NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1952979823|ref|XP_038412503|]
View 

filamin-C isoform X2 [Canis lupus familiaris]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 151-265 1.30e-89

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: 286.58  E-value: 1.30e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  151 DEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVENAREAMQQADDWL 230
Cdd:cd21314      1 DEDEEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPVQNAREAMQQADDWL 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1952979823  231 GVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKP 265
Cdd:cd21314     81 GVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKP 115
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 23-147 3.23e-85

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: 274.60  E-value: 3.23e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   23 PSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVS 102
Cdd:cd21310      1 PATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQMKLENVS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1952979823  103 VALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 147
Cdd:cd21310     81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 125
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1849-1935 1.02e-33

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: 125.79  E-value: 1.02e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1849 VSAYGPGLSHGMVNKPATFTIVTKDAGEGGLSLAVEGPS--KAEITCKDNKDGTCTVSYLPTAPGDYSIIVRFDDKHIPG 1926
Cdd:smart00557    4 VKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83


                    ....*....
gi 1952979823  1927 SPFTAKITG 1935
Cdd:smart00557   84 SPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1156-1248 6.26e-33

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: 123.48  E-value: 6.26e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1156 PSKVRASGPGLERGKAGEAATFTVDCSEAGEAELTIEILSDAGVKAEVLIHNNADGTYHITYSPAFPGTYTITIKYGGHP 1235
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 1952979823  1236 VPKFPTRVHVQPA 1248
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1444-1537 3.29e-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: 3.29e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1444 PGKVKCSGPGLGAGvRARVPQTFTVDCSQAGRAPLQVAVLGPTGVAEPVEVLDNGGGTHTVHYTPATDGPYTVAVKYADQ 1523
Cdd:smart00557    1 ASKVKASGPGLEKG-VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 1952979823  1524 EVPRSPFKIKVLPA 1537
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2028-2117 6.31e-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: 120.79  E-value: 6.31e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  2028 ASKVRVWGKGLSEGHTFQVAEFIVDTRNAGYGGLGLSIEGPS--KVDINCEDMEDGTCKVTYCPTEPGTYIINIKFADKH 2105
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1952979823  2106 VPGSPFTVKVTG 2117
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 668-762 2.48e-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: 119.25  E-value: 2.48e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   668 PDKVKAFGPGLEPTgcIVDKPAEFTIDARAAGKGDLNLYAQDADGCPVNIMVIPNGDGTFRCSYVPTKPIKHTIIISWGG 747
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 1952979823   748 VNVPKSPFRVNVGEG 762
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1540-1634 3.14e-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: 118.86  E-value: 3.14e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1540 ASKVRASGPGLNasGIPASLPVEFTIDARDAGEGLLTVQILDPEGKPKKANIRDNGDGTYTVSYLPDMSGRYTITIKYGG 1619
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 1952979823  1620 DEIPYSPFRIHALPT 1634
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2301-2389 4.53e-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: 4.53e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  2301 AHKVRAGGTGLERGVAGVPAEFSIWTREAGAGGLSIAVEGPS--KAEIAFEDRKDGSCGVSYVVQEPGDYEVSIKFNDEH 2378
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 1952979823  2379 IPDSPFVVPVA 2389
Cdd:smart00557   81 IPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 475-568 7.23e-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: 117.70  E-value: 7.23e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   475 PNACRASGRGLQPKgvRVKEVADFKVFTKGAGSGELKVTVKGPKGTEEPVKVREAGDGVFECEYYPVVPGKYVVTITWGG 554
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....
gi 1952979823   555 YAIPRSPFEVQVSP 568
Cdd:smart00557   79 EHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 276-372 2.21e-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: 113.47  E-value: 2.21e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   276 PKKAIAYGPGIEPHgnTVLQPAHFTVQTVDAGVGEVLVYIEDPEGHTEEAKVVPNNDknRTYAVSYVPKVAGLHKVTVLF 355
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGD--GTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 1952979823   356 AGQNIERSPFEVNVGMA 372
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2622-2711 2.32e-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: 113.47  E-value: 2.32e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  2622 ASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMMVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWGDES 2701
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 1952979823  2702 VPGSPFKVNV 2711
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 376-472 4.81e-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: 106.92  E-value: 4.81e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   376 ANKVSARGPGLEPmgNVANKPTYFDIYTAGAGTGDVAVVIVDPQGRRdtVEVALEDKGDNTFRCTYRPVMEGPHTVHVAF 455
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 1952979823   456 AGAPITRSPFPVHVAEA 472
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1637-1725 1.06e-26

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: 105.76  E-value: 1.06e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1637 ASKCLVTGACLGPrIQIGEETVITVDAKAAGKGKVTCTVSTPDGAELDVDVVENHDGTFDIYYTAPEPGKYVITIRFGGE 1716
Cdd:smart00557    1 ASKVKASGPGLEK-GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79


                    ....*....
gi 1952979823  1717 HIPNSPFHV 1725
Cdd:smart00557   80 HIPGSPFTV 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 765-865 1.67e-26

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: 105.38  E-value: 1.67e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   765 PERVKVYGPGVEKTglKANEPTYFTVDCSEAGQGDVSIGikcapgVVGPAEADIDFDIIKNDNDTFTVKYTPPGAGRYTI 844
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVE------VTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTV 72

                            90       100
                    ....*....|....*....|.
gi 1952979823   845 MVLFANQEIPASPFHIKVDPS 865
Cdd:smart00557   73 TVKFGGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 573-662 2.11e-26

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: 104.99  E-value: 2.11e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   573 QKVRAWGPGLKTGQVGKSADFVVEAIGTEVGTLGFSIEGPSQAKIECD--DKGDGSCDVRYWPTEPGEYAVHVICDDEDI 650
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEvkDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|..
gi 1952979823   651 RDSPFIAHIQPA 662
Cdd:smart00557   82 PGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1252-1348 2.39e-26

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: 104.99  E-value: 2.39e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1252 SGIKVSGPGVEPHGVLreVTTEFTVDARSltaTGGNHVTARVLNPSGAKTDTYVTDNGDGTYRVQYTAYEEGVHLVEVLY 1331
Cdd:smart00557    2 SKVKASGPGLEKGVVG--EPAEFTVDTRD---AGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 1952979823  1332 DDVAVPKSPFRVGVTEG 1348
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1063-1152 4.37e-26

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: 104.22  E-value: 4.37e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1063 PSKVCAYGPGLKGGLVGSPAPFSIDTKGAGTGGLGLTVEGP--CEAKIECQDNGDGSCAVSYLPTEPGEYTINILFAEAH 1140
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1952979823  1141 IPGSPFKATIRP 1152
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 868-964 4.45e-26

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: 104.22  E-value: 4.45e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   868 ASKVKAEGPGLNRTgvEVGKPTHFTVLTKGAGKAKLDVHFAGAAKGEAvrDFEIIDNHDYSYTVKYTAVQQGNMAVTVTY 947
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKV--PVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 1952979823   948 GGDPVPKSPFVVNVAPP 964
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2492-2582 1.81e-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: 102.30  E-value: 1.81e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  2492 PGLVSAYGPGLEGGTTGVSSEFIVNTLNAGSGALSVTIDGPS--KVQLDCRECPEGHV-VTYTPMAPGNYLIAIKYGGpQ 2568
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYtVSYTPTEPGDYTVTVKFGG-E 79

                            90
                    ....*....|....
gi 1952979823  2569 HIVGSPFKAKVTGP 2582
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1351-1440 2.21e-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: 102.30  E-value: 2.21e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1351 PTRVRAFGPGLESGLVNKANHFTVETRGAGTGGLGLAIEGPS--EAKMSCKDNKDGSCTVEYIPFTPGDYDVNITFGGRP 1428
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1952979823  1429 IPGSPFRVPVKD 1440
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 968-1061 1.30e-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: 1.30e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   968 SKVKVQGLN-SKVAVGQEQAFSVNTRGAGGqGQLDVRMTSPSRRPIPCKVEPGGGAeTQAVRYMPPEEGPYKVDITYDGH 1046
Cdd:smart00557    2 SKVKASGPGlEKGVVGEPAEFTVDTRDAGG-GELEVEVTGPSGKKVPVEVKDNGDG-TYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....*
gi 1952979823  1047 PVPGSPFAVEgVLPP 1061
Cdd:smart00557   80 HIPGSPFTVK-VGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2394-2480 1.02e-17

Filamin/ABP280 repeat;


:

Pssm-ID: 395505  Cd Length: 89  Bit Score: 80.03  E-value: 1.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 2394 DARRLTVTSLQETGLKVNQPASFAVQLNGARGVIDARVHTPSGAVEECYVSELDSDKHTIRFIPHENGVHSIDVKFNGAH 2473
Cdd:pfam00630    3 DASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQH 82


                   ....*..
gi 1952979823 2474 IPGSPFK 2480
Cdd:pfam00630   83 IPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1778-1842 8.87e-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: 74.95  E-value: 8.87e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1778 FTVQ-----KGELTGEVRMPSGKTARPNITDNKDGTITVRYAPTEKGLHQMGIKYDGNHIPGSPLQFYVD 1842
Cdd:smart00557   22 FTVDtrdagGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2231-2295 3.64e-15

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: 73.02  E-value: 3.64e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952979823  2231 EASSQDMTAQVTSPSGKMEAAEIVEGEDSAYSVRFVPQEMGPHTVTVKYRGQHVPGSPFQFTVGP 2295
Cdd:smart00557   28 DAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGP 92
 
Name Accession Description Interval E-value
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 151-265 1.30e-89

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: 286.58  E-value: 1.30e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  151 DEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVENAREAMQQADDWL 230
Cdd:cd21314      1 DEDEEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPVQNAREAMQQADDWL 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1952979823  231 GVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKP 265
Cdd:cd21314     81 GVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKP 115
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 23-147 3.23e-85

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: 274.60  E-value: 3.23e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   23 PSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVS 102
Cdd:cd21310      1 PATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQMKLENVS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1952979823  103 VALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 147
Cdd:cd21310     81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 125
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1849-1935 1.02e-33

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: 125.79  E-value: 1.02e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1849 VSAYGPGLSHGMVNKPATFTIVTKDAGEGGLSLAVEGPS--KAEITCKDNKDGTCTVSYLPTAPGDYSIIVRFDDKHIPG 1926
Cdd:smart00557    4 VKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83


                    ....*....
gi 1952979823  1927 SPFTAKITG 1935
Cdd:smart00557   84 SPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1156-1248 6.26e-33

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: 123.48  E-value: 6.26e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1156 PSKVRASGPGLERGKAGEAATFTVDCSEAGEAELTIEILSDAGVKAEVLIHNNADGTYHITYSPAFPGTYTITIKYGGHP 1235
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 1952979823  1236 VPKFPTRVHVQPA 1248
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1444-1537 3.29e-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: 3.29e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1444 PGKVKCSGPGLGAGvRARVPQTFTVDCSQAGRAPLQVAVLGPTGVAEPVEVLDNGGGTHTVHYTPATDGPYTVAVKYADQ 1523
Cdd:smart00557    1 ASKVKASGPGLEKG-VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 1952979823  1524 EVPRSPFKIKVLPA 1537
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2028-2117 6.31e-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: 120.79  E-value: 6.31e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  2028 ASKVRVWGKGLSEGHTFQVAEFIVDTRNAGYGGLGLSIEGPS--KVDINCEDMEDGTCKVTYCPTEPGTYIINIKFADKH 2105
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1952979823  2106 VPGSPFTVKVTG 2117
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 668-762 2.48e-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: 119.25  E-value: 2.48e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   668 PDKVKAFGPGLEPTgcIVDKPAEFTIDARAAGKGDLNLYAQDADGCPVNIMVIPNGDGTFRCSYVPTKPIKHTIIISWGG 747
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 1952979823   748 VNVPKSPFRVNVGEG 762
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1540-1634 3.14e-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: 118.86  E-value: 3.14e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1540 ASKVRASGPGLNasGIPASLPVEFTIDARDAGEGLLTVQILDPEGKPKKANIRDNGDGTYTVSYLPDMSGRYTITIKYGG 1619
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 1952979823  1620 DEIPYSPFRIHALPT 1634
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2301-2389 4.53e-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: 4.53e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  2301 AHKVRAGGTGLERGVAGVPAEFSIWTREAGAGGLSIAVEGPS--KAEIAFEDRKDGSCGVSYVVQEPGDYEVSIKFNDEH 2378
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 1952979823  2379 IPDSPFVVPVA 2389
Cdd:smart00557   81 IPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 475-568 7.23e-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: 117.70  E-value: 7.23e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   475 PNACRASGRGLQPKgvRVKEVADFKVFTKGAGSGELKVTVKGPKGTEEPVKVREAGDGVFECEYYPVVPGKYVVTITWGG 554
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....
gi 1952979823   555 YAIPRSPFEVQVSP 568
Cdd:smart00557   79 EHIPGSPFTVKVGP 92
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
35-261 4.58e-30

