLHFIGSLMAV 614
Cdd:pfam00307  83 IEPEDLVEGDNKSVLTYLASLFRR 106
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
385-492 9.89e-13

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 65.16  E-value: 9.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  385 EREARVFTLWLNS-----------LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKAPASGDEMMRFKAVENC 453
Cdd:cd21294   5 EDERREFTKHINAvlagdpdvgsrLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPPRKNKPLNNFQMIENN 84
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 4539245  454 NYAVDLGKNQGFSLVGIQGADITDGSRTLTLALVWQMMR 492
Cdd:cd21294  85 NIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIR 123
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
384-488 1.27e-10

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: 58.92  E-value: 1.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  384 GEREA---RVFTLWLNS--LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVnwkkvnKAPASGDemMRFKAVENCNYAVD 458
Cdd:cd21246  11 DEREAvqkKTFTKWVNShlARVGCRINDLYTDLRDGRMLIKLLEVLSGERL------PKPTKGK--MRIHCLENVDKALQ 82
                        90       100       110
                ....*....|....*....|....*....|
gi 4539245  459 LGKNQGFSLVGIQGADITDGSRTLTLALVW 488
Cdd:cd21246  83 FLKEQRVHLENMGSHDIVDGNHRLTLGLIW 112
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
381-491 1.63e-10

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: 59.23  E-value: 1.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  381 DAEGEREARVFTLWLNS--LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKvnkapasgdEMMRFKAVENCNYAVD 458
Cdd:cd21236  12 DERDKVQKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREK---------GRMRFHRLQNVQIALD 82
                        90       100       110
                ....*....|....*....|....*....|...
gi 4539245  459 LGKNQGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21236  83 YLKRRQVKLVNIRNDDITDGNPKLTLGLIWTII 115
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
385-491 2.12e-10

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: 58.91  E-value: 2.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  385 EREA---RVFTLWLNS--LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVnwkkvnKAPASGdeMMRFKAVENCNYAVDL 459
Cdd:cd21317  27 EREAvqkKTFTKWVNShlARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQL------PKPTKG--RMRIHCLENVDKALQF 98
                        90       100       110
                ....*....|....*....|....*....|..
gi 4539245  460 GKNQGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21317  99 LKEQKVHLENMGSHDIVDGNHRLTLGLIWTII 130
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
389-488 4.46e-10

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 57.01  E-value: 4.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  389 RVFTLWLNSL--DVTPSIHDFFNNLRDGLILLQAYDKITPNTVnwkkvnkaPASGDEMMRFKAVENCNYAVDLGKNQGFS 466
Cdd:cd21214   8 KTFTAWCNSHlrKAGTQIENIEEDFRDGLKLMLLLEVISGERL--------PKPERGKMRFHKIANVNKALDFIASKGVK 79
                        90       100
                ....*....|....*....|..
gi 4539245  467 LVGIQGADITDGSRTLTLALVW 488
Cdd:cd21214  80 LVSIGAEEIVDGNLKMTLGMIW 101
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
389-488 5.22e-10

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: 57.03  E-value: 5.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  389 RVFTLWLNS--LDVTPSIHDFFNNLRDG---LILLQAYdkitpntvnwkkvnkapaSGDEM------MRFKAVENCNYAV 457
Cdd:cd21188   6 KTFTKWVNKhlIKARRRVVDLFEDLRDGhnlISLLEVL------------------SGESLprergrMRFHRLQNVQTAL 67
                        90       100       110
                ....*....|....*....|....*....|.
gi 4539245  458 DLGKNQGFSLVGIQGADITDGSRTLTLALVW 488
Cdd:cd21188  68 DFLKYRKIKLVNIRAEDIVDGNPKLTLGLIW 98
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
389-488 5.94e-10

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: 56.64  E-value: 5.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  389 RVFTLWLNS-LDVT-PSIHDFFNNLRDGLILLQAYDKITPNTVNwkKVNKAPAsgdemMRFKAVENCNYAVDLGKNQGFS 466
Cdd:cd21215   7 KTFTKWLNTkLSSRgLSITDLVTDLSDGVRLIQLLEIIGDESLG--RYNKNPK-----MRVQKLENVNKALEFIKSRGVK 79
                        90       100
                ....*....|....*....|..
gi 4539245  467 LVGIQGADITDGSRTLTLALVW 488
Cdd:cd21215  80 LTNIGAEDIVDGNLKLILGLLW 101
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
385-491 7.69e-10

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: 57.34  E-value: 7.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  385 EREA---RVFTLWLNS--LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVnwkkvnKAPASGdeMMRFKAVENCNYAVDL 459
Cdd:cd21318  34 EREAvqkKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLEVLSGEQL------PKPTRG--RMRIHSLENVDKALQF 105
                        90       100       110
                ....*....|....*....|....*....|..
gi 4539245  460 GKNQGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21318 106 LKEQRVHLENVGSHDIVDGNHRLTLGLIWTII 137
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
389-488 1.05e-09

