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Conserved domains on  [gi|688547228|ref|XP_009298480|]
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filamin-C isoform X1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 159-273 3.44e-85

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


The actual alignment was detected with superfamily member cd21314:

Pssm-ID: 469584  Cd Length: 115  Bit Score: 273.87  E-value: 3.44e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  159 DEDDEDARKLTPKQRLLGWIQNKVPQLHINNFHRDWRDGKALGALVDNCAPGLCPDWETWDPSQPVENAREAMQQADDWL 238
Cdd:cd21314     1 DEDEEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPVQNAREAMQQADDWL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 688547228  239 GVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKP 273
Cdd:cd21314    81 GVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKP 115
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 31-155 1.26e-82

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


The actual alignment was detected with superfamily member cd21310:

Pssm-ID: 469584  Cd Length: 125  Bit Score: 267.28  E-value: 1.26e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   31 PATEKDLAEDAPWKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPNFRQMKLENVS 110
Cdd:cd21310     1 PATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQMKLENVS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 688547228  111 VALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 155
Cdd:cd21310    81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 125
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1205-1297 3.30e-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: 3.30e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1205 PSKVTASGPGLERGKVNEAGSFTVDCSKAGEAELTIEIISDSGAQAEVHVQNNSDGTYSITYIPPFHGMYTITIKYGGHA 1284
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 688547228   1285 VPKFPARVQVDPA 1297
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1910-1996 4.60e-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: 121.17  E-value: 4.60e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1910 VNAYGPGLSHGMVNKSATFTIVTKDAGEGGLSLAVEGPS--KAEISCKDNKDGTCTVSYLPTAPGDYNIIVKFDDKHIAG 1987
Cdd:smart00557    4 VKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83


                    ....*....
gi 688547228   1988 SPFTAKITG 1996
Cdd:smart00557   84 SPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1493-1586 9.71e-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: 120.40  E-value: 9.71e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1493 PSKVKCTGPGLGSGvRAHVPQTFTVDCSKAGLAPLEVLLYGPTGMTEPVNITDNGDGTHTVVYTPAKDGPYTVCVKYADQ 1572
Cdd:smart00557    1 ASKVKASGPGLEKG-VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 688547228   1573 EVPRSPFKIKVLPA 1586
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1589-1683 1.24e-30

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 117.32  E-value: 1.24e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1589 ASKVRASGPGLNasGVPASLPVEFTIDARDAGEGLLTVQILDPEGKPKKANIRDNRDGTYTVSYVPDMTGRYTITIKYGG 1668
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 688547228   1669 DEIPYSPYRIHALPS 1683
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2089-2178 2.33e-30

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 116.55  E-value: 2.33e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   2089 ASKVKVSGKGLIEGHTFEVAEFIVDTRSAGYGGLGLSIEGPS--KVDINCSDVDDGTCKVTYCPTEPGTYIINIKFADQH 2166
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 688547228   2167 VPGSPFTVKVLG 2178
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2363-2451 7.61e-30

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 115.01  E-value: 7.61e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   2363 AHKVRAGGTGLDRGVAGVPAEFSIWTREAGAGGLSIAVEGPS--KAEISFEDRKDGSCGVAYIVQEPGDYEVSIKFNDEH 2440
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 688547228   2441 IPDSPFIVPIA 2451
Cdd:smart00557   81 IPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 717-811 7.25e-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: 111.93  E-value: 7.25e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    717 PEKVKCYGPGLEPTgcIVNKPAEFTIDARGAGRGQLQIYAQDSEGFPINIQITDNGDSTYFCVYIPIKPIKHTIIITWGE 796
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 688547228    797 VNVPNSPFRVTIGEG 811
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1112-1199 1.26e-28

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: 111.54  E-value: 1.26e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1112 PSKVRAYGPGLKGGIVGKPAPFAIDTKGAGTGGLGLTVEGP--CEAKIECQDNGDGSCSVSYLPTEPGEYSINILFADAH 1189
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 688547228   1190 IPGSPFKAMV 1199
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 621-711 1.07e-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: 108.85  E-value: 1.07e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    621 PQKVRAWGPGLETGMVGKSADFVVEAIGTEVGTLGFSIEGPSQAKIECD--DKGDGSCDVLYWPTEPGDYAVHVICDDED 698
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEvkDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 688547228    699 IKDSPFMAHILPA 711
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2683-2772 6.52e-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: 106.53  E-value: 6.52e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   2683 ASKVVSRGAGLSKAFIGQKNTFTVDCSKAGTNMLMVGVHGPKTPCEEVYVKHMGNRMYNVTYTVKEKGDYILIVKWGEEM 2762
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 688547228   2763 VPGSPFHVTV 2772
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2554-2644 1.71e-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: 1.71e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   2554 PGMVTAFGPGLEGGTTGVPSDFIVNTCNAGSGALSVTIDGPS--KVKMDCQECPEG-YKVTYTPMAPGSYLISIKYGGpQ 2630
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGG-E 79

                            90
                    ....*....|....
gi 688547228   2631 HIVGSPFKAKVSGA 2644
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 524-617 1.72e-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: 1.72e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    524 PNACRAIGRGLQPKgvRVKEVADFKVYTKGAGSGELRVHVKGPTGGDEPVKVEDLGDGVYECDYYPIFCGKYIITVTWGG 603
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....
gi 688547228    604 HAIPRSPFEVIISE 617
Cdd:smart00557   79 EHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 814-914 8.82e-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: 103.45  E-value: 8.82e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    814 PENVKVHGPGVEKTglKANEPTYFTVDCSEAGQGDVSIGikcapgVVGPAEADIDFDIIKNDNDTFTVKYTPPGAGRYTI 893
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVE------VTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTV 72

                            90       100
                    ....*....|....*....|.
gi 688547228    894 MVLFADQEIPISPFRIKVDPS 914
Cdd:smart00557   73 TVKFGGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1400-1487 1.23e-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: 103.07  E-value: 1.23e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1400 PSRVRAYGPGLEEGLVNKPNRFTVETRGAGTGGLGLAIEGPS--EAKMSCKDNKDGSCSVEYIPFTPGEYDVNITFGGLP 1477
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 688547228   1478 IPGSPFRVPV 1487
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 284-380 2.47e-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: 101.91  E-value: 2.47e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    284 PKRAKAYGPGIEPrgNVVLKPAEFVVETVEAGLGEVLVYIEDPEGHTEEARVIPNNDRnrSYSVVYVPKVEGLHKVKVLF 363
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDG--TYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 688547228    364 AGQDIDRSPFLVNVSKA 380
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1301-1397 9.64e-25

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 100.37  E-value: 9.64e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1301 SGIKVYGPGVEPRGVLreVTTHFIVDTRvhnKMGGNHIKVRIVNPSGANTDAYVTDKADGTYRVEYTAYEDGVHLIEVLY 1380
Cdd:smart00557    2 SKVKASGPGLEKGVVG--EPAEFTVDTR---DAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 688547228   1381 DDVPVPKSPFRVAVAEG 1397
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1709-1787 3.48e-24

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 98.83  E-value: 3.48e-24
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688547228   1709 QIGEETVITVDAKAAGKGKVTCKVSTPDGAELDVDVVENADGTFDIYYTAPEPGKYVITIRFGGEHIPNSPFHVVASDT 1787
Cdd:smart00557   15 VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 384-480 4.89e-24

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 98.44  E-value: 4.89e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    384 PNKVQARGPGLEPVgnVANKPTYFDIYTAGAGAGDVGVIIVDSQGRRdtVEIILENKGDSVFRCTYGPILEGPHTIYVTF 463
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 688547228    464 AGQQIPRSPFTVHISEA 480
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 917-1013 4.03e-23

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 95.75  E-value: 4.03e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    917 ANKVKAEGPGLNKTgvEVGKPTHFTIYTKGAGKATPEVHFTaSGRGDAVsDFEIIDNHDYSFTVRYTALQQGNMTISVCH 996
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVT-GPSGKKV-PVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 688547228    997 GGDPIPKSPFTISVAPP 1013
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1018-1105 4.04e-22

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.05  E-value: 4.04e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1018 KVKVHGLN-NKVDVGKDEEFTVNTRGAGGqGKVDVKITSPSRRPIPCKVESgASNEVHTVKYIPPEEGPYKVDISYDGNP 1096
Cdd:smart00557    3 KVKASGPGlEKGVVGEPAEFTVDTRDAGG-GELEVEVTGPSGKKVPVEVKD-NGDGTYTVSYTPTEPGDYTVTVKFGGEH 80


                    ....*....
gi 688547228   1097 VPGSPFTVE 1105
Cdd:smart00557   81 IPGSPFTVK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2471-2548 6.62e-19

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 83.81  E-value: 6.62e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688547228   2471 KVNQEASFAVQLNGA-RGAIDAKVHTPSGAVEECYITELDNDKHAIRFIPRENGVHSIDVRFNGSHIPGSPFKIRVGEP 2548
Cdd:smart00557   15 VVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2295-2357 6.68e-17

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 78.03  E-value: 6.68e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688547228   2295 GTQEMTAQVTSPSGNTEDAEIIEGEDSTYSVRFVPHEMGPHTVNVKYRGQHVPGSPFQFTVGP 2357
Cdd:smart00557   30 GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1839-1903 9.90e-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: 74.56  E-value: 9.90e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1839 FTVQ-----KGEITGEVHMPSGKTASPHITDNKDGTVTVKYAPTEKGLHEMDIKYDGNHIPGSPLQFYVD 1903
Cdd:smart00557   22 FTVDtrdagGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
 
Name Accession Description Interval E-value
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 159-273 3.44e-85

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: 273.87  E-value: 3.44e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  159 DEDDEDARKLTPKQRLLGWIQNKVPQLHINNFHRDWRDGKALGALVDNCAPGLCPDWETWDPSQPVENAREAMQQADDWL 238
Cdd:cd21314     1 DEDEEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPVQNAREAMQQADDWL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 688547228  239 GVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKP 273
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 ...
 31-155 1.26e-82

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: 267.28  E-value: 1.26e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   31 PATEKDLAEDAPWKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPNFRQMKLENVS 110
Cdd:cd21310     1 PATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQMKLENVS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 688547228  111 VALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 155
Cdd:cd21310    81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 125
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
43-269 1.31e-32

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 136.99  E-value: 1.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   43 WKKIQQNTFTRWCNEHL-KCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRkYHARPNFRQMKLENVSVALEFLEREHI 121
Cdd:COG5069     6 WQKVQKKTFTKWTNEKLiSGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGE-YNETPETRIHVMENVSGRLEFIKGKGV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  122 KLVSIDSKAIVDGNLKLILGLIWTLILHYSISmpmwedeDDEDARKLTPKQRLLGW----IQNKVPQLHINNFHRDWRDG 197
Cdd:COG5069    85 KLFNIGPQDIVDGNPKLILGLIWSLISRLTIA-------TINEEGELTKHINLLLWcdedTGGYKPEVDTFDFFRSWRDG 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688547228  198 KALGALVDNCAP-GLCPDWETWDPSQPVENAREAMQQADDWLGVPQVIAPEEIVDPNV-DEHSVMTYLSQFPKA 269
Cdd:COG5069   158 LAFSALIHDSRPdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSWYIIR 231
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1205-1297 3.30e-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: 3.30e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1205 PSKVTASGPGLERGKVNEAGSFTVDCSKAGEAELTIEIISDSGAQAEVHVQNNSDGTYSITYIPPFHGMYTITIKYGGHA 1284
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 688547228   1285 VPKFPARVQVDPA 1297
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1910-1996 4.60e-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: 121.17  E-value: 4.60e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1910 VNAYGPGLSHGMVNKSATFTIVTKDAGEGGLSLAVEGPS--KAEISCKDNKDGTCTVSYLPTAPGDYNIIVKFDDKHIAG 1987
Cdd:smart00557    4 VKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83


                    ....*....
gi 688547228   1988 SPFTAKITG 1996
Cdd:smart00557   84 SPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1493-1586 9.71e-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: 120.40  E-value: 9.71e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1493 PSKVKCTGPGLGSGvRAHVPQTFTVDCSKAGLAPLEVLLYGPTGMTEPVNITDNGDGTHTVVYTPAKDGPYTVCVKYADQ 1572
Cdd:smart00557    1 ASKVKASGPGLEKG-VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 688547228   1573 EVPRSPFKIKVLPA 1586
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1589-1683 1.24e-30

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 117.32  E-value: 1.24e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1589 ASKVRASGPGLNasGVPASLPVEFTIDARDAGEGLLTVQILDPEGKPKKANIRDNRDGTYTVSYVPDMTGRYTITIKYGG 1668
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 688547228   1669 DEIPYSPYRIHALPS 1683
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2089-2178 2.33e-30

