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Conserved domains on  [gi|697835384|ref|XP_009638051|]
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plastin-1 isoform X2 [Egretta garzetta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
73-217 4.60e-108

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).


The actual alignment was detected with superfamily member cd21323:

Pssm-ID: 469584  Cd Length: 145  Bit Score: 320.84  E-value: 4.60e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  73 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALQDDPDCKHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDE 152
Cdd:cd21323    1 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697835384 153 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKAGLFADIEI 217
Cdd:cd21323   81 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
365-482 1.86e-87

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: 266.85  E-value: 1.86e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 365 LEGESKEERTFRNWMNSLGVSPYVNHLYSDLSDALIIFQLYDMTRVPVDWNHVNKPPYPLLGGNMKKIENCNYAVELGKT 444
Cdd:cd21329    1 LEGESSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRVPVDWGHVNKPPYPALGGNMKKIENCNYAVELGKN 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 697835384 445 KAKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTLNVL 482
Cdd:cd21329   81 KAKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
SAC6 super family cl26648
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
18-595 1.74e-83

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


The actual alignment was detected with superfamily member COG5069:

Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 273.36  E-value: 1.74e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  18 EAFSKIDIDNSGYVSDYELQDLFKEANL----PLPgYRIIQELKSKDISKSFRKSinKKEGITAIGGTSAI--------- 84
Cdd:COG5069   28 KEFGDLDTDLKDGVKLAQLLEALQKDNAgeynETP-ETRIHVMENVSGRLEFIKG--KGVKLFNIGPQDIVdgnpklilg 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  85 -----SSEGTQHSYSEEEKvaFVNWINKALQDDPDCKHLLPmNPSDASLFKCLADGILLCKMINFSQPDTIDERAINK-- 157
Cdd:COG5069  105 liwslISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLqk 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 158 --KKLTPFTISENLNLALNSASAIG-CTVVNIGSQDLQEgkpHLVLgLLWQIIKAGLFADIEISRNEaLIALLNEGEELD 234
Cdd:COG5069  182 knKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERS---IMTY-VSWYIIRFGLLEKIDIALHR-VYRLLEADETLI 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 235 QlMKLSPEELLLRWVN-YHLTNAGWqKISNFSQDIKDSRAYYHLLNQIAPKgddCNELPvkidfsgfHDKSDL-RRAECM 312
Cdd:COG5069  257 Q-LRLPYEIILLRLLNlIHLKQANW-KVVNFSKDVSDGENYTDLLNQLNAL---CSRAP--------LETTDLhSLAGQI 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 313 LQQADKLGCRQFVTPadvvAGNPKLNLAFVANLFNTYPAL------HKPDNSSYDvnlLEGEsKEERTFRNWMNSLGVSP 386
Cdd:COG5069  324 LQNAEKYDCRKYLPP----AGNPKLDLAFVAHLFNTHPGQepleeeEKPEIEEFD---AEGE-FEARVFTFWLNSLDVSP 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 387 YVNHLYSDLSDALIIFQLYDMTRVP--VDWNHVNKPPYPLLGGN-MKKIENCNYAVELGKTKAkFSLVGIAGHDLNEGNp 463
Cdd:COG5069  396 EITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVGIKGLEILDGI- 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 464 TLTLALVWQLMRRYTLNVLSDLGEGEK-VNDDVIIKWVNQTLAKANKETSITSFKDKSISTSLP-VLDLIDAIAPRAVRP 541
Cdd:COG5069  474 RLKLTLVWQVLRSNTALFNHVLKKDGCgLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDVLKGIHSELVDY 553
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 697835384 542 EMVKREDLSYQDKMNNAKYAIS--VARKIGARIYALPDDLVEVKPKM-VMTVFACLM 595
Cdd:COG5069  554 DLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
 
Name Accession Description Interval E-value
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
73-217 4.60e-108

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: 320.84  E-value: 4.60e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  73 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALQDDPDCKHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDE 152
Cdd:cd21323    1 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697835384 153 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKAGLFADIEI 217
Cdd:cd21323   81 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
365-482 1.86e-87

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: 266.85  E-value: 1.86e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 365 LEGESKEERTFRNWMNSLGVSPYVNHLYSDLSDALIIFQLYDMTRVPVDWNHVNKPPYPLLGGNMKKIENCNYAVELGKT 444
Cdd:cd21329    1 LEGESSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRVPVDWGHVNKPPYPALGGNMKKIENCNYAVELGKN 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 697835384 445 KAKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTLNVL 482
Cdd:cd21329   81 KAKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
18-595 1.74e-83

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 273.36  E-value: 1.74e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  18 EAFSKIDIDNSGYVSDYELQDLFKEANL----PLPgYRIIQELKSKDISKSFRKSinKKEGITAIGGTSAI--------- 84
Cdd:COG5069   28 KEFGDLDTDLKDGVKLAQLLEALQKDNAgeynETP-ETRIHVMENVSGRLEFIKG--KGVKLFNIGPQDIVdgnpklilg 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  85 -----SSEGTQHSYSEEEKvaFVNWINKALQDDPDCKHLLPmNPSDASLFKCLADGILLCKMINFSQPDTIDERAINK-- 157
Cdd:COG5069  105 liwslISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLqk 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 158 --KKLTPFTISENLNLALNSASAIG-CTVVNIGSQDLQEgkpHLVLgLLWQIIKAGLFADIEISRNEaLIALLNEGEELD 234
Cdd:COG5069  182 knKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERS---IMTY-VSWYIIRFGLLEKIDIALHR-VYRLLEADETLI 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 235 QlMKLSPEELLLRWVN-YHLTNAGWqKISNFSQDIKDSRAYYHLLNQIAPKgddCNELPvkidfsgfHDKSDL-RRAECM 312
Cdd:COG5069  257 Q-LRLPYEIILLRLLNlIHLKQANW-KVVNFSKDVSDGENYTDLLNQLNAL---CSRAP--------LETTDLhSLAGQI 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 313 LQQADKLGCRQFVTPadvvAGNPKLNLAFVANLFNTYPAL------HKPDNSSYDvnlLEGEsKEERTFRNWMNSLGVSP 386
Cdd:COG5069  324 LQNAEKYDCRKYLPP----AGNPKLDLAFVAHLFNTHPGQepleeeEKPEIEEFD---AEGE-FEARVFTFWLNSLDVSP 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 387 YVNHLYSDLSDALIIFQLYDMTRVP--VDWNHVNKPPYPLLGGN-MKKIENCNYAVELGKTKAkFSLVGIAGHDLNEGNp 463
Cdd:COG5069  396 EITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVGIKGLEILDGI- 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 464 TLTLALVWQLMRRYTLNVLSDLGEGEK-VNDDVIIKWVNQTLAKANKETSITSFKDKSISTSLP-VLDLIDAIAPRAVRP 541
Cdd:COG5069  474 RLKLTLVWQVLRSNTALFNHVLKKDGCgLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDVLKGIHSELVDY 553
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 697835384 542 EMVKREDLSYQDKMNNAKYAIS--VARKIGARIYALPDDLVEVKPKM-VMTVFACLM 595
Cdd:COG5069  554 DLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
229-350 5.00e-78

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: 242.48  E-value: 5.00e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 229 EGEELDQLMKLSPEELLLRWVNYHLTNAGWQKISNFSQDIKDSRAYYHLLNQIAPKGDDCNELpVKIDFSGFHDKSDLRR 308
Cdd:cd21326    1 EGEELEELMKLSPEELLLRWVNYHLTNAGWQNISNFSQDIKDSRAYFHLLNQIAPKGDVFDEN-IEIDFSGFNEKNDLKR 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 697835384 309 AECMLQQADKLGCRQFVTPADVVAGNPKLNLAFVANLFNTYP 350
Cdd:cd21326   80 AEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 121
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
95-210 3.35e-23

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: 94.66  E-value: 3.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384   95 EEEKVAFVNWINKALQDDPDCKHLLpmnpsdaSLFKCLADGILLCKMINFSQPDTIDERAINKKkltPFTISENLNLALN 174
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVT-------NFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 697835384  175 SAS-AIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKAG 210
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
239-351 1.18e-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: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  239 LSPEELLLRWVNYHLTNAGW-QKISNFSQDIKDSRAYYHLLNQIAPKGDDcnelPVKIDFSGFHdksDLRRAECMLQQA- 316
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPgVRVTNFTTDLRDGLALCALLNKLAPGLVD----KKKLNKSEFD---KLENINLALDVAe 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 697835384  317 DKLGCRQF-VTPADVVAGNPKLNLAFVANLFNTYPA 351
Cdd:pfam00307  74 KKLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
100-207 3.57e-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: 82.75  E-value: 3.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384   100 AFVNWINKALQDDPdckhllpmNPSDASLFKCLADGILLCKMINFSQPDTIDERAINKKKlTPFTISENLNLALNSASAI 179
Cdd:smart00033   2 TLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEKL 72
                           90       100
                   ....*....|....*....|....*...
gi 697835384   180 GCTVVNIGSQDLQEGkPHLVLGLLWQII 207
Cdd:smart00033  73 GGKVVLFEPEDLVEG-PKLILGVIWTLI 99
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
371-477 2.55e-16

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: 75.02  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  371 EERTFRNWMNSL----GVSPYVNHLYSDLSDALIIFQLYDMTRvP--VDWNHVNKPPypllggnMKKIENCNYAVELGKT 444
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 697835384  445 KAKFSLVGIAGHDLNEGNPTLTLALVWQLMRRY 477
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
243-346 1.09e-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: 72.73  E-value: 1.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384   243 ELLLRWVNYHLTNAGWQKISNFSQDIKDSRAYYHLLNQIAPkgDDCNELPVKIDFSGFHDKSDLRRAecmLQQADKLGC- 321
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSP--GLVDKKKVAASLSRFKKIENINLA---LSFAEKLGGk 75
                           90       100
                   ....*....|....*....|....*
gi 697835384   322 RQFVTPADVVAGnPKLNLAFVANLF 346
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLI 99
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
373-476 3.83e-15