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: 56.24  E-value: 1.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  389 RVFTLWLNSLDV---TPSIHDFFNNLRDGLILLQAYDKITPNTVNwkkvnkaPASGDemMRFKAVENCNYAVDLGKNQGF 465
Cdd:cd21186   5 KTFTKWINSQLSkanKPPIKDLFEDLRDGTRLLALLEVLTGKKLK-------PEKGR--MRVHHLNNVNRALQVLEQNNV 75
                        90       100
                ....*....|....*....|...
gi 4539245  466 SLVGIQGADITDGSRTLTLALVW 488
Cdd:cd21186  76 KLVNISSNDIVDGNPKLTLGLVW 98
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
146-234 1.31e-09

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


Pssm-ID: 409148  Cd Length: 114  Bit Score: 55.97  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  146 FDQCKDGLILSKLINDSVPDTIDERVLNKQRNNKPldnFKCIENNNVVINSAKAMGgISITNIGAGDILEGREHLILGLV 225
Cdd:cd21299  26 FEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMP---FKKVENCNQVVKIGKQLK-FSLVNVAGNDIVQGNKKLILALL 101

                ....*....
gi 4539245  226 WQIIRRGLL 234
Cdd:cd21299 102 WQLMRYHML 110
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
385-491 1.69e-09

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: 55.70  E-value: 1.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  385 ERE---ARVFTLWLNSLDVT---PSIHDFFNNLRDGLILLQAYDKITPntvnwKKVNKAPASgdemMRFKAVENCNYAVD 458
Cdd:cd21231   2 EREdvqKKTFTKWINAQFAKfgkPPIEDLFTDLQDGRRLLELLEGLTG-----QKLVKEKGS----TRVHALNNVNKALQ 72
                        90       100       110
                ....*....|....*....|....*....|...
gi 4539245  459 LGKNQGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21231  73 VLQKNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
385-495 2.23e-09

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 56.21  E-value: 2.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  385 EREARVFTLWLNS-----------LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKapasgDEMMRFKAVENC 453
Cdd:cd21323  23 EEEKVAFVNWINKalegdpdckhvVPMNPTDESLFKSLADGILLCKMINLSQPDTIDERAINK-----KKLTPFTISENL 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4539245  454 NYAVDLGKNQGFSLVGIQGADITDGSRTLTLALVWQMMRMNI 495
Cdd:cd21323  98 NLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGL 139
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
517-613 3.47e-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: 54.24  E-value: 3.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245     517 WANSMAAKGGKGSqIRSFRDpSISTGVFVLDVLHGIKSEYVDYNLVTDGSTEELAIQNARLAISIARKLG-AVIFILPED 595
Cdd:smart00033   6 WVNSLLAEYDKPP-VTNFSS-DLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGgKVVLFEPED 83
                           90
                   ....*....|....*...
gi 4539245     596 IVAVRPrLVLHFIGSLMA 613
Cdd:smart00033  84 LVEGPK-LILGVIWTLIS 100
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
385-493 1.23e-08

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


Pssm-ID: 409141  Cd Length: 145  Bit Score: 54.21  E-value: 1.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  385 EREARVFTLWLNS-----------LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKAPASgdemmRFKAVENC 453
Cdd:cd21292  23 EEEKVAFVNWINKnlgddpdckhlLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDERAINKKKLT-----VFTIHENL 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4539245  454 NYAVDLGKNQGFSLVGIQGADITDGSRTLTLALVWQMMRM 493
Cdd:cd21292  98 TLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRI 137
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
262-349 2.08e-08

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


Pssm-ID: 409033  Cd Length: 103  Bit Score: 52.24  E-value: 2.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  262 PPEKILLRWFNYHLKaanwPRTVSNFSKDVSDGENYTVLLNQLAPELCSR-APLQTTDVLQRAEQVLQNAE-KLDCRKYL 339
Cdd:cd21184   1 SGKSLLLEWVNSKIP----EYKVKNFTTDWNDGKALAALVDALKPGLIPDnESLDKENPLENATKAMDIAEeELGIPKII 76
                        90
                ....*....|
gi 4539245  340 TPTAMVAGNP 349
Cdd:cd21184  77 TPEDMVSPNV 86
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
381-491 2.95e-08

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: 52.33  E-value: 2.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  381 DAEGEREARVFTLWLNS--LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKvnkapasgdEMMRFKAVENCNYAVD 458
Cdd:cd21235   1 DERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---------GRMRFHKLQNVQIALD 71
                        90       100       110
                ....*....|....*....|....*....|...
gi 4539245  459 LGKNQGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21235  72 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 104
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
387-491 3.01e-08

