NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|537544626|ref|NP_001269267|]
View 

plastin-3 isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
56-200 1.45e-106

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: 316.53  E-value: 1.45e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  56 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 135
Cdd:cd21292    1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537544626 136 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIEL 200
Cdd:cd21292   81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
332-465 2.46e-102

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: 305.39  E-value: 2.46e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 332 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGAN 411
Cdd:cd21331    1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 537544626 412 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVL 465
Cdd:cd21331   81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
209-330 7.28e-89

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: 270.30  E-value: 7.28e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 209 LLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEGEPRIDINMSGFNETDD 288
Cdd:cd21328    1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEPRIDINMSGFNEKDD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 537544626 289 LKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 330
Cdd:cd21328   81 LKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
474-585 5.66e-78

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: 241.72  E-value: 5.66e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 474 ANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMARRIGA 553
Cdd:cd21334    1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 537544626 554 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 585
Cdd:cd21334   81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
EFh super family cl08302
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
6-37 3.42e-05

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.


The actual alignment was detected with superfamily member cd00051:

Pssm-ID: 415501 [Multi-domain]  Cd Length: 63  Bit Score: 41.76  E-value: 3.42e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 537544626   6 YKVREIIQKLMLDGDRNKDGKISFDEFVYIFQ 37
Cdd:cd00051   32 GLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
56-200 1.45e-106

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: 316.53  E-value: 1.45e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  56 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 135
Cdd:cd21292    1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537544626 136 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIEL 200
Cdd:cd21292   81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
332-465 2.46e-102

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: 305.39  E-value: 2.46e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 332 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGAN 411
Cdd:cd21331    1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 537544626 412 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVL 465
Cdd:cd21331   81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
209-330 7.28e-89

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: 270.30  E-value: 7.28e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 209 LLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEGEPRIDINMSGFNETDD 288
Cdd:cd21328    1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEPRIDINMSGFNEKDD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 537544626 289 LKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 330
Cdd:cd21328   81 LKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
22-578 8.02e-88

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 284.14  E-value: 8.02e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  22 NKDGKISFDEFVyifqEVKSSDIAKTFRKAINRKEGicaLGGTSELSSEGTQHSYSEEEKyaFVNWINKALENDPDCRHV 101
Cdd:COG5069   71 NVSGRLEFIKGK----GVKLFNIGPQDIVDGNPKLI---LGLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGY 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 102 IPmNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINK----KKLTPFIIQENLNLALNSASAIG-CHVVNIGAEDLRA 176
Cdd:COG5069  142 KP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLqkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERS 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 177 gkpHLVLgLLWQIIKIGLFADIELSRNEaLAALLRDGETLEElMKLSPEELLLRWAN-FHLENSGWqKINNFSADIKDSK 255
Cdd:COG5069  221 ---IMTY-VSWYIIRFGLLEKIDIALHR-VYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANW-KVVNFSKDVSDGE 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 256 AYFHLLNQIAPKGQKEGEPRIDInmsgfnetddLKRAESMLQQADKLGCRQFVTPAdvvsGNPKLNLAFVANLFNKYPAL 335
Cdd:COG5069  294 NYTDLLNQLNALCSRAPLETTDL----------HSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQ 359
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 336 TKPENQ---DIDWTLLEGEtREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVP--VDWSKVNKPPYPKLGA 410
Cdd:COG5069  360 EPLEEEekpEIEEFDAEGE-FEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEE 438
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 411 N-MKKLENCNYAVELGKHpAKFSLVGIGGQDLNDGNQtLTLALVWQLMRRYTLNVLEDLG-DGQKANDDIIVNWVNRTLS 488
Cdd:COG5069  439 NrFKAFENENYAVDLGIT-EGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKkDGCGLSDSDLCAWLGSLGL 516
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 489 EAGKSTSIQSFKDKTISSSLA-VVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVS--MARRIGARVYALPEDLVEV 565
Cdd:COG5069  517 KGDKEEGIRSFGDPAGSVSGVfYLDVLKGIHSELVDYDLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGV 596
                        570
                 ....*....|....
gi 537544626 566 KPKM-VMTVFACLM 578
Cdd:COG5069  597 RPRLdVLTFIESLM 610
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
474-585 5.66e-78

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: 241.72  E-value: 5.66e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 474 ANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMARRIGA 553
Cdd:cd21334    1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 537544626 554 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 585
Cdd:cd21334   81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
78-193 1.26e-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: 95.82  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626   78 EEEKYAFVNWINKALENDPDCRHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKkltPFIIQENLNLALN 157
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRV-------TNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 537544626  158 SAS-AIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIG 193
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
82-192 4.09e-22

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: 91.22  E-value: 4.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626    82 YAFVNWINKALENDPdcrhvipmNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKlTPFIIQENLNLALNSASA 161
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEK 71
                           90       100       110
                   ....*....|....*....|....*....|.
gi 537544626   162 IGCHVVNIGAEDLRAGkPHLVLGLLWQIIKI 192
Cdd:smart00033  72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
222-334 1.99e-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: 89.27  E-value: 1.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  222 LSPEELLLRWANFHLENSGW-QKINNFSADIKDSKAYFHLLNQIAPKGQKEGEPRidinmsgFNETDDLKRAESMLQQA- 299
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLN-------KSEFDKLENINLALDVAe 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 537544626  300 DKLGCRQF-VTPADVVSGNPKLNLAFVANLFNKYPA 334
Cdd:pfam00307  74 KKLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
476-583 1.46e-20

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 86.96  E-value: 1.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  476 DDIIVNWVNRTLSEAGKSTSIQSFKdKTISSSLAVVDLIDAIQPGCINYDLVksgNLTEDDKHNNAKYAVSMARR-IGAR 554
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKL---NKSEFDKLENINLALDVAEKkLGVP 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 537544626  555 VYAL-PEDLVEVKPKMVMTVFACLMGRGMK 583
Cdd:pfam00307  80 KVLIePEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
354-460 5.97e-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: 79.64  E-value: 5.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  354 EERTFRNWMNSL----GVNPHVNHLYADLQDALVILQLYERIKvP--VDWSKVNKPPypklganMKKLENCNYAVELGKH 427
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 537544626  428 PAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRY 460
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
226-331 4.57e-17

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: 76.59  E-value: 4.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626   226 ELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEgepriDINMSGFNETDDLKRAESMLQQADKLGC- 304
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDK-----KKVAASLSRFKKIENINLALSFAEKLGGk 75
                           90       100
                   ....*....|....*....|....*..
gi 537544626   305 RQFVTPADVVSGnPKLNLAFVANLFNK 331
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
356-459 1.27e-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: 1.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626   356 RTFRNWMNSLGVN---PHVNHLYADLQDALVILQLYERIKVP-VDWSKVNKPPYPklganMKKLENCNYAVELGKHpAKF 431
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAEK-LGG 74
                           90       100
                   ....*....|....*....|....*...
gi 537544626   432 SLVGIGGQDLNDGNqTLTLALVWQLMRR 459
Cdd:smart00033  75 KVVLFEPEDLVEGP-KLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
477-578 1.11e-14

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: 70.04  E-value: 1.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626   477 DIIVNWVNRTLSEAGKSTSiqSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEdDKHNNAKYAVSMARRIG-ARV 555
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPV--TNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRF-KKIENINLALSFAEKLGgKVV 77
                           90       100
                   ....*....|....*....|...
gi 537544626   556 YALPEDLVEvKPKMVMTVFACLM 578
Cdd:smart00033  78 LFEPEDLVE-GPKLILGVIWTLI 99
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
6-37 3.42e-05

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: 41.76  E-value: 3.42e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 537544626   6 YKVREIIQKLMLDGDRNKDGKISFDEFVYIFQ 37
Cdd:cd00051   32 GLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
12-39 4.44e-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: 4.44e-04
                           10        20
                   ....*....|....*....|....*...
gi 537544626    12 IQKLMLDGDRNKDGKISFDEFVYIFQEV 39
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_7 pfam13499
EF-hand domain pair;
9-37 1.52e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.23  E-value: 1.52e-03
                          10        20
                  ....*....|....*....|....*....
gi 537544626    9 REIIQKLMLDGDRNKDGKISFDEFVYIFQ 37
Cdd:pfam13499  39 DEEVEELFKEFDLDKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
56-200 1.45e-106

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: 316.53  E-value: 1.45e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  56 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 135
Cdd:cd21292    1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537544626 136 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIEL 200
Cdd:cd21292   81 RAINKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
332-465 2.46e-102

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: 305.39  E-value: 2.46e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 332 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGAN 411
Cdd:cd21331    1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 537544626 412 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVL 465
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 ...
56-203 3.93e-101

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: 302.75  E-value: 3.93e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  56 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 135
Cdd:cd21325    1 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537544626 136 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRN 203
Cdd:cd21325   81 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRN 148
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
56-200 3.89e-97

