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Conserved domains on  [gi|320542951|ref|NP_001189238|]
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cheerio, isoform I [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 32-154 6.63e-83

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


:

Pssm-ID: 409160  Cd Length: 124  Bit Score: 267.40  E-value: 6.63e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   32 EAERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVA 111
Cdd:cd21311     1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 320542951  112 LKFLQ-DEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMP 154
Cdd:cd21311    81 LKFLEeDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISMP 124
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 155-272 1.46e-79

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: 257.79  E-value: 1.46e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  155 MWDGEDDKQLNGSGHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGL 234
Cdd:cd21315     1 MWEGEDDGPDDGKGPTPKQRLLGWIQSKVPDLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAVKNAKEAMDL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 320542951  235 ADDWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPNSKL 272
Cdd:cd21315    81 AEDWLDVPQLIKPEEMVNPKVDELSMMTYLSQFPNAKL 118
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 965-1055 7.97e-31

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 117.32  E-value: 7.97e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    965 PARCKAYGPGLEKGLTNQKNKFTVETKGAGNGGLSLAIEGPS--EAKMTCTDNRDGSCDVDYLATDPGEYDITIRFADKH 1042
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 320542951   1043 IPGSPFRVLVEET 1055
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1835-1923 1.13e-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: 116.93  E-value: 1.13e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1835 HLVKAGGSGLERGVVGEAAEFNVWTREAGGGSLAISVEGPS--KADIEFKDRKDGSCDVSYKVTEPGEYRVGLKFNDRHI 1912
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|.
gi 320542951   1913 PDSPFKVYVSP 1923
Cdd:smart00557   82 PGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1641-1730 5.10e-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: 5.10e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1641 AKKVKVSGTGLKEGQTHADNIFSVDTRNAGFGGLSVSIEGPS--KAEIQCTDKDDGTLNISYKPTEPGYYIVNLKFADHH 1718
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 320542951   1719 VEGSPFTVKVAG 1730
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1460-1547 5.35e-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: 112.31  E-value: 5.35e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1460 YVTAYGPGLTHGVTGEPANFTISTKGASAGGLTMAVEGPS--KADINYHDNKDGTVSVQYLPTAPGEYQVSVRFGDKHIK 1537
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|
gi 320542951   1538 GSPYFAKITG 1547
Cdd:smart00557   83 GSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 673-765 4.72e-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: 4.72e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    673 PELVKASGPGLEKngVTINQPTSFTVDPSKAGNAPLDVVVQDVFGTKLPVELKNNPDGTKKVTYTPTSGVPHTVEVNYGG 752
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|...
gi 320542951    753 VSTPNSPHRVYVG 765
Cdd:smart00557   79 EHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 284-379 6.02e-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: 6.02e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    284 PNRVRAYGPGIEPIgpVVGAPANFTVETFSAGKGSVDVDIQGPNGEIEKADVRFNNDKnlTYTVSYIPKSEGSHKVAVKF 363
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDG--TYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*.
gi 320542951    364 SGRDIPKSPFPVKVEG 379
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 483-576 1.06e-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: 99.99  E-value: 1.06e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    483 ARKVRASGRGLQatGVRVGDDADFKIYTEGAGEGEPEVRVIGPGGMNQNVMQSKVDGNTYECHYYPTKEGRYVIMVTFAG 562
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....
gi 320542951    563 QEVAKSPFEVKVGP 576
Cdd:smart00557   79 EHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 384-479 5.32e-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: 98.06  E-value: 5.32e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    384 ASKVKVTGPGIQPngVTIKKPTFFDILAKDAGRGVPEVIIIDPANHKtsVAAKVRQLENDTWRCEYVTALQGLHSVNVFY 463
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*.
gi 320542951    464 AGTPIPNSPFPVKVAP 479
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2023-2111 2.16e-23

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 96.13  E-value: 2.16e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   2023 PAAVHASGNGLDEVKTGHKADFIINTCNAGVGTLAVSIDGPS--KVAMDCTEVEEG-YKVRYTPLLPGEHYITVKYNNMH 2099
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 320542951   2100 IVGSPFKVNATG 2111
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2151-2240 5.99e-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: 94.98  E-value: 5.99e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   2151 ASKVVSKGMGLKKAYIGKQNQFSISATDAGNNILYVGMYGPKGPCEEFHVKHAGHNNYNVQYLVRDRGQYVLLIKWGEEH 2230
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 320542951   2231 IPGSPFQIDV 2240
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 580-667 2.16e-22

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.44  E-value: 2.16e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    580 SSIVAYGPGLSSGVIGYPAAFVVETNG-ETGALGFTVAGPSQ--AEIECHDNGDGSALVKYHPTAVGEYAVHILCDNEDI 656
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDaGGGELEVEVTGPSGkkVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|.
gi 320542951    657 PKSPFIAQILP 667
Cdd:smart00557   82 PGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1058-1153 3.48e-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: 92.67  E-value: 3.48e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1058 PSKVKVYGPGIEHGQVREsvPTFFNVDVGEAGPGRIAVKLTNSEGIPVDnLRVEDKGNCIYAVHYVPPKAGsVLTCQVKF 1137
Cdd:smart00557    1 ASKVKASGPGLEKGVVGE--PAEFTVDTRDAGGGELEVEVTGPSGKKVP-VEVKDNGDGTYTVSYTPTEPG-DYTVTVKF 76

                            90
                    ....*....|....*.
gi 320542951   1138 SEVEVPCSPFVMTVFP 1153
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1157-1250 5.29e-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: 92.28  E-value: 5.29e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1157 PTKVKVKGVNEKKKTpASLPAEFEIDTKQAGQADINVAIKNPKGKAMQPRLEEVSTGTYVVSFVPDECGTYQCSIKYGDK 1236
Cdd:smart00557    1 ASKVKASGPGLEKGV-VGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 320542951   1237 EIEGSPFKLEAFPT 1250
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1928-2017 6.05e-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: 83.42  E-value: 6.05e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1928 AHKLEVQQFPQGNIQADAPYQFMVRKNGA-KGELDAKIVAPSGTDDDCFIQVIDGEMYSVRFYPRENGIHAIHVKFNGVH 2006
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 320542951   2007 IPDSPFRIKVG 2017
Cdd:smart00557   81 IPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1394-1454 2.54e-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: 78.80  E-value: 2.54e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320542951   1394 GGNVTAEVRMPSGKVDKPVIQDNRDGTVSVKYDPREEGSHELVVKYNGEPVQGSPFKFHVD 1454
Cdd:smart00557   31 GGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 770-853 2.38e-16

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 76.10  E-value: 2.38e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    770 AAKVQAFGPWLQPGvRPNAATHFNVDAREAGDAELKVKIIHEETKiEVPCRIIDNEDNTYSVEVIPPSKGAYTTTMTYGG 849
Cdd:smart00557    1 ASKVKASGPGLEKG-VVGEPAEFTVDTRDAGGGELEVEVTGPSGK-KVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78


                    ....
gi 320542951    850 QRVP 853
Cdd:smart00557   79 EHIP 82
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 867-960 1.52e-15

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 73.79  E-value: 1.52e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    867 SKIKVD--GLEPSVImNAATDFMVDMSKVGSnidsGKLSCAIFDPMGHVLPSKIVQGPtDDIFRIMYTPFEAGRHTIELM 944
Cdd:smart00557    2 SKVKASgpGLEKGVV-GEPAEFTVDTRDAGG----GELEVEVTGPSGKKVPVEVKDNG-DGTYTVSYTPTEPGDYTVTVK 75

                            90
                    ....*....|....*.
gi 320542951    945 YDNIPVPGSPFVVNVK 960
Cdd:smart00557   76 FGGEHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1269-1345 1.39e-13

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 68.40  E-value: 1.39e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320542951   1269 GSQSHLKVDAREAGDGAVTCKITNKAGSEiVDIDVIE-KDGFFDILYALNDPGDYDINVKFGGKDIPNGSFSIKAVES 1345
Cdd:smart00557   17 GEPAEFTVDTRDAGGGELEVEVTGPSGKK-VPVEVKDnGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1774-1822 4.74e-11

Filamin/ABP280 repeat;


:

Pssm-ID: 395505  Cd Length: 89  Bit Score: 60.77  E-value: 4.74e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 320542951  1774 VTSPSNVTEDAEIQEVEDGLYAVHFVPKELGVHTVSVRYSEMHIPGSPF 1822
Cdd:pfam00630   40 VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
 
Name Accession Description Interval E-value
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 32-154 6.63e-83

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


Pssm-ID: 409160  Cd Length: 124  Bit Score: 267.40  E-value: 6.63e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   32 EAERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVA 111
Cdd:cd21311     1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 320542951  112 LKFLQ-DEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMP 154
Cdd:cd21311    81 LKFLEeDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISMP 124
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 155-272 1.46e-79

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: 257.79  E-value: 1.46e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  155 MWDGEDDKQLNGSGHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGL 234
Cdd:cd21315     1 MWEGEDDGPDDGKGPTPKQRLLGWIQSKVPDLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAVKNAKEAMDL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 320542951  235 ADDWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPNSKL 272
Cdd:cd21315    81 AEDWLDVPQLIKPEEMVNPKVDELSMMTYLSQFPNAKL 118
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
39-267 1.43e-31

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 133.14  E-value: 1.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   39 EDAQWKKIQQNTFTRWANEHLKTID-RSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQD 117
Cdd:COG5069     2 EAKKWQKVQKKTFTKWTNEKLISGGqKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  118 EGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMPMWDGEDDKQLNgsghtpkqrLLNWIHAKI----PDLPINNFTN 193
Cdd:COG5069    82 KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGELTKHIN---------LLLWCDEDTggykPEVDTFDFFR 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320542951  194 DWTTGKAVGALVDACAP-GLCPDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELVNPNV-DEQSMMTYLSQY 267
Cdd:COG5069   153 SWRDGLAFSALIHDSRPdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSWY 228
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 965-1055 7.97e-31

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 117.32  E-value: 7.97e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    965 PARCKAYGPGLEKGLTNQKNKFTVETKGAGNGGLSLAIEGPS--EAKMTCTDNRDGSCDVDYLATDPGEYDITIRFADKH 1042
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 320542951   1043 IPGSPFRVLVEET 1055
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1835-1923 1.13e-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: 116.93  E-value: 1.13e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1835 HLVKAGGSGLERGVVGEAAEFNVWTREAGGGSLAISVEGPS--KADIEFKDRKDGSCDVSYKVTEPGEYRVGLKFNDRHI 1912
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|.
gi 320542951   1913 PDSPFKVYVSP 1923
Cdd:smart00557   82 PGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1641-1730 5.10e-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: 5.10e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1641 AKKVKVSGTGLKEGQTHADNIFSVDTRNAGFGGLSVSIEGPS--KAEIQCTDKDDGTLNISYKPTEPGYYIVNLKFADHH 1718
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 320542951   1719 VEGSPFTVKVAG 1730
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1460-1547 5.35e-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: 112.31  E-value: 5.35e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1460 YVTAYGPGLTHGVTGEPANFTISTKGASAGGLTMAVEGPS--KADINYHDNKDGTVSVQYLPTAPGEYQVSVRFGDKHIK 1537
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|
gi 320542951   1538 GSPYFAKITG 1547
Cdd:smart00557   83 GSPFTVKVGP 92
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 49-148 4.37e-27