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 128.91  E-value: 4.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   35 WKKIQQNTFTRWCNEHLKCVG-KRLTDLQRDLSDGLRLIALLEVLSQKRMYRkFHPRPNFRQMKLENVSVALEFLEREHI 113
Cdd:COG5069      6 WQKVQKKTFTKWTNEKLISGGqKEFGDLDTDLKDGVKLAQLLEALQKDNAGE-YNETPETRIHVMENVSGRLEFIKGKGV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  114 KLVSIDSKAIVDGNLKLILGLIWTLILHYSISmpmwedeDDEDARKQTPKQRLLGW----IQNKVPQLPITNFNRDWQDG 189
Cdd:COG5069     85 KLFNIGPQDIVDGNPKLILGLIWSLISRLTIA-------TINEEGELTKHINLLLWcdedTGGYKPEVDTFDFFRSWRDG 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952979823  190 KALGALVDNCAP-GLCPDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEEIVDPNV-DEHSVMTYLSQFPKA 261
Cdd:COG5069    158 LAFSALIHDSRPdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSWYIIR 231
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 276-372 2.21e-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: 113.47  E-value: 2.21e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   276 PKKAIAYGPGIEPHgnTVLQPAHFTVQTVDAGVGEVLVYIEDPEGHTEEAKVVPNNDknRTYAVSYVPKVAGLHKVTVLF 355
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGD--GTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 1952979823   356 AGQNIERSPFEVNVGMA 372
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2622-2711 2.32e-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: 113.47  E-value: 2.32e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  2622 ASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMMVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWGDES 2701
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 1952979823  2702 VPGSPFKVNV 2711
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 376-472 4.81e-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: 106.92  E-value: 4.81e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   376 ANKVSARGPGLEPmgNVANKPTYFDIYTAGAGTGDVAVVIVDPQGRRdtVEVALEDKGDNTFRCTYRPVMEGPHTVHVAF 455
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 1952979823   456 AGAPITRSPFPVHVAEA 472
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1637-1725 1.06e-26

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: 105.76  E-value: 1.06e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1637 ASKCLVTGACLGPrIQIGEETVITVDAKAAGKGKVTCTVSTPDGAELDVDVVENHDGTFDIYYTAPEPGKYVITIRFGGE 1716
Cdd:smart00557    1 ASKVKASGPGLEK-GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79


                    ....*....
gi 1952979823  1717 HIPNSPFHV 1725
Cdd:smart00557   80 HIPGSPFTV 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 765-865 1.67e-26

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: 105.38  E-value: 1.67e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   765 PERVKVYGPGVEKTglKANEPTYFTVDCSEAGQGDVSIGikcapgVVGPAEADIDFDIIKNDNDTFTVKYTPPGAGRYTI 844
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVE------VTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTV 72

                            90       100
                    ....*....|....*....|.
gi 1952979823   845 MVLFANQEIPASPFHIKVDPS 865
Cdd:smart00557   73 TVKFGGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 573-662 2.11e-26

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: 104.99  E-value: 2.11e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   573 QKVRAWGPGLKTGQVGKSADFVVEAIGTEVGTLGFSIEGPSQAKIECD--DKGDGSCDVRYWPTEPGEYAVHVICDDEDI 650
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEvkDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|..
gi 1952979823   651 RDSPFIAHIQPA 662
Cdd:smart00557   82 PGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1252-1348 2.39e-26

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: 104.99  E-value: 2.39e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1252 SGIKVSGPGVEPHGVLreVTTEFTVDARSltaTGGNHVTARVLNPSGAKTDTYVTDNGDGTYRVQYTAYEEGVHLVEVLY 1331
Cdd:smart00557    2 SKVKASGPGLEKGVVG--EPAEFTVDTRD---AGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 1952979823  1332 DDVAVPKSPFRVGVTEG 1348
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1063-1152 4.37e-26

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: 104.22  E-value: 4.37e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1063 PSKVCAYGPGLKGGLVGSPAPFSIDTKGAGTGGLGLTVEGP--CEAKIECQDNGDGSCAVSYLPTEPGEYTINILFAEAH 1140
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1952979823  1141 IPGSPFKATIRP 1152
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 868-964 4.45e-26

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: 104.22  E-value: 4.45e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   868 ASKVKAEGPGLNRTgvEVGKPTHFTVLTKGAGKAKLDVHFAGAAKGEAvrDFEIIDNHDYSYTVKYTAVQQGNMAVTVTY 947
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKV--PVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 1952979823   948 GGDPVPKSPFVVNVAPP 964
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1843-1930 6.11e-26

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 103.52  E-value: 6.11e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1843 AINSRHVSAYGPGLSHGMVNKPATFTIVTKDAGeGGLSLAVEGPS--KAEITCKDNKDGTCTVSYLPTAPGDYSIIVRFD 1920
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1952979823 1921 DKHIPGSPFT 1930
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2492-2582 1.81e-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: 102.30  E-value: 1.81e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  2492 PGLVSAYGPGLEGGTTGVSSEFIVNTLNAGSGALSVTIDGPS--KVQLDCRECPEGHV-VTYTPMAPGNYLIAIKYGGpQ 2568
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYtVSYTPTEPGDYTVTVKFGG-E 79

                            90
                    ....*....|....
gi 1952979823  2569 HIVGSPFKAKVTGP 2582
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1539-1628 2.16e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 101.98  E-value: 2.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1539 DASKVRASGPGLNASgiPASLPVEFTIDARDAGeGLLTVQILDPEGKPKKANIRDNGDGTYTVSYLPDMSGRYTITIKYG 1618
Cdd:pfam00630    3 DASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1952979823 1619 GDEIPYSPFR 1628
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1351-1440 2.21e-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: 102.30  E-value: 2.21e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1351 PTRVRAFGPGLESGLVNKANHFTVETRGAGTGGLGLAIEGPS--EAKMSCKDNKDGSCTVEYIPFTPGDYDVNITFGGRP 1428
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1952979823  1429 IPGSPFRVPVKD 1440
Cdd:smart00557   81 IPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
1153-1240 7.58e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 100.44  E-value: 7.58e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1153 VFDPSKVRASGPGLERGKAGEAATFTVDCSEAGEaELTIEILSDAGVKAEVLIHNNADGTYHITYSPAFPGTYTITIKYG 1232
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*...
gi 1952979823 1233 GHPVPKFP 1240
Cdd:pfam00630   80 GQHIPGSP 87
Filamin pfam00630
Filamin/ABP280 repeat;
2026-2112 7.80e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 100.44  E-value: 7.80e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 2026 GDASKVRVWGKGLSEGHTFQVAEFIVDTRNAGyGGLGLSIEGPS--KVDINCEDMEDGTCKVTYCPTEPGTYIINIKFAD 2103
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 1952979823 2104 KHVPGSPFT 2112
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1441-1531 3.88e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 98.52  E-value: 3.88e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1441 VVDPGKVKCSGPGLGAGVRARvPQTFTVDCSQAGrAPLQVAVLGPTGVAEPVEVLDNGGGTHTVHYTPATDGPYTVAVKY 1520
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGK-PAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 1952979823 1521 ADQEVPRSPFK 1531
Cdd:pfam00630   79 NGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2299-2385 5.62e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 98.13  E-value: 5.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 2299 GGAHKVRAGGTGLERGVAGVPAEFSIWTREAGaGGLSIAVEGPS--KAEIAFEDRKDGSCGVSYVVQEPGDYEVSIKFND 2376
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 1952979823 2377 EHIPDSPFV 2385
Cdd:pfam00630   81 QHIPGSPFK 89
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 41-141 2.37e-23

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: 96.62  E-value: 2.37e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823    41 NTFTRWCNEHLKCVGKR-LTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSID 119
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 1952979823   120 SKAIVDGNlKLILGLIWTLILH 141
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
1635-1724 3.11e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 95.82  E-value: 3.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1635 GDASKCLVTGACLGPRiQIGEETVITVDAKAAGkGKVTCTVSTPDGAELDVDVVENHDGTFDIYYTAPEPGKYVITIRFG 1714
Cdd:pfam00630    2 ADASKVKASGPGLEPG-VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1952979823 1715 GEHIPNSPFH 1724
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
666-756 3.14e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 95.82  E-value: 3.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  666 CFPDKVKAFGPGLEPTgcIVDKPAEFTIDARAAGkGDLNLYAQDADGCPVNIMVIPNGDGTFRCSYVPTKPIKHTIIISW 745
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 1952979823  746 GGVNVPKSPFR 756
Cdd:pfam00630   79 NGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1060-1147 4.37e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 95.43  E-value: 4.37e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1060 PPDPSKVCAYGPGLKGGLVGSPAPFSIDTKGAGTGGLGLtVEGP--CEAKIECQDNGDGSCAVSYLPTEPGEYTINILFA 1137
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVE-VTGPdgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1952979823 1138 EAHIPGSPFK 1147
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 968-1061 1.30e-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: 1.30e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   968 SKVKVQGLN-SKVAVGQEQAFSVNTRGAGGqGQLDVRMTSPSRRPIPCKVEPGGGAeTQAVRYMPPEEGPYKVDITYDGH 1046
Cdd:smart00557    2 SKVKASGPGlEKGVVGEPAEFTVDTRDAGG-GELEVEVTGPSGKKVPVEVKDNGDG-TYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....*
gi 1952979823  1047 PVPGSPFAVEgVLPP 1061
Cdd:smart00557   80 HIPGSPFTVK-VGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
374-465 4.13e-22

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 92.74  E-value: 4.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  374 GDANKVSARGPGLEPmgNVANKPTYFDIYTAGAGtGDVAVVIVDPQGRRDTVEValEDKGDNTFRCTYRPVMEGPHTVHV 453
Cdd:pfam00630    2 ADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEV--TDNGDGTYTVSYTPTEPGDYTVSV 76

                           90
                   ....*....|..
gi 1952979823  454 AFAGAPITRSPF 465
Cdd:pfam00630   77 KFNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
472-563 5.32e-22

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 92.35  E-value: 5.32e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  472 ACNPNACRASGRGLQPkgVRVKEVADFKVFTKGAGsGELKVTVKGPKGTEEPVKVREAGDGVFECEYYPVVPGKYVVTIT 551
Cdd:pfam00630    1 AADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 1952979823  552 WGGYAIPRSPFE 563
Cdd:pfam00630   78 FNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
275-366 6.04e-22

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 92.35  E-value: 6.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  275 NPKKAIAYGPGIEPHgnTVLQPAHFTVQTVDAGvGEVLVYIEDPEGHTEEAKVVPNNDknRTYAVSYVPKVAGLHKVTVL 354
Cdd:pfam00630    3 DASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGD--GTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 1952979823  355 FAGQNIERSPFE 366
Cdd:pfam00630   78 FNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
763-859 1.87e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 90.81  E-value: 1.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  763 SHPERVKVYGPGVEKTglKANEPTYFTVDCSEA-GQGDVSIgikcapgvVGPAEADIDFDIIKNDNDTFTVKYTPPGAGR 841
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAgGEGEVEV--------TGPDGSPVPVEVTDNGDGTYTVSYTPTEPGD 71

                           90
                   ....*....|....*...
gi 1952979823  842 YTIMVLFANQEIPASPFH 859
Cdd:pfam00630   72 YTVSVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1349-1435 8.86e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 88.89  E-value: 8.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1349 CDPTRVRAFGPGLESGLVNKANHFTVETRGAGTGGLGLaIEGPS--EAKMSCKDNKDGSCTVEYIPFTPGDYDVNITFGG 1426
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVE-VTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 1952979823 1427 RPIPGSPFR 1435
Cdd:pfam00630   81 QHIPGSPFK 89
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 37-144 4.08e-20

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 87.73  E-value: 4.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   37 KIQQNTFTRWCNEHLKC--VGKRLTDLQRDLSDGLRLIALLEVLSQKRM-YRKFHPRPnfrQMKLENVSVALEFLERE-H 112
Cdd:pfam00307    1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVdKKKLNKSE---FDKLENINLALDVAEKKlG 77

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1952979823  113 IKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 144
Cdd:pfam00307   78 VPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
Filamin pfam00630
Filamin/ABP280 repeat;
573-656 1.58e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.42  E-value: 1.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  573 QKVRAWGPGLKTGQVGKSADFVVEAIGtEVGTLGFSIEGPS--QAKIECDDKGDGSCDVRYWPTEPGEYAVHVICDDEDI 650
Cdd:pfam00630    5 SKVKASGPGLEPGVVGKPAEFTVDTRD-AGGEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHI 83