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: 292.33  E-value: 3.89e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  56 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 135
Cdd:cd21323    1 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537544626 136 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIEL 200
Cdd:cd21323   81 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
56-200 5.83e-93

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: 281.51  E-value: 5.83e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  56 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 135
Cdd:cd21324    1 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537544626 136 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIEL 200
Cdd:cd21324   81 RTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
209-330 7.28e-89

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: 270.30  E-value: 7.28e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 209 LLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEGEPRIDINMSGFNETDD 288
Cdd:cd21328    1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIKDSRAYFHLLNQIAPKGQKEGEPRIDINMSGFNEKDD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 537544626 289 LKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 330
Cdd:cd21328   81 LKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
22-578 8.02e-88

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 284.14  E-value: 8.02e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  22 NKDGKISFDEFVyifqEVKSSDIAKTFRKAINRKEGicaLGGTSELSSEGTQHSYSEEEKyaFVNWINKALENDPDCRHV 101
Cdd:COG5069   71 NVSGRLEFIKGK----GVKLFNIGPQDIVDGNPKLI---LGLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGY 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 102 IPmNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINK----KKLTPFIIQENLNLALNSASAIG-CHVVNIGAEDLRA 176
Cdd:COG5069  142 KP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLqkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERS 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 177 gkpHLVLgLLWQIIKIGLFADIELSRNEaLAALLRDGETLEElMKLSPEELLLRWAN-FHLENSGWqKINNFSADIKDSK 255
Cdd:COG5069  221 ---IMTY-VSWYIIRFGLLEKIDIALHR-VYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANW-KVVNFSKDVSDGE 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 256 AYFHLLNQIAPKGQKEGEPRIDInmsgfnetddLKRAESMLQQADKLGCRQFVTPAdvvsGNPKLNLAFVANLFNKYPAL 335
Cdd:COG5069  294 NYTDLLNQLNALCSRAPLETTDL----------HSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQ 359
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 336 TKPENQ---DIDWTLLEGEtREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVP--VDWSKVNKPPYPKLGA 410
Cdd:COG5069  360 EPLEEEekpEIEEFDAEGE-FEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEE 438
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 411 N-MKKLENCNYAVELGKHpAKFSLVGIGGQDLNDGNQtLTLALVWQLMRRYTLNVLEDLG-DGQKANDDIIVNWVNRTLS 488
Cdd:COG5069  439 NrFKAFENENYAVDLGIT-EGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKkDGCGLSDSDLCAWLGSLGL 516
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 489 EAGKSTSIQSFKDKTISSSLA-VVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVS--MARRIGARVYALPEDLVEV 565
Cdd:COG5069  517 KGDKEEGIRSFGDPAGSVSGVfYLDVLKGIHSELVDYDLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGV 596
                        570
                 ....*....|....
gi 537544626 566 KPKM-VMTVFACLM 578
Cdd:COG5069  597 RPRLdVLTFIESLM 610
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
341-465 4.98e-81

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: 250.29  E-value: 4.98e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 341 QDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNY 420
Cdd:cd21330    1 QDIDWSSIEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGENMKKLENCNY 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 537544626 421 AVELGKHPAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVL 465
Cdd:cd21330   81 AVELGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 125
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
474-585 5.66e-78

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: 241.72  E-value: 5.66e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 474 ANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMARRIGA 553
Cdd:cd21334    1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 537544626 554 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 585
Cdd:cd21334   81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
209-333 1.28e-77

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: 241.40  E-value: 1.28e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 209 LLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEGEPRIDINMSGFNETDD 288
Cdd:cd21327    1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNKINNFSSDIKDSKAYYHLLNQVAPKGDEEGIPAIVIDMSGLREKDD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 537544626 289 LKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFNKYP 333
Cdd:cd21327   81 LKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
348-465 8.48e-77

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: 238.73  E-value: 8.48e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 348 LEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNYAVELGKH 427
Cdd:cd21329    1 LEGESSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRVPVDWGHVNKPPYPALGGNMKKIENCNYAVELGKN 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 537544626 428 PAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVL 465
Cdd:cd21329   81 KAKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
348-465 1.92e-76

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: 237.90  E-value: 1.92e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 348 LEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNYAVELGKH 427
Cdd:cd21298    1 VIEETREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGANMKKIENCNYAVELGKK 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 537544626 428 PaKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVL 465
Cdd:cd21298   81 L-KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLSIL 117
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
212-333 1.66e-72

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: 227.84  E-value: 1.66e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 212 DGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEGePRIDINMSGFNETDDLKR 291
Cdd:cd21326    1 EGEELEELMKLSPEELLLRWVNYHLTNAGWQNISNFSQDIKDSRAYFHLLNQIAPKGDVFD-ENIEIDFSGFNEKNDLKR 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 537544626 292 AESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFNKYP 333
Cdd:cd21326   80 AEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 121
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
469-583 5.74e-71

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: 223.71  E-value: 5.74e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 469 GDGQKANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMA 548
Cdd:cd21333    1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNNAKYAISMA 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 537544626 549 RRIGARVYALPEDLVEVKPKMVMTVFACLMGRGMK 583
Cdd:cd21333   81 RKIGARVYALPEDLVEVKPKMVMTVFACLMGRGMK 115
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
212-330 2.77e-69

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: 219.07  E-value: 2.77e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 212 DGETLEELMKLSPEELLLRWANFHLENSGWQK-INNFSADIKDSKAYFHLLNQIAPKGQKEGepridinMSGFNETDDLK 290
Cdd:cd21295    1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRrIKNFSGDIKDSEAYTHLLKQIAPKDAGVD-------TSALRESDLLQ 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 537544626 291 RAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 330
Cdd:cd21295   74 RAELMLQNADKIGCRKFVTPKDVVTGNPKLNLAFVANLFN 113
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
475-581 6.24e-62

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: 199.81  E-value: 6.24e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 475 NDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNlTEDDKHNNAKYAVSMARRIGAR 554
Cdd:cd21301    2 SDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLVLEGN-SEEDKLSNAKYAISMARKIGAR 80
                         90       100
                 ....*....|....*....|....*..
gi 537544626 555 VYALPEDLVEVKPKMVMTVFACLMGRG 581
Cdd:cd21301   81 VYALPEDIVEVKPKMVMTVFACLMALD 107
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
467-581 7.91e-59

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: 191.70  E-value: 7.91e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 467 DLGDGQKANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVS 546
Cdd:cd21332    1 DLGEGEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDLSDADKLNNAKYAIS 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 537544626 547 MARRIGARVYALPEDLVEVKPKMVMTVFACLMGRG 581
Cdd:cd21332   81 VARKIGARVYALPEDLVEVKPKMVMTVFACLMGKG 115
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
79-191 3.17e-55

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: 182.39  E-value: 3.17e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  79 EEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKK-LTPFIIQENLNLALN 157
Cdd:cd21217    1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKpKNIFEATENLNLALN 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 537544626 158 SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 191
Cdd:cd21217   81 AAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
350-465 1.29e-52

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: 175.16  E-value: 1.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 350 GETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKV-PVDWSKVNKppyPKLGANMKKLENCNYAVELGKHp 428
Cdd:cd21219    1 EGSREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPgCVNWKKVNK---PKPLNKFKKVENCNYAVDLAKK- 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 537544626 429 AKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVL 465
Cdd:cd21219   77 LGFSLVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
474-578 2.92e-46

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: 158.20  E-value: 2.92e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 474 ANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGnLTEDDKHNNAKYAVSMARRIGA 553
Cdd:cd21220    1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLVTEG-ETDEEKEQNAKYAISLARKIGA 79
                         90       100
                 ....*....|....*....|....*
gi 537544626 554 RVYALPEDLVEVKPKMVMTVFACLM 578
Cdd:cd21220   80 VIFLLWEDIVEVKPKMILTFVASLM 104
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
80-192 1.57e-45

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: 156.53  E-value: 1.57e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAIN-KKKLTPFIIQENLNLALNS 158
Cdd:cd21293    2 EKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINtKKVLNPWERNENHTLCLNS 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 537544626 159 ASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKI 192
Cdd:cd21293   82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKI 115
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
214-330 3.90e-45

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: 155.15  E-value: 3.90e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 214 ETLEELMKLSPEELLLRWANFHLENSGWQK--INNFSADIKDSKAYFHLLNQIAPKGQKEgepriDINMSGFNETDDLKR 291
Cdd:cd21218    1 ETLESLLYLPPEEILLRWVNYHLKKAGPTKkrVTNFSSDLKDGEVYALLLHSLAPELCDK-----ELVLEVLSEEDLEKR 75
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 537544626 292 AESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 330
Cdd:cd21218   76 AEKVLQAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
348-465 6.51e-45

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: 154.89  E-value: 6.51e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 348 LEGEtREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIkVP--VDWSKVNKPPYPKLGANMKKLENCNYAVELG 425
Cdd:cd21300    3 AEGE-REARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKV-IPgsVNWKKVNKAPASAEISRFKAVENTNYAVELG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 537544626 426 KHpAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVL 465
Cdd:cd21300   81 KQ-LGFSLVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
74-193 1.20e-42