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 116.55  E-value: 2.33e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   2089 ASKVKVSGKGLIEGHTFEVAEFIVDTRSAGYGGLGLSIEGPS--KVDINCSDVDDGTCKVTYCPTEPGTYIINIKFADQH 2166
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 688547228   2167 VPGSPFTVKVLG 2178
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2363-2451 7.61e-30

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 115.01  E-value: 7.61e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   2363 AHKVRAGGTGLDRGVAGVPAEFSIWTREAGAGGLSIAVEGPS--KAEISFEDRKDGSCGVAYIVQEPGDYEVSIKFNDEH 2440
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 688547228   2441 IPDSPFIVPIA 2451
Cdd:smart00557   81 IPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 717-811 7.25e-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: 111.93  E-value: 7.25e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    717 PEKVKCYGPGLEPTgcIVNKPAEFTIDARGAGRGQLQIYAQDSEGFPINIQITDNGDSTYFCVYIPIKPIKHTIIITWGE 796
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 688547228    797 VNVPNSPFRVTIGEG 811
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1112-1199 1.26e-28

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: 111.54  E-value: 1.26e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1112 PSKVRAYGPGLKGGIVGKPAPFAIDTKGAGTGGLGLTVEGP--CEAKIECQDNGDGSCSVSYLPTEPGEYSINILFADAH 1189
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 688547228   1190 IPGSPFKAMV 1199
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 621-711 1.07e-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: 108.85  E-value: 1.07e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    621 PQKVRAWGPGLETGMVGKSADFVVEAIGTEVGTLGFSIEGPSQAKIECD--DKGDGSCDVLYWPTEPGDYAVHVICDDED 698
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEvkDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 688547228    699 IKDSPFMAHILPA 711
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2683-2772 6.52e-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: 106.53  E-value: 6.52e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   2683 ASKVVSRGAGLSKAFIGQKNTFTVDCSKAGTNMLMVGVHGPKTPCEEVYVKHMGNRMYNVTYTVKEKGDYILIVKWGEEM 2762
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 688547228   2763 VPGSPFHVTV 2772
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2554-2644 1.71e-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: 1.71e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   2554 PGMVTAFGPGLEGGTTGVPSDFIVNTCNAGSGALSVTIDGPS--KVKMDCQECPEG-YKVTYTPMAPGSYLISIKYGGpQ 2630
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGG-E 79

                            90
                    ....*....|....
gi 688547228   2631 HIVGSPFKAKVSGA 2644
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 524-617 1.72e-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: 1.72e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    524 PNACRAIGRGLQPKgvRVKEVADFKVYTKGAGSGELRVHVKGPTGGDEPVKVEDLGDGVYECDYYPIFCGKYIITVTWGG 603
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....
gi 688547228    604 HAIPRSPFEVIISE 617
Cdd:smart00557   79 EHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 814-914 8.82e-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: 103.45  E-value: 8.82e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    814 PENVKVHGPGVEKTglKANEPTYFTVDCSEAGQGDVSIGikcapgVVGPAEADIDFDIIKNDNDTFTVKYTPPGAGRYTI 893
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVE------VTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTV 72

                            90       100
                    ....*....|....*....|.
gi 688547228    894 MVLFADQEIPISPFRIKVDPS 914
Cdd:smart00557   73 TVKFGGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1588-1677 9.97e-26

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 103.14  E-value: 9.97e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1588 DASKVRASGPGLNasGVPASLPVEFTIDARDAGeGLLTVQILDPEGKPKKANIRDNRDGTYTVSYVPDMTGRYTITIKYG 1667
Cdd:pfam00630    3 DASKVKASGPGLE--PGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 688547228  1668 GDEIPYSPYR 1677
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1400-1487 1.23e-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: 103.07  E-value: 1.23e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1400 PSRVRAYGPGLEEGLVNKPNRFTVETRGAGTGGLGLAIEGPS--EAKMSCKDNKDGSCSVEYIPFTPGEYDVNITFGGLP 1477
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 688547228   1478 IPGSPFRVPV 1487
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 284-380 2.47e-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: 101.91  E-value: 2.47e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    284 PKRAKAYGPGIEPrgNVVLKPAEFVVETVEAGLGEVLVYIEDPEGHTEEARVIPNNDRnrSYSVVYVPKVEGLHKVKVLF 363
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDG--TYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 688547228    364 AGQDIDRSPFLVNVSKA 380
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1491-1580 3.85e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 101.21  E-value: 3.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1491 VDPSKVKCTGPGLgSGVRAHVPQTFTVDCSKAGlAPLEVLLYGPTGMTEPVNITDNGDGTHTVVYTPAKDGPYTVCVKYA 1570
Cdd:pfam00630    2 ADASKVKASGPGL-EPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 688547228  1571 DQEVPRSPFK 1580
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1301-1397 9.64e-25

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 100.37  E-value: 9.64e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1301 SGIKVYGPGVEPRGVLreVTTHFIVDTRvhnKMGGNHIKVRIVNPSGANTDAYVTDKADGTYRVEYTAYEDGVHLIEVLY 1380
Cdd:smart00557    2 SKVKASGPGLEKGVVG--EPAEFTVDTR---DAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 688547228   1381 DDVPVPKSPFRVAVAEG 1397
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1109-1196 1.12e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 100.06  E-value: 1.12e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1109 PPDPSKVRAYGPGLKGGIVGKPAPFAIDTKGAGTGGLGLtVEGP--CEAKIECQDNGDGSCSVSYLPTEPGEYSINILFA 1186
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVE-VTGPdgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 688547228  1187 DAHIPGSPFK 1196
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1202-1289 1.79e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 99.29  E-value: 1.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1202 VFDPSKVTASGPGLERGKVNEAGSFTVDCSKAGEaELTIEIISDSGAQAEVHVQNNSDGTYSITYIPPFHGMYTITIKYG 1281
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*...
gi 688547228  1282 GHAVPKFP 1289
Cdd:pfam00630   80 GQHIPGSP 87
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1709-1787 3.48e-24

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 98.83  E-value: 3.48e-24
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688547228   1709 QIGEETVITVDAKAAGKGKVTCKVSTPDGAELDVDVVENADGTFDIYYTAPEPGKYVITIRFGGEHIPNSPFHVVASDT 1787
Cdd:smart00557   15 VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1904-1991 3.60e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 98.52  E-value: 3.60e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1904 AINSGHVNAYGPGLSHGMVNKSATFTIVTKDAGeGGLSLAVEGPS--KAEISCKDNKDGTCTVSYLPTAPGDYNIIVKFD 1981
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 688547228  1982 DKHIAGSPFT 1991
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 384-480 4.89e-24

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 98.44  E-value: 4.89e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    384 PNKVQARGPGLEPVgnVANKPTYFDIYTAGAGAGDVGVIIVDSQGRRdtVEIILENKGDSVFRCTYGPILEGPHTIYVTF 463
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 688547228    464 AGQQIPRSPFTVHISEA 480
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2087-2173 7.40e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 97.74  E-value: 7.40e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  2087 GDASKVKVSGKGLIEGHTFEVAEFIVDTRSAGyGGLGLSIEGPS--KVDINCSDVDDGTCKVTYCPTEPGTYIINIKFAD 2164
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 688547228  2165 QHVPGSPFT 2173
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
715-805 1.76e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.59  E-value: 1.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   715 VFPEKVKCYGPGLEPTgcIVNKPAEFTIDARGAGrGQLQIYAQDSEGFPINIQITDNGDSTYFCVYIPIKPIKHTIIITW 794
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 688547228   795 GEVNVPNSPFR 805
Cdd:pfam00630   79 NGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 917-1013 4.03e-23

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 95.75  E-value: 4.03e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    917 ANKVKAEGPGLNKTgvEVGKPTHFTIYTKGAGKATPEVHFTaSGRGDAVsDFEIIDNHDYSFTVRYTALQQGNMTISVCH 996
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVT-GPSGKKV-PVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 688547228    997 GGDPIPKSPFTISVAPP 1013
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 49-149 6.54e-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: 95.46  E-value: 6.54e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228     49 NTFTRWCNEHLKC-LNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPNFRQMKLENVSVALEFLEREHIKLVSID 127
Cdd:smart00033    1 KTLLRWVNSLLAEyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 688547228    128 SKAIVDGNlKLILGLIWTLILH 149
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
2361-2447 2.10e-22

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 93.51  E-value: 2.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  2361 GGAHKVRAGGTGLDRGVAGVPAEFSIWTREAGaGGLSIAVEGPS--KAEISFEDRKDGSCGVAYIVQEPGDYEVSIKFND 2438
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 688547228  2439 EHIPDSPFI 2447
Cdd:pfam00630   81 QHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1018-1105 4.04e-22

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.05  E-value: 4.04e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1018 KVKVHGLN-NKVDVGKDEEFTVNTRGAGGqGKVDVKITSPSRRPIPCKVESgASNEVHTVKYIPPEEGPYKVDISYDGNP 1096
Cdd:smart00557    3 KVKASGPGlEKGVVGEPAEFTVDTRDAGG-GELEVEVTGPSGKKVPVEVKD-NGDGTYTVSYTPTEPGDYTVTVKFGGEH 80


                    ....*....
gi 688547228   1097 VPGSPFTVE 1105
Cdd:smart00557   81 IPGSPFTVK 89
Filamin pfam00630
Filamin/ABP280 repeat;
812-908 4.20e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 89.66  E-value: 4.20e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   812 SHPENVKVHGPGVEKTglKANEPTYFTVDCSEA-GQGDVSIgikcapgvVGPAEADIDFDIIKNDNDTFTVKYTPPGAGR 890
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAgGEGEVEV--------TGPDGSPVPVEVTDNGDGTYTVSYTPTEPGD 71

                           90
                   ....*....|....*...
gi 688547228   891 YTIMVLFADQEIPISPFR 908
Cdd:pfam00630   72 YTVSVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2551-2638 5.62e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 89.66  E-value: 5.62e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  2551 AGDPGMVTAFGPGLEGGTTGVPSDFIVNTCNAGsGALSVTIDGPS--KVKMDCQECPEG-YKVTYTPMAPGSYLISIKYG 2627
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|.
gi 688547228  2628 GpQHIVGSPFK 2638
Cdd:pfam00630   80 G-QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1398-1484 5.68e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 89.27  E-value: 5.68e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1398 CDPSRVRAYGPGLEEGLVNKPNRFTVETRGAGTGGLGLaIEGPS--EAKMSCKDNKDGSCSVEYIPFTPGEYDVNITFGG 1475
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVE-VTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 688547228  1476 LPIPGSPFR 1484
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
522-612 8.88e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 88.89  E-value: 8.88e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   522 SNPNACRAIGRGLQPkgVRVKEVADFKVYTKGAGsGELRVHVKGPTGGDEPVKVEDLGDGVYECDYYPIFCGKYIITVTW 601
Cdd:pfam00630    2 ADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 688547228   602 GGHAIPRSPFE 612
Cdd:pfam00630   79 NGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
283-373 1.67e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 88.11  E-value: 1.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   283 HPKRAKAYGPGIEPrgNVVLKPAEFVVETVEAGlGEVLVYIEDPEGHTEEARVIPNNDRnrSYSVVYVPKVEGLHKVKVL 362
Cdd:pfam00630    3 DASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDG--TYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 688547228   363 FAGQDIDRSPF 373
Cdd:pfam00630   78 FNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
619-704 2.24e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 87.73  E-value: 2.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   619 AGPQKVRAWGPGLETGMVGKSADFVVEAIGtEVGTLGFSIEGPS--QAKIECDDKGDGSCDVLYWPTEPGDYAVHVICDD 696
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRD-AGGEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 688547228   697 EDIKDSPF 704
Cdd:pfam00630   81 QHIPGSPF 88
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 45-152 3.03e-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: 88.11  E-value: 3.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    45 KIQQNTFTRWCNEHLKCL--NRKILDLQKDLTDGLKLIGLLEVLSQKKmyRKYHARPNFRQMKLENVSVALEFLERE-HI 121
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGL--VDKKKLNKSEFDKLENINLALDVAEKKlGV 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 688547228   122 KLVSIDSKAIVDGNLKLILGLIWTLILHYSI 152
Cdd:pfam00307   79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
Filamin pfam00630
Filamin/ABP280 repeat;
382-474 3.79e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.96  E-value: 3.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   382 GDPNKVQARGPGLEPVgnVANKPTYFDIYTAGAGaGDVGVIIVDSQGRRDTVEIIleNKGDSVFRCTYGPILEGPHTIYV 461
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVT--DNGDGTYTVSYTPTEPGDYTVSV 76

                           90
                   ....*....|...
gi 688547228   462 TFAGQQIPRSPFT 474
Cdd:pfam00630   77 KFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1297-1391 5.17e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.57  E-value: 5.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1297 ALDTSGIKVYGPGVEPRGVLREvtTHFIVDTRvhNKMGGnhIKVRIVNPSGANTDAYVTDKADGTYRVEYTAYEDGVHLI 1376
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKP--AEFTVDTR--DAGGE--GEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTV 74