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: 51.93  E-value: 3.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  387 EARVFTLWLN---SLDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKapasgdemmRFKAVENCNYAVDLGKNQ 463
Cdd:cd21232   3 QKKTFTKWINarfSKSGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGST---------RVHALNNVNRVLQVLHQN 73
                        90       100
                ....*....|....*....|....*...
gi 4539245  464 GFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21232  74 NVELVNIGGTDIVDGNHKLTLGLLWSII 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
389-492 5.88e-08

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: 50.80  E-value: 5.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  389 RVFTLWLNSL---DVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKapasgdeMMRFKAVENCNYAVDLGKNQGF 465
Cdd:cd00014   2 EELLKWINEVlgeELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKP-------KSPFKKRENINLFLNACKKLGL 74
                        90       100
                ....*....|....*....|....*....
gi 4539245  466 -SLVGIQGADIT-DGSRTLTLALVWQMMR 492
Cdd:cd00014  75 pELDLFEPEDLYeKGNLKKVLGTLWALAL 103
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
385-488 6.28e-08

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: 51.14  E-value: 6.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  385 EREA---RVFTLWLNSL--DVTPSIHDFFNNLRDGLILLQAYDKITPNTVNwkkvnkAPASGdeMMRFKAVENCNYAVDL 459
Cdd:cd21193  12 ERINiqkKTFTKWINSFleKANLEIGDLFTDLSDGKLLLKLLEIISGEKLG------KPNRG--RLRVQKIENVNKALAF 83
                        90       100
                ....*....|....*....|....*....
gi 4539245  460 GKNQgFSLVGIQGADITDGSRTLTLALVW 488
Cdd:cd21193  84 LKTK-VRLENIGAEDIVDGNPRLILGLIW 111
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
381-491 6.60e-08

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409086  Cd Length: 118  Bit Score: 51.19  E-value: 6.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  381 DAEGEREARVFTLWLNS--LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKvnkapasgdEMMRFKAVENCNYAVD 458
Cdd:cd21237   1 DERDRVQKKTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREK---------GRMRFHRLQNVQIALD 71
                        90       100       110
                ....*....|....*....|....*....|...
gi 4539245  459 LGKNQGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21237  72 FLKQRQVKLVNIRNDDITDGNPKLTLGLIWTII 104
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
151-231 7.39e-08

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: 50.75  E-value: 7.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  151 DGLILSKLIndsvpDTIDERVLnKQRNNKPLDNFKCIENNNVVINsAKAMGGISITNIGAGDILEGREHLILGLVWQIIR 230
Cdd:cd21227  33 DGVKLIALV-----EILQGRKL-GRVIKKPLNQHQKLENVTLALK-AMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLIL 105

                .
gi 4539245  231 R 231
Cdd:cd21227 106 R 106
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
114-231 1.03e-07

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: 50.48  E-value: 1.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  114 ERREFIKHINSVLAGdpdvgSRVPINTETFEFfdqcKDGLILSKLIndsvpDTIDERVLNKQrNNKPLDNFKCIENNNVV 193
Cdd:cd21215   5 QKKTFTKWLNTKLSS-----RGLSITDLVTDL----SDGVRLIQLL-----EIIGDESLGRY-NKNPKMRVQKLENVNKA 69
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4539245  194 INSAKAMGgISITNIGAGDILEGREHLILGLVWQIIRR 231
Cdd:cd21215  70 LEFIKSRG-VKLTNIGAEDIVDGNLKLILGLLWTLILR 106
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
385-495 1.83e-07

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


Pssm-ID: 409173  Cd Length: 145  Bit Score: 50.78  E-value: 1.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  385 EREARVFTLWLNS-----------LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKapasgDEMMRFKAVENC 453
Cdd:cd21324  23 EEEKYAFVNWINKalendpdckhvIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINK-----KKLTPFTIQENL 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4539245  454 NYAVDLGKNQGFSLVGIQGADITDGSRTLTLALVWQMMRMNI 495
Cdd:cd21324  98 NLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGL 139
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
385-491 2.52e-07

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409165  Cd Length: 154  Bit Score: 50.43  E-value: 2.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  385 EREA---RVFTLWLNS--LDVTPSIHDFFNNLRDGLILLQAYDKITPNtvnwkkvnKAPASGDEMMRFKAVENCNYAVDL 459
Cdd:cd21316  49 EREAvqkKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLEVLSGE--------RLPKPTKGRMRIHCLENVDKALQF 120
                        90       100       110
                ....*....|....*....|....*....|..
gi 4539245  460 GKNQGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21316 121 LKEQRVHLENMGSHDIVDGNHRLTLGLIWTII 152
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
114-231 3.24e-07