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: 149.14  E-value: 1.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  74 HSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINK-----KKLTPFII 148
Cdd:cd21294    1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKpprknKPLNNFQM 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 537544626 149 QENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIG 193
Cdd:cd21294   81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRRG 125
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
214-330 2.72e-38

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: 136.54  E-value: 2.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 214 ETLEELMKLSPEELLLRWANFHLENSGW-QKINNFSADIKDSKAYFHLLNQIAPkGQKEGEPridinmsgFNETDDLKRA 292
Cdd:cd21297    1 ETLEQFLRLPPEQILLRWFNYHLKAANWpRRVSNFSKDVSDGENYTVLLNQLAP-ELCSRAP--------LQTTDLLQRA 71
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 537544626 293 ESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 330
Cdd:cd21297   72 EQVLQNAEKLDCRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
214-329 1.95e-34

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: 126.09  E-value: 1.95e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 214 ETLEELMKLSPEELLLRWANFHLENSGWQK-INNFSADIKDSKAYFHLLNQIAPKGQkegepridiNMSGFNETDDLKRA 292
Cdd:cd21296    1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKtVTNFSSDVKDAEAYAYLLNVLAPEHC---------DPATLEAKDPLERA 71
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 537544626 293 ESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLF 329
Cdd:cd21296   72 KLVLEQAEKMNCKRYLTAKDIVEGSANLNLAFVAQIF 108
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
350-465 3.50e-33

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: 122.61  E-value: 3.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 350 GETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKV-PVDWSKVNKPPyPKLgaNMKKLENCNYAVELGKHp 428
Cdd:cd21299    1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPgSVNWKHANKPP-IKM--PFKKVENCNQVVKIGKQ- 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 537544626 429 AKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVL 465
Cdd:cd21299   77 LKFSLVNVAGNDIVQGNKKLILALLWQLMRYHMLQLL 113
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
471-578 5.03e-31

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: 116.37  E-value: 5.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 471 GQKANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNlTEDDKHNNAKYAVSMARR 550
Cdd:cd21303    1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLVTPGN-TEDEAYLNAKLAISIARK 79
                         90       100
                 ....*....|....*....|....*...
gi 537544626 551 IGARVYALPEDLVEVKPKMVMTVFACLM 578
Cdd:cd21303   80 LGALIFLVPEDIVEVRPRLVLTFIGSLM 107
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
476-578 2.41e-27

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: 106.10  E-value: 2.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 476 DDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGnLTEDDKHNNAKYAVSMARRIGARV 555
Cdd:cd21302    4 DADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKG-ETDEEKRLNATYIISVARKLGCSI 82
                         90       100
                 ....*....|....*....|...
gi 537544626 556 YALPEDLVEVKPKMVMTVFACLM 578
Cdd:cd21302   83 FLLPEDIVEVNQKMILILTASIM 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
78-193 1.26e-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: 95.82  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626   78 EEEKYAFVNWINKALENDPDCRHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKkltPFIIQENLNLALN 157
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRV-------TNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 537544626  158 SAS-AIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIG 193
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
82-192 4.09e-22

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: 91.22  E-value: 4.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626    82 YAFVNWINKALENDPdcrhvipmNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKlTPFIIQENLNLALNSASA 161
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEK 71
                           90       100       110
                   ....*....|....*....|....*....|.
gi 537544626   162 IGCHVVNIGAEDLRAGkPHLVLGLLWQIIKI 192
Cdd:smart00033  72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
222-334 1.99e-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: 89.27  E-value: 1.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  222 LSPEELLLRWANFHLENSGW-QKINNFSADIKDSKAYFHLLNQIAPKGQKEGEPRidinmsgFNETDDLKRAESMLQQA- 299
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLN-------KSEFDKLENINLALDVAe 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 537544626  300 DKLGCRQF-VTPADVVSGNPKLNLAFVANLFNKYPA 334
Cdd:pfam00307  74 KKLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
476-583 1.46e-20

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 86.96  E-value: 1.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  476 DDIIVNWVNRTLSEAGKSTSIQSFKdKTISSSLAVVDLIDAIQPGCINYDLVksgNLTEDDKHNNAKYAVSMARR-IGAR 554
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKL---NKSEFDKLENINLALDVAEKkLGVP 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 537544626  555 VYAL-PEDLVEVKPKMVMTVFACLMGRGMK 583
Cdd:pfam00307  80 KVLIePEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
354-460 5.97e-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: 79.64  E-value: 5.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  354 EERTFRNWMNSL----GVNPHVNHLYADLQDALVILQLYERIKvP--VDWSKVNKPPypklganMKKLENCNYAVELGKH 427
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 537544626  428 PAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRY 460
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
226-331 4.57e-17

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: 76.59  E-value: 4.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626   226 ELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEgepriDINMSGFNETDDLKRAESMLQQADKLGC- 304
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDK-----KKVAASLSRFKKIENINLALSFAEKLGGk 75
                           90       100
                   ....*....|....*....|....*..
gi 537544626   305 RQFVTPADVVSGnPKLNLAFVANLFNK 331
Cdd:smart00033  76 VVLFEPEDLVEG-PKLILGVIWTLISL 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
81-191 4.62e-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: 76.99  E-value: 4.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  81 KYAFVNWINKALENDPdcrhvipmNPNTDDLFKAVGDGIVLCKMINLSVPDTIDEraINKKKLTPFIIQENLNLALNSAS 160
Cdd:cd00014    1 EEELLKWINEVLGEEL--------PVSITDLFESLRDGVLLCKLINKLSPGSIPK--INKKPKSPFKKRENINLFLNACK 70
                         90       100       110
                 ....*....|....*....|....*....|...
gi 537544626 161 AIG-CHVVNIGAEDLRAGK-PHLVLGLLWQIIK 191
Cdd:cd00014   71 KLGlPELDLFEPEDLYEKGnLKKVLGTLWALAL 103
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
356-459 1.27e-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: 1.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626   356 RTFRNWMNSLGVN---PHVNHLYADLQDALVILQLYERIKVP-VDWSKVNKPPYPklganMKKLENCNYAVELGKHpAKF 431
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAEK-LGG 74
                           90       100
                   ....*....|....*....|....*...
gi 537544626   432 SLVGIGGQDLNDGNqTLTLALVWQLMRR 459
Cdd:smart00033  75 KVVLFEPEDLVEGP-KLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
477-578 1.11e-14

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: 70.04  E-value: 1.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626   477 DIIVNWVNRTLSEAGKSTSiqSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEdDKHNNAKYAVSMARRIG-ARV 555
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPV--TNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRF-KKIENINLALSFAEKLGgKVV 77
                           90       100
                   ....*....|....*....|...
gi 537544626   556 YALPEDLVEvKPKMVMTVFACLM 578
Cdd:smart00033  78 LFEPEDLVE-GPKLILGVIWTLI 99
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
354-459 7.37e-13

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: 65.40  E-value: 7.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 354 EERTFRNWMNSL--GVNPHVNHLYADLQDALVILQLYERIKvpvdWSKVNKPPYPKLgaNMKKLENCNYAVELGKhpAKF 431
Cdd:cd21193   17 QKKTFTKWINSFleKANLEIGDLFTDLSDGKLLLKLLEIIS----GEKLGKPNRGRL--RVQKIENVNKALAFLK--TKV 88
                         90       100
                 ....*....|....*....|....*...
gi 537544626 432 SLVGIGGQDLNDGNQTLTLALVWQLMRR 459
Cdd:cd21193   89 RLENIGAEDIVDGNPRLILGLIWTIILR 116
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
77-191 2.05e-12

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: 63.84  E-value: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  77 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLTPFIIQENLNLA 155
Cdd:cd21219    3 SREER-AFRMWLNS-----------LGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNwKKVNKPKPLNKFKKVENCNYA 70
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 537544626 156 LNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 191
Cdd:cd21219   71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMR 106
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
354-460 1.32e-11

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: 61.26  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 354 EERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIkvpvdwSKVNKPPY---PKLgaNMKKLENCNYAVELGKHp 428
Cdd:cd21215    5 QKKTFTKWLNTklSSRGLSITDLVTDLSDGVRLIQLLEII------GDESLGRYnknPKM--RVQKLENVNKALEFIKS- 75
                         90       100       110
                 ....*....|....*....|....*....|..
gi 537544626 429 AKFSLVGIGGQDLNDGNQTLTLALVWQLMRRY 460
Cdd:cd21215   76 RGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
349-459 2.50e-11

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: 61.58  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 349 EGETREERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKVpvdwskvNKPPYPKLG-ANMKKLENCNYAVELG 425
Cdd:cd21318   34 EREAVQKKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLEVLSG-------EQLPKPTRGrMRIHSLENVDKALQFL 106
                         90       100       110
                 ....*....|....*....|....*....|....
gi 537544626 426 KHpAKFSLVGIGGQDLNDGNQTLTLALVWQLMRR 459
Cdd:cd21318  107 KE-QRVHLENVGSHDIVDGNHRLTLGLIWTIILR 139
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
349-459 3.40e-11