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 107.02  E-value: 4.37e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951     49 NTFTRWANEHL-KTIDRSINNLETDLSDGLRLIALIEVLSQKRMPK-YNKRPTFRSQKLENVSVALKFLQDEGIKIVNID 126
Cdd:smart00033    1 KTLLRWVNSLLaEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 320542951    127 SSDIVDcKLKLILGLIWTLILH 148
Cdd:smart00033   81 PEDLVE-GPKLILGVIWTLISL 101
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 673-765 4.72e-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: 4.72e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    673 PELVKASGPGLEKngVTINQPTSFTVDPSKAGNAPLDVVVQDVFGTKLPVELKNNPDGTKKVTYTPTSGVPHTVEVNYGG 752
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|...
gi 320542951    753 VSTPNSPHRVYVG 765
Cdd:smart00557   79 EHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 284-379 6.02e-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: 6.02e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    284 PNRVRAYGPGIEPIgpVVGAPANFTVETFSAGKGSVDVDIQGPNGEIEKADVRFNNDKnlTYTVSYIPKSEGSHKVAVKF 363
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDG--TYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*.
gi 320542951    364 SGRDIPKSPFPVKVEG 379
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 483-576 1.06e-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: 99.99  E-value: 1.06e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    483 ARKVRASGRGLQatGVRVGDDADFKIYTEGAGEGEPEVRVIGPGGMNQNVMQSKVDGNTYECHYYPTKEGRYVIMVTFAG 562
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....
gi 320542951    563 QEVAKSPFEVKVGP 576
Cdd:smart00557   79 EHIPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
963-1049 1.70e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 99.29  E-value: 1.70e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   963 CDPARCKAYGPGLEKGLTNQKNKFTVETKGAGnGGLSLAIEGPS--EAKMTCTDNRDGSCDVDYLATDPGEYDITIRFAD 1040
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 320542951  1041 KHIPGSPFR 1049
Cdd:pfam00630   81 QHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 384-479 5.32e-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: 98.06  E-value: 5.32e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    384 ASKVKVTGPGIQPngVTIKKPTFFDILAKDAGRGVPEVIIIDPANHKtsVAAKVRQLENDTWRCEYVTALQGLHSVNVFY 463
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*.
gi 320542951    464 AGTPIPNSPFPVKVAP 479
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
1638-1725 7.90e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 97.36  E-value: 7.90e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1638 VGDAKKVKVSGTGLKEGQTHADNIFSVDTRNAGfGGLSVSIEGPS--KAEIQCTDKDDGTLNISYKPTEPGYYIVNLKFA 1715
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 320542951  1716 DHHVEGSPFT 1725
Cdd:pfam00630   80 GQHIPGSPFK 89
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 45-151 1.41e-23

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 97.36  E-value: 1.41e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    45 KIQQNTFTRWANEHLK--TIDRSINNLETDLSDGLRLIALIEVLSQKrMPKYNKRPTFRSQKLENVSVALKFLQDE-GIK 121
Cdd:pfam00307    1 LELEKELLRWINSHLAeyGPGVRVTNFTTDLRDGLALCALLNKLAPG-LVDKKKLNKSEFDKLENINLALDVAEKKlGVP 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 320542951   122 IVNIDSSDIVDCKLKLILGLIWTLILHYSI 151
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2023-2111 2.16e-23

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 96.13  E-value: 2.16e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   2023 PAAVHASGNGLDEVKTGHKADFIINTCNAGVGTLAVSIDGPS--KVAMDCTEVEEG-YKVRYTPLLPGEHYITVKYNNMH 2099
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 320542951   2100 IVGSPFKVNATG 2111
Cdd:smart00557   81 IPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
282-373 3.02e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 95.82  E-value: 3.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   282 TNPNRVRAYGPGIEPigPVVGAPANFTVETFSAGkGSVDVDIQGPNGEIEKADVRFNNDKnlTYTVSYIPKSEGSHKVAV 361
Cdd:pfam00630    2 ADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDG--TYTVSYTPTEPGDYTVSV 76

                           90
                   ....*....|..
gi 320542951   362 KFSGRDIPKSPF 373
Cdd:pfam00630   77 KFNGQHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2151-2240 5.99e-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: 94.98  E-value: 5.99e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   2151 ASKVVSKGMGLKKAYIGKQNQFSISATDAGNNILYVGMYGPKGPCEEFHVKHAGHNNYNVQYLVRDRGQYVLLIKWGEEH 2230
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 320542951   2231 IPGSPFQIDV 2240
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 580-667 2.16e-22

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.44  E-value: 2.16e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    580 SSIVAYGPGLSSGVIGYPAAFVVETNG-ETGALGFTVAGPSQ--AEIECHDNGDGSALVKYHPTAVGEYAVHILCDNEDI 656
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDaGGGELEVEVTGPSGkkVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|.
gi 320542951    657 PKSPFIAQILP 667
Cdd:smart00557   82 PGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1058-1153 3.48e-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: 92.67  E-value: 3.48e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1058 PSKVKVYGPGIEHGQVREsvPTFFNVDVGEAGPGRIAVKLTNSEGIPVDnLRVEDKGNCIYAVHYVPPKAGsVLTCQVKF 1137
Cdd:smart00557    1 ASKVKASGPGLEKGVVGE--PAEFTVDTRDAGGGELEVEVTGPSGKKVP-VEVKDNGDGTYTVSYTPTEPG-DYTVTVKF 76

                            90
                    ....*....|....*.
gi 320542951   1138 SEVEVPCSPFVMTVFP 1153
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1157-1250 5.29e-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: 92.28  E-value: 5.29e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1157 PTKVKVKGVNEKKKTpASLPAEFEIDTKQAGQADINVAIKNPKGKAMQPRLEEVSTGTYVVSFVPDECGTYQCSIKYGDK 1236
Cdd:smart00557    1 ASKVKASGPGLEKGV-VGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 320542951   1237 EIEGSPFKLEAFPT 1250
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1837-1918 6.05e-22

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 91.97  E-value: 6.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1837 VKAGGSGLERGVVGEAAEFNVWTREAGGGsLAISVEGPS--KADIEFKDRKDGSCDVSYKVTEPGEYRVGLKFNDRHIPD 1914
Cdd:pfam00630    7 VKASGPGLEPGVVGKPAEFTVDTRDAGGE-GEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPG 85


                   ....
gi 320542951  1915 SPFK 1918
Cdd:pfam00630   86 SPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1461-1541 8.52e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 88.50  E-value: 8.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1461 VTAYGPGLTHGVTGEPANFTISTKGASaGGLTMAVEGPS--KADINYHDNKDGTVSVQYLPTAPGEYQVSVRFGDKHIKG 1538
Cdd:pfam00630    7 VKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPG 85


                   ...
gi 320542951  1539 SPY 1541
Cdd:pfam00630   86 SPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
481-571 1.12e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.42  E-value: 1.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   481 SDARKVRASGRGLQatGVRVGDDADFKIYTEGAGeGEPEVRVIGPGGMNQNVMQSKVDGNTYECHYYPTKEGRYVIMVTF 560
Cdd:pfam00630    2 ADASKVKASGPGLE--PGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 320542951   561 AGQEVAKSPFE 571
Cdd:pfam00630   79 NGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
580-662 1.13e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.42  E-value: 1.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   580 SSIVAYGPGLSSGVIGYPAAFVVETNGETGALGFTVAGPS--QAEIECHDNGDGSALVKYHPTAVGEYAVHILCDNEDIP 657
Cdd:pfam00630    5 SKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIP 84


                   ....*
gi 320542951   658 KSPFI 662
Cdd:pfam00630   85 GSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
671-759 5.49e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 83.49  E-value: 5.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   671 FHPELVKASGPGLEknGVTINQPTSFTVDPSKAGNaPLDVVVQDVFGTKLPVELKNNPDGTKKVTYTPTSGVPHTVEVNY 750
Cdd:pfam00630    2 ADASKVKASGPGLE--PGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78


                   ....*....
gi 320542951   751 GGVSTPNSP 759
Cdd:pfam00630   79 NGQHIPGSP 87
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1928-2017 6.05e-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: 83.42  E-value: 6.05e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1928 AHKLEVQQFPQGNIQADAPYQFMVRKNGA-KGELDAKIVAPSGTDDDCFIQVIDGEMYSVRFYPRENGIHAIHVKFNGVH 2006
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 320542951   2007 IPDSPFRIKVG 2017
Cdd:smart00557   81 IPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
381-473 7.42e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 83.11  E-value: 7.42e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   381 AGDASKVKVTGPGIQPngVTIKKPTFFDILAKDAGrGVPEVIIIDPANHKtsVAAKVRQLENDTWRCEYVTALQGLHSVN 460
Cdd:pfam00630    1 AADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSP--VPVEVTDNGDGTYTVSYTPTEPGDYTVS 75

                           90
                   ....*....|...
gi 320542951   461 VFYAGTPIPNSPF 473
Cdd:pfam00630   76 VKFNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
2020-2106 1.27e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 82.34  E-value: 1.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  2020 VADPAAVHASGNGLDEVKTGHKADFIINTCNAGvGTLAVSIDGPS--KVAMDCTEVEEG-YKVRYTPLLPGEHYITVKYN 2096
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 320542951  2097 NMHIVGSPFK 2106
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1155-1244 2.09e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 78.87  E-value: 2.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1155 SEPTKVKVKGVNeKKKTPASLPAEFEIDTKQAGQaDINVAIKNPKGKAMQPRLEEVSTGTYVVSFVPDECGTYQCSIKYG 1234
Cdd:pfam00630    2 ADASKVKASGPG-LEPGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 320542951  1235 DKEIEGSPFK 1244
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1394-1454 2.54e-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: 78.80  E-value: 2.54e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320542951   1394 GGNVTAEVRMPSGKVDKPVIQDNRDGTVSVKYDPREEGSHELVVKYNGEPVQGSPFKFHVD 1454
Cdd:smart00557   31 GGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 770-853 2.38e-16

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 76.10  E-value: 2.38e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    770 AAKVQAFGPWLQPGvRPNAATHFNVDAREAGDAELKVKIIHEETKiEVPCRIIDNEDNTYSVEVIPPSKGAYTTTMTYGG 849
Cdd:smart00557    1 ASKVKASGPGLEKG-VVGEPAEFTVDTRDAGGGELEVEVTGPSGK-KVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78


                    ....
gi 320542951    850 QRVP 853
Cdd:smart00557   79 EHIP 82
Filamin pfam00630
Filamin/ABP280 repeat;
767-853 1.40e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 73.86  E-value: 1.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   767 PVDAAKVQAFGPWLQPGvRPNAATHFNVDAREAGDaELKVKIIHEETKiEVPCRIIDNEDNTYSVEVIPPSKGAYTTTMT 846
Cdd:pfam00630    1 AADASKVKASGPGLEPG-VVGKPAEFTVDTRDAGG-EGEVEVTGPDGS-PVPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77


                   ....*..
gi 320542951   847 YGGQRVP 853
Cdd:pfam00630   78 FNGQHIP 84
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 867-960 1.52e-15

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 73.79  E-value: 1.52e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    867 SKIKVD--GLEPSVImNAATDFMVDMSKVGSnidsGKLSCAIFDPMGHVLPSKIVQGPtDDIFRIMYTPFEAGRHTIELM 944
Cdd:smart00557    2 SKVKASgpGLEKGVV-GEPAEFTVDTRDAGG----GELEVEVTGPSGKKVPVEVKDNG-DGTYTVSYTPTEPGDYTVTVK 75

                            90
                    ....*....|....*.
gi 320542951    945 YDNIPVPGSPFVVNVK 960
Cdd:smart00557   76 FGGEHIPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
1056-1148 2.67e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 73.09  E-value: 2.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1056 VDPSKVKVYGPGIEHGQVreSVPTFFNVDVGEAGpGRIAVKLTNSEGIPVDNlRVEDKGNCIYAVHYVPPKAGsVLTCQV 1135
Cdd:pfam00630    2 ADASKVKASGPGLEPGVV--GKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPV-EVTDNGDGTYTVSYTPTEPG-DYTVSV 76

                           90
                   ....*....|...
gi 320542951  1136 KFSEVEVPCSPFV 1148
Cdd:pfam00630   77 KFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1925-2013 4.52e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 72.32  E-value: 4.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1925 AGDAHKLEVQQFPQGNIQADAPYQFMVRKNGAKGELDAKIVAPSGTDDDCFIQVIDGEMYSVRFYPRENGIHAIHVKFNG 2004
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 320542951  2005 VHIPDSPFR 2013
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
864-956 8.60e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 71.55  E-value: 8.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   864 VDVSKIKV--DGLEPSVImNAATDFMVDMSKVGsnidsGKLSCAIFDPMGHVLPSKIVQGPtDDIFRIMYTPFEAGRHTI 941
Cdd:pfam00630    2 ADASKVKAsgPGLEPGVV-GKPAEFTVDTRDAG-----GEGEVEVTGPDGSPVPVEVTDNG-DGTYTVSYTPTEPGDYTV 74