                   ....*.
gi 1952979823  651 RDSPFI 656
Cdd:pfam00630   84 PGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2619-2708 3.57e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 84.26  E-value: 3.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 2619 SSDASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMmVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWG 2698
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGE-VEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1952979823 2699 DESVPGSPFK 2708
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1248-1342 3.64e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 84.26  E-value: 3.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1248 AVDTSGIKVSGPGVEPHGVLREvtTEFTVDARslTATGGnhVTARVLNPSGAKTDTYVTDNGDGTYRVQYTAYEEGVHLV 1327
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKP--AEFTVDTR--DAGGE--GEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTV 74

                           90
                   ....*....|....*
gi 1952979823 1328 EVLYDDVAVPKSPFR 1342
Cdd:pfam00630   75 SVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2489-2576 7.71e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 83.49  E-value: 7.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 2489 AGDPGLVSAYGPGLEGGTTGVSSEFIVNTLNAGsGALSVTIDGPS--KVQLDCRECPEG-HVVTYTPMAPGNYLIAIKYG 2565
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|.
gi 1952979823 2566 GpQHIVGSPFK 2576
Cdd:pfam00630   80 G-QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
964-1053 1.24e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 82.72  E-value: 1.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  964 PLDLSKVKVQGLN-SKVAVGQEQAFSVNTRGAGGQGQLDVrmTSPSRRPIPCKVEPGGGAeTQAVRYMPPEEGPYKVDIT 1042
Cdd:pfam00630    1 AADASKVKASGPGlEPGVVGKPAEFTVDTRDAGGEGEVEV--TGPDGSPVPVEVTDNGDG-TYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 1952979823 1043 YDGHPVPGSPF 1053
Cdd:pfam00630   78 FNGQHIPGSPF 88
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 166-258 2.11e-18

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 82.36  E-value: 2.11e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   166 LLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDW---EAWDPNQPVENAREAMQQADDWLGVPQVIAPE 239
Cdd:smart00033    3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKkvaASLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90
                    ....*....|....*....
gi 1952979823   240 EIVDPNVDEHSVMTYLSQF 258
Cdd:smart00033   83 DLVEGPKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 160-258 4.28e-18

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 81.95  E-value: 4.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  160 QTPKQRLLGWIQNKV----PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWE-AWDPNQPVENAREAMQQADDWLGVPQ 234
Cdd:pfam00307    1 LELEKELLRWINSHLaeygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKLGVPK 80

                           90       100
                   ....*....|....*....|....*
gi 1952979823  235 V-IAPEEIVDPnvDEHSVMTYLSQF 258
Cdd:pfam00307   81 VlIEPEDLVEG--DNKSVLTYLASL 103
Filamin pfam00630
Filamin/ABP280 repeat;
867-958 5.67e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 80.80  E-value: 5.67e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  867 DASKVKAEGPGLNRtgVEVGKPTHFTVLTKGAGkAKLDVHFAGAAKGEAvrDFEIIDNHDYSYTVKYTAVQQGNMAVTVT 946
Cdd:pfam00630    3 DASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPV--PVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 1952979823  947 YGGDPVPKSPFV 958
Cdd:pfam00630   78 FNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2394-2480 1.02e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 80.03  E-value: 1.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 2394 DARRLTVTSLQETGLKVNQPASFAVQLNGARGVIDARVHTPSGAVEECYVSELDSDKHTIRFIPHENGVHSIDVKFNGAH 2473
Cdd:pfam00630    3 DASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQH 82


                   ....*..
gi 1952979823 2474 IPGSPFK 2480
Cdd:pfam00630   83 IPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1778-1842 8.87e-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: 74.95  E-value: 8.87e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1778 FTVQ-----KGELTGEVRMPSGKTARPNITDNKDGTITVRYAPTEKGLHQMGIKYDGNHIPGSPLQFYVD 1842
Cdd:smart00557   22 FTVDtrdagGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2231-2295 3.64e-15

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: 73.02  E-value: 3.64e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952979823  2231 EASSQDMTAQVTSPSGKMEAAEIVEGEDSAYSVRFVPQEMGPHTVTVKYRGQHVPGSPFQFTVGP 2295
Cdd:smart00557   28 DAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
1778-1836 4.22e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 64.23  E-value: 4.22e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952979823 1778 FTVQ----KGELTGEVRMPSGKTARPNITDNKDGTITVRYAPTEKGLHQMGIKYDGNHIPGSP 1836
Cdd:pfam00630   25 FTVDtrdaGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSP 87
Filamin pfam00630
Filamin/ABP280 repeat;
2225-2289 1.74e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 62.31  E-value: 1.74e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952979823 2225 TRQQEGEAssqdmTAQVTSPSGKMEAAEIVEGEDSAYSVRFVPQEMGPHTVTVKYRGQHVPGSPF 2289
Cdd:pfam00630   29 TRDAGGEG-----EVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
 
Name Accession Description Interval E-value
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 151-265 1.30e-89

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: 286.58  E-value: 1.30e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  151 DEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVENAREAMQQADDWL 230
Cdd:cd21314      1 DEDEEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPVQNAREAMQQADDWL 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1952979823  231 GVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKP 265
Cdd:cd21314     81 GVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKP 115
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 23-147 3.23e-85

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: 274.60  E-value: 3.23e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   23 PSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVS 102
Cdd:cd21310      1 PATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQMKLENVS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1952979823  103 VALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 147
Cdd:cd21310     81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 125
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 22-152 2.63e-77

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: 252.31  E-value: 2.63e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   22 MPSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENV 101
Cdd:cd21309      1 MPVTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFRQMQLENV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952979823  102 SVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDE 152
Cdd:cd21309     81 SVALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISMPVWEDE 131
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 161-263 5.81e-75

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: 244.21  E-value: 5.81e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  161 TPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEE 240
Cdd:cd21230      1 TPKQRLLGWIQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALENATEAMQLAEDWLGVPQLITPEE 80

                           90       100
                   ....*....|....*....|...
gi 1952979823  241 IVDPNVDEHSVMTYLSQFPKAKL 263
Cdd:cd21230     81 IINPNVDEMSVMTYLSQFPKAKL 103
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 21-147 1.53e-74

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: 244.22  E-value: 1.53e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   21 DMPSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLEN 100
Cdd:cd21308      3 EMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLEN 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1952979823  101 VSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 147
Cdd:cd21308     83 VSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 129
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
 154-263 4.49e-74

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: 241.92  E-value: 4.49e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  154 DEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVENAREAMQQADDWLGVP 233
Cdd:cd21313      1 DDDAKKQTPKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPQKPVDNAREAMQQADDWLGVP 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 1952979823  234 QVIAPEEIVDPNVDEHSVMTYLSQFPKAKL 263
Cdd:cd21313     81 QVITPEEIIHPDVDEHSVMTYLSQFPKAKL 110
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 35-142 3.31e-71

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: 233.53  E-value: 3.31e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   35 WKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIK 114
Cdd:cd21228      1 WKKIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRPTFRQMKLENVSVALEFLERESIK 80

                           90       100
                   ....*....|....*....|....*...
gi 1952979823  115 LVSIDSKAIVDGNLKLILGLIWTLILHY 142
Cdd:cd21228     81 LVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 150-263 4.61e-71

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: 233.54  E-value: 4.61e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  150 EDEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVENAREAMQQADDW 229
Cdd:cd21312      1 DEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDW 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1952979823  230 LGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKL 263
Cdd:cd21312     81 LGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKL 114
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 25-147 1.18e-69

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: 230.03  E-value: 1.18e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   25 TEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMyRKFHPRPNFRQMKLENVSVA 104
Cdd:cd21311      2 AERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKF-PKFNKRPTFRSQKLENVSVA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1952979823  105 LEFLER-EHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 147
Cdd:cd21311     81 LKFLEEdEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISMP 124
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 148-263 5.42e-67

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: 221.96  E-value: 5.42e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  148 MWEDEDD--EDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVENAREAMQQ 225
Cdd:cd21315      1 MWEGEDDgpDDGKGPTPKQRLLGWIQSKVPDLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAVKNAKEAMDL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1952979823  226 ADDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKL 263
Cdd:cd21315     81 AEDWLDVPQLIKPEEMVNPKVDELSMMTYLSQFPNAKL 118
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 35-142 4.17e-59

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: 199.24  E-value: 4.17e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   35 WKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIK 114
Cdd:cd21183      1 WKRIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYNRRPAFQQHYLENVSTALKFIEADHIK 80

                           90       100
                   ....*....|....*....|....*...
gi 1952979823  115 LVSIDSKAIVDGNLKLILGLIWTLILHY 142
Cdd:cd21183     81 LVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 161-262 6.45e-51

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: 175.50  E-value: 6.45e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  161 TPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEE 240
Cdd:cd21184      1 SGKSLLLEWVNSKIPEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMDIAEEELGIPKIITPED 80

                           90       100
                   ....*....|....*....|..
gi 1952979823  241 IVDPNVDEHSVMTYLSQFPKAK 262
Cdd:cd21184     81 MVSPNVDELSVMTYLSYFRNAK 102
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 35-144 1.93e-44

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: 157.06  E-value: 1.93e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   35 WKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLsQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIK 114
Cdd:cd21227      1 WVEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEIL-QGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 1952979823  115 LVSIDSKAIVDGNLKLILGLIWTLILHYSI 144
Cdd:cd21227     80 LVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 35-142 4.38e-39

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: 141.77  E-value: 4.38e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   35 WKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRkFHPRPNFRQMKLENVSVALEFLEREHIK 114
Cdd:cd21215      1 WVDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGR-YNKNPKMRVQKLENVNKALEFIKSRGVK 79

                           90       100
                   ....*....|....*....|....*...
gi 1952979823  115 LVSIDSKAIVDGNLKLILGLIWTLILHY 142
Cdd:cd21215     80 LTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 37-142 2.61e-37

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: 136.76  E-value: 2.61e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   37 KIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKfhpRPNFRQMKLENVSVALEFLEREHIKLV 116
Cdd:cd21188      2 AVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRE---RGRMRFHRLQNVQTALDFLKYRKIKLV 78

                           90       100
                   ....*....|....*....|....*.
gi 1952979823  117 SIDSKAIVDGNLKLILGLIWTLILHY 142
Cdd:cd21188     79 NIRAEDIVDGNPKLTLGLIWTIILHF 104
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 159-260 1.70e-35

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: 131.35  E-value: 1.70e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  159 KQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVENAREAMQQADDWLGVPQVIAP 238
Cdd:cd21229      1 KIPPKKLMLAWLQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSP 80

                           90       100
                   ....*....|....*....|..
gi 1952979823  239 EEIVDPNVDEHSVMTYLSQFPK 260
Cdd:cd21229     81 EDLSSPHLDELSGMTYLSYFMK 102
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1849-1935 1.02e-33

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: 125.79  E-value: 1.02e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1849 VSAYGPGLSHGMVNKPATFTIVTKDAGEGGLSLAVEGPS--KAEITCKDNKDGTCTVSYLPTAPGDYSIIVRFDDKHIPG 1926
Cdd:smart00557    4 VKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83


                    ....*....
gi 1952979823  1927 SPFTAKITG 1935
Cdd:smart00557   84 SPFTVKVGP 92
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 35-140 2.24e-33

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: 125.58  E-value: 2.24e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   35 WKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKfhPRPNFRQMKLENVSVALEFLEREHIK 114
Cdd:cd21214      2 WEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKP--ERGKMRFHKIANVNKALDFIASKGVK 79

                           90       100
                   ....*....|....*....|....*.
gi 1952979823  115 LVSIDSKAIVDGNLKLILGLIWTLIL 140
Cdd:cd21214     80 LVSIGAEEIVDGNLKMTLGMIWTIIL 105
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1156-1248 6.26e-33

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: 123.48  E-value: 6.26e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1156 PSKVRASGPGLERGKAGEAATFTVDCSEAGEAELTIEILSDAGVKAEVLIHNNADGTYHITYSPAFPGTYTITIKYGGHP 1235
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 1952979823  1236 VPKFPTRVHVQPA 1248
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1444-1537 3.29e-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: 3.29e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1444 PGKVKCSGPGLGAGvRARVPQTFTVDCSQAGRAPLQVAVLGPTGVAEPVEVLDNGGGTHTVHYTPATDGPYTVAVKYADQ 1523
Cdd:smart00557    1 ASKVKASGPGLEKG-VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 1952979823  1524 EVPRSPFKIKVLPA 1537
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2028-2117 6.31e-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: 120.79  E-value: 6.31e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  2028 ASKVRVWGKGLSEGHTFQVAEFIVDTRNAGYGGLGLSIEGPS--KVDINCEDMEDGTCKVTYCPTEPGTYIINIKFADKH 2105
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1952979823  2106 VPGSPFTVKVTG 2117
Cdd:smart00557   81 IPGSPFTVKVGP 92
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 27-140 1.09e-31

