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Conserved domains on  [gi|1834198951|ref|NP_001262657|]
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cheerio, isoform P [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 175-297 7.64e-83

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: 267.40  E-value: 7.64e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  175 EAERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVA 254
Cdd:cd21311      1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1834198951  255 LKFLQ-DEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMP 297
Cdd:cd21311     81 LKFLEeDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISMP 124
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 298-415 6.96e-80

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


:

Pssm-ID: 409164  Cd Length: 118  Bit Score: 258.94  E-value: 6.96e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  298 MWDGEDDKQLNGSGHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGL 377
Cdd:cd21315      1 MWEGEDDGPDDGKGPTPKQRLLGWIQSKVPDLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAVKNAKEAMDL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1834198951  378 ADDWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPNSKL 415
Cdd:cd21315     81 AEDWLDVPQLIKPEEMVNPKVDELSMMTYLSQFPNAKL 118
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1104-1191 3.44e-32

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 121.56  E-value: 3.44e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1104 KVQAFGPGLERGIVGQPAEFMIDTRGAGQGGLGVTVEGP--CEAAINCRDNGDGTCNVAYLPTEAGDYTVNITFNERHIT 1181
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|
gi 1834198951  1182 GSPFQPLIVP 1191
Cdd:smart00557   83 GSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1297-1387 4.42e-31

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 118.48  E-value: 4.42e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1297 PARCKAYGPGLEKGLTNQKNKFTVETKGAGNGGLSLAIEGPS--EAKMTCTDNRDGSCDVDYLATDPGEYDITIRFADKH 1374
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 1834198951  1375 IPGSPFRVLVEET 1387
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2167-2255 5.98e-31

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 118.09  E-value: 5.98e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  2167 HLVKAGGSGLERGVVGEAAEFNVWTREAGGGSLAISVEGPS--KADIEFKDRKDGSCDVSYKVTEPGEYRVGLKFNDRHI 2244
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|.
gi 1834198951  2245 PDSPFKVYVSP 2255
Cdd:smart00557   82 PGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1973-2062 2.83e-30

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 116.16  E-value: 2.83e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1973 AKKVKVSGTGLKEGQTHADNIFSVDTRNAGFGGLSVSIEGPS--KAEIQCTDKDDGTLNISYKPTEPGYYIVNLKFADHH 2050
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1834198951  2051 VEGSPFTVKVAG 2062
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1792-1879 2.97e-29

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 113.08  E-value: 2.97e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1792 YVTAYGPGLTHGVTGEPANFTISTKGASAGGLTMAVEGPS--KADINYHDNKDGTVSVQYLPTAPGEYQVSVRFGDKHIK 1869
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|
gi 1834198951  1870 GSPYFAKITG 1879
Cdd:smart00557   83 GSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 816-908 2.80e-27

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 107.30  E-value: 2.80e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   816 PELVKASGPGLEKngVTINQPTSFTVDPSKAGNAPLDVVVQDVFGTKLPVELKNNPDGTKKVTYTPTSGVPHTVEVNYGG 895
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|...
gi 1834198951   896 VSTPNSPHRVYVG 908
Cdd:smart00557   79 EHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 427-522 3.57e-27

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 107.30  E-value: 3.57e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   427 PNRVRAYGPGIEPIgpVVGAPANFTVETFSAGKGSVDVDIQGPNGEIEKADVRFNNDKnlTYTVSYIPKSEGSHKVAVKF 506
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDG--TYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*.
gi 1834198951   507 SGRDIPKSPFPVKVEG 522
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 626-719 6.54e-25

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 100.76  E-value: 6.54e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   626 ARKVRASGRGLQatGVRVGDDADFKIYTEGAGEGEPEVRVIGPGGMNQNVMQSKVDGNTYECHYYPTKEGRYVIMVTFAG 705
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....
gi 1834198951   706 QEVAKSPFEVKVGP 719
Cdd:smart00557   79 EHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 527-622 3.16e-24

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 98.83  E-value: 3.16e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   527 ASKVKVTGPGIQPngVTIKKPTFFDILAKDAGRGVPEVIIIDPANHKtsVAAKVRQLENDTWRCEYVTALQGLHSVNVFY 606
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*.
gi 1834198951   607 AGTPIPNSPFPVKVAP 622
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2355-2443 1.29e-23

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 96.90  E-value: 1.29e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  2355 PAAVHASGNGLDEVKTGHKADFIINTCNAGVGTLAVSIDGPS--KVAMDCTEVEEG-YKVRYTPLLPGEHYITVKYNNMH 2431
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1834198951  2432 IVGSPFKVNATG 2443
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2483-2572 3.81e-23

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 95.75  E-value: 3.81e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  2483 ASKVVSKGMGLKKAYIGKQNQFSISATDAGNNILYVGMYGPKGPCEEFHVKHAGHNNYNVQYLVRDRGQYVLLIKWGEEH 2562
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 1834198951  2563 IPGSPFQIDV 2572
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 723-810 1.28e-22

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 94.21  E-value: 1.28e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   723 SSIVAYGPGLSSGVIGYPAAFVVETNG-ETGALGFTVAGPSQ--AEIECHDNGDGSALVKYHPTAVGEYAVHILCDNEDI 799
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDaGGGELEVEVTGPSGkkVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|.
gi 1834198951   800 PKSPFIAQILP 810
Cdd:smart00557   82 PGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1390-1485 2.17e-22

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.44  E-value: 2.17e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1390 PSKVKVYGPGIEHGQVREsvPTFFNVDVGEAGPGRIAVKLTNSEGIPVDnLRVEDKGNCIYAVHYVPPKAGsVLTCQVKF 1469
Cdd:smart00557    1 ASKVKASGPGLEKGVVGE--PAEFTVDTRDAGGGELEVEVTGPSGKKVP-VEVKDNGDGTYTVSYTPTEPG-DYTVTVKF 76

                            90
                    ....*....|....*.
gi 1834198951  1470 SEVEVPCSPFVMTVFP 1485
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1489-1582 3.40e-22

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.05  E-value: 3.40e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1489 PTKVKVKGVNEKKKTpASLPAEFEIDTKQAGQADINVAIKNPKGKAMQPRLEEVSTGTYVVSFVPDECGTYQCSIKYGDK 1568
Cdd:smart00557    1 ASKVKASGPGLEKGV-VGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 1834198951  1569 EIEGSPFKLEAFPT 1582
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2260-2349 4.04e-19

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 84.19  E-value: 4.04e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  2260 AHKLEVQQFPQGNIQADAPYQFMVRKNGA-KGELDAKIVAPSGTDDDCFIQVIDGEMYSVRFYPRENGIHAIHVKFNGVH 2338
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 1834198951  2339 IPDSPFRIKVG 2349
Cdd:smart00557   81 IPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1726-1786 1.81e-17

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 79.57  E-value: 1.81e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834198951  1726 GGNVTAEVRMPSGKVDKPVIQDNRDGTVSVKYDPREEGSHELVVKYNGEPVQGSPFKFHVD 1786
Cdd:smart00557   31 GGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 913-996 1.67e-16

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 76.87  E-value: 1.67e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   913 AAKVQAFGPWLQPGvRPNAATHFNVDAREAGDAELKVKIIHEETKiEVPCRIIDNEDNTYSVEVIPPSKGAYTTTMTYGG 992
Cdd:smart00557    1 ASKVKASGPGLEKG-VVGEPAEFTVDTRDAGGGELEVEVTGPSGK-KVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78


                    ....
gi 1834198951   993 QRVP 996
Cdd:smart00557   79 EHIP 82
Filamin pfam00630
Filamin/ABP280 repeat;
1192-1288 5.28e-14

Filamin/ABP280 repeat;


:

Pssm-ID: 395505  Cd Length: 89  Bit Score: 69.63  E-value: 5.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1192 VPNLKNTRVSGIGIQPhgVIMNAATDFMVDMSKVGsnidsGKLSCAIFDPMGHVLPSKIVQGPtDDIFRIMYTPFEAGRH 1271
Cdd:pfam00630    1 AADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-----GEGEVEVTGPDGSPVPVEVTDNG-DGTYTVSYTPTEPGDY 72

                           90
                   ....*....|....*..
gi 1834198951 1272 TIELMYDNIPVPGSPFV 1288
Cdd:pfam00630   73 TVSVKFNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1601-1677 1.03e-13

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 68.78  E-value: 1.03e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834198951  1601 GSQSHLKVDAREAGDGAVTCKITNKAGSEiVDIDVIE-KDGFFDILYALNDPGDYDINVKFGGKDIPNGSFSIKAVES 1677
Cdd:smart00557   17 GEPAEFTVDTRDAGGGELEVEVTGPSGKK-VPVEVKDnGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1007-1093 1.28e-11

Filamin/ABP280 repeat;


:

Pssm-ID: 395505  Cd Length: 89  Bit Score: 62.69  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1007 VDVSKIKV--DGLEPtAPLNSLQQFRIITHGlPKADLAVTITSPSGNRIKAHIIPTAEG-FLVNFTPTQLGEYLLSICFG 1083
Cdd:pfam00630    2 ADASKVKAsgPGLEP-GVVGKPAEFTVDTRD-AGGEGEVEVTGPDGSPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1834198951 1084 GTPITPRPFR 1093
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2106-2154 3.96e-11

Filamin/ABP280 repeat;


:

Pssm-ID: 395505  Cd Length: 89  Bit Score: 61.54  E-value: 3.96e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1834198951 2106 VTSPSNVTEDAEIQEVEDGLYAVHFVPKELGVHTVSVRYSEMHIPGSPF 2154
Cdd:pfam00630   40 VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
 
Name Accession Description Interval E-value
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 175-297 7.64e-83

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: 267.40  E-value: 7.64e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  175 EAERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVA 254
Cdd:cd21311      1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1834198951  255 LKFLQ-DEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMP 297
Cdd:cd21311     81 LKFLEeDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISMP 124
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 298-415 6.96e-80

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


Pssm-ID: 409164  Cd Length: 118  Bit Score: 258.94  E-value: 6.96e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  298 MWDGEDDKQLNGSGHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGL 377
Cdd:cd21315      1 MWEGEDDGPDDGKGPTPKQRLLGWIQSKVPDLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAVKNAKEAMDL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1834198951  378 ADDWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPNSKL 415
Cdd:cd21315     81 AEDWLDVPQLIKPEEMVNPKVDELSMMTYLSQFPNAKL 118
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1104-1191 3.44e-32

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 121.56  E-value: 3.44e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1104 KVQAFGPGLERGIVGQPAEFMIDTRGAGQGGLGVTVEGP--CEAAINCRDNGDGTCNVAYLPTEAGDYTVNITFNERHIT 1181
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|
gi 1834198951  1182 GSPFQPLIVP 1191
Cdd:smart00557   83 GSPFTVKVGP 92
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
182-410 1.70e-31

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 133.14  E-value: 1.70e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  182 EDAQWKKIQQNTFTRWANEHLKTID-RSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQD 260
Cdd:COG5069      2 EAKKWQKVQKKTFTKWTNEKLISGGqKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  261 EGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMPMWDGEDDKQLNgsghtpkqrLLNWIHAKI----PDLPINNFTN 336
Cdd:COG5069     82 KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGELTKHIN---------LLLWCDEDTggykPEVDTFDFFR 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834198951  337 DWTTGKAVGALVDACAP-GLCPDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELVNPNV-DEQSMMTYLSQY 410
Cdd:COG5069    153 SWRDGLAFSALIHDSRPdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSWY 228
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1297-1387 4.42e-31

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 118.48  E-value: 4.42e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1297 PARCKAYGPGLEKGLTNQKNKFTVETKGAGNGGLSLAIEGPS--EAKMTCTDNRDGSCDVDYLATDPGEYDITIRFADKH 1374
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 1834198951  1375 IPGSPFRVLVEET 1387
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2167-2255 5.98e-31

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 118.09  E-value: 5.98e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  2167 HLVKAGGSGLERGVVGEAAEFNVWTREAGGGSLAISVEGPS--KADIEFKDRKDGSCDVSYKVTEPGEYRVGLKFNDRHI 2244
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|.
gi 1834198951  2245 PDSPFKVYVSP 2255
Cdd:smart00557   82 PGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1973-2062 2.83e-30