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: 49.22  E-value: 3.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  114 ERREFIKHINSVLAgdpdvgsrvPINTETFEFFDQCKDGLILSKLI----NDSVPdtidervlnkqRNNKPLDNFKCIEN 189
Cdd:cd21193  17 QKKTFTKWINSFLE---------KANLEIGDLFTDLSDGKLLLKLLeiisGEKLG-----------KPNRGRLRVQKIEN 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4539245  190 NNVVINSAKAMggISITNIGAGDILEGREHLILGLVWQIIRR 231
Cdd:cd21193  77 VNKALAFLKTK--VRLENIGAEDIVDGNPRLILGLIWTIILR 116
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
385-495 3.81e-07

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


Pssm-ID: 409174  Cd Length: 148  Bit Score: 50.06  E-value: 3.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  385 EREARVFTLWLNS-----------LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKapasgDEMMRFKAVENC 453
Cdd:cd21325  23 EEEKYAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINK-----KKLTPFIIQENL 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4539245  454 NYAVDLGKNQGFSLVGIQGADITDGSRTLTLALVWQMMRMNI 495
Cdd:cd21325  98 NLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGL 139
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
389-491 3.82e-07

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409091  Cd Length: 111  Bit Score: 49.06  E-value: 3.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  389 RVFTLWLNSL---DVTPS-IHDFFNNLRDGLILLQAYDKItpntvnwkkvnkapaSGDEMMR------FKAVENCNYAVD 458
Cdd:cd21242   8 RTFTNWINSQlakHSPPSvVSDLFTDIQDGHRLLDLLEVL---------------SGQQLPRekghnvFQCRSNIETALS 72
                        90       100       110
                ....*....|....*....|....*....|...
gi 4539245  459 LGKNQGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21242  73 FLKNKSIKLINIHVPDIIEGKPSIILGLIWTII 105
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
387-491 5.81e-07

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: 48.34  E-value: 5.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  387 EARVFTLWLNS----LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKvnkapasGDEMMRFKAVENCNYAVDLGKN 462
Cdd:cd21190   6 QKKTFTNWINShlakLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIES-------GRVLQRAHKLSNIRNALDFLTK 78
                        90       100
                ....*....|....*....|....*....
gi 4539245  463 QGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21190  79 RCIKLVNINSTDIVDGKPSIVLGLIWTII 107
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
183-231 1.23e-06

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 47.67  E-value: 1.23e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 4539245  183 NFKCIENNNVVINSAKAMGGISITNIGAGDILEGREHLILGLVWQIIRR 231
Cdd:cd21329  64 NMKKIENCNYAVELGKNKAKFSLVGIAGSDLNEGNKTLTLALIWQLMRR 112
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
385-491 1.43e-06

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


Pssm-ID: 409040  Cd Length: 114  Bit Score: 47.19  E-value: 1.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  385 EREA---RVFTLWLN----SLDVTPSIHDFFNNLRDGLILLQAYDKITPNTVnwkkVNKAPASGDEMMRfkaVENCNYAV 457
Cdd:cd21191   1 ERENvqkRTFTRWINlhleKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNL----LQEYKPSSHRIFR---LNNIAKAL 73
                        90       100       110
                ....*....|....*....|....*....|....
gi 4539245  458 DLGKNQGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21191  74 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNII 107
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
383-488 2.44e-06

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


Pssm-ID: 409090  Cd Length: 113  Bit Score: 46.60  E-value: 2.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  383 EGER-EARVFTLWLNS--LDVTPSIH--DFFNNLRDGLILLQAYDKITPNTVNWKKvnkapasGDEMMRFKAVENCNYAV 457
Cdd:cd21241   1 EQERvQKKTFTNWINSylAKRKPPMKveDLFEDIKDGTKLLALLEVLSGEKLPCEK-------GRRLKRVHFLSNINTAL 73
                        90       100       110
                ....*....|....*....|....*....|.
gi 4539245  458 DLGKNQGFSLVGIQGADITDGSRTLTLALVW 488
Cdd:cd21241  74 KFLESKKIKLVNINPTDIVDGKPSIVLGLIW 104
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
138-231 5.39e-06

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 46.15  E-value: 5.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  138 INTETFEFFDQCKDGLILSKLIND-SVPdtIDERVLNKQRNNKPLDNFKCIENNNVVINSAKAMGGISITNIGAGDILEG 216
Cdd:cd21331  36 VNPHVNHLYGDLQDALVILQLYEKiKVP--VDWNKVNKPPYPKLGANMKKLENCNYAVELGKHPAKFSLVGIGGQDLNDG 113
                        90
                ....*....|....*
gi 4539245  217 REHLILGLVWQIIRR 231
Cdd:cd21331 114 NPTLTLALVWQLMRR 128
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
114-229 5.45e-06

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: 45.45  E-value: 5.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  114 ERREFIKHINSVLAGdpdvGSRVPINtetfEFFDQCKDGLILSKLIndsvpDTIDERVLNKQR--------NNkpLDN-F 184
Cdd:cd21186   3 QKKTFTKWINSQLSK----ANKPPIK----DLFEDLRDGTRLLALL-----EVLTGKKLKPEKgrmrvhhlNN--VNRaL 67
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 4539245  185 KCIENNNVvinsakamggiSITNIGAGDILEGREHLILGLVWQII 229
Cdd:cd21186  68 QVLEQNNV-----------KLVNISSNDIVDGNPKLTLGLVWSII 101
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
114-231 6.24e-06