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 71.19  E-value: 3.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384   373 RTFRNWMNSLGV---SPYVNHLYSDLSDALIIFQLYDMTRVP-VDWNHVNKPPYPllggnMKKIENCNYAVELGKtKAKF 448
Cdd:smart00033   1 KTLLRWVNSLLAeydKPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAE-KLGG 74
                           90       100
                   ....*....|....*....|....*...
gi 697835384   449 SLVGIAGHDLNEGNPtLTLALVWQLMRR 476
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
 
Name Accession Description Interval E-value
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
73-217 4.60e-108

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: 320.84  E-value: 4.60e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  73 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALQDDPDCKHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDE 152
Cdd:cd21323    1 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697835384 153 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKAGLFADIEI 217
Cdd:cd21323   81 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
73-217 4.14e-100

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: 300.35  E-value: 4.14e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  73 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALQDDPDCKHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDE 152
Cdd:cd21292    1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697835384 153 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKAGLFADIEI 217
Cdd:cd21292   81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
365-482 1.86e-87

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: 266.85  E-value: 1.86e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 365 LEGESKEERTFRNWMNSLGVSPYVNHLYSDLSDALIIFQLYDMTRVPVDWNHVNKPPYPLLGGNMKKIENCNYAVELGKT 444
Cdd:cd21329    1 LEGESSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRVPVDWGHVNKPPYPALGGNMKKIENCNYAVELGKN 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 697835384 445 KAKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTLNVL 482
Cdd:cd21329   81 KAKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
18-595 1.74e-83

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 273.36  E-value: 1.74e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  18 EAFSKIDIDNSGYVSDYELQDLFKEANL----PLPgYRIIQELKSKDISKSFRKSinKKEGITAIGGTSAI--------- 84
Cdd:COG5069   28 KEFGDLDTDLKDGVKLAQLLEALQKDNAgeynETP-ETRIHVMENVSGRLEFIKG--KGVKLFNIGPQDIVdgnpklilg 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  85 -----SSEGTQHSYSEEEKvaFVNWINKALQDDPDCKHLLPmNPSDASLFKCLADGILLCKMINFSQPDTIDERAINK-- 157
Cdd:COG5069  105 liwslISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLqk 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 158 --KKLTPFTISENLNLALNSASAIG-CTVVNIGSQDLQEgkpHLVLgLLWQIIKAGLFADIEISRNEaLIALLNEGEELD 234
Cdd:COG5069  182 knKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERS---IMTY-VSWYIIRFGLLEKIDIALHR-VYRLLEADETLI 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 235 QlMKLSPEELLLRWVN-YHLTNAGWqKISNFSQDIKDSRAYYHLLNQIAPKgddCNELPvkidfsgfHDKSDL-RRAECM 312
Cdd:COG5069  257 Q-LRLPYEIILLRLLNlIHLKQANW-KVVNFSKDVSDGENYTDLLNQLNAL---CSRAP--------LETTDLhSLAGQI 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 313 LQQADKLGCRQFVTPadvvAGNPKLNLAFVANLFNTYPAL------HKPDNSSYDvnlLEGEsKEERTFRNWMNSLGVSP 386
Cdd:COG5069  324 LQNAEKYDCRKYLPP----AGNPKLDLAFVAHLFNTHPGQepleeeEKPEIEEFD---AEGE-FEARVFTFWLNSLDVSP 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 387 YVNHLYSDLSDALIIFQLYDMTRVP--VDWNHVNKPPYPLLGGN-MKKIENCNYAVELGKTKAkFSLVGIAGHDLNEGNp 463
Cdd:COG5069  396 EITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGITEG-FSLVGIKGLEILDGI- 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 464 TLTLALVWQLMRRYTLNVLSDLGEGEK-VNDDVIIKWVNQTLAKANKETSITSFKDKSISTSLP-VLDLIDAIAPRAVRP 541
Cdd:COG5069  474 RLKLTLVWQVLRSNTALFNHVLKKDGCgLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDVLKGIHSELVDY 553
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 697835384 542 EMVKREDLSYQDKMNNAKYAIS--VARKIGARIYALPDDLVEVKPKM-VMTVFACLM 595
Cdd:COG5069  554 DLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
349-482 7.64e-83

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: 255.70  E-value: 7.64e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 349 YPALHKPDNSSYDVNLLEGESKEERTFRNWMNSLGVSPYVNHLYSDLSDALIIFQLYDMTRVPVDWNHVNKPPYPLLGGN 428
Cdd:cd21331    1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 697835384 429 MKKIENCNYAVELGKTKAKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTLNVL 482
Cdd:cd21331   81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
73-220 4.34e-82

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: 254.21  E-value: 4.34e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  73 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALQDDPDCKHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDE 152
Cdd:cd21325    1 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697835384 153 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKAGLFADIEISRN 220
Cdd:cd21325   81 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRN 148
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
73-217 3.95e-78

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: 243.76  E-value: 3.95e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  73 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALQDDPDCKHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDE 152
Cdd:cd21324    1 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697835384 153 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKAGLFADIEI 217
Cdd:cd21324   81 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
229-350 5.00e-78

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: 242.48  E-value: 5.00e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 229 EGEELDQLMKLSPEELLLRWVNYHLTNAGWQKISNFSQDIKDSRAYYHLLNQIAPKGDDCNELpVKIDFSGFHDKSDLRR 308
Cdd:cd21326    1 EGEELEELMKLSPEELLLRWVNYHLTNAGWQNISNFSQDIKDSRAYFHLLNQIAPKGDVFDEN-IEIDFSGFNEKNDLKR 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 697835384 309 AECMLQQADKLGCRQFVTPADVVAGNPKLNLAFVANLFNTYP 350
Cdd:cd21326   80 AEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 121
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
484-598 2.93e-76

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: 237.92  E-value: 2.93e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 484 DLGEGEKVNDDVIIKWVNQTLAKANKETSITSFKDKSISTSLPVLDLIDAIAPRAVRPEMVKREDLSYQDKMNNAKYAIS 563
Cdd:cd21332    1 DLGEGEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDLSDADKLNNAKYAIS 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 697835384 564 VARKIGARIYALPDDLVEVKPKMVMTVFACLMGRG 598
Cdd:cd21332   81 VARKIGARVYALPEDLVEVKPKMVMTVFACLMGKG 115
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
365-482 8.78e-73

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: 228.66  E-value: 8.78e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 365 LEGESKEERTFRNWMNSLGVSPYVNHLYSDLSDALIIFQLYDMTRVPVDWNHVNKPPYPLLGGNMKKIENCNYAVELGKT 444
Cdd:cd21298    1 VIEETREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGANMKKIENCNYAVELGKK 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 697835384 445 KaKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTLNVL 482
Cdd:cd21298   81 L-KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLSIL 117
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
361-482 2.70e-72

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: 227.95  E-value: 2.70e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 361 DVNLLEGESKEERTFRNWMNSLGVSPYVNHLYSDLSDALIIFQLYDMTRVPVDWNHVNKPPYPLLGGNMKKIENCNYAVE 440
Cdd:cd21330    4 DWSSIEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGENMKKLENCNYAVE 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 697835384 441 LGKTKAKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTLNVL 482
Cdd:cd21330   84 LGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 125
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
226-347 9.84e-71

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: 223.69  E-value: 9.84e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 226 LLNEGEELDQLMKLSPEELLLRWVNYHLTNAGWQKISNFSQDIKDSRAYYHLLNQIAPKGDDCNELPVKIDFSGFHDKSD 305
Cdd:cd21328    1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEPRIDINMSGFNEKDD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 697835384 306 LRRAECMLQQADKLGCRQFVTPADVVAGNPKLNLAFVANLFN 347
Cdd:cd21328   81 LKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
226-350 2.47e-69

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: 220.22  E-value: 2.47e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 226 LLNEGEELDQLMKLSPEELLLRWVNYHLTNAGWQKISNFSQDIKDSRAYYHLLNQIAPKGDDCNELPVKIDFSGFHDKSD 305
Cdd:cd21327    1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNKINNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAIVIDMSGLREKDD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 697835384 306 LRRAECMLQQADKLGCRQFVTPADVVAGNPKLNLAFVANLFNTYP 350
Cdd:cd21327   81 LKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
229-347 4.62e-66

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: 210.98  E-value: 4.62e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 229 EGEELDQLMKLSPEELLLRWVNYHLTNAGWQK-ISNFSQDIKDSRAYYHLLNQIAPKGDdcnelpvKIDFSGFHDKSDLR 307
Cdd:cd21295    1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRrIKNFSGDIKDSEAYTHLLKQIAPKDA-------GVDTSALRESDLLQ 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 697835384 308 RAECMLQQADKLGCRQFVTPADVVAGNPKLNLAFVANLFN 347
Cdd:cd21295   74 RAELMLQNADKIGCRKFVTPKDVVTGNPKLNLAFVANLFN 113
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
486-599 8.62e-62

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: 199.83  E-value: 8.62e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 486 GEGEKVNDDVIIKWVNQTLAKANKETSITSFKDKSISTSLPVLDLIDAIAPRAVRPEMVKREDLSYQDKMNNAKYAISVA 565
Cdd:cd21333    1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNNAKYAISMA 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 697835384 566 RKIGARIYALPDDLVEVKPKMVMTVFACLMGRGL 599
Cdd:cd21333   81 RKIGARVYALPEDLVEVKPKMVMTVFACLMGRGM 114
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
491-602 2.41e-59