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 116.16  E-value: 2.83e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1973 AKKVKVSGTGLKEGQTHADNIFSVDTRNAGFGGLSVSIEGPS--KAEIQCTDKDDGTLNISYKPTEPGYYIVNLKFADHH 2050
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1834198951  2051 VEGSPFTVKVAG 2062
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1792-1879 2.97e-29

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 113.08  E-value: 2.97e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1792 YVTAYGPGLTHGVTGEPANFTISTKGASAGGLTMAVEGPS--KADINYHDNKDGTVSVQYLPTAPGEYQVSVRFGDKHIK 1869
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|
gi 1834198951  1870 GSPYFAKITG 1879
Cdd:smart00557   83 GSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
1100-1185 4.44e-28

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 109.69  E-value: 4.44e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1100 SDSNKVQAFGPGLERGIVGQPAEFMIDTRGAGqGGLGVTVEGP--CEAAINCRDNGDGTCNVAYLPTEAGDYTVNITFNE 1177
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPdgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 1834198951 1178 RHITGSPF 1185
Cdd:pfam00630   81 QHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 816-908 2.80e-27

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 107.30  E-value: 2.80e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   816 PELVKASGPGLEKngVTINQPTSFTVDPSKAGNAPLDVVVQDVFGTKLPVELKNNPDGTKKVTYTPTSGVPHTVEVNYGG 895
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|...
gi 1834198951   896 VSTPNSPHRVYVG 908
Cdd:smart00557   79 EHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 427-522 3.57e-27

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 107.30  E-value: 3.57e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   427 PNRVRAYGPGIEPIgpVVGAPANFTVETFSAGKGSVDVDIQGPNGEIEKADVRFNNDKnlTYTVSYIPKSEGSHKVAVKF 506
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDG--TYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*.
gi 1834198951   507 SGRDIPKSPFPVKVEG 522
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 192-291 5.03e-27

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: 107.02  E-value: 5.03e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   192 NTFTRWANEHL-KTIDRSINNLETDLSDGLRLIALIEVLSQKRMPK-YNKRPTFRSQKLENVSVALKFLQDEGIKIVNID 269
Cdd:smart00033    1 KTLLRWVNSLLaEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 1834198951   270 SSDIVDcKLKLILGLIWTLILH 291
Cdd:smart00033   81 PEDLVE-GPKLILGVIWTLISL 101
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 626-719 6.54e-25

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 100.76  E-value: 6.54e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   626 ARKVRASGRGLQatGVRVGDDADFKIYTEGAGEGEPEVRVIGPGGMNQNVMQSKVDGNTYECHYYPTKEGRYVIMVTFAG 705
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....
gi 1834198951   706 QEVAKSPFEVKVGP 719
Cdd:smart00557   79 EHIPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
1295-1381 9.90e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 100.06  E-value: 9.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1295 CDPARCKAYGPGLEKGLTNQKNKFTVETKGAGnGGLSLAIEGPS--EAKMTCTDNRDGSCDVDYLATDPGEYDITIRFAD 1372
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 1834198951 1373 KHIPGSPFR 1381
Cdd:pfam00630   81 QHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 527-622 3.16e-24

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 98.83  E-value: 3.16e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   527 ASKVKVTGPGIQPngVTIKKPTFFDILAKDAGRGVPEVIIIDPANHKtsVAAKVRQLENDTWRCEYVTALQGLHSVNVFY 606
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*.
gi 1834198951   607 AGTPIPNSPFPVKVAP 622
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
1970-2057 5.02e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 98.13  E-value: 5.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1970 VGDAKKVKVSGTGLKEGQTHADNIFSVDTRNAGfGGLSVSIEGPS--KAEIQCTDKDDGTLNISYKPTEPGYYIVNLKFA 2047
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1834198951 2048 DHHVEGSPFT 2057
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2355-2443 1.29e-23

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 96.90  E-value: 1.29e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  2355 PAAVHASGNGLDEVKTGHKADFIINTCNAGVGTLAVSIDGPS--KVAMDCTEVEEG-YKVRYTPLLPGEHYITVKYNNMH 2431
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1834198951  2432 IVGSPFKVNATG 2443
Cdd:smart00557   81 IPGSPFTVKVGP 92
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 188-294 1.63e-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: 97.36  E-value: 1.63e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  188 KIQQNTFTRWANEHLK--TIDRSINNLETDLSDGLRLIALIEVLSQKrMPKYNKRPTFRSQKLENVSVALKFLQDE-GIK 264
Cdd:pfam00307    1 LELEKELLRWINSHLAeyGPGVRVTNFTTDLRDGLALCALLNKLAPG-LVDKKKLNKSEFDKLENINLALDVAEKKlGVP 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 1834198951  265 IVNIDSSDIVDCKLKLILGLIWTLILHYSI 294
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
Filamin pfam00630
Filamin/ABP280 repeat;
425-516 1.74e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.59  E-value: 1.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  425 TNPNRVRAYGPGIEPigPVVGAPANFTVETFSAGkGSVDVDIQGPNGEIEKADVRFNNDKnlTYTVSYIPKSEGSHKVAV 504
Cdd:pfam00630    2 ADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDG--TYTVSYTPTEPGDYTVSV 76

                           90
                   ....*....|..
gi 1834198951  505 KFSGRDIPKSPF 516
Cdd:pfam00630   77 KFNGQHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2483-2572 3.81e-23

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 95.75  E-value: 3.81e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  2483 ASKVVSKGMGLKKAYIGKQNQFSISATDAGNNILYVGMYGPKGPCEEFHVKHAGHNNYNVQYLVRDRGQYVLLIKWGEEH 2562
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 1834198951  2563 IPGSPFQIDV 2572
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 723-810 1.28e-22

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 94.21  E-value: 1.28e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   723 SSIVAYGPGLSSGVIGYPAAFVVETNG-ETGALGFTVAGPSQ--AEIECHDNGDGSALVKYHPTAVGEYAVHILCDNEDI 799
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDaGGGELEVEVTGPSGkkVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|.
gi 1834198951   800 PKSPFIAQILP 810
Cdd:smart00557   82 PGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1390-1485 2.17e-22

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.44  E-value: 2.17e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1390 PSKVKVYGPGIEHGQVREsvPTFFNVDVGEAGPGRIAVKLTNSEGIPVDnLRVEDKGNCIYAVHYVPPKAGsVLTCQVKF 1469
Cdd:smart00557    1 ASKVKASGPGLEKGVVGE--PAEFTVDTRDAGGGELEVEVTGPSGKKVP-VEVKDNGDGTYTVSYTPTEPG-DYTVTVKF 76

                            90
                    ....*....|....*.
gi 1834198951  1470 SEVEVPCSPFVMTVFP 1485
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1489-1582 3.40e-22

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.05  E-value: 3.40e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1489 PTKVKVKGVNEKKKTpASLPAEFEIDTKQAGQADINVAIKNPKGKAMQPRLEEVSTGTYVVSFVPDECGTYQCSIKYGDK 1568
Cdd:smart00557    1 ASKVKASGPGLEKGV-VGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 1834198951  1569 EIEGSPFKLEAFPT 1582
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2169-2250 3.96e-22

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 92.74  E-value: 3.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 2169 VKAGGSGLERGVVGEAAEFNVWTREAGGGsLAISVEGPS--KADIEFKDRKDGSCDVSYKVTEPGEYRVGLKFNDRHIPD 2246
Cdd:pfam00630    7 VKASGPGLEPGVVGKPAEFTVDTRDAGGE-GEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPG 85


                   ....
gi 1834198951 2247 SPFK 2250
Cdd:pfam00630   86 SPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1793-1873 5.63e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 89.27  E-value: 5.63e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1793 VTAYGPGLTHGVTGEPANFTISTKGASaGGLTMAVEGPS--KADINYHDNKDGTVSVQYLPTAPGEYQVSVRFGDKHIKG 1870
Cdd:pfam00630    7 VKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPG 85


                   ...
gi 1834198951 1871 SPY 1873
Cdd:pfam00630   86 SPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
723-805 7.57e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.19  E-value: 7.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  723 SSIVAYGPGLSSGVIGYPAAFVVETNGETGALGFTVAGPS--QAEIECHDNGDGSALVKYHPTAVGEYAVHILCDNEDIP 800
Cdd:pfam00630    5 SKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIP 84


                   ....*
gi 1834198951  801 KSPFI 805
Cdd:pfam00630   85 GSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
624-714 7.72e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.19  E-value: 7.72e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  624 SDARKVRASGRGLQatGVRVGDDADFKIYTEGAGeGEPEVRVIGPGGMNQNVMQSKVDGNTYECHYYPTKEGRYVIMVTF 703
Cdd:pfam00630    2 ADASKVKASGPGLE--PGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 1834198951  704 AGQEVAKSPFE 714
Cdd:pfam00630   79 NGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
814-902 3.92e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 84.26  E-value: 3.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  814 FHPELVKASGPGLEknGVTINQPTSFTVDPSKAGNaPLDVVVQDVFGTKLPVELKNNPDGTKKVTYTPTSGVPHTVEVNY 893
Cdd:pfam00630    2 ADASKVKASGPGLE--PGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78


                   ....*....
gi 1834198951  894 GGVSTPNSP 902
Cdd:pfam00630   79 NGQHIPGSP 87
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2260-2349 4.04e-19

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 84.19  E-value: 4.04e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  2260 AHKLEVQQFPQGNIQADAPYQFMVRKNGA-KGELDAKIVAPSGTDDDCFIQVIDGEMYSVRFYPRENGIHAIHVKFNGVH 2338
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 1834198951  2339 IPDSPFRIKVG 2349
Cdd:smart00557   81 IPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
524-616 4.76e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 83.88  E-value: 4.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  524 AGDASKVKVTGPGIQPngVTIKKPTFFDILAKDAGrGVPEVIIIDPANHKtsVAAKVRQLENDTWRCEYVTALQGLHSVN 603
Cdd:pfam00630    1 AADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSP--VPVEVTDNGDGTYTVSYTPTEPGDYTVS 75

                           90
                   ....*....|...
gi 1834198951  604 VFYAGTPIPNSPF 616
Cdd:pfam00630   76 VKFNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
2352-2438 8.45e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 83.11  E-value: 8.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 2352 VADPAAVHASGNGLDEVKTGHKADFIINTCNAGvGTLAVSIDGPS--KVAMDCTEVEEG-YKVRYTPLLPGEHYITVKYN 2428
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1834198951 2429 NMHIVGSPFK 2438
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1487-1576 1.44e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 79.64  E-value: 1.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1487 SEPTKVKVKGVNeKKKTPASLPAEFEIDTKQAGQaDINVAIKNPKGKAMQPRLEEVSTGTYVVSFVPDECGTYQCSIKYG 1566
Cdd:pfam00630    2 ADASKVKASGPG-LEPGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1834198951 1567 DKEIEGSPFK 1576
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1726-1786 1.81e-17

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 79.57  E-value: 1.81e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834198951  1726 GGNVTAEVRMPSGKVDKPVIQDNRDGTVSVKYDPREEGSHELVVKYNGEPVQGSPFKFHVD 1786
Cdd:smart00557   31 GGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 913-996 1.67e-16

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 76.87  E-value: 1.67e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   913 AAKVQAFGPWLQPGvRPNAATHFNVDAREAGDAELKVKIIHEETKiEVPCRIIDNEDNTYSVEVIPPSKGAYTTTMTYGG 992
Cdd:smart00557    1 ASKVKASGPGLEKG-VVGEPAEFTVDTRDAGGGELEVEVTGPSGK-KVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78


                    ....
gi 1834198951   993 QRVP 996
Cdd:smart00557   79 EHIP 82
Filamin pfam00630
Filamin/ABP280 repeat;
910-996 9.74e-16

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 74.63  E-value: 9.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  910 PVDAAKVQAFGPWLQPGvRPNAATHFNVDAREAGDaELKVKIIHEETKiEVPCRIIDNEDNTYSVEVIPPSKGAYTTTMT 989
Cdd:pfam00630    1 AADASKVKASGPGLEPG-VVGKPAEFTVDTRDAGG-EGEVEVTGPDGS-PVPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77