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: 120.93  E-value: 1.09e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   27 KDLAEDApwKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMyrkfhPRPNFRQMK---LENVSV 103
Cdd:cd21246      7 KALADER--EAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERL-----PKPTKGKMRihcLENVDK 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1952979823  104 ALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLIL 140
Cdd:cd21246     80 ALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 668-762 2.48e-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: 119.25  E-value: 2.48e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   668 PDKVKAFGPGLEPTgcIVDKPAEFTIDARAAGKGDLNLYAQDADGCPVNIMVIPNGDGTFRCSYVPTKPIKHTIIISWGG 747
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 1952979823   748 VNVPKSPFRVNVGEG 762
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1540-1634 3.14e-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: 118.86  E-value: 3.14e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1540 ASKVRASGPGLNasGIPASLPVEFTIDARDAGEGLLTVQILDPEGKPKKANIRDNGDGTYTVSYLPDMSGRYTITIKYGG 1619
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 1952979823  1620 DEIPYSPFRIHALPT 1634
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2301-2389 4.53e-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: 4.53e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  2301 AHKVRAGGTGLERGVAGVPAEFSIWTREAGAGGLSIAVEGPS--KAEIAFEDRKDGSCGVSYVVQEPGDYEVSIKFNDEH 2378
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 1952979823  2379 IPDSPFVVPVA 2389
Cdd:smart00557   81 IPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 475-568 7.23e-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: 117.70  E-value: 7.23e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   475 PNACRASGRGLQPKgvRVKEVADFKVFTKGAGSGELKVTVKGPKGTEEPVKVREAGDGVFECEYYPVVPGKYVVTITWGG 554
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....
gi 1952979823   555 YAIPRSPFEVQVSP 568
Cdd:smart00557   79 EHIPGSPFTVKVGP 92
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 38-140 2.62e-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: 117.01  E-value: 2.62e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   38 IQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMyrkfhPRPN---FRQMKLENVSVALEFLeREHIK 114
Cdd:cd21193     16 IQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKL-----GKPNrgrLRVQKIENVNKALAFL-KTKVR 89

                           90       100
                   ....*....|....*....|....*.
gi 1952979823  115 LVSIDSKAIVDGNLKLILGLIWTLIL 140
Cdd:cd21193     90 LENIGAEDIVDGNPRLILGLIWTIIL 115
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
35-261 4.58e-30

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 128.91  E-value: 4.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   35 WKKIQQNTFTRWCNEHLKCVG-KRLTDLQRDLSDGLRLIALLEVLSQKRMYRkFHPRPNFRQMKLENVSVALEFLEREHI 113
Cdd:COG5069      6 WQKVQKKTFTKWTNEKLISGGqKEFGDLDTDLKDGVKLAQLLEALQKDNAGE-YNETPETRIHVMENVSGRLEFIKGKGV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  114 KLVSIDSKAIVDGNLKLILGLIWTLILHYSISmpmwedeDDEDARKQTPKQRLLGW----IQNKVPQLPITNFNRDWQDG 189
Cdd:COG5069     85 KLFNIGPQDIVDGNPKLILGLIWSLISRLTIA-------TINEEGELTKHINLLLWcdedTGGYKPEVDTFDFFRSWRDG 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952979823  190 KALGALVDNCAP-GLCPDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEEIVDPNV-DEHSVMTYLSQFPKA 261
Cdd:COG5069    158 LAFSALIHDSRPdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSWYIIR 231
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 37-145 1.35e-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: 115.47  E-value: 1.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   37 KIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKfhpRPNFRQMKLENVSVALEFLEREHIKLV 116
Cdd:cd21236     16 KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE---KGRMRFHRLQNVQIALDYLKRRQVKLV 92

                           90       100
                   ....*....|....*....|....*....
gi 1952979823  117 SIDSKAIVDGNLKLILGLIWTLILHYSIS 145
Cdd:cd21236     93 NIRNDDITDGNPKLTLGLIWTIILHFQIS 121
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 276-372 2.21e-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: 113.47  E-value: 2.21e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   276 PKKAIAYGPGIEPHgnTVLQPAHFTVQTVDAGVGEVLVYIEDPEGHTEEAKVVPNNDknRTYAVSYVPKVAGLHKVTVLF 355
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGD--GTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 1952979823   356 AGQNIERSPFEVNVGMA 372
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2622-2711 2.32e-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: 113.47  E-value: 2.32e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  2622 ASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMMVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWGDES 2701
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 1952979823  2702 VPGSPFKVNV 2711
Cdd:smart00557   81 IPGSPFTVKV 90
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 38-142 4.13e-28

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: 110.55  E-value: 4.13e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   38 IQQNTFTRWCNEHLKCVGKRL-TDLQRDLSDGLRLIALLEVLSQKRMYRKfhpRPNFRQMKLENVSVALEFLEREHIKLV 116
Cdd:cd21186      2 VQKKTFTKWINSQLSKANKPPiKDLFEDLRDGTRLLALLEVLTGKKLKPE---KGRMRVHHLNNVNRALQVLEQNNVKLV 78

                           90       100
                   ....*....|....*....|....*.
gi 1952979823  117 SIDSKAIVDGNLKLILGLIWTLILHY 142
Cdd:cd21186     79 NISSNDIVDGNPKLTLGLVWSIILHW 104
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 37-154 8.22e-28

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: 110.11  E-value: 8.22e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   37 KIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKfhpRPNFRQMKLENVSVALEFLEREHIKLV 116
Cdd:cd21235      5 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 81

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1952979823  117 SIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDEDD 154
Cdd:cd21235     82 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 37-144 1.65e-27

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: 109.00  E-value: 1.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   37 KIQQNTFTRWCNEHL-KCVGK-RLTDLQRDLSDGLRLIALLEVLSQKRMyrkfhPRPNFRQMK----LENVSVALEFLER 110
Cdd:cd21241      4 RVQKKTFTNWINSYLaKRKPPmKVEDLFEDIKDGTKLLALLEVLSGEKL-----PCEKGRRLKrvhfLSNINTALKFLES 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1952979823  111 EHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 144
Cdd:cd21241     79 KKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 376-472 4.81e-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: 106.92  E-value: 4.81e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   376 ANKVSARGPGLEPmgNVANKPTYFDIYTAGAGTGDVAVVIVDPQGRRdtVEVALEDKGDNTFRCTYRPVMEGPHTVHVAF 455
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 1952979823   456 AGAPITRSPFPVHVAEA 472
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 37-145 4.82e-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: 107.81  E-value: 4.82e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   37 KIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKfhpRPNFRQMKLENVSVALEFLEREHIKLV 116
Cdd:cd21237      5 RVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPRE---KGRMRFHRLQNVQIALDFLKQRQVKLV 81

                           90       100
                   ....*....|....*....|....*....
gi 1952979823  117 SIDSKAIVDGNLKLILGLIWTLILHYSIS 145
Cdd:cd21237     82 NIRNDDITDGNPKLTLGLIWTIILHFQIS 110
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1637-1725 1.06e-26

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: 105.76  E-value: 1.06e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1637 ASKCLVTGACLGPrIQIGEETVITVDAKAAGKGKVTCTVSTPDGAELDVDVVENHDGTFDIYYTAPEPGKYVITIRFGGE 1716
Cdd:smart00557    1 ASKVKASGPGLEK-GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79


                    ....*....
gi 1952979823  1717 HIPNSPFHV 1725
Cdd:smart00557   80 HIPGSPFTV 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 765-865 1.67e-26

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: 105.38  E-value: 1.67e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   765 PERVKVYGPGVEKTglKANEPTYFTVDCSEAGQGDVSIGikcapgVVGPAEADIDFDIIKNDNDTFTVKYTPPGAGRYTI 844
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVE------VTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTV 72

                            90       100
                    ....*....|....*....|.
gi 1952979823   845 MVLFANQEIPASPFHIKVDPS 865
Cdd:smart00557   73 TVKFGGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 573-662 2.11e-26

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: 104.99  E-value: 2.11e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   573 QKVRAWGPGLKTGQVGKSADFVVEAIGTEVGTLGFSIEGPSQAKIECD--DKGDGSCDVRYWPTEPGEYAVHVICDDEDI 650
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEvkDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|..
gi 1952979823   651 RDSPFIAHIQPA 662
Cdd:smart00557   82 PGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1252-1348 2.39e-26

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: 104.99  E-value: 2.39e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1252 SGIKVSGPGVEPHGVLreVTTEFTVDARSltaTGGNHVTARVLNPSGAKTDTYVTDNGDGTYRVQYTAYEEGVHLVEVLY 1331
Cdd:smart00557    2 SKVKASGPGLEKGVVG--EPAEFTVDTRD---AGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 1952979823  1332 DDVAVPKSPFRVGVTEG 1348
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1063-1152 4.37e-26

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: 104.22  E-value: 4.37e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1063 PSKVCAYGPGLKGGLVGSPAPFSIDTKGAGTGGLGLTVEGP--CEAKIECQDNGDGSCAVSYLPTEPGEYTINILFAEAH 1140
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1952979823  1141 IPGSPFKATIRP 1152
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 868-964 4.45e-26

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: 104.22  E-value: 4.45e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   868 ASKVKAEGPGLNRTgvEVGKPTHFTVLTKGAGKAKLDVHFAGAAKGEAvrDFEIIDNHDYSYTVKYTAVQQGNMAVTVTY 947
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKV--PVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 1952979823   948 GGDPVPKSPFVVNVAPP 964
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1843-1930 6.11e-26

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 103.52  E-value: 6.11e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1843 AINSRHVSAYGPGLSHGMVNKPATFTIVTKDAGeGGLSLAVEGPS--KAEITCKDNKDGTCTVSYLPTAPGDYSIIVRFD 1920
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1952979823 1921 DKHIPGSPFT 1930
Cdd:pfam00630   80 GQHIPGSPFK 89
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 38-144 1.06e-25

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: 103.81  E-value: 1.06e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   38 IQQNTFTRWCNEHLKCVGKRLT--DLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNfRQMKLENVSVALEFLEREHIKL 115
Cdd:cd21191      5 VQKRTFTRWINLHLEKCNPPLEvkDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSH-RIFRLNNIAKALKFLEDSNVKL 83

                           90       100
                   ....*....|....*....|....*....
gi 1952979823  116 VSIDSKAIVDGNLKLILGLIWTLILHYSI 144
Cdd:cd21191     84 VSIDAAEIADGNPSLVLGLIWNIILFFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2492-2582 1.81e-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: 102.30  E-value: 1.81e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  2492 PGLVSAYGPGLEGGTTGVSSEFIVNTLNAGSGALSVTIDGPS--KVQLDCRECPEGHV-VTYTPMAPGNYLIAIKYGGpQ 2568
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYtVSYTPTEPGDYTVTVKFGG-E 79

                            90
                    ....*....|....
gi 1952979823  2569 HIVGSPFKAKVTGP 2582
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1539-1628 2.16e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 101.98  E-value: 2.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1539 DASKVRASGPGLNASgiPASLPVEFTIDARDAGeGLLTVQILDPEGKPKKANIRDNGDGTYTVSYLPDMSGRYTITIKYG 1618
Cdd:pfam00630    3 DASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1952979823 1619 GDEIPYSPFR 1628
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1351-1440 2.21e-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: 102.30  E-value: 2.21e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1351 PTRVRAFGPGLESGLVNKANHFTVETRGAGTGGLGLAIEGPS--EAKMSCKDNKDGSCTVEYIPFTPGDYDVNITFGGRP 1428
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 1952979823  1429 IPGSPFRVPVKD 1440
Cdd:smart00557   81 IPGSPFTVKVGP 92
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 27-140 3.27e-25

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: 103.57  E-value: 3.27e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   27 KDLAEDApwKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMyrkfhPRPNFRQMK---LENVSV 103
Cdd:cd21318     29 KALADER--EAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQL-----PKPTRGRMRihsLENVDK 101

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1952979823  104 ALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLIL 140
Cdd:cd21318    102 ALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 27-140 4.79e-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: 102.82  E-value: 4.79e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   27 KDLAEDApwKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMyrkfhPRPNFRQMK---LENVSV 103
Cdd:cd21317     22 KALADER--EAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQL-----PKPTKGRMRihcLENVDK 94

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1952979823  104 ALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLIL 140
Cdd:cd21317     95 ALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
Filamin pfam00630
Filamin/ABP280 repeat;
1153-1240 7.58e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 100.44  E-value: 7.58e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1153 VFDPSKVRASGPGLERGKAGEAATFTVDCSEAGEaELTIEILSDAGVKAEVLIHNNADGTYHITYSPAFPGTYTITIKYG 1232
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*...
gi 1952979823 1233 GHPVPKFP 1240
Cdd:pfam00630   80 GQHIPGSP 87
Filamin pfam00630
Filamin/ABP280 repeat;
2026-2112 7.80e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 100.44  E-value: 7.80e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 2026 GDASKVRVWGKGLSEGHTFQVAEFIVDTRNAGyGGLGLSIEGPS--KVDINCEDMEDGTCKVTYCPTEPGTYIINIKFAD 2103
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 1952979823 2104 KHVPGSPFT 2112
Cdd:pfam00630   81 QHIPGSPFK 89
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 35-143 1.51e-24