                           90
                   ....*....|....*
gi 320542951   942 ELMYDNIPVPGSPFV 956
Cdd:pfam00630   75 SVKFNGQHIPGSPFK 89
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 175-267 1.39e-14

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 71.58  E-value: 1.39e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    175 LLNWI---HAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWEL---WDPKDAVQNASEAMGLADDWLNVRQLIKPE 248
Cdd:smart00033    3 LLRWVnslLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVaasLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90
                    ....*....|....*....
gi 320542951    249 ELVNPNVDEQSMMTYLSQY 267
Cdd:smart00033   83 DLVEGPKLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
2149-2236 2.32e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.40  E-value: 2.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  2149 SDASKVVSKGMGLKKAYIGKQNQFSISATDAGNNILyVGMYGPKGPCEEFHVKHAGHNNYNVQYLVRDRGQYVLLIKWGE 2228
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGE-VEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 320542951  2229 EHIPGSPF 2236
Cdd:pfam00630   81 QHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1269-1345 1.39e-13

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 68.40  E-value: 1.39e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320542951   1269 GSQSHLKVDAREAGDGAVTCKITNKAGSEiVDIDVIE-KDGFFDILYALNDPGDYDINVKFGGKDIPNGSFSIKAVES 1345
Cdd:smart00557   17 GEPAEFTVDTRDAGGGELEVEVTGPSGKK-VPVEVKDnGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGPA 93
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 171-267 2.55e-13

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 68.08  E-value: 2.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   171 PKQRLLNWI----HAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWEL-WDPKDAVQNASEAMGLADDWLNVRQ-L 244
Cdd:pfam00307    3 LEKELLRWInshlAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnKSEFDKLENINLALDVAEKKLGVPKvL 82

                           90       100
                   ....*....|....*....|...
gi 320542951   245 IKPEELVNPnvDEQSMMTYLSQY 267
Cdd:pfam00307   83 IEPEDLVEG--DNKSVLTYLASL 103
Filamin pfam00630
Filamin/ABP280 repeat;
1394-1450 2.20e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 64.62  E-value: 2.20e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 320542951  1394 GGNVTAEVRMPSGKVDKPVIQDNRDGTVSVKYDPREEGSHELVVKYNGEPVQGSPFK 1450
Cdd:pfam00630   33 GGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1774-1822 4.74e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 60.77  E-value: 4.74e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 320542951  1774 VTSPSNVTEDAEIQEVEDGLYAVHFVPKELGVHTVSVRYSEMHIPGSPF 1822
Cdd:pfam00630   40 VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
1251-1338 1.54e-09

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 56.53  E-value: 1.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1251 GEAKKCKLVEQAPKIQTSGSQSHLKVDAREAGdGAVTCKITNKAGSEIvDIDVIE-KDGFFDILYALNDPGDYDINVKFG 1329
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPV-PVEVTDnGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*....
gi 320542951  1330 GKDIPNGSF 1338
Cdd:pfam00630   80 GQHIPGSPF 88
 
Name Accession Description Interval E-value
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 32-154 6.63e-83

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


Pssm-ID: 409160  Cd Length: 124  Bit Score: 267.40  E-value: 6.63e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   32 EAERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVA 111
Cdd:cd21311     1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 320542951  112 LKFLQ-DEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMP 154
Cdd:cd21311    81 LKFLEeDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISMP 124
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 155-272 1.46e-79

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: 257.79  E-value: 1.46e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  155 MWDGEDDKQLNGSGHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGL 234
Cdd:cd21315     1 MWEGEDDGPDDGKGPTPKQRLLGWIQSKVPDLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAVKNAKEAMDL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 320542951  235 ADDWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPNSKL 272
Cdd:cd21315    81 AEDWLDVPQLIKPEEMVNPKVDELSMMTYLSQFPNAKL 118
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 170-272 1.29e-69

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


Pssm-ID: 409079  Cd Length: 103  Bit Score: 228.81  E-value: 1.29e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEE 249
Cdd:cd21230     1 TPKQRLLGWIQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALENATEAMQLAEDWLGVPQLITPEE 80

                          90       100
                  ....*....|....*....|...
gi 320542951  250 LVNPNVDEQSMMTYLSQYPNSKL 272
Cdd:cd21230    81 IINPNVDEMSVMTYLSQFPKAKL 103
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 43-149 2.84e-66

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


Pssm-ID: 409077  Cd Length: 108  Bit Score: 219.28  E-value: 2.84e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   43 WKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPK-YNKRPTFRSQKLENVSVALKFLQDEGIK 121
Cdd:cd21228     1 WKKIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkYNKRPTFRQMKLENVSVALEFLERESIK 80

                          90       100
                  ....*....|....*....|....*...
gi 320542951  122 IVNIDSSDIVDCKLKLILGLIWTLILHY 149
Cdd:cd21228    81 LVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 34-159 6.13e-60

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


Pssm-ID: 409158  Cd Length: 131  Bit Score: 202.23  E-value: 6.13e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   34 ERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRM-PKYNKRPTFRSQKLENVSVAL 112
Cdd:cd21309     5 EKDLAEDAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVAL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 320542951  113 KFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMPMWDGE 159
Cdd:cd21309    85 EFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISMPVWEDE 131
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 34-154 6.87e-58

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


Pssm-ID: 409159  Cd Length: 125  Bit Score: 196.02  E-value: 6.87e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   34 ERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRM-PKYNKRPTFRSQKLENVSVAL 112
Cdd:cd21310     4 EKDLAEDAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMyRKYHPRPNFRQMKLENVSVAL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 320542951  113 KFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMP 154
Cdd:cd21310    84 EFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 125
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 28-154 7.36e-57

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


Pssm-ID: 409157  Cd Length: 129  Bit Score: 193.38  E-value: 7.36e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   28 DEDMEA-ERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRM-PKYNKRPTFRSQKL 105
Cdd:cd21308     1 DAEMPAtEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 320542951  106 ENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMP 154
Cdd:cd21308    81 ENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 129
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 157-273 9.16e-57

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


Pssm-ID: 409163  Cd Length: 115  Bit Score: 192.59  E-value: 9.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  157 DGEDDKQlngsgHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLAD 236
Cdd:cd21314     3 DEEDARK-----QTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPVQNAREAMQQAD 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 320542951  237 DWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPNSKLK 273
Cdd:cd21314    78 DWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLK 114
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
 165-272 1.48e-52

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


Pssm-ID: 409162  Cd Length: 110  Bit Score: 180.29  E-value: 1.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  165 NGSGHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLADDWLNVRQL 244
Cdd:cd21313     3 DAKKQTPKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPQKPVDNAREAMQQADDWLGVPQV 82

                          90       100
                  ....*....|....*....|....*...
gi 320542951  245 IKPEELVNPNVDEQSMMTYLSQYPNSKL 272
Cdd:cd21313    83 ITPEEIIHPDVDEHSVMTYLSQFPKAKL 110
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 43-149 3.24e-51

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 176.13  E-value: 3.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   43 WKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRM-PKYNKRPTFRSQKLENVSVALKFLQDEGIK 121
Cdd:cd21183     1 WKRIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLkRSYNRRPAFQQHYLENVSTALKFIEADHIK 80

                          90       100
                  ....*....|....*....|....*...
gi 320542951  122 IVNIDSSDIVDCKLKLILGLIWTLILHY 149
Cdd:cd21183    81 LVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 43-151 5.17e-49

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


Pssm-ID: 409076  Cd Length: 109  Bit Score: 170.16  E-value: 5.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   43 WKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKI 122
Cdd:cd21227     1 WVEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKL 80

                          90       100
                  ....*....|....*....|....*....
gi 320542951  123 VNIDSSDIVDCKLKLILGLIWTLILHYSI 151
Cdd:cd21227    81 VNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 157-272 1.29e-48

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


Pssm-ID: 409161  Cd Length: 114  Bit Score: 169.22  E-value: 1.29e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  157 DGEDDKQlnGSGHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLAD 236
Cdd:cd21312     1 DEEEDEE--AKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQAD 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 320542951  237 DWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPNSKL 272
Cdd:cd21312    79 DWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKL 114
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 43-149 4.12e-47

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 164.50  E-value: 4.12e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   43 WKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKI 122
Cdd:cd21215     1 WVDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKL 80

                          90       100
                  ....*....|....*....|....*..
gi 320542951  123 VNIDSSDIVDCKLKLILGLIWTLILHY 149
Cdd:cd21215    81 TNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 170-271 1.65e-45

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


Pssm-ID: 409033  Cd Length: 103  Bit Score: 159.71  E-value: 1.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEE 249
Cdd:cd21184     1 SGKSLLLEWVNSKIPEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMDIAEEELGIPKIITPED 80

                          90       100
                  ....*....|....*....|..
gi 320542951  250 LVNPNVDEQSMMTYLSQYPNSK 271
Cdd:cd21184    81 MVSPNVDELSVMTYLSYFRNAK 102
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 45-149 1.60e-36

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


Pssm-ID: 409037  Cd Length: 105  Bit Score: 134.07  E-value: 1.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   45 KIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRptFRSQKLENVSVALKFLQDEGIKIVN 124
Cdd:cd21188     2 AVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGR--MRFHRLQNVQTALDFLKYRKIKLVN 79

                          90       100
                  ....*....|....*....|....*
gi 320542951  125 IDSSDIVDCKLKLILGLIWTLILHY 149
Cdd:cd21188    80 IRAEDIVDGNPKLTLGLIWTIILHF 104
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 42-147 9.08e-35

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


Pssm-ID: 409063  Cd Length: 105  Bit Score: 129.05  E-value: 9.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   42 QWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKyNKRPTFRSQKLENVSVALKFLQDEGIK 121
Cdd:cd21214     1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPK-PERGKMRFHKIANVNKALDFIASKGVK 79

                          90       100
                  ....*....|....*....|....*.
gi 320542951  122 IVNIDSSDIVDCKLKLILGLIWTLIL 147
Cdd:cd21214    80 LVSIGAEEIVDGNLKMTLGMIWTIIL 105
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 171-267 6.09e-33

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


Pssm-ID: 409078  Cd Length: 105  Bit Score: 124.04  E-value: 6.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  171 PKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEEL 250
Cdd:cd21229     4 PKKLMLAWLQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPEDL 83

                          90
                  ....*....|....*..
gi 320542951  251 VNPNVDEQSMMTYLSQY 267
Cdd:cd21229    84 SSPHLDELSGMTYLSYF 100
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
39-267 1.43e-31

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 133.14  E-value: 1.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   39 EDAQWKKIQQNTFTRWANEHLKTID-RSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQD 117
Cdd:COG5069     2 EAKKWQKVQKKTFTKWTNEKLISGGqKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  118 EGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMPMWDGEDDKQLNgsghtpkqrLLNWIHAKI----PDLPINNFTN 193
Cdd:COG5069    82 KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGELTKHIN---------LLLWCDEDTggykPEVDTFDFFR 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320542951  194 DWTTGKAVGALVDACAP-GLCPDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELVNPNV-DEQSMMTYLSQY 267
Cdd:COG5069   153 SWRDGLAFSALIHDSRPdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSWY 228
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 965-1055 7.97e-31

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 117.32  E-value: 7.97e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    965 PARCKAYGPGLEKGLTNQKNKFTVETKGAGNGGLSLAIEGPS--EAKMTCTDNRDGSCDVDYLATDPGEYDITIRFADKH 1042
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 320542951   1043 IPGSPFRVLVEET 1055
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1835-1923 1.13e-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: 116.93  E-value: 1.13e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1835 HLVKAGGSGLERGVVGEAAEFNVWTREAGGGSLAISVEGPS--KADIEFKDRKDGSCDVSYKVTEPGEYRVGLKFNDRHI 1912
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|.
gi 320542951   1913 PDSPFKVYVSP 1923
Cdd:smart00557   82 PGSPFTVKVGP 92
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 23-147 3.14e-30

