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Conserved domains on  [gi|1907202322|ref|XP_036017657|]
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plastin-3 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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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 ...
 101-245 8.49e-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: 316.14  E-value: 8.49e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 101 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 180
Cdd:cd21292     1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907202322 181 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIEL 245
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 ...
 386-519 2.88e-101

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: 304.23  E-value: 2.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 386 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGAN 465
Cdd:cd21331     1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907202322 466 MKKLENCNYAVELGKNPAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVL 519
Cdd:cd21331    81 MKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 254-384 6.98e-85

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


The actual alignment was detected with superfamily member cd21328:

Pssm-ID: 469584 [Multi-domain]  Cd Length: 122  Bit Score: 261.44  E-value: 6.98e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 254 LLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKlidfsnsvkDSKAYFHLLNQIAPKGQKEGEPRIDIN 333
Cdd:cd21328     1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIK---------DSRAYFHLLNQIAPKGQKEGEPRIDIN 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907202322 334 MSGFNETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 384
Cdd:cd21328    72 MSGFNEKDDLKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 528-639 3.77e-77

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: 240.95  E-value: 3.77e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 528 ANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMARRIGA 607
Cdd:cd21334     1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907202322 608 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 639
Cdd:cd21334    81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 16-82 2.08e-14

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: 67.96  E-value: 2.08e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907202322  16 ELKEAFAKVDLNSNGFICDYELHELFKEANMPLPgykvREIIQKLMVDGDRNKDGKISFNEFVYIFQ 82
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS----EEEIDEMIREVDKDGDGKIDFEEFLELMA 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 ...
 101-245 8.49e-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: 316.14  E-value: 8.49e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 101 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 180
Cdd:cd21292     1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907202322 181 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIEL 245
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 ...
 386-519 2.88e-101

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: 304.23  E-value: 2.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 386 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGAN 465
Cdd:cd21331     1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907202322 466 MKKLENCNYAVELGKNPAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVL 519
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 ...
 254-384 6.98e-85

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: 261.44  E-value: 6.98e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 254 LLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKlidfsnsvkDSKAYFHLLNQIAPKGQKEGEPRIDIN 333
Cdd:cd21328     1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIK---------DSRAYFHLLNQIAPKGQKEGEPRIDIN 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907202322 334 MSGFNETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 384
Cdd:cd21328    72 MSGFNEKDDLKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
106-632 1.69e-83

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 274.51  E-value: 1.69e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 106 LGGTSELSSEGTQHSYSEEEKyaFVNWINKALENDPDCRHVIPmNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINK 185
Cdd:COG5069   103 LGLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDL 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 186 ----KKLTPFIIQENLNLALNSASAIG-CHVVNIGAEDLRAgkpHLVLgLLWQIIKIGLFADIELSRNEaLAALLRDGET 260
Cdd:COG5069   180 qkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERS---IMTY-VSWYIIRFGLLEKIDIALHR-VYRLLEADET 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 261 LEElMKLSPEELLLRWAN-FHLENSGWQKINnfsadiklidFSNSVKDSKAYFHLLNQIAPKGQKEGEPRIDInmsgfne 339
Cdd:COG5069   255 LIQ-LRLPYEIILLRLLNlIHLKQANWKVVN----------FSKDVSDGENYTDLLNQLNALCSRAPLETTDL------- 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 340 tddLKRAESMLQQADKLGCRQFVTPAdvvsGNPKLNLAFVANLFNKYPALTKPENQ---DIDWTLLEGEtREERTFRNWM 416
Cdd:COG5069   317 ---HSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQEPLEEEekpEIEEFDAEGE-FEARVFTFWL 388

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 417 NSLGVNPHVNHLYADLQDALVILQLYERIKVP--VDWSKVNKPPYPKLGAN-MKKLENCNYAVELGKNpAKFSLVGIGGQ 493
Cdd:COG5069   389 NSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGIT-EGFSLVGIKGL 467

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 494 DLNDGNpTLTLAVVWQLMRRYTLNVLEDLGEGQKA-NDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLA-VVDLIDAI 571
Cdd:COG5069   468 EILDGI-RLKLTLVWQVLRSNTALFNHVLKKDGCGlSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDVLKGI 546

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907202322 572 QPGCINYDLVKSGNLTEDDKHNNAKYAVS--MARRIGARVYALPEDLVEVKPKM-VMTVFACLM 632
Cdd:COG5069   547 HSELVDYDLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 528-639 3.77e-77

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: 240.95  E-value: 3.77e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 528 ANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMARRIGA 607
Cdd:cd21334     1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907202322 608 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 639
Cdd:cd21334    81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 123-238 1.96e-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: 95.43  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 123 EEEKYAFVNWINKALENDPDCRHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKkltPFIIQENLNLALN 202
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRV-------TNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907202322 203 SAS-AIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIG 238
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 127-237 7.20e-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: 90.45  E-value: 7.20e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  127 YAFVNWINKALENDPdcrhvipmNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKlTPFIIQENLNLALNSASA 206
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEK 71

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907202322  207 IGCHVVNIGAEDLRAGkPHLVLGLLWQIIKI 237
Cdd:smart00033  72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 530-637 2.05e-20

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 86.57  E-value: 2.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 530 DDIIVNWVNRTLSEAGKSTSIQSFKdKTISSSLAVVDLIDAIQPGCINYDLVksgNLTEDDKHNNAKYAVSMARR-IGAR 608
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKL---NKSEFDKLENINLALDVAEKkLGVP 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907202322 609 VYAL-PEDLVEVKPKMVMTVFACLMGRGMK 637
Cdd:pfam00307  80 KVLIePEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 267-388 1.49e-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: 81.56  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 267 LSPEELLLRWANFHLENSGWQKINNfsadikliDFSNSVKDSKAYFHLLNQIAPKGQKEGEPRidinmsgFNETDDLKRA 346
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVT--------NFTTDLRDGLALCALLNKLAPGLVDKKKLN-------KSEFDKLENI 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907202322 347 ESMLQQA-DKLGCRQF-VTPADVVSGNPKLNLAFVANLFNKYPA 388
Cdd:pfam00307  66 NLALDVAeKKLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 408-514 6.04e-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: 6.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNSL----GVNPHVNHLYADLQDALVILQLYERIKvP--VDWSKVNKPPypklganMKKLENCNYAVELGKN 481
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907202322 482 PAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRY 514
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 410-513 7.03e-16

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: 73.50  E-value: 7.03e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  410 RTFRNWMNSLGVN---PHVNHLYADLQDALVILQLYERIKVP-VDWSKVNKPPYPklganMKKLENCNYAVELGKNpAKF 485
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAEK-LGG 74

                           90       100
                   ....*....|....*....|....*...
gi 1907202322  486 SLVGIGGQDLNDGNPtLTLAVVWQLMRR 513
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 531-632 1.61e-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: 69.65  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  531 DIIVNWVNRTLSEAGKSTSiqSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEdDKHNNAKYAVSMARRIG-ARV 609
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPV--TNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRF-KKIENINLALSFAEKLGgKVV 77

                           90       100
                   ....*....|....*....|...
gi 1907202322  610 YALPEDLVEvKPKMVMTVFACLM 632
Cdd:smart00033  78 LFEPEDLVE-GPKLILGVIWTLI 99
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 16-82 2.08e-14

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: 67.96  E-value: 2.08e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907202322  16 ELKEAFAKVDLNSNGFICDYELHELFKEANMPLPgykvREIIQKLMVDGDRNKDGKISFNEFVYIFQ 82
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS----EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 271-385 3.51e-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: 68.50  E-value: 3.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  271 ELLLRWANFHLENSGWQKINNFSADIklidfsnsvKDSKAYFHLLNQIAPKGQKEgepriDINMSGFNETDDLKRAESML 350
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDL---------KDGVALCALLNSLSPGLVDK-----KKVAASLSRFKKIENINLAL 66

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907202322  351 QQADKLGC-RQFVTPADVVSGnPKLNLAFVANLFNK 385
Cdd:smart00033  67 SFAEKLGGkVVLFEPEDLVEG-PKLILGVIWTLISL 101
EF-hand_7 pfam13499
EF-hand domain pair;
15-82 6.88e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 55.34  E-value: 6.88e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907202322  15 DELKEAFAKVDLNSNGFICDYELHELFKEANMPLPgyKVREIIQKLMVDGDRNKDGKISFNEFVYIFQ 82
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEP--LSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-88 1.30e-07

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.95  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322   1 MDEMATTQISKDELD---ELKEAFAKVDLNSNGFICDYELHELFKEANMPLPgyKVREIIQKLmvdgDRNKDGKISFNEF 77
Cdd:COG5126    52 REEFVAGMESLFEATvepFARAAFDLLDTDGDGKISADEFRRLLTALGVSEE--EADELFARL----DTDGDGKISFEEF 125

                          90
                  ....*....|.
gi 1907202322  78 VYIFQEVKSSD 88
Cdd:COG5126   126 VAAVRDYYTPD 136
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
402-619 1.32e-07

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 54.56  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 402 LEGETREERTFRNWMN---SLGVNPHVNHLYADLQDALVILQLYERIKvpvDWSKVNKPPYPKlgANMKKLENCNYAVEL 478
Cdd:COG5069     4 KKWQKVQKKTFTKWTNeklISGGQKEFGDLDTDLKDGVKLAQLLEALQ---KDNAGEYNETPE--TRIHVMENVSGRLEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 479 GKNpAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVLEDLGEGQKANDdiIVNWVNRTLSEAGKSTSIQSFKDKTi 558
Cdd:COG5069    79 IKG-KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGELTKHIN--LLLWCDEDTGGYKPEVDTFDFFRSW- 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907202322 559 SSSLAVVDLIDAIQPGCINY---DLVKSGN-LTEDDKHNNAKYAVSMARRIGArvyalpEDLVEV 619
Cdd:COG5069   155 RDGLAFSALIHDSRPDTLDPnvlDLQKKNKaLNNFQAFENANKVIGIARLIGV------EDIVNV 213
PTZ00184 PTZ00184
calmodulin; Provisional
 4-78 1.04e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 42.83  E-value: 1.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907202322   4 MATTQISKDELDELKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKLMVDGdrnkDGKISFNEFV 78
Cdd:PTZ00184   73 MARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDG----DGQINYEEFV 143
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 57-84 1.26e-03