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: 193.57  E-value: 2.41e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 491 VNDDVIIKWVNQTLAKANKETSITSFKDKSISTSLPVLDLIDAIAPRAVRPEMVKREDLSYQDKMNNAKYAISVARKIGA 570
Cdd:cd21334    1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 697835384 571 RIYALPDDLVEVKPKMVMTVFACLMGRGLNKV 602
Cdd:cd21334   81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
491-598 1.27e-54

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: 180.55  E-value: 1.27e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 491 VNDDVIIKWVNQTLAKANKETSITSFKDKSISTSLPVLDLIDAIAPRAVRPEMVkREDLSYQDKMNNAKYAISVARKIGA 570
Cdd:cd21301    1 ISDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLV-LEGNSEEDKLSNAKYAISMARKIGA 79
                         90       100
                 ....*....|....*....|....*...
gi 697835384 571 RIYALPDDLVEVKPKMVMTVFACLMGRG 598
Cdd:cd21301   80 RVYALPEDIVEVKPKMVMTVFACLMALD 107
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
96-208 6.91e-54

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: 178.92  E-value: 6.91e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  96 EEKVAFVNWINKALQDDPDCKHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDERAINKKK-LTPFTISENLNLALN 174
Cdd:cd21217    1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKpKNIFEATENLNLALN 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 697835384 175 SASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIK 208
Cdd:cd21217   81 AAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
367-482 3.04e-49

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: 166.69  E-value: 3.04e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 367 GESKEERTFRNWMNSLGVSPYVNHLYSDLSDALIIFQLYDMTRV-PVDWNHVNKPPyplLGGNMKKIENCNYAVELGKtK 445
Cdd:cd21219    1 EGSREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPgCVNWKKVNKPK---PLNKFKKVENCNYAVDLAK-K 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 697835384 446 AKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTLNVL 482
Cdd:cd21219   77 LGFSLVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
97-208 1.10e-44

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: 154.61  E-value: 1.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKALQDDPDCKHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDERAIN-KKKLTPFTISENLNLALNS 175
Cdd:cd21293    2 EKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINtKKVLNPWERNENHTLCLNS 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 697835384 176 ASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIK 208
Cdd:cd21293   82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIK 114
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
491-595 2.36e-43

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: 150.50  E-value: 2.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 491 VNDDVIIKWVNQTLAKANKETSITSFKDKSISTSLPVLDLIDAIAPRAVRPEMVKrEDLSYQDKMNNAKYAISVARKIGA 570
Cdd:cd21220    1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLVT-EGETDEEKEQNAKYAISLARKIGA 79
                         90       100
                 ....*....|....*....|....*
gi 697835384 571 RIYALPDDLVEVKPKMVMTVFACLM 595
Cdd:cd21220   80 VIFLLWEDIVEVKPKMILTFVASLM 104
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
91-210 5.17e-43

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: 150.29  E-value: 5.17e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  91 HSYSEEEKVAFVNWINKALQDDPDCKHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDERAINK-----KKLTPFTI 165
Cdd:cd21294    1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKpprknKPLNNFQM 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 697835384 166 SENLNLALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKAG 210
Cdd:cd21294   81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRRG 125
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
231-347 1.27e-42

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: 148.60  E-value: 1.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 231 EELDQLMKLSPEELLLRWVNYHLTNAGWQK--ISNFSQDIKDSRAYYHLLNQIAPKgdDCNELPVKIDFSgfhDKSDLRR 308
Cdd:cd21218    1 ETLESLLYLPPEEILLRWVNYHLKKAGPTKkrVTNFSSDLKDGEVYALLLHSLAPE--LCDKELVLEVLS---EEDLEKR 75
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 697835384 309 AECMLQQADKLGCRQFVTPADVVAGNPKLNLAFVANLFN 347
Cdd:cd21218   76 AEKVLQAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
365-482 2.53e-41

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: 145.26  E-value: 2.53e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 365 LEGEsKEERTFRNWMNSLGVSPYVNHLYSDLSDALIIFQLYDMTrVP--VDWNHVNKPPYPLLGGNMKKIENCNYAVELG 442
Cdd:cd21300    3 AEGE-REARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKV-IPgsVNWKKVNKAPASAEISRFKAVENTNYAVELG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 697835384 443 KTKaKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTLNVL 482
Cdd:cd21300   81 KQL-GFSLVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
231-347 1.86e-39

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: 140.01  E-value: 1.86e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 231 EELDQLMKLSPEELLLRWVNYHLTNAGW-QKISNFSQDIKDSRAYYHLLNQIAPkgDDCNELPVKIdfsgfhdkSDL-RR 308
Cdd:cd21297    1 ETLEQFLRLPPEQILLRWFNYHLKAANWpRRVSNFSKDVSDGENYTVLLNQLAP--ELCSRAPLQT--------TDLlQR 70
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 697835384 309 AECMLQQADKLGCRQFVTPADVVAGNPKLNLAFVANLFN 347
Cdd:cd21297   71 AEQVLQNAEKLDCRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
367-483 3.09e-35

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: 128.39  E-value: 3.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 367 GESKEERTFRNWMNSLGVSPYVNHLYSDLSDALIIFQLYD-MTRVPVDWNHVNKPPYPLlggNMKKIENCNYAVELGKtK 445
Cdd:cd21299    1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDkVSPGSVNWKHANKPPIKM---PFKKVENCNQVVKIGK-Q 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 697835384 446 AKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTLNVLS 483
Cdd:cd21299   77 LKFSLVNVAGNDIVQGNKKLILALLWQLMRYHMLQLLK 114
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
231-346 2.63e-33

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: 123.01  E-value: 2.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 231 EELDQLMKLSPEELLLRWVNYHLTNAGWQK-ISNFSQDIKDSRAYYHLLNQIAPkgDDCNELPVkidfsgfHDKSDLRRA 309
Cdd:cd21296    1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKtVTNFSSDVKDAEAYAYLLNVLAP--EHCDPATL-------EAKDPLERA 71
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 697835384 310 ECMLQQADKLGCRQFVTPADVVAGNPKLNLAFVANLF 346
Cdd:cd21296   72 KLVLEQAEKMNCKRYLTAKDIVEGSANLNLAFVAQIF 108
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
488-595 3.05e-27

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: 105.97  E-value: 3.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 488 GEKVNDDVIIKWVNQTLAKANKETSITSFKDKSISTSLPVLDLIDAIAPRAVRPEMV---KREDLSYQdkmnNAKYAISV 564
Cdd:cd21303    1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLVtpgNTEDEAYL----NAKLAISI 76
                         90       100       110
                 ....*....|....*....|....*....|.
gi 697835384 565 ARKIGARIYALPDDLVEVKPKMVMTVFACLM 595
Cdd:cd21303   77 ARKLGALIFLVPEDIVEVRPRLVLTFIGSLM 107
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
491-595 7.33e-24

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: 96.47  E-value: 7.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 491 VNDDVIIKWVNQTLAKANKETSITSFKDKSISTSLPVLDLIDAIAPRAVRPEMVKREDlSYQDKMNNAKYAISVARKIGA 570
Cdd:cd21302    2 MTDADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKGE-TDEEKRLNATYIISVARKLGC 80
                         90       100
                 ....*....|....*....|....*
gi 697835384 571 RIYALPDDLVEVKPKMVMTVFACLM 595
Cdd:cd21302   81 SIFLLPEDIVEVNQKMILILTASIM 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
95-210 3.35e-23

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: 94.66  E-value: 3.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384   95 EEEKVAFVNWINKALQDDPDCKHLLpmnpsdaSLFKCLADGILLCKMINFSQPDTIDERAINKKkltPFTISENLNLALN 174
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVT-------NFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 697835384  175 SAS-AIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKAG 210
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
239-351 1.18e-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: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  239 LSPEELLLRWVNYHLTNAGW-QKISNFSQDIKDSRAYYHLLNQIAPKGDDcnelPVKIDFSGFHdksDLRRAECMLQQA- 316
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPgVRVTNFTTDLRDGLALCALLNKLAPGLVD----KKKLNKSEFD---KLENINLALDVAe 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 697835384  317 DKLGCRQF-VTPADVVAGNPKLNLAFVANLFNTYPA 351
Cdd:pfam00307  74 KKLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
100-207 3.57e-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: 82.75  E-value: 3.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384   100 AFVNWINKALQDDPdckhllpmNPSDASLFKCLADGILLCKMINFSQPDTIDERAINKKKlTPFTISENLNLALNSASAI 179
Cdd:smart00033   2 TLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEKL 72
                           90       100
                   ....*....|....*....|....*...
gi 697835384   180 GCTVVNIGSQDLQEGkPHLVLGLLWQII 207
Cdd:smart00033  73 GGKVVLFEPEDLVEG-PKLILGVIWTLI 99
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
493-598 9.37e-18

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: 78.87  E-value: 9.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  493 DDVIIKWVNQTLAKANKETSITSFKdKSISTSLPVLDLIDAIAPRAVRPEMVKRedlSYQDKMNNAKYAISVAR-KIGAR 571
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKLNK---SEFDKLENINLALDVAEkKLGVP 79
                          90       100
                  ....*....|....*....|....*...
gi 697835384  572 IYAL-PDDLVEVKPKMVMTVFACLMGRG 598
Cdd:pfam00307  80 KVLIePEDLVEGDNKSVLTYLASLFRRF 107
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
100-208 1.50e-17