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409095  Cd Length: 117  Bit Score: 45.44  E-value: 6.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  114 ERREFIKHINSVLAgdpdvgsRVPINTEtfEFFDQCKDGLILSKLIndsvpdtideRVLNKQRNNKPLDN---FKCIENN 190
Cdd:cd21246  17 QKKTFTKWVNSHLA-------RVGCRIN--DLYTDLRDGRMLIKLL----------EVLSGERLPKPTKGkmrIHCLENV 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 4539245  191 NVVINSAKAMGgISITNIGAGDILEGREHLILGLVWQIIRR 231
Cdd:cd21246  78 DKALQFLKEQR-VHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
151-231 7.46e-06

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 45.16  E-value: 7.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  151 DGLILSKLIndsvpDTIDERVLNKQRNNKPLDNFKCIENNNVVINSAKAMGgISITNIGAGDILEGREHLILGLVWQIIR 230
Cdd:cd21183  33 DGLCLIALL-----ENLSTRPLKRSYNRRPAFQQHYLENVSTALKFIEADH-IKLVNIGSGDIVNGNIKLILGLIWTLIL 106

                .
gi 4539245  231 R 231
Cdd:cd21183 107 H 107
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
138-231 1.00e-05

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 45.37  E-value: 1.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  138 INTETFEFFDQCKDGLILSKLIND-SVPdtIDERVLNKQRNNKPLDNFKCIENNNVVINSAKAMGGISITNIGAGDILEG 216
Cdd:cd21330  27 VNPRVNHLYSDLSDALVIFQLYEKiKVP--VDWNRVNKPPYPKLGENMKKLENCNYAVELGKNKAKFSLVGIAGQDLNEG 104
                        90
                ....*....|....*
gi 4539245  217 REHLILGLVWQIIRR 231
Cdd:cd21330 105 NRTLTLALIWQLMRR 119
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
251-352 1.04e-05

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


Pssm-ID: 409164  Cd Length: 118  Bit Score: 45.16  E-value: 1.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  251 EDETLDQFLRLPPEKILLRWFNYhlKAANWPrtVSNFSKDVSDGENYTVLLNQLAPELCSR-APLQTTDVLQRAEQVLQN 329
Cdd:cd21315   5 EDDGPDDGKGPTPKQRLLGWIQS--KVPDLP--ITNFTNDWNDGKAIGALVDALAPGLCPDwEDWDPKDAVKNAKEAMDL 80
                        90       100
                ....*....|....*....|....
gi 4539245  330 AEK-LDCRKYLTPTAMVagNPKLN 352
Cdd:cd21315  81 AEDwLDVPQLIKPEEMV--NPKVD 102
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
385-490 1.32e-05

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: 44.59  E-value: 1.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  385 EREARVFTLWLN-SLDVT-PSIHDFFNNLRDGLILLQAYDKITPNTVnwKKVNKAPASGDEMMrfkavENCNYAVDLGKN 462
Cdd:cd21227   3 EIQKNTFTNWVNeQLKPTgMSVEDLATDLEDGVKLIALVEILQGRKL--GRVIKKPLNQHQKL-----ENVTLALKAMAE 75
                        90       100
                ....*....|....*....|....*...
gi 4539245  463 QGFSLVGIQGADITDGSRTLTLALVWQM 490
Cdd:cd21227  76 DGIKLVNIGNEDIVNGNLKLILGLIWHL 103
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
114-231 1.90e-05

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409167  Cd Length: 139  Bit Score: 44.63  E-value: 1.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  114 ERREFIKHINSVLAgdpdvgsRVPINTEtfEFFDQCKDGLILSKLIndsvpdtideRVLNKQRNNKPLDN---FKCIENN 190
Cdd:cd21318  39 QKKTFTKWVNSHLA-------RVPCRIN--DLYTDLRDGYVLTRLL----------EVLSGEQLPKPTRGrmrIHSLENV 99
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 4539245  191 NVVINSAKAMGgISITNIGAGDILEGREHLILGLVWQIIRR 231
Cdd:cd21318 100 DKALQFLKEQR-VHLENVGSHDIVDGNHRLTLGLIWTIILR 139
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
262-350 3.35e-05