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: 60.46  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 349 EGETREERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKvpvdWSKVNKPPYPKLGANMkkLENCNYAVELGK 426
Cdd:cd21246   12 EREAVQKKTFTKWVNShlARVGCRINDLYTDLRDGRMLIKLLEVLS----GERLPKPTKGKMRIHC--LENVDKALQFLK 85
                         90       100       110
                 ....*....|....*....|....*....|...
gi 537544626 427 HpAKFSLVGIGGQDLNDGNQTLTLALVWQLMRR 459
Cdd:cd21246   86 E-QRVHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
78-190 4.82e-11

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: 59.99  E-value: 4.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  78 EEEKYAFVNWINKALEndpdcrhviPMNPNTDDLFKAVGDGIVLCKMInlsvpDTIDER---AINKKKLTPFIIQENLNL 154
Cdd:cd21227    3 EIQKNTFTNWVNEQLK---------PTGMSVEDLATDLEDGVKLIALV-----EILQGRklgRVIKKPLNQHQKLENVTL 68
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 537544626 155 ALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21227   69 ALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLI 104
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
80-190 8.83e-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: 56.54  E-value: 8.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALEndpDCRHVIpmnpntDDLFKAVGDGIVLCKMINLSVPDTIDEraINKKKLTPFIIqENLNLALNSA 159
Cdd:cd21193   17 QKKTFTKWINSFLE---KANLEI------GDLFTDLSDGKLLLKLLEIISGEKLGK--PNRGRLRVQKI-ENVNKALAFL 84
                         90       100       110
                 ....*....|....*....|....*....|.
gi 537544626 160 SAiGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21193   85 KT-KVRLENIGAEDIVDGNPRLILGLIWTII 114
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
80-190 2.41e-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: 55.22  E-value: 2.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALEndpdcRHVIPMNPNtdDLFKAVGDGIVLCKMIN-LSVPDTIDERAINkkkltPFIIQENLNLALNS 158
Cdd:cd21242    6 QKRTFTNWINSQLA-----KHSPPSVVS--DLFTDIQDGHRLLDLLEvLSGQQLPREKGHN-----VFQCRSNIETALSF 73
                         90       100       110
                 ....*....|....*....|....*....|..
gi 537544626 159 ASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21242   74 LKNKSIKLINIHVPDIIEGKPSIILGLIWTII 105
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
80-199 3.40e-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: 54.69  E-value: 3.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALendpdCRHVIPMNpnTDDLFKAVGDGIVLCKMIN-LSVPDTIDERAINKKKLTpFIiqENLNLALNS 158
Cdd:cd21241    6 QKKTFTNWINSYL-----AKRKPPMK--VEDLFEDIKDGTKLLALLEvLSGEKLPCEKGRRLKRVH-FL--SNINTALKF 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 537544626 159 ASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIkigLFADIE 199
Cdd:cd21241   76 LESKKIKLVNINPTDIVDGKPSIVLGLIWTII---LYFQIE 113
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
349-459 3.57e-09

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: 55.45  E-value: 3.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 349 EGETREERTFRNWMNS-LG-VNPHVNHLYADLQDALVILQLYERIKvpvdWSKVNKPPYPKLgaNMKKLENCNYAVELGK 426
Cdd:cd21317   27 EREAVQKKTFTKWVNShLArVTCRIGDLYTDLRDGRMLIRLLEVLS----GEQLPKPTKGRM--RIHCLENVDKALQFLK 100
                         90       100       110
                 ....*....|....*....|....*....|...
gi 537544626 427 HpAKFSLVGIGGQDLNDGNQTLTLALVWQLMRR 459
Cdd:cd21317  101 E-QKVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
77-191 9.40e-09

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: 53.39  E-value: 9.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  77 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINK---KKLTPFIIQENLN 153
Cdd:cd21298    5 TREEK-TYRNWMNS-----------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKpfkKLGANMKKIENCN 72
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 537544626 154 LALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 191
Cdd:cd21298   73 YAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMR 110
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
354-454 1.20e-08

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409035  Cd Length: 107  Bit Score: 53.15  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 354 EERTFRNWMNSLGVN---PHVNHLYADLQDALVILQLYERIkvpvdwSKVNKPPyPKLGANMKKLENCNYAVE-LGKHPA 429
Cdd:cd21186    3 QKKTFTKWINSQLSKankPPIKDLFEDLRDGTRLLALLEVL------TGKKLKP-EKGRMRVHHLNNVNRALQvLEQNNV 75
                         90       100
                 ....*....|....*....|....*
gi 537544626 430 KfsLVGIGGQDLNDGNQTLTLALVW 454
Cdd:cd21186   76 K--LVNISSNDIVDGNPKLTLGLVW 98
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
349-463 1.74e-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: 53.06  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 349 EGETREERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKVpvdwskvNKPPYPKLGANMKKLENCNYAVELGK 426
Cdd:cd21236   13 ERDKVQKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVLSG-------DTLPREKGRMRFHRLQNVQIALDYLK 85
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 537544626 427 HpAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLN 463
Cdd:cd21236   86 R-RQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 121
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
80-191 2.31e-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: 52.02  E-value: 2.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALEndpdcRHVIPMNpntdDLFKAVGDGIVLCKMINLsVPDTIDERAINKKKLTpfiIQ--ENLNLALN 157
Cdd:cd21215    5 QKKTFTKWLNTKLS-----SRGLSIT----DLVTDLSDGVRLIQLLEI-IGDESLGRYNKNPKMR---VQklENVNKALE 71
                         90       100       110
                 ....*....|....*....|....*....|....
gi 537544626 158 SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 191
Cdd:cd21215   72 FIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLIL 105
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
354-458 3.77e-08

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: 51.81  E-value: 3.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 354 EERTFRNWMNS-LGVNPHVNH----------LYADLQDALVILQLYERIKvP--VDWSKVNKPPyPKlgANMKKLENCNY 420
Cdd:cd21217    2 EKEAFVEHINSlLADDPDLKHllpidpdgddLFEALRDGVLLCKLINKIV-PgtIDERKLNKKK-PK--NIFEATENLNL 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 537544626 421 AVELGKHpAKFSLVGIGGQDLNDGNQTLTLALVWQLMR 458
Cdd:cd21217   78 ALNAAKK-IGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
349-469 4.76e-08

first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409084  Cd Length: 119  Bit Score: 51.56  E-value: 4.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 349 EGETREERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKVpvdwskvNKPPYPKLGANMKKLENCNYAVELGK 426
Cdd:cd21235    2 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSG-------DSLPREKGRMRFHKLQNVQIALDYLR 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 537544626 427 HpAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVLEDLG 469
Cdd:cd21235   75 H-RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSG 116
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
78-194 8.28e-08

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: 50.89  E-value: 8.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  78 EEEKYAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKK----LTPFIIQENLN 153
Cdd:cd21300    6 EREARVFTLWLNS-----------LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaeISRFKAVENTN 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 537544626 154 LALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGL 194
Cdd:cd21300   75 YAVELGKQLGFSLVGIQGADITDGSRTLTLALVWQLMRFHI 115
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
80-190 9.94e-08

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


Pssm-ID: 409037  Cd Length: 105  Bit Score: 50.48  E-value: 9.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKkkltpFIIQENLNLALNS 158
Cdd:cd21188    4 QKKTFTKWVNK---------HLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPrERGRMR-----FHRLQNVQTALDF 69
                         90       100       110
                 ....*....|....*....|....*....|..
gi 537544626 159 ASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21188   70 LKYRKIKLVNIRAEDIVDGNPKLTLGLIWTII 101
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
349-457 1.35e-07

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


Pssm-ID: 409080  Cd Length: 111  Bit Score: 50.31  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 349 EGETREERTFRNWMNSLGVN---PHVNHLYADLQDALVILQLYERIKVpvdwskvNKPPYPKLGANMKKLENCNYAVELG 425
Cdd:cd21231    2 EREDVQKKTFTKWINAQFAKfgkPPIEDLFTDLQDGRRLLELLEGLTG-------QKLVKEKGSTRVHALNNVNKALQVL 74
                         90       100       110
                 ....*....|....*....|....*....|..
gi 537544626 426 KHpAKFSLVGIGGQDLNDGNQTLTLALVWQLM 457
Cdd:cd21231   75 QK-NNVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
354-457 1.58e-07

first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.