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: 36.59  E-value: 1.26e-03
                           10        20
                   ....*....|....*....|....*...
gi 1907202322   57 IQKLMVDGDRNKDGKISFNEFVYIFQEV 84
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 101-245 8.49e-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: 316.14  E-value: 8.49e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 101 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 180
Cdd:cd21292     1 EGIDAKGGTSEASSEGTTHSYSEEEKVAFVNWINKNLGDDPDCKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907202322 181 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIEL 245
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 ...
 386-519 2.88e-101

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: 304.23  E-value: 2.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 386 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGAN 465
Cdd:cd21331     1 YPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVNKPPYPKLGAN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907202322 466 MKKLENCNYAVELGKNPAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVL 519
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 ...
 101-248 2.97e-100

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: 301.98  E-value: 2.97e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 101 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 180
Cdd:cd21325     1 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907202322 181 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRN 248
Cdd:cd21325    81 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRN 148
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 101-245 1.62e-96

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: 1.62e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 101 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 180
Cdd:cd21323     1 EGITAIGGTSAISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907202322 181 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIEL 245
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 ...
 101-245 6.64e-92

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: 280.36  E-value: 6.64e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 101 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 180
Cdd:cd21324     1 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALENDPDCKHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907202322 181 RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIEL 245
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 ...
 254-384 6.98e-85

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: 261.44  E-value: 6.98e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 254 LLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKlidfsnsvkDSKAYFHLLNQIAPKGQKEGEPRIDIN 333
Cdd:cd21328     1 LLRDGETLEDLMKLSPEELLLRWANFHLENAGWQKINNFSSDIK---------DSRAYFHLLNQIAPKGQKEGEPRIDIN 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907202322 334 MSGFNETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 384
Cdd:cd21328    72 MSGFNEKDDLKRAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 122
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
106-632 1.69e-83

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 274.51  E-value: 1.69e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 106 LGGTSELSSEGTQHSYSEEEKyaFVNWINKALENDPDCRHVIPmNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINK 185
Cdd:COG5069   103 LGLIWSLISRLTIATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDL 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 186 ----KKLTPFIIQENLNLALNSASAIG-CHVVNIGAEDLRAgkpHLVLgLLWQIIKIGLFADIELSRNEaLAALLRDGET 260
Cdd:COG5069   180 qkknKALNNFQAFENANKVIGIARLIGvEDIVNVSIPDERS---IMTY-VSWYIIRFGLLEKIDIALHR-VYRLLEADET 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 261 LEElMKLSPEELLLRWAN-FHLENSGWQKINnfsadiklidFSNSVKDSKAYFHLLNQIAPKGQKEGEPRIDInmsgfne 339
Cdd:COG5069   255 LIQ-LRLPYEIILLRLLNlIHLKQANWKVVN----------FSKDVSDGENYTDLLNQLNALCSRAPLETTDL------- 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 340 tddLKRAESMLQQADKLGCRQFVTPAdvvsGNPKLNLAFVANLFNKYPALTKPENQ---DIDWTLLEGEtREERTFRNWM 416
Cdd:COG5069   317 ---HSLAGQILQNAEKYDCRKYLPPA----GNPKLDLAFVAHLFNTHPGQEPLEEEekpEIEEFDAEGE-FEARVFTFWL 388

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 417 NSLGVNPHVNHLYADLQDALVILQLYERIKVP--VDWSKVNKPPYPKLGAN-MKKLENCNYAVELGKNpAKFSLVGIGGQ 493
Cdd:COG5069   389 NSLDVSPEITNLFGDLRDQLILLQALSKKLMPmtVTHKLVKKQPASGIEENrFKAFENENYAVDLGIT-EGFSLVGIKGL 467

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 494 DLNDGNpTLTLAVVWQLMRRYTLNVLEDLGEGQKA-NDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLA-VVDLIDAI 571
Cdd:COG5069   468 EILDGI-RLKLTLVWQVLRSNTALFNHVLKKDGCGlSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVSGVfYLDVLKGI 546

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907202322 572 QPGCINYDLVKSGNLTEDDKHNNAKYAVS--MARRIGARVYALPEDLVEVKPKM-VMTVFACLM 632
Cdd:COG5069   547 HSELVDYDLVTRGFTEFDDIADARSLAISskILRSLGAIIKFLPEDINGVRPRLdVLTFIESLM 610
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 395-519 3.17e-80

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: 249.52  E-value: 3.17e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 395 QDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNY 474
Cdd:cd21330     1 QDIDWSSIEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGENMKKLENCNY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907202322 475 AVELGKNPAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVL 519
Cdd:cd21330    81 AVELGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 125
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 402-519 2.75e-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: 241.43  E-value: 2.75e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 402 LEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNYAVELGKN 481
Cdd:cd21329     1 LEGESSEERTFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRVPVDWGHVNKPPYPALGGNMKKIENCNYAVELGKN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907202322 482 PAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVL 519
Cdd:cd21329    81 KAKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
CH_PLS3_rpt4 cd21334
fourth calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 528-639 3.77e-77

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: 240.95  E-value: 3.77e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 528 ANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMARRIGA 607
Cdd:cd21334     1 VNDDIIVNWVNRTLSEAGKSTSIQNFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTDDDKLDNAKYAVSMARKIGA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907202322 608 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 639
Cdd:cd21334    81 RVYALPEDLVEVKPKMVMTVFACLMGRGMKRV 112
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 402-519 7.17e-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: 237.52  E-value: 7.17e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 402 LEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNYAVELGKN 481
Cdd:cd21298     1 VIEETREEKTYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKPFKKLGANMKKIENCNYAVELGKK 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907202322 482 PaKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVL 519
Cdd:cd21298    81 L-KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLSIL 117
CH_PLS2_rpt2 cd21327
second calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 254-387 1.04e-73

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: 232.54  E-value: 1.04e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 254 LLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKlidfsnsvkDSKAYFHLLNQIAPKGQKEGEPRIDIN 333
Cdd:cd21327     1 LLRDGESLEDLMKLSPEELLLRWANYHLENAGCNKINNFSSDIK---------DSKAYYHLLNQVAPKGDEEGIPAIVID 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907202322 334 MSGFNETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFNKYP 387
Cdd:cd21327    72 MSGLREKDDLKRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYP 125
CH_PLS2_rpt4 cd21333
fourth calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 523-637 1.60e-69

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: 221.02  E-value: 1.60e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 523 GEGQKANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMA 602
Cdd:cd21333     1 GGGQKVNDETIVNWVNETLTEAGKSSSISSFKDGKISTSMPVLDLIDAIQPGSINYDLLKTEDLNDEEKLNNAKYAISMA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907202322 603 RRIGARVYALPEDLVEVKPKMVMTVFACLMGRGMK 637
Cdd:cd21333    81 RKIGARVYALPEDLVEVKPKMVMTVFACLMGRGMK 115
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 257-387 1.67e-68

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: 218.60  E-value: 1.67e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 257 DGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKlidfsnsvkDSKAYFHLLNQIAPKGQKEGePRIDINMSG 336
Cdd:cd21326     1 EGEELEELMKLSPEELLLRWVNYHLTNAGWQNISNFSQDIK---------DSRAYFHLLNQIAPKGDVFD-ENIEIDFSG 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907202322 337 FNETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFNKYP 387
Cdd:cd21326    71 FNEKNDLKRAEYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYP 121
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
 257-384 1.28e-65

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


Pssm-ID: 409144  Cd Length: 113  Bit Score: 210.59  E-value: 1.28e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 257 DGETLEELMKLSPEELLLRWANFHLENSGWQK-INNFSADIKlidfsnsvkDSKAYFHLLNQIAPKGQKEGepridinMS 335
Cdd:cd21295     1 DGETLEDLLKLSPEEILLRWVNYHLERAGCDRrIKNFSGDIK---------DSEAYTHLLKQIAPKDAGVD-------TS 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907202322 336 GFNETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 384
Cdd:cd21295    65 ALRESDLLQRAELMLQNADKIGCRKFVTPKDVVTGNPKLNLAFVANLFN 113
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 529-635 3.45e-61

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: 198.66  E-value: 3.45e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 529 NDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNlTEDDKHNNAKYAVSMARRIGAR 608
Cdd:cd21301     2 SDKEIVEWANEKLKSAGKSTSISSFKDPSISTSLPILDLIDAIKPGSVDYSLVLEGN-SEEDKLSNAKYAISMARKIGAR 80

                          90       100
                  ....*....|....*....|....*..
gi 1907202322 609 VYALPEDLVEVKPKMVMTVFACLMGRG 635
Cdd:cd21301    81 VYALPEDIVEVKPKMVMTVFACLMALD 107
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 521-635 1.02e-58

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: 192.47  E-value: 1.02e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 521 DLGEGQKANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVS 600
Cdd:cd21332     1 DLGEGEKVNDEIIIKWVNQTLANANKTTSITSFKDKSISTSLPVLDLIDAIAPNAIREEMVKREDLSDADKLNNAKYAIS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907202322 601 MARRIGARVYALPEDLVEVKPKMVMTVFACLMGRG 635
Cdd:cd21332    81 VARKIGARVYALPEDLVEVKPKMVMTVFACLMGKG 115
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 124-236 1.07e-54

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 181.62  E-value: 1.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 124 EEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKK-LTPFIIQENLNLALN 202
Cdd:cd21217     1 EEKEAFVEHINSLLADDPDLKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKpKNIFEATENLNLALN 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907202322 203 SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 236
Cdd:cd21217    81 AAKKIGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 404-519 2.10e-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: 175.55  E-value: 2.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 404 GETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKV-PVDWSKVNKppyPKLGANMKKLENCNYAVELGKNp 482
Cdd:cd21219     1 EGSREERAFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQPgCVNWKKVNK---PKPLNKFKKVENCNYAVDLAKK- 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907202322 483 AKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVL 519
Cdd:cd21219    77 LGFSLVGIGGKDIADGNRKLTLALVWQLMRYHVLQIL 113
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 528-632 9.14e-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: 157.43  E-value: 9.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 528 ANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGnLTEDDKHNNAKYAVSMARRIGA 607
Cdd:cd21220     1 VTDADILAWANSKVREAGKSSPISSFKDPSLSTGLFLLDLLAAIDPGAVDYDLVTEG-ETDEEKEQNAKYAISLARKIGA 79