                   ....*..
gi 1834198951  990 YGGQRVP 996
Cdd:pfam00630   78 FNGQHIP 84
Filamin pfam00630
Filamin/ABP280 repeat;
1388-1480 1.83e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 73.86  E-value: 1.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1388 VDPSKVKVYGPGIEHGQVreSVPTFFNVDVGEAGpGRIAVKLTNSEGIPVDNlRVEDKGNCIYAVHYVPPKAGsVLTCQV 1467
Cdd:pfam00630    2 ADASKVKASGPGLEPGVV--GKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPV-EVTDNGDGTYTVSYTPTEPG-DYTVSV 76

                           90
                   ....*....|...
gi 1834198951 1468 KFSEVEVPCSPFV 1480
Cdd:pfam00630   77 KFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2257-2345 3.52e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 72.71  E-value: 3.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 2257 AGDAHKLEVQQFPQGNIQADAPYQFMVRKNGAKGELDAKIVAPSGTDDDCFIQVIDGEMYSVRFYPRENGIHAIHVKFNG 2336
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 1834198951 2337 VHIPDSPFR 2345
Cdd:pfam00630   81 QHIPGSPFK 89
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 318-410 1.60e-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: 71.58  E-value: 1.60e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   318 LLNWI---HAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWEL---WDPKDAVQNASEAMGLADDWLNVRQLIKPE 391
Cdd:smart00033    3 LLRWVnslLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVaasLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90
                    ....*....|....*....
gi 1834198951   392 ELVNPNVDEQSMMTYLSQY 410
Cdd:smart00033   83 DLVEGPKLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
2481-2568 1.79e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.78  E-value: 1.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 2481 SDASKVVSKGMGLKKAYIGKQNQFSISATDAGNNILyVGMYGPKGPCEEFHVKHAGHNNYNVQYLVRDRGQYVLLIKWGE 2560
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGE-VEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 1834198951 2561 EHIPGSPF 2568
Cdd:pfam00630   81 QHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
1192-1288 5.28e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 69.63  E-value: 5.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1192 VPNLKNTRVSGIGIQPhgVIMNAATDFMVDMSKVGsnidsGKLSCAIFDPMGHVLPSKIVQGPtDDIFRIMYTPFEAGRH 1271
Cdd:pfam00630    1 AADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-----GEGEVEVTGPDGSPVPVEVTDNG-DGTYTVSYTPTEPGDY 72

                           90
                   ....*....|....*..
gi 1834198951 1272 TIELMYDNIPVPGSPFV 1288
Cdd:pfam00630   73 TVSVKFNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1601-1677 1.03e-13

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 68.78  E-value: 1.03e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834198951  1601 GSQSHLKVDAREAGDGAVTCKITNKAGSEiVDIDVIE-KDGFFDILYALNDPGDYDINVKFGGKDIPNGSFSIKAVES 1677
Cdd:smart00557   17 GEPAEFTVDTRDAGGGELEVEVTGPSGKK-VPVEVKDnGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGPA 93
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 314-410 2.93e-13

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 68.08  E-value: 2.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  314 PKQRLLNWI----HAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWEL-WDPKDAVQNASEAMGLADDWLNVRQ-L 387
Cdd:pfam00307    3 LEKELLRWInshlAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnKSEFDKLENINLALDVAEKKLGVPKvL 82

                           90       100
                   ....*....|....*....|...
gi 1834198951  388 IKPEELVNPnvDEQSMMTYLSQY 410
Cdd:pfam00307   83 IEPEDLVEG--DNKSVLTYLASL 103
Filamin pfam00630
Filamin/ABP280 repeat;
1726-1782 1.73e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 65.39  E-value: 1.73e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1834198951 1726 GGNVTAEVRMPSGKVDKPVIQDNRDGTVSVKYDPREEGSHELVVKYNGEPVQGSPFK 1782
Cdd:pfam00630   33 GGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1007-1093 1.28e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 62.69  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1007 VDVSKIKV--DGLEPtAPLNSLQQFRIITHGlPKADLAVTITSPSGNRIKAHIIPTAEG-FLVNFTPTQLGEYLLSICFG 1083
Cdd:pfam00630    2 ADASKVKAsgPGLEP-GVVGKPAEFTVDTRD-AGGEGEVEVTGPDGSPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1834198951 1084 GTPITPRPFR 1093
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2106-2154 3.96e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 61.54  E-value: 3.96e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1834198951 2106 VTSPSNVTEDAEIQEVEDGLYAVHFVPKELGVHTVSVRYSEMHIPGSPF 2154
Cdd:pfam00630   40 VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1010-1097 4.38e-11

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 61.47  E-value: 4.38e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1010 SKIKVD--GLEPtAPLNSLQQFRIITHGLPKADLAVTITSPSGNRIKAHIIPTAEG-FLVNFTPTQLGEYLLSICFGGTP 1086
Cdd:smart00557    2 SKVKASgpGLEK-GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 1834198951  1087 ITPRPFRLQCL 1097
Cdd:smart00557   81 IPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
1583-1670 1.17e-09

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 57.30  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1583 GEAKKCKLVEQAPKIQTSGSQSHLKVDAREAGdGAVTCKITNKAGSEIvDIDVIE-KDGFFDILYALNDPGDYDINVKFG 1661
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPV-PVEVTDnGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*....
gi 1834198951 1662 GKDIPNGSF 1670
Cdd:pfam00630   80 GQHIPGSPF 88
 
Name Accession Description Interval E-value
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 175-297 7.64e-83

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: 267.40  E-value: 7.64e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  175 EAERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVA 254
Cdd:cd21311      1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1834198951  255 LKFLQ-DEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMP 297
Cdd:cd21311     81 LKFLEeDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISMP 124
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 298-415 6.96e-80

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


Pssm-ID: 409164  Cd Length: 118  Bit Score: 258.94  E-value: 6.96e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  298 MWDGEDDKQLNGSGHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGL 377
Cdd:cd21315      1 MWEGEDDGPDDGKGPTPKQRLLGWIQSKVPDLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAVKNAKEAMDL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1834198951  378 ADDWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPNSKL 415
Cdd:cd21315     81 AEDWLDVPQLIKPEEMVNPKVDELSMMTYLSQFPNAKL 118
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 313-415 1.48e-69

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


Pssm-ID: 409079  Cd Length: 103  Bit Score: 228.81  E-value: 1.48e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEE 392
Cdd:cd21230      1 TPKQRLLGWIQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALENATEAMQLAEDWLGVPQLITPEE 80

                           90       100
                   ....*....|....*....|...
gi 1834198951  393 LVNPNVDEQSMMTYLSQYPNSKL 415
Cdd:cd21230     81 IINPNVDEMSVMTYLSQFPKAKL 103
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 186-292 3.26e-66

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: 219.28  E-value: 3.26e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  186 WKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPK-YNKRPTFRSQKLENVSVALKFLQDEGIK 264
Cdd:cd21228      1 WKKIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkYNKRPTFRQMKLENVSVALEFLERESIK 80

                           90       100
                   ....*....|....*....|....*...
gi 1834198951  265 IVNIDSSDIVDCKLKLILGLIWTLILHY 292
Cdd:cd21228     81 LVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 177-302 7.06e-60

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: 202.23  E-value: 7.06e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  177 ERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRM-PKYNKRPTFRSQKLENVSVAL 255
Cdd:cd21309      5 EKDLAEDAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVAL 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1834198951  256 KFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMPMWDGE 302
Cdd:cd21309     85 EFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISMPVWEDE 131
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 177-297 7.92e-58

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: 196.02  E-value: 7.92e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  177 ERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRM-PKYNKRPTFRSQKLENVSVAL 255
Cdd:cd21310      4 EKDLAEDAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMyRKYHPRPNFRQMKLENVSVAL 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1834198951  256 KFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMP 297
Cdd:cd21310     84 EFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 125
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 171-297 8.48e-57

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: 193.38  E-value: 8.48e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  171 DEDMEA-ERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRM-PKYNKRPTFRSQKL 248
Cdd:cd21308      1 DAEMPAtEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1834198951  249 ENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMP 297
Cdd:cd21308     81 ENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 129
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 300-416 1.06e-56

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


Pssm-ID: 409163  Cd Length: 115  Bit Score: 192.59  E-value: 1.06e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  300 DGEDDKQlngsgHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLAD 379
Cdd:cd21314      3 DEEDARK-----QTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPVQNAREAMQQAD 77

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1834198951  380 DWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPNSKLK 416
Cdd:cd21314     78 DWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLK 114
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
 308-415 1.22e-52

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


Pssm-ID: 409162  Cd Length: 110  Bit Score: 180.67  E-value: 1.22e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  308 NGSGHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLADDWLNVRQL 387
Cdd:cd21313      3 DAKKQTPKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPQKPVDNAREAMQQADDWLGVPQV 82

                           90       100
                   ....*....|....*....|....*...
gi 1834198951  388 IKPEELVNPNVDEQSMMTYLSQYPNSKL 415
Cdd:cd21313     83 ITPEEIIHPDVDEHSVMTYLSQFPKAKL 110
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 186-292 3.73e-51

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: 176.13  E-value: 3.73e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  186 WKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRM-PKYNKRPTFRSQKLENVSVALKFLQDEGIK 264
Cdd:cd21183      1 WKRIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLkRSYNRRPAFQQHYLENVSTALKFIEADHIK 80

                           90       100
                   ....*....|....*....|....*...
gi 1834198951  265 IVNIDSSDIVDCKLKLILGLIWTLILHY 292
Cdd:cd21183     81 LVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 186-294 5.96e-49

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: 170.16  E-value: 5.96e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  186 WKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKI 265
Cdd:cd21227      1 WVEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKL 80

                           90       100
                   ....*....|....*....|....*....
gi 1834198951  266 VNIDSSDIVDCKLKLILGLIWTLILHYSI 294
Cdd:cd21227     81 VNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 300-415 8.13e-49

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


Pssm-ID: 409161  Cd Length: 114  Bit Score: 169.99  E-value: 8.13e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  300 DGEDDKQlnGSGHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLAD 379
Cdd:cd21312      1 DEEEDEE--AKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQAD 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1834198951  380 DWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPNSKL 415
Cdd:cd21312     79 DWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKL 114
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 186-292 4.74e-47

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: 164.50  E-value: 4.74e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  186 WKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKI 265
Cdd:cd21215      1 WVDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKL 80

                           90       100
                   ....*....|....*....|....*..
gi 1834198951  266 VNIDSSDIVDCKLKLILGLIWTLILHY 292
Cdd:cd21215     81 TNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 313-414 1.90e-45

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: 159.71  E-value: 1.90e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEE 392
Cdd:cd21184      1 SGKSLLLEWVNSKIPEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMDIAEEELGIPKIITPED 80

                           90       100
                   ....*....|....*....|..
gi 1834198951  393 LVNPNVDEQSMMTYLSQYPNSK 414
Cdd:cd21184     81 MVSPNVDELSVMTYLSYFRNAK 102
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 188-292 1.85e-36

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: 134.07  E-value: 1.85e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  188 KIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRptFRSQKLENVSVALKFLQDEGIKIVN 267
Cdd:cd21188      2 AVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGR--MRFHRLQNVQTALDFLKYRKIKLVN 79

                           90       100
                   ....*....|....*....|....*
gi 1834198951  268 IDSSDIVDCKLKLILGLIWTLILHY 292
Cdd:cd21188     80 IRAEDIVDGNPKLTLGLIWTIILHF 104
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 185-290 1.05e-34

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: 129.05  E-value: 1.05e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  185 QWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKyNKRPTFRSQKLENVSVALKFLQDEGIK 264
Cdd:cd21214      1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPK-PERGKMRFHKIANVNKALDFIASKGVK 79

                           90       100
                   ....*....|....*....|....*.
gi 1834198951  265 IVNIDSSDIVDCKLKLILGLIWTLIL 290
Cdd:cd21214     80 LVSIGAEEIVDGNLKMTLGMIWTIIL 105
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 314-410 7.01e-33

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409078  Cd Length: 105  Bit Score: 124.04  E-value: 7.01e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  314 PKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEEL 393
Cdd:cd21229      4 PKKLMLAWLQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPEDL 83

                           90
                   ....*....|....*..
gi 1834198951  394 VNPNVDEQSMMTYLSQY 410
Cdd:cd21229     84 SSPHLDELSGMTYLSYF 100
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1104-1191 3.44e-32