Pssm-ID: 409081  Cd Length: 107  Bit Score: 50.01  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 354 EERTFRNWMN---SLGVNPHVNHLYADLQDALVILQLYERIkvpvdwskVNKP-PYPKLGANMKKLENCNYAVELgKHPA 429
Cdd:cd21232    3 QKKTFTKWINarfSKSGKPPIKDMFTDLRDGRKLLDLLEGL--------TGKSlPKERGSTRVHALNNVNRVLQV-LHQN 73
                         90       100
                 ....*....|....*....|....*...
gi 537544626 430 KFSLVGIGGQDLNDGNQTLTLALVWQLM 457
Cdd:cd21232   74 NVELVNIGGTDIVDGNHKLTLGLLWSII 101
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
352-460 1.58e-07

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: 50.14  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 352 TREERTFRNWMNSL----GVNPHVNHLYADLQDALVILQLYERIKvpvdWSKVNKPPYPKLGANMkkLENCNYAVELGKH 427
Cdd:cd21247   19 TMQKKTFTKWMNNVfsknGAKIEITDIYTELKDGIHLLRLLELIS----GEQLPRPSRGKMRVHF--LENNSKAITFLKT 92
                         90       100       110
                 ....*....|....*....|....*....|...
gi 537544626 428 PAKFSLvgIGGQDLNDGNQTLTLALVWQLMRRY 460
Cdd:cd21247   93 KVPVKL--IGPENIVDGDRTLILGLIWIIILRF 123
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
349-463 1.89e-07

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: 50.03  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 349 EGETREERTFRNWMNS--LGVNPHVNHLYADLQDA---LVILQLYERIKVPVDWSKVNkppypklganMKKLENCNYAVE 423
Cdd:cd21237    2 ERDRVQKKTFTKWVNKhlMKVRKHINDLYEDLRDGhnlISLLEVLSGVKLPREKGRMR----------FHRLQNVQIALD 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 537544626 424 LGKHpAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLN 463
Cdd:cd21237   72 FLKQ-RQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 110
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
80-199 2.01e-07

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409039  Cd Length: 113  Bit Score: 49.88  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALEndpdcRHVIPMNpnTDDLFKAVGDGIVLCKMINLSVPDTIDERaiNKKKLTPFIIQENLNLALNSA 159
Cdd:cd21190    6 QKKTFTNWINSHLA-----KLSQPIV--INDLFVDIKDGTALLRLLEVLSGQKLPIE--SGRVLQRAHKLSNIRNALDFL 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 537544626 160 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIkigLFADIE 199
Cdd:cd21190   77 TKRCIKLVNINSTDIVDGKPSIVLGLIWTII---LYFQIE 113
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
354-460 2.43e-07

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: 49.21  E-value: 2.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 354 EERTFRNWMNSL--GVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPklganMKKLENCNYAVELGKHPAkF 431
Cdd:cd21227    5 QKNTFTNWVNEQlkPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQ-----HQKLENVTLALKAMAEDG-I 78
                         90       100
                 ....*....|....*....|....*....
gi 537544626 432 SLVGIGGQDLNDGNQTLTLALVWQLMRRY 460
Cdd:cd21227   79 KLVNIGNEDIVNGNLKLILGLIWHLILRY 107
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
476-571 2.95e-07

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: 49.22  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 476 DDIIVNWVNRTLSEAG-KSTSIQSFkDKTISSSLAVVDLIDAIQPGCINYDLVKSGnLTEDDKHNNAKYAVSMARRIGAR 554
Cdd:cd21218   12 EEILLRWVNYHLKKAGpTKKRVTNF-SSDLKDGEVYALLLHSLAPELCDKELVLEV-LSEEDLEKRAEKVLQAAEKLGCK 89
                         90
                 ....*....|....*..
gi 537544626 555 VYALPEDLVEVKPKMVM 571
Cdd:cd21218   90 YFLTPEDIVSGNPRLNL 106
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
351-457 3.01e-07

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: 48.92  E-value: 3.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 351 ETREERTFRNWMNSL--GVNPHVNHLYADLQDALVILQLYERIkvpvdwSKVNKPPYPKLGANMKKLENCNYAVE-LGKH 427
Cdd:cd21214    3 EKQQRKTFTAWCNSHlrKAGTQIENIEEDFRDGLKLMLLLEVI------SGERLPKPERGKMRFHKIANVNKALDfIASK 76
                         90       100       110
                 ....*....|....*....|....*....|
gi 537544626 428 PAKfsLVGIGGQDLNDGNQTLTLALVWQLM 457
Cdd:cd21214   77 GVK--LVSIGAEEIVDGNLKMTLGMIWTII 104
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
223-318 5.67e-07

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


Pssm-ID: 409033  Cd Length: 103  Bit Score: 48.00  E-value: 5.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 223 SPEELLLRWANFHLENsgwQKINNFSADIKDSKAYFHLLNQIAPkGQkegeprIDINMSgFNETDDLKRAESMLQQA-DK 301
Cdd:cd21184    1 SGKSLLLEWVNSKIPE---YKVKNFTTDWNDGKALAALVDALKP-GL------IPDNES-LDKENPLENATKAMDIAeEE 69
                         90
                 ....*....|....*..
gi 537544626 302 LGCRQFVTPADVVSGNP 318
Cdd:cd21184   70 LGIPKIITPEDMVSPNV 86
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
354-454 5.84e-07

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


Pssm-ID: 409037  Cd Length: 105  Bit Score: 48.17  E-value: 5.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 354 EERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIkvpvdwSKVNkppYPKLGANMK--KLENCNYAVELGKHpA 429
Cdd:cd21188    4 QKKTFTKWVNKhlIKARRRVVDLFEDLRDGHNLISLLEVL------SGES---LPRERGRMRfhRLQNVQTALDFLKY-R 73
                         90       100
                 ....*....|....*....|....*
gi 537544626 430 KFSLVGIGGQDLNDGNQTLTLALVW 454
Cdd:cd21188   74 KIKLVNIRAEDIVDGNPKLTLGLIW 98
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
349-459 7.87e-07

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


Pssm-ID: 409165  Cd Length: 154  Bit Score: 48.89  E-value: 7.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 349 EGETREERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKvpvdWSKVNKPPYPKLgaNMKKLENCNYAVELGK 426
Cdd:cd21316   49 EREAVQKKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLEVLS----GERLPKPTKGRM--RIHCLENVDKALQFLK 122
                         90       100       110
                 ....*....|....*....|....*....|...
gi 537544626 427 HpAKFSLVGIGGQDLNDGNQTLTLALVWQLMRR 459
Cdd:cd21316  123 E-QRVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
351-460 8.30e-07

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: 47.91  E-value: 8.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 351 ETREERTFRNWMNSLGVN---PHVNHLYADLQDALVILQLYERIKvpvdwSKVNKPPYPKLGAN-MKKLENCNYAVELGK 426
Cdd:cd21225    2 EKVQIKAFTAWVNSVLEKrgiPKISDLATDLSDGVRLIFFLELVS-----GKKFPKKFDLEPKNrIQMIQNLHLAMLFIE 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 537544626 427 HPAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRY 460
Cdd:cd21225   77 EDLKIRVQGIGAEDFVDNNKKLILGLLWTLYRKY 110
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
333-464 8.98e-07

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: 48.10  E-value: 8.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 333 PALTKPENQDIDWTLLEgetreERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKvpvdWSKVNKPPYPKLGA 410
Cdd:cd21310    1 PATEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVQKRLNDLQKDLSDGLRLIALLEVLS----QKKMYRKYHPRPNF 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 537544626 411 NMKKLENCNYAVELGKHpAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNV 464
Cdd:cd21310   72 RQMKLENVSVALEFLDR-EHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 124
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
341-462 1.13e-06

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: 47.83  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 341 QDIDWTLLEgetreERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERI---KVPvdwsKVNKPPypklgaNMK-- 413
Cdd:cd21311    8 EDAQWKRIQ-----QNTFTRWANEhlKTANKHIADLETDLSDGLRLIALVEVLsgkKFP----KFNKRP------TFRsq 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 537544626 414 KLENCNYAVELGKHPAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTL 462
Cdd:cd21311   73 KLENVSVALKFLEEDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
80-190 1.25e-06

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 47.09  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALEndpdCRhvipmNPNTDDLFKAVGDGIVLCKMINLsVPDTIDERAINKKKLTPFIIQENLNLALNSA 159
Cdd:cd21183    5 QANTFTRWCNEHLK----ER-----GMQIHDLATDFSDGLCLIALLEN-LSTRPLKRSYNRRPAFQQHYLENVSTALKFI 74
                         90       100       110
                 ....*....|....*....|....*....|.
gi 537544626 160 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21183   75 EADHIKLVNIGSGDIVNGNIKLILGLIWTLI 105
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
333-464 1.26e-06

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


Pssm-ID: 409157  Cd Length: 129  Bit Score: 47.77  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 333 PALTKPENQDIDWTLLEgetreERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKlga 410
Cdd:cd21308    5 PATEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFR--- 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 537544626 411 nMKKLENCNYAVELGKHPAkFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNV 464
Cdd:cd21308   77 -QMQLENVSVALEFLDRES-IKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 128
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
80-190 2.31e-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: 46.90  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 159
Cdd:cd21236   18 QKKTFTKWINQ---------HLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHRLQNVQIALDYL 84
                         90       100       110
                 ....*....|....*....|....*....|.
gi 537544626 160 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21236   85 KRRQVKLVNIRNDDITDGNPKLTLGLIWTII 115
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
354-460 2.95e-06