                          90       100
                  ....*....|....*....|....*
gi 1907202322 608 RVYALPEDLVEVKPKMVMTVFACLM 632
Cdd:cd21220    80 VIFLLWEDIVEVKPKMILTFVASLM 104
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 125-237 3.41e-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: 156.15  E-value: 3.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAIN-KKKLTPFIIQENLNLALNS 203
Cdd:cd21293     2 EKGSYVDHINRYLGDDPFLKQFLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINtKKVLNPWERNENHTLCLNS 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907202322 204 ASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKI 237
Cdd:cd21293    82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQIIKI 115
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 402-519 3.15e-44

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: 153.73  E-value: 3.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 402 LEGEtREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIkVP--VDWSKVNKPPYPKLGANMKKLENCNYAVELG 479
Cdd:cd21300     3 AEGE-REARVFTLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKV-IPgsVNWKKVNKAPASAEISRFKAVENTNYAVELG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907202322 480 KNpAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVL 519
Cdd:cd21300    81 KQ-LGFSLVGIQGADITDGSRTLTLALVWQLMRFHITKTL 119
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 119-238 2.93e-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: 148.75  E-value: 2.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 119 HSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINK-----KKLTPFII 193
Cdd:cd21294     1 HTINEDERREFTKHINAVLAGDPDVGSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIDERVLNKpprknKPLNNFQM 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907202322 194 QENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIG 238
Cdd:cd21294    81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRRG 125
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 259-384 7.48e-42

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 147.06  E-value: 7.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 259 ETLEELMKLSPEELLLRWANFHLENSGWQK--INNFSADIKlidfsnsvkDSKAYFHLLNQIAPKGQKEgepriDINMSG 336
Cdd:cd21218     1 ETLESLLYLPPEEILLRWVNYHLKKAGPTKkrVTNFSSDLK---------DGEVYALLLHSLAPELCDK-----ELVLEV 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907202322 337 FNETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 384
Cdd:cd21218    67 LSEEDLEKRAEKVLQAAEKLGCKYFLTPEDIVSGNPRLNLAFVATLFN 114
CH_FIMB_rpt2 cd21297
second calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 259-384 1.84e-35

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: 129.22  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 259 ETLEELMKLSPEELLLRWANFHLENSGW-QKINNFSADiklidfsnsVKDSKAYFHLLNQIAPkGQKEGEPridinmsgF 337
Cdd:cd21297     1 ETLEQFLRLPPEQILLRWFNYHLKAANWpRRVSNFSKD---------VSDGENYTVLLNQLAP-ELCSRAP--------L 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907202322 338 NETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 384
Cdd:cd21297    63 QTTDLLQRAEQVLQNAEKLDCRKFLTPTSLVAGNPKLNLAFVANLFN 109
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 404-519 3.14e-32

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: 120.30  E-value: 3.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 404 GETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKV-PVDWSKVNKPPyPKLgaNMKKLENCNYAVELGKNp 482
Cdd:cd21299     1 ETSREERCFRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPgSVNWKHANKPP-IKM--PFKKVENCNQVVKIGKQ- 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907202322 483 AKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVL 519
Cdd:cd21299    77 LKFSLVNVAGNDIVQGNKKLILALLWQLMRYHMLQLL 113
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 259-383 1.40e-31

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: 118.39  E-value: 1.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 259 ETLEELMKLSPEELLLRWANFHLENSGWQK-INNFSADiklidfsnsVKDSKAYFHLLNQIAPKGQkegepridiNMSGF 337
Cdd:cd21296     1 EDVEELLRLPPEKVLLKWMNFHLKKAGYKKtVTNFSSD---------VKDAEAYAYLLNVLAPEHC---------DPATL 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907202322 338 NETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLF 383
Cdd:cd21296    63 EAKDPLERAKLVLEQAEKMNCKRYLTAKDIVEGSANLNLAFVAQIF 108
CH_FIMB_rpt4 cd21303
fourth calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 525-632 6.29e-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: 6.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 525 GQKANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNlTEDDKHNNAKYAVSMARR 604
Cdd:cd21303     1 GKEITDSDMVKWANDMVAKGGKNSSIRSFKDPSLSTGHFFLDVLNGLKSGYVDYDLVTPGN-TEDEAYLNAKLAISIARK 79

                          90       100
                  ....*....|....*....|....*...
gi 1907202322 605 IGARVYALPEDLVEVKPKMVMTVFACLM 632
Cdd:cd21303    80 LGALIFLVPEDIVEVRPRLVLTFIGSLM 107
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 530-632 3.85e-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: 105.71  E-value: 3.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 530 DDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGnLTEDDKHNNAKYAVSMARRIGARV 609
Cdd:cd21302     4 DADILSWANRKVRTMGRKSQIESFKDKSLSSGLFFLELLWAVEPRVVNWNLVTKG-ETDEEKRLNATYIISVARKLGCSI 82

                          90       100
                  ....*....|....*....|...
gi 1907202322 610 YALPEDLVEVKPKMVMTVFACLM 632
Cdd:cd21302    83 FLLPEDIVEVNQKMILILTASIM 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 123-238 1.96e-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: 95.43  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 123 EEEKYAFVNWINKALENDPDCRHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKkltPFIIQENLNLALN 202
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRV-------TNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLALD 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907202322 203 SAS-AIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIG 238
Cdd:pfam00307  71 VAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 127-237 7.20e-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: 90.45  E-value: 7.20e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  127 YAFVNWINKALENDPdcrhvipmNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKlTPFIIQENLNLALNSASA 206
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL-SRFKKIENINLALSFAEK 71

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907202322  207 IGCHVVNIGAEDLRAGkPHLVLGLLWQIIKI 237
Cdd:smart00033  72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 530-637 2.05e-20

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 86.57  E-value: 2.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 530 DDIIVNWVNRTLSEAGKSTSIQSFKdKTISSSLAVVDLIDAIQPGCINYDLVksgNLTEDDKHNNAKYAVSMARR-IGAR 608
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTNFT-TDLRDGLALCALLNKLAPGLVDKKKL---NKSEFDKLENINLALDVAEKkLGVP 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907202322 609 VYAL-PEDLVEVKPKMVMTVFACLMGRGMK 637
Cdd:pfam00307  80 KVLIePEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 267-388 1.49e-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: 81.56  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 267 LSPEELLLRWANFHLENSGWQKINNfsadikliDFSNSVKDSKAYFHLLNQIAPKGQKEGEPRidinmsgFNETDDLKRA 346
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVT--------NFTTDLRDGLALCALLNKLAPGLVDKKKLN-------KSEFDKLENI 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907202322 347 ESMLQQA-DKLGCRQF-VTPADVVSGNPKLNLAFVANLFNKYPA 388
Cdd:pfam00307  66 NLALDVAeKKLGVPKVlIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 408-514 6.04e-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: 6.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNSL----GVNPHVNHLYADLQDALVILQLYERIKvP--VDWSKVNKPPypklganMKKLENCNYAVELGKN 481
Cdd:pfam00307   3 LEKELLRWINSHlaeyGPGVRVTNFTTDLRDGLALCALLNKLA-PglVDKKKLNKSE-------FDKLENINLALDVAEK 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907202322 482 PAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRY 514
Cdd:pfam00307  75 KLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 126-236 6.75e-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: 76.61  E-value: 6.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 126 KYAFVNWINKALENDPdcrhvipmNPNTDDLFKAVGDGIVLCKMINLSVPDTIDEraINKKKLTPFIIQENLNLALNSAS 205
Cdd:cd00014     1 EEELLKWINEVLGEEL--------PVSITDLFESLRDGVLLCKLINKLSPGSIPK--INKKPKSPFKKRENINLFLNACK 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907202322 206 AIG-CHVVNIGAEDLRAGK-PHLVLGLLWQIIK 236
Cdd:cd00014    71 KLGlPELDLFEPEDLYEKGnLKKVLGTLWALAL 103
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 410-513 7.03e-16

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: 73.50  E-value: 7.03e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  410 RTFRNWMNSLGVN---PHVNHLYADLQDALVILQLYERIKVP-VDWSKVNKPPYPklganMKKLENCNYAVELGKNpAKF 485
Cdd:smart00033   1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSR-----FKKIENINLALSFAEK-LGG 74

                           90       100
                   ....*....|....*....|....*...
gi 1907202322  486 SLVGIGGQDLNDGNPtLTLAVVWQLMRR 513
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 531-632 1.61e-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: 69.65  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  531 DIIVNWVNRTLSEAGKSTSiqSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEdDKHNNAKYAVSMARRIG-ARV 609
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPV--TNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRF-KKIENINLALSFAEKLGgKVV 77

                           90       100
                   ....*....|....*....|...
gi 1907202322  610 YALPEDLVEvKPKMVMTVFACLM 632
Cdd:smart00033  78 LFEPEDLVE-GPKLILGVIWTLI 99
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 16-82 2.08e-14

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: 67.96  E-value: 2.08e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907202322  16 ELKEAFAKVDLNSNGFICDYELHELFKEANMPLPgykvREIIQKLMVDGDRNKDGKISFNEFVYIFQ 82
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS----EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 271-385 3.51e-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: 68.50  E-value: 3.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  271 ELLLRWANFHLENSGWQKINNFSADIklidfsnsvKDSKAYFHLLNQIAPKGQKEgepriDINMSGFNETDDLKRAESML 350
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDL---------KDGVALCALLNSLSPGLVDK-----KKVAASLSRFKKIENINLAL 66

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907202322  351 QQADKLGC-RQFVTPADVVSGnPKLNLAFVANLFNK 385
Cdd:smart00033  67 SFAEKLGGkVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 408-513 1.11e-12

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: 65.01  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNSL--GVNPHVNHLYADLQDALVILQLYERIKvpvdWSKVNKPPYPKLgaNMKKLENCNYAVELGKnpAKF 485
Cdd:cd21193    17 QKKTFTKWINSFleKANLEIGDLFTDLSDGKLLLKLLEIIS----GEKLGKPNRGRL--RVQKIENVNKALAFLK--TKV 88

                          90       100
                  ....*....|....*....|....*...
gi 1907202322 486 SLVGIGGQDLNDGNPTLTLAVVWQLMRR 513
Cdd:cd21193    89 RLENIGAEDIVDGNPRLILGLIWTIILR 116
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 122-236 1.93e-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: 64.23  E-value: 1.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 122 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLTPFIIQENLNLA 200
Cdd:cd21219     3 SREER-AFRMWLNS-----------LGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVNwKKVNKPKPLNKFKKVENCNYA 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907202322 201 LNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 236
Cdd:cd21219    71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMR 106
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 403-513 3.27e-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: 60.84  E-value: 3.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 403 EGETREERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKvpvdWSKVNKPPYPKLGANMkkLENCNYAVELGK 480
Cdd:cd21246    12 EREAVQKKTFTKWVNShlARVGCRINDLYTDLRDGRMLIKLLEVLS----GERLPKPTKGKMRIHC--LENVDKALQFLK 85