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 121.56  E-value: 3.44e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1104 KVQAFGPGLERGIVGQPAEFMIDTRGAGQGGLGVTVEGP--CEAAINCRDNGDGTCNVAYLPTEAGDYTVNITFNERHIT 1181
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|
gi 1834198951  1182 GSPFQPLIVP 1191
Cdd:smart00557   83 GSPFTVKVGP 92
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
182-410 1.70e-31

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 133.14  E-value: 1.70e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  182 EDAQWKKIQQNTFTRWANEHLKTID-RSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQD 260
Cdd:COG5069      2 EAKKWQKVQKKTFTKWTNEKLISGGqKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  261 EGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMPMWDGEDDKQLNgsghtpkqrLLNWIHAKI----PDLPINNFTN 336
Cdd:COG5069     82 KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGELTKHIN---------LLLWCDEDTggykPEVDTFDFFR 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834198951  337 DWTTGKAVGALVDACAP-GLCPDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELVNPNV-DEQSMMTYLSQY 410
Cdd:COG5069    153 SWRDGLAFSALIHDSRPdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSWY 228
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1297-1387 4.42e-31

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 118.48  E-value: 4.42e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1297 PARCKAYGPGLEKGLTNQKNKFTVETKGAGNGGLSLAIEGPS--EAKMTCTDNRDGSCDVDYLATDPGEYDITIRFADKH 1374
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 1834198951  1375 IPGSPFRVLVEET 1387
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2167-2255 5.98e-31

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 118.09  E-value: 5.98e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  2167 HLVKAGGSGLERGVVGEAAEFNVWTREAGGGSLAISVEGPS--KADIEFKDRKDGSCDVSYKVTEPGEYRVGLKFNDRHI 2244
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|.
gi 1834198951  2245 PDSPFKVYVSP 2255
Cdd:smart00557   82 PGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1973-2062 2.83e-30

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 116.16  E-value: 2.83e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1973 AKKVKVSGTGLKEGQTHADNIFSVDTRNAGFGGLSVSIEGPS--KAEIQCTDKDDGTLNISYKPTEPGYYIVNLKFADHH 2050
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1834198951  2051 VEGSPFTVKVAG 2062
Cdd:smart00557   81 IPGSPFTVKVGP 92
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 166-290 3.62e-30

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: 116.63  E-value: 3.62e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  166 YEENFDEDMEAERdlaedaqwKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNkRPTFRS 245
Cdd:cd21193      1 FEKGRIRALQEER--------INIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPN-RGRLRV 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1834198951  246 QKLENVSVALKFLQDEgIKIVNIDSSDIVDCKLKLILGLIWTLIL 290
Cdd:cd21193     72 QKIENVNKALAFLKTK-VRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 188-294 5.82e-30

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: 115.93  E-value: 5.82e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  188 KIQQNTFTRWANEHLKTIDR--SINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKI 265
Cdd:cd21241      4 RVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKKIKL 83

                           90       100
                   ....*....|....*....|....*....
gi 1834198951  266 VNIDSSDIVDCKLKLILGLIWTLILHYSI 294
Cdd:cd21241     84 VNINPTDIVDGKPSIVLGLIWTIILYFQI 112
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 188-304 6.97e-30

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: 115.89  E-value: 6.97e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  188 KIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRptFRSQKLENVSVALKFLQDEGIKIVN 267
Cdd:cd21235      5 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 82

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1834198951  268 IDSSDIVDCKLKLILGLIWTLILHYSISMPMWDGEDD 304
Cdd:cd21235     83 IRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 189-292 2.96e-29

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: 113.63  E-value: 2.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  189 IQQNTFTRWANEHLKTIDRS-INNLETDLSDGLRLIALIEVLSQKRMPKynKRPTFRSQKLENVSVALKFLQDEGIKIVN 267
Cdd:cd21186      2 VQKKTFTKWINSQLSKANKPpIKDLFEDLRDGTRLLALLEVLTGKKLKP--EKGRMRVHHLNNVNRALQVLEQNNVKLVN 79

                           90       100
                   ....*....|....*....|....*
gi 1834198951  268 IDSSDIVDCKLKLILGLIWTLILHY 292
Cdd:cd21186     80 ISSNDIVDGNPKLTLGLVWSIILHW 104
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1792-1879 2.97e-29

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 113.08  E-value: 2.97e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1792 YVTAYGPGLTHGVTGEPANFTISTKGASAGGLTMAVEGPS--KADINYHDNKDGTVSVQYLPTAPGEYQVSVRFGDKHIK 1869
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|
gi 1834198951  1870 GSPYFAKITG 1879
Cdd:smart00557   83 GSPFTVKVGP 92
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 165-295 3.18e-29

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: 114.31  E-value: 3.18e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  165 QYEENFDEDMEAERDlaedaqwkKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRptFR 244
Cdd:cd21236      1 QAYENVLERYKDERD--------KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGR--MR 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1834198951  245 SQKLENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSIS 295
Cdd:cd21236     71 FHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 121
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 187-294 6.85e-29

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: 113.05  E-value: 6.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  187 KKIQQNTFTRWANEHL--KTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIK 264
Cdd:cd21190      3 ERVQKKTFTNWINSHLakLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIK 82

                           90       100       110
                   ....*....|....*....|....*....|
gi 1834198951  265 IVNIDSSDIVDCKLKLILGLIWTLILHYSI 294
Cdd:cd21190     83 LVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 180-290 1.66e-28

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: 112.08  E-value: 1.66e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  180 LAEDAQwkKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNkRPTFRSQKLENVSVALKFLQ 259
Cdd:cd21246      9 LADERE--AVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPT-KGKMRIHCLENVDKALQFLK 85

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1834198951  260 DEGIKIVNIDSSDIVDCKLKLILGLIWTLIL 290
Cdd:cd21246     86 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
Filamin pfam00630
Filamin/ABP280 repeat;
1100-1185 4.44e-28

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 109.69  E-value: 4.44e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1100 SDSNKVQAFGPGLERGIVGQPAEFMIDTRGAGqGGLGVTVEGP--CEAAINCRDNGDGTCNVAYLPTEAGDYTVNITFNE 1177
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPdgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 1834198951 1178 RHITGSPF 1185
Cdd:pfam00630   81 QHIPGSPF 88
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 188-302 1.23e-27

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: 109.35  E-value: 1.23e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  188 KIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRptFRSQKLENVSVALKFLQDEGIKIVN 267
Cdd:cd21237      5 RVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGR--MRFHRLQNVQIALDFLKQRQVKLVN 82

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1834198951  268 IDSSDIVDCKLKLILGLIWTLILHYSISMPMWDGE 302
Cdd:cd21237     83 IRNDDITDGNPKLTLGLIWTIILHFQISDIYISGE 117
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 816-908 2.80e-27

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 107.30  E-value: 2.80e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   816 PELVKASGPGLEKngVTINQPTSFTVDPSKAGNAPLDVVVQDVFGTKLPVELKNNPDGTKKVTYTPTSGVPHTVEVNYGG 895
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|...
gi 1834198951   896 VSTPNSPHRVYVG 908
Cdd:smart00557   79 EHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 427-522 3.57e-27

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 107.30  E-value: 3.57e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   427 PNRVRAYGPGIEPIgpVVGAPANFTVETFSAGKGSVDVDIQGPNGEIEKADVRFNNDKnlTYTVSYIPKSEGSHKVAVKF 506
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDG--TYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*.
gi 1834198951   507 SGRDIPKSPFPVKVEG 522
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 192-291 5.03e-27

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: 107.02  E-value: 5.03e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   192 NTFTRWANEHL-KTIDRSINNLETDLSDGLRLIALIEVLSQKRMPK-YNKRPTFRSQKLENVSVALKFLQDEGIKIVNID 269
Cdd:smart00033    1 KTLLRWVNSLLaEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 1834198951   270 SSDIVDcKLKLILGLIWTLILH 291
Cdd:smart00033   81 PEDLVE-GPKLILGVIWTLISL 101
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 194-292 7.87e-27

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: 106.51  E-value: 7.87e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  194 FTRWANEHLK--TIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKIVNIDSS 271
Cdd:cd21212      5 YTDWANHYLEkgGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQGITAE 84

                           90       100
                   ....*....|....*....|.
gi 1834198951  272 DIVDCKLKLILGLIWTLILHY 292
Cdd:cd21212     85 DIVDGNLKAILGLFFSLSRYK 105
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 167-290 3.27e-25

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: 103.21  E-value: 3.27e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  167 EENFDEDMEAERdLAEDAQWKK-------IQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNK 239
Cdd:cd21317      3 DDDWDNDNSSAR-LFERSRIKAladereaVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTK 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1834198951  240 rPTFRSQKLENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLIL 290
Cdd:cd21317     82 -GRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 626-719 6.54e-25

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 100.76  E-value: 6.54e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   626 ARKVRASGRGLQatGVRVGDDADFKIYTEGAGEGEPEVRVIGPGGMNQNVMQSKVDGNTYECHYYPTKEGRYVIMVTFAG 705
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....
gi 1834198951   706 QEVAKSPFEVKVGP 719
Cdd:smart00557   79 EHIPGSPFTVKVGP 92
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 189-294 6.95e-25

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: 101.45  E-value: 6.95e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  189 IQQNTFTRWANEHL--KTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFrsQKLENVSVALKFLQDEGIKIV 266
Cdd:cd21242      5 TQKRTFTNWINSQLakHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVF--QCRSNIETALSFLKNKSIKLI 82

                           90       100
                   ....*....|....*....|....*...
gi 1834198951  267 NIDSSDIVDCKLKLILGLIWTLILHYSI 294
Cdd:cd21242     83 NIHVPDIIEGKPSIILGLIWTIILHFHI 110
Filamin pfam00630
Filamin/ABP280 repeat;
1295-1381 9.90e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 100.06  E-value: 9.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1295 CDPARCKAYGPGLEKGLTNQKNKFTVETKGAGnGGLSLAIEGPS--EAKMTCTDNRDGSCDVDYLATDPGEYDITIRFAD 1372
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 1834198951 1373 KHIPGSPFR 1381
Cdd:pfam00630   81 QHIPGSPFK 89
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 189-290 1.01e-24

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: 102.03  E-value: 1.01e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  189 IQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKyNKRPTFRSQKLENVSVALKFLQDEGIKIVNI 268
Cdd:cd21318     38 VQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPK-PTRGRMRIHSLENVDKALQFLKEQRVHLENV 116

                           90       100
                   ....*....|....*....|..
gi 1834198951  269 DSSDIVDCKLKLILGLIWTLIL 290
Cdd:cd21318    117 GSHDIVDGNHRLTLGLIWTIIL 138
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 527-622 3.16e-24

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 98.83  E-value: 3.16e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   527 ASKVKVTGPGIQPngVTIKKPTFFDILAKDAGRGVPEVIIIDPANHKtsVAAKVRQLENDTWRCEYVTALQGLHSVNVFY 606
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*.
gi 1834198951   607 AGTPIPNSPFPVKVAP 622
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
1970-2057 5.02e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 98.13  E-value: 5.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1970 VGDAKKVKVSGTGLKEGQTHADNIFSVDTRNAGfGGLSVSIEGPS--KAEIQCTDKDDGTLNISYKPTEPGYYIVNLKFA 2047
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1834198951 2048 DHHVEGSPFT 2057
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2355-2443 1.29e-23

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 96.90  E-value: 1.29e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  2355 PAAVHASGNGLDEVKTGHKADFIINTCNAGVGTLAVSIDGPS--KVAMDCTEVEEG-YKVRYTPLLPGEHYITVKYNNMH 2431
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1834198951  2432 IVGSPFKVNATG 2443
Cdd:smart00557   81 IPGSPFTVKVGP 92
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 186-293 1.34e-23

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: 97.60  E-value: 1.34e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  186 WKKIQQNTFTRWANEHL-KTIDRSINNLETDLSDGLRLIALIEVLSQKRMP-KYNKRPTFRSQKLENVSVALKFLQDE-G 262
Cdd:cd21225      1 WEKVQIKAFTAWVNSVLeKRGIPKISDLATDLSDGVRLIFFLELVSGKKFPkKFDLEPKNRIQMIQNLHLAMLFIEEDlK 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1834198951  263 IKIVNIDSSDIVDCKLKLILGLIWTLILHYS 293
Cdd:cd21225     81 IRVQGIGAEDFVDNNKKLILGLLWTLYRKYR 111
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 189-294 1.39e-23