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: 100.30  E-value: 1.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   35 WKKIQQNTFTRWCNEHL-KCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLERE-H 112
Cdd:cd21225      1 WEKVQIKAFTAWVNSVLeKRGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQMIQNLHLAMLFIEEDlK 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1952979823  113 IKLVSIDSKAIVDGNLKLILGLIWTLILHYS 143
Cdd:cd21225     81 IRVQGIGAEDFVDNNKKLILGLLWTLYRKYR 111
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 36-144 3.36e-24

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: 99.57  E-value: 3.36e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   36 KKIQQNTFTRWCNEHLKcvgKR-----LTDLQRDLSDGLRLIALLEVLSQKRMYRKfHPRPNFRQMKLENVSVALEFLER 110
Cdd:cd21190      3 ERVQKKTFTNWINSHLA---KLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIE-SGRVLQRAHKLSNIRNALDFLTK 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1952979823  111 EHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 144
Cdd:cd21190     79 RCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
Filamin pfam00630
Filamin/ABP280 repeat;
1441-1531 3.88e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 98.52  E-value: 3.88e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1441 VVDPGKVKCSGPGLGAGVRARvPQTFTVDCSQAGrAPLQVAVLGPTGVAEPVEVLDNGGGTHTVHYTPATDGPYTVAVKY 1520
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGK-PAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 1952979823 1521 ADQEVPRSPFK 1531
Cdd:pfam00630   79 NGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2299-2385 5.62e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 98.13  E-value: 5.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 2299 GGAHKVRAGGTGLERGVAGVPAEFSIWTREAGaGGLSIAVEGPS--KAEIAFEDRKDGSCGVSYVVQEPGDYEVSIKFND 2376
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 1952979823 2377 EHIPDSPFV 2385
Cdd:pfam00630   81 QHIPGSPFK 89
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 27-140 1.22e-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: 99.35  E-value: 1.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   27 KDLAEDApwKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMyrkfhPRPNFRQMK---LENVSV 103
Cdd:cd21316     44 KALADER--EAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERL-----PKPTKGRMRihcLENVDK 116

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1952979823  104 ALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLIL 140
Cdd:cd21316    117 ALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 41-141 2.37e-23

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: 96.62  E-value: 2.37e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823    41 NTFTRWCNEHLKCVGKR-LTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSID 119
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 1952979823   120 SKAIVDGNlKLILGLIWTLILH 141
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
1635-1724 3.11e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 95.82  E-value: 3.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1635 GDASKCLVTGACLGPRiQIGEETVITVDAKAAGkGKVTCTVSTPDGAELDVDVVENHDGTFDIYYTAPEPGKYVITIRFG 1714
Cdd:pfam00630    2 ADASKVKASGPGLEPG-VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1952979823 1715 GEHIPNSPFH 1724
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
666-756 3.14e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 95.82  E-value: 3.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  666 CFPDKVKAFGPGLEPTgcIVDKPAEFTIDARAAGkGDLNLYAQDADGCPVNIMVIPNGDGTFRCSYVPTKPIKHTIIISW 745
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 1952979823  746 GGVNVPKSPFR 756
Cdd:pfam00630   79 NGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1060-1147 4.37e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 95.43  E-value: 4.37e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1060 PPDPSKVCAYGPGLKGGLVGSPAPFSIDTKGAGTGGLGLtVEGP--CEAKIECQDNGDGSCAVSYLPTEPGEYTINILFA 1137
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVE-VTGPdgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1952979823 1138 EAHIPGSPFK 1147
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 968-1061 1.30e-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: 1.30e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   968 SKVKVQGLN-SKVAVGQEQAFSVNTRGAGGqGQLDVRMTSPSRRPIPCKVEPGGGAeTQAVRYMPPEEGPYKVDITYDGH 1046
Cdd:smart00557    2 SKVKASGPGlEKGVVGEPAEFTVDTRDAGG-GELEVEVTGPSGKKVPVEVKDNGDG-TYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....*
gi 1952979823  1047 PVPGSPFAVEgVLPP 1061
Cdd:smart00557   80 HIPGSPFTVK-VGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
374-465 4.13e-22

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 92.74  E-value: 4.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  374 GDANKVSARGPGLEPmgNVANKPTYFDIYTAGAGtGDVAVVIVDPQGRRDTVEValEDKGDNTFRCTYRPVMEGPHTVHV 453
Cdd:pfam00630    2 ADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEV--TDNGDGTYTVSYTPTEPGDYTVSV 76

                           90
                   ....*....|..
gi 1952979823  454 AFAGAPITRSPF 465
Cdd:pfam00630   77 KFNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
472-563 5.32e-22

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 92.35  E-value: 5.32e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  472 ACNPNACRASGRGLQPkgVRVKEVADFKVFTKGAGsGELKVTVKGPKGTEEPVKVREAGDGVFECEYYPVVPGKYVVTIT 551
Cdd:pfam00630    1 AADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 1952979823  552 WGGYAIPRSPFE 563
Cdd:pfam00630   78 FNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
275-366 6.04e-22

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 92.35  E-value: 6.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  275 NPKKAIAYGPGIEPHgnTVLQPAHFTVQTVDAGvGEVLVYIEDPEGHTEEAKVVPNNDknRTYAVSYVPKVAGLHKVTVL 354
Cdd:pfam00630    3 DASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGD--GTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 1952979823  355 FAGQNIERSPFE 366
Cdd:pfam00630   78 FNGQHIPGSPFK 89
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 38-144 1.36e-21

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: 91.91  E-value: 1.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   38 IQQNTFTRWCNEHLKCVGKR-LTDLQRDLSDGLRLIALLEVLSQKRMYRKfhpRPNFRQMKLENVSVALEFLEREHIKLV 116
Cdd:cd21231      6 VQKKTFTKWINAQFAKFGKPpIEDLFTDLQDGRRLLELLEGLTGQKLVKE---KGSTRVHALNNVNKALQVLQKNNVDLV 82

                           90       100
                   ....*....|....*....|....*...
gi 1952979823  117 SIDSKAIVDGNLKLILGLIWTLILHYSI 144
Cdd:cd21231     83 NIGSADIVDGNHKLTLGLIWSIILHWQV 110
Filamin pfam00630
Filamin/ABP280 repeat;
763-859 1.87e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 90.81  E-value: 1.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  763 SHPERVKVYGPGVEKTglKANEPTYFTVDCSEA-GQGDVSIgikcapgvVGPAEADIDFDIIKNDNDTFTVKYTPPGAGR 841
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAgGEGEVEV--------TGPDGSPVPVEVTDNGDGTYTVSYTPTEPGD 71

                           90
                   ....*....|....*...
gi 1952979823  842 YTIMVLFANQEIPASPFH 859
Cdd:pfam00630   72 YTVSVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1349-1435 8.86e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 88.89  E-value: 8.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1349 CDPTRVRAFGPGLESGLVNKANHFTVETRGAGTGGLGLaIEGPS--EAKMSCKDNKDGSCTVEYIPFTPGDYDVNITFGG 1426
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVE-VTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 1952979823 1427 RPIPGSPFR 1435
Cdd:pfam00630   81 QHIPGSPFK 89
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 38-144 2.66e-20

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: 88.35  E-value: 2.66e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   38 IQQNTFTRWCNEHLkcvGKR-----LTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPnFRQMKleNVSVALEFLEREH 112
Cdd:cd21242      5 TQKRTFTNWINSQL---AKHsppsvVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNV-FQCRS--NIETALSFLKNKS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1952979823  113 IKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 144
Cdd:cd21242     79 IKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 37-144 4.08e-20

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 87.73  E-value: 4.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   37 KIQQNTFTRWCNEHLKC--VGKRLTDLQRDLSDGLRLIALLEVLSQKRM-YRKFHPRPnfrQMKLENVSVALEFLERE-H 112
Cdd:pfam00307    1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVdKKKLNKSE---FDKLENINLALDVAEKKlG 77

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1952979823  113 IKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 144
Cdd:pfam00307   78 VPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 167-258 1.15e-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: 86.20  E-value: 1.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  167 LGWIQNKVPQLPITNFNRDWQDGKALGALVDNCApGLCPDWEAWDPNQPVENAREAMQQADDwLGVPQVIAPEEIVDPNV 246
Cdd:cd21185      7 LRWVRQLLPDVDVNNFTTDWNDGRLLCGLVNALG-GSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEV 84

                           90
                   ....*....|..
gi 1952979823  247 DEHSVMTYLSQF 258
Cdd:cd21185     85 EHLGIMAYAAQL 96
Filamin pfam00630
Filamin/ABP280 repeat;
573-656 1.58e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.42  E-value: 1.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  573 QKVRAWGPGLKTGQVGKSADFVVEAIGtEVGTLGFSIEGPS--QAKIECDDKGDGSCDVRYWPTEPGEYAVHVICDDEDI 650
Cdd:pfam00630    5 SKVKASGPGLEPGVVGKPAEFTVDTRD-AGGEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHI 83


                   ....*.
gi 1952979823  651 RDSPFI 656
Cdd:pfam00630   84 PGSPFK 89
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 43-142 1.94e-19

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: 85.71  E-value: 1.94e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   43 FTRWCNEHLKCVGKRL--TDLQRDLSDGLRLIALLEVLSQKRMyRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDS 120
Cdd:cd21212      5 YTDWANHYLEKGGHKRiiTDLQKDLGDGLTLVNLIEAVAGEKV-PGIHSRPKTRAQKLENIQACLQFLAALGVDVQGITA 83

                           90       100
                   ....*....|....*....|..
gi 1952979823  121 KAIVDGNLKLILGLIWTLILHY 142
Cdd:cd21212     84 EDIVDGNLKAILGLFFSLSRYK 105
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 38-144 2.64e-19

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: 85.97  E-value: 2.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   38 IQQNTFTRWCNEHLKCVGKR--LTDLQRDLSDGLRLIALLEVLSQKRMyrkfhPRPNFRQMK---LENVSVALEFLeREH 112
Cdd:cd21247     20 MQKKTFTKWMNNVFSKNGAKieITDIYTELKDGIHLLRLLELISGEQL-----PRPSRGKMRvhfLENNSKAITFL-KTK 93

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1952979823  113 IKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 144
Cdd:cd21247     94 VPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
Filamin pfam00630
Filamin/ABP280 repeat;
2619-2708 3.57e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 84.26  E-value: 3.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 2619 SSDASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMmVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWG 2698
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGE-VEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 1952979823 2699 DESVPGSPFK 2708
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1248-1342 3.64e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 84.26  E-value: 3.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 1248 AVDTSGIKVSGPGVEPHGVLREvtTEFTVDARslTATGGnhVTARVLNPSGAKTDTYVTDNGDGTYRVQYTAYEEGVHLV 1327
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKP--AEFTVDTR--DAGGE--GEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTV 74

                           90
                   ....*....|....*
gi 1952979823 1328 EVLYDDVAVPKSPFR 1342
Cdd:pfam00630   75 SVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2489-2576 7.71e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 83.49  E-value: 7.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 2489 AGDPGLVSAYGPGLEGGTTGVSSEFIVNTLNAGsGALSVTIDGPS--KVQLDCRECPEG-HVVTYTPMAPGNYLIAIKYG 2565
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|.
gi 1952979823 2566 GpQHIVGSPFK 2576
Cdd:pfam00630   80 G-QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
964-1053 1.24e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 82.72  E-value: 1.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  964 PLDLSKVKVQGLN-SKVAVGQEQAFSVNTRGAGGQGQLDVrmTSPSRRPIPCKVEPGGGAeTQAVRYMPPEEGPYKVDIT 1042
Cdd:pfam00630    1 AADASKVKASGPGlEPGVVGKPAEFTVDTRDAGGEGEVEV--TGPDGSPVPVEVTDNGDG-TYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 1952979823 1043 YDGHPVPGSPF 1053
Cdd:pfam00630   78 FNGQHIPGSPF 88
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 166-258 2.11e-18

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 82.36  E-value: 2.11e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   166 LLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDW---EAWDPNQPVENAREAMQQADDWLGVPQVIAPE 239
Cdd:smart00033    3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKkvaASLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90
                    ....*....|....*....
gi 1952979823   240 EIVDPNVDEHSVMTYLSQF 258
Cdd:smart00033   83 DLVEGPKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 160-258 4.28e-18