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907202322 481 NpAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRR 513
Cdd:cd21246    86 E-QRVHLENMGSHDIVDGNHRLTLGLIWTIILR 117
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 123-235 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 1907202322 123 EEEKYAFVNWINKALEndpdcrhviPMNPNTDDLFKAVGDGIVLCKMInlsvpDTIDER---AINKKKLTPFIIQENLNL 199
Cdd:cd21227     3 EIQKNTFTNWVNEQLK---------PTGMSVEDLATDLEDGVKLIALV-----EILQGRklgRVIKKPLNQHQKLENVTL 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907202322 200 ALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21227    69 ALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLI 104
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 408-514 7.74e-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: 59.34  E-value: 7.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIkvpvdwSKVNKPPY---PKLgaNMKKLENCNYAVELGKNp 482
Cdd:cd21215     5 QKKTFTKWLNTklSSRGLSITDLVTDLSDGVRLIQLLEII------GDESLGRYnknPKM--RVQKLENVNKALEFIKS- 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907202322 483 AKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRY 514
Cdd:cd21215    76 RGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 403-513 2.53e-10

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


Pssm-ID: 409167  Cd Length: 139  Bit Score: 58.88  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 403 EGETREERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKVpvdwskvNKPPYPKLG-ANMKKLENCNYAVELG 479
Cdd:cd21318    34 EREAVQKKTFTKWVNShlARVPCRINDLYTDLRDGYVLTRLLEVLSG-------EQLPKPTRGrMRIHSLENVDKALQFL 106

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907202322 480 KNpAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRR 513
Cdd:cd21318   107 KE-QRVHLENVGSHDIVDGNHRLTLGLIWTIILR 139
EF-hand_7 pfam13499
EF-hand domain pair;
15-82 6.88e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 55.34  E-value: 6.88e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907202322  15 DELKEAFAKVDLNSNGFICDYELHELFKEANMPLPgyKVREIIQKLMVDGDRNKDGKISFNEFVYIFQ 82
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEP--LSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 125-235 9.45e-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: 9.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKALEndpDCRHVIpmnpntDDLFKAVGDGIVLCKMINLSVPDTIDEraINKKKLTPFIIqENLNLALNSA 204
Cdd:cd21193    17 QKKTFTKWINSFLE---KANLEI------GDLFTDLSDGKLLLKLLEIISGEKLGK--PNRGRLRVQKI-ENVNKALAFL 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907202322 205 SAiGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21193    85 KT-KVRLENIGAEDIVDGNPRLILGLIWTII 114
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 125-235 2.16e-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: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKALEndpdcRHVIPMNPNtdDLFKAVGDGIVLCKMIN-LSVPDTIDERAINkkkltPFIIQENLNLALNS 203
Cdd:cd21242     6 QKRTFTNWINSQLA-----KHSPPSVVS--DLFTDIQDGHRLLDLLEvLSGQQLPREKGHN-----VFQCRSNIETALSF 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907202322 204 ASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21242    74 LKNKSIKLINIHVPDIIEGKPSIILGLIWTII 105
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 403-524 2.18e-09

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: 55.76  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 403 EGETREERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKVpvdwskvNKPPYPKLGANMKKLENCNYAVELGK 480
Cdd:cd21236    13 ERDKVQKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVLSG-------DTLPREKGRMRFHRLQNVQIALDYLK 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907202322 481 NpAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVLEDLGE 524
Cdd:cd21236    86 R-RQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 125-244 3.47e-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: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKALendpdCRHVIPMNpnTDDLFKAVGDGIVLCKMIN-LSVPDTIDERAINKKKLTpFIiqENLNLALNS 203
Cdd:cd21241     6 QKKTFTNWINSYL-----AKRKPPMK--VEDLFEDIKDGTKLLALLEvLSGEKLPCEKGRRLKRVH-FL--SNINTALKF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907202322 204 ASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIkigLFADIE 244
Cdd:cd21241    76 LESKKIKLVNINPTDIVDGKPSIVLGLIWTII---LYFQIE 113
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 122-236 1.08e-08

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: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 122 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINK---KKLTPFIIQENLN 198
Cdd:cd21298     5 TREEK-TYRNWMNS-----------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSRVNKpfkKLGANMKKIENCN 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907202322 199 LALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 236
Cdd:cd21298    73 YAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMR 110
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 408-512 1.75e-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: 52.96  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNS-LGVNPHVNH----------LYADLQDALVILQLYERIKvP--VDWSKVNKPPyPKlgANMKKLENCNY 474
Cdd:cd21217     2 EKEAFVEHINSlLADDPDLKHllpidpdgddLFEALRDGVLLCKLINKIV-PgtIDERKLNKKK-PK--NIFEATENLNL 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907202322 475 AVELGKNpAKFSLVGIGGQDLNDGNPTLTLAVVWQLMR 512
Cdd:cd21217    78 ALNAAKK-IGCKVVNIGPQDILDGNPHLVLGLLWQIIR 114
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 125-236 2.38e-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: 52.40  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKALEndpdcRHVIPMNpntdDLFKAVGDGIVLCKMINLsVPDTIDERAINKKKLTpfiIQ--ENLNLALN 202
Cdd:cd21215     5 QKKTFTKWLNTKLS-----SRGLSIT----DLVTDLSDGVRLIQLLEI-IGDESLGRYNKNPKMR---VQklENVNKALE 71

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907202322 203 SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 236
Cdd:cd21215    72 FIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLIL 105
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 403-524 2.59e-08

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


Pssm-ID: 409086  Cd Length: 118  Bit Score: 52.34  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 403 EGETREERTFRNWMNS--LGVNPHVNHLYADLQDA---LVILQLYERIKVPVDWSKVNkppypklganMKKLENCNYAVE 477
Cdd:cd21237     2 ERDRVQKKTFTKWVNKhlMKVRKHINDLYEDLRDGhnlISLLEVLSGVKLPREKGRMR----------FHRLQNVQIALD 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907202322 478 LGKNpAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVLEDLGE 524
Cdd:cd21237    72 FLKQ-RQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGE 117
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 403-513 3.54e-08

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: 52.36  E-value: 3.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 403 EGETREERTFRNWMNS-LG-VNPHVNHLYADLQDALVILQLYERIKvpvdWSKVNKPPYPKLgaNMKKLENCNYAVELGK 480
Cdd:cd21317    27 EREAVQKKTFTKWVNShLArVTCRIGDLYTDLRDGRMLIRLLEVLS----GEQLPKPTKGRM--RIHCLENVDKALQFLK 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907202322 481 NpAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRR 513
Cdd:cd21317   101 E-QKVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 408-508 3.84e-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: 51.61  E-value: 3.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNSLGVN---PHVNHLYADLQDALVILQLYERIkvpvdwSKVNKPPyPKLGANMKKLENCNYAVE-LGKNPA 483
Cdd:cd21186     3 QKKTFTKWINSQLSKankPPIKDLFEDLRDGTRLLALLEVL------TGKKLKP-EKGRMRVHHLNNVNRALQvLEQNNV 75

                          90       100
                  ....*....|....*....|....*
gi 1907202322 484 KfsLVGIGGQDLNDGNPTLTLAVVW 508
Cdd:cd21186    76 K--LVNISSNDIVDGNPKLTLGLVW 98
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 403-524 4.91e-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: 4.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 403 EGETREERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKVpvdwskvNKPPYPKLGANMKKLENCNYAVELGK 480
Cdd:cd21235     2 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSG-------DSLPREKGRMRFHKLQNVQIALDYLR 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907202322 481 NpAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVLEDLGE 524
Cdd:cd21235    75 H-RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 117
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 123-239 8.45e-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: 8.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 123 EEEKYAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKK----LTPFIIQENLN 198
Cdd:cd21300     6 EREARVFTLWLNS-----------LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKVNKAPasaeISRFKAVENTN 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907202322 199 LALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGL 239
Cdd:cd21300    75 YAVELGKQLGFSLVGIQGADITDGSRTLTLALVWQLMRFHI 115
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 125-235 1.00e-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: 50.48  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKkkltpFIIQENLNLALNS 203
Cdd:cd21188     4 QKKTFTKWVNK---------HLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPrERGRMR-----FHRLQNVQTALDF 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907202322 204 ASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21188    70 LKYRKIKLVNIRAEDIVDGNPKLTLGLIWTII 101
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-88 1.30e-07

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.95  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322   1 MDEMATTQISKDELD---ELKEAFAKVDLNSNGFICDYELHELFKEANMPLPgyKVREIIQKLmvdgDRNKDGKISFNEF 77
Cdd:COG5126    52 REEFVAGMESLFEATvepFARAAFDLLDTDGDGKISADEFRRLLTALGVSEE--EADELFARL----DTDGDGKISFEEF 125

                          90
                  ....*....|.
gi 1907202322  78 VYIFQEVKSSD 88
Cdd:COG5126   126 VAAVRDYYTPD 136
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
402-619 1.32e-07

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 54.56  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 402 LEGETREERTFRNWMN---SLGVNPHVNHLYADLQDALVILQLYERIKvpvDWSKVNKPPYPKlgANMKKLENCNYAVEL 478
Cdd:COG5069     4 KKWQKVQKKTFTKWTNeklISGGQKEFGDLDTDLKDGVKLAQLLEALQ---KDNAGEYNETPE--TRIHVMENVSGRLEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 479 GKNpAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVLEDLGEGQKANDdiIVNWVNRTLSEAGKSTSIQSFKDKTi 558
Cdd:COG5069    79 IKG-KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGELTKHIN--LLLWCDEDTGGYKPEVDTFDFFRSW- 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907202322 559 SSSLAVVDLIDAIQPGCINY---DLVKSGN-LTEDDKHNNAKYAVSMARRIGArvyalpEDLVEV 619
Cdd:COG5069   155 RDGLAFSALIHDSRPDTLDPnvlDLQKKNKaLNNFQAFENANKVIGIARLIGV------EDIVNV 213
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 408-508 1.96e-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: 49.71  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIkvpvdwSKVNkppYPKLGANMK--KLENCNYAVELGKNpA 483
Cdd:cd21188     4 QKKTFTKWVNKhlIKARRRVVDLFEDLRDGHNLISLLEVL------SGES---LPRERGRMRfhRLQNVQTALDFLKY-R 73