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


Pssm-ID: 409079  Cd Length: 103  Bit Score: 43.14  E-value: 3.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  262 PPEKILLRWFNYHLKAANwprtVSNFSKDVSDGENYTVLLNQLAPELCSRAPL-QTTDVLQRAEQVLQNAEK-LDCRKYL 339
Cdd:cd21230   1 TPKQRLLGWIQNKIPQLP----ITNFTTDWNDGRALGALVDSCAPGLCPDWETwDPNDALENATEAMQLAEDwLGVPQLI 76
                        90
                ....*....|.
gi 4539245  340 TPTAMVagNPK 350
Cdd:cd21230  77 TPEEII--NPN 85
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
112-229 4.67e-05

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


Pssm-ID: 409090  Cd Length: 113  Bit Score: 43.13  E-value: 4.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  112 EEER---REFIKHINSVLAgdpdvgSRVPiNTETFEFFDQCKDGLILSKLIndsvpdtideRVLNKQR----NNKPLDNF 184
Cdd:cd21241   1 EQERvqkKTFTNWINSYLA------KRKP-PMKVEDLFEDIKDGTKLLALL----------EVLSGEKlpceKGRRLKRV 63
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 4539245  185 KCIENnnvvINSA-KAMGG--ISITNIGAGDILEGREHLILGLVWQII 229
Cdd:cd21241  64 HFLSN----INTAlKFLESkkIKLVNINPTDIVDGKPSIVLGLIWTII 107
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
391-492 6.03e-05

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409074  Cd Length: 111  Bit Score: 42.52  E-value: 6.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  391 FTLWLNSL---DVTPSIHDFFNNLRDGLILLQAYDKITPNTVNwKKVNKAPASgdemmRFKAVENCNYAVD-LGKNQGFS 466
Cdd:cd21225   9 FTAWVNSVlekRGIPKISDLATDLSDGVRLIFFLELVSGKKFP-KKFDLEPKN-----RIQMIQNLHLAMLfIEEDLKIR 82
                        90       100
                ....*....|....*....|....*.
gi 4539245  467 LVGIQGADITDGSRTLTLALVWQMMR 492
Cdd:cd21225  83 VQGIGAEDFVDNNKKLILGLLWTLYR 108
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
114-231 7.91e-05

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409166  Cd Length: 132  Bit Score: 42.73  E-value: 7.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  114 ERREFIKHINSVLAgdpDVGSRVpintetFEFFDQCKDGLILSKLIndsvpdtideRVLNKQRNNKPLDN---FKCIENN 190
Cdd:cd21317  32 QKKTFTKWVNSHLA---RVTCRI------GDLYTDLRDGRMLIRLL----------EVLSGEQLPKPTKGrmrIHCLENV 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 4539245  191 NVVINSAKAMGgISITNIGAGDILEGREHLILGLVWQIIRR 231
Cdd:cd21317  93 DKALQFLKEQK-VHLENMGSHDIVDGNHRLTLGLIWTIILR 132
EF-hand_7 pfam13499
EF-hand domain pair;
21-80 7.95e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.08  E-value: 7.95e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4539245     21 LTDQFNKLDVDGKGYLDQ---PTTIKAFEDSKKGSYDEVREAIREVNVDSSGRVEPEDFVGIF 80
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVeelKKLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
517-611 8.23e-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: 42.29  E-value: 8.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  517 WANS-MAAKGGKGSQIRSFrDPSISTGVFVLDVLHGIKSEYVDYNLVTDGSTEELAIQNARLAISIARKLGAVIFILPED 595
Cdd:cd21218  18 WVNYhLKKAGPTKKRVTNF-SSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYFLTPED 96
                        90
                ....*....|....*.
gi 4539245  596 IVAVRPRLVLHFIGSL 611
Cdd:cd21218  97 IVSGNPRLNLAFVATL 112
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
403-491 1.60e-04

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: 41.42  E-value: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  403 SIHDFFNNLRDGLILLQAYDKITPNTVNWKKVnKAPASGdemmRFKAVENCNYAV----DLGKNQGFSLVGIQGADITDG 478
Cdd:cd21223  25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKL-RVPAIS----RLQKLHNVEVALkalkEAGVLRGGDGGGITAKDIVDG 99
                        90
                ....*....|...
gi 4539245  479 SRTLTLALVWQMM 491
Cdd:cd21223 100 HREKTLALLWRII 112
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
391-491 1.64e-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: 41.32  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  391 FTLWLNS--LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVnWKKVNKAPAsgdemMRFKAVENCNYAVDLGKNQGFSLV 468
Cdd:cd21228   9 FTRWCNEhlKCVNKRIYNLETDLSDGLRLIALLEVLSQKRM-YKKYNKRPT-----FRQMKLENVSVALEFLERESIKLV 82
                        90       100
                ....*....|....*....|...
gi 4539245  469 GIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21228  83 SIDSSAIVDGNLKLILGLIWTLI 105
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
114-229 1.83e-04