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 46.32  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 354 EERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKvpvdwSKVNKPPYPKLGANMK-KLENCNYAVELGKHpAK 430
Cdd:cd21183    5 QANTFTRWCNEhlKERGMQIHDLATDFSDGLCLIALLENLS-----TRPLKRSYNRRPAFQQhYLENVSTALKFIEA-DH 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 537544626 431 FSLVGIGGQDLNDGNQTLTLALVWQLMRRY 460
Cdd:cd21183   79 IKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
349-460 3.88e-06

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


Pssm-ID: 409090  Cd Length: 113  Bit Score: 45.83  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 349 EGETREERTFRNWMNS--LGVNP--HVNHLYADLQDALVILQLYERIkvpvdwsKVNKPPYPKlGANMKK---LENCNYA 421
Cdd:cd21241    1 EQERVQKKTFTNWINSylAKRKPpmKVEDLFEDIKDGTKLLALLEVL-------SGEKLPCEK-GRRLKRvhfLSNINTA 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 537544626 422 VEL--GKhpaKFSLVGIGGQDLNDGNQTLTLALVWQLMRRY 460
Cdd:cd21241   73 LKFleSK---KIKLVNINPTDIVDGKPSIVLGLIWTIILYF 110
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
228-328 4.89e-06

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: 45.35  E-value: 4.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 228 LLRWANFHLENSG-WQKINNFS-ADIKDSKAYFHLLNQIAPKGqkegeprIDINM--SGFNETDDLKRAESMLQQADKLG 303
Cdd:cd21301    6 IVEWANEKLKSAGkSTSISSFKdPSISTSLPILDLIDAIKPGS-------VDYSLvlEGNSEEDKLSNAKYAISMARKIG 78
                         90       100
                 ....*....|....*....|....*
gi 537544626 304 CRQFVTPADVVSGNPKLNLAFVANL 328
Cdd:cd21301   79 ARVYALPEDIVEVKPKMVMTVFACL 103
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
80-201 5.03e-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: 5.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 159
Cdd:cd21235    7 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 537544626 160 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 201
Cdd:cd21235   74 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 115
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
333-464 5.26e-06

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


Pssm-ID: 409158  Cd Length: 131  Bit Score: 46.23  E-value: 5.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 333 PALTKPENQDIDWTLLEgetreERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKlga 410
Cdd:cd21309    2 PVTEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFR--- 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 537544626 411 nMKKLENCNYAVELGKHPAkFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNV 464
Cdd:cd21309   74 -QMQLENVSVALEFLDRES-IKLVSIDSKAIVDGNLKLILGLVWTLILHYSISM 125
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
225-329 6.00e-06

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: 45.34  E-value: 6.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 225 EELLLRWANFHLENSGWQ-KINNFSaD--IKDSKAYFHLLNQIAPkgqkeGEPRIDINMSGFNETDDLKRAESMLQQADK 301
Cdd:cd21220    3 DADILAWANSKVREAGKSsPISSFK-DpsLSTGLFLLDLLAAIDP-----GAVDYDLVTEGETDEEKEQNAKYAISLARK 76
                         90       100
                 ....*....|....*....|....*...
gi 537544626 302 LGCRQFVTPADVVSGNPKLNLAFVANLF 329
Cdd:cd21220   77 IGAVIFLLWEDIVEVKPKMILTFVASLM 104
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
354-460 6.26e-06

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: 45.17  E-value: 6.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 354 EERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKlganMKKLENCNYAVELGKHpAKF 431
Cdd:cd21228    5 QQNTFTRWCNEhlKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRPTFR----QMKLENVSVALEFLER-ESI 79
                         90       100
                 ....*....|....*....|....*....
gi 537544626 432 SLVGIGGQDLNDGNQTLTLALVWQLMRRY 460
Cdd:cd21228   80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
80-190 1.01e-05

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


Pssm-ID: 409095  Cd Length: 117  Bit Score: 45.05  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMIN-LSvpdtiDER--AINKKKLTPFIIqENLNLAL 156
Cdd:cd21246   17 QKKTFTKWVNS---------HLARVGCRINDLYTDLRDGRMLIKLLEvLS-----GERlpKPTKGKMRIHCL-ENVDKAL 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 537544626 157 NSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21246   82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTII 115
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
80-190 1.05e-05

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


Pssm-ID: 409167  Cd Length: 139  Bit Score: 45.40  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALENDPdCRhvipmnpnTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFiiqENLNLALNSA 159
Cdd:cd21318   39 QKKTFTKWVNSHLARVP-CR--------INDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRMRIHSL---ENVDKALQFL 106
                         90       100       110
                 ....*....|....*....|....*....|.
gi 537544626 160 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21318  107 KEQRVHLENVGSHDIVDGNHRLTLGLIWTII 137
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
80-189 1.57e-05

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 44.11  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALENDPDCRHVIpmnpntdDLFKAVGDGIVLCKMINLSVPDTIDerAINKKKLTPFIIQENLNLALNSA 159
Cdd:cd21212    1 EIEIYTDWANHYLEKGGHKRIIT-------DLQKDLGDGLTLVNLIEAVAGEKVP--GIHSRPKTRAQKLENIQACLQFL 71
                         90       100       110
                 ....*....|....*....|....*....|
gi 537544626 160 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQI 189
Cdd:cd21212   72 AALGVDVQGITAEDIVDGNLKAILGLFFSL 101
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
365-459 2.05e-05

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: 44.36  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 365 LGVNPHVNHLYADLQDALVILQLYERIkVP--VDWSKVNKPPYPKLGAN-MKKLENCNYAVELGKhPAKFSLVGIGGQDL 441
Cdd:cd21294   29 LPFPTDTFQLFDECKDGLVLSKLINDS-VPdtIDERVLNKPPRKNKPLNnFQMIENNNIVINSAK-AIGCSVVNIGAGDI 106
                         90
                 ....*....|....*...
gi 537544626 442 NDGNQTLTLALVWQLMRR 459
Cdd:cd21294  107 IEGREHLILGLIWQIIRR 124
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
77-191 3.09e-05

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: 43.64  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  77 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLT-PFIIQENLNLA 155
Cdd:cd21299    3 SREER-CFRLWINS-----------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKmPFKKVENCNQV 70
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 537544626 156 LNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 191
Cdd:cd21299   71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMR 106
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
349-457 3.17e-05

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: 43.34  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 349 EGETREERTFRNWMNSL--GVNP--HVNHLYADLQDALVILQLYErikVPVDWSKVNKppYPKLGANMKKLENCNYAVEL 424
Cdd:cd21191    1 ERENVQKRTFTRWINLHleKCNPplEVKDLFVDIQDGKILMALLE---VLSGQNLLQE--YKPSSHRIFRLNNIAKALKF 75
                         90       100       110
                 ....*....|....*....|....*....|...
gi 537544626 425 GKHpAKFSLVGIGGQDLNDGNQTLTLALVWQLM 457
Cdd:cd21191   76 LED-SNVKLVSIDAAEIADGNPSLVLGLIWNII 107
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
6-37 3.42e-05

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: 41.76  E-value: 3.42e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 537544626   6 YKVREIIQKLMLDGDRNKDGKISFDEFVYIFQ 37
Cdd:cd00051   32 GLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
223-319 4.42e-05

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


Pssm-ID: 409079  Cd Length: 103  Bit Score: 42.75  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 223 SPEELLLRWANFHLENSgwqKINNFSADIKDSKAYFHLLNQIAPKGQKEGEpridinmsGFNETDDLKRAESMLQQADK- 301
Cdd:cd21230    1 TPKQRLLGWIQNKIPQL---PITNFTTDWNDGRALGALVDSCAPGLCPDWE--------TWDPNDALENATEAMQLAEDw 69
                         90
                 ....*....|....*...
gi 537544626 302 LGCRQFVTPADVVsgNPK 319
Cdd:cd21230   70 LGVPQLITPEEII--NPN 85
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
225-330 4.51e-05

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 42.71  E-value: 4.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 225 EELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEgepridINMSGFNETDDLKRAESMLQQADKLGC 304
Cdd:cd00014    1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPK------INKKPKSPFKKRENINLFLNACKKLGL 74
                         90       100
                 ....*....|....*....|....*....
gi 537544626 305 --RQFVTPADVVS-GNPKLNLAFVANLFN 330
Cdd:cd00014   75 peLDLFEPEDLYEkGNLKKVLGTLWALAL 103
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
77-191 8.38e-05

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: 42.28  E-value: 8.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  77 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLS-VPdtIDERAINKKkltPFIIQ------ 149
Cdd:cd21329    5 SSEER-TFRNWMNS-----------LGVNPYVNHLYSDLCDALVIFQLYEMTrVP--VDWGHVNKP---PYPALggnmkk 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 537544626 150 -ENLNLALN-SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 191
Cdd:cd21329   68 iENCNYAVElGKNKAKFSLVGIAGSDLNEGNKTLTLALIWQLMR 111
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
80-191 9.40e-05