                          90       100
                  ....*....|....*....|....*
gi 1907202322 484 KFSLVGIGGQDLNDGNPTLTLAVVW 508
Cdd:cd21188    74 KIKLVNIRAEDIVDGNPKLTLGLIW 98
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 125-244 2.11e-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: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKALEndpdcRHVIPMNpnTDDLFKAVGDGIVLCKMINLSVPDTIDERaiNKKKLTPFIIQENLNLALNSA 204
Cdd:cd21190     6 QKKTFTNWINSHLA-----KLSQPIV--INDLFVDIKDGTALLRLLEVLSGQKLPIE--SGRVLQRAHKLSNIRNALDFL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907202322 205 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIkigLFADIE 244
Cdd:cd21190    77 TKRCIKLVNINSTDIVDGKPSIVLGLIWTII---LYFQIE 113
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 403-511 2.56e-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: 49.54  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 403 EGETREERTFRNWMNSLGVN---PHVNHLYADLQDALVILQLYERIKVpvdwskvNKPPYPKLGANMKKLENCNYAVE-L 478
Cdd:cd21231     2 EREDVQKKTFTKWINAQFAKfgkPPIEDLFTDLQDGRRLLELLEGLTG-------QKLVKEKGSTRVHALNNVNKALQvL 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907202322 479 GKNpaKFSLVGIGGQDLNDGNPTLTLAVVWQLM 511
Cdd:cd21231    75 QKN--NVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 530-625 4.03e-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: 48.83  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 530 DDIIVNWVNRTLSEAG-KSTSIQSFkDKTISSSLAVVDLIDAIQPGCINYDLVKSGnLTEDDKHNNAKYAVSMARRIGAR 608
Cdd:cd21218    12 EEILLRWVNYHLKKAGpTKKRVTNF-SSDLKDGEVYALLLHSLAPELCDKELVLEV-LSEEDLEKRAEKVLQAAEKLGCK 89

                          90
                  ....*....|....*..
gi 1907202322 609 VYALPEDLVEVKPKMVM 625
Cdd:cd21218    90 YFLTPEDIVSGNPRLNL 106
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 403-514 7.82e-07

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: 48.14  E-value: 7.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 403 EGETREERTFRNWMNS--LGVNP--HVNHLYADLQDALVILQLYERIKVpvdwskvNKPPYPKlGANMKK---LENCNYA 475
Cdd:cd21241     1 EQERVQKKTFTNWINSylAKRKPpmKVEDLFEDIKDGTKLLALLEVLSG-------EKLPCEK-GRRLKRvhfLSNINTA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907202322 476 VEL--GKnpaKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRY 514
Cdd:cd21241    73 LKFleSK---KIKLVNINPTDIVDGKPSIVLGLIWTIILYF 110
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 125-235 1.09e-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: 47.48  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKALEndpdCRhvipmNPNTDDLFKAVGDGIVLCKMINLsVPDTIDERAINKKKLTPFIIQENLNLALNSA 204
Cdd:cd21183     5 QANTFTRWCNEHLK----ER-----GMQIHDLATDFSDGLCLIALLEN-LSTRPLKRSYNRRPAFQQHYLENVSTALKFI 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907202322 205 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21183    75 EADHIKLVNIGSGDIVNGNIKLILGLIWTLI 105
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 405-514 1.44e-06

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: 47.14  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 405 ETREERTFRNWMNSLGVN---PHVNHLYADLQDALVILQLYERIKvpvdwSKVNKPPYPKLGAN-MKKLENCNYAVELGK 480
Cdd:cd21225     2 EKVQIKAFTAWVNSVLEKrgiPKISDLATDLSDGVRLIFFLELVS-----GKKFPKKFDLEPKNrIQMIQNLHLAMLFIE 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907202322 481 NPAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRY 514
Cdd:cd21225    77 EDLKIRVQGIGAEDFVDNNKKLILGLLWTLYRKY 110
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 125-235 2.18e-06

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409085  Cd Length: 128  Bit Score: 47.29  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 204
Cdd:cd21236    18 QKKTFTKWINQ---------HLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHRLQNVQIALDYL 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907202322 205 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21236    85 KRRQVKLVNIRNDDITDGNPKLTLGLIWTII 115
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 406-514 2.20e-06

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: 47.06  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 406 TREERTFRNWMNSL----GVNPHVNHLYADLQDALVILQLYERIKvpvdWSKVNKPPYPKLGANMkkLENCNYAVELGKN 481
Cdd:cd21247    19 TMQKKTFTKWMNNVfsknGAKIEITDIYTELKDGIHLLRLLELIS----GEQLPRPSRGKMRVHF--LENNSKAITFLKT 92

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907202322 482 PAKFSLvgIGGQDLNDGNPTLTLAVVWQLMRRY 514
Cdd:cd21247    93 KVPVKL--IGPENIVDGDRTLILGLIWIIILRF 123
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 408-514 2.90e-06

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


Pssm-ID: 409076  Cd Length: 109  Bit Score: 46.51  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNSL--GVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPklganMKKLENCNYAVELGKNPAkF 485
Cdd:cd21227     5 QKNTFTNWVNEQlkPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQ-----HQKLENVTLALKAMAEDG-I 78

                          90       100
                  ....*....|....*....|....*....
gi 1907202322 486 SLVGIGGQDLNDGNPTLTLAVVWQLMRRY 514
Cdd:cd21227    79 KLVNIGNEDIVNGNLKLILGLIWHLILRY 107
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 387-518 3.62e-06

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: 46.56  E-value: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 387 PALTKPENQDIDWTLLEgetreERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKvpvdWSKVNKPPYPKLGA 464
Cdd:cd21310     1 PATEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVQKRLNDLQKDLSDGLRLIALLEVLS----QKKMYRKYHPRPNF 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907202322 465 NMKKLENCNYAVELgKNPAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNV 518
Cdd:cd21310    72 RQMKLENVSVALEF-LDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 124
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 405-511 3.85e-06

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: 45.84  E-value: 3.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 405 ETREERTFRNWMNSL--GVNPHVNHLYADLQDALVILQLYERIkvpvdwSKVNKPPYPKLGANMKKLENCNYAVE-LGKN 481
Cdd:cd21214     3 EKQQRKTFTAWCNSHlrKAGTQIENIEEDFRDGLKLMLLLEVI------SGERLPKPERGKMRFHKIANVNKALDfIASK 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907202322 482 PAKfsLVGIGGQDLNDGNPTLTLAVVWQLM 511
Cdd:cd21214    77 GVK--LVSIGAEEIVDGNLKMTLGMIWTII 104
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 387-518 4.59e-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: 46.23  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 387 PALTKPENQDIDWTLLEgetreERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKlga 464
Cdd:cd21308     5 PATEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFR--- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907202322 465 nMKKLENCNYAVELgKNPAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNV 518
Cdd:cd21308    77 -QMQLENVSVALEF-LDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 128
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 403-511 4.74e-06

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


Pssm-ID: 409040  Cd Length: 114  Bit Score: 46.03  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 403 EGETREERTFRNWMNSL--GVNP--HVNHLYADLQDALVILQLYErikVPVDWSKVNKppYPKLGANMKKLENCNYAVEL 478
Cdd:cd21191     1 ERENVQKRTFTRWINLHleKCNPplEVKDLFVDIQDGKILMALLE---VLSGQNLLQE--YKPSSHRIFRLNNIAKALKF 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907202322 479 GKNpAKFSLVGIGGQDLNDGNPTLTLAVVWQLM 511
Cdd:cd21191    76 LED-SNVKLVSIDAAEIADGNPSLVLGLIWNII 107
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 125-246 4.85e-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: 46.17  E-value: 4.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 204
Cdd:cd21235     7 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907202322 205 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 246
Cdd:cd21235    74 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 115
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 403-513 5.78e-06

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: 46.58  E-value: 5.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 403 EGETREERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKvpvdWSKVNKPPYPKLgaNMKKLENCNYAVELGK 480
Cdd:cd21316    49 EREAVQKKTFTKWVNShlARVSCRITDLYMDLRDGRMLIKLLEVLS----GERLPKPTKGRM--RIHCLENVDKALQFLK 122

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907202322 481 NpAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRR 513
Cdd:cd21316   123 E-QRVHLENMGSHDIVDGNHRLTLGLIWTIILR 154
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 17-101 6.44e-06

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 46.12  E-value: 6.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  17 LKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKLmvdgDRNKDGKISFNEFVyifqevkssdiaKTFRKA 96
Cdd:cd15898     2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEV----DTNGDGTLTFDEFE------------ELYKSL 65


                  ....*
gi 1907202322  97 INRKE 101
Cdd:cd15898    66 TERPE 70
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 408-511 7.56e-06

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: 45.00  E-value: 7.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMN---SLGVNPHVNHLYADLQDALVILQLYERIkvpvdwskVNKP-PYPKLGANMKKLENCNYAVE-LGKNp 482
Cdd:cd21232     3 QKKTFTKWINarfSKSGKPPIKDMFTDLRDGRKLLDLLEGL--------TGKSlPKERGSTRVHALNNVNRVLQvLHQN- 73

                          90       100
                  ....*....|....*....|....*....
gi 1907202322 483 aKFSLVGIGGQDLNDGNPTLTLAVVWQLM 511
Cdd:cd21232    74 -NVELVNIGGTDIVDGNHKLTLGLLWSII 101
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 395-516 7.78e-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: 45.52  E-value: 7.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 395 QDIDWTLLEgetreERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERI---KVPvdwsKVNKPPypklgaNMK-- 467
Cdd:cd21311     8 EDAQWKRIQ-----QNTFTRWANEhlKTANKHIADLETDLSDGLRLIALVEVLsgkKFP----KFNKRP------TFRsq 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907202322 468 KLENCNYAVELGKNPAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTL 516
Cdd:cd21311    73 KLENVSVALKFLEEDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 125-235 9.61e-06

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


Pssm-ID: 409095  Cd Length: 117  Bit Score: 45.05  E-value: 9.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMIN-LSvpdtiDER--AINKKKLTPFIIqENLNLAL 201
Cdd:cd21246    17 QKKTFTKWVNS---------HLARVGCRINDLYTDLRDGRMLIKLLEvLS-----GERlpKPTKGKMRIHCL-ENVDKAL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907202322 202 NSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21246    82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTII 115
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 125-235 1.16e-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: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKALENDPdCRhvipmnpnTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFiiqENLNLALNSA 204
Cdd:cd21318    39 QKKTFTKWVNSHLARVP-CR--------INDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRMRIHSL---ENVDKALQFL 106