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: 97.69  E-value: 1.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  189 IQQNTFTRWANEHL-KTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKynKRPTFRSQKLENVSVALKFLQDEGIKIVN 267
Cdd:cd21231      6 VQKKTFTKWINAQFaKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVK--EKGSTRVHALNNVNKALQVLQKNNVDLVN 83

                           90       100
                   ....*....|....*....|....*..
gi 1834198951  268 IDSSDIVDCKLKLILGLIWTLILHYSI 294
Cdd:cd21231     84 IGSADIVDGNHKLTLGLIWSIILHWQV 110
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 188-294 1.63e-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: 97.36  E-value: 1.63e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  188 KIQQNTFTRWANEHLK--TIDRSINNLETDLSDGLRLIALIEVLSQKrMPKYNKRPTFRSQKLENVSVALKFLQDE-GIK 264
Cdd:pfam00307    1 LELEKELLRWINSHLAeyGPGVRVTNFTTDLRDGLALCALLNKLAPG-LVDKKKLNKSEFDKLENINLALDVAEKKlGVP 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 1834198951  265 IVNIDSSDIVDCKLKLILGLIWTLILHYSI 294
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
Filamin pfam00630
Filamin/ABP280 repeat;
425-516 1.74e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.59  E-value: 1.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  425 TNPNRVRAYGPGIEPigPVVGAPANFTVETFSAGkGSVDVDIQGPNGEIEKADVRFNNDKnlTYTVSYIPKSEGSHKVAV 504
Cdd:pfam00630    2 ADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDG--TYTVSYTPTEPGDYTVSV 76

                           90
                   ....*....|..
gi 1834198951  505 KFSGRDIPKSPF 516
Cdd:pfam00630   77 KFNGQHIPGSPF 88
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 139-290 3.66e-23

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: 98.19  E-value: 3.66e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  139 AAHYDvcHQQTNDYYQPARQEGQQADQYEENFDEDM-EAERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLS 217
Cdd:cd21316      4 ATDFD--NIDIQQQYSDVNNRWDVDEWDNENSSARLfERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLR 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834198951  218 DGLRLIALIEVLSQKRMPKYNKrPTFRSQKLENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLIL 290
Cdd:cd21316     82 DGRMLIKLLEVLSGERLPKPTK-GRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2483-2572 3.81e-23

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 95.75  E-value: 3.81e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  2483 ASKVVSKGMGLKKAYIGKQNQFSISATDAGNNILYVGMYGPKGPCEEFHVKHAGHNNYNVQYLVRDRGQYVLLIKWGEEH 2562
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 1834198951  2563 IPGSPFQIDV 2572
Cdd:smart00557   81 IPGSPFTVKV 90
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 189-294 4.28e-23

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: 96.49  E-value: 4.28e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  189 IQQNTFTRWANEHLKTIDR--SINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKIV 266
Cdd:cd21191      5 VQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSNVKLV 84

                           90       100
                   ....*....|....*....|....*...
gi 1834198951  267 NIDSSDIVDCKLKLILGLIWTLILHYSI 294
Cdd:cd21191     85 SIDAAEIADGNPSLVLGLIWNIILFFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 723-810 1.28e-22

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 94.21  E-value: 1.28e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   723 SSIVAYGPGLSSGVIGYPAAFVVETNG-ETGALGFTVAGPSQ--AEIECHDNGDGSALVKYHPTAVGEYAVHILCDNEDI 799
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDaGGGELEVEVTGPSGkkVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|.
gi 1834198951   800 PKSPFIAQILP 810
Cdd:smart00557   82 PGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1390-1485 2.17e-22

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.44  E-value: 2.17e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1390 PSKVKVYGPGIEHGQVREsvPTFFNVDVGEAGPGRIAVKLTNSEGIPVDnLRVEDKGNCIYAVHYVPPKAGsVLTCQVKF 1469
Cdd:smart00557    1 ASKVKASGPGLEKGVVGE--PAEFTVDTRDAGGGELEVEVTGPSGKKVP-VEVKDNGDGTYTVSYTPTEPG-DYTVTVKF 76

                            90
                    ....*....|....*.
gi 1834198951  1470 SEVEVPCSPFVMTVFP 1485
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1489-1582 3.40e-22

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.05  E-value: 3.40e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1489 PTKVKVKGVNEKKKTpASLPAEFEIDTKQAGQADINVAIKNPKGKAMQPRLEEVSTGTYVVSFVPDECGTYQCSIKYGDK 1568
Cdd:smart00557    1 ASKVKASGPGLEKGV-VGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 1834198951  1569 EIEGSPFKLEAFPT 1582
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2169-2250 3.96e-22

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 92.74  E-value: 3.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 2169 VKAGGSGLERGVVGEAAEFNVWTREAGGGsLAISVEGPS--KADIEFKDRKDGSCDVSYKVTEPGEYRVGLKFNDRHIPD 2246
Cdd:pfam00630    7 VKASGPGLEPGVVGKPAEFTVDTRDAGGE-GEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPG 85


                   ....
gi 1834198951 2247 SPFK 2250
Cdd:pfam00630   86 SPFK 89
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 191-290 1.94e-21

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: 91.25  E-value: 1.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  191 QNTFTRWANEHLK-TIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGI-KIVNI 268
Cdd:cd00014      1 EEELLKWINEVLGeELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLpELDLF 80

                           90       100
                   ....*....|....*....|...
gi 1834198951  269 DSSDIVDCK-LKLILGLIWTLIL 290
Cdd:cd00014     81 EPEDLYEKGnLKKVLGTLWALAL 103
Filamin pfam00630
Filamin/ABP280 repeat;
1793-1873 5.63e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 89.27  E-value: 5.63e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1793 VTAYGPGLTHGVTGEPANFTISTKGASaGGLTMAVEGPS--KADINYHDNKDGTVSVQYLPTAPGEYQVSVRFGDKHIKG 1870
Cdd:pfam00630    7 VKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPG 85


                   ...
gi 1834198951 1871 SPY 1873
Cdd:pfam00630   86 SPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
723-805 7.57e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.19  E-value: 7.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  723 SSIVAYGPGLSSGVIGYPAAFVVETNGETGALGFTVAGPS--QAEIECHDNGDGSALVKYHPTAVGEYAVHILCDNEDIP 800
Cdd:pfam00630    5 SKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIP 84


                   ....*
gi 1834198951  801 KSPFI 805
Cdd:pfam00630   85 GSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
624-714 7.72e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.19  E-value: 7.72e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  624 SDARKVRASGRGLQatGVRVGDDADFKIYTEGAGeGEPEVRVIGPGGMNQNVMQSKVDGNTYECHYYPTKEGRYVIMVTF 703
Cdd:pfam00630    2 ADASKVKASGPGLE--PGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 1834198951  704 AGQEVAKSPFE 714
Cdd:pfam00630   79 NGQHIPGSPFK 89
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 189-294 1.31e-19

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: 86.22  E-value: 1.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  189 IQQNTFTRWANEHL-KTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKynKRPTFRSQKLENVSVALKFLQDEGIKIVN 267
Cdd:cd21232      2 VQKKTFTKWINARFsKSGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPK--ERGSTRVHALNNVNRVLQVLHQNNVELVN 79

                           90       100
                   ....*....|....*....|....*..
gi 1834198951  268 IDSSDIVDCKLKLILGLIWTLILHYSI 294
Cdd:cd21232     80 IGGTDIVDGNHKLTLGLLWSIILHWQV 106
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 319-410 1.53e-19

third 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 third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409034  Cd Length: 98  Bit Score: 85.43  E-value: 1.53e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  319 LNWIHAKIPDLPINNFTNDWTTGKAVGALVDACApGLCPDWELWDPKDAVQNASEAMGLADDwLNVRQLIKPEELVNPNV 398
Cdd:cd21185      7 LRWVRQLLPDVDVNNFTTDWNDGRLLCGLVNALG-GSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEV 84

                           90
                   ....*....|..
gi 1834198951  399 DEQSMMTYLSQY 410
Cdd:cd21185     85 EHLGIMAYAAQL 96
Filamin pfam00630
Filamin/ABP280 repeat;
814-902 3.92e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 84.26  E-value: 3.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  814 FHPELVKASGPGLEknGVTINQPTSFTVDPSKAGNaPLDVVVQDVFGTKLPVELKNNPDGTKKVTYTPTSGVPHTVEVNY 893
Cdd:pfam00630    2 ADASKVKASGPGLE--PGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78


                   ....*....
gi 1834198951  894 GGVSTPNSP 902
Cdd:pfam00630   79 NGQHIPGSP 87
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2260-2349 4.04e-19

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 84.19  E-value: 4.04e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  2260 AHKLEVQQFPQGNIQADAPYQFMVRKNGA-KGELDAKIVAPSGTDDDCFIQVIDGEMYSVRFYPRENGIHAIHVKFNGVH 2338
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 1834198951  2339 IPDSPFRIKVG 2349
Cdd:smart00557   81 IPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
524-616 4.76e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 83.88  E-value: 4.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  524 AGDASKVKVTGPGIQPngVTIKKPTFFDILAKDAGrGVPEVIIIDPANHKtsVAAKVRQLENDTWRCEYVTALQGLHSVN 603
Cdd:pfam00630    1 AADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSP--VPVEVTDNGDGTYTVSYTPTEPGDYTVS 75

                           90
                   ....*....|...
gi 1834198951  604 VFYAGTPIPNSPF 616
Cdd:pfam00630   76 VKFNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
2352-2438 8.45e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 83.11  E-value: 8.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 2352 VADPAAVHASGNGLDEVKTGHKADFIINTCNAGvGTLAVSIDGPS--KVAMDCTEVEEG-YKVRYTPLLPGEHYITVKYN 2428
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1834198951 2429 NMHIVGSPFK 2438
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1487-1576 1.44e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 79.64  E-value: 1.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1487 SEPTKVKVKGVNeKKKTPASLPAEFEIDTKQAGQaDINVAIKNPKGKAMQPRLEEVSTGTYVVSFVPDECGTYQCSIKYG 1566
Cdd:pfam00630    2 ADASKVKASGPG-LEPGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1834198951 1567 DKEIEGSPFK 1576
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1726-1786 1.81e-17

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 79.57  E-value: 1.81e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834198951  1726 GGNVTAEVRMPSGKVDKPVIQDNRDGTVSVKYDPREEGSHELVVKYNGEPVQGSPFKFHVD 1786
Cdd:smart00557   31 GGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 913-996 1.67e-16

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 76.87  E-value: 1.67e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   913 AAKVQAFGPWLQPGvRPNAATHFNVDAREAGDAELKVKIIHEETKiEVPCRIIDNEDNTYSVEVIPPSKGAYTTTMTYGG 992
Cdd:smart00557    1 ASKVKASGPGLEKG-VVGEPAEFTVDTRDAGGGELEVEVTGPSGK-KVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78


                    ....
gi 1834198951   993 QRVP 996
Cdd:smart00557   79 EHIP 82
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 168-292 1.73e-16

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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: 409071  Cd Length: 121  Bit Score: 77.63  E-value: 1.73e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  168 ENFDEDMEAERDlaedaqwkKIQ--QNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMP--KYNKRPTF 243
Cdd:cd21222      1 DAFDDLFDEAPE--------KLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlhEYHLTPST 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1834198951  244 RSQKLENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLILHY 292
Cdd:cd21222     73 DDEKLHNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 178-294 3.41e-16

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: 77.11  E-value: 3.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  178 RDLAEdaQWKKIQQNTFTRWANEHLKTIDRSI--NNLETDLSDGLRLIALIEVLSQKRMPKYNKRpTFRSQKLENVSVAL 255
Cdd:cd21247     11 RKLQE--QRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRPSRG-KMRVHFLENNSKAI 87

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1834198951  256 KFLQDEgIKIVNIDSSDIVDCKLKLILGLIWTLILHYSI 294
Cdd:cd21247     88 TFLKTK-VPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
Filamin pfam00630
Filamin/ABP280 repeat;
910-996 9.74e-16

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 74.63  E-value: 9.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  910 PVDAAKVQAFGPWLQPGvRPNAATHFNVDAREAGDaELKVKIIHEETKiEVPCRIIDNEDNTYSVEVIPPSKGAYTTTMT 989
Cdd:pfam00630    1 AADASKVKASGPGLEPG-VVGKPAEFTVDTRDAGG-EGEVEVTGPDGS-PVPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77


                   ....*..
gi 1834198951  990 YGGQRVP 996
Cdd:pfam00630   78 FNGQHIP 84
Filamin pfam00630
Filamin/ABP280 repeat;
1388-1480 1.83e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 73.86  E-value: 1.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1388 VDPSKVKVYGPGIEHGQVreSVPTFFNVDVGEAGpGRIAVKLTNSEGIPVDNlRVEDKGNCIYAVHYVPPKAGsVLTCQV 1467
Cdd:pfam00630    2 ADASKVKASGPGLEPGVV--GKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPV-EVTDNGDGTYTVSYTPTEPG-DYTVSV 76

                           90
                   ....*....|...
gi 1834198951 1468 KFSEVEVPCSPFV 1480
Cdd:pfam00630   77 KFNGQHIPGSPFK 89
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 205-289 2.82e-15

first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409072  Cd Length: 113  Bit Score: 74.16  E-value: 2.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  205 IDRSINNLETDLSDGLRLIALIEVL-------SQKRMPKYNkrptfRSQKLENVSVALKFLQDEGI----KIVNIDSSDI 273
Cdd:cd21223     22 FDFAVTNLAVDLRDGVRLCRLVELLtgdwsllSKLRVPAIS-----RLQKLHNVEVALKALKEAGVlrggDGGGITAKDI 96

                           90
                   ....*....|....*.
gi 1834198951  274 VDCKLKLILGLIWTLI 289
Cdd:cd21223     97 VDGHREKTLALLWRII 112
Filamin pfam00630
Filamin/ABP280 repeat;
2257-2345 3.52e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 72.71  E-value: 3.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 2257 AGDAHKLEVQQFPQGNIQADAPYQFMVRKNGAKGELDAKIVAPSGTDDDCFIQVIDGEMYSVRFYPRENGIHAIHVKFNG 2336
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 1834198951 2337 VHIPDSPFR 2345
Cdd:pfam00630   81 QHIPGSPFK 89
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 190-292 1.31e-14

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. 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: 409062  Cd Length: 107  Bit Score: 71.95  E-value: 1.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  190 QQNTFTRWANEHLKTID--RSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKIVN 267
Cdd:cd21213      1 QLQAYVAWVNSQLKKRPgiRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80

                           90       100
                   ....*....|....*....|....*
gi 1834198951  268 IDSSDIVDCKLKLILGLIWTLILHY 292
Cdd:cd21213     81 TSAKDIVDGNLKAIMRLILALAAHF 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 318-410 1.60e-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: 71.58  E-value: 1.60e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951   318 LLNWI---HAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWEL---WDPKDAVQNASEAMGLADDWLNVRQLIKPE 391
Cdd:smart00033    3 LLRWVnslLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVaasLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90
                    ....*....|....*....
gi 1834198951   392 ELVNPNVDEQSMMTYLSQY 410
Cdd:smart00033   83 DLVEGPKLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
2481-2568 1.79e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.78  E-value: 1.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 2481 SDASKVVSKGMGLKKAYIGKQNQFSISATDAGNNILyVGMYGPKGPCEEFHVKHAGHNNYNVQYLVRDRGQYVLLIKWGE 2560
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGE-VEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 1834198951 2561 EHIPGSPF 2568
Cdd:pfam00630   81 QHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
1192-1288 5.28e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 69.63  E-value: 5.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1192 VPNLKNTRVSGIGIQPhgVIMNAATDFMVDMSKVGsnidsGKLSCAIFDPMGHVLPSKIVQGPtDDIFRIMYTPFEAGRH 1271
Cdd:pfam00630    1 AADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-----GEGEVEVTGPDGSPVPVEVTDNG-DGTYTVSYTPTEPGDY 72

                           90
                   ....*....|....*..
gi 1834198951 1272 TIELMYDNIPVPGSPFV 1288
Cdd:pfam00630   73 TVSVKFNGQHIPGSPFK 89
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 181-288 5.29e-14

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (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. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409134  Cd Length: 121  Bit Score: 70.76  E-value: 5.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  181 AEDAQWKKIqqntFTRWANEHLKTI--DRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFL 258
Cdd:cd21285      6 AENGFDKQI----YTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFL 81

                           90       100       110
                   ....*....|....*....|....*....|
gi 1834198951  259 QDEGIKIVNIDSSDIVDCKLKLILGLIWTL 288
Cdd:cd21285     82 AAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1601-1677 1.03e-13

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 68.78  E-value: 1.03e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834198951  1601 GSQSHLKVDAREAGDGAVTCKITNKAGSEiVDIDVIE-KDGFFDILYALNDPGDYDINVKFGGKDIPNGSFSIKAVES 1677
Cdd:smart00557   17 GEPAEFTVDTRDAGGGELEVEVTGPSGKK-VPVEVKDnGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGPA 93
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 192-292 2.65e-13

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: 68.46  E-value: 2.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  192 NTFTRWANEHLktIDRSINNLETDLSDGLRLIALIE-----VLSQKRMPKYNKRPTFrsQKLENVSVALKFLQDEGIKIV 266
Cdd:cd21219      7 RAFRMWLNSLG--LDPLINNLYEDLRDGLVLLQVLDkiqpgCVNWKKVNKPKPLNKF--KKVENCNYAVDLAKKLGFSLV 82

                           90       100
                   ....*....|....*....|....*.
gi 1834198951  267 NIDSSDIVDCKLKLILGLIWTLILHY 292
Cdd:cd21219     83 GIGGKDIADGNRKLTLALVWQLMRYH 108
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 314-410 2.93e-13

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 68.08  E-value: 2.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  314 PKQRLLNWI----HAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWEL-WDPKDAVQNASEAMGLADDWLNVRQ-L 387
Cdd:pfam00307    3 LEKELLRWInshlAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnKSEFDKLENINLALDVAEKKLGVPKvL 82

                           90       100
                   ....*....|....*....|...
gi 1834198951  388 IKPEELVNPnvDEQSMMTYLSQY 410
Cdd:pfam00307   83 IEPEDLVEG--DNKSVLTYLASL 103
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 194-288 5.18e-13

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: 67.36  E-value: 5.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  194 FTRWANEHLKTI--DRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKIVNIDSS 271
Cdd:cd21286      5 YTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAE 84

                           90
                   ....*....|....*..
gi 1834198951  272 DIVDCKLKLILGLIWTL 288
Cdd:cd21286     85 EIRNGNLKAILGLFFSL 101
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 315-410 6.94e-13

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409043  Cd Length: 105  Bit Score: 67.05  E-value: 6.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  315 KQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 391
Cdd:cd21194      4 KDALLLWCQRKTagyPGVNIQNFTTSWRDGLAFNALIHAHRPDLI-DYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAE 82

                           90
                   ....*....|....*....
gi 1834198951  392 ELVNPNVDEQSMMTYLSQY 410
Cdd:cd21194     83 DVDVARPDEKSIMTYVASY 101
Filamin pfam00630
Filamin/ABP280 repeat;
1726-1782 1.73e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 65.39  E-value: 1.73e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1834198951 1726 GGNVTAEVRMPSGKVDKPVIQDNRDGTVSVKYDPREEGSHELVVKYNGEPVQGSPFK 1782
Cdd:pfam00630   33 GGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 313-408 5.28e-12

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409038  Cd Length: 105  Bit Score: 64.34  E-value: 5.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNWIH---AKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 389
Cdd:cd21189      1 SAKEALLLWARrttEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLI-DFRSVRNQSNRENLENAFNVAEKEFGVTRLLD 79

                           90
                   ....*....|....*....
gi 1834198951  390 PEELVNPNVDEQSMMTYLS 408
Cdd:cd21189     80 PEDVDVPEPDEKSIITYVS 98
Filamin pfam00630
Filamin/ABP280 repeat;
1007-1093 1.28e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 62.69  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1007 VDVSKIKV--DGLEPtAPLNSLQQFRIITHGlPKADLAVTITSPSGNRIKAHIIPTAEG-FLVNFTPTQLGEYLLSICFG 1083
Cdd:pfam00630    2 ADASKVKAsgPGLEP-GVVGKPAEFTVDTRD-AGGEGEVEVTGPDGSPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1834198951 1084 GTPITPRPFR 1093
Cdd:pfam00630   80 GQHIPGSPFK 89
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 315-410 3.24e-11

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409098  Cd Length: 109  Bit Score: 62.19  E-value: 3.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  315 KQRLLNWIHAKIP---DLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 391
Cdd:cd21249      6 KEALLIWCQRKTAgytNVNVQDFSRSWRDGLAFNALIHAHRPDLI-DYGSLRPDRPLYNLANAFLVAEQELGISQLLDPE 84

                           90
                   ....*....|....*....
gi 1834198951  392 ELVNPNVDEQSMMTYLSQY 410
Cdd:cd21249     85 DVAVPHPDERSIMTYVSLY 103
Filamin pfam00630
Filamin/ABP280 repeat;
2106-2154 3.96e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 61.54  E-value: 3.96e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1834198951 2106 VTSPSNVTEDAEIQEVEDGLYAVHFVPKELGVHTVSVRYSEMHIPGSPF 2154
Cdd:pfam00630   40 VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1010-1097 4.38e-11

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 61.47  E-value: 4.38e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  1010 SKIKVD--GLEPtAPLNSLQQFRIITHGLPKADLAVTITSPSGNRIKAHIIPTAEG-FLVNFTPTQLGEYLLSICFGGTP 1086
Cdd:smart00557    2 SKVKASgpGLEK-GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 1834198951  1087 ITPRPFRLQCL 1097
Cdd:smart00557   81 IPGSPFTVKVG 91
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
 313-416 5.12e-11

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) 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. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409168  Cd Length: 112  Bit Score: 61.94  E-value: 5.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 389
Cdd:cd21319      5 SAKDALLLWCQMKTagyPNVNVTNFTSSWKDGLAFNALIHKHRPDLV-DFGKLKKSNARHNLEHAFNVAERQLGITKLLD 83

                           90       100
                   ....*....|....*....|....*....
gi 1834198951  390 PEELVNPNVDEQSMMTYLSQYPN--SKLK 416
Cdd:cd21319     84 PEDVFTENPDEKSIITYVVAFYHyfSKMK 112
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 209-296 9.13e-11

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 61.10  E-value: 9.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  209 INNLETDLSDGLRLIALIE------VLSQKRMPKYNKRPTFRsQKLENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLIL 282
Cdd:cd21298     24 VNHLYSDLRDGLVLLQLYDkikpgvVDWSRVNKPFKKLGANM-KKIENCNYAVELGKKLKFSLVGIGGKDIYDGNRTLTL 102

                           90
                   ....*....|....
gi 1834198951  283 GLIWTLILHYSISM 296
Cdd:cd21298    103 ALVWQLMRAYTLSI 116
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 315-410 1.17e-10

second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409041  Cd Length: 107  Bit Score: 60.51  E-value: 1.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  315 KQRLLNWIHAKIPDL---PINNFTNDWTTGKAVGALVDAcapgLCPDweLWD--------PKDavqNASEAMGLADDWLN 383
Cdd:cd21192      5 EKALLKWVQAEIGKYygiRVTDFDKSWRDGVAFLALIHA----IRPD--LVDmktvknrsPRD---NLELAFRIAEQHLN 75

                           90       100
                   ....*....|....*....|....*..
gi 1834198951  384 VRQLIKPEELVNPNVDEQSMMTYLSQY 410
Cdd:cd21192     76 IPRLLEVEDVLVDKPDERSIMTYVSQF 102
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
 315-410 1.21e-10

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409093  Cd Length: 109  Bit Score: 60.62  E-value: 1.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  315 KQRLLNWIH---AKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 391
Cdd:cd21244      7 RKALLLWAQeqcAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLV-DMEKLKGRSNRENLEEAFRIAEQELKIPRLLEPE 85

                           90
                   ....*....|....*....
gi 1834198951  392 ELVNPNVDEQSMMTYLSQY 410
Cdd:cd21244     86 DVDVVNPDEKSIMTYVAQF 104
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 318-410 1.43e-10

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409094  Cd Length: 106  Bit Score: 60.19  E-value: 1.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  318 LLNWIHAKIPD--LPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELVN 395
Cdd:cd21245      8 LLNWVQRRTRKygVAVQDFGSSWRSGLAFLALIKAIDPSLV-DMRQALEKSPRENLEDAFRIAQESLGIPPLLEPEDVMV 86

                           90
                   ....*....|....*
gi 1834198951  396 PNVDEQSMMTYLSQY 410
Cdd:cd21245     87 DSPDEQSIMTYVAQF 101
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 313-410 2.20e-10

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409065  Cd Length: 115  Bit Score: 60.07  E-value: 2.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNWIHAKI-PDLPIN--NFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 389
Cdd:cd21216     10 SAKEGLLLWCQRKTaPYKNVNvqNFHTSWKDGLAFCALIHRHRPDLL-DYDKLRKDDPRENLNLAFDVAEKHLDIPKMLD 88

                           90       100
                   ....*....|....*....|..
gi 1834198951  390 PEELVN-PNVDEQSMMTYLSQY 410
Cdd:cd21216     89 AEDIVNtPRPDERSVMTYVSCY 110
Filamin pfam00630
Filamin/ABP280 repeat;
1583-1670 1.17e-09

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 57.30  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951 1583 GEAKKCKLVEQAPKIQTSGSQSHLKVDAREAGdGAVTCKITNKAGSEIvDIDVIE-KDGFFDILYALNDPGDYDINVKFG 1661
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPV-PVEVTDnGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*....
gi 1834198951 1662 GKDIPNGSF 1670
Cdd:pfam00630   80 GQHIPGSPF 88
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
 189-292 1.97e-09

second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409186  Cd Length: 129  Bit Score: 57.70  E-value: 1.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  189 IQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYN--KRPTFRSQKLENVSVALKFLQDEGIKIV 266
Cdd:cd21337     20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSffLTPDSFEQKVLNVSFAFELMQDGGLEKP 99

                           90       100
                   ....*....|....*....|....*.
gi 1834198951  267 NIDSSDIVDCKLKLILGLIWTLILHY 292
Cdd:cd21337    100 KPRPEDIVNCDLKSTLRVLYNLFTKY 125
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
 315-411 2.83e-09

second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409092  Cd Length: 109  Bit Score: 56.56  E-value: 2.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  315 KQRLLNWIH---AKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 391
Cdd:cd21243      7 KKALLKWVQnaaAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLV-DMESLKRRSNRENLETAFTVAEKELGIPRLLDPE 85

                           90       100
                   ....*....|....*....|....
gi 1834198951  392 ELVNPNVDEQSMMTYLSQ----YP 411
Cdd:cd21243     86 DVDVDKPDEKSIMTYVAQflkkYP 109
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 307-410 5.53e-09

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409140  Cd Length: 115  Bit Score: 56.00  E-value: 5.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  307 LNGSGHTPKQRLLNWIHAKIP---DLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLN 383
Cdd:cd21291      4 INEEGLTAKEGLLLWCQRKTAgydEVDVQDFTTSWTDGLAFCALIHRHRPDLI-DYDKLDKKDHRGNMQLAFDIASKEIG 82

                           90       100
                   ....*....|....*....|....*...
gi 1834198951  384 VRQLIKPEELVN-PNVDEQSMMTYLSQY 410
Cdd:cd21291     83 IPQLLDVEDVCDvAKPDERSIMTYVAYY 110
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 194-289 1.10e-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: 55.27  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  194 FTRWANEHL---------KTIDRSINNLETDLSDGLRLIALIEvlsqKRMP---------KYNKRPTFrsQKLENVSVAL 255
Cdd:cd21217      6 FVEHINSLLaddpdlkhlLPIDPDGDDLFEALRDGVLLCKLIN----KIVPgtiderklnKKKPKNIF--EATENLNLAL 79

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1834198951  256 KFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLI 289
Cdd:cd21217     80 NAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 313-400 1.67e-08

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 54.61  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNWI--HAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCPD---WELWDPKDAVQNASEAMGLADDwLNV 384
Cdd:cd21218     10 PPEEILLRWVnyHLKKagpTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKelvLEVLSEEDLEKRAEKVLQAAEK-LGC 88

                           90
                   ....*....|....*.
gi 1834198951  385 RQLIKPEELVNPNVDE 400
Cdd:cd21218     89 KYFLTPEDIVSGNPRL 104
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 198-292 2.34e-08

second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 54.67  E-value: 2.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  198 ANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMP--KYNKRPTFRSQKLENVSVALKFLQDEGIKIVNIDSSDIVD 275
Cdd:cd21307     25 VNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHlsEFFLTPSSTSEMLHNVTLALELLKEGGLLNFPVNPEDIVN 104

                           90
                   ....*....|....*..
gi 1834198951  276 CKLKLILGLIWTLILHY 292
Cdd:cd21307    105 GDSKATIRVLYCLFSKY 121
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
 189-292 3.05e-08

second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409187  Cd Length: 130  Bit Score: 54.59  E-value: 3.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  189 IQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYN--KRPTFRSQKLENVSVALKFLQDEGIKIV 266
Cdd:cd21338     21 VVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNfyLTPESFDQKVHNVSFAFELMQDGGLKKP 100

                           90       100
                   ....*....|....*....|....*.
gi 1834198951  267 NIDSSDIVDCKLKLILGLIWTLILHY 292
Cdd:cd21338    101 KARPEDVVNLDLKSTLRVLYNLFTKY 126
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 313-408 3.12e-08

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409087  Cd Length: 106  Bit Score: 53.87  E-value: 3.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 389
Cdd:cd21238      2 TAKEKLLLWSQRMVegyQGLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80

                           90
                   ....*....|....*....
gi 1834198951  390 PEELVNPNVDEQSMMTYLS 408
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVS 99
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 315-410 3.76e-08

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409097  Cd Length: 105  Bit Score: 53.55  E-value: 3.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  315 KQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 391
Cdd:cd21248      4 KDALLLWCQMKTagyPNVNVRNFTTSWRDGLAFNALIHKHRPDLI-DYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPE 82

                           90
                   ....*....|....*....
gi 1834198951  392 ELVNPNVDEQSMMTYLSQY 410
Cdd:cd21248     83 DVNVEQPDEKSIITYVVTY 101
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 197-292 5.06e-08

second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily 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: 409155  Cd Length: 121  Bit Score: 53.58  E-value: 5.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  197 WANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMP--KYNKRPTFRSQKLENVSVALKFLQDEGIKIVNIDSSDIV 274
Cdd:cd21306     24 FVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPlhSFHLTPTSFEQKVHNVQFAFELMQDAGLPKPKARPEDIV 103

                           90
                   ....*....|....*...
gi 1834198951  275 DCKLKLILGLIWTLILHY 292
Cdd:cd21306    104 NLDLKSTLRVLYNLFTKY 121
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 315-419 8.00e-08

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409170  Cd Length: 119  Bit Score: 53.14  E-value: 8.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  315 KQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 391
Cdd:cd21321      7 KDALLLWCQMKTagyPNVNVHNFTTSWRDGLAFNAIVHKHRPDLI-DFETLKKSNAHYNLQNAFNVAEKELGLTKLLDPE 85

                           90       100       110
                   ....*....|....*....|....*....|
gi 1834198951  392 ELVNPNVDEQSMMTYLSQYPN--SKLKTGA 419
Cdd:cd21321     86 DVNVDQPDEKSIITYVATYYHyfSKMKALA 115
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 313-410 9.43e-08

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409169  Cd Length: 108  Bit Score: 52.41  E-value: 9.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 389
Cdd:cd21320      2 SAKDALLLWCQMKTagyPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 80

                           90       100
                   ....*....|....*....|.
gi 1834198951  390 PEELVNPNVDEQSMMTYLSQY 410
Cdd:cd21320     81 PEDISVDHPDEKSIITYVVTY 101
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 302-419 1.19e-07

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409171  Cd Length: 130  Bit Score: 52.75  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  302 EDDKQLNGSghtpKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLA 378
Cdd:cd21322     10 EDNRETRSA----KDALLLWCQMKTagyPEVNIQNFTTSWRDGLAFNALIHRHRPDLI-DFSKLTKSNATYNLQQAFNTA 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1834198951  379 DDWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPN--SKLKTGA 419
Cdd:cd21322     85 EQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFYHyfSKMKALA 127
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 316-410 1.37e-07

calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409188  Cd Length: 105  Bit Score: 51.90  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  316 QRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEE 392
Cdd:cd22198      3 EELLSWCQEQTegyRGVKVTDLTSSWRSGLALCAIIHRFRPDLI-DFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQE 81

                           90
                   ....*....|....*....
gi 1834198951  393 LVNPNV-DEQSMMTYLSQY 410
Cdd:cd22198     82 MASLAVpDKLSMVSYLSQF 100
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 314-412 1.49e-07

calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409046  Cd Length: 105  Bit Score: 51.77  E-value: 1.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  314 PKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKP 390
Cdd:cd21197      1 KIQALLRWCRRQCegyPGVNITNLTSSFRDGLAFCAILHRHRPELI-DFHSLKKDNWLENNRLAFRVAETSLGIPALLDA 79

                           90       100
                   ....*....|....*....|...
gi 1834198951  391 EELVNPNV-DEQSMMTYLSQYPN 412
Cdd:cd21197     80 EDMVTMHVpDRLSIITYVSQYYN 102
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 196-288 3.84e-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: 50.76  E-value: 3.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  196 RWANEHLK---TIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTF-RSQKLENVSVALKFLQDEGIKIVnIDSS 271
Cdd:cd21218     17 RWVNYHLKkagPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLsEEDLEKRAEKVLQAAEKLGCKYF-LTPE 95

                           90
                   ....*....|....*..
gi 1834198951  272 DIVDCKLKLILGLIWTL 288
Cdd:cd21218     96 DIVSGNPRLNLAFVATL 112
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 313-410 2.94e-06

second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409138  Cd Length: 124  Bit Score: 48.57  E-value: 2.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNWIHAKIP---DLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 389
Cdd:cd21289     10 SAKEGLLLWCQRKTApyrNVNVQNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLD 88

                           90       100
                   ....*....|....*....|..
gi 1834198951  390 PEELVN-PNVDEQSMMTYLSQY 410
Cdd:cd21289     89 AEDIVNtPKPDEKAIMTYVSCF 110
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 318-408 3.93e-06

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


Pssm-ID: 409082  Cd Length: 111  Bit Score: 48.00  E-value: 3.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  318 LLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKD-AVQNASEAMGLADDWLNVRQLIKPEEL 393
Cdd:cd21233      5 LLSWVRQSTrnyPQVNVINFTSSWSDGLAFNALIHSHRPDLF-DWNSVVSQQsATERLDHAFNIARQHLGIEKLLDPEDV 83

                           90
                   ....*....|....*
gi 1834198951  394 VNPNVDEQSMMTYLS 408
Cdd:cd21233     84 ATAHPDKKSILMYVT 98
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 313-409 4.12e-06

calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409047  Cd Length: 105  Bit Score: 47.81  E-value: 4.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNW---IHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDwLNVRQLIK 389
Cdd:cd21198      1 SSGQDLLEWcqeVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLI-DFSSLSPHDIKENCKLAFDAAAK-LGIPRLLD 78

                           90       100
                   ....*....|....*....|.
gi 1834198951  390 PEELVNPNV-DEQSMMTYLSQ 409
Cdd:cd21198     79 PADMVLLSVpDKLSVMTYLHQ 99
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
 313-408 5.88e-06

second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409137  Cd Length: 124  Bit Score: 47.76  E-value: 5.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNWIHAKIP---DLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 389
Cdd:cd21288     10 SAKEGLLLWCQRKTApyrNVNIQNFHTSWKDGLGLCALIHRHRPDLI-DYSKLNKDDPIGNINLAMEIAEKHLDIPKMLD 88

                           90       100
                   ....*....|....*....|
gi 1834198951  390 PEELVN-PNVDEQSMMTYLS 408
Cdd:cd21288     89 AEDIVNtPKPDERAIMTYVS 108
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 182-296 1.18e-05

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 46.91  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  182 EDAQWKKIQ-----QNTFTRWANEhlKTIDRSINNLETDLSDGLRLIALIEVLsqkRMP----KYNKRPTFR----SQKL 248
Cdd:cd21330      1 QDIDWSSIEgetreERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKI---KVPvdwnRVNKPPYPKlgenMKKL 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1834198951  249 ENVSVALKFLQDEG-IKIVNIDSSDIVDCKLKLILGLIWTLILHYSISM 296
Cdd:cd21330     76 ENCNYAVELGKNKAkFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNI 124
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 194-288 1.34e-05

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: 46.65  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  194 FTRWANEhlKTIDRSINNLETDLSDGLRLIALIEvlsqKRMP------KYNKRP----TFRSQKLENVSVALKFLQDEGI 263
Cdd:cd21300     12 FTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYD----KVIPgsvnwkKVNKAPasaeISRFKAVENTNYAVELGKQLGF 85

                           90       100
                   ....*....|....*....|....*
gi 1834198951  264 KIVNIDSSDIVDCKLKLILGLIWTL 288
Cdd:cd21300     86 SLVGIQGADITDGSRTLTLALVWQL 110
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 313-408 1.67e-05

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409089  Cd Length: 107  Bit Score: 45.80  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNW---IHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDwLNVRQLIK 389
Cdd:cd21240      4 SAKEKLLLWtqkVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGVTRLLD 81

                           90
                   ....*....|....*....
gi 1834198951  390 PEELVNPNVDEQSMMTYLS 408
Cdd:cd21240     82 AEDVDVPSPDEKSVITYVS 100
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 190-296 1.74e-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: 46.13  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  190 QQNTFTRWANEhlKTIDRSINNLETDLSDGLRLIALIEVLsqkRMP----KYNKRP----TFRSQKLENVSVALKFLQDE 261
Cdd:cd21329      7 EERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMT---RVPvdwgHVNKPPypalGGNMKKIENCNYAVELGKNK 81

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1834198951  262 G-IKIVNIDSSDIVDCKLKLILGLIWTLILHYSISM 296
Cdd:cd21329     82 AkFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNV 117
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
 315-418 2.04e-05

calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409109  Cd Length: 116  Bit Score: 45.85  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  315 KQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 391
Cdd:cd21260      3 KNMLLEWCRAKTrgyEHVDIQNFSSSWSSGMAFCALIHKFFPDAF-DYAELDPANRRHNFTLAFSTAEKHADCAPLLEVE 81

                           90       100
                   ....*....|....*....|....*...
gi 1834198951  392 ELVNPNV-DEQSMMTYLSQYPNSKLKTG 418
Cdd:cd21260     82 DMVRMSVpDSKCVYTYIQELYRSLVQKG 109
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
158-289 2.40e-05

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 49.94  E-value: 2.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  158 QEGQQADQYEENFDEDMEAERdlaedaqwkkiQQNTFTRWANEHlkTIDRSINNLETDLSDGLRLIaliEVLSQKRMP-- 235
Cdd:COG5069    359 QEPLEEEEKPEIEEFDAEGEF-----------EARVFTFWLNSL--DVSPEITNLFGDLRDQLILL---QALSKKLMPmt 422

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834198951  236 ----KYNKRPT-----FRSQKLENVSVALKFLQDEGIKIVNIDSSDIVDcKLKLILGLIWTLI 289
Cdd:COG5069    423 vthkLVKKQPAsgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILD-GIRLKLTLVWQVL 484
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 194-289 3.34e-05

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: 46.12  E-value: 3.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  194 FTRWANEHLKT---------IDRSINNLETDLSDGLRLIALIEvLSQ-----KRMPKYNKRPTFRSQklENVSVALKFLQ 259
Cdd:cd21292     29 FVNWINKNLGDdpdckhllpMDPNTDDLFEKVKDGILLCKMIN-LSVpdtidERAINKKKLTVFTIH--ENLTLALNSAS 105

                           90       100       110
                   ....*....|....*....|....*....|
gi 1834198951  260 DEGIKIVNIDSSDIVDCKLKLILGLIWTLI 289
Cdd:cd21292    106 AIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 191-261 7.72e-05

first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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: 409070  Cd Length: 106  Bit Score: 44.19  E-value: 7.72e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834198951  191 QNTFTRWANEHLKTiDRSI-NNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKlENVSVALKFLQDE 261
Cdd:cd21221      3 VRVLTEWINEELAD-DRIVvRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQK-QKLAVVLACVNFL 72
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 194-289 8.53e-05

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 45.03  E-value: 8.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  194 FTRWANE---------HLKTIDRSINNLETDLSDGLRLIALIEvLSQkrmPKYNKRPTFRSQKL------ENVSVALKFL 258
Cdd:cd21323     29 FVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMIN-LSQ---PDTIDERAINKKKLtpftisENLNLALNSA 104

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1834198951  259 QDEGIKIVNIDSSDIVDCKLKLILGLIWTLI 289
Cdd:cd21323    105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 318-408 1.32e-04

second 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 link 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409036  Cd Length: 104  Bit Score: 43.19  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  318 LLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELV 394
Cdd:cd21187      5 LLAWCRQSTrgyEQVDVKNFTTSWRDGLAFNALIHRHRPDLF-DFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVN 83

                           90
                   ....*....|....
gi 1834198951  395 NPNVDEQSMMTYLS 408
Cdd:cd21187     84 VEQPDKKSILMYVT 97
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 190-296 1.43e-04

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


Pssm-ID: 409148  Cd Length: 114  Bit Score: 43.64  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  190 QQNTFTRWANEhlKTIDRSINNLETDLSDGLRLIALIEVLSQKRM--PKYNKRPT---FRsqKLENVSVALKFLQDEGIK 264
Cdd:cd21299      5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVnwKHANKPPIkmpFK--KVENCNQVVKIGKQLKFS 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1834198951  265 IVNIDSSDIVDCKLKLILGLIWTLILHYSISM 296
Cdd:cd21299     81 LVNVAGNDIVQGNKKLILALLWQLMRYHMLQL 112
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 327-412 1.71e-04

calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409102  Cd Length: 106  Bit Score: 43.10  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  327 PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELVNPNV-DEQSMMT 405
Cdd:cd21253     18 RDVKVTNMTTSWRDGLAFCAIIHRFRPDLI-DFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDMVALKVpDKLSILT 96


                   ....*..
gi 1834198951  406 YLSQYPN 412
Cdd:cd21253     97 YVSQYYN 103
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 315-418 2.20e-04

calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409108  Cd Length: 112  Bit Score: 43.06  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  315 KQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 391
Cdd:cd21259      3 KQMLLDWCRAKTrgyENVDIQNFSSSWSDGMAFCALVHNFFPEAF-DYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVE 81

                           90       100
                   ....*....|....*....|....*...
gi 1834198951  392 ELVN-PNVDEQSMMTYLSQYPNSKLKTG 418
Cdd:cd21259     82 DMVRmREPDWKCVYTYIQEFYRCLVQKG 109
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 315-407 2.21e-04

calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409049  Cd Length: 107  Bit Score: 42.72  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  315 KQRLLNWIHAKIPDLP---INNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 391
Cdd:cd21200      3 KQMLLEWCQAKTRGYEhvdITNFSSSWSDGMAFCALIHHFFPDAF-DYSSLDPKNRRKNFELAFSTAEELADIAPLLEVE 81

                           90       100
                   ....*....|....*....|
gi 1834198951  392 ELV----NPnvDEQSMMTYL 407
Cdd:cd21200     82 DMVrmgnRP--DWKCVFTYV 99
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 313-408 2.39e-04

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409088  Cd Length: 104  Bit Score: 42.67  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  313 TPKQRLLNW---IHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDwLNVRQLIK 389
Cdd:cd21239      1 SAKERLLLWsqqMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLI-DMNTVAVQSNLANLEHAFYVAEK-LGVTRLLD 78

                           90
                   ....*....|....*....
gi 1834198951  390 PEELVNPNVDEQSMMTYLS 408
Cdd:cd21239     79 PEDVDVSSPDEKSVITYVS 97
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 217-289 2.67e-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: 42.82  E-value: 2.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  217 SDGLRLIALI----------EVLSQkrmPKYNKRPTFRSQKLENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLILGLIW 286
Cdd:cd21294     43 KDGLVLSKLIndsvpdtideRVLNK---PPRKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIW 119


                   ...
gi 1834198951  287 TLI 289
Cdd:cd21294    120 QII 122
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 315-409 3.77e-04

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 41.94  E-value: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  315 KQRLLNWI---HAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWEL--WDPKDAVQNASEAMGLADDW-LNVRQLI 388
Cdd:cd00014      1 EEELLKWInevLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKkpKSPFKKRENINLFLNACKKLgLPELDLF 80

                           90       100
                   ....*....|....*....|.
gi 1834198951  389 KPEELVNPNvDEQSMMTYLSQ 409
Cdd:cd00014     81 EPEDLYEKG-NLKKVLGTLWA 100
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 318-408 4.12e-04

second 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 second CH domain.


Pssm-ID: 409083 [Multi-domain]  Cd Length: 104  Bit Score: 41.87  E-value: 4.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  318 LLNWIHAKI-PDLPIN--NFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELV 394
Cdd:cd21234      5 LLSWVRQSTrPYSQVNvlNFTTSWTDGLAFNAVLHRHKPDLF-SWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVA 83

                           90
                   ....*....|....
gi 1834198951  395 NPNVDEQSMMTYLS 408
Cdd:cd21234     84 VQLPDKKSIIMYLT 97
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 311-409 1.24e-03

calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409106  Cd Length: 112  Bit Score: 40.78  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  311 GHTPKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELwDPKDAVQNASEAMGLADDwLNVRQL 387
Cdd:cd21257      6 GGSKRNALLKWCQKKTegyPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQEL-SSQDKKRNLLLAFQAAES-VGIKPS 83

                           90       100
                   ....*....|....*....|...
gi 1834198951  388 IKPEELVNPN-VDEQSMMTYLSQ 409
Cdd:cd21257     84 LELSEMMYTDrPDWQSVMQYVAQ 106
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
 311-408 2.23e-03

calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409105  Cd Length: 119  Bit Score: 40.06  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  311 GHTPKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELwDPKDAVQN------ASEAMGLADDw 381
Cdd:cd21256     12 GGSKRNALLKWCQKKTegyQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQEL-NSQDKRRNftlafqAAESVGIKST- 89

                           90       100
                   ....*....|....*....|....*..
gi 1834198951  382 LNVRQLIKPEElvnpnVDEQSMMTYLS 408
Cdd:cd21256     90 LDINEMVRTER-----PDWQSVMTYVT 111
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 314-408 3.56e-03

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409075  Cd Length: 103  Bit Score: 39.37  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  314 PKQRLLNWIHAKIPD---LPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKP 390
Cdd:cd21226      1 SEDGLLAWCRQTTEGydgVNITSFKSSFNDGRAFLALLHAYDPELF-KQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEA 79

                           90
                   ....*....|....*...
gi 1834198951  391 EELVNPNVDEQSMMTYLS 408
Cdd:cd21226     80 EDVMTGNPDERSIVLYTS 97
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
 315-394 3.83e-03

calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409110  Cd Length: 107  Bit Score: 39.18  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  315 KQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 391
Cdd:cd21261      3 KQILLEWCRSKTigyKNIDLQNFSSSWSDGMAFCALVHSFFPEAF-DYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVE 81


                   ...
gi 1834198951  392 ELV 394
Cdd:cd21261     82 DMM 84
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
 314-412 4.29e-03

calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409101  Cd Length: 107  Bit Score: 39.08  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834198951  314 PKQRLLNWIH---AKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKP 390
Cdd:cd21252      1 ARRALQAWCRrqcEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLI-DFDSLSKDNVYENNRLAFEVAERELGIPALLDP 79

                           90       100
                   ....*....|....*....|...
gi 1834198951  391 EELVNPNV-DEQSMMTYLSQYPN 412
Cdd:cd21252     80 EDMVSMKVpDCLSIMTYVSQYYN 102
 
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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