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 81.95  E-value: 4.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  160 QTPKQRLLGWIQNKV----PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWE-AWDPNQPVENAREAMQQADDWLGVPQ 234
Cdd:pfam00307    1 LELEKELLRWINSHLaeygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKLGVPK 80

                           90       100
                   ....*....|....*....|....*
gi 1952979823  235 V-IAPEEIVDPnvDEHSVMTYLSQF 258
Cdd:pfam00307   81 VlIEPEDLVEG--DNKSVLTYLASL 103
Filamin pfam00630
Filamin/ABP280 repeat;
867-958 5.67e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 80.80  E-value: 5.67e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  867 DASKVKAEGPGLNRtgVEVGKPTHFTVLTKGAGkAKLDVHFAGAAKGEAvrDFEIIDNHDYSYTVKYTAVQQGNMAVTVT 946
Cdd:pfam00630    3 DASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPV--PVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 1952979823  947 YGGDPVPKSPFV 958
Cdd:pfam00630   78 FNGQHIPGSPFK 89
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 38-144 7.78e-18

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: 81.21  E-value: 7.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   38 IQQNTFTRWCNEHLKCVGK-RLTDLQRDLSDGLRLIALLEVLSQKRMYRKfhpRPNFRQMKLENVSVALEFLEREHIKLV 116
Cdd:cd21232      2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKE---RGSTRVHALNNVNRVLQVLHQNNVELV 78

                           90       100
                   ....*....|....*....|....*...
gi 1952979823  117 SIDSKAIVDGNLKLILGLIWTLILHYSI 144
Cdd:cd21232     79 NIGGTDIVDGNHKLTLGLLWSIILHWQV 106
Filamin pfam00630
Filamin/ABP280 repeat;
2394-2480 1.02e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 80.03  E-value: 1.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823 2394 DARRLTVTSLQETGLKVNQPASFAVQLNGARGVIDARVHTPSGAVEECYVSELDSDKHTIRFIPHENGVHSIDVKFNGAH 2473
Cdd:pfam00630    3 DASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQH 82


                   ....*..
gi 1952979823 2474 IPGSPFK 2480
Cdd:pfam00630   83 IPGSPFK 89
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
 159-261 4.63e-16

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: 76.20  E-value: 4.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  159 KQTPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQV 235
Cdd:cd21243      3 KGGAKKALLKWVQNAAAKrfgIEVKDFGPSWRDGVAFNAIIHSIRPDLV-DMESLKRRSNRENLETAFTVAEKELGIPRL 81

                           90       100
                   ....*....|....*....|....*.
gi 1952979823  236 IAPEEIVDPNVDEHSVMTYLSQFPKA 261
Cdd:cd21243     82 LDPEDVDVDKPDEKSIMTYVAQFLKK 107
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1778-1842 8.87e-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: 74.95  E-value: 8.87e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  1778 FTVQ-----KGELTGEVRMPSGKTARPNITDNKDGTITVRYAPTEKGLHQMGIKYDGNHIPGSPLQFYVD 1842
Cdd:smart00557   22 FTVDtrdagGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 28-142 1.84e-15

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: 74.93  E-value: 1.84e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   28 DLAEDAPWK--KIQQnTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQkrmY----RKFHPRPNFRQMKLENV 101
Cdd:cd21222      5 DLFDEAPEKlaEVKE-LLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEG---FfvplHEYHLTPSTDDEKLHNV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1952979823  102 SVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHY 142
Cdd:cd21222     81 KLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 40-140 3.39e-15

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 73.53  E-value: 3.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   40 QNTFTRWCNEHLKCVGKRL-TDLQRDLSDGLRLIALLEVLSQKRMyRKFHPRPNFRQMKLENVSVALEFLEREHI-KLVS 117
Cdd:cd00014      1 EEELLKWINEVLGEELPVSiTDLFESLRDGVLLCKLINKLSPGSI-PKINKKPKSPFKKRENINLFLNACKKLGLpELDL 79

                           90       100
                   ....*....|....*....|....
gi 1952979823  118 IDSKAIV-DGNLKLILGLIWTLIL 140
Cdd:cd00014     80 FEPEDLYeKGNLKKVLGTLWALAL 103
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 163-258 3.55e-15

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: 73.60  E-value: 3.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  163 KQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPE 239
Cdd:cd21194      4 KDALLLWCQRKTagyPGVNIQNFTTSWRDGLAFNALIHAHRPDLI-DYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAE 82

                           90
                   ....*....|....*....
gi 1952979823  240 EIVDPNVDEHSVMTYLSQF 258
Cdd:cd21194     83 DVDVARPDEKSIMTYVASY 101
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2231-2295 3.64e-15

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: 73.02  E-value: 3.64e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952979823  2231 EASSQDMTAQVTSPSGKMEAAEIVEGEDSAYSVRFVPQEMGPHTVTVKYRGQHVPGSPFQFTVGP 2295
Cdd:smart00557   28 DAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGP 92
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 161-261 4.47e-15

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: 73.55  E-value: 4.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  161 TPKQRLLGWIQNKVP---QLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIA 237
Cdd:cd21216     10 SAKEGLLLWCQRKTApykNVNVQNFHTSWKDGLAFCALIHRHRPDLL-DYDKLRKDDPRENLNLAFDVAEKHLDIPKMLD 88

                           90       100
                   ....*....|....*....|....*
gi 1952979823  238 PEEIVD-PNVDEHSVMTYLSQFPKA 261
Cdd:cd21216     89 AEDIVNtPRPDERSVMTYVSCYYHA 113
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 161-259 4.59e-15

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: 73.19  E-value: 4.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  161 TPKQRLLGWIQ---NKVPQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIA 237
Cdd:cd21189      1 SAKEALLLWARrttEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLI-DFRSVRNQSNRENLENAFNVAEKEFGVTRLLD 79

                           90       100
                   ....*....|....*....|....*.
gi 1952979823  238 PEEIVDPNVDEHSVMTYLSQ----FP 259
Cdd:cd21189     80 PEDVDVPEPDEKSIITYVSSlydvFP 105
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 39-142 2.63e-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: 71.17  E-value: 2.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   39 QQNTFTRWCNEHL-KCVGKRL-TDLQRDLSDGLRLIALLEVLSQKRMyRKFHPRPNFRQMKLENVSVALEFLEREHIKLV 116
Cdd:cd21213      1 QLQAYVAWVNSQLkKRPGIRPvQDLRRDLRDGVALAQLIEILAGEKL-PGIDWNPTTDAERKENVEKVLQFMASKRIRMH 79

                           90       100
                   ....*....|....*....|....*.
gi 1952979823  117 SIDSKAIVDGNLKLILGLIWTLILHY 142
Cdd:cd21213     80 QTSAKDIVDGNLKAIMRLILALAAHF 105
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 166-258 1.10e-13

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: 69.43  E-value: 1.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  166 LLGWIQNKVPQ--LPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDpNQPVENAREAMQQADDWLGVPQVIAPEEIVD 243
Cdd:cd21245      8 LLNWVQRRTRKygVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALE-KSPRENLEDAFRIAQESLGIPPLLEPEDVMV 86

                           90
                   ....*....|....*
gi 1952979823  244 PNVDEHSVMTYLSQF 258
Cdd:cd21245     87 DSPDEQSIMTYVAQF 101
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
 160-258 1.27e-13

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: 69.26  E-value: 1.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  160 QTPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVI 236
Cdd:cd21319      4 RSAKDALLLWCQMKTagyPNVNVTNFTSSWKDGLAFNALIHKHRPDLV-DFGKLKKSNARHNLEHAFNVAERQLGITKLL 82

                           90       100
                   ....*....|....*....|..
gi 1952979823  237 APEEIVDPNVDEHSVMTYLSQF 258
Cdd:cd21319     83 DPEDVFTENPDEKSIITYVVAF 104
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
 159-258 1.51e-13

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: 69.09  E-value: 1.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  159 KQTPKQRLLGWIQN---KVPQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQV 235
Cdd:cd21244      3 KMSARKALLLWAQEqcaKVGSISVTDFKSSWRNGLAFLAIIHALRPGLV-DMEKLKGRSNRENLEEAFRIAEQELKIPRL 81

                           90       100
                   ....*....|....*....|...
gi 1952979823  236 IAPEEIVDPNVDEHSVMTYLSQF 258
Cdd:cd21244     82 LEPEDVDVVNPDEKSIMTYVAQF 104
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 159-258 1.53e-13

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: 68.99  E-value: 1.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  159 KQTPKQRLLGWIQNKVPQL---PITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQV 235
Cdd:cd21192      1 QGSAEKALLKWVQAEIGKYygiRVTDFDKSWRDGVAFLALIHAIRPDLV-DMKTVKNRSPRDNLELAFRIAEQHLNIPRL 79

                           90       100
                   ....*....|....*....|...
gi 1952979823  236 IAPEEIVDPNVDEHSVMTYLSQF 258
Cdd:cd21192     80 LEVEDVLVDKPDERSIMTYVSQF 102
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 159-258 1.73e-13

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: 68.74  E-value: 1.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  159 KQTPKQRLLGWIQNKVP---QLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQV 235
Cdd:cd21249      2 LRSAKEALLIWCQRKTAgytNVNVQDFSRSWRDGLAFNALIHAHRPDLI-DYGSLRPDRPLYNLANAFLVAEQELGISQL 80

                           90       100
                   ....*....|....*....|...
gi 1952979823  236 IAPEEIVDPNVDEHSVMTYLSQF 258
Cdd:cd21249     81 LDPEDVAVPHPDERSIMTYVSLY 103
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 152-249 2.44e-13

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: 68.48  E-value: 2.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  152 EDDEDARKQTPKQRLLGWI-----QNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPD---WEAWDPNQPVENAREAM 223
Cdd:cd21218      1 ETLESLLYLPPEEILLRWVnyhlkKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKelvLEVLSEEDLEKRAEKVL 80

                           90       100
                   ....*....|....*....|....*.
gi 1952979823  224 QQADDwLGVPQVIAPEEIVDPNVDEH 249
Cdd:cd21218     81 QAAEK-LGCKYFLTPEDIVSGNPRLN 105
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 59-139 1.03e-12

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: 66.85  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   59 TDLQRDLSDGLRLIALLEVLSQkrmYRKFHPRPNF----RQMKLENVSVALEFLER----EHIKLVSIDSKAIVDGNLKL 130
Cdd:cd21223     27 TNLAVDLRDGVRLCRLVELLTG---DWSLLSKLRVpaisRLQKLHNVEVALKALKEagvlRGGDGGGITAKDIVDGHREK 103


                   ....*....
gi 1952979823  131 ILGLIWTLI 139
Cdd:cd21223    104 TLALLWRII 112
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 163-258 1.78e-12

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: 65.88  E-value: 1.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  163 KQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPE 239
Cdd:cd21248      4 KDALLLWCQMKTagyPNVNVRNFTTSWRDGLAFNALIHKHRPDLI-DYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPE 82

                           90
                   ....*....|....*....
gi 1952979823  240 EIVDPNVDEHSVMTYLSQF 258
Cdd:cd21248     83 DVNVEQPDEKSIITYVVTY 101
Filamin pfam00630
Filamin/ABP280 repeat;
1778-1836 4.22e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 64.23  E-value: 4.22e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952979823 1778 FTVQ----KGELTGEVRMPSGKTARPNITDNKDGTITVRYAPTEKGLHQMGIKYDGNHIPGSP 1836
Cdd:pfam00630   25 FTVDtrdaGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSP 87
Filamin pfam00630
Filamin/ABP280 repeat;
2225-2289 1.74e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 62.31  E-value: 1.74e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952979823 2225 TRQQEGEAssqdmTAQVTSPSGKMEAAEIVEGEDSAYSVRFVPQEMGPHTVTVKYRGQHVPGSPF 2289
Cdd:pfam00630   29 TRDAGGEG-----EVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 154-261 4.11e-11

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: 62.43  E-value: 4.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  154 DEDARKQTPKQRLLGWIQNKVP---QLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWL 230
Cdd:cd21289      3 DISVEETSAKEGLLLWCQRKTApyrNVNVQNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKYL 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1952979823  231 GVPQVIAPEEIVD-PNVDEHSVMTYLSQFPKA 261
Cdd:cd21289     82 DIPKMLDAEDIVNtPKPDEKAIMTYVSCFYHA 113
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 30-138 4.51e-11

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: 62.29  E-value: 4.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   30 AEDAPWKKIqqntFTRWCNEHLKCVG-KRLT-DLQRDLSDGLRLIALLEVLSQKRMyRKFHPRPNFRQMKLENVSVALEF 107
Cdd:cd21285      6 AENGFDKQI----YTDWANHYLAKSGhKRLIkDLQQDVTDGVLLAEIIQVVANEKI-EDINGCPKNRSQMIENIDACLSF 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1952979823  108 LEREHIKLVSIDSKAIVDGNLKLILGLIWTL 138
Cdd:cd21285     81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 161-257 5.73e-11