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409091  Cd Length: 111  Bit Score: 41.35  E-value: 1.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  114 ERREFIKHINSVLAgdpdvgsRVPINTETFEFFDQCKDGLILSKLIndsvpdtideRVLNKQR--NNKPLDNFKCIENnn 191
Cdd:cd21242   6 QKRTFTNWINSQLA-------KHSPPSVVSDLFTDIQDGHRLLDLL----------EVLSGQQlpREKGHNVFQCRSN-- 66
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 4539245  192 vvINSAKAM---GGISITNIGAGDILEGREHLILGLVWQII 229
Cdd:cd21242  67 --IETALSFlknKSIKLINIHVPDIIEGKPSIILGLIWTII 105
PTZ00183 PTZ00183
centrin; Provisional
8-119 1.84e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.37  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245     8 KKYPELTNEEILTLTDQFNKLDVDGKGYLDqPTTIKA------FEdSKKgsyDEVREAIREVNVDSSGRVEPEDFVGIFN 81
Cdd:PTZ00183   6 SERPGLTEDQKKEIREAFDLFDTDGSGTID-PKELKVamrslgFE-PKK---EEIKQMIADVDKDGSGKIDFEEFLDIMT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4539245    82 V-LKKGVEGTEVKK----------GRITIKG---SSSSVSHTINEEERREFI 119
Cdd:PTZ00183  81 KkLGERDPREEILKafrlfdddktGKISLKNlkrVAKELGETITDEELQEMI 132
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
151-229 2.45e-04

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


Pssm-ID: 409160  Cd Length: 124  Bit Score: 41.28  E-value: 2.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  151 DGLILSKLIndsvpdtideRVLNKQR----NNKPLDNFKCIENNNVVINSAKAMGGISITNIGAGDILEGREHLILGLVW 226
Cdd:cd21311  44 DGLRLIALV----------EVLSGKKfpkfNKRPTFRSQKLENVSVALKFLEEDEGIKIVNIDSSDIVDGKLKLILGLIW 113

                ...
gi 4539245  227 QII 229
Cdd:cd21311 114 TLI 116
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
398-493 6.91e-04

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


Pssm-ID: 409142  Cd Length: 116  Bit Score: 39.82  E-value: 6.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  398 LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNkapaSGDEMMRFKAVENCNYAVDLGKNQGFSLVGIQGADITD 477
Cdd:cd21293  24 LPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAIN----TKKVLNPWERNENHTLCLNSAKAIGCSVVNIGTQDLAE 99
                        90
                ....*....|....*.
gi 4539245  478 GSRTLTLALVWQMMRM 493
Cdd:cd21293 100 GRPHLVLGLISQIIKI 115
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
264-364 8.81e-04

second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.


Pssm-ID: 409082  Cd Length: 111  Bit Score: 39.14  E-value: 8.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  264 EKILLRWFNYHLKaaNWPR-TVSNFSKDVSDGENYTVLLNQLAPELCS-RAPLQTTDVLQRAEQVLQNAEK-LDCRKYLT 340
Cdd:cd21233   2 EKILLSWVRQSTR--NYPQvNVINFTSSWSDGLAFNALIHSHRPDLFDwNSVVSQQSATERLDHAFNIARQhLGIEKLLD 79
                        90       100
                ....*....|....*....|....*.
gi 4539245  341 PTAMVAGNP--KLNLAFVAHLFNTHP 364
Cdd:cd21233  80 PEDVATAHPdkKSILMYVTSLFQVLP 105
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
114-231 8.92e-04

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409165  Cd Length: 154  Bit Score: 40.41  E-value: 8.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  114 ERREFIKHINSVLAgdpDVGSRVPintetfEFFDQCKDGLILSKLIndsvpdtideRVLNKQRNNKPLDN---FKCIENN 190
Cdd:cd21316  54 QKKTFTKWVNSHLA---RVSCRIT------DLYMDLRDGRMLIKLL----------EVLSGERLPKPTKGrmrIHCLENV 114
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 4539245  191 NVVINSAKAMGgISITNIGAGDILEGREHLILGLVWQIIRR 231
Cdd:cd21316 115 DKALQFLKEQR-VHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
368-491 2.19e-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: 38.52  E-value: 2.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  368 PLNEEEKPEIEPFDaegEREARVFTLWLNS--LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVnWKKVNKAPAsgdemM 445
Cdd:cd21309   2 PVTEKDLAEDAPWK---KIQQNTFTRWCNEhlKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRM-YRKYHQRPT-----F 72
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4539245  446 RFKAVENCNYAVDLGKNQGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21309  73 RQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLI 118
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
184-229 2.54e-03

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: 37.77  E-value: 2.54e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 4539245  184 FKCIENNNVVINSAKaMGGISITNIGAGDILEGREHLILGLVWQII 229
Cdd:cd21188  57 FHRLQNVQTALDFLK-YRKIKLVNIRAEDIVDGNPKLTLGLIWTII 101
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
151-229 3.50e-03