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: 78.15  E-value: 1.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 100 AFVNWINKALQDDPdckhllpmNPSDASLFKCLADGILLCKMINFSQPDTIDEraINKKKLTPFTISENLNLALNSASAI 179
Cdd:cd00014    3 ELLKWINEVLGEEL--------PVSITDLFESLRDGVLLCKLINKLSPGSIPK--INKKPKSPFKKRENINLFLNACKKL 72
                         90       100       110
                 ....*....|....*....|....*....|.
gi 697835384 180 G-CTVVNIGSQDLQEGK-PHLVLGLLWQIIK 208
Cdd:cd00014   73 GlPELDLFEPEDLYEKGnLKKVLGTLWALAL 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
371-477 2.55e-16

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: 75.02  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  371 EERTFRNWMNSL----GVSPYVNHLYSDLSDALIIFQLYDMTRvP--VDWNHVNKPPypllggnMKKIENCNYAVELGKT 444
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 697835384  445 KAKFSLVGIAGHDLNEGNPTLTLALVWQLMRRY 477
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
243-346 1.09e-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: 72.73  E-value: 1.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384   243 ELLLRWVNYHLTNAGWQKISNFSQDIKDSRAYYHLLNQIAPkgDDCNELPVKIDFSGFHDKSDLRRAecmLQQADKLGC- 321
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSP--GLVDKKKVAASLSRFKKIENINLA---LSFAEKLGGk 75
                           90       100
                   ....*....|....*....|....*
gi 697835384   322 RQFVTPADVVAGnPKLNLAFVANLF 346
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLI 99
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
373-476 3.83e-15

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 71.19  E-value: 3.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384   373 RTFRNWMNSLGV---SPYVNHLYSDLSDALIIFQLYDMTRVP-VDWNHVNKPPYPllggnMKKIENCNYAVELGKtKAKF 448
Cdd:smart00033   1 KTLLRWVNSLLAeydKPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAE-KLGG 74
                           90       100
                   ....*....|....*....|....*...
gi 697835384   449 SLVGIAGHDLNEGNPtLTLALVWQLMRR 476
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 ...
94-208 7.19e-15

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: 70.77  E-value: 7.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  94 SEEEKvAFVNWINKalqddpdckhlLPMNPSDASLFKCLADGILLCKMINFSQPDTID-ERAINKKKLTPFTISENLNLA 172
Cdd:cd21219    3 SREER-AFRMWLNS-----------LGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNwKKVNKPKPLNKFKKVENCNYA 70
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 697835384 173 LNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIK 208
Cdd:cd21219   71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
494-595 2.43e-12

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: 63.49  E-value: 2.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384   494 DVIIKWVNQTLAKANKeTSITSFkDKSISTSLPVLDLIDAIAPRAVrPEMVKREDLSYQDKMNNAKYAISVARKIG-ARI 572
Cdd:smart00033   1 KTLLRWVNSLLAEYDK-PPVTNF-SSDLKDGVALCALLNSLSPGLV-DKKKVAASLSRFKKIENINLALSFAEKLGgKVV 77
                           90       100
                   ....*....|....*....|...
gi 697835384   573 YALPDDLVEvKPKMVMTVFACLM 595
Cdd:smart00033  78 LFEPEDLVE-GPKLILGVIWTLI 99
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
101-207 4.21e-12

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: 63.08  E-value: 4.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 101 FVNWINKALQddpdckhllPMNPSDASLFKCLADGILLCKMINFSQPDTIdeRAINKKKLTPFTISENLNLALNSASAIG 180
Cdd:cd21227    9 FTNWVNEQLK---------PTGMSVEDLATDLEDGVKLIALVEILQGRKL--GRVIKKPLNQHQKLENVTLALKAMAEDG 77
                         90       100
                 ....*....|....*....|....*..
gi 697835384 181 CTVVNIGSQDLQEGKPHLVLGLLWQII 207
Cdd:cd21227   78 IKLVNIGNEDIVNGNLKLILGLIWHLI 104
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
94-209 8.12e-11

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: 59.56  E-value: 8.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  94 SEEEKvAFVNWINKalqddpdckhlLPMNPSDASLFKCLADGILLCKMINFSQPDTIDERAINK---KKLTPFTISENLN 170
Cdd:cd21298    5 TREEK-TYRNWMNS-----------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKpfkKLGANMKKIENCN 72
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 697835384 171 LALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKA 209
Cdd:cd21298   73 YAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRA 111
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
366-476 4.90e-10

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409042  Cd Length: 116  Bit Score: 57.31  E-value: 4.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMNSL--GVSPYVNHLYSDLSDALIIFQLYDMtrvpVDWNHVNKPPYpllgGNMK--KIENCNYAVEL 441
Cdd:cd21193   12 ERINIQKKTFTKWINSFleKANLEIGDLFTDLSDGKLLLKLLEI----ISGEKLGKPNR----GRLRvqKIENVNKALAF 83
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 697835384 442 GKTKAKFSLVGiaGHDLNEGNPTLTLALVWQLMRR 476
Cdd:cd21193   84 LKTKVRLENIG--AEDIVDGNPRLILGLIWTIILR 116
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
95-208 1.93e-09

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: 55.51  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  95 EEEKVAFVNWINKalqddpdckhlLPMNPSDASLFKCLADGILLCKMINFSQPDTIDERAINKKK----LTPFTISENLN 170
Cdd:cd21300    6 EREARVFTLWLNS-----------LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaeISRFKAVENTN 74
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 697835384 171 LALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIK 208
Cdd:cd21300   75 YAVELGKQLGFSLVGIQGADITDGSRTLTLALVWQLMR 112
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
366-476 3.73e-09

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: 55.42  E-value: 3.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMNS--LGVSPYVNHLYSDLSDALIIFQLYDMtrvpVDWNHVNKPPYpllgGNMK--KIENCNYAVEL 441
Cdd:cd21318   34 EREAVQKKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLEV----LSGEQLPKPTR----GRMRihSLENVDKALQF 105
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 697835384 442 GKTKaKFSLVGIAGHDLNEGNPTLTLALVWQLMRR 476
Cdd:cd21318  106 LKEQ-RVHLENVGSHDIVDGNHRLTLGLIWTIILR 139
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
95-216 6.29e-09

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: 53.92  E-value: 6.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  95 EEEKV---AFVNWINKALqddpdCKHLLPMNPSDasLFKCLADGILLCKMINFSQPDTID-ERAINKKKLTPFTiseNLN 170
Cdd:cd21241    1 EQERVqkkTFTNWINSYL-----AKRKPPMKVED--LFEDIKDGTKLLALLEVLSGEKLPcEKGRRLKRVHFLS---NIN 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 697835384 171 LALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIkagLFADIE 216
Cdd:cd21241   71 TALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTII---LYFQIE 113
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
366-476 7.51e-09

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: 53.91  E-value: 7.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMNS--LGVSPYVNHLYSDLSDALIIFQLYDMtrvpVDWNHVNKPPYpllgGNMK--KIENCNYAVEL 441
Cdd:cd21246   12 EREAVQKKTFTKWVNShlARVGCRINDLYTDLRDGRMLIKLLEV----LSGERLPKPTK----GKMRihCLENVDKALQF 83
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 697835384 442 GKTKaKFSLVGIAGHDLNEGNPTLTLALVWQLMRR 476
Cdd:cd21246   84 LKEQ-RVHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
97-207 9.13e-09

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: 53.68  E-value: 9.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKALQddpdcKHLLPMNPSDasLFKCLADGILLCKMIN-FSQPDTIDERAINkkkltPFTISENLNLALNS 175
Cdd:cd21242    6 QKRTFTNWINSQLA-----KHSPPSVVSD--LFTDIQDGHRLLDLLEvLSGQQLPREKGHN-----VFQCRSNIETALSF 73
                         90       100       110
                 ....*....|....*....|....*....|..
gi 697835384 176 ASAIGCTVVNIGSQDLQEGKPHLVLGLLWQII 207
Cdd:cd21242   74 LKNKSIKLINIHVPDIIEGKPSIILGLIWTII 105
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
371-477 1.07e-08

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 53.17  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 371 EERTFRNWMN----SLGVSpyVNHLYSDLSDALIIFQLYDMTRVPVDWNHVNKPPYpllggNMKKIENCNYAVELGKTKa 446
Cdd:cd21215    5 QKKTFTKWLNtklsSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKM-----RVQKLENVNKALEFIKSR- 76
                         90       100       110
                 ....*....|....*....|....*....|.
gi 697835384 447 KFSLVGIAGHDLNEGNPTLTLALVWQLMRRY 477
Cdd:cd21215   77 GVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
97-209 1.13e-08

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 53.17  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKALQddpdcKHLLPMNpsdaSLFKCLADGILLCKMINFSQPDTIDERAINKK----KLtpftisENLNLA 172
Cdd:cd21215    5 QKKTFTKWLNTKLS-----SRGLSIT----DLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKmrvqKL------ENVNKA 69
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 697835384 173 LNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKA 209
Cdd:cd21215   70 LEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILR 106
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
493-588 3.12e-08

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: 51.92  E-value: 3.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 493 DDVIIKWVNQTLAKAN-KETSITSFkDKSISTSLPVLDLIDAIAPRAVRPEMVKrEDLSYQDKMNNAKYAISVARKIGAR 571
Cdd:cd21218   12 EEILLRWVNYHLKKAGpTKKRVTNF-SSDLKDGEVYALLLHSLAPELCDKELVL-EVLSEEDLEKRAEKVLQAAEKLGCK 89
                         90
                 ....*....|....*..
gi 697835384 572 IYALPDDLVEVKPKMVM 588
Cdd:cd21218   90 YFLTPEDIVSGNPRLNL 106
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
366-480 3.75e-08

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: 52.29  E-value: 3.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMNS--LGVSPYVNHLYSDLSDALIIFQLYDMtrvpvdwnhVNKPPYPLLGGNMK--KIENCNYAVEL 441
Cdd:cd21236   13 ERDKVQKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEV---------LSGDTLPREKGRMRfhRLQNVQIALDY 83
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 697835384 442 GKtKAKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTLN 480
Cdd:cd21236   84 LK-RRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 121
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
101-207 4.61e-08