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: 61.67  E-value: 5.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  161 TPKQRLLGWIQN---KVPQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDwLGVPQVIA 237
Cdd:cd21198      1 SSGQDLLEWCQEvtkGYRGVKITNLTTSWRNGLAFCAILHHFRPDLI-DFSSLSPHDIKENCKLAFDAAAK-LGIPRLLD 78

                           90       100
                   ....*....|....*....|.
gi 1952979823  238 PEEIVDPNV-DEHSVMTYLSQ 257
Cdd:cd21198     79 PADMVLLSVpDKLSVMTYLHQ 99
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 150-258 6.00e-11

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: 62.38  E-value: 6.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  150 EDEDDEDARkqTPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQA 226
Cdd:cd21322      8 ETEDNRETR--SAKDALLLWCQMKTagyPEVNIQNFTTSWRDGLAFNALIHRHRPDLI-DFSKLTKSNATYNLQQAFNTA 84

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1952979823  227 DDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQF 258
Cdd:cd21322     85 EQHLGLTKLLDPEDVNMEAPDEKSIITYVVSF 116
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
 154-261 6.47e-11

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: 62.01  E-value: 6.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  154 DEDARKQTPKQRLLGWIQNKVP---QLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWL 230
Cdd:cd21288      3 DISVEETSAKEGLLLWCQRKTApyrNVNIQNFHTSWKDGLGLCALIHRHRPDLI-DYSKLNKDDPIGNINLAMEIAEKHL 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1952979823  231 GVPQVIAPEEIVD-PNVDEHSVMTYLSQFPKA 261
Cdd:cd21288     82 DIPKMLDAEDIVNtPKPDERAIMTYVSCFYHA 113
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 161-258 1.25e-10

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: 61.00  E-value: 1.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  161 TPKQRLLGWIQNKVP---QLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIA 237
Cdd:cd21291     10 TAKEGLLLWCQRKTAgydEVDVQDFTTSWTDGLAFCALIHRHRPDLI-DYDKLDKKDHRGNMQLAFDIASKEIGIPQLLD 88

                           90       100
                   ....*....|....*....|..
gi 1952979823  238 PEEIVD-PNVDEHSVMTYLSQF 258
Cdd:cd21291     89 VEDVCDvAKPDERSIMTYVAYY 110
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 164-258 1.82e-10

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: 59.99  E-value: 1.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  164 QRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEE 240
Cdd:cd22198      3 EELLSWCQEQTegyRGVKVTDLTSSWRSGLALCAIIHRFRPDLI-DFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQE 81

                           90
                   ....*....|....*....
gi 1952979823  241 IVDPNV-DEHSVMTYLSQF 258
Cdd:cd22198     82 MASLAVpDKLSMVSYLSQF 100
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
 154-261 2.63e-10

second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 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. 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: 409139  Cd Length: 125  Bit Score: 60.48  E-value: 2.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  154 DEDARKQTPKQRLLGWIQNKVP---QLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWL 230
Cdd:cd21290      6 DISVEETSAKEGLLLWCQRKTApykNVNVQNFHISWKDGLAFNALIHRHRPELI-EYDKLRKDDPVTNLNNAFEVAEKYL 84

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1952979823  231 GVPQVIAPEEIVD-PNVDEHSVMTYLSQFPKA 261
Cdd:cd21290     85 DIPKMLDAEDIVNtARPDEKAIMTYVSSFYHA 116
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 43-138 2.90e-10

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: 59.66  E-value: 2.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   43 FTRWCNEHLKCVG-KRL-TDLQRDLSDGLRLIALLEVLSQKRMyRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDS 120
Cdd:cd21286      5 YTDWANHYLAKSGhKRLiKDLQQDIADGVLLAEIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 83

                           90
                   ....*....|....*...
gi 1952979823  121 KAIVDGNLKLILGLIWTL 138
Cdd:cd21286     84 EEIRNGNLKAILGLFFSL 101
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 42-146 7.77e-10

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: 58.79  E-value: 7.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   42 TFTRWCNEhlKCVGKRLTDLQRDLSDGLRLIALLE-----VLSQKRMYRKFHP-RPNFRqmKLENVSVALEFLEREHIKL 115
Cdd:cd21298     10 TYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDkikpgVVDWSRVNKPFKKlGANMK--KIENCNYAVELGKKLKFSL 85

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1952979823  116 VSIDSKAIVDGNLKLILGLIWTLILHYSISM 146
Cdd:cd21298     86 VGIGGKDIYDGNRTLTLALVWQLMRAYTLSI 116
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 163-258 1.20e-09

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: 57.73  E-value: 1.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  163 KQRLLGWIQ---NKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDW--EAWDPNQPVENAREAMQQADDW-LGVPQVI 236
Cdd:cd00014      1 EEELLKWINevlGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLgLPELDLF 80

                           90       100
                   ....*....|....*....|..
gi 1952979823  237 APEEIVDPNvDEHSVMTYLSQF 258
Cdd:cd00014     81 EPEDLYEKG-NLKKVLGTLWAL 101
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 161-256 1.78e-09

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: 57.34  E-value: 1.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  161 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQpVENAREAMQQADDWLGVPQVIA 237
Cdd:cd21238      2 TAKEKLLLWSQRMVegyQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLD 80

                           90
                   ....*....|....*....
gi 1952979823  238 PEEIVDPNVDEHSVMTYLS 256
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVS 99
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 162-258 5.50e-09

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: 56.01  E-value: 5.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  162 PKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAP 238
Cdd:cd21197      1 KIQALLRWCRRQCegyPGVNITNLTSSFRDGLAFCAILHRHRPELI-DFHSLKKDNWLENNRLAFRVAETSLGIPALLDA 79

                           90       100
                   ....*....|....*....|.
gi 1952979823  239 EEIVDPNV-DEHSVMTYLSQF 258
Cdd:cd21197     80 EDMVTMHVpDRLSIITYVSQY 100
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 161-257 1.60e-08

calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; 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. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409103  Cd Length: 107  Bit Score: 54.47  E-value: 1.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  161 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDwLGVPQVIA 237
Cdd:cd21254      1 NASQSLLAWCKEVTKGyrgVKITNFTTSWRNGLAFCAILHHFRPDLI-DYKSLNPHDIKENNKKAYDGFAS-LGISRLLE 78

                           90       100
                   ....*....|....*....|.
gi 1952979823  238 PEEIVDPNV-DEHSVMTYLSQ 257
Cdd:cd21254     79 PSDMVLLAVpDKLTVMTYLYQ 99
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 54-142 2.30e-08

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: 54.21  E-value: 2.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   54 VGKRLTDLQRDLSDGLRLIALLEVLSQK----RMYRKFHPRPNFRqmKLENVSVALEFLEREHIKLVSIDSKAIVDGNLK 129
Cdd:cd21219     18 LDPLINNLYEDLRDGLVLLQVLDKIQPGcvnwKKVNKPKPLNKFK--KVENCNYAVDLAKKLGFSLVGIGGKDIADGNRK 95

                           90
                   ....*....|...
gi 1952979823  130 LILGLIWTLILHY 142
Cdd:cd21219     96 LTLALVWQLMRYH 108
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
 154-261 2.63e-08

second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. 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: 409136  Cd Length: 124  Bit Score: 54.71  E-value: 2.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  154 DEDARKQTPKQRLLGWIQNKVP---QLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWL 230
Cdd:cd21287      3 DISVEETSAKEGLLLWCQRKTApykNVNIQNFHISWKDGLGFCALIHRHRPELI-DYGKLRKDDPLTNLNTAFDVAEKYL 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1952979823  231 GVPQVIAPEEIV-DPNVDEHSVMTYLSQFPKA 261
Cdd:cd21287     82 DIPKMLDAEDIVgTARPDEKAIMTYVSSFYHA 113
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 159-258 3.63e-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: 53.91  E-value: 3.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  159 KQTPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQV 235
Cdd:cd21321      3 KKSAKDALLLWCQMKTagyPNVNVHNFTTSWRDGLAFNAIVHKHRPDLI-DFETLKKSNAHYNLQNAFNVAEKELGLTKL 81

                           90       100
                   ....*....|....*....|...
gi 1952979823  236 IAPEEIVDPNVDEHSVMTYLSQF 258
Cdd:cd21321     82 LDPEDVNVDQPDEKSIITYVATY 104
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 161-259 4.59e-08

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: 53.51  E-value: 4.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  161 TPKQRLLGWIQnKV----PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDwLGVPQVI 236
Cdd:cd21240      4 SAKEKLLLWTQ-KVtagyTGIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGVTRLL 80

                           90       100
                   ....*....|....*....|....*..
gi 1952979823  237 APEEIVDPNVDEHSVMTYLSQ----FP 259
Cdd:cd21240     81 DAEDVDVPSPDEKSVITYVSSiydaFP 107
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 164-257 1.12e-07

calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may 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 subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409104  Cd Length: 105  Bit Score: 52.10  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  164 QRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDwLGVPQVIAPEE 240
Cdd:cd21255      4 QSLLEWCQEVTagyRGVRVTNFTTSWRNGLAFCAILHHFHPDLV-DYESLDPLDIKENNKKAFEAFAS-LGVPRLLEPAD 81

                           90
                   ....*....|....*...
gi 1952979823  241 IVDPNV-DEHSVMTYLSQ 257
Cdd:cd21255     82 MVLLPIpDKLIVMTYLCQ 99
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 166-258 1.25e-07

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: 52.05  E-value: 1.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  166 LLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEEIV 242
Cdd:cd21187      5 LLAWCRQSTrgyEQVDVKNFTTSWRDGLAFNALIHRHRPDLF-DFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVN 83

                           90
                   ....*....|....*.
gi 1952979823  243 DPNVDEHSVMTYLSQF 258
Cdd:cd21187     84 VEQPDKKSILMYVTSL 99
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 160-258 1.85e-07

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: 51.64  E-value: 1.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  160 QTPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVI 236
Cdd:cd21320      1 KSAKDALLLWCQMKTagyPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQHLGLTKLL 79

                           90       100
                   ....*....|....*....|..
gi 1952979823  237 APEEIVDPNVDEHSVMTYLSQF 258
Cdd:cd21320     80 DPEDISVDHPDEKSIITYVVTY 101
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 166-256 5.66e-07

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: 50.31  E-value: 5.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  166 LLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQ-PVENAREAMQQADDWLGVPQVIAPEEI 241
Cdd:cd21233      5 LLSWVRQSTrnyPQVNVINFTSSWSDGLAFNALIHSHRPDLF-DWNSVVSQQsATERLDHAFNIARQHLGIEKLLDPEDV 83

                           90
                   ....*....|....*
gi 1952979823  242 VDPNVDEHSVMTYLS 256
Cdd:cd21233     84 ATAHPDKKSILMYVT 98
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 166-256 6.12e-07

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: 49.96  E-value: 6.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  166 LLGWI-QNKVP--QLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEEIV 242
Cdd:cd21234      5 LLSWVrQSTRPysQVNVLNFTTSWTDGLAFNAVLHRHKPDLF-SWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVA 83

                           90
                   ....*....|....
gi 1952979823  243 DPNVDEHSVMTYLS 256
Cdd:cd21234     84 VQLPDKKSIIMYLT 97
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
 162-258 1.27e-06

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: 49.10  E-value: 1.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  162 PKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAP 238
Cdd:cd21252      1 ARRALQAWCRRQCegyPGVEIRDLSSSFRDGLAFCAILHRHRPDLI-DFDSLSKDNVYENNRLAFEVAERELGIPALLDP 79

                           90       100
                   ....*....|....*....|.
gi 1952979823  239 EEIVDPNV-DEHSVMTYLSQF 258
Cdd:cd21252     80 EDMVSMKVpDCLSIMTYVSQY 100
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 179-258 2.57e-06

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: 48.11  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  179 ITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEEIVDPNV-DEHSVMTYLSQ 257
Cdd:cd21253     22 VTNMTTSWRDGLAFCAIIHRFRPDLI-DFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDMVALKVpDKLSILTYVSQ 100


                   .
gi 1952979823  258 F 258
Cdd:cd21253    101 Y 101
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 163-266 3.48e-06

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: 48.06  E-value: 3.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  163 KQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPE 239
Cdd:cd21259      3 KQMLLDWCRAKTrgyENVDIQNFSSSWSDGMAFCALVHNFFPEAF-DYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVE 81

                           90       100       110
                   ....*....|....*....|....*....|
gi 1952979823  240 EIV---DPnvDEHSVMTYLSQFPKAKLKPG 266
Cdd:cd21259     82 DMVrmrEP--DWKCVYTYIQEFYRCLVQKG 109
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 45-138 4.24e-06