                           90
                   ....*....|....*
gi 688547228  1377 EVLYDDVPVPKSPFR 1391
Cdd:pfam00630   75 SVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1013-1103 6.53e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.57  E-value: 6.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1013 PLDLNKVKVHGLN-NKVDVGKDEEFTVNTRGAGGQGkvDVKITSPSRRPIPCKVESgASNEVHTVKYIPPEEGPYKVDIS 1091
Cdd:pfam00630    1 AADASKVKASGPGlEPGVVGKPAEFTVDTRDAGGEG--EVEVTGPDGSPVPVEVTD-NGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 688547228  1092 YDGNPVPGSPFT 1103
Cdd:pfam00630   78 FNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1683-1781 1.48e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.42  E-value: 1.48e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1683 SGDASKCLVTvsigghglgSGLGPTIQIGEETVITVDAKAAGkGKVTCKVSTPDGAELDVDVVENADGTFDIYYTAPEPG 1762
Cdd:pfam00630    1 AADASKVKAS---------GPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPG 70

                           90
                   ....*....|....*....
gi 688547228  1763 KYVITIRFGGEHIPNSPFH 1781
Cdd:pfam00630   71 DYTVSVKFNGQHIPGSPFK 89
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 168-266 1.59e-19

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 86.19  E-value: 1.59e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   168 LTPKQRLLGWIQNKV----PQLHINNFHRDWRDGKALGALVDNCAPGLCPDWE-TWDPSQPVENAREAMQQADDWLGVPQ 242
Cdd:pfam00307    1 LELEKELLRWINSHLaeygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKLGVPK 80

                           90       100
                   ....*....|....*....|....*
gi 688547228   243 V-IAPEEIVDPnvDEHSVMTYLSQF 266
Cdd:pfam00307   81 VlIEPEDLVEG--DNKSVLTYLASL 103
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2471-2548 6.62e-19

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 83.81  E-value: 6.62e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688547228   2471 KVNQEASFAVQLNGA-RGAIDAKVHTPSGAVEECYITELDNDKHAIRFIPRENGVHSIDVRFNGSHIPGSPFKIRVGEP 2548
Cdd:smart00557   15 VVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGPA 93
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 174-266 8.47e-19

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 83.52  E-value: 8.47e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    174 LLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCPDW---ETWDPSQPVENAREAMQQADDWLGVPQVIAPE 247
Cdd:smart00033    3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKkvaASLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90
                    ....*....|....*....
gi 688547228    248 EIVDPNVDEHSVMTYLSQF 266
Cdd:smart00033   83 DLVEGPKLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
916-1007 1.52e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 79.64  E-value: 1.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   916 DANKVKAEGPGLNktGVEVGKPTHFTIYTKGA-GKATPEVhftaSGRGDAVSDFEIIDNHDYSFTVRYTALQQGNMTISV 994
Cdd:pfam00630    3 DASKVKASGPGLE--PGVVGKPAEFTVDTRDAgGEGEVEV----TGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSV 76

                           90
                   ....*....|...
gi 688547228   995 CHGGDPIPKSPFT 1007
Cdd:pfam00630   77 KFNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2295-2357 6.68e-17

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 78.03  E-value: 6.68e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688547228   2295 GTQEMTAQVTSPSGNTEDAEIIEGEDSTYSVRFVPHEMGPHTVNVKYRGQHVPGSPFQFTVGP 2357
Cdd:smart00557   30 GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
2471-2542 7.36e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 77.71  E-value: 7.36e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688547228  2471 KVNQEASFAVQLNGARGAIDAKVHTPSGAVEECYITELDNDKHAIRFIPRENGVHSIDVRFNGSHIPGSPFK 2542
Cdd:pfam00630   18 VVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2680-2769 8.27e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 77.71  E-value: 8.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  2680 SSDASKVVSRGAGLSKAFIGQKNTFTVDCSKAGTNmLMVGVHGPKTPCEEVYVKHMGNRMYNVTYTVKEKGDYILIVKWG 2759
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGE-GEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 688547228  2760 EEMVPGSPFH 2769
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1839-1903 9.90e-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: 74.56  E-value: 9.90e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1839 FTVQ-----KGEITGEVHMPSGKTASPHITDNKDGTVTVKYAPTEKGLHEMDIKYDGNHIPGSPLQFYVD 1903
Cdd:smart00557   22 FTVDtrdagGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
2303-2351 5.02e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 69.63  E-value: 5.02e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 688547228  2303 VTSPSGNTEDAEIIEGEDSTYSVRFVPHEMGPHTVNVKYRGQHVPGSPF 2351
Cdd:pfam00630   40 VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
1839-1897 2.25e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 65.00  E-value: 2.25e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688547228  1839 FTVQ----KGEITGEVHMPSGKTASPHITDNKDGTVTVKYAPTEKGLHEMDIKYDGNHIPGSP 1897
Cdd:pfam00630   25 FTVDtrdaGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSP 87
 
Name Accession Description Interval E-value
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 159-273 3.44e-85

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: 273.87  E-value: 3.44e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  159 DEDDEDARKLTPKQRLLGWIQNKVPQLHINNFHRDWRDGKALGALVDNCAPGLCPDWETWDPSQPVENAREAMQQADDWL 238
Cdd:cd21314     1 DEDEEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPVQNAREAMQQADDWL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 688547228  239 GVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKP 273
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 ...
 31-155 1.26e-82

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: 267.28  E-value: 1.26e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   31 PATEKDLAEDAPWKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPNFRQMKLENVS 110
Cdd:cd21310     1 PATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQMKLENVS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 688547228  111 VALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 155
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 ...
 30-160 6.08e-76

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: 248.07  E-value: 6.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   30 MPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPNFRQMKLENV 109
Cdd:cd21309     1 MPVTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFRQMQLENV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 688547228  110 SVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDE 160
Cdd:cd21309    81 SVALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISMPVWEDE 131
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 27-155 9.49e-75

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: 244.61  E-value: 9.49e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   27 DEEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPNFRQMKL 106
Cdd:cd21308     1 DAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 688547228  107 ENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 155
Cdd:cd21308    81 ENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 129
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 169-271 5.38e-73

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: 238.44  E-value: 5.38e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  169 TPKQRLLGWIQNKVPQLHINNFHRDWRDGKALGALVDNCAPGLCPDWETWDPSQPVENAREAMQQADDWLGVPQVIAPEE 248
Cdd:cd21230     1 TPKQRLLGWIQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALENATEAMQLAEDWLGVPQLITPEE 80

                          90       100
                  ....*....|....*....|...
gi 688547228  249 IVDPNVDEHSVMTYLSQFPKAKL 271
Cdd:cd21230    81 IINPNVDEMSVMTYLSQFPKAKL 103
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
 162-271 7.10e-69

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: 227.28  E-value: 7.10e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  162 DEDARKLTPKQRLLGWIQNKVPQLHINNFHRDWRDGKALGALVDNCAPGLCPDWETWDPSQPVENAREAMQQADDWLGVP 241
Cdd:cd21313     1 DDDAKKQTPKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPQKPVDNAREAMQQADDWLGVP 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 688547228  242 QVIAPEEIVDPNVDEHSVMTYLSQFPKAKL 271
Cdd:cd21313    81 QVITPEEIIHPDVDEHSVMTYLSQFPKAKL 110
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 158-271 7.98e-68

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: 224.30  E-value: 7.98e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  158 EDEDDEDARKLTPKQRLLGWIQNKVPQLHINNFHRDWRDGKALGALVDNCAPGLCPDWETWDPSQPVENAREAMQQADDW 237
Cdd:cd21312     1 DEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDW 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 688547228  238 LGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKL 271
Cdd:cd21312    81 LGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKL 114
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 32-155 1.11e-67

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: 224.25  E-value: 1.11e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   32 ATEKDLAEDAPWKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMyRKYHARPNFRQMKLENVSV 111
Cdd:cd21311     1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKF-PKFNKRPTFRSQKLENVSV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 688547228  112 ALEFLER-EHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 155
Cdd:cd21311    80 ALKFLEEdEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISMP 124
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 43-150 3.65e-67

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: 221.98  E-value: 3.65e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   43 WKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPNFRQMKLENVSVALEFLEREHIK 122
Cdd:cd21228     1 WKKIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRPTFRQMKLENVSVALEFLERESIK 80

                          90       100
                  ....*....|....*....|....*...
gi 688547228  123 LVSIDSKAIVDGNLKLILGLIWTLILHY 150
Cdd:cd21228    81 LVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 156-271 4.38e-65

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: 216.57  E-value: 4.38e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  156 MWEDEDD--EDARKLTPKQRLLGWIQNKVPQLHINNFHRDWRDGKALGALVDNCAPGLCPDWETWDPSQPVENAREAMQQ 233
Cdd:cd21315     1 MWEGEDDgpDDGKGPTPKQRLLGWIQSKVPDLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAVKNAKEAMDL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 688547228  234 ADDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKL 271
Cdd:cd21315    81 AEDWLDVPQLIKPEEMVNPKVDELSMMTYLSQFPNAKL 118
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 43-150 4.90e-58

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: 196.16  E-value: 4.90e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   43 WKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPNFRQMKLENVSVALEFLEREHIK 122
Cdd:cd21183     1 WKRIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYNRRPAFQQHYLENVSTALKFIEADHIK 80

                          90       100
                  ....*....|....*....|....*...
gi 688547228  123 LVSIDSKAIVDGNLKLILGLIWTLILHY 150
Cdd:cd21183    81 LVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 169-270 1.98e-49

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: 171.27  E-value: 1.98e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  169 TPKQRLLGWIQNKVPQLHINNFHRDWRDGKALGALVDNCAPGLCPDWETWDPSQPVENAREAMQQADDWLGVPQVIAPEE 248
Cdd:cd21184     1 SGKSLLLEWVNSKIPEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMDIAEEELGIPKIITPED 80

                          90       100
                  ....*....|....*....|..
gi 688547228  249 IVDPNVDEHSVMTYLSQFPKAK 270
Cdd:cd21184    81 MVSPNVDELSVMTYLSYFRNAK 102
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 43-152 4.14e-43

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: 153.21  E-value: 4.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   43 WKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRkYHARPNFRQMKLENVSVALEFLEREHIK 122
Cdd:cd21227     1 WVEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR-VIKKPLNQHQKLENVTLALKAMAEDGIK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 688547228  123 LVSIDSKAIVDGNLKLILGLIWTLILHYSI 152
Cdd:cd21227    80 LVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 43-150 1.70e-40

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: 146.01  E-value: 1.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   43 WKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRkYHARPNFRQMKLENVSVALEFLEREHIK 122
Cdd:cd21215     1 WVDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGR-YNKNPKMRVQKLENVNKALEFIKSRGVK 79

                          90       100
                  ....*....|....*....|....*...
gi 688547228  123 LVSIDSKAIVDGNLKLILGLIWTLILHY 150
Cdd:cd21215    80 LTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 45-150 1.03e-36

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


Pssm-ID: 409037  Cd Length: 105  Bit Score: 134.84  E-value: 1.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   45 KIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKyhaRPNFRQMKLENVSVALEFLEREHIKLV 124
Cdd:cd21188     2 AVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRE---RGRMRFHRLQNVQTALDFLKYRKIKLV 78

                          90       100
                  ....*....|....*....|....*.
gi 688547228  125 SIDSKAIVDGNLKLILGLIWTLILHY 150
Cdd:cd21188    79 NIRAEDIVDGNPKLTLGLIWTIILHF 104
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 167-268 3.36e-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: 130.58  E-value: 3.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  167 KLTPKQRLLGWIQNKVPQLHINNFHRDWRDGKALGALVDNCAPGLCPDWETWDPSQPVENAREAMQQADDWLGVPQVIAP 246
Cdd:cd21229     1 KIPPKKLMLAWLQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSP 80

                          90       100
                  ....*....|....*....|..
gi 688547228  247 EEIVDPNVDEHSVMTYLSQFPK 268
Cdd:cd21229    81 EDLSSPHLDELSGMTYLSYFMK 102
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 43-148 4.15e-34

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 127.51  E-value: 4.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   43 WKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKyhARPNFRQMKLENVSVALEFLEREHIK 122
Cdd:cd21214     2 WEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKP--ERGKMRFHKIANVNKALDFIASKGVK 79

                          90       100
                  ....*....|....*....|....*.
gi 688547228  123 LVSIDSKAIVDGNLKLILGLIWTLIL 148
Cdd:cd21214    80 LVSIGAEEIVDGNLKMTLGMIWTIIL 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
43-269 1.31e-32

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 136.99  E-value: 1.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   43 WKKIQQNTFTRWCNEHL-KCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRkYHARPNFRQMKLENVSVALEFLEREHI 121
Cdd:COG5069     6 WQKVQKKTFTKWTNEKLiSGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGE-YNETPETRIHVMENVSGRLEFIKGKGV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  122 KLVSIDSKAIVDGNLKLILGLIWTLILHYSISmpmwedeDDEDARKLTPKQRLLGW----IQNKVPQLHINNFHRDWRDG 197
Cdd:COG5069    85 KLFNIGPQDIVDGNPKLILGLIWSLISRLTIA-------TINEEGELTKHINLLLWcdedTGGYKPEVDTFDFFRSWRDG 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688547228  198 KALGALVDNCAP-GLCPDWETWDPSQPVENAREAMQQADDWLGVPQVIAPEEIVDPNV-DEHSVMTYLSQFPKA 269
Cdd:COG5069   158 LAFSALIHDSRPdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSWYIIR 231
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1205-1297 3.30e-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: 3.30e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1205 PSKVTASGPGLERGKVNEAGSFTVDCSKAGEAELTIEIISDSGAQAEVHVQNNSDGTYSITYIPPFHGMYTITIKYGGHA 1284
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 688547228   1285 VPKFPARVQVDPA 1297
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1910-1996 4.60e-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: 121.17  E-value: 4.60e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1910 VNAYGPGLSHGMVNKSATFTIVTKDAGEGGLSLAVEGPS--KAEISCKDNKDGTCTVSYLPTAPGDYNIIVKFDDKHIAG 1987
Cdd:smart00557    4 VKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83


                    ....*....
gi 688547228   1988 SPFTAKITG 1996
Cdd:smart00557   84 SPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1493-1586 9.71e-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: 120.40  E-value: 9.71e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1493 PSKVKCTGPGLGSGvRAHVPQTFTVDCSKAGLAPLEVLLYGPTGMTEPVNITDNGDGTHTVVYTPAKDGPYTVCVKYADQ 1572
Cdd:smart00557    1 ASKVKASGPGLEKG-VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 688547228   1573 EVPRSPFKIKVLPA 1586
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1589-1683 1.24e-30

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 117.32  E-value: 1.24e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1589 ASKVRASGPGLNasGVPASLPVEFTIDARDAGEGLLTVQILDPEGKPKKANIRDNRDGTYTVSYVPDMTGRYTITIKYGG 1668
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 688547228   1669 DEIPYSPYRIHALPS 1683
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2089-2178 2.33e-30

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 116.55  E-value: 2.33e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   2089 ASKVKVSGKGLIEGHTFEVAEFIVDTRSAGYGGLGLSIEGPS--KVDINCSDVDDGTCKVTYCPTEPGTYIINIKFADQH 2166
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 688547228   2167 VPGSPFTVKVLG 2178
Cdd:smart00557   81 IPGSPFTVKVGP 92
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 46-148 4.35e-30

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


Pssm-ID: 409042  Cd Length: 116  Bit Score: 116.63  E-value: 4.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   46 IQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMyrkyhARPN---FRQMKLENVSVALEFLeREHIK 122
Cdd:cd21193    16 IQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKL-----GKPNrgrLRVQKIENVNKALAFL-KTKVR 89

                          90       100
                  ....*....|....*....|....*.
gi 688547228  123 LVSIDSKAIVDGNLKLILGLIWTLIL 148
Cdd:cd21193    90 LENIGAEDIVDGNPRLILGLIWTIIL 115
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2363-2451 7.61e-30

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 115.01  E-value: 7.61e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   2363 AHKVRAGGTGLDRGVAGVPAEFSIWTREAGAGGLSIAVEGPS--KAEISFEDRKDGSCGVAYIVQEPGDYEVSIKFNDEH 2440
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 688547228   2441 IPDSPFIVPIA 2451
Cdd:smart00557   81 IPGSPFTVKVG 91
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 35-148 1.58e-29

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: 114.77  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   35 KDLAEDApwKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMyrkyhARPNFRQMK---LENVSV 111
Cdd:cd21246     7 KALADER--EAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERL-----PKPTKGKMRihcLENVDK 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 688547228  112 ALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLIL 148
Cdd:cd21246    80 ALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 717-811 7.25e-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: 111.93  E-value: 7.25e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    717 PEKVKCYGPGLEPTgcIVNKPAEFTIDARGAGRGQLQIYAQDSEGFPINIQITDNGDSTYFCVYIPIKPIKHTIIITWGE 796
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 688547228    797 VNVPNSPFRVTIGEG 811
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1112-1199 1.26e-28

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: 111.54  E-value: 1.26e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1112 PSKVRAYGPGLKGGIVGKPAPFAIDTKGAGTGGLGLTVEGP--CEAKIECQDNGDGSCSVSYLPTEPGEYSINILFADAH 1189
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 688547228   1190 IPGSPFKAMV 1199
Cdd:smart00557   81 IPGSPFTVKV 90
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 45-153 1.51e-28

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: 112.77  E-value: 1.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   45 KIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKyhaRPNFRQMKLENVSVALEFLEREHIKLV 124
Cdd:cd21236    16 KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE---KGRMRFHRLQNVQIALDYLKRRQVKLV 92

                          90       100
                  ....*....|....*....|....*....
gi 688547228  125 SIDSKAIVDGNLKLILGLIWTLILHYSIS 153
Cdd:cd21236    93 NIRNDDITDGNPKLTLGLIWTIILHFQIS 121
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 45-162 6.80e-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: 110.50  E-value: 6.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   45 KIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKyhaRPNFRQMKLENVSVALEFLEREHIKLV 124
Cdd:cd21235     5 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 688547228  125 SIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDEDD 162
Cdd:cd21235    82 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 621-711 1.07e-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: 108.85  E-value: 1.07e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    621 PQKVRAWGPGLETGMVGKSADFVVEAIGTEVGTLGFSIEGPSQAKIECD--DKGDGSCDVLYWPTEPGDYAVHVICDDED 698
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEvkDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 688547228    699 IKDSPFMAHILPA 711
Cdd:smart00557   81 IPGSPFTVKVGPA 93
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 46-150 2.92e-27

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: 108.24  E-value: 2.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   46 IQQNTFTRWCNEHLKCLNRK-ILDLQKDLTDGLKLIGLLEVLSQKKMYRKyhaRPNFRQMKLENVSVALEFLEREHIKLV 124
Cdd:cd21186     2 VQKKTFTKWINSQLSKANKPpIKDLFEDLRDGTRLLALLEVLTGKKLKPE---KGRMRVHHLNNVNRALQVLEQNNVKLV 78

                          90       100
                  ....*....|....*....|....*.
gi 688547228  125 SIDSKAIVDGNLKLILGLIWTLILHY 150
Cdd:cd21186    79 NISSNDIVDGNPKLTLGLVWSIILHW 104
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 45-152 3.88e-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: 107.85  E-value: 3.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   45 KIQQNTFTRWCNEHLKCLNR--KILDLQKDLTDGLKLIGLLEVLSQKKM---YRKYHARPNFrqmkLENVSVALEFLERE 119
Cdd:cd21241     4 RVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLpceKGRRLKRVHF----LSNINTALKFLESK 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 688547228  120 HIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 152
Cdd:cd21241    80 KIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2683-2772 6.52e-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: 106.53  E-value: 6.52e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   2683 ASKVVSRGAGLSKAFIGQKNTFTVDCSKAGTNMLMVGVHGPKTPCEEVYVKHMGNRMYNVTYTVKEKGDYILIVKWGEEM 2762
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 688547228   2763 VPGSPFHVTV 2772
Cdd:smart00557   81 IPGSPFTVKV 90
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 45-153 1.38e-26

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: 106.66  E-value: 1.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   45 KIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKyhaRPNFRQMKLENVSVALEFLEREHIKLV 124
Cdd:cd21237     5 RVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPRE---KGRMRFHRLQNVQIALDFLKQRQVKLV 81

                          90       100
                  ....*....|....*....|....*....
gi 688547228  125 SIDSKAIVDGNLKLILGLIWTLILHYSIS 153
Cdd:cd21237    82 NIRNDDITDGNPKLTLGLIWTIILHFQIS 110
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2554-2644 1.71e-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: 1.71e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   2554 PGMVTAFGPGLEGGTTGVPSDFIVNTCNAGSGALSVTIDGPS--KVKMDCQECPEG-YKVTYTPMAPGSYLISIKYGGpQ 2630
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGG-E 79

                            90
                    ....*....|....
gi 688547228   2631 HIVGSPFKAKVSGA 2644
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 524-617 1.72e-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: 1.72e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    524 PNACRAIGRGLQPKgvRVKEVADFKVYTKGAGSGELRVHVKGPTGGDEPVKVEDLGDGVYECDYYPIFCGKYIITVTWGG 603
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....
gi 688547228    604 HAIPRSPFEVIISE 617
Cdd:smart00557   79 EHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 814-914 8.82e-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: 103.45  E-value: 8.82e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    814 PENVKVHGPGVEKTglKANEPTYFTVDCSEAGQGDVSIGikcapgVVGPAEADIDFDIIKNDNDTFTVKYTPPGAGRYTI 893
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVE------VTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTV 72

                            90       100
                    ....*....|....*....|.
gi 688547228    894 MVLFADQEIPISPFRIKVDPS 914
Cdd:smart00557   73 TVKFGGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1588-1677 9.97e-26

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 103.14  E-value: 9.97e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1588 DASKVRASGPGLNasGVPASLPVEFTIDARDAGeGLLTVQILDPEGKPKKANIRDNRDGTYTVSYVPDMTGRYTITIKYG 1667
Cdd:pfam00630    3 DASKVKASGPGLE--PGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 688547228  1668 GDEIPYSPYR 1677
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1400-1487 1.23e-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: 103.07  E-value: 1.23e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1400 PSRVRAYGPGLEEGLVNKPNRFTVETRGAGTGGLGLAIEGPS--EAKMSCKDNKDGSCSVEYIPFTPGEYDVNITFGGLP 1477
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 688547228   1478 IPGSPFRVPV 1487
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 284-380 2.47e-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: 101.91  E-value: 2.47e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    284 PKRAKAYGPGIEPrgNVVLKPAEFVVETVEAGLGEVLVYIEDPEGHTEEARVIPNNDRnrSYSVVYVPKVEGLHKVKVLF 363
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDG--TYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 688547228    364 AGQDIDRSPFLVNVSKA 380
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 44-152 2.48e-25

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: 102.65  E-value: 2.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   44 KKIQQNTFTRWCNEHLKCLNRKIL--DLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPNfRQMKLENVSVALEFLEREHI 121
Cdd:cd21190     3 ERVQKKTFTNWINSHLAKLSQPIVinDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQ-RAHKLSNIRNALDFLTKRCI 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 688547228  122 KLVSIDSKAIVDGNLKLILGLIWTLILHYSI 152
Cdd:cd21190    82 KLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
Filamin pfam00630
Filamin/ABP280 repeat;
1491-1580 3.85e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 101.21  E-value: 3.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1491 VDPSKVKCTGPGLgSGVRAHVPQTFTVDCSKAGlAPLEVLLYGPTGMTEPVNITDNGDGTHTVVYTPAKDGPYTVCVKYA 1570
Cdd:pfam00630    2 ADASKVKASGPGL-EPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 688547228  1571 DQEVPRSPFK 1580
Cdd:pfam00630   80 GQHIPGSPFK 89
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 43-151 8.39e-25

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: 101.07  E-value: 8.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   43 WKKIQQNTFTRWCNEHL-KCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPNFRQMKLENVSVALEFLERE-H 120
Cdd:cd21225     1 WEKVQIKAFTAWVNSVLeKRGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQMIQNLHLAMLFIEEDlK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 688547228  121 IKLVSIDSKAIVDGNLKLILGLIWTLILHYS 151
Cdd:cd21225    81 IRVQGIGAEDFVDNNKKLILGLLWTLYRKYR 111
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1301-1397 9.64e-25

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 100.37  E-value: 9.64e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1301 SGIKVYGPGVEPRGVLreVTTHFIVDTRvhnKMGGNHIKVRIVNPSGANTDAYVTDKADGTYRVEYTAYEDGVHLIEVLY 1380
Cdd:smart00557    2 SKVKASGPGLEKGVVG--EPAEFTVDTR---DAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 688547228   1381 DDVPVPKSPFRVAVAEG 1397
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 46-152 9.88e-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: 101.12  E-value: 9.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   46 IQQNTFTRWCNEHLKCLNR--KILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPNfRQMKLENVSVALEFLEREHIKL 123
Cdd:cd21191     5 VQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSH-RIFRLNNIAKALKFLEDSNVKL 83

                          90       100
                  ....*....|....*....|....*....
gi 688547228  124 VSIDSKAIVDGNLKLILGLIWTLILHYSI 152
Cdd:cd21191    84 VSIDAAEIADGNPSLVLGLIWNIILFFQI 112
Filamin pfam00630
Filamin/ABP280 repeat;
1109-1196 1.12e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 100.06  E-value: 1.12e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1109 PPDPSKVRAYGPGLKGGIVGKPAPFAIDTKGAGTGGLGLtVEGP--CEAKIECQDNGDGSCSVSYLPTEPGEYSINILFA 1186
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVE-VTGPdgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 688547228  1187 DAHIPGSPFK 1196
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1202-1289 1.79e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 99.29  E-value: 1.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1202 VFDPSKVTASGPGLERGKVNEAGSFTVDCSKAGEaELTIEIISDSGAQAEVHVQNNSDGTYSITYIPPFHGMYTITIKYG 1281
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*...
gi 688547228  1282 GHAVPKFP 1289
Cdd:pfam00630   80 GQHIPGSP 87
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1709-1787 3.48e-24