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


Pssm-ID: 409042  Cd Length: 116  Bit Score: 116.63  E-value: 3.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   23 YEENFDEDMEAERdlaedaqwKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNkRPTFRS 102
Cdd:cd21193     1 FEKGRIRALQEER--------INIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPN-RGRLRV 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 320542951  103 QKLENVSVALKFLQDEgIKIVNIDSSDIVDCKLKLILGLIWTLIL 147
Cdd:cd21193    72 QKIENVNKALAFLKTK-VRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 45-151 5.05e-30

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


Pssm-ID: 409090  Cd Length: 113  Bit Score: 115.93  E-value: 5.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   45 KIQQNTFTRWANEHLKTIDR--SINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKI 122
Cdd:cd21241     4 RVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKKIKL 83

                          90       100
                  ....*....|....*....|....*....
gi 320542951  123 VNIDSSDIVDCKLKLILGLIWTLILHYSI 151
Cdd:cd21241    84 VNINPTDIVDGKPSIVLGLIWTIILYFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1641-1730 5.10e-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: 5.10e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1641 AKKVKVSGTGLKEGQTHADNIFSVDTRNAGFGGLSVSIEGPS--KAEIQCTDKDDGTLNISYKPTEPGYYIVNLKFADHH 1718
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 320542951   1719 VEGSPFTVKVAG 1730
Cdd:smart00557   81 IPGSPFTVKVGP 92
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 45-161 6.05e-30

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


Pssm-ID: 409084  Cd Length: 119  Bit Score: 115.89  E-value: 6.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   45 KIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRptFRSQKLENVSVALKFLQDEGIKIVN 124
Cdd:cd21235     5 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 320542951  125 IDSSDIVDCKLKLILGLIWTLILHYSISMPMWDGEDD 161
Cdd:cd21235    83 IRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 46-149 2.57e-29

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


Pssm-ID: 409035  Cd Length: 107  Bit Score: 113.63  E-value: 2.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   46 IQQNTFTRWANEHLKTIDRS-INNLETDLSDGLRLIALIEVLSQKRMPKynKRPTFRSQKLENVSVALKFLQDEGIKIVN 124
Cdd:cd21186     2 VQKKTFTKWINSQLSKANKPpIKDLFEDLRDGTRLLALLEVLTGKKLKP--EKGRMRVHHLNNVNRALQVLEQNNVKLVN 79

                          90       100
                  ....*....|....*....|....*
gi 320542951  125 IDSSDIVDCKLKLILGLIWTLILHY 149
Cdd:cd21186    80 ISSNDIVDGNPKLTLGLVWSIILHW 104
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 22-152 2.76e-29

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


Pssm-ID: 409085  Cd Length: 128  Bit Score: 114.31  E-value: 2.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   22 QYEENFDEDMEAERDlaedaqwkKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRptFR 101
Cdd:cd21236     1 QAYENVLERYKDERD--------KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGR--MR 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 320542951  102 SQKLENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSIS 152
Cdd:cd21236    71 FHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 121
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1460-1547 5.35e-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: 112.31  E-value: 5.35e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1460 YVTAYGPGLTHGVTGEPANFTISTKGASAGGLTMAVEGPS--KADINYHDNKDGTVSVQYLPTAPGEYQVSVRFGDKHIK 1537
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|
gi 320542951   1538 GSPYFAKITG 1547
Cdd:smart00557   83 GSPFTVKVGP 92
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 44-151 5.95e-29

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


Pssm-ID: 409039  Cd Length: 113  Bit Score: 113.05  E-value: 5.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   44 KKIQQNTFTRWANEHL--KTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIK 121
Cdd:cd21190     3 ERVQKKTFTNWINSHLakLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIK 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 320542951  122 IVNIDSSDIVDCKLKLILGLIWTLILHYSI 151
Cdd:cd21190    83 LVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 37-147 1.44e-28

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


Pssm-ID: 409095  Cd Length: 117  Bit Score: 112.08  E-value: 1.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   37 LAEDAQwkKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNkRPTFRSQKLENVSVALKFLQ 116
Cdd:cd21246     9 LADERE--AVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPT-KGKMRIHCLENVDKALQFLK 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 320542951  117 DEGIKIVNIDSSDIVDCKLKLILGLIWTLIL 147
Cdd:cd21246    86 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 45-159 1.07e-27

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


Pssm-ID: 409086  Cd Length: 118  Bit Score: 109.35  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   45 KIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRptFRSQKLENVSVALKFLQDEGIKIVN 124
Cdd:cd21237     5 RVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGR--MRFHRLQNVQIALDFLKQRQVKLVN 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 320542951  125 IDSSDIVDCKLKLILGLIWTLILHYSISMPMWDGE 159
Cdd:cd21237    83 IRNDDITDGNPKLTLGLIWTIILHFQISDIYISGE 117
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 49-148 4.37e-27

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 107.02  E-value: 4.37e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951     49 NTFTRWANEHL-KTIDRSINNLETDLSDGLRLIALIEVLSQKRMPK-YNKRPTFRSQKLENVSVALKFLQDEGIKIVNID 126
Cdd:smart00033    1 KTLLRWVNSLLaEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 320542951    127 SSDIVDcKLKLILGLIWTLILH 148
Cdd:smart00033   81 PEDLVE-GPKLILGVIWTLISL 101
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 673-765 4.72e-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: 4.72e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    673 PELVKASGPGLEKngVTINQPTSFTVDPSKAGNAPLDVVVQDVFGTKLPVELKNNPDGTKKVTYTPTSGVPHTVEVNYGG 752
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|...
gi 320542951    753 VSTPNSPHRVYVG 765
Cdd:smart00557   79 EHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 284-379 6.02e-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: 6.02e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    284 PNRVRAYGPGIEPIgpVVGAPANFTVETFSAGKGSVDVDIQGPNGEIEKADVRFNNDKnlTYTVSYIPKSEGSHKVAVKF 363
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDG--TYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*.
gi 320542951    364 SGRDIPKSPFPVKVEG 379
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 51-149 6.83e-27

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


Pssm-ID: 409061  Cd Length: 105  Bit Score: 106.51  E-value: 6.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   51 FTRWANEHLK--TIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKIVNIDSS 128
Cdd:cd21212     5 YTDWANHYLEkgGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQGITAE 84

                          90       100
                  ....*....|....*....|.
gi 320542951  129 DIVDCKLKLILGLIWTLILHY 149
Cdd:cd21212    85 DIVDGNLKAILGLFFSLSRYK 105
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 24-147 2.83e-25

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


Pssm-ID: 409166  Cd Length: 132  Bit Score: 103.21  E-value: 2.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   24 EENFDEDMEAERdLAEDAQWKK-------IQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNK 96
Cdd:cd21317     3 DDDWDNDNSSAR-LFERSRIKAladereaVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTK 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 320542951   97 rPTFRSQKLENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLIL 147
Cdd:cd21317    82 -GRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 46-151 6.03e-25

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


Pssm-ID: 409091  Cd Length: 111  Bit Score: 101.45  E-value: 6.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   46 IQQNTFTRWANEHL--KTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFrsQKLENVSVALKFLQDEGIKIV 123
Cdd:cd21242     5 TQKRTFTNWINSQLakHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVF--QCRSNIETALSFLKNKSIKLI 82

                          90       100
                  ....*....|....*....|....*...
gi 320542951  124 NIDSSDIVDCKLKLILGLIWTLILHYSI 151
Cdd:cd21242    83 NIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 46-147 8.75e-25

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


Pssm-ID: 409167  Cd Length: 139  Bit Score: 102.03  E-value: 8.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   46 IQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKyNKRPTFRSQKLENVSVALKFLQDEGIKIVNI 125
Cdd:cd21318    38 VQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPK-PTRGRMRIHSLENVDKALQFLKEQRVHLENV 116

                          90       100
                  ....*....|....*....|..
gi 320542951  126 DSSDIVDCKLKLILGLIWTLIL 147
Cdd:cd21318   117 GSHDIVDGNHRLTLGLIWTIIL 138
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 483-576 1.06e-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: 99.99  E-value: 1.06e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    483 ARKVRASGRGLQatGVRVGDDADFKIYTEGAGEGEPEVRVIGPGGMNQNVMQSKVDGNTYECHYYPTKEGRYVIMVTFAG 562
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....
gi 320542951    563 QEVAKSPFEVKVGP 576
Cdd:smart00557   79 EHIPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
963-1049 1.70e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 99.29  E-value: 1.70e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   963 CDPARCKAYGPGLEKGLTNQKNKFTVETKGAGnGGLSLAIEGPS--EAKMTCTDNRDGSCDVDYLATDPGEYDITIRFAD 1040
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 320542951  1041 KHIPGSPFR 1049
Cdd:pfam00630   81 QHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 384-479 5.32e-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: 98.06  E-value: 5.32e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    384 ASKVKVTGPGIQPngVTIKKPTFFDILAKDAGRGVPEVIIIDPANHKtsVAAKVRQLENDTWRCEYVTALQGLHSVNVFY 463
Cdd:smart00557    1 ASKVKASGPGLEK--GVVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*.
gi 320542951    464 AGTPIPNSPFPVKVAP 479
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
1638-1725 7.90e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 97.36  E-value: 7.90e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1638 VGDAKKVKVSGTGLKEGQTHADNIFSVDTRNAGfGGLSVSIEGPS--KAEIQCTDKDDGTLNISYKPTEPGYYIVNLKFA 1715
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 320542951  1716 DHHVEGSPFT 1725
Cdd:pfam00630   80 GQHIPGSPFK 89
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 43-150 1.16e-23

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409074  Cd Length: 111  Bit Score: 97.60  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   43 WKKIQQNTFTRWANEHL-KTIDRSINNLETDLSDGLRLIALIEVLSQKRMP-KYNKRPTFRSQKLENVSVALKFLQDE-G 119
Cdd:cd21225     1 WEKVQIKAFTAWVNSVLeKRGIPKISDLATDLSDGVRLIFFLELVSGKKFPkKFDLEPKNRIQMIQNLHLAMLFIEEDlK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 320542951  120 IKIVNIDSSDIVDCKLKLILGLIWTLILHYS 150
Cdd:cd21225    81 IRVQGIGAEDFVDNNKKLILGLLWTLYRKYR 111
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 46-151 1.21e-23

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


Pssm-ID: 409080  Cd Length: 111  Bit Score: 97.69  E-value: 1.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   46 IQQNTFTRWANEHL-KTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKynKRPTFRSQKLENVSVALKFLQDEGIKIVN 124
Cdd:cd21231     6 VQKKTFTKWINAQFaKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVK--EKGSTRVHALNNVNKALQVLQKNNVDLVN 83

                          90       100
                  ....*....|....*....|....*..
gi 320542951  125 IDSSDIVDCKLKLILGLIWTLILHYSI 151
Cdd:cd21231    84 IGSADIVDGNHKLTLGLIWSIILHWQV 110
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 45-151 1.41e-23

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 97.36  E-value: 1.41e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    45 KIQQNTFTRWANEHLK--TIDRSINNLETDLSDGLRLIALIEVLSQKrMPKYNKRPTFRSQKLENVSVALKFLQDE-GIK 121
Cdd:pfam00307    1 LELEKELLRWINSHLAeyGPGVRVTNFTTDLRDGLALCALLNKLAPG-LVDKKKLNKSEFDKLENINLALDVAEKKlGVP 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 320542951   122 IVNIDSSDIVDCKLKLILGLIWTLILHYSI 151
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2023-2111 2.16e-23

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 96.13  E-value: 2.16e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   2023 PAAVHASGNGLDEVKTGHKADFIINTCNAGVGTLAVSIDGPS--KVAMDCTEVEEG-YKVRYTPLLPGEHYITVKYNNMH 2099
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 320542951   2100 IVGSPFKVNATG 2111
Cdd:smart00557   81 IPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
282-373 3.02e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 95.82  E-value: 3.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   282 TNPNRVRAYGPGIEPigPVVGAPANFTVETFSAGkGSVDVDIQGPNGEIEKADVRFNNDKnlTYTVSYIPKSEGSHKVAV 361
Cdd:pfam00630    2 ADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDG--TYTVSYTPTEPGDYTVSV 76

                           90
                   ....*....|..
gi 320542951   362 KFSGRDIPKSPF 373
Cdd:pfam00630   77 KFNGQHIPGSPF 88
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 46-151 3.72e-23

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


Pssm-ID: 409040  Cd Length: 114  Bit Score: 96.49  E-value: 3.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   46 IQQNTFTRWANEHLKTIDR--SINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKIV 123
Cdd:cd21191     5 VQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSNVKLV 84

                          90       100
                  ....*....|....*....|....*...
gi 320542951  124 NIDSSDIVDCKLKLILGLIWTLILHYSI 151
Cdd:cd21191    85 SIDAAEIADGNPSLVLGLIWNIILFFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2151-2240 5.99e-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: 94.98  E-value: 5.99e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   2151 ASKVVSKGMGLKKAYIGKQNQFSISATDAGNNILYVGMYGPKGPCEEFHVKHAGHNNYNVQYLVRDRGQYVLLIKWGEEH 2230
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 320542951   2231 IPGSPFQIDV 2240
Cdd:smart00557   81 IPGSPFTVKV 90
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 46-147 1.35e-22

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: 96.27  E-value: 1.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   46 IQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKrPTFRSQKLENVSVALKFLQDEGIKIVNI 125
Cdd:cd21316    53 VQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKPTK-GRMRIHCLENVDKALQFLKEQRVHLENM 131

                          90       100
                  ....*....|....*....|..
gi 320542951  126 DSSDIVDCKLKLILGLIWTLIL 147
Cdd:cd21316   132 GSHDIVDGNHRLTLGLIWTIIL 153
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 580-667 2.16e-22

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.44  E-value: 2.16e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    580 SSIVAYGPGLSSGVIGYPAAFVVETNG-ETGALGFTVAGPSQ--AEIECHDNGDGSALVKYHPTAVGEYAVHILCDNEDI 656
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDaGGGELEVEVTGPSGkkVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|.
gi 320542951    657 PKSPFIAQILP 667
Cdd:smart00557   82 PGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1058-1153 3.48e-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: 92.67  E-value: 3.48e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1058 PSKVKVYGPGIEHGQVREsvPTFFNVDVGEAGPGRIAVKLTNSEGIPVDnLRVEDKGNCIYAVHYVPPKAGsVLTCQVKF 1137
Cdd:smart00557    1 ASKVKASGPGLEKGVVGE--PAEFTVDTRDAGGGELEVEVTGPSGKKVP-VEVKDNGDGTYTVSYTPTEPG-DYTVTVKF 76

                            90
                    ....*....|....*.
gi 320542951   1138 SEVEVPCSPFVMTVFP 1153
Cdd:smart00557   77 GGEHIPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1157-1250 5.29e-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: 92.28  E-value: 5.29e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1157 PTKVKVKGVNEKKKTpASLPAEFEIDTKQAGQADINVAIKNPKGKAMQPRLEEVSTGTYVVSFVPDECGTYQCSIKYGDK 1236
Cdd:smart00557    1 ASKVKASGPGLEKGV-VGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 320542951   1237 EIEGSPFKLEAFPT 1250
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1837-1918 6.05e-22

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 91.97  E-value: 6.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1837 VKAGGSGLERGVVGEAAEFNVWTREAGGGsLAISVEGPS--KADIEFKDRKDGSCDVSYKVTEPGEYRVGLKFNDRHIPD 1914
Cdd:pfam00630    7 VKASGPGLEPGVVGKPAEFTVDTRDAGGE-GEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPG 85


                   ....
gi 320542951  1915 SPFK 1918
Cdd:pfam00630   86 SPFK 89
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 48-147 1.68e-21

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 91.25  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   48 QNTFTRWANEHLK-TIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGI-KIVNI 125
Cdd:cd00014     1 EEELLKWINEVLGeELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLpELDLF 80

                          90       100
                  ....*....|....*....|...
gi 320542951  126 DSSDIVDCK-LKLILGLIWTLIL 147
Cdd:cd00014    81 EPEDLYEKGnLKKVLGTLWALAL 103
Filamin pfam00630
Filamin/ABP280 repeat;
1461-1541 8.52e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 88.50  E-value: 8.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1461 VTAYGPGLTHGVTGEPANFTISTKGASaGGLTMAVEGPS--KADINYHDNKDGTVSVQYLPTAPGEYQVSVRFGDKHIKG 1538
Cdd:pfam00630    7 VKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPG 85


                   ...
gi 320542951  1539 SPY 1541
Cdd:pfam00630   86 SPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
481-571 1.12e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.42  E-value: 1.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   481 SDARKVRASGRGLQatGVRVGDDADFKIYTEGAGeGEPEVRVIGPGGMNQNVMQSKVDGNTYECHYYPTKEGRYVIMVTF 560
Cdd:pfam00630    2 ADASKVKASGPGLE--PGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 320542951   561 AGQEVAKSPFE 571
Cdd:pfam00630   79 NGQHIPGSPFK 89
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 46-151 1.13e-19

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


Pssm-ID: 409081  Cd Length: 107  Bit Score: 86.22  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   46 IQQNTFTRWANEHL-KTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKynKRPTFRSQKLENVSVALKFLQDEGIKIVN 124
Cdd:cd21232     2 VQKKTFTKWINARFsKSGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPK--ERGSTRVHALNNVNRVLQVLHQNNVELVN 79

                          90       100
                  ....*....|....*....|....*..
gi 320542951  125 IDSSDIVDCKLKLILGLIWTLILHYSI 151
Cdd:cd21232    80 IGGTDIVDGNHKLTLGLLWSIILHWQV 106
Filamin pfam00630
Filamin/ABP280 repeat;
580-662 1.13e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.42  E-value: 1.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   580 SSIVAYGPGLSSGVIGYPAAFVVETNGETGALGFTVAGPS--QAEIECHDNGDGSALVKYHPTAVGEYAVHILCDNEDIP 657
Cdd:pfam00630    5 SKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIP 84


                   ....*
gi 320542951   658 KSPFI 662
Cdd:pfam00630   85 GSPFK 89
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 176-267 1.33e-19

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


Pssm-ID: 409034  Cd Length: 98  Bit Score: 85.43  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  176 LNWIHAKIPDLPINNFTNDWTTGKAVGALVDACApGLCPDWELWDPKDAVQNASEAMGLADDwLNVRQLIKPEELVNPNV 255
Cdd:cd21185     7 LRWVRQLLPDVDVNNFTTDWNDGRLLCGLVNALG-GSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEV 84

                          90
                  ....*....|..
gi 320542951  256 DEQSMMTYLSQY 267
Cdd:cd21185    85 EHLGIMAYAAQL 96
Filamin pfam00630
Filamin/ABP280 repeat;
671-759 5.49e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 83.49  E-value: 5.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   671 FHPELVKASGPGLEknGVTINQPTSFTVDPSKAGNaPLDVVVQDVFGTKLPVELKNNPDGTKKVTYTPTSGVPHTVEVNY 750
Cdd:pfam00630    2 ADASKVKASGPGLE--PGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78


                   ....*....
gi 320542951   751 GGVSTPNSP 759
Cdd:pfam00630   79 NGQHIPGSP 87
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1928-2017 6.05e-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: 83.42  E-value: 6.05e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   1928 AHKLEVQQFPQGNIQADAPYQFMVRKNGA-KGELDAKIVAPSGTDDDCFIQVIDGEMYSVRFYPRENGIHAIHVKFNGVH 2006
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 320542951   2007 IPDSPFRIKVG 2017
Cdd:smart00557   81 IPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
381-473 7.42e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 83.11  E-value: 7.42e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   381 AGDASKVKVTGPGIQPngVTIKKPTFFDILAKDAGrGVPEVIIIDPANHKtsVAAKVRQLENDTWRCEYVTALQGLHSVN 460
Cdd:pfam00630    1 AADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSP--VPVEVTDNGDGTYTVSYTPTEPGDYTVS 75

                           90
                   ....*....|...
gi 320542951   461 VFYAGTPIPNSPF 473
Cdd:pfam00630   76 VKFNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
2020-2106 1.27e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 82.34  E-value: 1.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  2020 VADPAAVHASGNGLDEVKTGHKADFIINTCNAGvGTLAVSIDGPS--KVAMDCTEVEEG-YKVRYTPLLPGEHYITVKYN 2096
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 320542951  2097 NMHIVGSPFK 2106
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1155-1244 2.09e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 78.87  E-value: 2.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1155 SEPTKVKVKGVNeKKKTPASLPAEFEIDTKQAGQaDINVAIKNPKGKAMQPRLEEVSTGTYVVSFVPDECGTYQCSIKYG 1234
Cdd:pfam00630    2 ADASKVKASGPG-LEPGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 320542951  1235 DKEIEGSPFK 1244
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1394-1454 2.54e-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: 78.80  E-value: 2.54e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320542951   1394 GGNVTAEVRMPSGKVDKPVIQDNRDGTVSVKYDPREEGSHELVVKYNGEPVQGSPFKFHVD 1454
Cdd:smart00557   31 GGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 25-149 1.50e-16

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409071  Cd Length: 121  Bit Score: 77.63  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   25 ENFDEDMEAERDlaedaqwkKIQ--QNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMP--KYNKRPTF 100
Cdd:cd21222     1 DAFDDLFDEAPE--------KLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlhEYHLTPST 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 320542951  101 RSQKLENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLILHY 149
Cdd:cd21222    73 DDEKLHNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 770-853 2.38e-16

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 76.10  E-value: 2.38e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    770 AAKVQAFGPWLQPGvRPNAATHFNVDAREAGDAELKVKIIHEETKiEVPCRIIDNEDNTYSVEVIPPSKGAYTTTMTYGG 849
Cdd:smart00557    1 ASKVKASGPGLEKG-VVGEPAEFTVDTRDAGGGELEVEVTGPSGK-KVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78


                    ....
gi 320542951    850 QRVP 853
Cdd:smart00557   79 EHIP 82
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 35-151 2.96e-16

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409096  Cd Length: 125  Bit Score: 77.11  E-value: 2.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   35 RDLAEdaQWKKIQQNTFTRWANEHLKTIDRSI--NNLETDLSDGLRLIALIEVLSQKRMPKYNKRpTFRSQKLENVSVAL 112
Cdd:cd21247    11 RKLQE--QRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRPSRG-KMRVHFLENNSKAI 87

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 320542951  113 KFLQDEgIKIVNIDSSDIVDCKLKLILGLIWTLILHYSI 151
Cdd:cd21247    88 TFLKTK-VPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
Filamin pfam00630
Filamin/ABP280 repeat;
767-853 1.40e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 73.86  E-value: 1.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   767 PVDAAKVQAFGPWLQPGvRPNAATHFNVDAREAGDaELKVKIIHEETKiEVPCRIIDNEDNTYSVEVIPPSKGAYTTTMT 846
Cdd:pfam00630    1 AADASKVKASGPGLEPG-VVGKPAEFTVDTRDAGG-EGEVEVTGPDGS-PVPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77


                   ....*..
gi 320542951   847 YGGQRVP 853
Cdd:pfam00630   78 FNGQHIP 84
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 867-960 1.52e-15

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 73.79  E-value: 1.52e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    867 SKIKVD--GLEPSVImNAATDFMVDMSKVGSnidsGKLSCAIFDPMGHVLPSKIVQGPtDDIFRIMYTPFEAGRHTIELM 944
Cdd:smart00557    2 SKVKASgpGLEKGVV-GEPAEFTVDTRDAGG----GELEVEVTGPSGKKVPVEVKDNG-DGTYTVSYTPTEPGDYTVTVK 75