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 48.06  E-value: 4.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   45 RWCNEHLKCVG---KRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVsIDSK 121
Cdd:cd21218     17 RWVNYHLKKAGptkKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPE 95

                           90
                   ....*....|....*..
gi 1952979823  122 AIVDGNLKLILGLIWTL 138
Cdd:cd21218     96 DIVSGNPRLNLAFVATL 112
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
 166-257 4.31e-06

calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, 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-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409048  Cd Length: 112  Bit Score: 47.74  E-value: 4.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  166 LLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPdWEAWDPNQPVENAREAMQQADDwLGVPQVIAPEEIV 242
Cdd:cd21199     13 LLKWCQEKTqgyKGIDITNFSSSWNDGLAFCALLHSYLPDKIP-YSELNPQDKRRNFTLAFKAAES-VGIPTTLTIDEMV 90

                           90
                   ....*....|....*.
gi 1952979823  243 -DPNVDEHSVMTYLSQ 257
Cdd:cd21199     91 sMERPDWQSVMSYVTA 106
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
 165-258 4.96e-06

calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (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. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409044 [Multi-domain]  Cd Length: 110  Bit Score: 47.73  E-value: 4.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  165 RLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEEI 241
Cdd:cd21195      8 KLLTWCQQQTegyQHVNVTDLTTSWRSGLALCAIIHRFRPELI-NFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEM 86

                           90       100
                   ....*....|....*....|
gi 1952979823  242 V---DPnvDEHSVMTYLSQF 258
Cdd:cd21195     87 AsaqEP--DKLSMVMYLSKF 104
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 23-146 5.91e-06

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 48.07  E-value: 5.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   23 PSTEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVGKRLTDLQRDLSDGLRLIALLEVLS----QKRMYRKFHPRPNF 93
Cdd:cd21331      2 PALTKPENQDIDWTLLEgetreERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIKvpvdWNKVNKPPYPKLGA 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1952979823   94 RQMKLENVSVALEF-LEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 146
Cdd:cd21331     80 NMKKLENCNYAVELgKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNV 133
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 31-146 7.13e-06

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: 47.68  E-value: 7.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   31 EDAPWKKIQ-----QNTFTRWCNEhlKCVGKRLTDLQRDLSDGLRLIALLEVLS----QKRMYRKFHPRPNFRQMKLENV 101
Cdd:cd21330      1 QDIDWSSIEgetreERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLGENMKKLENC 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1952979823  102 SVALEFLERE-HIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 146
Cdd:cd21330     79 NYAVELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNI 124
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 161-259 7.60e-06

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: 46.90  E-value: 7.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  161 TPKQRLLGWIQNKVP---QLPITNFNRDWQDGKALGALVDNCAPGLCpdweawDPNQ-PVENAREAMQQA---DDWLGVP 233
Cdd:cd21239      1 SAKERLLLWSQQMTEgytGIRCENFTTCWRDGRLFNAIIHKYRPDLI------DMNTvAVQSNLANLEHAfyvAEKLGVT 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 1952979823  234 QVIAPEEIVDPNVDEHSVMTYLSQ----FP 259
Cdd:cd21239     75 RLLDPEDVDVSSPDEKSVITYVSSlydvFP 104
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 48-142 9.24e-06

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: 47.35  E-value: 9.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   48 NEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMY-RKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDG 126
Cdd:cd21307     26 NKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHlSEFFLTPSSTSEMLHNVTLALELLKEGGLLNFPVNPEDIVNG 105

                           90
                   ....*....|....*.
gi 1952979823  127 NLKLILGLIWTLILHY 142
Cdd:cd21307    106 DSKATIRVLYCLFSKY 121
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
 163-261 1.19e-05

calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409045  Cd Length: 106  Bit Score: 46.58  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  163 KQRLLGWIQNKVPQLP---ITNFNRDWQDGKALGALVDNCAPGLCpdweawDPNQ-----PVENAREAMQQADDWLGVPQ 234
Cdd:cd21196      5 QEELLRWCQEQTAGYPgvhVSDLSSSWADGLALCALVYRLQPGLL------EPSElqglgALEATAWALKVAENELGITP 78

                           90       100
                   ....*....|....*....|....*..
gi 1952979823  235 VIAPEEIVdPNVDEHSVMTYLSQFPKA 261
Cdd:cd21196     79 VVSAQAVV-AGSDPLGLIAYLSHFHSA 104
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 163-258 1.85e-05

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: 45.80  E-value: 1.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  163 KQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPE 239
Cdd:cd21200      3 KQMLLEWCQAKTrgyEHVDITNFSSSWSDGMAFCALIHHFFPDAF-DYSSLDPKNRRKNFELAFSTAEELADIAPLLEVE 81

                           90       100
                   ....*....|....*....|.
gi 1952979823  240 EIV--DPNVDEHSVMTYLSQF 258
Cdd:cd21200     82 DMVrmGNRPDWKCVFTYVQSL 102
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 166-260 7.93e-05

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: 44.25  E-value: 7.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  166 LLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPvENAREAMQQADDwLGV-PQVIAPEEI 241
Cdd:cd21257     13 LLKWCQKKTegyPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKK-RNLLLAFQAAES-VGIkPSLELSEMM 90

                           90
                   ....*....|....*....
gi 1952979823  242 VDPNVDEHSVMTYLSQFPK 260
Cdd:cd21257     91 YTDRPDWQSVMQYVAQIYK 109
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 43-138 1.31e-04

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: 43.95  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   43 FTRWCNEhLKcVGKRLTDLQRDLSDGLRLI-ALLEVLSQKRMYRKFHPRPNFRQMK----LENVSVALEFLEREHIKLVS 117
Cdd:cd21300     12 FTLWLNS-LD-VEPAVNDLFEDLRDGLILLqAYDKVIPGSVNWKKVNKAPASAEISrfkaVENTNYAVELGKQLGFSLVG 89

                           90       100
                   ....*....|....*....|.
gi 1952979823  118 IDSKAIVDGNLKLILGLIWTL 138
Cdd:cd21300     90 IQGADITDGSRTLTLALVWQL 110
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
 165-258 1.39e-04

calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409099 [Multi-domain]  Cd Length: 110  Bit Score: 43.33  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  165 RLLGWIQNKVP---QLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEEI 241
Cdd:cd21250      8 KLLTWCQKQTEgyqNVNVTDLTTSWKSGLALCAIIHRFRPELI-DFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEM 86

                           90
                   ....*....|....*...
gi 1952979823  242 VDPN-VDEHSVMTYLSQF 258
Cdd:cd21250     87 ASAEePDKLSMVMYLSKF 104
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 162-258 1.77e-04

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: 42.84  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  162 PKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAP 238
Cdd:cd21226      1 SEDGLLAWCRQTTEGydgVNITSFKSSFNDGRAFLALLHAYDPELF-KQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEA 79

                           90       100
                   ....*....|....*....|
gi 1952979823  239 EEIVDPNVDEHSVMTYLSQF 258
Cdd:cd21226     80 EDVMTGNPDERSIVLYTSLF 99
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 97-139 2.69e-04

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: 42.56  E-value: 2.69e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1952979823   97 KLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLI 139
Cdd:cd21217     71 ATENLNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
 165-258 3.16e-04

calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409100 [Multi-domain]  Cd Length: 111  Bit Score: 42.63  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  165 RLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEE- 240
Cdd:cd21251      9 KLLGWCQRQTegyAGVNVTDLTMSWKSGLALCAIIHRYRPDLI-DFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEm 87

                           90       100
                   ....*....|....*....|
gi 1952979823  241 --IVDPnvDEHSVMTYLSQF 258
Cdd:cd21251     88 asVGEP--DKLSMVMYLTQF 105
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 150-245 8.71e-04

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


Pssm-ID: 409175  Cd Length: 121  Bit Score: 41.41  E-value: 8.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  150 EDEDDEDARKQTPKQRLLGWIQNKVPQL---PITNFNRDWQDGKALGALVDNCAP-------GLCPDWEAWDPNQPVENA 219
Cdd:cd21326      1 EGEELEELMKLSPEELLLRWVNYHLTNAgwqNISNFSQDIKDSRAYFHLLNQIAPkgdvfdeNIEIDFSGFNEKNDLKRA 80

                           90       100
                   ....*....|....*....|....*.
gi 1952979823  220 REAMQQADDwLGVPQVIAPEEIVDPN 245
Cdd:cd21326     81 EYMLQEADK-LGCRQFVTPADVVSGN 105
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
 150-245 1.75e-03

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


Pssm-ID: 409144  Cd Length: 113  Bit Score: 40.34  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  150 EDEDDEDARKQTPKQRLLGWI----QNKVPQLPITNFNRDWQDGKALGALVDNCAP-GLCPDWEAWDPNQPVENAREAMQ 224
Cdd:cd21295      1 DGETLEDLLKLSPEEILLRWVnyhlERAGCDRRIKNFSGDIKDSEAYTHLLKQIAPkDAGVDTSALRESDLLQRAELMLQ 80

                           90       100
                   ....*....|....*....|.
gi 1952979823  225 QADDwLGVPQVIAPEEIVDPN 245
Cdd:cd21295     81 NADK-IGCRKFVTPKDVVTGN 100
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 40-142 2.30e-03

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: 39.95  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   40 QNTFTRWCNEHLkcVGKRLT--DLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQM-KLENVSVALEFLER--EHIK 114
Cdd:cd21221      3 VRVLTEWINEEL--ADDRIVvrDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQKqKLAVVLACVNFLLGleEDEA 80

                           90       100
                   ....*....|....*....|....*...
gi 1952979823  115 LVSIDSkaIVDGNLKLILGLIWTLILHY 142
Cdd:cd21221     81 RWTVDG--IYNKDLVSILHLLVALAHHY 106
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
 161-260 2.40e-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: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  161 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPdWEAWDPNQPVENAREAMQQADDwLGVPQVIA 237
Cdd:cd21256     14 SKRNALLKWCQKKTegyQNIDITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKRRNFTLAFQAAES-VGIKSTLD 91

                           90       100
                   ....*....|....*....|....
gi 1952979823  238 PEEIV-DPNVDEHSVMTYLSQFPK 260
Cdd:cd21256     92 INEMVrTERPDWQSVMTYVTAIYK 115
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 46-142 3.37e-03

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: 39.71  E-value: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   46 WCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRM-YRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIV 124
Cdd:cd21306     24 FVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVpLHSFHLTPTSFEQKVHNVQFAFELMQDAGLPKPKARPEDIV 103

                           90
                   ....*....|....*...
gi 1952979823  125 DGNLKLILGLIWTLILHY 142
Cdd:cd21306    104 NLDLKSTLRVLYNLFTKY 121
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 39-146 3.41e-03

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: 39.58  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   39 QQNTFTRWCNEhlKCVGKRLTDLQRDLSDGLRLIALLEV----LSQKRMYRKFHPRPNFRQMKLENVSVALEFLE-REHI 113
Cdd:cd21329      7 EERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpVDWGHVNKPPYPALGGNMKKIENCNYAVELGKnKAKF 84

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1952979823  114 KLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 146
Cdd:cd21329     85 SLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNV 117
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 64-146 3.62e-03

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: 39.41  E-value: 3.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   64 DLSDGLRLIALLEVLSQKRMYRKFHPRP----NFRqmKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLI 139
Cdd:cd21299     28 DVRDGWVLLEVLDKVSPGSVNWKHANKPpikmPFK--KVENCNQVVKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLM 105


                   ....*..
gi 1952979823  140 LHYSISM 146
Cdd:cd21299    106 RYHMLQL 112
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
 29-142 6.02e-03

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: 39.18  E-value: 6.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   29 LAEDAPWK-KIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRM-YRKFHPRPNFRQMKLENVSVALE 106
Cdd:cd21338     11 LFDHAPDKlSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVpLHNFYLTPESFDQKVHNVSFAFE 90

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1952979823  107 FLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHY 142
Cdd:cd21338     91 LMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKY 126
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
 163-255 6.56e-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: 38.79  E-value: 6.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823  163 KQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPE 239
Cdd:cd21261      3 KQILLEWCRSKTigyKNIDLQNFSSSWSDGMAFCALVHSFFPEAF-DYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVE 81

                           90
                   ....*....|....*...
gi 1952979823  240 E--IVDPNVDEHSVMTYL 255
Cdd:cd21261     82 DmmVMGRKPDPMCVFTYV 99
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
 29-142 8.46e-03

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: 38.82  E-value: 8.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952979823   29 LAEDAPWK-KIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRM-YRKFHPRPNFRQMKLENVSVALE 106
Cdd:cd21337     10 LFDHAPDKlNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVpLHSFFLTPDSFEQKVLNVSFAFE 89

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1952979823  107 FLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHY 142
Cdd:cd21337     90 LMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKY 125
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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