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907202322 205 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21318   107 KEQRVHLENVGSHDIVDGNHRLTLGLIWTII 137
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 408-514 1.25e-05

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 44.39  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKvpvdwSKVNKPPYPKLGANMK-KLENCNYAVELgKNPAK 484
Cdd:cd21183     5 QANTFTRWCNEhlKERGMQIHDLATDFSDGLCLIALLENLS-----TRPLKRSYNRRPAFQQhYLENVSTALKF-IEADH 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907202322 485 FSLVGIGGQDLNDGNPTLTLAVVWQLMRRY 514
Cdd:cd21183    79 IKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 125-234 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 1907202322 125 EKYAFVNWINKALENDPDCRHVIpmnpntdDLFKAVGDGIVLCKMINLSVPDTIDerAINKKKLTPFIIQENLNLALNSA 204
Cdd:cd21212     1 EIEIYTDWANHYLEKGGHKRIIT-------DLQKDLGDGLTLVNLIEAVAGEKVP--GIHSRPKTRAQKLENIQACLQFL 71

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907202322 205 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQI 234
Cdd:cd21212    72 AALGVDVQGITAEDIVDGNLKAILGLFFSL 101
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 403-511 1.68e-05

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: 44.48  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 403 EGETREERTFRNWMNS----LGVNPHVNHLYADLQDALVILQLYERI---KVPVDWSKVNKppypklgaNMKKLENCNYA 475
Cdd:cd21190     1 EQERVQKKTFTNWINShlakLSQPIVINDLFVDIKDGTALLRLLEVLsgqKLPIESGRVLQ--------RAHKLSNIRNA 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907202322 476 VELGKNpAKFSLVGIGGQDLNDGNPTLTLAVVWQLM 511
Cdd:cd21190    73 LDFLTK-RCIKLVNINSTDIVDGKPSIVLGLIWTII 107
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 387-518 1.69e-05

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: 44.69  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 387 PALTKPENQDIDWTLLEgetreERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKlga 464
Cdd:cd21309     2 PVTEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFR--- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907202322 465 nMKKLENCNYAVELgKNPAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNV 518
Cdd:cd21309    74 -QMQLENVSVALEF-LDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISM 125
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 408-514 2.26e-05

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: 43.63  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNS--LGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKlganMKKLENCNYAVELGKNpAKF 485
Cdd:cd21228     5 QQNTFTRWCNEhlKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRPTFR----QMKLENVSVALEFLER-ESI 79

                          90       100
                  ....*....|....*....|....*....
gi 1907202322 486 SLVGIGGQDLNDGNPTLTLAVVWQLMRRY 514
Cdd:cd21228    80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 403-511 2.52e-05

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


Pssm-ID: 409091  Cd Length: 111  Bit Score: 43.67  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 403 EGETREERTFRNWMNS-LGVNPH---VNHLYADLQDALVILQLYERIkvpvdwsKVNKPPYPKLGANMKKLENCNYAVEL 478
Cdd:cd21242     1 EQEQTQKRTFTNWINSqLAKHSPpsvVSDLFTDIQDGHRLLDLLEVL-------SGQQLPREKGHNVFQCRSNIETALSF 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907202322 479 GKNPAkFSLVGIGGQDLNDGNPTLTLAVVWQLM 511
Cdd:cd21242    74 LKNKS-IKLINIHVPDIIEGKPSIILGLIWTII 105
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 122-236 3.51e-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: 43.26  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 122 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLT-PFIIQENLNLA 200
Cdd:cd21299     3 SREER-CFRLWINS-----------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKmPFKKVENCNQV 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907202322 201 LNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 236
Cdd:cd21299    71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMR 106
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
 17-82 7.38e-05

EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1, or phospholipase C-eta-1 (PLC-eta-1), or phospholipase C-like protein 3 (PLC-L3), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the zona incerta and in the spinal cord. PI-PLC-eta1 may perform a fundamental role in the brain. It may also act in synergy with other PLC subtypes. For instance, it is activated via intracellular Ca2+ mobilization and then plays a role in the amplification of GPCR (G-protein-coupled receptor)-mediated PLC-beta signals. In addition, its activity can be stimulated by ionomycin. PI-PLC-eta1 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases.


Pssm-ID: 320050 [Multi-domain]  Cd Length: 141  Bit Score: 43.09  E-value: 7.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907202322  17 LKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKlmVDGDRNKdGKISFNEFVYIFQ 82
Cdd:cd16220     2 VKQTFEEADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQMFQE--ADTDENQ-GTLTFEEFCVFYK 64
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 125-236 8.82e-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: 8.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMIN-LSVPdtIDERAINK----------KKLtpfii 193
Cdd:cd21331    23 EERTFRNWMNS-----------LGVNPHVNHLYGDLQDALVILQLYEkIKVP--VDWNKVNKppypklganmKKL----- 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907202322 194 qENLNLALN-SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 236
Cdd:cd21331    85 -ENCNYAVElGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMR 127
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 270-383 9.21e-05

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


Pssm-ID: 409069  Cd Length: 105  Bit Score: 41.87  E-value: 9.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 270 EELLLRWANFHLENSGWQ-KINNFSadiklidfSNSVKDSKAYFHLLNQIAPkgqkeGEPRIDINMSGFNETDDLKRAES 348
Cdd:cd21220     3 DADILAWANSKVREAGKSsPISSFK--------DPSLSTGLFLLDLLAAIDP-----GAVDYDLVTEGETDEEKEQNAKY 69

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907202322 349 MLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLF 383
Cdd:cd21220    70 AISLARKIGAVIFLLWEDIVEVKPKMILTFVASLM 104
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 122-236 9.24e-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: 9.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 122 SEEEKyAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLS-VPdtIDERAINKKkltPFIIQ------ 194
Cdd:cd21329     5 SSEER-TFRNWMNS-----------LGVNPYVNHLYSDLCDALVIFQLYEMTrVP--VDWGHVNKP---PYPALggnmkk 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907202322 195 -ENLNLALN-SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 236
Cdd:cd21329    68 iENCNYAVElGKNKAKFSLVGIAGSDLNEGNKTLTLALIWQLMR 111
PTZ00184 PTZ00184
calmodulin; Provisional
 4-78 1.04e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 42.83  E-value: 1.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907202322   4 MATTQISKDELDELKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKLMVDGdrnkDGKISFNEFV 78
Cdd:PTZ00184   73 MARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDG----DGQINYEEFV 143
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 408-512 1.20e-04

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: 42.72  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNS-----------LGVNPHVNHLYADLQDALVILQLYErIKVP--VDWSKVNKppypklganmKKL----- 469
Cdd:cd21323    25 EKVAFVNWINKalegdpdckhvVPMNPTDESLFKSLADGILLCKMIN-LSQPdtIDERAINK----------KKLtpfti 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907202322 470 -ENCNYAVElGKNPAKFSLVGIGGQDLNDGNPTLTLAVVWQLMR 512
Cdd:cd21323    94 sENLNLALN-SASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIK 136
CH_PLS_rpt4 cd21301
fourth calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 273-382 1.44e-04

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: 41.50  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 273 LLRWANFHLENSG-WQKINNFSADiklidfsnSVKDSKAYFHLLNQIAPKGqkegeprIDINM--SGFNETDDLKRAESM 349
Cdd:cd21301     6 IVEWANEKLKSAGkSTSISSFKDP--------SISTSLPILDLIDAIKPGS-------VDYSLvlEGNSEEDKLSNAKYA 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907202322 350 LQQADKLGCRQFVTPADVVSGNPKLNLAFVANL 382
Cdd:cd21301    71 ISMARKIGARVYALPEDIVEVKPKMVMTVFACL 103
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 520-631 1.51e-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: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 520 EDLGEGQKAN-DDIIVNWVNRTLSEAGKSTsIQSFKdKTISSSLAVVDLIDAIQPGCINYDLVKSGNLT---EDDKHNNA 595
Cdd:cd21326     3 EELEELMKLSpEELLLRWVNYHLTNAGWQN-ISNFS-QDIKDSRAYFHLLNQIAPKGDVFDENIEIDFSgfnEKNDLKRA 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907202322 596 KYAVSMARRIGARVYALPEDLVEVKPKMVMTVFACL 631
Cdd:cd21326    81 EYMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANL 116
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 268-372 1.56e-04

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: 41.07  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 268 SPEELLLRWanfhlensgwqkINNFSADIKLIDFSNSVKDSKAYFHLLNQIAPkGQkegeprIDINMSgFNETDDLKRAE 347
Cdd:cd21184     1 SGKSLLLEW------------VNSKIPEYKVKNFTTDWNDGKALAALVDALKP-GL------IPDNES-LDKENPLENAT 60

                          90       100
                  ....*....|....*....|....*.
gi 1907202322 348 SMLQQA-DKLGCRQFVTPADVVSGNP 372
Cdd:cd21184    61 KAMDIAeEELGIPKIITPEDMVSPNV 86
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 124-235 1.69e-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: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 124 EEKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERaiNKKKLTPFIIQeNLNLALNS 203
Cdd:cd21214     5 QQRKTFTAWCNS---------HLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKP--ERGKMRFHKIA-NVNKALDF 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907202322 204 ASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21214    73 IASKGVKLVSIGAEEIVDGNLKMTLGMIWTII 104
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 125-235 2.29e-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: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKALeNDPDCRHVipmnpntDDLFKAVGDGIVLckminLSVPDTIDERAINKKKLTPFIIQ-ENLNLALNS 203
Cdd:cd21186     3 QKKTFTKWINSQL-SKANKPPI-------KDLFEDLRDGTRL-----LALLEVLTGKKLKPEKGRMRVHHlNNVNRALQV 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907202322 204 ASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21186    70 LEQNNVKLVNISSNDIVDGNPKLTLGLVWSII 101
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 125-246 2.72e-04

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


Pssm-ID: 409086  Cd Length: 118  Bit Score: 41.17  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMinLSVPDTIdeRAINKKKLTPFIIQENLNLALNSA 204
Cdd:cd21237     7 QKKTFTKWVNK---------HLMKVRKHINDLYEDLRDGHNLISL--LEVLSGV--KLPREKGRMRFHRLQNVQIALDFL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907202322 205 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 246
Cdd:cd21237    74 KQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYIS 115
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 125-235 2.83e-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: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKALENdpdCrhvipmNP--NTDDLFKAVGDGIVLCKMIN-LSVPDTIDERAINKKKLTPFiiqENLNLAL 201
Cdd:cd21191     6 QKRTFTRWINLHLEK---C------NPplEVKDLFVDIQDGKILMALLEvLSGQNLLQEYKPSSHRIFRL---NNIAKAL 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907202322 202 NSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21191    74 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNII 107
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 388-512 2.87e-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: 41.53  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 388 ALTKPENQDIDWTLLEGETREERTFRNWMNS-----------LGVNPHVNHLYADLQDALVILQLYErIKVP--VDWSKV 454
Cdd:cd21324     5 AIGGTSEQSSAGTQHSYSEEEKYAFVNWINKalendpdckhvIPMNPNTDDLFKAVGDGIVLCKMIN-FSVPdtIDERTI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907202322 455 NKPPYPKLGANmkklENCNYAVElGKNPAKFSLVGIGGQDLNDGNPTLTLAVVWQLMR 512
Cdd:cd21324    84 NKKKLTPFTIQ----ENLNLALN-SASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 136
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 419-513 3.08e-04

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: 40.89  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 419 LGVNPHVNHLYADLQDALVILQLYERIkVP--VDWSKVNKPPYPKLGAN-MKKLENCNYAVELGKNPAkFSLVGIGGQDL 495
Cdd:cd21294    29 LPFPTDTFQLFDECKDGLVLSKLINDS-VPdtIDERVLNKPPRKNKPLNnFQMIENNNIVINSAKAIG-CSVVNIGAGDI 106

                          90
                  ....*....|....*...
gi 1907202322 496 NDGNPTLTLAVVWQLMRR 513
Cdd:cd21294   107 IEGREHLILGLIWQIIRR 124
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 17-96 3.93e-04

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 41.06  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  17 LKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKLMVDGdrnkDGKISFNEFVYIFQEV-KSSDIAKTFRK 95
Cdd:cd16202     2 LKDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSG----EDVLDEEEFVQFYNRLtKRPEIEELFKK 77


                  .
gi 1907202322  96 A 96
Cdd:cd16202    78 Y 78
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 13-78 4.91e-04

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 41.05  E-value: 4.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907202322  13 ELDELKEAFAKVDLNSNGFICDYELHELFKEAnmplpGYKV-REIIQKLMVD-GDRNkdGKISFNEFV 78
Cdd:cd16182    70 DLKKWQAIFKKFDTDRSGTLSSYELRKALESA-----GFHLsNKVLQALVLRyADST--GRITFEDFV 130
PTZ00183 PTZ00183
centrin; Provisional
 7-80 5.30e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.83  E-value: 5.30e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907202322   7 TQISKDELDELKEAFAKVDLNSNGFICDYElhelFKEANMPLPGYKVREIIQKLMVDGDRNKDGKISFNEFVYI 80
Cdd:PTZ00183    9 PGLTEDQKKEIREAFDLFDTDGSGTIDPKE----LKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDI 78
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 16-78 6.09e-04

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 41.05  E-value: 6.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907202322  16 ELKEAFAKVDLNSNGFICDYELHELFKEANMPLpGYKVreiIQKLMVDGDRNKDGKISFNEFV 78
Cdd:cd16185     1 ELRQWFRAVDRDRSGSIDVNELQKALAGGGLLF-SLAT---AEKLIRMFDRDGNGTIDFEEFA 59
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 125-235 6.52e-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: 39.91  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKALENdpdCRhvipmNPNTDDLFKAVGDGIVLCKMINlsvpDTIDERAINKKKLTPFIIQENLNLALNSA 204
Cdd:cd21231     7 QKKTFTKWINAQFAK---FG-----KPPIEDLFTDLQDGRRLLELLE----GLTGQKLVKEKGSTRVHALNNVNKALQVL 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907202322 205 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21231    75 QKNNVDLVNIGSADIVDGNHKLTLGLIWSII 105
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 408-513 6.75e-04

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: 40.34  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNS-----------LGVNPHVNHLYADLQDALVILQLYErIKVP--VDWSKVNKPpypKLGAnMKKLENCNY 474
Cdd:cd21292    25 EKVAFVNWINKnlgddpdckhlLPMDPNTDDLFEKVKDGILLCKMIN-LSVPdtIDERAINKK---KLTV-FTIHENLTL 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907202322 475 AVelgkNPAKF---SLVGIGGQDLNDGNPTLTLAVVWQLMRR 513
Cdd:cd21292   100 AL----NSASAigcNVVNIGAEDLKEGKPHLVLGLLWQIIRI 137
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 519-631 7.93e-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: 7.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 519 LEDLGegQKANDDIIVNWVNRTLSEAGKStSIQSFKDKtISSSLAVVDLIDAIQP-----GCINYDLVKSGnLTEDDKHN 593
Cdd:cd21328     8 LEDLM--KLSPEELLLRWANFHLENAGWQ-KINNFSSD-IKDSRAYFHLLNQIAPkgqkeGEPRIDINMSG-FNEKDDLK 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907202322 594 NAKYAVSMARRIGARVYALPEDLVEVKPKMVMTVFACL 631
Cdd:cd21328    83 RAEYMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANL 120
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 125-235 9.65e-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: 9.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKALENdPDCRhvipmnpnTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFiiqENLNLALNSA 204
Cdd:cd21317    32 QKKTFTKWVNSHLAR-VTCR--------IGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKGRMRIHCL---ENVDKALQFL 99

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907202322 205 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21317   100 KEQKVHLENMGSHDIVDGNHRLTLGLIWTII 130
EFh_PRIP cd16206
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ...
 17-84 1.07e-03

EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); This family represents a class of metazoan phospholipase C related, but catalytically inactive proteins (PRIP), which belong to a group of novel inositol 1,4,5-trisphosphate (InsP3) binding protein. PRIP has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP do not have PLC enzymatic activity. PRIP consists of two subfamilies, PRIP-1(also known as p130 or PLC-L1), which is predominantly expressed in the brain, and PRIP-2 (also known as PLC-L2), which exhibits a relatively ubiquitous expression. Experiments show both, PRIP-1 and PRIP-2, are involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. In addition, PRIP-2 acts as a negative regulator of B-cell receptor signaling and immune responses.


Pssm-ID: 320036 [Multi-domain]  Cd Length: 143  Bit Score: 39.89  E-value: 1.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  17 LKEAFAKVDLNSNGFICDYELHELFKEANmplPGYKVREIIQKL--MVDGDRNKDGKISFNEFVYIFQEV 84
Cdd:cd16206     2 LESVFEEADTNKSGFLDEEEAVQLIKQLN---PGLSTSRIKQKLkeLQKKKDGARGRVSSDEFVELFKEL 68
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 57-84 1.26e-03

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: 36.59  E-value: 1.26e-03
                           10        20
                   ....*....|....*....|....*...
gi 1907202322   57 IQKLMVDGDRNKDGKISFNEFVYIFQEV 84
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_PEF_CAPN13_14 cd16195
Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and ...
 12-104 1.32e-03

Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and similar proteins; CAPN13, also termed calcium-activated neutral proteinase 13 (CANP 13), a 63.6 kDa calpain large subunit that exhibits a restricted tissue distribution with low levels of expression detected only in human testis and lung. In calpain family, CAPN13 is most closely related to calpain-14 (CAPN14). CAPN14, also termed calcium-activated neutral proteinase 14 (CANP 14), is a 76.7 kDa calpain large subunit that is most highly expressed in the oesophagus. Its expression and calpain activity can be induced by IL-13. Both CAPN13 and CAPN14 contain a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain.


Pssm-ID: 320070 [Multi-domain]  Cd Length: 168  Bit Score: 39.88  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  12 DELDELKEAFAKVDLNSNGFICDYELHELFKEAnmplpGYKVREIIQKLMVDGDRNKDGKISFNEFVYIFQEVKSsdIAK 91
Cdd:cd16195    70 KKLRKYKDIFQKADVSKSGFLSLSELRNAIQAA-----GIRVSDDLLNLMALRYGDSSGRISFESFICLMLRLEC--MAK 142

                          90
                  ....*....|...
gi 1907202322  92 TFRKAINRKEGIC 104
Cdd:cd16195   143 IFRNLSKDGGGIY 155
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 408-512 1.32e-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: 39.66  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 408 EERTFRNWMNS-----------LGVNPHVNHLYADLQDALVILQLYErIKVP--VDWSKVNKPpypKLGANMKKlENCNY 474
Cdd:cd21325    25 EKYAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMIN-LSVPdtIDERAINKK---KLTPFIIQ-ENLNL 99

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907202322 475 AVElGKNPAKFSLVGIGGQDLNDGNPTLTLAVVWQLMR 512
Cdd:cd21325   100 ALN-SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 136
CH_AtFIM_like_rpt4 cd21302
fourth calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 273-384 1.47e-03

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: 38.69  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 273 LLRWANFHLENSGWQ-KINNFSadiklidfSNSVKDSKAYFHLLNQIapkgqkegEPR-IDINMSGFNETDDLKR--AES 348
Cdd:cd21302     7 ILSWANRKVRTMGRKsQIESFK--------DKSLSSGLFFLELLWAV--------EPRvVNWNLVTKGETDEEKRlnATY 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907202322 349 MLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFN 384
Cdd:cd21302    71 IISVARKLGCSIFLLPEDIVEVNQKMILILTASIMY 106
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 125-236 1.59e-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: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKalendpdcrhvIPMNPNTDDLFKAVGDGIVLCKMI-NLSVPdtIDERAINK----------KKLtpfii 193
Cdd:cd21330    14 EERTFRNWMNS-----------LGVNPRVNHLYSDLSDALVIFQLYeKIKVP--VDWNRVNKppypklgenmKKL----- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907202322 194 qENLNLALN-SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 236
Cdd:cd21330    76 -ENCNYAVElGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMR 118
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
 152-208 1.96e-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: 1.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907202322 152 NTDDLFKAVGDGIVLCKMINLSVPDTIdeRAINKKKLtPFIIQENLNLALNSASAIG 208
Cdd:cd21210    18 AQGDLLDALKDGVVLCKLANRILPADI--RKYKESKM-PFVQMENISAFLNAARKLG 71
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 508-571 2.38e-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: 40.95  E-value: 2.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907202322 508 WQLMRRYTLNVLEDLGEGQKANDDIIVNWVNRTLSEagkstsIQSFKDK----TISSSLAVVDLIDAI 571
Cdd:cd20664    60 WKEMRRFTLTTLRDFGMGKKTSEDKILEEIPYLIEV------FEKHKGKpfetTLSMNVAVSNIIASI 121
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 531-631 2.60e-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: 37.70  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 531 DIIVNWVNRTLSEAGKSTS---IQSFKDKTIsssLAvvDLIDAIQPGCINYDLVKSgnLTEDDKHNNAKYAVSMARRIGA 607
Cdd:cd00014     2 EELLKWINEVLGEELPVSItdlFESLRDGVL---LC--KLINKLSPGSIPKINKKP--KSPFKKRENINLFLNACKKLGL 74

                          90       100
                  ....*....|....*....|....*..
gi 1907202322 608 RVYAL--PEDLVEVK-PKMVMTVFACL 631
Cdd:cd00014    75 PELDLfePEDLYEKGnLKKVLGTLWAL 101
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 126-180 2.61e-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: 2.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907202322 126 KYAFVNWINKALENDpdcrhvIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 180
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 ...
 152-208 2.92e-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: 2.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907202322 152 NTDDLFKAVGDGIVLCKMINLSVPDTIdeRAINKKKlTPFIIQENLNLALNSASAIG 208
Cdd:cd21208    18 PSDDFRESLEDGILLCELINAIKPGSI--KKINRLP-TPIAGLDNLNLFLKACEDLG 71
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 13-78 3.08e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 39.99  E-value: 3.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907202322  13 ELDELKEAFAKVDLNSNGFICDYELHELFKEANMP-LPGYkvreIIQKLMVDGDRNKDGKISFNEFV 78
Cdd:cd16227   120 LLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPhMHPV----LIEQTLRDKDKDNDGFISFQEFL 182
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
 18-78 3.27e-03

Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), calpain-B (CalpB), and similar proteins; The family contains two calpains that have been found in Drosophila, CalpA and CalpB. CalpA, also termed calcium-activated neutral proteinase A (CANP A), or calpain-A catalytic subunit, is a Drosophila calpain homolog specifically expressed in a few neurons in the central nervous system, in scattered endocrine cells in the midgut, and in blood cells. CalpB, also termed calcium-activated neutral proteinase B (CANP B), contains calpain-B catalytic subunit 1 and calpain-B catalytic subunit 2. Both CalpA and CalpB are closely related to that of vertebrate calpains, and they share similar domain architecture, which consists of four domains: the N-terminal domain I, the catalytic domain II carrying the three active site residues, Cys, His and Asn, the Ca2+-regulated phospholipid-binding domain III, and penta-EF-hand Ca2+-binding domain IV. Besides, CalpA and CalpB display some distinguishing structural features that are not found in mammalian typical calpains. CalpA harbors a 76 amino acid long hydrophobic stretch inserted in domain IV, which may be involved in membrane attachment of this enzyme. CalpB has an unusually long N-terminal tail of 224 amino acids, which belongs to the class of intrinsically unstructured proteins (IUP) and may become ordered upon binding to target protein(s). Moreover, they do not need small regulatory subunits for their catalytic activity, and their proteolytic function is not regulated by an intrinsic inhibitor as the Drosophila genome contains neither regulatory subunit nor calpastatin orthologs. As a result, they may exist as a monomer or perhaps as a homo- or heterodimer together with a second large subunit. Furthermore, both CalpA and CalpB are dispensable for viability and fertility and do not share vital functions during Drosophila development. Phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol, and phosphatidic acid can stimulate the activity and the rate of activation of CalpA, but not CalpB. Calpain A modulates Toll responses by limited Cactus/IkappaB proteolysis. CalpB directly interacts with talin, an important component of the focal adhesion complex, and functions as an important modulator in border cell migration within egg chambers, which may act via the digestion of talin. CalpB can be phosphorylated by cAMP-dependent protein kinase (protein kinase A, PKA; EC 2.7.11.11) at Ser240 and Ser845, as well as by mitogen-activated protein kinase (ERK1 and ERK2; EC 2.7.11.24) at Thr747. The activation of the ERK pathway by extracellular signals results in the phosphorylation and activation of calpain B. In Schneider cells (S2), calpain B was mainly in the cytoplasm and upon a rise in Ca2+ the enzyme adhered to intracellular membranes.


Pssm-ID: 320071 [Multi-domain]  Cd Length: 167  Bit Score: 38.72  E-value: 3.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907202322  18 KEAFAKVDLNSNGFICDYELHELFKEAnmplpGYKVREIIQKLMVDGDRNKDGKISFNEFV 78
Cdd:cd16196    74 KRVFKLFDTDGSGSFSSFELRNALNSA-----GFRLSNATLNALVLRYSNKDGRISFDDFI 129
CH_PLS1_rpt4 cd21332
fourth calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 270-385 3.63e-03

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: 37.62  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 270 EELLLRWANFHLENSGWQ-KINNFSadiklidfSNSVKDSKAYFHLLNQIAPKGQKEGEPRIDinmsGFNETDDLKRAES 348
Cdd:cd21332    10 DEIIIKWVNQTLANANKTtSITSFK--------DKSISTSLPVLDLIDAIAPNAIREEMVKRE----DLSDADKLNNAKY 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907202322 349 MLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFNK 385
Cdd:cd21332    78 AISVARKIGARVYALPEDLVEVKPKMVMTVFACLMGK 114
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
 530-631 3.78e-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: 37.64  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 530 DDIIVNWVNRTLSEAGKSTSIQSFKdKTISSSLAVVDLIDAIQPGCinyDLVKSGNLTEDDKHNNAKYAVSMARRIGARV 609
Cdd:cd21295    14 EEILLRWVNYHLERAGCDRRIKNFS-GDIKDSEAYTHLLKQIAPKD---AGVDTSALRESDLLQRAELMLQNADKIGCRK 89

                          90       100
                  ....*....|....*....|..
gi 1907202322 610 YALPEDLVEVKPKMVMTVFACL 631
Cdd:cd21295    90 FVTPKDVVTGNPKLNLAFVANL 111
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 419-512 4.36e-03

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: 37.51  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 419 LGVNPHVNHLYADLQDALVILQLYErIKVP--VDWSKVNkppypklganMKKLENCNYAVE---LGKNPAKF---SLVGI 490
Cdd:cd21293    24 LPIDPSTNDLFDLVKDGVLLCKLIN-VAVPgtIDERAIN----------TKKVLNPWERNEnhtLCLNSAKAigcSVVNI 92

                          90       100
                  ....*....|....*....|..
gi 1907202322 491 GGQDLNDGNPTLTLAVVWQLMR 512
Cdd:cd21293    93 GTQDLAEGRPHLVLGLISQIIK 114
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 12-95 4.86e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 38.28  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322  12 DELDELKEAFAKVDLNSNGFIcdyELHElFKEANMPLpGYKV-REIIQKLMVDGDRNKDGKISFNEFVYIFQEVKSsdIA 90
Cdd:cd16180    64 KYIQDWRRLFRRFDRDRSGSI---DFNE-LQNALSSF-GYRLsPQFVQLLVRKFDRRRRGSISFDDFVEACVTLKR--LT 136


                  ....*
gi 1907202322  91 KTFRK 95
Cdd:cd16180   137 DAFRK 141
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 16-78 5.83e-03

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 38.87  E-value: 5.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907202322  16 ELKEAFAKVDLNSNGFICDYEL----HELFKEANMPLPGYKVREIIQKLMVDGDRNKDGKISFNEFV 78
Cdd:cd15902    91 EFMKIWRKYDTDGSGFIEAKELkgflKDLLLKNKKHVSPPKLDEYTKLILKEFDANKDGKLELDEMA 157
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 19-80 6.55e-03

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 38.87  E-value: 6.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907202322  19 EAFAKVDLNSNGFICDYEL----HELFKEANMPLP-GYKVREIIQKLMVDGDRNKDGKISFNEFVYI 80
Cdd:cd15902     3 EVWMHFDADGNGYIEGKELdsflRELLKALNGKDKtDDEVAEKKKEFMEKYDENEDGKIEIRELANI 69
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 129-234 7.07e-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: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 129 FVNWINKALENDpDCRHVIpmnpntDDLFKAVGDGIVLCKMINLSVPDTIDEraINKKKLTPFIIQENLNLALNSASAIG 208
Cdd:cd21286     5 YTDWANHYLAKS-GHKRLI------KDLQQDIADGVLLAEIIQIIANEKVED--INGCPRSQSQMIENVDVCLSFLAARG 75

                          90       100
                  ....*....|....*....|....*.
gi 1907202322 209 CHVVNIGAEDLRAGKPHLVLGLLWQI 234
Cdd:cd21286    76 VNVQGLSAEEIRNGNLKAILGLFFSL 101
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
 9-83 7.31e-03

EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix.


Pssm-ID: 319997 [Multi-domain]  Cd Length: 101  Bit Score: 36.34  E-value: 7.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907202322   9 ISKDELDELKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIiQKLMVDGDRNKDGKISFNEFVYIFQE 83
Cdd:cd16254    28 LKKKSADDVKKVFHILDKDKSGFIEEDELKFVLKGFSPDGRDLSDKET-KALLAAGDKDGDGKIGIDEFATLVAE 101
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 125-235 8.05e-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: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907202322 125 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFiiqENLNLALNSA 204
Cdd:cd21316    54 QKKTFTKWVNS---------HLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCL---ENVDKALQFL 121

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907202322 205 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 235
Cdd:cd21316   122 KEQRVHLENMGSHDIVDGNHRLTLGLIWTII 152
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 52-84 8.17e-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: 34.30  E-value: 8.17e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907202322  52 KVREIIQKLmvdgDRNKDGKISFNEFVYIFQEV 84
Cdd:pfam00036   1 ELKEIFRLF----DKDGDGKIDFEEFKELLKKL 29
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 16-86 9.82e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 37.51  E-value: 9.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907202322  16 ELKEAFAKVDLNSNGFICDYELHELFKEANmpLPGYKVREIiqKLMVDG-DRNKDGKISFNEFVYIFQEVKS 86
Cdd:cd16180     1 ELRRIFQAVDRDRSGRISAKELQRALSNGD--WTPFSIETV--RLMINMfDRDRSGTINFDEFVGLWKYIQD 68
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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