                            90
                    ....*....|....*.
gi 320542951    945 YDNIPVPGSPFVVNVK 960
Cdd:smart00557   76 FGGEHIPGSPFTVKVG 91
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 62-146 2.45e-15

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


Pssm-ID: 409072  Cd Length: 113  Bit Score: 74.16  E-value: 2.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   62 IDRSINNLETDLSDGLRLIALIEVL-------SQKRMPKYNkrptfRSQKLENVSVALKFLQDEGI----KIVNIDSSDI 130
Cdd:cd21223    22 FDFAVTNLAVDLRDGVRLCRLVELLtgdwsllSKLRVPAIS-----RLQKLHNVEVALKALKEAGVlrggDGGGITAKDI 96

                          90
                  ....*....|....*.
gi 320542951  131 VDCKLKLILGLIWTLI 146
Cdd:cd21223    97 VDGHREKTLALLWRII 112
Filamin pfam00630
Filamin/ABP280 repeat;
1056-1148 2.67e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 73.09  E-value: 2.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1056 VDPSKVKVYGPGIEHGQVreSVPTFFNVDVGEAGpGRIAVKLTNSEGIPVDNlRVEDKGNCIYAVHYVPPKAGsVLTCQV 1135
Cdd:pfam00630    2 ADASKVKASGPGLEPGVV--GKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPV-EVTDNGDGTYTVSYTPTEPG-DYTVSV 76

                           90
                   ....*....|...
gi 320542951  1136 KFSEVEVPCSPFV 1148
Cdd:pfam00630   77 KFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1925-2013 4.52e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 72.32  E-value: 4.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1925 AGDAHKLEVQQFPQGNIQADAPYQFMVRKNGAKGELDAKIVAPSGTDDDCFIQVIDGEMYSVRFYPRENGIHAIHVKFNG 2004
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 320542951  2005 VHIPDSPFR 2013
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
864-956 8.60e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 71.55  E-value: 8.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   864 VDVSKIKV--DGLEPSVImNAATDFMVDMSKVGsnidsGKLSCAIFDPMGHVLPSKIVQGPtDDIFRIMYTPFEAGRHTI 941
Cdd:pfam00630    2 ADASKVKAsgPGLEPGVV-GKPAEFTVDTRDAG-----GEGEVEVTGPDGSPVPVEVTDNG-DGTYTVSYTPTEPGDYTV 74

                           90
                   ....*....|....*
gi 320542951   942 ELMYDNIPVPGSPFV 956
Cdd:pfam00630   75 SVKFNGQHIPGSPFK 89
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 47-149 1.14e-14

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 71.95  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   47 QQNTFTRWANEHLKTID--RSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKIVN 124
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPgiRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80

                          90       100
                  ....*....|....*....|....*
gi 320542951  125 IDSSDIVDCKLKLILGLIWTLILHY 149
Cdd:cd21213    81 TSAKDIVDGNLKAIMRLILALAAHF 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 175-267 1.39e-14

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 71.58  E-value: 1.39e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951    175 LLNWI---HAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWEL---WDPKDAVQNASEAMGLADDWLNVRQLIKPE 248
Cdd:smart00033    3 LLRWVnslLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVaasLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90
                    ....*....|....*....
gi 320542951    249 ELVNPNVDEQSMMTYLSQY 267
Cdd:smart00033   83 DLVEGPKLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
2149-2236 2.32e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.40  E-value: 2.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  2149 SDASKVVSKGMGLKKAYIGKQNQFSISATDAGNNILyVGMYGPKGPCEEFHVKHAGHNNYNVQYLVRDRGQYVLLIKWGE 2228
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGE-VEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 320542951  2229 EHIPGSPF 2236
Cdd:pfam00630   81 QHIPGSPF 88
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 38-145 4.59e-14

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409134  Cd Length: 121  Bit Score: 70.76  E-value: 4.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   38 AEDAQWKKIqqntFTRWANEHLKTI--DRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFL 115
Cdd:cd21285     6 AENGFDKQI----YTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFL 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 320542951  116 QDEGIKIVNIDSSDIVDCKLKLILGLIWTL 145
Cdd:cd21285    82 AAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1269-1345 1.39e-13

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 68.40  E-value: 1.39e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320542951   1269 GSQSHLKVDAREAGDGAVTCKITNKAGSEiVDIDVIE-KDGFFDILYALNDPGDYDINVKFGGKDIPNGSFSIKAVES 1345
Cdd:smart00557   17 GEPAEFTVDTRDAGGGELEVEVTGPSGKK-VPVEVKDnGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGPA 93
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 49-149 2.30e-13

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 68.46  E-value: 2.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   49 NTFTRWANEHLktIDRSINNLETDLSDGLRLIALIE-----VLSQKRMPKYNKRPTFrsQKLENVSVALKFLQDEGIKIV 123
Cdd:cd21219     7 RAFRMWLNSLG--LDPLINNLYEDLRDGLVLLQVLDkiqpgCVNWKKVNKPKPLNKF--KKVENCNYAVDLAKKLGFSLV 82

                          90       100
                  ....*....|....*....|....*.
gi 320542951  124 NIDSSDIVDCKLKLILGLIWTLILHY 149
Cdd:cd21219    83 GIGGKDIADGNRKLTLALVWQLMRYH 108
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 171-267 2.55e-13

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 68.08  E-value: 2.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   171 PKQRLLNWI----HAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWEL-WDPKDAVQNASEAMGLADDWLNVRQ-L 244
Cdd:pfam00307    3 LEKELLRWInshlAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnKSEFDKLENINLALDVAEKKLGVPKvL 82

                           90       100
                   ....*....|....*....|...
gi 320542951   245 IKPEELVNPnvDEQSMMTYLSQY 267
Cdd:pfam00307   83 IEPEDLVEG--DNKSVLTYLASL 103
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 51-145 4.50e-13

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


Pssm-ID: 409135  Cd Length: 105  Bit Score: 67.36  E-value: 4.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   51 FTRWANEHLKTI--DRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKIVNIDSS 128
Cdd:cd21286     5 YTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAE 84

                          90
                  ....*....|....*..
gi 320542951  129 DIVDCKLKLILGLIWTL 145
Cdd:cd21286    85 EIRNGNLKAILGLFFSL 101
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 172-267 6.03e-13

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


Pssm-ID: 409043  Cd Length: 105  Bit Score: 67.05  E-value: 6.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  172 KQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 248
Cdd:cd21194     4 KDALLLWCQRKTagyPGVNIQNFTTSWRDGLAFNALIHAHRPDLI-DYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAE 82

                          90
                  ....*....|....*....
gi 320542951  249 ELVNPNVDEQSMMTYLSQY 267
Cdd:cd21194    83 DVDVARPDEKSIMTYVASY 101
Filamin pfam00630
Filamin/ABP280 repeat;
1394-1450 2.20e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 64.62  E-value: 2.20e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 320542951  1394 GGNVTAEVRMPSGKVDKPVIQDNRDGTVSVKYDPREEGSHELVVKYNGEPVQGSPFK 1450
Cdd:pfam00630   33 GGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 170-265 4.58e-12

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


Pssm-ID: 409038  Cd Length: 105  Bit Score: 64.34  E-value: 4.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNWIH---AKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 246
Cdd:cd21189     1 SAKEALLLWARrttEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLI-DFRSVRNQSNRENLENAFNVAEKEFGVTRLLD 79

                          90
                  ....*....|....*....
gi 320542951  247 PEELVNPNVDEQSMMTYLS 265
Cdd:cd21189    80 PEDVDVPEPDEKSIITYVS 98
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 172-267 2.81e-11

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409098  Cd Length: 109  Bit Score: 62.19  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  172 KQRLLNWIHAKIP---DLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 248
Cdd:cd21249     6 KEALLIWCQRKTAgytNVNVQDFSRSWRDGLAFNALIHAHRPDLI-DYGSLRPDRPLYNLANAFLVAEQELGISQLLDPE 84

                          90
                  ....*....|....*....
gi 320542951  249 ELVNPNVDEQSMMTYLSQY 267
Cdd:cd21249    85 DVAVPHPDERSIMTYVSLY 103
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
 170-273 4.44e-11

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409168  Cd Length: 112  Bit Score: 61.94  E-value: 4.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 246
Cdd:cd21319     5 SAKDALLLWCQMKTagyPNVNVTNFTSSWKDGLAFNALIHKHRPDLV-DFGKLKKSNARHNLEHAFNVAERQLGITKLLD 83

                          90       100
                  ....*....|....*....|....*....
gi 320542951  247 PEELVNPNVDEQSMMTYLSQYPN--SKLK 273
Cdd:cd21319    84 PEDVFTENPDEKSIITYVVAFYHyfSKMK 112
Filamin pfam00630
Filamin/ABP280 repeat;
1774-1822 4.74e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 60.77  E-value: 4.74e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 320542951  1774 VTSPSNVTEDAEIQEVEDGLYAVHFVPKELGVHTVSVRYSEMHIPGSPF 1822
Cdd:pfam00630   40 VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 66-153 7.92e-11

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 61.10  E-value: 7.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   66 INNLETDLSDGLRLIALIE------VLSQKRMPKYNKRPTFRsQKLENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLIL 139
Cdd:cd21298    24 VNHLYSDLRDGLVLLQLYDkikpgvVDWSRVNKPFKKLGANM-KKIENCNYAVELGKKLKFSLVGIGGKDIYDGNRTLTL 102

                          90
                  ....*....|....
gi 320542951  140 GLIWTLILHYSISM 153
Cdd:cd21298   103 ALVWQLMRAYTLSI 116
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 172-267 1.01e-10

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


Pssm-ID: 409041  Cd Length: 107  Bit Score: 60.51  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  172 KQRLLNWIHAKIPDL---PINNFTNDWTTGKAVGALVDAcapgLCPDweLWD--------PKDavqNASEAMGLADDWLN 240
Cdd:cd21192     5 EKALLKWVQAEIGKYygiRVTDFDKSWRDGVAFLALIHA----IRPD--LVDmktvknrsPRD---NLELAFRIAEQHLN 75

                          90       100
                  ....*....|....*....|....*..
gi 320542951  241 VRQLIKPEELVNPNVDEQSMMTYLSQY 267
Cdd:cd21192    76 IPRLLEVEDVLVDKPDERSIMTYVSQF 102
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
 172-267 1.05e-10

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


Pssm-ID: 409093  Cd Length: 109  Bit Score: 60.62  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  172 KQRLLNWIH---AKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 248
Cdd:cd21244     7 RKALLLWAQeqcAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLV-DMEKLKGRSNRENLEEAFRIAEQELKIPRLLEPE 85

                          90
                  ....*....|....*....
gi 320542951  249 ELVNPNVDEQSMMTYLSQY 267
Cdd:cd21244    86 DVDVVNPDEKSIMTYVAQF 104
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 175-267 1.24e-10

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


Pssm-ID: 409094  Cd Length: 106  Bit Score: 60.19  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  175 LLNWIHAKIPD--LPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELVN 252
Cdd:cd21245     8 LLNWVQRRTRKygVAVQDFGSSWRSGLAFLALIKAIDPSLV-DMRQALEKSPRENLEDAFRIAQESLGIPPLLEPEDVMV 86

                          90
                  ....*....|....*
gi 320542951  253 PNVDEQSMMTYLSQY 267
Cdd:cd21245    87 DSPDEQSIMTYVAQF 101
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 170-267 1.91e-10

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


Pssm-ID: 409065  Cd Length: 115  Bit Score: 60.07  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNWIHAKI-PDLPIN--NFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 246
Cdd:cd21216    10 SAKEGLLLWCQRKTaPYKNVNvqNFHTSWKDGLAFCALIHRHRPDLL-DYDKLRKDDPRENLNLAFDVAEKHLDIPKMLD 88