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: 37.47  E-value: 3.50e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4539245  151 DGLILSKLIndsvpDTIDERVLNKQRNNKPLDNFKCIENNNVVINSAKAMGgISITNIGAGDILEGREHLILGLVWQII 229
Cdd:cd21228  33 DGLRLIALL-----EVLSQKRMYKKYNKRPTFRQMKLENVSVALEFLERES-IKLVSIDSSAIVDGNLKLILGLIWTLI 105
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
387-491 3.69e-03

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 37.46  E-value: 3.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  387 EARVFTLWLNS--LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNwKKVNKAPAsgdemMRFKAVENCNYAVDLGKNQG 464
Cdd:cd21183   5 QANTFTRWCNEhlKERGMQIHDLATDFSDGLCLIALLENLSTRPLK-RSYNRRPA-----FQQHYLENVSTALKFIEADH 78
                        90       100
                ....*....|....*....|....*..
gi 4539245  465 FSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21183  79 IKLVNIGSGDIVNGNIKLILGLIWTLI 105
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
114-229 4.05e-03

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: 37.59  E-value: 4.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  114 ERREFIKHINSVLAGdpdvGSRVPINtetfEFFDQCKDGLILSKLINDSVPDTI-----DERVLNKQRNNKPLdnfKCIE 188
Cdd:cd21231   7 QKKTFTKWINAQFAK----FGKPPIE----DLFTDLQDGRRLLELLEGLTGQKLvkekgSTRVHALNNVNKAL---QVLQ 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 4539245  189 NNNVvinsakamggiSITNIGAGDILEGREHLILGLVWQII 229
Cdd:cd21231  76 KNNV-----------DLVNIGSADIVDGNHKLTLGLIWSII 105
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
389-488 4.44e-03

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409096  Cd Length: 125  Bit Score: 37.43  E-value: 4.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  389 RVFTLWLNSL----DVTPSIHDFFNNLRDGLILLQAYDKITPNtvnwkkvnKAPASGDEMMRFKAVENCNYAVDLGKNQ- 463
Cdd:cd21247  23 KTFTKWMNNVfsknGAKIEITDIYTELKDGIHLLRLLELISGE--------QLPRPSRGKMRVHFLENNSKAITFLKTKv 94
                        90       100
                ....*....|....*....|....*
gi 4539245  464 GFSLVGIQgaDITDGSRTLTLALVW 488
Cdd:cd21247  95 PVKLIGPE--NIVDGDRTLILGLIW 117
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
114-229 4.47e-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: 37.16  E-value: 4.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  114 ERREFIKHINSVLAgdpDVGSRVPINtetfEFFDQCKDGLILSKLIndsvpdtideRVLNKQR----NNKPLDNFKCIEN 189
Cdd:cd21190   6 QKKTFTNWINSHLA---KLSQPIVIN----DLFVDIKDGTALLRLL----------EVLSGQKlpieSGRVLQRAHKLSN 68
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4539245  190 nnvVINSAKAMGG--ISITNIGAGDILEGREHLILGLVWQII 229
Cdd:cd21190  69 ---IRNALDFLTKrcIKLVNINSTDIVDGKPSIVLGLIWTII 107
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
145-228 6.05e-03

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 36.89  E-value: 6.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  145 FFDQCKDGLILSKLINDSVPDTIDERVlnkqrNNKPLDNFKCIENNNVVINSAKAMGGISItnIGAGDILEGREHLILGL 224
Cdd:cd21218  36 FSSDLKDGEVYALLLHSLAPELCDKEL-----VLEVLSEEDLEKRAEKVLQAAEKLGCKYF--LTPEDIVSGNPRLNLAF 108

                ....
gi 4539245  225 VWQI 228
Cdd:cd21218 109 VATL 112
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
368-491 6.24e-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: 37.37  E-value: 6.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  368 PLNEEEKPEIEPFDaegEREARVFTLWLNS--LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVnWKKVNKAPAsgdemM 445
Cdd:cd21308   5 PATEKDLAEDAPWK---KIQQNTFTRWCNEhlKCVSKRIANLQTDLSDGLRLIALLEVLSQKKM-HRKHNQRPT-----F 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4539245  446 RFKAVENCNYAVDLGKNQGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21308  76 RQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLI 121
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
368-491 7.78e-03

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


Pssm-ID: 409159  Cd Length: 125  Bit Score: 36.93  E-value: 7.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4539245  368 PLNEEEKPEIEPFDaegEREARVFTLWLNS--LDVTPSIHDFFNNLRDGLILLQAYDKITPNTVnWKKVNKAPAsgdemM 445
Cdd:cd21310   1 PATEKDLAEDAPWK---KIQQNTFTRWCNEhlKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKM-YRKYHPRPN-----F 71
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4539245  446 RFKAVENCNYAVDLGKNQGFSLVGIQGADITDGSRTLTLALVWQMM 491
Cdd:cd21310  72 RQMKLENVSVALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLI 117
 
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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