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: 51.33  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 101 FVNWINKalqddpdckHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIdERAINKKKLTPFTISENLNLALNSASAIG 180
Cdd:cd21183    9 FTRWCNE---------HLKERGMQIHDLATDFSDGLCLIALLENLSTRPL-KRSYNRRPAFQQHYLENVSTALKFIEADH 78
                         90       100
                 ....*....|....*....|....*..
gi 697835384 181 CTVVNIGSQDLQEGKPHLVLGLLWQII 207
Cdd:cd21183   79 IKLVNIGSGDIVNGNIKLILGLIWTLI 105
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
97-207 6.15e-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: 6.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKALQDdpdckhlLPMNPSDasLFKCLADGILLCKMINFSQPDTIDEraINKKKLTPFTIsENLNLALNSA 176
Cdd:cd21193   17 QKKTFTKWINSFLEK-------ANLEIGD--LFTDLSDGKLLLKLLEIISGEKLGK--PNRGRLRVQKI-ENVNKALAFL 84
                         90       100       110
                 ....*....|....*....|....*....|.
gi 697835384 177 SAiGCTVVNIGSQDLQEGKPHLVLGLLWQII 207
Cdd:cd21193   85 KT-KVRLENIGAEDIVDGNPRLILGLIWTII 114
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
97-216 8.01e-08

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: 51.03  E-value: 8.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKALQddpdcKHLLPMNPSDasLFKCLADGILLCKMINFSQPDTIDERaiNKKKLTPFTISENLNLALNSA 176
Cdd:cd21190    6 QKKTFTNWINSHLA-----KLSQPIVIND--LFVDIKDGTALLRLLEVLSGQKLPIE--SGRVLQRAHKLSNIRNALDFL 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 697835384 177 SAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIkagLFADIE 216
Cdd:cd21190   77 TKRCIKLVNINSTDIVDGKPSIVLGLIWTII---LYFQIE 113
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
366-476 1.24e-07

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: 50.82  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMNS-LG-VSPYVNHLYSDLSDALIIFQLYDMtrvpVDWNHVNKPPypllGGNMKK--IENCNYAVEL 441
Cdd:cd21317   27 EREAVQKKTFTKWVNShLArVTCRIGDLYTDLRDGRMLIRLLEV----LSGEQLPKPT----KGRMRIhcLENVDKALQF 98
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 697835384 442 GKTKaKFSLVGIAGHDLNEGNPTLTLALVWQLMRR 476
Cdd:cd21317   99 LKEQ-KVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
366-489 1.38e-06

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: 47.71  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMNS--LGVSPYVNHLYSDLSDALIIFQLYDMtrvpvdwnhVNKPPYPLLGGNMK--KIENCNYAVEL 441
Cdd:cd21235    2 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 697835384 442 GKTKaKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTLNVLSDLGEGE 489
Cdd:cd21235   73 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
240-335 1.72e-06

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: 46.85  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 240 SPEELLLRWVNYHLTNAgwqKISNFSQDIKDSRAYYHLLNQIAPKGDDcnelpvkiDFSGFHDKSDLRRAECMLQQA-DK 318
Cdd:cd21184    1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIP--------DNESLDKENPLENATKAMDIAeEE 69
                         90
                 ....*....|....*..
gi 697835384 319 LGCRQFVTPADVVAGNP 335
Cdd:cd21184   70 LGIPKIITPEDMVSPNV 86
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
366-487 1.79e-06

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: 47.33  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMNS--LGVSPYVNHLYSDLSDALIIFQLYDMtrvpvdwnhVNKPPYPLLGGNMK--KIENCNYAVEL 441
Cdd:cd21237    2 ERDRVQKKTFTKWVNKhlMKVRKHINDLYEDLRDGHNLISLLEV---------LSGVKLPREKGRMRfhRLQNVQIALDF 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 697835384 442 GKTKaKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTLNVLSDLGE 487
Cdd:cd21237   73 LKQR-QVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGE 117
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
93-218 2.12e-06

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: 47.29  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  93 YSEEEKV---AFVNWINKalqddpdckHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDErainKKKLTPFTISENL 169
Cdd:cd21236   11 KDERDKVqkkTFTKWINQ---------HLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHRLQNV 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 697835384 170 NLALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKAGLFADIEIS 218
Cdd:cd21236   78 QIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVT 126
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
94-208 2.36e-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: 46.90  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  94 SEEEKvAFVNWINKalqddpdckhlLPMNPSDASLFKCLADGILLCKMINFSQPdTIDERAINKKkltPFTI-------S 166
Cdd:cd21329    5 SSEER-TFRNWMNS-----------LGVNPYVNHLYSDLCDALVIFQLYEMTRV-PVDWGHVNKP---PYPAlggnmkkI 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 697835384 167 ENLNLALN-SASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIK 208
Cdd:cd21329   69 ENCNYAVElGKNKAKFSLVGIAGSDLNEGNKTLTLALIWQLMR 111
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
97-207 5.03e-06

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 45.47  E-value: 5.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKalqddpdckHLLPMNPSDASLFKCLADGILLCKMINFSQPDTID-ERAINKkkltpFTISENLNLALNS 175
Cdd:cd21188    4 QKKTFTKWVNK---------HLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPrERGRMR-----FHRLQNVQTALDF 69
                         90       100       110
                 ....*....|....*....|....*....|..
gi 697835384 176 ASAIGCTVVNIGSQDLQEGKPHLVLGLLWQII 207
Cdd:cd21188   70 LKYRKIKLVNIRAEDIVDGNPKLTLGLIWTII 101
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
97-218 5.15e-06

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: 45.79  E-value: 5.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKalqddpdckHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDErainKKKLTPFTISENLNLALNSA 176
Cdd:cd21235    7 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 697835384 177 SAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKAGLFADIEIS 218
Cdd:cd21235   74 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 115
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
371-477 5.20e-06

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


Pssm-ID: 409076  Cd Length: 109  Bit Score: 45.36  E-value: 5.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 371 EERTFRNWMNS----LGVSpyVNHLYSDLSDALIIFQLYDMTRVPVDWNHVNKPPYPLlggnmKKIENCNYAVELgKTKA 446
Cdd:cd21227    5 QKNTFTNWVNEqlkpTGMS--VEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQH-----QKLENVTLALKA-MAED 76
                         90       100       110
                 ....*....|....*....|....*....|.
gi 697835384 447 KFSLVGIAGHDLNEGNPTLTLALVWQLMRRY 477
Cdd:cd21227   77 GIKLVNIGNEDIVNGNLKLILGLIWHLILRY 107
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
487-594 5.48e-06

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: 46.03  E-value: 5.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 487 EGEKVND-------DVIIKWVNQTLAKANKETsITSFKdKSISTSLPVLDLIDAIAPRAVRPEMVKREDLS---YQDKMN 556
Cdd:cd21326    1 EGEELEElmklspeELLLRWVNYHLTNAGWQN-ISNFS-QDIKDSRAYFHLLNQIAPKGDVFDENIEIDFSgfnEKNDLK 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 697835384 557 NAKYAISVARKIGARIYALPDDLVEVKPKMVMTVFACL 594
Cdd:cd21326   79 RAEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANL 116
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
94-208 7.60e-06

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: 45.19  E-value: 7.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  94 SEEEKvAFVNWINKalqddpdckhlLPMNPSDASLFKCLADGILLCKMINFSQPDTIDERAINKKKLT-PFTISENLNLA 172
Cdd:cd21299    3 SREER-CFRLWINS-----------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKmPFKKVENCNQV 70
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 697835384 173 LNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIK 208
Cdd:cd21299   71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMR 106
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
430-475 8.09e-06

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: 45.26  E-value: 8.09e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 697835384 430 KKIENCNYAVELGKtKAKFSLVGIAGHDLNEGNPTLTLALVWQLMR 475
Cdd:cd21217   70 EATENLNLALNAAK-KIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
100-152 1.13e-05

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


Pssm-ID: 409052 [Multi-domain]  Cd Length: 112  Bit Score: 44.71  E-value: 1.13e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 697835384 100 AFVNWINKALQDDpdckhlLPMNPSDASLFKCLADGILLCKMINFSQPDTIDE 152
Cdd:cd21203    4 EAAEWIQNVLGVL------VLPDPSEEEFRLCLRDGVVLCKLLNKLQPGAVPK 50
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
371-471 1.17e-05

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: 44.68  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 371 EERTFRNWMNSLGV---SPYVNHLYSDLSDALIIFQLYDMtrvpvdwnhvnkppypLLGGNMKK---------IENCNYA 438
Cdd:cd21186    3 QKKTFTKWINSQLSkanKPPIKDLFEDLRDGTRLLALLEV----------------LTGKKLKPekgrmrvhhLNNVNRA 66
                         90       100       110
                 ....*....|....*....|....*....|....
gi 697835384 439 VE-LGKTKAKfsLVGIAGHDLNEGNPTLTLALVW 471
Cdd:cd21186   67 LQvLEQNNVK--LVNISSNDIVDGNPKLTLGLVW 98
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
245-345 1.28e-05

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: 44.19  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 245 LLRWVNYHLTNAG-WQKISNFS-QDIKDSRAYYHLLNQIAPKGddcnelpvkIDFS----GFHDKSDLRRAECMLQQADK 318
Cdd:cd21301    6 IVEWANEKLKSAGkSTSISSFKdPSISTSLPILDLIDAIKPGS---------VDYSlvleGNSEEDKLSNAKYAISMARK 76
                         90       100
                 ....*....|....*....|....*..
gi 697835384 319 LGCRQFVTPADVVAGNPKLNLAFVANL 345
Cdd:cd21301   77 IGARVYALPEDIVEVKPKMVMTVFACL 103
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
231-355 1.85e-05