                          90       100
                  ....*....|....*....|..
gi 320542951  247 PEELVN-PNVDEQSMMTYLSQY 267
Cdd:cd21216    89 AEDIVNtPRPDERSVMTYVSCY 110
Filamin pfam00630
Filamin/ABP280 repeat;
1251-1338 1.54e-09

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 56.53  E-value: 1.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  1251 GEAKKCKLVEQAPKIQTSGSQSHLKVDAREAGdGAVTCKITNKAGSEIvDIDVIE-KDGFFDILYALNDPGDYDINVKFG 1329
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPV-PVEVTDnGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*....
gi 320542951  1330 GKDIPNGSF 1338
Cdd:pfam00630   80 GQHIPGSPF 88
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
 46-149 1.71e-09

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


Pssm-ID: 409186  Cd Length: 129  Bit Score: 57.70  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   46 IQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYN--KRPTFRSQKLENVSVALKFLQDEGIKIV 123
Cdd:cd21337    20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSffLTPDSFEQKVLNVSFAFELMQDGGLEKP 99

                          90       100
                  ....*....|....*....|....*.
gi 320542951  124 NIDSSDIVDCKLKLILGLIWTLILHY 149
Cdd:cd21337   100 KPRPEDIVNCDLKSTLRVLYNLFTKY 125
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
 172-268 3.45e-09

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


Pssm-ID: 409092  Cd Length: 109  Bit Score: 56.17  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  172 KQRLLNWIH---AKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 248
Cdd:cd21243     7 KKALLKWVQnaaAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLV-DMESLKRRSNRENLETAFTVAEKELGIPRLLDPE 85

                          90       100
                  ....*....|....*....|....
gi 320542951  249 ELVNPNVDEQSMMTYLSQ----YP 268
Cdd:cd21243    86 DVDVDKPDEKSIMTYVAQflkkYP 109
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 164-267 4.80e-09

second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409140  Cd Length: 115  Bit Score: 56.00  E-value: 4.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  164 LNGSGHTPKQRLLNWIHAKIP---DLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLN 240
Cdd:cd21291     4 INEEGLTAKEGLLLWCQRKTAgydEVDVQDFTTSWTDGLAFCALIHRHRPDLI-DYDKLDKKDHRGNMQLAFDIASKEIG 82

                          90       100
                  ....*....|....*....|....*...
gi 320542951  241 VRQLIKPEELVN-PNVDEQSMMTYLSQY 267
Cdd:cd21291    83 IPQLLDVEDVCDvAKPDERSIMTYVAYY 110
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 51-146 9.53e-09

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 55.27  E-value: 9.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   51 FTRWANEHL---------KTIDRSINNLETDLSDGLRLIALIEvlsqKRMP---------KYNKRPTFrsQKLENVSVAL 112
Cdd:cd21217     6 FVEHINSLLaddpdlkhlLPIDPDGDDLFEALRDGVLLCKLIN----KIVPgtiderklnKKKPKNIF--EATENLNLAL 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 320542951  113 KFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLI 146
Cdd:cd21217    80 NAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 170-257 1.45e-08

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 54.61  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNWI--HAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCPD---WELWDPKDAVQNASEAMGLADDwLNV 241
Cdd:cd21218    10 PPEEILLRWVnyHLKKagpTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKelvLEVLSEEDLEKRAEKVLQAAEK-LGC 88

                          90
                  ....*....|....*.
gi 320542951  242 RQLIKPEELVNPNVDE 257
Cdd:cd21218    89 KYFLTPEDIVSGNPRL 104
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 55-149 2.03e-08

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


Pssm-ID: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 54.67  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   55 ANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMP--KYNKRPTFRSQKLENVSVALKFLQDEGIKIVNIDSSDIVD 132
Cdd:cd21307    25 VNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHlsEFFLTPSSTSEMLHNVTLALELLKEGGLLNFPVNPEDIVN 104

                          90
                  ....*....|....*..
gi 320542951  133 CKLKLILGLIWTLILHY 149
Cdd:cd21307   105 GDSKATIRVLYCLFSKY 121
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
 46-149 2.65e-08

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


Pssm-ID: 409187  Cd Length: 130  Bit Score: 54.59  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   46 IQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYN--KRPTFRSQKLENVSVALKFLQDEGIKIV 123
Cdd:cd21338    21 VVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNfyLTPESFDQKVHNVSFAFELMQDGGLKKP 100

                          90       100
                  ....*....|....*....|....*.
gi 320542951  124 NIDSSDIVDCKLKLILGLIWTLILHY 149
Cdd:cd21338   101 KARPEDVVNLDLKSTLRVLYNLFTKY 126
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 170-265 2.71e-08

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


Pssm-ID: 409087  Cd Length: 106  Bit Score: 53.87  E-value: 2.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 246
Cdd:cd21238     2 TAKEKLLLWSQRMVegyQGLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80

                          90
                  ....*....|....*....
gi 320542951  247 PEELVNPNVDEQSMMTYLS 265
Cdd:cd21238    81 PEDVDVPQPDEKSIITYVS 99
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 172-267 3.26e-08

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


Pssm-ID: 409097  Cd Length: 105  Bit Score: 53.55  E-value: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  172 KQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 248
Cdd:cd21248     4 KDALLLWCQMKTagyPNVNVRNFTTSWRDGLAFNALIHKHRPDLI-DYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPE 82

                          90
                  ....*....|....*....
gi 320542951  249 ELVNPNVDEQSMMTYLSQY 267
Cdd:cd21248    83 DVNVEQPDEKSIITYVVTY 101
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 54-149 4.43e-08

second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409155  Cd Length: 121  Bit Score: 53.58  E-value: 4.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   54 WANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMP--KYNKRPTFRSQKLENVSVALKFLQDEGIKIVNIDSSDIV 131
Cdd:cd21306    24 FVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPlhSFHLTPTSFEQKVHNVQFAFELMQDAGLPKPKARPEDIV 103

                          90
                  ....*....|....*...
gi 320542951  132 DCKLKLILGLIWTLILHY 149
Cdd:cd21306   104 NLDLKSTLRVLYNLFTKY 121
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 172-276 6.94e-08

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


Pssm-ID: 409170  Cd Length: 119  Bit Score: 53.14  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  172 KQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 248
Cdd:cd21321     7 KDALLLWCQMKTagyPNVNVHNFTTSWRDGLAFNAIVHKHRPDLI-DFETLKKSNAHYNLQNAFNVAEKELGLTKLLDPE 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 320542951  249 ELVNPNVDEQSMMTYLSQYPN--SKLKTGA 276
Cdd:cd21321    86 DVNVDQPDEKSIITYVATYYHyfSKMKALA 115
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 170-267 7.72e-08

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


Pssm-ID: 409169  Cd Length: 108  Bit Score: 52.41  E-value: 7.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 246
Cdd:cd21320     2 SAKDALLLWCQMKTagyPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 80

                          90       100
                  ....*....|....*....|.
gi 320542951  247 PEELVNPNVDEQSMMTYLSQY 267
Cdd:cd21320    81 PEDISVDHPDEKSIITYVVTY 101
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 159-276 1.03e-07

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


Pssm-ID: 409171  Cd Length: 130  Bit Score: 52.75  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  159 EDDKQLNGSghtpKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLA 235
Cdd:cd21322    10 EDNRETRSA----KDALLLWCQMKTagyPEVNIQNFTTSWRDGLAFNALIHRHRPDLI-DFSKLTKSNATYNLQQAFNTA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 320542951  236 DDWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPN--SKLKTGA 276
Cdd:cd21322    85 EQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFYHyfSKMKALA 127
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 173-267 1.19e-07

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


Pssm-ID: 409188  Cd Length: 105  Bit Score: 51.90  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  173 QRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEE 249
Cdd:cd22198     3 EELLSWCQEQTegyRGVKVTDLTSSWRSGLALCAIIHRFRPDLI-DFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQE 81

                          90
                  ....*....|....*....
gi 320542951  250 LVNPNV-DEQSMMTYLSQY 267
Cdd:cd22198    82 MASLAVpDKLSMVSYLSQF 100
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 171-269 1.30e-07

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


Pssm-ID: 409046  Cd Length: 105  Bit Score: 51.77  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  171 PKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKP 247
Cdd:cd21197     1 KIQALLRWCRRQCegyPGVNITNLTSSFRDGLAFCAILHRHRPELI-DFHSLKKDNWLENNRLAFRVAETSLGIPALLDA 79

                          90       100
                  ....*....|....*....|...
gi 320542951  248 EELVNPNV-DEQSMMTYLSQYPN 269
Cdd:cd21197    80 EDMVTMHVpDRLSIITYVSQYYN 102
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 53-145 3.33e-07

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 50.76  E-value: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   53 RWANEHLK---TIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTF-RSQKLENVSVALKFLQDEGIKIVnIDSS 128
Cdd:cd21218    17 RWVNYHLKkagPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLsEEDLEKRAEKVLQAAEKLGCKYF-LTPE 95

                          90
                  ....*....|....*..
gi 320542951  129 DIVDCKLKLILGLIWTL 145
Cdd:cd21218    96 DIVSGNPRLNLAFVATL 112
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 170-267 2.87e-06

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


Pssm-ID: 409138  Cd Length: 124  Bit Score: 48.57  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNWIHAKIP---DLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 246
Cdd:cd21289    10 SAKEGLLLWCQRKTApyrNVNVQNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLD 88

                          90       100
                  ....*....|....*....|..
gi 320542951  247 PEELVN-PNVDEQSMMTYLSQY 267
Cdd:cd21289    89 AEDIVNtPKPDEKAIMTYVSCF 110
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 175-265 3.41e-06

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


Pssm-ID: 409082  Cd Length: 111  Bit Score: 48.00  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  175 LLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKD-AVQNASEAMGLADDWLNVRQLIKPEEL 250
Cdd:cd21233     5 LLSWVRQSTrnyPQVNVINFTSSWSDGLAFNALIHSHRPDLF-DWNSVVSQQsATERLDHAFNIARQHLGIEKLLDPEDV 83

                          90
                  ....*....|....*
gi 320542951  251 VNPNVDEQSMMTYLS 265
Cdd:cd21233    84 ATAHPDKKSILMYVT 98
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 170-266 3.58e-06

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


Pssm-ID: 409047  Cd Length: 105  Bit Score: 47.81  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNW---IHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDwLNVRQLIK 246
Cdd:cd21198     1 SSGQDLLEWcqeVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLI-DFSSLSPHDIKENCKLAFDAAAK-LGIPRLLD 78

                          90       100
                  ....*....|....*....|.
gi 320542951  247 PEELVNPNV-DEQSMMTYLSQ 266
Cdd:cd21198    79 PADMVLLSVpDKLSVMTYLHQ 99
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
 170-265 5.46e-06

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


Pssm-ID: 409137  Cd Length: 124  Bit Score: 47.76  E-value: 5.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNWIHAKIP---DLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIK 246
Cdd:cd21288    10 SAKEGLLLWCQRKTApyrNVNIQNFHTSWKDGLGLCALIHRHRPDLI-DYSKLNKDDPIGNINLAMEIAEKHLDIPKMLD 88

                          90       100
                  ....*....|....*....|
gi 320542951  247 PEELVN-PNVDEQSMMTYLS 265
Cdd:cd21288    89 AEDIVNtPKPDERAIMTYVS 108
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 39-153 1.03e-05

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 46.91  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   39 EDAQWKKIQ-----QNTFTRWANEhlKTIDRSINNLETDLSDGLRLIALIEVLsqkRMP----KYNKRPTFR----SQKL 105
Cdd:cd21330     1 QDIDWSSIEgetreERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKI---KVPvdwnRVNKPPYPKlgenMKKL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 320542951  106 ENVSVALKFLQDEG-IKIVNIDSSDIVDCKLKLILGLIWTLILHYSISM 153
Cdd:cd21330    76 ENCNYAVELGKNKAkFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNI 124
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 51-145 1.16e-05

third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409149  Cd Length: 119  Bit Score: 46.65  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   51 FTRWANEhlKTIDRSINNLETDLSDGLRLIALIEvlsqKRMP------KYNKRP----TFRSQKLENVSVALKFLQDEGI 120
Cdd:cd21300    12 FTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYD----KVIPgsvnwkKVNKAPasaeISRFKAVENTNYAVELGKQLGF 85