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 98.83  E-value: 3.48e-24
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688547228   1709 QIGEETVITVDAKAAGKGKVTCKVSTPDGAELDVDVVENADGTFDIYYTAPEPGKYVITIRFGGEHIPNSPFHVVASDT 1787
Cdd:smart00557   15 VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1904-1991 3.60e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 98.52  E-value: 3.60e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1904 AINSGHVNAYGPGLSHGMVNKSATFTIVTKDAGeGGLSLAVEGPS--KAEISCKDNKDGTCTVSYLPTAPGDYNIIVKFD 1981
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 688547228  1982 DKHIAGSPFT 1991
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 384-480 4.89e-24

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 98.44  E-value: 4.89e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    384 PNKVQARGPGLEPVgnVANKPTYFDIYTAGAGAGDVGVIIVDSQGRRdtVEIILENKGDSVFRCTYGPILEGPHTIYVTF 463
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 688547228    464 AGQQIPRSPFTVHISEA 480
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2087-2173 7.40e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 97.74  E-value: 7.40e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  2087 GDASKVKVSGKGLIEGHTFEVAEFIVDTRSAGyGGLGLSIEGPS--KVDINCSDVDDGTCKVTYCPTEPGTYIINIKFAD 2164
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 688547228  2165 QHVPGSPFT 2173
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
715-805 1.76e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.59  E-value: 1.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   715 VFPEKVKCYGPGLEPTgcIVNKPAEFTIDARGAGrGQLQIYAQDSEGFPINIQITDNGDSTYFCVYIPIKPIKHTIIITW 794
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 688547228   795 GEVNVPNSPFR 805
Cdd:pfam00630   79 NGQHIPGSPFK 89
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 35-148 3.36e-23

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: 97.43  E-value: 3.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   35 KDLAEDApwKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARpnFRQMKLENVSVALE 114
Cdd:cd21317    22 KALADER--EAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKGR--MRIHCLENVDKALQ 97

                          90       100       110
                  ....*....|....*....|....*....|....
gi 688547228  115 FLEREHIKLVSIDSKAIVDGNLKLILGLIWTLIL 148
Cdd:cd21317    98 FLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 917-1013 4.03e-23

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 95.75  E-value: 4.03e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    917 ANKVKAEGPGLNKTgvEVGKPTHFTIYTKGAGKATPEVHFTaSGRGDAVsDFEIIDNHDYSFTVRYTALQQGNMTISVCH 996
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVT-GPSGKKV-PVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 688547228    997 GGDPIPKSPFTISVAPP 1013
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 27-148 6.20e-23

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: 97.02  E-value: 6.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   27 DEEMPATE-------KDLAEDApwKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARp 99
Cdd:cd21318    14 DEPAATAKlfecsriKALADER--EAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGR- 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 688547228  100 nFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLIL 148
Cdd:cd21318    91 -MRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 49-149 6.54e-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: 95.46  E-value: 6.54e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228     49 NTFTRWCNEHLKC-LNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPNFRQMKLENVSVALEFLEREHIKLVSID 127
Cdd:smart00033    1 KTLLRWVNSLLAEyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 688547228    128 SKAIVDGNlKLILGLIWTLILH 149
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
2361-2447 2.10e-22

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 93.51  E-value: 2.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  2361 GGAHKVRAGGTGLDRGVAGVPAEFSIWTREAGaGGLSIAVEGPS--KAEISFEDRKDGSCGVAYIVQEPGDYEVSIKFND 2438
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 688547228  2439 EHIPDSPFI 2447
Cdd:pfam00630   81 QHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1018-1105 4.04e-22

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.05  E-value: 4.04e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1018 KVKVHGLN-NKVDVGKDEEFTVNTRGAGGqGKVDVKITSPSRRPIPCKVESgASNEVHTVKYIPPEEGPYKVDISYDGNP 1096
Cdd:smart00557    3 KVKASGPGlEKGVVGEPAEFTVDTRDAGG-GELEVEVTGPSGKKVPVEVKD-NGDGTYTVSYTPTEPGDYTVTVKFGGEH 80


                    ....*....
gi 688547228   1097 VPGSPFTVE 1105
Cdd:smart00557   81 IPGSPFTVK 89
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 46-152 8.78e-22

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: 92.68  E-value: 8.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   46 IQQNTFTRWCNEHL-KCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKyhaRPNFRQMKLENVSVALEFLEREHIKLV 124
Cdd:cd21231     6 VQKKTFTKWINAQFaKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKE---KGSTRVHALNNVNKALQVLQKNNVDLV 82

                          90       100
                  ....*....|....*....|....*...
gi 688547228  125 SIDSKAIVDGNLKLILGLIWTLILHYSI 152
Cdd:cd21231    83 NIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 6-148 1.62e-21

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: 93.57  E-value: 1.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    6 TYYDQQLPPQYYQGTDNGEDGDE---EMPATE-------KDLAEDApwKKIQQNTFTRWCNEHLKCLNRKILDLQKDLTD 75
Cdd:cd21316     5 TDFDNIDIQQQYSDVNNRWDVDEwdnENSSARlfersriKALADER--EAVQKKTFTKWVNSHLARVSCRITDLYMDLRD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688547228   76 GLKLIGLLEVLSQKKMYRKYHARpnFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLIL 148
Cdd:cd21316    83 GRMLIKLLEVLSGERLPKPTKGR--MRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
Filamin pfam00630
Filamin/ABP280 repeat;
812-908 4.20e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 89.66  E-value: 4.20e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   812 SHPENVKVHGPGVEKTglKANEPTYFTVDCSEA-GQGDVSIgikcapgvVGPAEADIDFDIIKNDNDTFTVKYTPPGAGR 890
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAgGEGEVEV--------TGPDGSPVPVEVTDNGDGTYTVSYTPTEPGD 71

                           90
                   ....*....|....*...
gi 688547228   891 YTIMVLFADQEIPISPFR 908
Cdd:pfam00630   72 YTVSVKFNGQHIPGSPFK 89
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 51-150 5.18e-21

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: 90.33  E-value: 5.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   51 FTRWCNEHLKCLN--RKILDLQKDLTDGLKLIGLLEVLSQKKMyRKYHARPNFRQMKLENVSVALEFLEREHIKLVSIDS 128
Cdd:cd21212     5 YTDWANHYLEKGGhkRIITDLQKDLGDGLTLVNLIEAVAGEKV-PGIHSRPKTRAQKLENIQACLQFLAALGVDVQGITA 83

                          90       100
                  ....*....|....*....|..
gi 688547228  129 KAIVDGNLKLILGLIWTLILHY 150
Cdd:cd21212    84 EDIVDGNLKAILGLFFSLSRYK 105
Filamin pfam00630
Filamin/ABP280 repeat;
2551-2638 5.62e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 89.66  E-value: 5.62e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  2551 AGDPGMVTAFGPGLEGGTTGVPSDFIVNTCNAGsGALSVTIDGPS--KVKMDCQECPEG-YKVTYTPMAPGSYLISIKYG 2627
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|.
gi 688547228  2628 GpQHIVGSPFK 2638
Cdd:pfam00630   80 G-QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1398-1484 5.68e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 89.27  E-value: 5.68e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1398 CDPSRVRAYGPGLEEGLVNKPNRFTVETRGAGTGGLGLaIEGPS--EAKMSCKDNKDGSCSVEYIPFTPGEYDVNITFGG 1475
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVE-VTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 688547228  1476 LPIPGSPFR 1484
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
522-612 8.88e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 88.89  E-value: 8.88e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   522 SNPNACRAIGRGLQPkgVRVKEVADFKVYTKGAGsGELRVHVKGPTGGDEPVKVEDLGDGVYECDYYPIFCGKYIITVTW 601
Cdd:pfam00630    2 ADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 688547228   602 GGHAIPRSPFE 612
Cdd:pfam00630   79 NGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
283-373 1.67e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 88.11  E-value: 1.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   283 HPKRAKAYGPGIEPrgNVVLKPAEFVVETVEAGlGEVLVYIEDPEGHTEEARVIPNNDRnrSYSVVYVPKVEGLHKVKVL 362
Cdd:pfam00630    3 DASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDG--TYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 688547228   363 FAGQDIDRSPF 373
Cdd:pfam00630   78 FNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
619-704 2.24e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 87.73  E-value: 2.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   619 AGPQKVRAWGPGLETGMVGKSADFVVEAIGtEVGTLGFSIEGPS--QAKIECDDKGDGSCDVLYWPTEPGDYAVHVICDD 696
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRD-AGGEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 688547228   697 EDIKDSPF 704
Cdd:pfam00630   81 QHIPGSPF 88
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 45-152 3.03e-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: 88.11  E-value: 3.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    45 KIQQNTFTRWCNEHLKCL--NRKILDLQKDLTDGLKLIGLLEVLSQKKmyRKYHARPNFRQMKLENVSVALEFLERE-HI 121
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGL--VDKKKLNKSEFDKLENINLALDVAEKKlGV 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 688547228   122 KLVSIDSKAIVDGNLKLILGLIWTLILHYSI 152
Cdd:pfam00307   79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
Filamin pfam00630
Filamin/ABP280 repeat;
382-474 3.79e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.96  E-value: 3.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   382 GDPNKVQARGPGLEPVgnVANKPTYFDIYTAGAGaGDVGVIIVDSQGRRDTVEIIleNKGDSVFRCTYGPILEGPHTIYV 461
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVT--DNGDGTYTVSYTPTEPGDYTVSV 76

                           90
                   ....*....|...
gi 688547228   462 TFAGQQIPRSPFT 474
Cdd:pfam00630   77 KFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1297-1391 5.17e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.57  E-value: 5.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1297 ALDTSGIKVYGPGVEPRGVLREvtTHFIVDTRvhNKMGGnhIKVRIVNPSGANTDAYVTDKADGTYRVEYTAYEDGVHLI 1376
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKP--AEFTVDTR--DAGGE--GEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTV 74

                           90
                   ....*....|....*
gi 688547228  1377 EVLYDDVPVPKSPFR 1391
Cdd:pfam00630   75 SVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1013-1103 6.53e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.57  E-value: 6.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1013 PLDLNKVKVHGLN-NKVDVGKDEEFTVNTRGAGGQGkvDVKITSPSRRPIPCKVESgASNEVHTVKYIPPEEGPYKVDIS 1091
Cdd:pfam00630    1 AADASKVKASGPGlEPGVVGKPAEFTVDTRDAGGEG--EVEVTGPDGSPVPVEVTD-NGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 688547228  1092 YDGNPVPGSPFT 1103
Cdd:pfam00630   78 FNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1683-1781 1.48e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.42  E-value: 1.48e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  1683 SGDASKCLVTvsigghglgSGLGPTIQIGEETVITVDAKAAGkGKVTCKVSTPDGAELDVDVVENADGTFDIYYTAPEPG 1762
Cdd:pfam00630    1 AADASKVKAS---------GPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPG 70

                           90
                   ....*....|....*....
gi 688547228  1763 KYVITIRFGGEHIPNSPFH 1781
Cdd:pfam00630   71 DYTVSVKFNGQHIPGSPFK 89
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 168-266 1.59e-19

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 86.19  E-value: 1.59e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   168 LTPKQRLLGWIQNKV----PQLHINNFHRDWRDGKALGALVDNCAPGLCPDWE-TWDPSQPVENAREAMQQADDWLGVPQ 242
Cdd:pfam00307    1 LELEKELLRWINSHLaeygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKLGVPK 80

                           90       100
                   ....*....|....*....|....*
gi 688547228   243 V-IAPEEIVDPnvDEHSVMTYLSQF 266
Cdd:pfam00307   81 VlIEPEDLVEG--DNKSVLTYLASL 103
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 46-152 2.73e-19

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: 85.65  E-value: 2.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   46 IQQNTFTRWCNEHL--KCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHARPnFRQMKleNVSVALEFLEREHIKL 123
Cdd:cd21242     5 TQKRTFTNWINSQLakHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNV-FQCRS--NIETALSFLKNKSIKL 81

                          90       100
                  ....*....|....*....|....*....
gi 688547228  124 VSIDSKAIVDGNLKLILGLIWTLILHYSI 152
Cdd:cd21242    82 INIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 175-266 4.95e-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: 84.28  E-value: 4.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  175 LGWIQNKVPQLHINNFHRDWRDGKALGALVDNCApGLCPDWETWDPSQPVENAREAMQQADDwLGVPQVIAPEEIVDPNV 254
Cdd:cd21185     7 LRWVRQLLPDVDVNNFTTDWNDGRLLCGLVNALG-GSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEV 84