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


Pssm-ID: 409163  Cd Length: 115  Bit Score: 44.29  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 231 EELDQLMKLSPEELLLRWVNYHLTNAgwqKISNFSQDIKDSRAYYHLLNQIAPkgddcNELPvkiDFSGFHDKSDLRRAE 310
Cdd:cd21314    2 EDEEDARKQTPKQRLLGWIQNKVPQL---PITNFNRDWQDGKALGALVDNCAP-----GLCP---DWESWDPNQPVQNAR 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 697835384 311 CMLQQADK-LGCRQFVTPADVVagNPKLNLAFVANLFNTYP-ALHKP 355
Cdd:cd21314   71 EAMQQADDwLGVPQVIAPEEIV--DPNVDEHSVMTYLSQFPkAKLKP 115
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
371-471 1.94e-05

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: 43.93  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 371 EERTFRNWMNS--LGVSPYVNHLYSDLSDALIIFQLYDMtrvpvdwnhVNKPPYPLLGGNMK--KIENCNYAVELGKTKa 446
Cdd:cd21188    4 QKKTFTKWVNKhlIKARRRVVDLFEDLRDGHNLISLLEV---------LSGESLPRERGRMRfhRLQNVQTALDFLKYR- 73
                         90       100
                 ....*....|....*....|....*
gi 697835384 447 KFSLVGIAGHDLNEGNPTLTLALVW 471
Cdd:cd21188   74 KIKLVNIRAEDIVDGNPKLTLGLIW 98
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
371-477 2.27e-05

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: 43.62  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 371 EERTFRNWMNS--LGVSPYVNHLYSDLSDAL-IIFQLYDMTRVPVDWNHVNKPPYPllggnMKKIENCNYAVELgKTKAK 447
Cdd:cd21183    5 QANTFTRWCNEhlKERGMQIHDLATDFSDGLcLIALLENLSTRPLKRSYNRRPAFQ-----QHYLENVSTALKF-IEADH 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 697835384 448 FSLVGIAGHDLNEGNPTLTLALVWQLMRRY 477
Cdd:cd21183   79 IKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
366-476 2.36e-05

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: 44.65  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMNS--LGVSPYVNHLYSDLSDALIIFQLYDM---TRVPvdwnhvnKPPypllGGNMKK--IENCNYA 438
Cdd:cd21316   49 EREAVQKKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLEVlsgERLP-------KPT----KGRMRIhcLENVDKA 117
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 697835384 439 VELGKTKaKFSLVGIAGHDLNEGNPTLTLALVWQLMRR 476
Cdd:cd21316  118 LQFLKEQ-RVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
231-350 2.73e-05

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


Pssm-ID: 409161  Cd Length: 114  Bit Score: 43.64  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 231 EELDQLMKLSPEELLLRWVNYHLTNAgwqKISNFSQDIKDSRAYYHLLNQIAPKgddcnelpVKIDFSGFHDKSDLRRAE 310
Cdd:cd21312    3 EEDEEAKKQTPKQRLLGWIQNKLPQL---PITNFSRDWQSGRALGALVDSCAPG--------LCPDWDSWDASKPVTNAR 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 697835384 311 CMLQQADK-LGCRQFVTPADVVagNPKLNLAFVANLFNTYP 350
Cdd:cd21312   72 EAMQQADDwLGIPQVITPEEIV--DPNVDEHSVMTYLSQFP 110
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
369-475 4.83e-05

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: 43.88  E-value: 4.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 369 SKEER-TFRNWMNS-----------LGVSPYVNHLYSDLSDALIIFQLYDMTRV-PVDWNHVNKP---PYPLlggnmkkI 432
Cdd:cd21323   22 SEEEKvAFVNWINKalegdpdckhvVPMNPTDESLFKSLADGILLCKMINLSQPdTIDERAINKKkltPFTI-------S 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 697835384 433 ENCNYAVElGKTKAKFSLVGIAGHDLNEGNPTLTLALVWQLMR 475
Cdd:cd21323   95 ENLNLALN-SASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIK 136
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
366-474 6.22e-05

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: 42.51  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMNSL---GVSP-YVNHLYSDLSDALIIFQLYDM---TRVPVDWNHvnkppypllgGNMKKIENCNYA 438
Cdd:cd21242    1 EQEQTQKRTFTNWINSQlakHSPPsVVSDLFTDIQDGHRLLDLLEVlsgQQLPREKGH----------NVFQCRSNIETA 70
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 697835384 439 VELGKTKAkFSLVGIAGHDLNEGNPTLTLALVWQLM 474
Cdd:cd21242   71 LSFLKNKS-IKLINIHVPDIIEGKPSIILGLIWTII 105
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
368-477 9.49e-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: 42.13  E-value: 9.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 368 ESKEERTFRNWMNSL----GVSPyVNHLYSDLSDAL-IIFQLYDMTRVPVdwnhvnKPPYPLLGGN-MKKIENCNYAVEL 441
Cdd:cd21225    2 EKVQIKAFTAWVNSVlekrGIPK-ISDLATDLSDGVrLIFFLELVSGKKF------PKKFDLEPKNrIQMIQNLHLAMLF 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 697835384 442 GKTKAKFSLVGIAGHDLNEGNPTLTLALVWQLMRRY 477
Cdd:cd21225   75 IEEDLKIRVQGIGAEDFVDNNKKLILGLLWTLYRKY 110
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
366-477 1.16e-04

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


Pssm-ID: 409090  Cd Length: 113  Bit Score: 41.98  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMNS--LGVSP--YVNHLYSDLSDA---LIIFQLYDMTRVPVDwnhvnkppyplLGGNMKKIE---NC 435
Cdd:cd21241    1 EQERVQKKTFTNWINSylAKRKPpmKVEDLFEDIKDGtklLALLEVLSGEKLPCE-----------KGRRLKRVHflsNI 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 697835384 436 NYAVELGKTKaKFSLVGIAGHDLNEGNPTLTLALVWQLMRRY 477
Cdd:cd21241   70 NTALKFLESK-KIKLVNINPTDIVDGKPSIVLGLIWTIILYF 110
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
97-208 1.42e-04

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: 42.29  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKalqddpdckhlLPMNPSDASLFKCLADGILLCKMINFSQPdTIDERAINK----------KKLtpftis 166
Cdd:cd21331   23 EERTFRNWMNS-----------LGVNPHVNHLYGDLQDALVILQLYEKIKV-PVDWNKVNKppypklganmKKL------ 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 697835384 167 ENLNLALN-SASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIK 208
Cdd:cd21331   85 ENCNYAVElGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMR 127
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
123-195 1.51e-04

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


Pssm-ID: 409056 [Multi-domain]  Cd Length: 107  Bit Score: 41.14  E-value: 1.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697835384 123 PSDASLFKCLADGILLCKMINFSQPDTIdeRAINKKKLtPFTISENLNLALNSASAIGCTVVNI-GSQDLQEGK 195
Cdd:cd21207   23 DDGKDYEDVLKDGVILCKLINILKPGSV--KKINTSKM-AFKLMENIENFLTACKGYGVPKTDLfQTVDLYEKK 93
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
242-346 1.59e-04

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: 41.10  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 242 EELLLRWVNYHLTNAGWQ-KISNFS-QDIKDSRAYYHLLNQIAPKgddcnelpvKIDFS----GFHDKSDLRRAECMLQQ 315
Cdd:cd21220    3 DADILAWANSKVREAGKSsPISSFKdPSLSTGLFLLDLLAAIDPG---------AVDYDlvteGETDEEKEQNAKYAISL 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 697835384 316 ADKLGCRQFVTPADVVAGNPKLNLAFVANLF 346
Cdd:cd21220   74 ARKIGAVIFLLWEDIVEVKPKMILTFVASLM 104
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
97-218 1.66e-04

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: 41.56  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKalqddpdckHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDErainKKKLTPFTISENLNLALNSA 176
Cdd:cd21237    7 QKKTFTKWVNK---------HLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPR----EKGRMRFHRLQNVQIALDFL 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 697835384 177 SAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIKAGLFADIEIS 218
Cdd:cd21237   74 KQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYIS 115
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
240-336 1.71e-04

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: 41.21  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 240 SPEELLLRWVNYHLTNagwQKISNFSQDIKDSRAYYHLLNQIAPkgddcNELPvkiDFSGFHDKSDLRRAECMLQQADK- 318
Cdd:cd21230    1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAP-----GLCP---DWETWDPNDALENATEAMQLAEDw 69
                         90
                 ....*....|....*...
gi 697835384 319 LGCRQFVTPADVVagNPK 336
Cdd:cd21230   70 LGVPQLITPEEII--NPN 85
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
132-180 1.88e-04

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


Pssm-ID: 409057 [Multi-domain]  Cd Length: 119  Bit Score: 41.17  E-value: 1.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 697835384 132 LADGILLCKMINFSQPDTIdeRAINKKKlTPFTISENLNLALNSASAIG 180
Cdd:cd21208   26 LEDGILLCELINAIKPGSI--KKINRLP-TPIAGLDNLNLFLKACEDLG 71
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
234-350 1.96e-04

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


Pssm-ID: 409162  Cd Length: 110  Bit Score: 41.23  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 234 DQLMKLSPEELLLRWVNYHLTnagWQKISNFSQDIKDSRAYYHLLNQIAPKgddcnelpVKIDFSGFHDKSDLRRAECML 313
Cdd:cd21313    2 DDAKKQTPKQRLLGWIQNKIP---YLPITNFNQNWQDGKALGALVDSCAPG--------LCPDWESWDPQKPVDNAREAM 70
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 697835384 314 QQADK-LGCRQFVTPADVVagNPKLNLAFVANLFNTYP 350
Cdd:cd21313   71 QQADDwLGVPQVITPEEII--HPDVDEHSVMTYLSQFP 106
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
368-474 2.32e-04

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: 40.84  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 368 ESKEERTFRNWMNSL--GVSPYVNHLYSDLSDALIIFQLYDMtrvpVDWNHVNKPPYpllgGNMK--KIENCNYAVELGK 443
Cdd:cd21214    3 EKQQRKTFTAWCNSHlrKAGTQIENIEEDFRDGLKLMLLLEV----ISGERLPKPER----GKMRfhKIANVNKALDFIA 74
                         90       100       110
                 ....*....|....*....|....*....|.
gi 697835384 444 TKAkFSLVGIAGHDLNEGNPTLTLALVWQLM 474
Cdd:cd21214   75 SKG-VKLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
229-338 3.15e-04

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: 40.53  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 229 EGEELDQLMK--LSPEELLLRWVNYHLTNagwQKISNFSQDIKDSRAYYHLLNQIAPkgddcNELPvkiDFSGFHDKSDL 306
Cdd:cd21315    3 EGEDDGPDDGkgPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAP-----GLCP---DWEDWDPKDAV 71
                         90       100       110
                 ....*....|....*....|....*....|...
gi 697835384 307 RRAECMLQQADK-LGCRQFVTPADVVagNPKLN 338
Cdd:cd21315   72 KNAKEAMDLAEDwLDVPQLIKPEEMV--NPKVD 102
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
227-345 3.97e-04

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: 40.32  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 227 LNEGEELDqlmklspEELLLRWVNYHLTNAGWQ-KISNFS-QDIKDSRAYYHLLNQIAPKGDDcNELPVKIDFSgfhDKS 304
Cdd:cd21332    2 LGEGEKVN-------DEIIIKWVNQTLANANKTtSITSFKdKSISTSLPVLDLIDAIAPNAIR-EEMVKREDLS---DAD 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 697835384 305 DLRRAECMLQQADKLGCRQFVTPADVVAGNPKLNLAFVANL 345
Cdd:cd21332   71 KLNNAKYAISVARKIGARVYALPEDLVEVKPKMVMTVFACL 111
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
15-42 4.39e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.74  E-value: 4.39e-04
                           10        20
                   ....*....|....*....|....*...
gi 697835384    15 ELKEAFSKIDIDNSGYVSDYELQDLFKE 42
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKA 28
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
242-347 4.45e-04

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 40.01  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 242 EELLLRWVNYHLTNAGWQKISNFSQDIKDSRAYYHLLNQIAPKGDDCNELPVKidfSGFHDKSDLRRAecmLQQADKLGC 321
Cdd:cd00014    1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPK---SPFKKRENINLF---LNACKKLGL 74
                         90       100
                 ....*....|....*....|....*....
gi 697835384 322 --RQFVTPADVVA-GNPKLNLAFVANLFN 347
Cdd:cd00014   75 peLDLFEPEDLYEkGNLKKVLGTLWALAL 103
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
15-48 4.72e-04

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 38.68  E-value: 4.72e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 697835384  15 ELKEAFSKIDIDNSGYVSDYELQDLFKEANLPLP 48
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS 34
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
371-477 4.73e-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: 39.78  E-value: 4.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 371 EERTFRNWMNS--LGVSPYVNHLYSDLSDALIIFQLYDM---TRVPVDWNhvNKPPYpllggNMKKIENCNYAVELGKTK 445
Cdd:cd21228    5 QQNTFTRWCNEhlKCVNKRIYNLETDLSDGLRLIALLEVlsqKRMYKKYN--KRPTF-----RQMKLENVSVALEFLERE 77
                         90       100       110
                 ....*....|....*....|....*....|..
gi 697835384 446 aKFSLVGIAGHDLNEGNPTLTLALVWQLMRRY 477
Cdd:cd21228   78 -SIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
101-207 4.82e-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: 39.78  E-value: 4.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 101 FVNWINKalqddpdckHLLPMNPSDASLFKCLADGILLCKMIN-FSQPDTidERAINKKKLTPFTISENLNLALNSASAI 179
Cdd:cd21228    9 FTRWCNE---------HLKCVNKRIYNLETDLSDGLRLIALLEvLSQKRM--YKKYNKRPTFRQMKLENVSVALEFLERE 77
                         90       100
                 ....*....|....*....|....*...
gi 697835384 180 GCTVVNIGSQDLQEGKPHLVLGLLWQII 207
Cdd:cd21228   78 SIKLVSIDSSAIVDGNLKLILGLIWTLI 105
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
96-207 5.29e-04

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: 39.68  E-value: 5.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  96 EEKVAFVNWINKalqddpdckHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDERaiNKKKLTPFTISeNLNLALNS 175
Cdd:cd21214    5 QQRKTFTAWCNS---------HLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKP--ERGKMRFHKIA-NVNKALDF 72
                         90       100       110
                 ....*....|....*....|....*....|..
gi 697835384 176 ASAIGCTVVNIGSQDLQEGKPHLVLGLLWQII 207
Cdd:cd21214   73 IASKGVKLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
494-594 5.51e-04

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 39.63  E-value: 5.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 494 DVIIKWVNQTLAKANKEtSITSFKDkSISTSLPVLDLIDAIAPRAVrpEMVKREDLSYQDKMNNAKYAISVARKIGARIY 573
Cdd:cd00014    2 EELLKWINEVLGEELPV-SITDLFE-SLRDGVLLCKLINKLSPGSI--PKINKKPKSPFKKRENINLFLNACKKLGLPEL 77
                         90       100
                 ....*....|....*....|....
gi 697835384 574 AL--PDDLVEVK-PKMVMTVFACL 594
Cdd:cd00014   78 DLfePEDLYEKGnLKKVLGTLWAL 101
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
97-207 8.08e-04

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


Pssm-ID: 409167  Cd Length: 139  Bit Score: 40.01  E-value: 8.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKALQDdpdckhlLPMNPSDasLFKCLADGILLCKMINFSQPDTIDERAINKKKLTPFtisENLNLALNSA 176
Cdd:cd21318   39 QKKTFTKWVNSHLAR-------VPCRIND--LYTDLRDGYVLTRLLEVLSGEQLPKPTRGRMRIHSL---ENVDKALQFL 106
                         90       100       110
                 ....*....|....*....|....*....|.
gi 697835384 177 SAIGCTVVNIGSQDLQEGKPHLVLGLLWQII 207
Cdd:cd21318  107 KEQRVHLENVGSHDIVDGNHRLTLGLIWTII 137
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
371-477 8.23e-04

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


Pssm-ID: 409096  Cd Length: 125  Bit Score: 39.74  E-value: 8.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 371 EERTFRNWMNSL----GVSPYVNHLYSDLSDALIIFQLYDMtrvpVDWNHVNKPPYpllgGNMKK--IENCNYAVELGKT 444
Cdd:cd21247   21 QKKTFTKWMNNVfsknGAKIEITDIYTELKDGIHLLRLLEL----ISGEQLPRPSR----GKMRVhfLENNSKAITFLKT 92
                         90       100       110
                 ....*....|....*....|....*....|...
gi 697835384 445 KAKFSLVGiaGHDLNEGNPTLTLALVWQLMRRY 477
Cdd:cd21247   93 KVPVKLIG--PENIVDGDRTLILGLIWIIILRF 123
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
242-345 9.85e-04

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: 39.20  E-value: 9.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 242 EELLLRWVNYHLTNAG-WQKISNFSQ-DIKDSRAYYHLLNQIAPKGDDCNELPVKidfsGFHDKSDLRRAECMLQQADKL 319
Cdd:cd21333    8 DETIVNWVNETLTEAGkSSSISSFKDgKISTSMPVLDLIDAIQPGSINYDLLKTE----DLNDEEKLNNAKYAISMARKI 83
                         90       100
                 ....*....|....*....|....*.
gi 697835384 320 GCRQFVTPADVVAGNPKLNLAFVANL 345
Cdd:cd21333   84 GARVYALPEDLVEVKPKMVMTVFACL 109
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
391-476 1.07e-03

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 39.35  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 391 LYSDLSDALIIFQLYDMTrVP--VDWNHVNKPP---YPLlgGNMKKIENCNYAVELGKTKAkFSLVGIAGHDLNEGNPTL 465
Cdd:cd21294   38 LFDECKDGLVLSKLINDS-VPdtIDERVLNKPPrknKPL--NNFQMIENNNIVINSAKAIG-CSVVNIGAGDIIEGREHL 113
                         90
                 ....*....|.
gi 697835384 466 TLALVWQLMRR 476
Cdd:cd21294  114 ILGLIWQIIRR 124
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
15-42 1.26e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 36.61  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....*...
gi 697835384   15 ELKEAFSKIDIDNSGYVSDYELQDLFKE 42
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
168-207 1.37e-03

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: 38.52  E-value: 1.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 697835384 168 NLNLALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQII 207
Cdd:cd21186   62 NVNRALQVLEQNNVKLVNISSNDIVDGNPKLTLGLVWSII 101
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
369-476 1.88e-03

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: 39.19  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 369 SKEERT-FRNWMNS-----------LGVSPYVNHLYSDLSDALIIFQLYDMTrVP--VDWNHVNKPPYPLLggnmKKIEN 434
Cdd:cd21292   22 SEEEKVaFVNWINKnlgddpdckhlLPMDPNTDDLFEKVKDGILLCKMINLS-VPdtIDERAINKKKLTVF----TIHEN 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 697835384 435 CNYAVE----LGKTkakfsLVGIAGHDLNEGNPTLTLALVWQLMRR 476
Cdd:cd21292   97 LTLALNsasaIGCN-----VVNIGAEDLKEGKPHLVLGLLWQIIRI 137
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
366-474 1.96e-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: 38.32  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMNS----LGVSPYVNHLYSDLSDALIIFQLYDM---TRVPVDWNHVNKppypllggNMKKIENCNYA 438
Cdd:cd21190    1 EQERVQKKTFTNWINShlakLSQPIVINDLFVDIKDGTALLRLLEVlsgQKLPIESGRVLQ--------RAHKLSNIRNA 72
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 697835384 439 VELgKTKAKFSLVGIAGHDLNEGNPTLTLALVWQLM 474
Cdd:cd21190   73 LDF-LTKRCIKLVNINSTDIVDGKPSIVLGLIWTII 107
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
97-207 2.17e-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: 37.98  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKALQDdpdckhllPMNPSDASLFKCLADGILLCKMINfsqpDTIDERAINKKKLTPFTISENLNLALNSA 176
Cdd:cd21231    7 QKKTFTKWINAQFAK--------FGKPPIEDLFTDLQDGRRLLELLE----GLTGQKLVKEKGSTRVHALNNVNKALQVL 74
                         90       100       110
                 ....*....|....*....|....*....|.
gi 697835384 177 SAIGCTVVNIGSQDLQEGKPHLVLGLLWQII 207
Cdd:cd21231   75 QKNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
242-345 2.25e-03

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: 37.95  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 242 EELLLRWVNYHLTNAGWQ-KISNFS-QDIKDSRAYYHLLNQIAPkGDDCNELPVKIDFSgfhDKSDLRRAECMLQQADKL 319
Cdd:cd21334    3 DDIIVNWVNRTLSEAGKStSIQNFKdKTISSSLAVVDLIDAIQP-GCINYDLVKTGNLT---DDDKLDNAKYAVSMARKI 78
                         90       100
                 ....*....|....*....|....*.
gi 697835384 320 GCRQFVTPADVVAGNPKLNLAFVANL 345
Cdd:cd21334   79 GARVYALPEDLVEVKPKMVMTVFACL 104
EF-hand_6 pfam13405
EF-hand domain;
15-41 2.42e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 35.62  E-value: 2.42e-03
                          10        20
                  ....*....|....*....|....*..
gi 697835384   15 ELKEAFSKIDIDNSGYVSDYELQDLFK 41
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALR 27
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
97-208 2.54e-03

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: 38.43  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKalqddpdckhlLPMNPSDASLFKCLADGILLCKMI-NFSQPdtIDERAINK----------KKLtpfti 165
Cdd:cd21330   14 EERTFRNWMNS-----------LGVNPRVNHLYSDLSDALVIFQLYeKIKVP--VDWNRVNKppypklgenmKKL----- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 697835384 166 sENLNLALN-SASAIGCTVVNIGSQDLQEGKPHLVLGLLWQIIK 208
Cdd:cd21330   76 -ENCNYAVElGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMR 118
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
366-474 2.55e-03

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: 37.94  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMN----SLGVSPYVNHLYSDLSDALIIFQLYDmtrVPVDWNHVNKppYPLLGGNMKKIENCNYAVEL 441
Cdd:cd21191    1 ERENVQKRTFTRWINlhleKCNPPLEVKDLFVDIQDGKILMALLE---VLSGQNLLQE--YKPSSHRIFRLNNIAKALKF 75
                         90       100       110
                 ....*....|....*....|....*....|...
gi 697835384 442 GKTKaKFSLVGIAGHDLNEGNPTLTLALVWQLM 474
Cdd:cd21191   76 LEDS-NVKLVSIDAAEIADGNPSLVLGLIWNII 107
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
94-207 2.92e-03

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


Pssm-ID: 409095  Cd Length: 117  Bit Score: 37.73  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  94 SEEEKV---AFVNWINKalqddpdckHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIDEraINKKKLTPFTIsENLN 170
Cdd:cd21246   11 DEREAVqkkTFTKWVNS---------HLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPK--PTKGKMRIHCL-ENVD 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 697835384 171 LALNSASAIGCTVVNIGSQDLQEGKPHLVLGLLWQII 207
Cdd:cd21246   79 KALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTII 115
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
485-594 3.09e-03

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: 38.02  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 485 LGEGEKVND-------DVIIKWVNQTLAKANKEtSITSFKdKSISTSLPVLDLIDAIAPRAVRpEMVKREDLSY-----Q 552
Cdd:cd21328    2 LRDGETLEDlmklspeELLLRWANFHLENAGWQ-KINNFS-SDIKDSRAYFHLLNQIAPKGQK-EGEPRIDINMsgfneK 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 697835384 553 DKMNNAKYAISVARKIGARIYALPDDLVEVKPKMVMTVFACL 594
Cdd:cd21328   79 DDLKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANL 120
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
371-479 4.93e-03

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: 37.43  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 371 EERTFRNWMNS--LGVSPYVNHLYSDLSDALIIFQLYDM---TRVPvdwnHVNKPPypllggNMK--KIENCNYAVELGK 443
Cdd:cd21311   16 QQNTFTRWANEhlKTANKHIADLETDLSDGLRLIALVEVlsgKKFP----KFNKRP------TFRsqKLENVSVALKFLE 85
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 697835384 444 TKAKFSLVGIAGHDLNEGNPTLTLALVWQLMRRYTL 479
Cdd:cd21311   86 EDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
97-207 5.48e-03

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: 37.43  E-value: 5.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384  97 EKVAFVNWINKalqddpdckHLLPMNPSDASLFKCLADGILLCKMINFSQPDTIdeRAINKKKLTPFTISENLNLALNS- 175
Cdd:cd21311   16 QQNTFTRWANE---------HLKTANKHIADLETDLSDGLRLIALVEVLSGKKF--PKFNKRPTFRSQKLENVSVALKFl 84
                         90       100       110
                 ....*....|....*....|....*....|..
gi 697835384 176 ASAIGCTVVNIGSQDLQEGKPHLVLGLLWQII 207
Cdd:cd21311   85 EEDEGIKIVNIDSSDIVDGKLKLILGLIWTLI 116
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
114-191 5.59e-03

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


Pssm-ID: 409050  Cd Length: 117  Bit Score: 37.23  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 114 DCKHLLPMNPS---DASLF---KCLADGILLCKMINFSQPDTIDERAIN-KKKLTPFTISENLNLALNSAsaigCTVVNI 186
Cdd:cd21201   12 RCGVLPPDHRAtqpNATVFdlaQALRDGVLLCQLLNRLSPGSVDDREINlRPQMSQFLCLKNIRTFLQAC----RTVFGL 87

                 ....*
gi 697835384 187 GSQDL 191
Cdd:cd21201   88 RSADL 92
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
369-475 6.43e-03

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: 37.73  E-value: 6.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 369 SKEER-TFRNWMNS-----------LGVSPYVNHLYSDLSDALIIFQLYDMTrVP--VDWNHVNKP---PYPLLggnmkk 431
Cdd:cd21325   22 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLS-VPdtIDERAINKKkltPFIIQ------ 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 697835384 432 iENCNYAVElGKTKAKFSLVGIAGHDLNEGNPTLTLALVWQLMR 475
Cdd:cd21325   95 -ENLNLALN-SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 136
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
371-481 7.91e-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: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 371 EERTFRNWMNS--LGVSPYVNHLYSDLSDALIIFQLYDMtrvpVDWNHVNKPPYPLLGGNMKKIENCNYAVELgKTKAKF 448
Cdd:cd21310   17 QQNTFTRWCNEhlKCVQKRLNDLQKDLSDGLRLIALLEV----LSQKKMYRKYHPRPNFRQMKLENVSVALEF-LDREHI 91
                         90       100       110
                 ....*....|....*....|....*....|...
gi 697835384 449 SLVGIAGHDLNEGNPTLTLALVWQLMRRYTLNV 481
Cdd:cd21310   92 KLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 124
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
103-180 8.29e-03

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


Pssm-ID: 409059 [Multi-domain]  Cd Length: 101  Bit Score: 36.19  E-value: 8.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697835384 103 NWINKALQDdpdckhllPMNPSDasLFKCLADGILLCKMINFSQPDTIdeRAINKKKLtPFTISENLNLALNSASAIG 180
Cdd:cd21210    7 EWIEEVLGE--------KLAQGD--LLDALKDGVVLCKLANRILPADI--RKYKESKM-PFVQMENISAFLNAARKLG 71
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
369-475 8.31e-03

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: 37.30  E-value: 8.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 369 SKEER-TFRNWMNS-----------LGVSPYVNHLYSDLSDALIIFQLYDMTrVP--VDWNHVNKP---PYPLLggnmkk 431
Cdd:cd21324   22 SEEEKyAFVNWINKalendpdckhvIPMNPNTDDLFKAVGDGIVLCKMINFS-VPdtIDERTINKKkltPFTIQ------ 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 697835384 432 iENCNYAVElGKTKAKFSLVGIAGHDLNEGNPTLTLALVWQLMR 475
Cdd:cd21324   95 -ENLNLALN-SASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 136
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
366-474 8.67e-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: 36.44  E-value: 8.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697835384 366 EGESKEERTFRNWMNSLGVS---PYVNHLYSDLSDALiifQLYDMTRVPVDWNHVNKPPYPllggNMKKIENCNYAVELG 442
Cdd:cd21231    2 EREDVQKKTFTKWINAQFAKfgkPPIEDLFTDLQDGR---RLLELLEGLTGQKLVKEKGST----RVHALNNVNKALQVL 74
                         90       100       110
                 ....*....|....*....|....*....|..
gi 697835384 443 KtKAKFSLVGIAGHDLNEGNPTLTLALVWQLM 474
Cdd:cd21231   75 Q-KNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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