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: 42.68  E-value: 9.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMIN-LSVPdtIDERAINK----------KKLtpfii 148
Cdd:cd21331   23 EERTFRNWMNS-----------LGVNPHVNHLYGDLQDALVILQLYEkIKVP--VDWNKVNKppypklganmKKL----- 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 537544626 149 qENLNLALN-SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 191
Cdd:cd21331   85 -ENCNYAVElGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMR 127
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
466-577 1.28e-04

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: 41.79  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 466 EDLGDGQKAN-DDIIVNWVNRTLSEAGKSTsIQSFKdKTISSSLAVVDLIDAIQPGCINYDLVKSGNLT---EDDKHNNA 541
Cdd:cd21326    3 EELEELMKLSpEELLLRWVNYHLTNAGWQN-ISNFS-QDIKDSRAYFHLLNQIAPKGDVFDENIEIDFSgfnEKNDLKRA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 537544626 542 KYAVSMARRIGARVYALPEDLVEVKPKMVMTVFACL 577
Cdd:cd21326   81 EYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANL 116
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
212-333 1.40e-04

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: 41.71  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 212 DGETLEELMKLSPEELLLRWANFHLENsgwQKINNFSADIKDSKAYFHLLNQIAPKgqkegeprIDINMSGFNETDDLKR 291
Cdd:cd21312    1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPG--------LCPDWDSWDASKPVTN 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 537544626 292 AESMLQQADK-LGCRQFVTPADVVsgNPKLNLAFVANLFNKYP 333
Cdd:cd21312   70 AREAMQQADDwLGIPQVITPEEIV--DPNVDEHSVMTYLSQFP 110
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
79-190 1.54e-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: 41.22  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  79 EEKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERaiNKKKLTPFIIQeNLNLALNS 158
Cdd:cd21214    5 QQRKTFTAWCNS---------HLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKP--ERGKMRFHKIA-NVNKALDF 72
                         90       100       110
                 ....*....|....*....|....*....|..
gi 537544626 159 ASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21214   73 IASKGVKLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
80-190 2.12e-04

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


Pssm-ID: 409040  Cd Length: 114  Bit Score: 41.03  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALENdpdCrhvipmNP--NTDDLFKAVGDGIVLCKMIN-LSVPDTIDERAINKKKLTPFiiqENLNLAL 156
Cdd:cd21191    6 QKRTFTRWINLHLEK---C------NPplEVKDLFVDIQDGKILMALLEvLSGQNLLQEYKPSSHRIFRL---NNIAKAL 73
                         90       100       110
                 ....*....|....*....|....*....|....
gi 537544626 157 NSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21191   74 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNII 107
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
228-330 2.20e-04

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: 41.00  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 228 LLRWANFHLENSGWQ-KINNFSADIKDSKAYF-HLLNQIapkgqkegEPR-IDINMSGFNETDDLKR--AESMLQQADKL 302
Cdd:cd21302    7 ILSWANRKVRTMGRKsQIESFKDKSLSSGLFFlELLWAV--------EPRvVNWNLVTKGETDEEKRlnATYIISVARKL 78
                         90       100
                 ....*....|....*....|....*...
gi 537544626 303 GCRQFVTPADVVSGNPKLNLAFVANLFN 330
Cdd:cd21302   79 GCSIFLLPEDIVEVNQKMILILTASIMY 106
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
80-190 2.52e-04

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: 40.83  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALeNDPDCRHVipmnpntDDLFKAVGDGIVLckminLSVPDTIDERAINKKKLTPFIIQ-ENLNLALNS 158
Cdd:cd21186    3 QKKTFTKWINSQL-SKANKPPI-------KDLFEDLRDGTRL-----LALLEVLTGKKLKPEKGRMRVHHlNNVNRALQV 69
                         90       100       110
                 ....*....|....*....|....*....|..
gi 537544626 159 ASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21186   70 LEQNNVKLVNISSNDIVDGNPKLTLGLVWSII 101
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
80-201 2.54e-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: 40.79  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMinLSVPDTIdeRAINKKKLTPFIIQENLNLALNSA 159
Cdd:cd21237    7 QKKTFTKWVNK---------HLMKVRKHINDLYEDLRDGHNLISL--LEVLSGV--KLPREKGRMRFHRLQNVQIALDFL 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 537544626 160 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 201
Cdd:cd21237   74 KQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYIS 115
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
225-331 3.32e-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: 40.70  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 225 EELLLRWANFHLENSGWQ-KINNFS-ADIKDSKAYFHLLNQIAPKGQKEGEPRIDinmsGFNETDDLKRAESMLQQADKL 302
Cdd:cd21332   10 DEIIIKWVNQTLANANKTtSITSFKdKSISTSLPVLDLIDAIAPNAIREEMVKRE----DLSDADKLNNAKYAISVARKI 85
                         90       100
                 ....*....|....*....|....*....
gi 537544626 303 GCRQFVTPADVVSGNPKLNLAFVANLFNK 331
Cdd:cd21332   86 GARVYALPEDLVEVKPKMVMTVFACLMGK 114
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
349-457 3.99e-04

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: 40.25  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 349 EGETREERTFRNWMNS----LGVNPHVNHLYADLQDALVILQLYERI---KVPVDWSKVNKppypklgaNMKKLENCNYA 421
Cdd:cd21190    1 EQERVQKKTFTNWINShlakLSQPIVINDLFVDIKDGTALLRLLEVLsgqKLPIESGRVLQ--------RAHKLSNIRNA 72
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 537544626 422 VELGKHpAKFSLVGIGGQDLNDGNQTLTLALVWQLM 457
Cdd:cd21190   73 LDFLTK-RCIKLVNINSTDIVDGKPSIVLGLIWTII 107
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
12-39 4.44e-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: 4.44e-04
                           10        20
                   ....*....|....*....|....*...
gi 537544626    12 IQKLMLDGDRNKDGKISFDEFVYIFQEV 39
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
212-333 4.67e-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: 40.15  E-value: 4.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 212 DGETLEELMKLSPEELLLRWANFHLENsgwQKINNFSADIKDSKAYFHLLNQIAPKgqkegeprIDINMSGFNETDDLKR 291
Cdd:cd21315    5 EDDGPDDGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPG--------LCPDWEDWDPKDAVKN 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 537544626 292 AESMLQQADK-LGCRQFVTPADVVsgNPKLNLAFVANLFNKYP 333
Cdd:cd21315   74 AKEAMDLAEDwLDVPQLIKPEEMV--NPKVDELSMMTYLSQFP 114
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
334-458 4.69e-04

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: 40.76  E-value: 4.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 334 ALTKPENQDIDWTLLEGETREERTFRNWMNS-----------LGVNPHVNHLYADLQDALVILQLYErIKVP--VDWSKV 400
Cdd:cd21324    5 AIGGTSEQSSAGTQHSYSEEEKYAFVNWINKalendpdckhvIPMNPNTDDLFKAVGDGIVLCKMIN-FSVPdtIDERTI 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 537544626 401 NKPPYPKLGANMKKLENCNYAVELGKHpakfsLVGIGGQDLNDGNQTLTLALVWQLMR 458
Cdd:cd21324   84 NKKKLTPFTIQENLNLALNSASAIGCH-----VVNIGAEDLKEGKPYLVLGLLWQVIK 136
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
225-331 4.90e-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: 39.97  E-value: 4.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 225 EELLLRWANFHLENSG-WQKINNFS-ADIKDSKAYFHLLNQIAPkgqkeGEPRID-INMSGFNETDDLKRAESMLQQADK 301
Cdd:cd21333    8 DETIVNWVNETLTEAGkSSSISSFKdGKISTSMPVLDLIDAIQP-----GSINYDlLKTEDLNDEEKLNNAKYAISMARK 82
                         90       100       110
                 ....*....|....*....|....*....|
gi 537544626 302 LGCRQFVTPADVVSGNPKLNLAFVANLFNK 331
Cdd:cd21333   83 IGARVYALPEDLVEVKPKMVMTVFACLMGR 112
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
80-190 6.03e-04

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: 39.52  E-value: 6.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALENdpdCRhvipmNPNTDDLFKAVGDGIVLCKMINlsvpDTIDERAINKKKLTPFIIQENLNLALNSA 159
Cdd:cd21231    7 QKKTFTKWINAQFAK---FG-----KPPIEDLFTDLQDGRRLLELLE----GLTGQKLVKEKGSTRVHALNNVNKALQVL 74
                         90       100       110
                 ....*....|....*....|....*....|.
gi 537544626 160 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21231   75 QKNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
465-577 6.16e-04