                          90
                  ....*....|..
gi 688547228  255 DEHSVMTYLSQF 266
Cdd:cd21185    85 EHLGIMAYAAQL 96
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2471-2548 6.62e-19

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 83.81  E-value: 6.62e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688547228   2471 KVNQEASFAVQLNGA-RGAIDAKVHTPSGAVEECYITELDNDKHAIRFIPRENGVHSIDVRFNGSHIPGSPFKIRVGEP 2548
Cdd:smart00557   15 VVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGPA 93
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 174-266 8.47e-19

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 83.52  E-value: 8.47e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228    174 LLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCPDW---ETWDPSQPVENAREAMQQADDWLGVPQVIAPE 247
Cdd:smart00033    3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKkvaASLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90
                    ....*....|....*....
gi 688547228    248 EIVDPNVDEHSVMTYLSQF 266
Cdd:smart00033   83 DLVEGPKLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
916-1007 1.52e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 79.64  E-value: 1.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   916 DANKVKAEGPGLNktGVEVGKPTHFTIYTKGA-GKATPEVhftaSGRGDAVSDFEIIDNHDYSFTVRYTALQQGNMTISV 994
Cdd:pfam00630    3 DASKVKASGPGLE--PGVVGKPAEFTVDTRDAgGEGEVEV----TGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSV 76

                           90
                   ....*....|...
gi 688547228   995 CHGGDPIPKSPFT 1007
Cdd:pfam00630   77 KFNGQHIPGSPFK 89
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 46-152 2.71e-17

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: 79.67  E-value: 2.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   46 IQQNTFTRWCNEHL-KCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKyhaRPNFRQMKLENVSVALEFLEREHIKLV 124
Cdd:cd21232     2 VQKKTFTKWINARFsKSGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKE---RGSTRVHALNNVNRVLQVLHQNNVELV 78

                          90       100
                  ....*....|....*....|....*...
gi 688547228  125 SIDSKAIVDGNLKLILGLIWTLILHYSI 152
Cdd:cd21232    79 NIGGTDIVDGNHKLTLGLLWSIILHWQV 106
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 46-152 3.69e-17

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: 79.80  E-value: 3.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   46 IQQNTFTRWCNEHLKCLNRKIL--DLQKDLTDGLKLIGLLEVLSQKKMyrkyhARPNFRQMK---LENVSVALEFLeREH 120
Cdd:cd21247    20 MQKKTFTKWMNNVFSKNGAKIEitDIYTELKDGIHLLRLLELISGEQL-----PRPSRGKMRvhfLENNSKAITFL-KTK 93

                          90       100       110
                  ....*....|....*....|....*....|..
gi 688547228  121 IKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 152
Cdd:cd21247    94 VPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
 167-269 5.21e-17

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: 78.90  E-value: 5.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  167 KLTPKQRLLGWIQNKVPQ---LHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQV 243
Cdd:cd21243     3 KGGAKKALLKWVQNAAAKrfgIEVKDFGPSWRDGVAFNAIIHSIRPDLV-DMESLKRRSNRENLETAFTVAEKELGIPRL 81

                          90       100
                  ....*....|....*....|....*.
gi 688547228  244 IAPEEIVDPNVDEHSVMTYLSQFPKA 269
Cdd:cd21243    82 LDPEDVDVDKPDEKSIMTYVAQFLKK 107
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2295-2357 6.68e-17

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 78.03  E-value: 6.68e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688547228   2295 GTQEMTAQVTSPSGNTEDAEIIEGEDSTYSVRFVPHEMGPHTVNVKYRGQHVPGSPFQFTVGP 2357
Cdd:smart00557   30 GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
2471-2542 7.36e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 77.71  E-value: 7.36e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688547228  2471 KVNQEASFAVQLNGARGAIDAKVHTPSGAVEECYITELDNDKHAIRFIPRENGVHSIDVRFNGSHIPGSPFK 2542
Cdd:pfam00630   18 VVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2680-2769 8.27e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 77.71  E-value: 8.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  2680 SSDASKVVSRGAGLSKAFIGQKNTFTVDCSKAGTNmLMVGVHGPKTPCEEVYVKHMGNRMYNVTYTVKEKGDYILIVKWG 2759
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGE-GEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 688547228  2760 EEMVPGSPFH 2769
Cdd:pfam00630   80 GQHIPGSPFK 89
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 168-269 1.13e-16

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: 78.17  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  168 LTPKQRLLGWIQNKVPQLH---INNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVI 244
Cdd:cd21216     9 LSAKEGLLLWCQRKTAPYKnvnVQNFHTSWKDGLAFCALIHRHRPDLL-DYDKLRKDDPRENLNLAFDVAEKHLDIPKML 87

                          90       100
                  ....*....|....*....|....*.
gi 688547228  245 APEEIVD-PNVDEHSVMTYLSQFPKA 269
Cdd:cd21216    88 DAEDIVNtPRPDERSVMTYVSCYYHA 113
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 169-267 2.40e-16

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: 77.05  E-value: 2.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  169 TPKQRLLGWIQ---NKVPQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIA 245
Cdd:cd21189     1 SAKEALLLWARrttEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLI-DFRSVRNQSNRENLENAFNVAEKEFGVTRLLD 79

                          90       100
                  ....*....|....*....|....*.
gi 688547228  246 PEEIVDPNVDEHSVMTYLSQ----FP 267
Cdd:cd21189    80 PEDVDVPEPDEKSIITYVSSlydvFP 105
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1839-1903 9.90e-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: 74.56  E-value: 9.90e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   1839 FTVQ-----KGEITGEVHMPSGKTASPHITDNKDGTVTVKYAPTEKGLHEMDIKYDGNHIPGSPLQFYVD 1903
Cdd:smart00557   22 FTVDtrdagGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 171-266 4.00e-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: 73.22  E-value: 4.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  171 KQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPE 247
Cdd:cd21194     4 KDALLLWCQRKTagyPGVNIQNFTTSWRDGLAFNALIHAHRPDLI-DYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAE 82

                          90
                  ....*....|....*....
gi 688547228  248 EIVDPNVDEHSVMTYLSQF 266
Cdd:cd21194    83 DVDVARPDEKSIMTYVASY 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 48-148 6.10e-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: 72.76  E-value: 6.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   48 QNTFTRWCNEHLKC-LNRKILDLQKDLTDGLKLIGLLEVLSQKKMyRKYHARPNFRQMKLENVSVALEFLEREHI-KLVS 125
Cdd:cd00014     1 EEELLKWINEVLGEeLPVSITDLFESLRDGVLLCKLINKLSPGSI-PKINKKPKSPFKKRENINLFLNACKKLGLpELDL 79

                          90       100
                  ....*....|....*....|....
gi 688547228  126 IDSKAIV-DGNLKLILGLIWTLIL 148
Cdd:cd00014    80 FEPEDLYeKGNLKKVLGTLWALAL 103
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
 167-266 7.49e-15

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: 72.94  E-value: 7.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  167 KLTPKQRLLGWIQN---KVPQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQV 243
Cdd:cd21244     3 KMSARKALLLWAQEqcaKVGSISVTDFKSSWRNGLAFLAIIHALRPGLV-DMEKLKGRSNRENLEEAFRIAEQELKIPRL 81

                          90       100
                  ....*....|....*....|...
gi 688547228  244 IAPEEIVDPNVDEHSVMTYLSQF 266
Cdd:cd21244    82 LEPEDVDVVNPDEKSIMTYVAQF 104
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 167-266 9.28e-15

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: 72.59  E-value: 9.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  167 KLTPKQRLLGWIQNKVP---QLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQV 243
Cdd:cd21249     2 LRSAKEALLIWCQRKTAgytNVNVQDFSRSWRDGLAFNALIHAHRPDLI-DYGSLRPDRPLYNLANAFLVAEQELGISQL 80

                          90       100
                  ....*....|....*....|...
gi 688547228  244 IAPEEIVDPNVDEHSVMTYLSQF 266
Cdd:cd21249    81 LDPEDVAVPHPDERSIMTYVSLY 103
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 174-266 2.03e-14

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: 71.36  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  174 LLGWIQNKVPQ--LHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPEEIVD 251
Cdd:cd21245     8 LLNWVQRRTRKygVAVQDFGSSWRSGLAFLALIKAIDPSLV-DMRQALEKSPRENLEDAFRIAQESLGIPPLLEPEDVMV 86

                          90
                  ....*....|....*
gi 688547228  252 PNVDEHSVMTYLSQF 266
Cdd:cd21245    87 DSPDEQSIMTYVAQF 101
Filamin pfam00630
Filamin/ABP280 repeat;
2303-2351 5.02e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 69.63  E-value: 5.02e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 688547228  2303 VTSPSGNTEDAEIIEGEDSTYSVRFVPHEMGPHTVNVKYRGQHVPGSPF 2351
Cdd:pfam00630   40 VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 36-150 5.90e-14

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: 70.69  E-value: 5.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   36 DLAEDAPWK--KIQQnTFTRWCNEHLKCLNRKILDLQKDLTDGLKLI---GLLE----VLSQkkmyrkYHARPNFRQMKL 106
Cdd:cd21222     5 DLFDEAPEKlaEVKE-LLLQFVNKHLAKLNIEVTDLATQFHDGVYLIlliGLLEgffvPLHE------YHLTPSTDDEKL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 688547228  107 ENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHY 150
Cdd:cd21222    78 HNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 47-150 6.71e-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: 70.02  E-value: 6.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   47 QQNTFTRWCNEHLK--CLNRKILDLQKDLTDGLKLIGLLEVLSQKKMyRKYHARPNFRQMKLENVSVALEFLEREHIKLV 124
Cdd:cd21213     1 QLQAYVAWVNSQLKkrPGIRPVQDLRRDLRDGVALAQLIEILAGEKL-PGIDWNPTTDAERKENVEKVLQFMASKRIRMH 79

                          90       100
                  ....*....|....*....|....*.
gi 688547228  125 SIDSKAIVDGNLKLILGLIWTLILHY 150
Cdd:cd21213    80 QTSAKDIVDGNLKAIMRLILALAAHF 105
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 171-266 1.11e-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: 69.37  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  171 KQRLLGWIQNKVPQLH---INNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPE 247
Cdd:cd21192     5 EKALLKWVQAEIGKYYgirVTDFDKSWRDGVAFLALIHAIRPDLV-DMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEVE 83

                          90
                  ....*....|....*....
gi 688547228  248 EIVDPNVDEHSVMTYLSQF 266
Cdd:cd21192    84 DVLVDKPDERSIMTYVSQF 102
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
 169-266 1.17e-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: 69.65  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  169 TPKQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIA 245
Cdd:cd21319     5 SAKDALLLWCQMKTagyPNVNVTNFTSSWKDGLAFNALIHKHRPDLV-DFGKLKKSNARHNLEHAFNVAERQLGITKLLD 83

                          90       100
                  ....*....|....*....|.
gi 688547228  246 PEEIVDPNVDEHSVMTYLSQF 266
Cdd:cd21319    84 PEDVFTENPDEKSIITYVVAF 104
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 160-257 2.80e-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: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  160 EDDEDARKLTPKQRLLGWI-----QNKVPQLHINNFHRDWRDGKALGALVDNCAPGLCPD---WETWDPSQPVENAREAM 231
Cdd:cd21218     1 ETLESLLYLPPEEILLRWVnyhlkKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKelvLEVLSEEDLEKRAEKVL 80

                          90       100
                  ....*....|....*....|....*.
gi 688547228  232 QQADDwLGVPQVIAPEEIVDPNVDEH 257
Cdd:cd21218    81 QAAEK-LGCKYFLTPEDIVSGNPRLN 105
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 171-266 3.88e-13

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: 67.81  E-value: 3.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  171 KQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPE 247
Cdd:cd21248     4 KDALLLWCQMKTagyPNVNVRNFTTSWRDGLAFNALIHKHRPDLI-DYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPE 82

                          90
                  ....*....|....*....
gi 688547228  248 EIVDPNVDEHSVMTYLSQF 266
Cdd:cd21248    83 DVNVEQPDEKSIITYVVTY 101
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 158-266 1.93e-12

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: 66.62  E-value: 1.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  158 EDEDDEDARklTPKQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQA 234
Cdd:cd21322     8 ETEDNRETR--SAKDALLLWCQMKTagyPEVNIQNFTTSWRDGLAFNALIHRHRPDLI-DFSKLTKSNATYNLQQAFNTA 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 688547228  235 DDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQF 266
Cdd:cd21322    85 EQHLGLTKLLDPEDVNMEAPDEKSIITYVVSF 116
Filamin pfam00630
Filamin/ABP280 repeat;
1839-1897 2.25e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 65.00  E-value: 2.25e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688547228  1839 FTVQ----KGEITGEVHMPSGKTASPHITDNKDGTVTVKYAPTEKGLHEMDIKYDGNHIPGSP 1897
Cdd:pfam00630   25 FTVDtrdaGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSP 87
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 162-269 2.58e-12

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: 65.90  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  162 DEDARKLTPKQRLLGWIQNKVP---QLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWL 238
Cdd:cd21289     3 DISVEETSAKEGLLLWCQRKTApyrNVNVQNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKYL 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 688547228  239 GVPQVIAPEEIVD-PNVDEHSVMTYLSQFPKA 269
Cdd:cd21289    82 DIPKMLDAEDIVNtPKPDEKAIMTYVSCFYHA 113
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
 162-269 3.41e-12

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: 65.86  E-value: 3.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  162 DEDARKLTPKQRLLGWIQNKVP---QLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWL 238
Cdd:cd21288     3 DISVEETSAKEGLLLWCQRKTApyrNVNIQNFHTSWKDGLGLCALIHRHRPDLI-DYSKLNKDDPIGNINLAMEIAEKHL 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 688547228  239 GVPQVIAPEEIVD-PNVDEHSVMTYLSQFPKA 269
Cdd:cd21288    82 DIPKMLDAEDIVNtPKPDERAIMTYVSCFYHA 113
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
 162-269 1.28e-11

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: 63.95  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  162 DEDARKLTPKQRLLGWIQNKVP---QLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWL 238
Cdd:cd21290     6 DISVEETSAKEGLLLWCQRKTApykNVNVQNFHISWKDGLAFNALIHRHRPELI-EYDKLRKDDPVTNLNNAFEVAEKYL 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 688547228  239 GVPQVIAPEEIVD-PNVDEHSVMTYLSQFPKA 269
Cdd:cd21290    85 DIPKMLDAEDIVNtARPDEKAIMTYVSSFYHA 116
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 38-146 2.21e-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: 63.44  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   38 AEDAPWKKIqqntFTRWCNEHLKCLNRK--ILDLQKDLTDGLKLIGLLEVLSQKKMyRKYHARPNFRQMKLENVSVALEF 115
Cdd:cd21285     6 AENGFDKQI----YTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKI-EDINGCPKNRSQMIENIDACLSF 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 688547228  116 LEREHIKLVSIDSKAIVDGNLKLILGLIWTL 146
Cdd:cd21285    81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 168-266 2.55e-11

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: 62.93  E-value: 2.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  168 LTPKQRLLGWIQNKVP---QLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVI 244
Cdd:cd21291     9 LTAKEGLLLWCQRKTAgydEVDVQDFTTSWTDGLAFCALIHRHRPDLI-DYDKLDKKDHRGNMQLAFDIASKEIGIPQLL 87

                          90       100
                  ....*....|....*....|...
gi 688547228  245 APEEIVD-PNVDEHSVMTYLSQF 266
Cdd:cd21291    88 DVEDVCDvAKPDERSIMTYVAYY 110
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 172-266 2.56e-11

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: 62.69  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  172 QRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPEE 248
Cdd:cd22198     3 EELLSWCQEQTegyRGVKVTDLTSSWRSGLALCAIIHRFRPDLI-DFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQE 81

                          90
                  ....*....|....*....
gi 688547228  249 IVDPNV-DEHSVMTYLSQF 266
Cdd:cd22198    82 MASLAVpDKLSMVSYLSQF 100
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 168-264 1.25e-10

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: 60.80  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  168 LTPKQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCPDWETWDPSQpVENAREAMQQADDWLGVPQVI 244
Cdd:cd21238     1 MTAKEKLLLWSQRMVegyQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLL 79

                          90       100
                  ....*....|....*....|
gi 688547228  245 APEEIVDPNVDEHSVMTYLS 264
Cdd:cd21238    80 DPEDVDVPQPDEKSIITYVS 99
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 169-265 1.52e-10

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: 60.52  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  169 TPKQRLLGWIQN---KVPQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDwLGVPQVIA 245
Cdd:cd21198     1 SSGQDLLEWCQEvtkGYRGVKITNLTTSWRNGLAFCAILHHFRPDLI-DFSSLSPHDIKENCKLAFDAAAK-LGIPRLLD 78

                          90       100
                  ....*....|....*....|.
gi 688547228  246 PEEIVDPNV-DEHSVMTYLSQ 265
Cdd:cd21198    79 PADMVLLSVpDKLSVMTYLHQ 99
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 66-147 1.54e-10

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: 60.68  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   66 ILDLQKDLTDGLKLIGLLEVLSQkkmYRKYHARPNF----RQMKLENVSVALEFLER----EHIKLVSIDSKAIVDGNLK 137
Cdd:cd21223    26 VTNLAVDLRDGVRLCRLVELLTG---DWSLLSKLRVpaisRLQKLHNVEVALKALKEagvlRGGDGGGITAKDIVDGHRE 102

                          90
                  ....*....|
gi 688547228  138 LILGLIWTLI 147
Cdd:cd21223   103 KTLALLWRII 112
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 171-266 2.59e-10

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: 59.66  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  171 KQRLLGWIQ---NKVPQLHINNFHRDWRDGKALGALVDNCAPGLCPDW--ETWDPSQPVENAREAMQQADDW-LGVPQVI 244
Cdd:cd00014     1 EEELLKWINevlGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLgLPELDLF 80

                          90       100
                  ....*....|....*....|..
gi 688547228  245 APEEIVDPNvDEHSVMTYLSQF 266
Cdd:cd00014    81 EPEDLYEKG-NLKKVLGTLWAL 101
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 167-266 7.54e-10

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: 58.92  E-value: 7.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  167 KLTPKQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQV 243
Cdd:cd21321     3 KKSAKDALLLWCQMKTagyPNVNVHNFTTSWRDGLAFNAIVHKHRPDLI-DFETLKKSNAHYNLQNAFNVAEKELGLTKL 81

                          90       100
                  ....*....|....*....|...
gi 688547228  244 IAPEEIVDPNVDEHSVMTYLSQF 266
Cdd:cd21321    82 LDPEDVNVDQPDEKSIITYVATY 104
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 51-146 7.86e-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: 58.50  E-value: 7.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   51 FTRWCNEHL--KCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMyRKYHARPNFRQMKLENVSVALEFLEREHIKLVSIDS 128
Cdd:cd21286     5 YTDWANHYLakSGHKRLIKDLQQDIADGVLLAEIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 83

                          90
                  ....*....|....*...
gi 688547228  129 KAIVDGNLKLILGLIWTL 146
Cdd:cd21286    84 EEIRNGNLKAILGLFFSL 101
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
 162-269 1.61e-09

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: 58.17  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  162 DEDARKLTPKQRLLGWIQNKVP---QLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWL 238
Cdd:cd21287     3 DISVEETSAKEGLLLWCQRKTApykNVNIQNFHISWKDGLGFCALIHRHRPELI-DYGKLRKDDPLTNLNTAFDVAEKYL 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 688547228  239 GVPQVIAPEEIV-DPNVDEHSVMTYLSQFPKA 269
Cdd:cd21287    82 DIPKMLDAEDIVgTARPDEKAIMTYVSSFYHA 113
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 170-266 1.78e-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: 57.16  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  170 PKQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAP 246
Cdd:cd21197     1 KIQALLRWCRRQCegyPGVNITNLTSSFRDGLAFCAILHRHRPELI-DFHSLKKDNWLENNRLAFRVAETSLGIPALLDA 79

                          90       100
                  ....*....|....*....|.
gi 688547228  247 EEIVDPNV-DEHSVMTYLSQF 266
Cdd:cd21197    80 EDMVTMHVpDRLSIITYVSQY 100
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 169-266 7.02e-09

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: 55.88  E-value: 7.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  169 TPKQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIA 245
Cdd:cd21320     2 SAKDALLLWCQMKTagyPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 80

                          90       100
                  ....*....|....*....|.
gi 688547228  246 PEEIVDPNVDEHSVMTYLSQF 266
Cdd:cd21320    81 PEDISVDHPDEKSIITYVVTY 101
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 69-154 1.92e-08

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 54.55  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   69 LQKDLTDGLKLIGLLE-----VLSQKKMYRKYHA-RPNFRqmKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGL 142
Cdd:cd21298    27 LYSDLRDGLVLLQLYDkikpgVVDWSRVNKPFKKlGANMK--KIENCNYAVELGKKLKFSLVGIGGKDIYDGNRTLTLAL 104

                          90
                  ....*....|..
gi 688547228  143 IWTLILHYSISM 154
Cdd:cd21298   105 VWQLMRAYTLSI 116
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 169-265 2.39e-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: 54.09  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  169 TPKQRLLGWIQnKVPQLH----INNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDwLGVPQVI 244
Cdd:cd21254     1 NASQSLLAWCK-EVTKGYrgvkITNFTTSWRNGLAFCAILHHFRPDLI-DYKSLNPHDIKENNKKAYDGFAS-LGISRLL 77

                          90       100
                  ....*....|....*....|..
gi 688547228  245 APEEIVDPNV-DEHSVMTYLSQ 265
Cdd:cd21254    78 EPSDMVLLAVpDKLTVMTYLYQ 99
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 62-150 2.92e-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: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   62 LNRKILDLQKDLTDGLKLIGLLEVLSQK----KMYRKYHARPNFRqmKLENVSVALEFLEREHIKLVSIDSKAIVDGNLK 137
Cdd:cd21219    18 LDPLINNLYEDLRDGLVLLQVLDKIQPGcvnwKKVNKPKPLNKFK--KVENCNYAVDLAKKLGFSLVGIGGKDIADGNRK 95

                          90
                  ....*....|...
gi 688547228  138 LILGLIWTLILHY 150
Cdd:cd21219    96 LTLALVWQLMRYH 108
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 172-265 4.21e-08

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: 53.25  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  172 QRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDwLGVPQVIAPEE 248
Cdd:cd21255     4 QSLLEWCQEVTagyRGVRVTNFTTSWRNGLAFCAILHHFHPDLV-DYESLDPLDIKENNKKAFEAFAS-LGVPRLLEPAD 81

                          90
                  ....*....|....*...
gi 688547228  249 IVDPNV-DEHSVMTYLSQ 265
Cdd:cd21255    82 MVLLPIpDKLIVMTYLCQ 99
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 169-267 1.18e-07

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: 52.30  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  169 TPKQRLLGWIQNKVP---QLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDwLGVPQVIA 245
Cdd:cd21239     1 SAKERLLLWSQQMTEgytGIRCENFTTCWRDGRLFNAIIHKYRPDLI-DMNTVAVQSNLANLEHAFYVAEK-LGVTRLLD 78

                          90       100
                  ....*....|....*....|....*.
gi 688547228  246 PEEIVDPNVDEHSVMTYLSQ----FP 267
Cdd:cd21239    79 PEDVDVSSPDEKSVITYVSSlydvFP 104
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
 170-266 1.30e-07

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: 52.18  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  170 PKQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAP 246
Cdd:cd21252     1 ARRALQAWCRRQCegyPGVEIRDLSSSFRDGLAFCAILHRHRPDLI-DFDSLSKDNVYENNRLAFEVAERELGIPALLDP 79

                          90       100
                  ....*....|....*....|.
gi 688547228  247 EEIVDPNV-DEHSVMTYLSQF 266
Cdd:cd21252    80 EDMVSMKVpDCLSIMTYVSQY 100
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 174-266 1.62e-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: 51.66  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  174 LLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPEEIV 250
Cdd:cd21187     5 LLAWCRQSTrgyEQVDVKNFTTSWRDGLAFNALIHRHRPDLF-DFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVN 83

                          90
                  ....*....|....*.
gi 688547228  251 DPNVDEHSVMTYLSQF 266
Cdd:cd21187    84 VEQPDKKSILMYVTSL 99
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 168-267 2.20e-07

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: 51.58  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  168 LTPKQRLLGWIQnKV----PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDwLGVPQV 243
Cdd:cd21240     3 MSAKEKLLLWTQ-KVtagyTGIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGVTRL 79

                          90       100
                  ....*....|....*....|....*...
gi 688547228  244 IAPEEIVDPNVDEHSVMTYLSQ----FP 267
Cdd:cd21240    80 LDAEDVDVPSPDEKSVITYVSSiydaFP 107
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
 171-269 7.52e-07

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: 50.04  E-value: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  171 KQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpdwetwDPSQ-----PVENAREAMQQADDWLGVPQ 242
Cdd:cd21196     5 QEELLRWCQEQTagyPGVHVSDLSSSWADGLALCALVYRLQPGLL------EPSElqglgALEATAWALKVAENELGITP 78

                          90       100
                  ....*....|....*....|....*..
gi 688547228  243 VIAPEEIVdPNVDEHSVMTYLSQFPKA 269
Cdd:cd21196    79 VVSAQAVV-AGSDPLGLIAYLSHFHSA 104
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 174-264 8.97e-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: 49.57  E-value: 8.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  174 LLGWI-QNKVP--QLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPEEIV 250
Cdd:cd21234     5 LLSWVrQSTRPysQVNVLNFTTSWTDGLAFNAVLHRHKPDLF-SWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVA 83

                          90
                  ....*....|....
gi 688547228  251 DPNVDEHSVMTYLS 264
Cdd:cd21234    84 VQLPDKKSIIMYLT 97
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 174-264 1.93e-06

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


Pssm-ID: 409082  Cd Length: 111  Bit Score: 48.77  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  174 LLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQ-PVENAREAMQQADDWLGVPQVIAPEEI 249
Cdd:cd21233     5 LLSWVRQSTrnyPQVNVINFTSSWSDGLAFNALIHSHRPDLF-DWNSVVSQQsATERLDHAFNIARQHLGIEKLLDPEDV 83

                          90
                  ....*....|....*
gi 688547228  250 VDPNVDEHSVMTYLS 264
Cdd:cd21233    84 ATAHPDKKSILMYVT 98
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 186-266 3.63e-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: 47.73  E-value: 3.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  186 HINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPEEIVDPNV-DEHSVMTYLS 264
Cdd:cd21253    21 KVTNMTTSWRDGLAFCAIIHRFRPDLI-DFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDMVALKVpDKLSILTYVS 99


                  ..
gi 688547228  265 QF 266
Cdd:cd21253   100 QY 101
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
 173-266 8.17e-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: 46.96  E-value: 8.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  173 RLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPEEI 249
Cdd:cd21195     8 KLLTWCQQQTegyQHVNVTDLTTSWRSGLALCAIIHRFRPELI-NFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEM 86

                          90       100
                  ....*....|....*....|
gi 688547228  250 V---DPnvDEHSVMTYLSQF 266
Cdd:cd21195    87 AsaqEP--DKLSMVMYLSKF 104
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 171-274 8.21e-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: 47.29  E-value: 8.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  171 KQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPE 247
Cdd:cd21259     3 KQMLLDWCRAKTrgyENVDIQNFSSSWSDGMAFCALVHNFFPEAF-DYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVE 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 688547228  248 EIV---DPnvDEHSVMTYLSQFPKAKLKPG 274
Cdd:cd21259    82 DMVrmrEP--DWKCVYTYIQEFYRCLVQKG 109
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 171-266 1.18e-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: 46.57  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  171 KQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPE 247
Cdd:cd21200     3 KQMLLEWCQAKTrgyEHVDITNFSSSWSDGMAFCALIHHFFPDAF-DYSSLDPKNRRKNFELAFSTAEELADIAPLLEVE 81

                          90       100
                  ....*....|....*....|.
gi 688547228  248 EIV--DPNVDEHSVMTYLSQF 266
Cdd:cd21200    82 DMVrmGNRPDWKCVFTYVQSL 102
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 31-154 1.26e-05

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 47.30  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   31 PATEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHaRPNFRQM- 104
Cdd:cd21331     2 PALTKPENQDIDWTLLEgetreERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVN-KPPYPKLg 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 688547228  105 ----KLENVSVALEF-LEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 154
Cdd:cd21331    79 anmkKLENCNYAVELgKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNV 133
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
 174-265 1.77e-05

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: 46.20  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  174 LLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCPdWETWDPSQPVENAREAMQQADDwLGVPQVIAPEEIV 250
Cdd:cd21199    13 LLKWCQEKTqgyKGIDITNFSSSWNDGLAFCALLHSYLPDKIP-YSELNPQDKRRNFTLAFKAAES-VGIPTTLTIDEMV 90

                          90
                  ....*....|....*.
gi 688547228  251 -DPNVDEHSVMTYLSQ 265
Cdd:cd21199    91 sMERPDWQSVMSYVTA 106
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 51-147 3.84e-05

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 45.26  E-value: 3.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   51 FTRWCN------EHLKCLnrKILDLQKD-----LTDGL---KLIGL-------LEVLSQKKMYRKYHARpnfrqmklENV 109
Cdd:cd21217     6 FVEHINslladdPDLKHL--LPIDPDGDdlfeaLRDGVllcKLINKivpgtidERKLNKKKPKNIFEAT--------ENL 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 688547228  110 SVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLI 147
Cdd:cd21217    76 NLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 158-253 5.36e-05

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: 44.87  E-value: 5.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  158 EDEDDEDARKLTPKQRLLGWIQNKVPQL---HINNFHRDWRDGKALGALVDNCAP-------GLCPDWETWDPSQPVENA 227
Cdd:cd21326     1 EGEELEELMKLSPEELLLRWVNYHLTNAgwqNISNFSQDIKDSRAYFHLLNQIAPkgdvfdeNIEIDFSGFNEKNDLKRA 80

                          90       100
                  ....*....|....*....|....*.
gi 688547228  228 REAMQQADDwLGVPQVIAPEEIVDPN 253
Cdd:cd21326    81 EYMLQEADK-LGCRQFVTPADVVSGN 105
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 56-150 1.05e-04

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: 44.26  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   56 NEHLKCLNRKILDLQKDLTDG---LKLIGLLEVLSQKkmYRKYHARPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIV 132
Cdd:cd21307    26 NKHLGNLGLNVKDLDSQFADGvilLLLIGQLEGFFIH--LSEFFLTPSSTSEMLHNVTLALELLKEGGLLNFPVNPEDIV 103

                          90
                  ....*....|....*...
gi 688547228  133 DGNLKLILGLIWTLILHY 150
Cdd:cd21307   104 NGDSKATIRVLYCLFSKY 121
CH_PLS3_rpt2 cd21328
second calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 158-253 1.73e-04

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


Pssm-ID: 409177 [Multi-domain]  Cd Length: 122  Bit Score: 43.42  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  158 EDEDDEDARKLTPKQRLLGW----IQNKVPQlHINNFHRDWRDGKALGALVDNCAP-GLCPDWETWDPSQPVENAR---- 228
Cdd:cd21328     4 DGETLEDLMKLSPEELLLRWanfhLENAGWQ-KINNFSSDIKDSRAYFHLLNQIAPkGQKEGEPRIDINMSGFNEKddlk 82

                          90       100
                  ....*....|....*....|....*..
gi 688547228  229 --EAMQQADDWLGVPQVIAPEEIVDPN 253
Cdd:cd21328    83 raEYMLQQADKLGCRQFVTPADVVSGN 109
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
 158-253 2.30e-04

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: 43.03  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  158 EDEDDEDARKLTPKQRLLGWI----QNKVPQLHINNFHRDWRDGKALGALVDNCAP-GLCPDWETWDPSQPVENAREAMQ 232
Cdd:cd21295     1 DGETLEDLLKLSPEEILLRWVnyhlERAGCDRRIKNFSGDIKDSEAYTHLLKQIAPkDAGVDTSALRESDLLQRAELMLQ 80

                          90       100
                  ....*....|....*....|.
gi 688547228  233 QADDwLGVPQVIAPEEIVDPN 253
Cdd:cd21295    81 NADK-IGCRKFVTPKDVVTGN 100
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 39-154 3.08e-04

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: 43.05  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   39 EDAPWKKIQ-----QNTFTRWCNEhlKCLNRKILDLQKDLTDGLKLIGLLEVLSQKKMYRKYHaRPNFRQM-----KLEN 108
Cdd:cd21330     1 QDIDWSSIEgetreERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVN-KPPYPKLgenmkKLEN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 688547228  109 VSVALEFLERE-HIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 154
Cdd:cd21330    78 CNYAVELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNI 124
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 170-266 3.16e-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: 42.45  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  170 PKQRLLGWIQNKVPQ---LHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAP 246
Cdd:cd21226     1 SEDGLLAWCRQTTEGydgVNITSFKSSFNDGRAFLALLHAYDPELF-KQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEA 79

                          90       100
                  ....*....|....*....|
gi 688547228  247 EEIVDPNVDEHSVMTYLSQF 266
Cdd:cd21226    80 EDVMTGNPDERSIVLYTSLF 99
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
 173-266 4.91e-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: 41.86  E-value: 4.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  173 RLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPEE- 248
Cdd:cd21251     9 KLLGWCQRQTegyAGVNVTDLTMSWKSGLALCAIIHRYRPDLI-DFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEm 87

                          90       100
                  ....*....|....*....|
gi 688547228  249 --IVDPnvDEHSVMTYLSQF 266
Cdd:cd21251    88 asVGEP--DKLSMVMYLTQF 105
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 51-146 5.38e-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: 42.03  E-value: 5.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   51 FTRWCNEhlkcLNRK--ILDLQKDLTDGLKLIGLLEVLSQKKM-YRKYHARPNFRQMK----LENVSVALEFLEREHIKL 123
Cdd:cd21300    12 FTLWLNS----LDVEpaVNDLFEDLRDGLILLQAYDKVIPGSVnWKKVNKAPASAEISrfkaVENTNYAVELGKQLGFSL 87

                          90       100
                  ....*....|....*....|...
gi 688547228  124 VSIDSKAIVDGNLKLILGLIWTL 146
Cdd:cd21300    88 VGIQGADITDGSRTLTLALVWQL 110
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
 37-150 5.81e-04

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: 42.27  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   37 LAEDAPWK-KIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQK--KMYRKYHARPNFRQmKLENVSVAL 113
Cdd:cd21338    11 LFDHAPDKlSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYfvPLHNFYLTPESFDQ-KVHNVSFAF 89

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 688547228  114 EFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHY 150
Cdd:cd21338    90 ELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKY 126
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 165-268 1.09e-03

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


Pssm-ID: 409106  Cd Length: 112  Bit Score: 41.17  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  165 ARKLTPKQR--LLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCPdWETWDPSQPVENAREAMQQADDwLG 239
Cdd:cd21257     2 AREYGGSKRnaLLKWCQKKTegyPNIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQDKKRNLLLAFQAAES-VG 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 688547228  240 V-PQVIAPEEIVDPNVDEHSVMTYLSQFPK 268
Cdd:cd21257    80 IkPSLELSEMMYTDRPDWQSVMQYVAQIYK 109
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 72-154 1.53e-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: 40.56  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   72 DLTDGLKLIGLLEVLSQKKMYRKYHARP----NFRqmKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLI 147
Cdd:cd21299    28 DVRDGWVLLEVLDKVSPGSVNWKHANKPpikmPFK--KVENCNQVVKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLM 105


                  ....*..
gi 688547228  148 LHYSISM 154
Cdd:cd21299   106 RYHMLQL 112
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
 37-150 1.58e-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: 41.13  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   37 LAEDAPWK-KIQQNTFTRWCNEHLKCLNRKILDLQKDLTDGLKLIGLLEVLSQK--KMYRKYHARPNFRQmKLENVSVAL 113
Cdd:cd21337    10 LFDHAPDKlNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYfvPLHSFFLTPDSFEQ-KVLNVSFAF 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 688547228  114 EFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHY 150
Cdd:cd21337    89 ELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKY 125
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
 171-263 3.15e-03

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


Pssm-ID: 409110  Cd Length: 107  Bit Score: 39.56  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  171 KQRLLGWIQNKV---PQLHINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQADDWLGVPQVIAPE 247
Cdd:cd21261     3 KQILLEWCRSKTigyKNIDLQNFSSSWSDGMAFCALVHSFFPEAF-DYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVE 81

                          90
                  ....*....|....*...
gi 688547228  248 E--IVDPNVDEHSVMTYL 263
Cdd:cd21261    82 DmmVMGRKPDPMCVFTYV 99
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 160-251 3.16e-03

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


Pssm-ID: 409145  Cd Length: 109  Bit Score: 39.42  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228  160 EDDEDARKLTPKQRLLGWIQNKVPQL----HINNFHRDWRDGKALGALVDNCAPGLCpDWETWDPSQPVENAREAMQQAD 235
Cdd:cd21296     1 EDVEELLRLPPEKVLLKWMNFHLKKAgykkTVTNFSSDVKDAEAYAYLLNVLAPEHC-DPATLEAKDPLERAKLVLEQAE 79

                          90
                  ....*....|....*.
gi 688547228  236 DwLGVPQVIAPEEIVD 251
Cdd:cd21296    80 K-MNCKRYLTAKDIVE 94
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 54-150 5.33e-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: 39.32  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688547228   54 WCNEHLKCLNRKILDLQKDLTDGLKLI---GLLEvlsqkkMY----RKYHARPNFRQMKLENVSVALEFLEREHIKLVSI 126
Cdd:cd21306    24 FVNKHLNKLNLEVTDLDTQFHDGVYLVllmGLLE------GYfvplHSFHLTPTSFEQKVHNVQFAFELMQDAGLPKPKA 97

                          90       100
                  ....*....|....*....|....
gi 688547228  127 DSKAIVDGNLKLILGLIWTLILHY 150
Cdd:cd21306    98 RPEDIVNLDLKSTLRVLYNLFTKY 121
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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