                          90       100
                  ....*....|....*....|....*
gi 320542951  121 KIVNIDSSDIVDCKLKLILGLIWTL 145
Cdd:cd21300    86 SLVGIQGADITDGSRTLTLALVWQL 110
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 170-265 1.45e-05

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


Pssm-ID: 409089  Cd Length: 107  Bit Score: 45.80  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNW---IHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDwLNVRQLIK 246
Cdd:cd21240     4 SAKEKLLLWtqkVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGVTRLLD 81

                          90
                  ....*....|....*....
gi 320542951  247 PEELVNPNVDEQSMMTYLS 265
Cdd:cd21240    82 AEDVDVPSPDEKSVITYVS 100
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 47-153 1.51e-05

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 46.13  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   47 QQNTFTRWANEhlKTIDRSINNLETDLSDGLRLIALIEVLsqkRMP----KYNKRP----TFRSQKLENVSVALKFLQDE 118
Cdd:cd21329     7 EERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMT---RVPvdwgHVNKPPypalGGNMKKIENCNYAVELGKNK 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 320542951  119 G-IKIVNIDSSDIVDCKLKLILGLIWTLILHYSISM 153
Cdd:cd21329    82 AkFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNV 117
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
 172-275 1.77e-05

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


Pssm-ID: 409109  Cd Length: 116  Bit Score: 45.85  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  172 KQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 248
Cdd:cd21260     3 KNMLLEWCRAKTrgyEHVDIQNFSSSWSSGMAFCALIHKFFPDAF-DYAELDPANRRHNFTLAFSTAEKHADCAPLLEVE 81

                          90       100
                  ....*....|....*....|....*...
gi 320542951  249 ELVNPNV-DEQSMMTYLSQYPNSKLKTG 275
Cdd:cd21260    82 DMVRMSVpDSKCVYTYIQELYRSLVQKG 109
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
15-146 2.07e-05

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 49.94  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   15 QEGQQADQYEENFDEDMEAERdlaedaqwkkiQQNTFTRWANEHlkTIDRSINNLETDLSDGLRLIaliEVLSQKRMP-- 92
Cdd:COG5069   359 QEPLEEEEKPEIEEFDAEGEF-----------EARVFTFWLNSL--DVSPEITNLFGDLRDQLILL---QALSKKLMPmt 422

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320542951   93 ----KYNKRPT-----FRSQKLENVSVALKFLQDEGIKIVNIDSSDIVDcKLKLILGLIWTLI 146
Cdd:COG5069   423 vthkLVKKQPAsgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILD-GIRLKLTLVWQVL 484
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 51-146 2.90e-05

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


Pssm-ID: 409141  Cd Length: 145  Bit Score: 46.12  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   51 FTRWANEHLKT---------IDRSINNLETDLSDGLRLIALIEvLSQ-----KRMPKYNKRPTFRSQklENVSVALKFLQ 116
Cdd:cd21292    29 FVNWINKNLGDdpdckhllpMDPNTDDLFEKVKDGILLCKMIN-LSVpdtidERAINKKKLTVFTIH--ENLTLALNSAS 105

                          90       100       110
                  ....*....|....*....|....*....|
gi 320542951  117 DEGIKIVNIDSSDIVDCKLKLILGLIWTLI 146
Cdd:cd21292   106 AIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 48-118 6.70e-05

first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409070  Cd Length: 106  Bit Score: 44.19  E-value: 6.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320542951   48 QNTFTRWANEHLKTiDRSI-NNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKlENVSVALKFLQDE 118
Cdd:cd21221     3 VRVLTEWINEELAD-DRIVvRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQK-QKLAVVLACVNFL 72
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 51-146 7.39e-05

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 45.03  E-value: 7.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   51 FTRWANE---------HLKTIDRSINNLETDLSDGLRLIALIEvLSQkrmPKYNKRPTFRSQKL------ENVSVALKFL 115
Cdd:cd21323    29 FVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMIN-LSQ---PDTIDERAINKKKLtpftisENLNLALNSA 104

                          90       100       110
                  ....*....|....*....|....*....|.
gi 320542951  116 QDEGIKIVNIDSSDIVDCKLKLILGLIWTLI 146
Cdd:cd21323   105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 175-265 1.15e-04

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


Pssm-ID: 409036  Cd Length: 104  Bit Score: 43.19  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  175 LLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELV 251
Cdd:cd21187     5 LLAWCRQSTrgyEQVDVKNFTTSWRDGLAFNALIHRHRPDLF-DFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVN 83

                          90
                  ....*....|....
gi 320542951  252 NPNVDEQSMMTYLS 265
Cdd:cd21187    84 VEQPDKKSILMYVT 97
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 47-153 1.24e-04

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


Pssm-ID: 409148  Cd Length: 114  Bit Score: 43.64  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   47 QQNTFTRWANEhlKTIDRSINNLETDLSDGLRLIALIEVLSQKRM--PKYNKRPT---FRsqKLENVSVALKFLQDEGIK 121
Cdd:cd21299     5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVnwKHANKPPIkmpFK--KVENCNQVVKIGKQLKFS 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 320542951  122 IVNIDSSDIVDCKLKLILGLIWTLILHYSISM 153
Cdd:cd21299    81 LVNVAGNDIVQGNKKLILALLWQLMRYHMLQL 112
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 184-269 1.48e-04

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


Pssm-ID: 409102  Cd Length: 106  Bit Score: 43.10  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  184 PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELVNPNV-DEQSMMT 262
Cdd:cd21253    18 RDVKVTNMTTSWRDGLAFCAIIHRFRPDLI-DFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDMVALKVpDKLSILT 96


                  ....*..
gi 320542951  263 YLSQYPN 269
Cdd:cd21253    97 YVSQYYN 103
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 172-275 1.91e-04

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


Pssm-ID: 409108  Cd Length: 112  Bit Score: 43.06  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  172 KQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 248
Cdd:cd21259     3 KQMLLDWCRAKTrgyENVDIQNFSSSWSDGMAFCALVHNFFPEAF-DYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVE 81

                          90       100
                  ....*....|....*....|....*...
gi 320542951  249 ELVN-PNVDEQSMMTYLSQYPNSKLKTG 275
Cdd:cd21259    82 DMVRmREPDWKCVYTYIQEFYRCLVQKG 109
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 172-264 1.92e-04

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


Pssm-ID: 409049  Cd Length: 107  Bit Score: 42.72  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  172 KQRLLNWIHAKIPDLP---INNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 248
Cdd:cd21200     3 KQMLLEWCQAKTRGYEhvdITNFSSSWSDGMAFCALIHHFFPDAF-DYSSLDPKNRRKNFELAFSTAEELADIAPLLEVE 81

                          90       100
                  ....*....|....*....|
gi 320542951  249 ELV----NPnvDEQSMMTYL 264
Cdd:cd21200    82 DMVrmgnRP--DWKCVFTYV 99
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 170-265 2.08e-04

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


Pssm-ID: 409088  Cd Length: 104  Bit Score: 42.67  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  170 TPKQRLLNW---IHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDwLNVRQLIK 246
Cdd:cd21239     1 SAKERLLLWsqqMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLI-DMNTVAVQSNLANLEHAFYVAEK-LGVTRLLD 78

                          90
                  ....*....|....*....
gi 320542951  247 PEELVNPNVDEQSMMTYLS 265
Cdd:cd21239    79 PEDVDVSSPDEKSVITYVS 97
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 74-146 2.23e-04

first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409143  Cd Length: 125  Bit Score: 43.21  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951   74 SDGLRLIALI----------EVLSQkrmPKYNKRPTFRSQKLENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLILGLIW 143
Cdd:cd21294    43 KDGLVLSKLIndsvpdtideRVLNK---PPRKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIW 119


                  ...
gi 320542951  144 TLI 146
Cdd:cd21294   120 QII 122
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 172-266 3.27e-04

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 41.94  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  172 KQRLLNWI---HAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWEL--WDPKDAVQNASEAMGLADDW-LNVRQLI 245
Cdd:cd00014     1 EEELLKWInevLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKkpKSPFKKRENINLFLNACKKLgLPELDLF 80

                          90       100
                  ....*....|....*....|.
gi 320542951  246 KPEELVNPNvDEQSMMTYLSQ 266
Cdd:cd00014    81 EPEDLYEKG-NLKKVLGTLWA 100
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 175-265 3.58e-04

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


Pssm-ID: 409083 [Multi-domain]  Cd Length: 104  Bit Score: 41.87  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  175 LLNWIHAKI-PDLPIN--NFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELV 251
Cdd:cd21234     5 LLSWVRQSTrPYSQVNvlNFTTSWTDGLAFNAVLHRHKPDLF-SWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVA 83

                          90
                  ....*....|....
gi 320542951  252 NPNVDEQSMMTYLS 265
Cdd:cd21234    84 VQLPDKKSIIMYLT 97
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 168-266 1.07e-03

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


Pssm-ID: 409106  Cd Length: 112  Bit Score: 40.78  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  168 GHTPKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELwDPKDAVQNASEAMGLADDwLNVRQL 244
Cdd:cd21257     6 GGSKRNALLKWCQKKTegyPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQEL-SSQDKKRNLLLAFQAAES-VGIKPS 83

                          90       100
                  ....*....|....*....|...
gi 320542951  245 IKPEELVNPN-VDEQSMMTYLSQ 266
Cdd:cd21257    84 LELSEMMYTDrPDWQSVMQYVAQ 106
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
 168-265 1.94e-03

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


Pssm-ID: 409105  Cd Length: 119  Bit Score: 40.06  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  168 GHTPKQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELwDPKDAVQN------ASEAMGLADDw 238
Cdd:cd21256    12 GGSKRNALLKWCQKKTegyQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQEL-NSQDKRRNftlafqAAESVGIKST- 89

                          90       100
                  ....*....|....*....|....*..
gi 320542951  239 LNVRQLIKPEElvnpnVDEQSMMTYLS 265
Cdd:cd21256    90 LDINEMVRTER-----PDWQSVMTYVT 111
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 171-265 3.10e-03

second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409075  Cd Length: 103  Bit Score: 39.37  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  171 PKQRLLNWIHAKIPD---LPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKP 247
Cdd:cd21226     1 SEDGLLAWCRQTTEGydgVNITSFKSSFNDGRAFLALLHAYDPELF-KQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEA 79

                          90
                  ....*....|....*...
gi 320542951  248 EELVNPNVDEQSMMTYLS 265
Cdd:cd21226    80 EDVMTGNPDERSIVLYTS 97
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
 172-251 3.32e-03

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


Pssm-ID: 409110  Cd Length: 107  Bit Score: 39.18  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  172 KQRLLNWIHAKI---PDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPE 248
Cdd:cd21261     3 KQILLEWCRSKTigyKNIDLQNFSSSWSDGMAFCALVHSFFPEAF-DYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVE 81


                  ...
gi 320542951  249 ELV 251
Cdd:cd21261    82 DMM 84
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
 171-269 3.73e-03

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


Pssm-ID: 409101  Cd Length: 107  Bit Score: 39.08  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542951  171 PKQRLLNWIH---AKIPDLPINNFTNDWTTGKAVGALVDACAPGLCpDWELWDPKDAVQNASEAMGLADDWLNVRQLIKP 247
Cdd:cd21252     1 ARRALQAWCRrqcEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLI-DFDSLSKDNVYENNRLAFEVAERELGIPALLDP 79

                          90       100
                  ....*....|....*....|...
gi 320542951  248 EELVNPNV-DEQSMMTYLSQYPN 269
Cdd:cd21252    80 EDMVSMKVpDCLSIMTYVSQYYN 102
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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