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: 39.95  E-value: 6.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 465 LEDLGdgQKANDDIIVNWVNRTLSEAGKStSIQSFKDKtISSSLAVVDLIDAIQP-----GCINYDLVKSGnLTEDDKHN 539
Cdd:cd21328    8 LEDLM--KLSPEELLLRWANFHLENAGWQ-KINNFSSD-IKDSRAYFHLLNQIAPkgqkeGEPRIDINMSG-FNEKDDLK 82
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 537544626 540 NAKYAVSMARRIGARVYALPEDLVEVKPKMVMTVFACL 577
Cdd:cd21328   83 RAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANL 120
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
80-190 8.74e-04

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


Pssm-ID: 409166  Cd Length: 132  Bit Score: 39.65  E-value: 8.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKALENdPDCRhvipmnpnTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFiiqENLNLALNSA 159
Cdd:cd21317   32 QKKTFTKWVNSHLAR-VTCR--------IGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKGRMRIHCL---ENVDKALQFL 99
                         90       100       110
                 ....*....|....*....|....*....|.
gi 537544626 160 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21317  100 KEQKVHLENMGSHDIVDGNHRLTLGLIWTII 130
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
225-331 9.55e-04

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: 39.10  E-value: 9.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 225 EELLLRWANFHLENSGWQ-KINNF-SADIKDSKAYFHLLNQIAPkgqkeGEPRIDINMSG-FNETDDLKRAESMLQQADK 301
Cdd:cd21334    3 DDIIVNWVNRTLSEAGKStSIQNFkDKTISSSLAVVDLIDAIQP-----GCINYDLVKTGnLTDDDKLDNAKYAVSMARK 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 537544626 302 LGCRQFVTPADVVSGNPKLNLAFVANLFNK 331
Cdd:cd21334   78 IGARVYALPEDLVEVKPKMVMTVFACLMGR 107
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
354-459 1.38e-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: 39.57  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 354 EERTFRNWMNS-----------LGVNPHVNHLYADLQDALVILQLYErIKVP--VDWSKVNKPpypKLGAnMKKLENCNY 420
Cdd:cd21292   25 EKVAFVNWINKnlgddpdckhlLPMDPNTDDLFEKVKDGILLCKMIN-LSVPdtIDERAINKK---KLTV-FTIHENLTL 99
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 537544626 421 AVE----LGKHpakfsLVGIGGQDLNDGNQTLTLALVWQLMRR 459
Cdd:cd21292  100 ALNsasaIGCN-----VVNIGAEDLKEGKPHLVLGLLWQIIRI 137
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
107-163 1.48e-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: 38.12  E-value: 1.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 537544626 107 NTDDLFKAVGDGIVLCKMINLSVPDTIdeRAINKKKLtPFIIQENLNLALNSASAIG 163
Cdd:cd21210   18 AQGDLLDALKDGVVLCKLANRILPADI--RKYKESKM-PFVQMENISAFLNAARKLG 71
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
80-191 1.51e-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: 38.82  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMI-NLSVPdtIDERAINK----------KKLtpfii 148
Cdd:cd21330   14 EERTFRNWMNS-----------LGVNPRVNHLYSDLSDALVIFQLYeKIKVP--VDWNRVNKppypklgenmKKL----- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 537544626 149 qENLNLALN-SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 191
Cdd:cd21330   76 -ENCNYAVElGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMR 118
EF-hand_7 pfam13499
EF-hand domain pair;
9-37 1.52e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.23  E-value: 1.52e-03
                          10        20
                  ....*....|....*....|....*....
gi 537544626    9 REIIQKLMLDGDRNKDGKISFDEFVYIFQ 37
Cdd:pfam13499  39 DEEVEELFKEFDLDKDGRISFEEFLELYS 67
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
466-577 1.83e-03

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: 38.41  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 466 EDLGDGQK-ANDDIIVNWVNRTLSEAGKSTSIQSFKdKTISSSLAVVDLIDAIQPGCinyDLVKSGNLTEDDKHNNAKYA 544
Cdd:cd21295    3 ETLEDLLKlSPEEILLRWVNYHLERAGCDRRIKNFS-GDIKDSEAYTHLLKQIAPKD---AGVDTSALRESDLLQRAELM 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 537544626 545 VSMARRIGARVYALPEDLVEVKPKMVMTVFACL 577
Cdd:cd21295   79 LQNADKIGCRKFVTPKDVVTGNPKLNLAFVANL 111
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
477-577 1.87e-03

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: 38.09  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 477 DIIVNWVNRTLSEAGKSTS---IQSFKDKTIsssLAvvDLIDAIQPGCINYDLVKSgnLTEDDKHNNAKYAVSMARRIGA 553
Cdd:cd00014    2 EELLKWINEVLGEELPVSItdlFESLRDGVL---LC--KLINKLSPGSIPKINKKP--KSPFKKRENINLFLNACKKLGL 74
                         90       100
                 ....*....|....*....|....*..
gi 537544626 554 RVYAL--PEDLVEVK-PKMVMTVFACL 577
Cdd:cd00014   75 PELDLfePEDLYEKGnLKKVLGTLWAL 101
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
81-135 2.37e-03

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: 38.16  E-value: 2.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 537544626  81 KYAFVNWINKALENDpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 135
Cdd:cd21203    2 RYEAAEWIQNVLGVL------VLPDPSEEEFRLCLRDGVVLCKLLNKLQPGAVPK 50
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
107-163 2.57e-03

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


Pssm-ID: 409057 [Multi-domain]  Cd Length: 119  Bit Score: 38.09  E-value: 2.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 537544626 107 NTDDLFKAVGDGIVLCKMINLSVPDTIdeRAINKKKlTPFIIQENLNLALNSASAIG 163
Cdd:cd21208   18 PSDDFRESLEDGILLCELINAIKPGSI--KKINRLP-TPIAGLDNLNLFLKACEDLG 71
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
7-39 2.59e-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: 35.45  E-value: 2.59e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 537544626    7 KVREIIQKLmldgDRNKDGKISFDEFVYIFQEV 39
Cdd:pfam00036   1 ELKEIFRLF----DKDGDGKIDFEEFKELLKKL 29
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
454-517 2.87e-03

cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and amphibians. CYP2K6 from zebrafish has been shown to catalyze the conversion of aflatoxin B1 (AFB1) to its cytotoxic derivative AFB1 exo-8,9-epoxide, while its ortholog in rainbow trout CYP2K1 is also capable of oxidizing lauric acid. In birds, CYP2K is one of the largest CYP2 subfamilies. The CYP2K subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 40.17  E-value: 2.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537544626 454 WQLMRRYTLNVLEDLGDGQKANDDIIVNWVNRTLSEagkstsIQSFKDK----TISSSLAVVDLIDAI 517
Cdd:cd20664   60 WKEMRRFTLTTLRDFGMGKKTSEDKILEEIPYLIEV------FEKHKGKpfetTLSMNVAVSNIIASI 121
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
354-458 3.52e-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: 38.50  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626 354 EERTFRNWMNS-----------LGVNPHVNHLYADLQDALVILQLYErIKVP--VDWSKVNKPPYPKLGANMKKLENCNY 420
Cdd:cd21325   25 EKYAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMIN-LSVPdtIDERAINKKKLTPFIIQENLNLALNS 103
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 537544626 421 AVELGKHpakfsLVGIGGQDLNDGNQTLTLALVWQLMR 458
Cdd:cd21325  104 ASAIGCH-----VVNIGAEDLRAGKPHLVLGLLWQIIK 136
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
3-33 5.77e-03

S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins.


Pssm-ID: 238131 [Multi-domain]  Cd Length: 88  Bit Score: 36.31  E-value: 5.77e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 537544626   3 LPGYKVREIIQKLMLDGDRNKDGKISFDEFV 33
Cdd:cd00213   44 LKNQKDPEAVDKIMKDLDVNKDGKVDFQEFL 74
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
84-189 6.12e-03

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409135  Cd Length: 105  Bit Score: 36.55  E-value: 6.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  84 FVNWINKALENDpDCRHVIpmnpntDDLFKAVGDGIVLCKMINLSVPDTIDEraINKKKLTPFIIQENLNLALNSASAIG 163
Cdd:cd21286    5 YTDWANHYLAKS-GHKRLI------KDLQQDIADGVLLAEIIQIIANEKVED--INGCPRSQSQMIENVDVCLSFLAARG 75
                         90       100
                 ....*....|....*....|....*.
gi 537544626 164 CHVVNIGAEDLRAGKPHLVLGLLWQI 189
Cdd:cd21286   76 VNVQGLSAEEIRNGNLKAILGLFFSL 101
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
80-190 7.28e-03

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


Pssm-ID: 409165  Cd Length: 154  Bit Score: 37.33  E-value: 7.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544626  80 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFiiqENLNLALNSA 159
Cdd:cd21316   54 QKKTFTKWVNS---------HLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCL---ENVDKALQFL 121
                         90       100       110
                 ....*....|....*....|....*....|.
gi 537544626 160 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 190
Cdd:cd21316  122 KEQRVHLENMGSHDIVDGNHRLTLGLIWTII 152
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH