NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|392898139|ref|NP_001255220|]
View 

Calponin-homology (CH) domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 13-136 1.79e-72

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: 237.73  E-value: 1.79e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   13 VVPAIRHDDAEWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLA 92
Cdd:cd21311     1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 392898139   93 LNFFQNEENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISMG 136
Cdd:cd21311    81 LKFLEEDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISMP 124
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 151-253 7.18e-62

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: 206.46  E-value: 7.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  151 TPKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAE 230
Cdd:cd21230     1 TPKQRLLGWIQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALENATEAMQLAEDWLGVPQLITPEE 80

                          90       100
                  ....*....|....*....|...
gi 392898139  231 MIHPEIDEMSVMTYLSQFPATKP 253
Cdd:cd21230    81 IINPNVDEMSVMTYLSQFPKAKL 103
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1429-1512 7.69e-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: 106.15  E-value: 7.69e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1429 TVYGPGLQNAVVGEPATFTVCAKGSQAKELSVSIEGPA--KSQIKIHDNKDGTCSAAWVPPVPGEYKVHVKLGGKAVKDS 1506
Cdd:smart00557    5 KASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGS 84


                    ....*.
gi 392898139   1507 PFRVLV 1512
Cdd:smart00557   85 PFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1799-1889 2.07e-26

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 104.99  E-value: 2.07e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1799 AHKVRAAGQGVVRGETGTFNAFNIYHREAGVGAVAVTIEGPS--KATLEFKDHNDGNCHVDYKVATPGEYVVAVKFNDQH 1876
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 392898139   1877 IPDSPFKVYIAPA 1889
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 928-1018 9.82e-26

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 103.07  E-value: 9.82e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    928 KCKAYGPGLEQAVVGEKAVFELDLDGAGEGALSMEMRGPA--KAESRIQDRGNGKCSVEYVAKAPGDYEMAIKFGkdeqK 1005
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFG----G 78

                            90
                    ....*....|...
gi 392898139   1006 EHVKGSPFKAVVD 1018
Cdd:smart00557   79 EHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1606-1695 1.07e-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: 1.07e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1606 ASKVEVSGSGKAKGITLQANELLVDTSKAGYGGLSVSVQGPS--KAELTCKEVKSGLIKVLYTPTEPGVYAIAIKFADHH 1683
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 392898139   1684 VKDSPLTVQCTG 1695
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 738-828 9.94e-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: 97.29  E-value: 9.94e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    738 ASKLKIFGPGVDGPVYsKEPTRFTIDATQAGPGAVEVALRDDQGENVDLDVLDNQDGSFTVKYTAQRPGAYQLNVVFAGE 817
Cdd:smart00557    1 ASKVKASGPGLEKGVV-GEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|...
gi 392898139    818 EI--SPIEINVKP 828
Cdd:smart00557   80 HIpgSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1990-2078 1.07e-22

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 94.21  E-value: 1.07e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1990 PTAISASGDGLVKGTTGQKCEFVINTANAGAGILTVQMDGPSKATLDAYELEKG---YKVRYTPLAPGSYFASVKYNGIH 2066
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGdgtYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 392898139   2067 APGSPFKIPVEG 2078
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 547-635 1.54e-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: 93.82  E-value: 1.54e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    547 SKIRAFGAGLEGGIVNEPCVFDVEMNG-ESKDLSFAVEGPS--KAEIGCQERPDGSAILSYTPTVAGVYKVGVLADGKHI 623
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDaGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|..
gi 392898139    624 QDSPFVLRVTEP 635
Cdd:smart00557   82 PGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2115-2203 2.64e-21

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: 90.36  E-value: 2.64e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   2115 AAKVTAKGAGLNKFFPGRPAAFQIDTGLAGTNLLMVGVVTTKGPCEEVVVRHQGSGHYVCSYRIPDRVKGFVFIKYGDKE 2194
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80


                    ....*....
gi 392898139   2195 IPGSPFAIE 2203
Cdd:smart00557   81 IPGSPFTVK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1904-1984 4.32e-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: 66.86  E-value: 4.32e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1904 QGIPAGKAFTFTVLTHRA-KGHLEAKVVTPNNEVDTIDIVPIEDGeSYAMRFVPKETGNHFIHVTLDGAPMRESPFRLRV 1982
Cdd:smart00557   12 EKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDG-TYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ..
gi 392898139   1983 GG 1984
Cdd:smart00557   91 GP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1351-1421 1.26e-12

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: 65.70  E-value: 1.26e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392898139   1351 KFNVRDLGYQPKDLEAIVMPPTQKKEVAEIIDNLDGTILVKYTPKVHGSHELSILQNGAQLQGTPIKFYVD 1421
Cdd:smart00557   21 EFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
IG_FLMN super family cl42963
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 641-735 4.39e-12

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).


The actual alignment was detected with superfamily member smart00557:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 64.16  E-value: 4.39e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    641 PSATRVTGIDESKVYnVGEKIPFRVDTRLCGVDlVPKVEILDPELNPISYGAREITPGLFEYTLIPDAPIKHKIDVSVAG 720
Cdd:smart00557    1 ASKVKASGPGLEKGV-VGEPAEFTVDTRDAGGG-ELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 392898139    721 VSVPGAPFSVKVKEP 735
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1734-1787 3.45e-08

Filamin/ABP280 repeat;


:

Pssm-ID: 395505  Cd Length: 89  Bit Score: 52.68  E-value: 3.45e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392898139  1734 DITARLMDPKGHTDDIEMRDLGQQYYQLKFTPKMEGIHTLSVMYKDAHVNGSPF 1787
Cdd:pfam00630   35 EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
1506-1595 5.46e-07

Filamin/ABP280 repeat;


:

Pssm-ID: 395505  Cd Length: 89  Bit Score: 49.21  E-value: 5.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1506 SPFRVLVMGEGQKRShlSVGSTSEVALpITQQELKGISASIKSPGGIEEPCFVRLLDGGRLGVSFTPREAGEHLITVKRD 1585
Cdd:pfam00630    3 DASKVKASGPGLEPG--VVGKPAEFTV-DTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 392898139  1586 GKLVPKAPFK 1595
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN super family cl42963
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 365-444 2.01e-06

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).


The actual alignment was detected with superfamily member smart00557:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 47.98  E-value: 2.01e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    365 KTAKVGDDVKFAV--VDAIEGPVEAIVVDPTGKEHRMVILDgTSPGEHSFEYKIPCIGLHSVNVFHKKLPLTGSPFPLRG 442
Cdd:smart00557   12 EKGVVGEPAEFTVdtRDAGGGELEVEVTGPSGKKVPVEVKD-NGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ..
gi 392898139    443 KP 444
Cdd:smart00557   91 GP 92
IG_FLMN super family cl42963
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 259-356 5.06e-03

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).


The actual alignment was detected with superfamily member smart00557:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 38.35  E-value: 5.06e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    259 KVQATISNLDKIlQVNDPREFDLKLSRDGF-KPKVSIRDEDGQDIHLSLKKVEDkeNAYKVKFTPTKIGFIHVDVAANDV 337
Cdd:smart00557    3 KVKASGPGLEKG-VVGEPAEFTVDTRDAGGgELEVEVTGPSGKKVPVEVKDNGD--GTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....*....
gi 392898139    338 HtfetqtIPEASVICQVVP 356
Cdd:smart00557   80 H------IPGSPFTVKVGP 92
 
Name Accession Description Interval E-value
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 13-136 1.79e-72

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: 237.73  E-value: 1.79e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   13 VVPAIRHDDAEWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLA 92
Cdd:cd21311     1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 392898139   93 LNFFQNEENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISMG 136
Cdd:cd21311    81 LKFLEEDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISMP 124
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 151-253 7.18e-62

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: 206.46  E-value: 7.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  151 TPKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAE 230
Cdd:cd21230     1 TPKQRLLGWIQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALENATEAMQLAEDWLGVPQLITPEE 80

                          90       100
                  ....*....|....*....|...
gi 392898139  231 MIHPEIDEMSVMTYLSQFPATKP 253
Cdd:cd21230    81 IINPNVDEMSVMTYLSQFPKAKL 103
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
23-275 5.42e-27

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 118.89  E-value: 5.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   23 EWKIIQQNTFTRWVKNHLQKAG-ETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQNeEN 101
Cdd:COG5069     5 KWQKVQKKTFTKWTNEKLISGGqKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKG-KG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  102 IKIINIDSTHIVDHNKKLILGLVWTLILHYSISMgwIQEKredgdnKEETPKQKLLNW----IRNRLPGMPISNFTSDWN 177
Cdd:COG5069    84 VKLFNIGPQDIVDGNPKLILGLIWSLISRLTIAT--INEE------GELTKHINLLLWcdedTGGYKPEVDTFDFFRSWR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  178 DGVALGALVNSMAPGAL-EDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEMIHPEI-DEMSVMTYLS-QFPATKPI 254
Cdd:COG5069   156 DGLAFSALIHDSRPDTLdPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSwYIIRFGLL 235

                         250       260
                  ....*....|....*....|.
gi 392898139  255 imkPKVQATISNLDKILQVND 275
Cdd:COG5069   236 ---EKIDIALHRVYRLLEADE 253
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1429-1512 7.69e-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: 106.15  E-value: 7.69e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1429 TVYGPGLQNAVVGEPATFTVCAKGSQAKELSVSIEGPA--KSQIKIHDNKDGTCSAAWVPPVPGEYKVHVKLGGKAVKDS 1506
Cdd:smart00557    5 KASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGS 84


                    ....*.
gi 392898139   1507 PFRVLV 1512
Cdd:smart00557   85 PFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1799-1889 2.07e-26

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 104.99  E-value: 2.07e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1799 AHKVRAAGQGVVRGETGTFNAFNIYHREAGVGAVAVTIEGPS--KATLEFKDHNDGNCHVDYKVATPGEYVVAVKFNDQH 1876
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 392898139   1877 IPDSPFKVYIAPA 1889
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 928-1018 9.82e-26

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 103.07  E-value: 9.82e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    928 KCKAYGPGLEQAVVGEKAVFELDLDGAGEGALSMEMRGPA--KAESRIQDRGNGKCSVEYVAKAPGDYEMAIKFGkdeqK 1005
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFG----G 78

                            90
                    ....*....|...
gi 392898139   1006 EHVKGSPFKAVVD 1018
Cdd:smart00557   79 EHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1606-1695 1.07e-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: 1.07e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1606 ASKVEVSGSGKAKGITLQANELLVDTSKAGYGGLSVSVQGPS--KAELTCKEVKSGLIKVLYTPTEPGVYAIAIKFADHH 1683
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 392898139   1684 VKDSPLTVQCTG 1695
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 738-828 9.94e-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: 97.29  E-value: 9.94e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    738 ASKLKIFGPGVDGPVYsKEPTRFTIDATQAGPGAVEVALRDDQGENVDLDVLDNQDGSFTVKYTAQRPGAYQLNVVFAGE 817
Cdd:smart00557    1 ASKVKASGPGLEKGVV-GEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|...
gi 392898139    818 EI--SPIEINVKP 828
Cdd:smart00557   80 HIpgSPFTVKVGP 92
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 27-133 1.77e-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: 96.97  E-value: 1.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    27 IQQNTFTRWVKNHLQKAGE--TIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAfRSQKLENVSLALNFFQNEENIKI 104
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPgvRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS-EFDKLENINLALDVAEKKLGVPK 80

                           90       100
                   ....*....|....*....|....*....
gi 392898139   105 INIDSTHIVDHNKKLILGLVWTLILHYSI 133
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1990-2078 1.07e-22

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 94.21  E-value: 1.07e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1990 PTAISASGDGLVKGTTGQKCEFVINTANAGAGILTVQMDGPSKATLDAYELEKG---YKVRYTPLAPGSYFASVKYNGIH 2066
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGdgtYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 392898139   2067 APGSPFKIPVEG 2078
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 547-635 1.54e-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: 93.82  E-value: 1.54e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    547 SKIRAFGAGLEGGIVNEPCVFDVEMNG-ESKDLSFAVEGPS--KAEIGCQERPDGSAILSYTPTVAGVYKVGVLADGKHI 623
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDaGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|..
gi 392898139    624 QDSPFVLRVTEP 635
Cdd:smart00557   82 PGSPFTVKVGPA 93
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 150-248 2.94e-22

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: 93.51  E-value: 2.94e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   150 ETPKQKLLNWIRNRL----PGMPISNFTSDWNDGVALGALVNSMAPGALEDWE-NWSPNDALENTEKAMKSAQDLLKVAP 224
Cdd:pfam00307    1 LELEKELLRWINSHLaeygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKLGVPK 80

                           90       100
                   ....*....|....*....|....*
gi 392898139   225 -LIAPAEMIHPeiDEMSVMTYLSQF 248
Cdd:pfam00307   81 vLIEPEDLVEG--DNKSVLTYLASL 103
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2115-2203 2.64e-21

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: 90.36  E-value: 2.64e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   2115 AAKVTAKGAGLNKFFPGRPAAFQIDTGLAGTNLLMVGVVTTKGPCEEVVVRHQGSGHYVCSYRIPDRVKGFVFIKYGDKE 2194
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80


                    ....*....
gi 392898139   2195 IPGSPFAIE 2203
Cdd:smart00557   81 IPGSPFTVK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1429-1509 7.06e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.19  E-value: 7.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1429 TVYGPGLQNAVVGEPATFTVCAKGSQAkELSVSIEGPAKSQIKIH--DNKDGTCSAAWVPPVPGEYKVHVKLGGKAVKDS 1506
Cdd:pfam00630    8 KASGPGLEPGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEvtDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGS 86


                   ...
gi 392898139  1507 PFR 1509
Cdd:pfam00630   87 PFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
924-1014 1.36e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.42  E-value: 1.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   924 TDVNKCKAYGPGLEQAVVGEKAVFELDLDGA-GEGALSMEMRGPAKAESRIQDRGNGKCSVEYVAKAPGDYEMAIKFGkd 1002
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAgGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN-- 79

                           90
                   ....*....|..
gi 392898139  1003 eqKEHVKGSPFK 1014
Cdd:pfam00630   80 --GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
543-629 4.97e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 80.80  E-value: 4.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   543 PESSSKIRAFGAGLEGGIVNEPCVFDVEMNGESKDLSFAVEGPS--KAEIGCQERPDGSAILSYTPTVAGVYKVGVLADG 620
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 392898139   621 KHIQDSPFV 629
Cdd:pfam00630   81 QHIPGSPFK 89
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 30-130 9.35e-18

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 80.44  E-value: 9.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139     30 NTFTRWVKNHLQKAGE-TIESLETDFSDGLKLIALAQVLShknVGKFNKKVA----FRSQKLENVSLALNFFQnEENIKI 104
Cdd:smart00033    1 KTLLRWVNSLLAEYDKpPVTNFSSDLKDGVALCALLNSLS---PGLVDKKKVaaslSRFKKIENINLALSFAE-KLGGKV 76

                            90       100
                    ....*....|....*....|....*.
gi 392898139    105 INIDSTHIVDhNKKLILGLVWTLILH 130
Cdd:smart00033   77 VLFEPEDLVE-GPKLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
735-821 9.63e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 80.03  E-value: 9.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   735 PTDASKLKIFGPGVDGPVySKEPTRFTIDATQAGpGAVEVALRDDQGENVDLDVLDNQDGSFTVKYTAQRPGAYQLNVVF 814
Cdd:pfam00630    1 AADASKVKASGPGLEPGV-VGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78


                   ....*....
gi 392898139   815 AGEEI--SP 821
Cdd:pfam00630   79 NGQHIpgSP 87
Filamin pfam00630
Filamin/ABP280 repeat;
1797-1883 3.35e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 78.48  E-value: 3.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1797 GGAHKVRAAGQGVVRGETGTFNAFNIYHREAGvGAVAVTIEGPS--KATLEFKDHNDGNCHVDYKVATPGEYVVAVKFND 1874
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 392898139  1875 QHIPDSPFK 1883
Cdd:pfam00630   81 QHIPGSPFK 89
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 156-248 2.41e-16

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 76.59  E-value: 2.41e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    156 LLNWIRNRL---PGMPISNFTSDWNDGVALGALVNSMAPGALEDW---ENWSPNDALENTEKAMKSAQDLLKVAPLIAPA 229
Cdd:smart00033    3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKkvaASLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90
                    ....*....|....*....
gi 392898139    230 EMIHPEIDEMSVMTYLSQF 248
Cdd:smart00033   83 DLVEGPKLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
2113-2200 3.27e-16

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 75.79  E-value: 3.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  2113 GDAAKVTAKGAGLNKFFPGRPAAFQIDTGLAGtNLLMVGVVTTKGPCEEVVVRHQGSGHYVCSYRIPDRVKGFVFIKYGD 2192
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 392898139  2193 KEIPGSPF 2200
Cdd:pfam00630   81 QHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
1988-2073 1.21e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 73.86  E-value: 1.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1988 CDPTAISASGDGLVKGTTGQKCEFVINTANAGaGILTVQMDGPSKATLDAYELEKG---YKVRYTPLAPGSYFASVKYNG 2064
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGdgtYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 392898139  2065 IHAPGSPFK 2073
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1603-1690 1.83e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 73.48  E-value: 1.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1603 VGDASKVEVSGSGKAKGITLQANELLVDTSKAGyGGLSVSVQGPS--KAELTCKEVKSGLIKVLYTPTEPGVYAIAIKFA 1680
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 392898139  1681 DHHVKDSPLT 1690
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1904-1984 4.32e-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: 66.86  E-value: 4.32e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1904 QGIPAGKAFTFTVLTHRA-KGHLEAKVVTPNNEVDTIDIVPIEDGeSYAMRFVPKETGNHFIHVTLDGAPMRESPFRLRV 1982
Cdd:smart00557   12 EKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDG-TYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ..
gi 392898139   1983 GG 1984
Cdd:smart00557   91 GP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1351-1421 1.26e-12

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: 65.70  E-value: 1.26e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392898139   1351 KFNVRDLGYQPKDLEAIVMPPTQKKEVAEIIDNLDGTILVKYTPKVHGSHELSILQNGAQLQGTPIKFYVD 1421
Cdd:smart00557   21 EFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
1903-1979 2.68e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 64.62  E-value: 2.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1903 GQGI---PAGKAFTFTVLTHRAKGHLEAKVVTPNNEVDTIDIVPIEDGeSYAMRFVPKETGNHFIHVTLDGAPMRESPFR 1979
Cdd:pfam00630   11 GPGLepgVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDG-TYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 641-735 4.39e-12

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: 64.16  E-value: 4.39e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    641 PSATRVTGIDESKVYnVGEKIPFRVDTRLCGVDlVPKVEILDPELNPISYGAREITPGLFEYTLIPDAPIKHKIDVSVAG 720
Cdd:smart00557    1 ASKVKASGPGLEKGV-VGEPAEFTVDTRDAGGG-ELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 392898139    721 VSVPGAPFSVKVKEP 735
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1734-1787 3.45e-08

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 52.68  E-value: 3.45e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392898139  1734 DITARLMDPKGHTDDIEMRDLGQQYYQLKFTPKMEGIHTLSVMYKDAHVNGSPF 1787
Cdd:pfam00630   35 EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
1506-1595 5.46e-07

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 49.21  E-value: 5.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1506 SPFRVLVMGEGQKRShlSVGSTSEVALpITQQELKGISASIKSPGGIEEPCFVRLLDGGRLGVSFTPREAGEHLITVKRD 1585
Cdd:pfam00630    3 DASKVKASGPGLEPG--VVGKPAEFTV-DTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 392898139  1586 GKLVPKAPFK 1595
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 365-444 2.01e-06

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: 47.98  E-value: 2.01e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    365 KTAKVGDDVKFAV--VDAIEGPVEAIVVDPTGKEHRMVILDgTSPGEHSFEYKIPCIGLHSVNVFHKKLPLTGSPFPLRG 442
Cdd:smart00557   12 EKGVVGEPAEFTVdtRDAGGGELEVEVTGPSGKKVPVEVKD-NGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ..
gi 392898139    443 KP 444
Cdd:smart00557   91 GP 92
Filamin pfam00630
Filamin/ABP280 repeat;
641-728 1.45e-05

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 45.36  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   641 PSATRVTGIDESKVYnVGEKIPFRVDTRlcGVDLVPKVEILDPELNPISYGAREITPGLFEYTLIPDAPIKHKIDVSVAG 720
Cdd:pfam00630    4 ASKVKASGPGLEPGV-VGKPAEFTVDTR--DAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 392898139   721 VSVPGAPF 728
Cdd:pfam00630   81 QHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
1363-1417 1.03e-04

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 43.05  E-value: 1.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392898139  1363 DLEAIVMPPTQKKEVAEIIDNLDGTILVKYTPKVHGSHELSILQNGAQLQGTPIK 1417
Cdd:pfam00630   35 EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
365-438 8.00e-04

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 40.35  E-value: 8.00e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392898139   365 KTAKVGDDVKFAV--VDAiEGPVEAIVVDPTGKEHRMVILDgTSPGEHSFEYKIPCIGLHSVNVFHKKLPLTGSPF 438
Cdd:pfam00630   15 EPGVVGKPAEFTVdtRDA-GGEGEVEVTGPDGSPVPVEVTD-NGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 259-356 5.06e-03

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: 38.35  E-value: 5.06e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    259 KVQATISNLDKIlQVNDPREFDLKLSRDGF-KPKVSIRDEDGQDIHLSLKKVEDkeNAYKVKFTPTKIGFIHVDVAANDV 337
Cdd:smart00557    3 KVKASGPGLEKG-VVGEPAEFTVDTRDAGGgELEVEVTGPSGKKVPVEVKDNGD--GTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....*....
gi 392898139    338 HtfetqtIPEASVICQVVP 356
Cdd:smart00557   80 H------IPGSPFTVKVGP 92
 
Name Accession Description Interval E-value
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 13-136 1.79e-72

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: 237.73  E-value: 1.79e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   13 VVPAIRHDDAEWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLA 92
Cdd:cd21311     1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 392898139   93 LNFFQNEENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISMG 136
Cdd:cd21311    81 LKFLEEDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISMP 124
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 151-253 7.18e-62

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: 206.46  E-value: 7.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  151 TPKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAE 230
Cdd:cd21230     1 TPKQRLLGWIQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALENATEAMQLAEDWLGVPQLITPEE 80

                          90       100
                  ....*....|....*....|...
gi 392898139  231 MIHPEIDEMSVMTYLSQFPATKP 253
Cdd:cd21230    81 IINPNVDEMSVMTYLSQFPKAKL 103
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 137-252 8.69e-50

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: 172.66  E-value: 8.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  137 WIQEKREDGDNKEETPKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSA 216
Cdd:cd21315     2 WEGEDDGPDDGKGPTPKQRLLGWIQSKVPDLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAVKNAKEAMDLA 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 392898139  217 QDLLKVAPLIAPAEMIHPEIDEMSVMTYLSQFPATK 252
Cdd:cd21315    82 EDWLDVPQLIKPEEMVNPKVDELSMMTYLSQFPNAK 117
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 24-131 6.82e-46

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: 161.12  E-value: 6.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   24 WKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGK-FNKKVAFRSQKLENVSLALNFFQnEENI 102
Cdd:cd21228     1 WKKIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkYNKRPTFRQMKLENVSVALEFLE-RESI 79

                          90       100
                  ....*....|....*....|....*....
gi 392898139  103 KIINIDSTHIVDHNKKLILGLVWTLILHY 131
Cdd:cd21228    80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 143-258 2.54e-45

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: 159.85  E-value: 2.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  143 EDGDNKEETPKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDLLKV 222
Cdd:cd21314     3 DEEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPVQNAREAMQQADDWLGV 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 392898139  223 APLIAPAEMIHPEIDEMSVMTYLSQFPATKpiiMKP 258
Cdd:cd21314    83 PQVIAPEEIVDPNVDEHSVMTYLSQFPKAK---LKP 115
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
 144-252 2.26e-43

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: 154.09  E-value: 2.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  144 DGDNKEETPKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDLLKVA 223
Cdd:cd21313     1 DDDAKKQTPKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPQKPVDNAREAMQQADDWLGVP 80

                          90       100
                  ....*....|....*....|....*....
gi 392898139  224 PLIAPAEMIHPEIDEMSVMTYLSQFPATK 252
Cdd:cd21313    81 QVITPEEIIHPDVDEHSVMTYLSQFPKAK 109
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 151-253 4.47e-43

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: 152.78  E-value: 4.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  151 TPKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAE 230
Cdd:cd21184     1 SGKSLLLEWVNSKIPEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMDIAEEELGIPKIITPED 80

                          90       100
                  ....*....|....*....|...
gi 392898139  231 MIHPEIDEMSVMTYLSQFPATKP 253
Cdd:cd21184    81 MVSPNVDELSVMTYLSYFRNAKV 103
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 24-133 5.00e-42

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: 150.13  E-value: 5.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   24 WKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQnEENIK 103
Cdd:cd21227     1 WVEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMA-EDGIK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 392898139  104 IINIDSTHIVDHNKKLILGLVWTLILHYSI 133
Cdd:cd21227    80 LVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 20-135 2.34e-40

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: 145.94  E-value: 2.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   20 DDAEWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNV-GKFNKKVAFRSQKLENVSLALNFFqN 98
Cdd:cd21310     9 EDAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMyRKYHPRPNFRQMKLENVSVALEFL-D 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 392898139   99 EENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISM 135
Cdd:cd21310    88 REHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 124
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 24-131 4.13e-40

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: 144.55  E-value: 4.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   24 WKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVG-KFNKKVAFRSQKLENVSLALNFFQnEENI 102
Cdd:cd21183     1 WKRIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKrSYNRRPAFQQHYLENVSTALKFIE-ADHI 79

                          90       100
                  ....*....|....*....|....*....
gi 392898139  103 KIINIDSTHIVDHNKKLILGLVWTLILHY 131
Cdd:cd21183    80 KLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 20-135 3.45e-38

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: 139.83  E-value: 3.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   20 DDAEWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNV-GKFNKKVAFRSQKLENVSLALNFFqN 98
Cdd:cd21309    10 EDAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVALEFL-D 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 392898139   99 EENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISM 135
Cdd:cd21309    89 RESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISM 125
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 24-131 7.91e-38

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: 137.92  E-value: 7.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   24 WKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQNeENIK 103
Cdd:cd21215     1 WVDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKS-RGVK 79

                          90       100
                  ....*....|....*....|....*...
gi 392898139  104 IINIDSTHIVDHNKKLILGLVWTLILHY 131
Cdd:cd21215    80 LTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 20-135 8.03e-38

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: 138.68  E-value: 8.03e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   20 DDAEWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNV-GKFNKKVAFRSQKLENVSLALNFFqN 98
Cdd:cd21308    13 EDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQLENVSVALEFL-D 91

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 392898139   99 EENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISM 135
Cdd:cd21308    92 RESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 128
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 140-252 1.31e-37

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: 137.63  E-value: 1.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  140 EKREDGDNKEETPKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDL 219
Cdd:cd21312     1 DEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDW 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 392898139  220 LKVAPLIAPAEMIHPEIDEMSVMTYLSQFPATK 252
Cdd:cd21312    81 LGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAK 113
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 27-131 8.46e-31

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: 117.89  E-value: 8.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   27 IQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFrsQKLENVSLALNFFQNeENIKIIN 106
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRF--HRLQNVQTALDFLKY-RKIKLVN 79

                          90       100
                  ....*....|....*....|....*
gi 392898139  107 IDSTHIVDHNKKLILGLVWTLILHY 131
Cdd:cd21188    80 IRAEDIVDGNPKLTLGLIWTIILHF 104
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 152-248 1.43e-30

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: 117.10  E-value: 1.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  152 PKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEM 231
Cdd:cd21229     4 PKKLMLAWLQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPEDL 83

                          90
                  ....*....|....*..
gi 392898139  232 IHPEIDEMSVMTYLSQF 248
Cdd:cd21229    84 SSPHLDELSGMTYLSYF 100
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 23-129 6.49e-30

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: 115.18  E-value: 6.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   23 EWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKfNKKVAFRSQKLENVSLALNFFQnEENI 102
Cdd:cd21214     1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPK-PERGKMRFHKIANVNKALDFIA-SKGV 78

                          90       100
                  ....*....|....*....|....*..
gi 392898139  103 KIINIDSTHIVDHNKKLILGLVWTLIL 129
Cdd:cd21214    79 KLVSIGAEEIVDGNLKMTLGMIWTIIL 105
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 9-129 3.19e-27

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: 108.15  E-value: 3.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    9 QEEEVVPAIRhddAEWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAfRSQKLEN 88
Cdd:cd21193     1 FEKGRIRALQ---EERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRGRL-RVQKIEN 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 392898139   89 VSLALNFFQneENIKIINIDSTHIVDHNKKLILGLVWTLIL 129
Cdd:cd21193    77 VNKALAFLK--TKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
23-275 5.42e-27

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 118.89  E-value: 5.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   23 EWKIIQQNTFTRWVKNHLQKAG-ETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQNeEN 101
Cdd:COG5069     5 KWQKVQKKTFTKWTNEKLISGGqKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKG-KG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  102 IKIINIDSTHIVDHNKKLILGLVWTLILHYSISMgwIQEKredgdnKEETPKQKLLNW----IRNRLPGMPISNFTSDWN 177
Cdd:COG5069    84 VKLFNIGPQDIVDGNPKLILGLIWSLISRLTIAT--INEE------GELTKHINLLLWcdedTGGYKPEVDTFDFFRSWR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  178 DGVALGALVNSMAPGAL-EDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEMIHPEI-DEMSVMTYLS-QFPATKPI 254
Cdd:COG5069   156 DGLAFSALIHDSRPDTLdPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSwYIIRFGLL 235

                         250       260
                  ....*....|....*....|.
gi 392898139  255 imkPKVQATISNLDKILQVND 275
Cdd:COG5069   236 ---EKIDIALHRVYRLLEADE 253
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1429-1512 7.69e-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: 106.15  E-value: 7.69e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1429 TVYGPGLQNAVVGEPATFTVCAKGSQAKELSVSIEGPA--KSQIKIHDNKDGTCSAAWVPPVPGEYKVHVKLGGKAVKDS 1506
Cdd:smart00557    5 KASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGS 84


                    ....*.
gi 392898139   1507 PFRVLV 1512
Cdd:smart00557   85 PFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1799-1889 2.07e-26

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 104.99  E-value: 2.07e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1799 AHKVRAAGQGVVRGETGTFNAFNIYHREAGVGAVAVTIEGPS--KATLEFKDHNDGNCHVDYKVATPGEYVVAVKFNDQH 1876
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 392898139   1877 IPDSPFKVYIAPA 1889
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 928-1018 9.82e-26

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 103.07  E-value: 9.82e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    928 KCKAYGPGLEQAVVGEKAVFELDLDGAGEGALSMEMRGPA--KAESRIQDRGNGKCSVEYVAKAPGDYEMAIKFGkdeqK 1005
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFG----G 78

                            90
                    ....*....|...
gi 392898139   1006 EHVKGSPFKAVVD 1018
Cdd:smart00557   79 EHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1606-1695 1.07e-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: 1.07e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1606 ASKVEVSGSGKAKGITLQANELLVDTSKAGYGGLSVSVQGPS--KAELTCKEVKSGLIKVLYTPTEPGVYAIAIKFADHH 1683
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 392898139   1684 VKDSPLTVQCTG 1695
Cdd:smart00557   81 IPGSPFTVKVGP 92
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 23-129 1.20e-24

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: 100.52  E-value: 1.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   23 EWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKvAFRSQKLENVSLALNFFQnEENI 102
Cdd:cd21246    12 EREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKG-KMRIHCLENVDKALQFLK-EQRV 89

                          90       100
                  ....*....|....*....|....*..
gi 392898139  103 KIINIDSTHIVDHNKKLILGLVWTLIL 129
Cdd:cd21246    90 HLENMGSHDIVDGNHRLTLGLIWTIIL 116
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 738-828 9.94e-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: 97.29  E-value: 9.94e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    738 ASKLKIFGPGVDGPVYsKEPTRFTIDATQAGPGAVEVALRDDQGENVDLDVLDNQDGSFTVKYTAQRPGAYQLNVVFAGE 817
Cdd:smart00557    1 ASKVKASGPGLEKGVV-GEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|...
gi 392898139    818 EI--SPIEINVKP 828
Cdd:smart00557   80 HIpgSPFTVKVGP 92
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 27-131 1.01e-23

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: 97.84  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   27 IQQNTFTRWVKNHLQKAGET-IESLETDFSDGLKLIALAQVLSHKNVGKfnKKVAFRSQKLENVSLALNFFQNEeNIKII 105
Cdd:cd21186     2 VQKKTFTKWINSQLSKANKPpIKDLFEDLRDGTRLLALLEVLTGKKLKP--EKGRMRVHHLNNVNRALQVLEQN-NVKLV 78

                          90       100
                  ....*....|....*....|....*.
gi 392898139  106 NIDSTHIVDHNKKLILGLVWTLILHY 131
Cdd:cd21186    79 NISSNDIVDGNPKLTLGLVWSIILHW 104
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 27-133 1.77e-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: 96.97  E-value: 1.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    27 IQQNTFTRWVKNHLQKAGE--TIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAfRSQKLENVSLALNFFQNEENIKI 104
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPgvRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKS-EFDKLENINLALDVAEKKLGVPK 80

                           90       100
                   ....*....|....*....|....*....
gi 392898139   105 INIDSTHIVDHNKKLILGLVWTLILHYSI 133
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 23-133 3.02e-23

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: 96.49  E-value: 3.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   23 EWKIIQQNTFTRWVKNHLQKAGE--TIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQNEe 100
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSQpiVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKR- 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 392898139  101 NIKIINIDSTHIVDHNKKLILGLVWTLILHYSI 133
Cdd:cd21190    80 CIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 157-248 4.25e-23

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: 95.45  E-value: 4.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  157 LNWIRNRLPGMPISNFTSDWNDGVALGALVNSMApGALEDWENWSPNDALENTEKAMKSAQDlLKVAPLIAPAEMIHPEI 236
Cdd:cd21185     7 LRWVRQLLPDVDVNNFTTDWNDGRLLCGLVNALG-GSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEV 84

                          90
                  ....*....|..
gi 392898139  237 DEMSVMTYLSQF 248
Cdd:cd21185    85 EHLGIMAYAAQL 96
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 27-143 9.23e-23

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: 95.48  E-value: 9.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   27 IQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKfnKKVAFRSQKLENVSLALNFFQNEEnIKIIN 106
Cdd:cd21235     6 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQ-VKLVN 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 392898139  107 IDSTHIVDHNKKLILGLVWTLILHYSISMGWIQEKRE 143
Cdd:cd21235    83 IRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1990-2078 1.07e-22

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 94.21  E-value: 1.07e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1990 PTAISASGDGLVKGTTGQKCEFVINTANAGAGILTVQMDGPSKATLDAYELEKG---YKVRYTPLAPGSYFASVKYNGIH 2066
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGdgtYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 392898139   2067 APGSPFKIPVEG 2078
Cdd:smart00557   81 IPGSPFTVKVGP 92
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 24-132 1.07e-22

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: 94.91  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   24 WKIIQQNTFTRWVKNHLQKAGET-IESLETDFSDGLKLIALAQVLSHKNVG-KFNKKVAFRSQKLENVSLALNFFQNEEN 101
Cdd:cd21225     1 WEKVQIKAFTAWVNSVLEKRGIPkISDLATDLSDGVRLIFFLELVSGKKFPkKFDLEPKNRIQMIQNLHLAMLFIEEDLK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 392898139  102 IKIINIDSTHIVDHNKKLILGLVWTLILHYS 132
Cdd:cd21225    81 IRVQGIGAEDFVDNNKKLILGLLWTLYRKYR 111
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 547-635 1.54e-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: 93.82  E-value: 1.54e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    547 SKIRAFGAGLEGGIVNEPCVFDVEMNG-ESKDLSFAVEGPS--KAEIGCQERPDGSAILSYTPTVAGVYKVGVLADGKHI 623
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDaGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|..
gi 392898139    624 QDSPFVLRVTEP 635
Cdd:smart00557   82 PGSPFTVKVGPA 93
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 150-248 2.94e-22

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: 93.51  E-value: 2.94e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   150 ETPKQKLLNWIRNRL----PGMPISNFTSDWNDGVALGALVNSMAPGALEDWE-NWSPNDALENTEKAMKSAQDLLKVAP 224
Cdd:pfam00307    1 LELEKELLRWINSHLaeygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKLGVPK 80

                           90       100
                   ....*....|....*....|....*
gi 392898139   225 -LIAPAEMIHPeiDEMSVMTYLSQF 248
Cdd:pfam00307   81 vLIEPEDLVEG--DNKSVLTYLASL 103
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 27-141 6.25e-22

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: 93.51  E-value: 6.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   27 IQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKfnKKVAFRSQKLENVSLALNFFQNEEnIKIIN 106
Cdd:cd21236    17 VQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHRLQNVQIALDYLKRRQ-VKLVN 93

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 392898139  107 IDSTHIVDHNKKLILGLVWTLILHYSISMGWIQEK 141
Cdd:cd21236    94 IRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 23-133 1.72e-21

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: 91.67  E-value: 1.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   23 EWKIIQQNTFTRWVKNHLQKAGE--TIESLETDFSDGLKLIALAQVLSHKNV----GKFNKKVAFrsqkLENVSLALNFF 96
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLpcekGRRLKRVHF----LSNINTALKFL 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 392898139   97 QNEeNIKIINIDSTHIVDHNKKLILGLVWTLILHYSI 133
Cdd:cd21241    77 ESK-KIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2115-2203 2.64e-21

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: 90.36  E-value: 2.64e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   2115 AAKVTAKGAGLNKFFPGRPAAFQIDTGLAGTNLLMVGVVTTKGPCEEVVVRHQGSGHYVCSYRIPDRVKGFVFIKYGDKE 2194
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80


                    ....*....
gi 392898139   2195 IPGSPFAIE 2203
Cdd:smart00557   81 IPGSPFTVK 89
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 27-133 1.27e-20

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: 89.21  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   27 IQQNTFTRWVKNHLQKAGET-IESLETDFSDGLKLIALAQVLSHKNVGKfnKKVAFRSQKLENVSLALNFFQNEeNIKII 105
Cdd:cd21231     6 VQKKTFTKWINAQFAKFGKPpIEDLFTDLQDGRRLLELLEGLTGQKLVK--EKGSTRVHALNNVNKALQVLQKN-NVDLV 82

                          90       100
                  ....*....|....*....|....*...
gi 392898139  106 NIDSTHIVDHNKKLILGLVWTLILHYSI 133
Cdd:cd21231    83 NIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 27-134 1.82e-20

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: 88.94  E-value: 1.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   27 IQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKfnKKVAFRSQKLENVSLALNFFQNEEnIKIIN 106
Cdd:cd21237     6 VQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPR--EKGRMRFHRLQNVQIALDFLKQRQ-VKLVN 82

                          90       100
                  ....*....|....*....|....*...
gi 392898139  107 IDSTHIVDHNKKLILGLVWTLILHYSIS 134
Cdd:cd21237    83 IRNDDITDGNPKLTLGLIWTIILHFQIS 110
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 27-133 3.15e-20

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: 88.02  E-value: 3.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   27 IQQNTFTRWVKNHLQKAGETIE--SLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQnEENIKI 104
Cdd:cd21191     5 VQKRTFTRWINLHLEKCNPPLEvkDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLE-DSNVKL 83

                          90       100
                  ....*....|....*....|....*....
gi 392898139  105 INIDSTHIVDHNKKLILGLVWTLILHYSI 133
Cdd:cd21191    84 VSIDAAEIADGNPSLVLGLIWNIILFFQI 112
Filamin pfam00630
Filamin/ABP280 repeat;
1429-1509 7.06e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.19  E-value: 7.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1429 TVYGPGLQNAVVGEPATFTVCAKGSQAkELSVSIEGPAKSQIKIH--DNKDGTCSAAWVPPVPGEYKVHVKLGGKAVKDS 1506
Cdd:pfam00630    8 KASGPGLEPGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEvtDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGS 86


                   ...
gi 392898139  1507 PFR 1509
Cdd:pfam00630   87 PFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
924-1014 1.36e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.42  E-value: 1.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   924 TDVNKCKAYGPGLEQAVVGEKAVFELDLDGA-GEGALSMEMRGPAKAESRIQDRGNGKCSVEYVAKAPGDYEMAIKFGkd 1002
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAgGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN-- 79

                           90
                   ....*....|..
gi 392898139  1003 eqKEHVKGSPFK 1014
Cdd:pfam00630   80 --GQHIPGSPFK 89
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 23-129 7.80e-19

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: 85.08  E-value: 7.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   23 EWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKvAFRSQKLENVSLALNFFQnEENI 102
Cdd:cd21318    34 EREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRG-RMRIHSLENVDKALQFLK-EQRV 111

                          90       100
                  ....*....|....*....|....*..
gi 392898139  103 KIINIDSTHIVDHNKKLILGLVWTLIL 129
Cdd:cd21318   112 HLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 23-129 1.58e-18

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: 83.95  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   23 EWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKvAFRSQKLENVSLALNFFQnEENI 102
Cdd:cd21317    27 EREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKG-RMRIHCLENVDKALQFLK-EQKV 104

                          90       100
                  ....*....|....*....|....*..
gi 392898139  103 KIINIDSTHIVDHNKKLILGLVWTLIL 129
Cdd:cd21317   105 HLENMGSHDIVDGNHRLTLGLIWTIIL 131
Filamin pfam00630
Filamin/ABP280 repeat;
543-629 4.97e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 80.80  E-value: 4.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   543 PESSSKIRAFGAGLEGGIVNEPCVFDVEMNGESKDLSFAVEGPS--KAEIGCQERPDGSAILSYTPTVAGVYKVGVLADG 620
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 392898139   621 KHIQDSPFV 629
Cdd:pfam00630   81 QHIPGSPFK 89
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 30-130 9.35e-18

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 80.44  E-value: 9.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139     30 NTFTRWVKNHLQKAGE-TIESLETDFSDGLKLIALAQVLShknVGKFNKKVA----FRSQKLENVSLALNFFQnEENIKI 104
Cdd:smart00033    1 KTLLRWVNSLLAEYDKpPVTNFSSDLKDGVALCALLNSLS---PGLVDKKKVaaslSRFKKIENINLALSFAE-KLGGKV 76

                            90       100
                    ....*....|....*....|....*.
gi 392898139    105 INIDSTHIVDhNKKLILGLVWTLILH 130
Cdd:smart00033   77 VLFEPEDLVE-GPKLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
735-821 9.63e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 80.03  E-value: 9.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   735 PTDASKLKIFGPGVDGPVySKEPTRFTIDATQAGpGAVEVALRDDQGENVDLDVLDNQDGSFTVKYTAQRPGAYQLNVVF 814
Cdd:pfam00630    1 AADASKVKASGPGLEPGV-VGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78


                   ....*....
gi 392898139   815 AGEEI--SP 821
Cdd:pfam00630   79 NGQHIpgSP 87
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 32-131 3.13e-17

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: 79.16  E-value: 3.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   32 FTRWVKNHLQKAG--ETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQNeENIKIINIDS 109
Cdd:cd21212     5 YTDWANHYLEKGGhkRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAA-LGVDVQGITA 83

                          90       100
                  ....*....|....*....|..
gi 392898139  110 THIVDHNKKLILGLVWTLILHY 131
Cdd:cd21212    84 EDIVDGNLKAILGLFFSLSRYK 105
Filamin pfam00630
Filamin/ABP280 repeat;
1797-1883 3.35e-17

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 78.48  E-value: 3.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1797 GGAHKVRAAGQGVVRGETGTFNAFNIYHREAGvGAVAVTIEGPS--KATLEFKDHNDGNCHVDYKVATPGEYVVAVKFND 1874
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 392898139  1875 QHIPDSPFK 1883
Cdd:pfam00630   81 QHIPGSPFK 89
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 23-129 1.44e-16

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: 78.93  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   23 EWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKvAFRSQKLENVSLALNFFQnEENI 102
Cdd:cd21316    49 EREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKG-RMRIHCLENVDKALQFLK-EQRV 126

                          90       100
                  ....*....|....*....|....*..
gi 392898139  103 KIINIDSTHIVDHNKKLILGLVWTLIL 129
Cdd:cd21316   127 HLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 29-129 1.48e-16

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 76.99  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   29 QNTFTRWVKNHLQKAG-ETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQNEENIKIINI 107
Cdd:cd00014     1 EEELLKWINEVLGEELpVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLPELDLF 80

                          90       100
                  ....*....|....*....|...
gi 392898139  108 DSTHIVDH-NKKLILGLVWTLIL 129
Cdd:cd00014    81 EPEDLYEKgNLKKVLGTLWALAL 103
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 156-248 2.41e-16

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 76.59  E-value: 2.41e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    156 LLNWIRNRL---PGMPISNFTSDWNDGVALGALVNSMAPGALEDW---ENWSPNDALENTEKAMKSAQDLLKVAPLIAPA 229
Cdd:smart00033    3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKkvaASLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90
                    ....*....|....*....
gi 392898139    230 EMIHPEIDEMSVMTYLSQF 248
Cdd:smart00033   83 DLVEGPKLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
2113-2200 3.27e-16

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 75.79  E-value: 3.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  2113 GDAAKVTAKGAGLNKFFPGRPAAFQIDTGLAGtNLLMVGVVTTKGPCEEVVVRHQGSGHYVCSYRIPDRVKGFVFIKYGD 2192
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 392898139  2193 KEIPGSPF 2200
Cdd:pfam00630   81 QHIPGSPF 88
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 27-133 3.86e-16

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: 76.41  E-value: 3.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   27 IQQNTFTRWVKNHLQK--AGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFrsQKLENVSLALNFFQNEeNIKI 104
Cdd:cd21242     5 TQKRTFTNWINSQLAKhsPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVF--QCRSNIETALSFLKNK-SIKL 81

                          90       100
                  ....*....|....*....|....*....
gi 392898139  105 INIDSTHIVDHNKKLILGLVWTLILHYSI 133
Cdd:cd21242    82 INIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 27-133 7.97e-16

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: 75.05  E-value: 7.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   27 IQQNTFTRWVKNHLQKAGE-TIESLETDFSDGLKLIALAQVLSHKNVGKfnKKVAFRSQKLENVSLALNFFqNEENIKII 105
Cdd:cd21232     2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPK--ERGSTRVHALNNVNRVLQVL-HQNNVELV 78

                          90       100
                  ....*....|....*....|....*...
gi 392898139  106 NIDSTHIVDHNKKLILGLVWTLILHYSI 133
Cdd:cd21232    79 NIGGTDIVDGNHKLTLGLLWSIILHWQV 106
Filamin pfam00630
Filamin/ABP280 repeat;
1988-2073 1.21e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 73.86  E-value: 1.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1988 CDPTAISASGDGLVKGTTGQKCEFVINTANAGaGILTVQMDGPSKATLDAYELEKG---YKVRYTPLAPGSYFASVKYNG 2064
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGdgtYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 392898139  2065 IHAPGSPFK 2073
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1603-1690 1.83e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 73.48  E-value: 1.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1603 VGDASKVEVSGSGKAKGITLQANELLVDTSKAGyGGLSVSVQGPS--KAELTCKEVKSGLIKVLYTPTEPGVYAIAIKFA 1680
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 392898139  1681 DHHVKDSPLT 1690
Cdd:pfam00630   80 GQHIPGSPFK 89
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 154-248 2.11e-15

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: 73.86  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  154 QKLLNWIRNRL---PGMPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAE 230
Cdd:cd22198     3 EELLSWCQEQTegyRGVKVTDLTSSWRSGLALCAIIHRFRPD-LIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQE 81

                          90
                  ....*....|....*....
gi 392898139  231 M-IHPEIDEMSVMTYLSQF 248
Cdd:cd22198    82 MaSLAVPDKLSMVSYLSQF 100
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 151-249 4.26e-15

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


Pssm-ID: 409038  Cd Length: 105  Bit Score: 73.19  E-value: 4.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  151 TPKQKLLNWIR---NRLPGMPISNFTSDWNDGVALGALVNSMAPGALeDWENWSPNDALENTEKAMKSAQDLLKVAPLIA 227
Cdd:cd21189     1 SAKEALLLWARrttEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLI-DFRSVRNQSNRENLENAFNVAEKEFGVTRLLD 79

                          90       100
                  ....*....|....*....|....*.
gi 392898139  228 PAEMIHPEIDEMSVMTYLSQ----FP 249
Cdd:cd21189    80 PEDVDVPEPDEKSIITYVSSlydvFP 105
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 153-248 8.70e-14

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: 69.29  E-value: 8.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNRLPGMP---ISNFTSDWNDGVALGALVNSMAPGALeDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPA 229
Cdd:cd21200     3 KQMLLEWCQAKTRGYEhvdITNFSSSWSDGMAFCALIHHFFPDAF-DYSSLDPKNRRKNFELAFSTAEELADIAPLLEVE 81

                          90       100
                  ....*....|....*....|.
gi 392898139  230 EMIH--PEIDEMSVMTYLSQF 248
Cdd:cd21200    82 DMVRmgNRPDWKCVFTYVQSL 102
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 17-133 1.08e-13

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: 69.79  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   17 IRHDDAEWKIIQQNTFTRWVKNHLQKAGETIE--SLETDFSDGLKLIALAQVLSHKNVGKFNKKvAFRSQKLENVSLALN 94
Cdd:cd21247    10 IRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIEitDIYTELKDGIHLLRLLELISGEQLPRPSRG-KMRVHFLENNSKAIT 88

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 392898139   95 FFQNEENIKIINIDSthIVDHNKKLILGLVWTLILHYSI 133
Cdd:cd21247    89 FLKTKVPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 153-248 1.83e-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: 68.21  E-value: 1.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNRLPGMP---ISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPA 229
Cdd:cd21194     4 KDALLLWCQRKTAGYPgvnIQNFTTSWRDGLAFNALIHAHRPD-LIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAE 82

                          90
                  ....*....|....*....
gi 392898139  230 EMIHPEIDEMSVMTYLSQF 248
Cdd:cd21194    83 DVDVARPDEKSIMTYVASY 101
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 151-247 2.78e-13

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: 67.84  E-value: 2.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  151 TPKQKLLNWIRN---RLPGMPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQdLLKVAPLIA 227
Cdd:cd21198     1 SSGQDLLEWCQEvtkGYRGVKITNLTTSWRNGLAFCAILHHFRPD-LIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLD 78

                          90       100
                  ....*....|....*....|.
gi 392898139  228 PAEMIHPEI-DEMSVMTYLSQ 247
Cdd:cd21198    79 PADMVLLSVpDKLSVMTYLHQ 99
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 156-248 3.00e-13

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


Pssm-ID: 409094  Cd Length: 106  Bit Score: 67.89  E-value: 3.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  156 LLNWIRNRLP--GMPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEMIH 233
Cdd:cd21245     8 LLNWVQRRTRkyGVAVQDFGSSWRSGLAFLALIKAIDPS-LVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPEDVMV 86

                          90
                  ....*....|....*
gi 392898139  234 PEIDEMSVMTYLSQF 248
Cdd:cd21245    87 DSPDEQSIMTYVAQF 101
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1904-1984 4.32e-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: 66.86  E-value: 4.32e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   1904 QGIPAGKAFTFTVLTHRA-KGHLEAKVVTPNNEVDTIDIVPIEDGeSYAMRFVPKETGNHFIHVTLDGAPMRESPFRLRV 1982
Cdd:smart00557   12 EKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDG-TYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ..
gi 392898139   1983 GG 1984
Cdd:smart00557   91 GP 92
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
 151-248 6.56e-13

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


Pssm-ID: 409168  Cd Length: 112  Bit Score: 66.95  E-value: 6.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  151 TPKQKLLNWIRNRLPGMP---ISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDLLKVAPLIA 227
Cdd:cd21319     5 SAKDALLLWCQMKTAGYPnvnVTNFTSSWKDGLAFNALIHKHRPD-LVDFGKLKKSNARHNLEHAFNVAERQLGITKLLD 83

                          90       100
                  ....*....|....*....|.
gi 392898139  228 PAEMIHPEIDEMSVMTYLSQF 248
Cdd:cd21319    84 PEDVFTENPDEKSIITYVVAF 104
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1351-1421 1.26e-12

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: 65.70  E-value: 1.26e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392898139   1351 KFNVRDLGYQPKDLEAIVMPPTQKKEVAEIIDNLDGTILVKYTPKVHGSHELSILQNGAQLQGTPIKFYVD 1421
Cdd:smart00557   21 EFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 153-248 2.20e-12

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: 65.52  E-value: 2.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNR---LPGMPISNFTSDWNDGVALGALVNSMAPgALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPA 229
Cdd:cd21192     5 EKALLKWVQAEigkYYGIRVTDFDKSWRDGVAFLALIHAIRP-DLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEVE 83

                          90
                  ....*....|....*....
gi 392898139  230 EMIHPEIDEMSVMTYLSQF 248
Cdd:cd21192    84 DVLVDKPDERSIMTYVSQF 102
Filamin pfam00630
Filamin/ABP280 repeat;
1903-1979 2.68e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 64.62  E-value: 2.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1903 GQGI---PAGKAFTFTVLTHRAKGHLEAKVVTPNNEVDTIDIVPIEDGeSYAMRFVPKETGNHFIHVTLDGAPMRESPFR 1979
Cdd:pfam00630   11 GPGLepgVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDG-TYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 151-250 3.23e-12

calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409103  Cd Length: 107  Bit Score: 64.87  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  151 TPKQKLLNWIRNRLP---GMPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAqDLLKVAPLIA 227
Cdd:cd21254     1 NASQSLLAWCKEVTKgyrGVKITNFTTSWRNGLAFCAILHHFRPD-LIDYKSLNPHDIKENNKKAYDGF-ASLGISRLLE 78

                          90       100
                  ....*....|....*....|....
gi 392898139  228 PAEMIHPEI-DEMSVMTYLSQFPA 250
Cdd:cd21254    79 PSDMVLLAVpDKLTVMTYLYQIRA 102
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
 153-248 3.87e-12

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: 64.65  E-value: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNRLP---GMPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPA 229
Cdd:cd21243     7 KKALLKWVQNAAAkrfGIEVKDFGPSWRDGVAFNAIIHSIRPD-LVDMESLKRRSNRENLETAFTVAEKELGIPRLLDPE 85

                          90
                  ....*....|....*....
gi 392898139  230 EMIHPEIDEMSVMTYLSQF 248
Cdd:cd21243    86 DVDVDKPDEKSIMTYVAQF 104
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 641-735 4.39e-12

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: 64.16  E-value: 4.39e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    641 PSATRVTGIDESKVYnVGEKIPFRVDTRLCGVDlVPKVEILDPELNPISYGAREITPGLFEYTLIPDAPIKHKIDVSVAG 720
Cdd:smart00557    1 ASKVKASGPGLEKGV-VGEPAEFTVDTRDAGGG-ELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 392898139    721 VSVPGAPFSVKVKEP 735
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 141-248 9.43e-12

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


Pssm-ID: 409171  Cd Length: 130  Bit Score: 64.30  E-value: 9.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  141 KREDGDNKE-ETPKQKLLNWIRNRLPGMP---ISNFTSDWNDGVALGALVNSMAPGALeDWENWSPNDALENTEKAMKSA 216
Cdd:cd21322     6 KIETEDNREtRSAKDALLLWCQMKTAGYPevnIQNFTTSWRDGLAFNALIHRHRPDLI-DFSKLTKSNATYNLQQAFNTA 84

                          90       100       110
                  ....*....|....*....|....*....|....
gi 392898139  217 QDLLKVAPLIAPAE--MIHPeiDEMSVMTYLSQF 248
Cdd:cd21322    85 EQHLGLTKLLDPEDvnMEAP--DEKSIITYVVSF 116
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 149-248 1.06e-11

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: 63.54  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  149 EETPKQKLLNWIRNRLPG---MPISNFTSDWNDGVALGALVNSMAPGALeDWENWSPNDALENTEKAMKSAQDLLKVAPL 225
Cdd:cd21216     8 ELSAKEGLLLWCQRKTAPyknVNVQNFHTSWKDGLAFCALIHRHRPDLL-DYDKLRKDDPRENLNLAFDVAEKHLDIPKM 86

                          90       100
                  ....*....|....*....|....
gi 392898139  226 IAPAEMIH-PEIDEMSVMTYLSQF 248
Cdd:cd21216    87 LDAEDIVNtPRPDERSVMTYVSCY 110
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
 153-242 1.16e-11

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


Pssm-ID: 409107  Cd Length: 111  Bit Score: 63.53  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNRLPG---MPISNFTSDWNDGVALGALVNSMAPGALeDWENWSPNDALENTEKAMKSAQDLLKVAPLIapa 229
Cdd:cd21258     3 KQMLLDWCRAKTRGyehVDIQNFSSSWSDGMAFCALVHNFFPDAF-DYSQLSPQNRRQNFEVAFSAAEMLADCVPLV--- 78

                          90
                  ....*....|...
gi 392898139  230 emihpEIDEMSVM 242
Cdd:cd21258    79 -----EVEDMMIM 86
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
 153-248 1.27e-11

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


Pssm-ID: 409045  Cd Length: 106  Bit Score: 63.14  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNR---LPGMPISNFTSDWNDGVALGALVNSMAPGALEDWEnWSPNDALENTEKAMKSAQDLLKVAPLIApA 229
Cdd:cd21196     5 QEELLRWCQEQtagYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSE-LQGLGALEATAWALKVAENELGITPVVS-A 82

                          90
                  ....*....|....*....
gi 392898139  230 EMIHPEIDEMSVMTYLSQF 248
Cdd:cd21196    83 QAVVAGSDPLGLIAYLSHF 101
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 153-248 3.90e-11

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: 61.64  E-value: 3.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNRLPGMP---ISNFTSDWNDGVALGALVNSMAPGALeDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPA 229
Cdd:cd21248     4 KDALLLWCQMKTAGYPnvnVRNFTTSWRDGLAFNALIHKHRPDLI-DYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPE 82

                          90       100
                  ....*....|....*....|.
gi 392898139  230 E--MIHPeiDEMSVMTYLSQF 248
Cdd:cd21248    83 DvnVEQP--DEKSIITYVVTY 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 153-248 4.23e-11

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: 61.59  E-value: 4.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNRL---PGMPISNFTSDWNDGVALGALVNSMAPGALEDW--ENWSPNDALENTEKAMKSAQDLLKVAPLIA 227
Cdd:cd00014     1 EEELLKWINEVLgeeLPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLPELDLF 80

                          90       100
                  ....*....|....*....|.
gi 392898139  228 PAEMIHPEIDEMSVMTYLSQF 248
Cdd:cd00014    81 EPEDLYEKGNLKKVLGTLWAL 101
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 154-250 8.73e-11

calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409104  Cd Length: 105  Bit Score: 60.57  E-value: 8.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  154 QKLLNW---IRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALeDWENWSPNDALENTEKAMKSAQDlLKVAPLIAPAE 230
Cdd:cd21255     4 QSLLEWcqeVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLV-DYESLDPLDIKENNKKAFEAFAS-LGVPRLLEPAD 81

                          90       100
                  ....*....|....*....|.
gi 392898139  231 MI-HPEIDEMSVMTYLSQFPA 250
Cdd:cd21255    82 MVlLPIPDKLIVMTYLCQLRA 102
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 156-248 9.07e-11

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: 60.52  E-value: 9.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  156 LLNWIRNRLPGMP---ISNFTSDWNDGVALGALVNSMAPgALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEMI 232
Cdd:cd21187     5 LLAWCRQSTRGYEqvdVKNFTTSWRDGLAFNALIHRHRP-DLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVN 83

                          90
                  ....*....|....*.
gi 392898139  233 HPEIDEMSVMTYLSQF 248
Cdd:cd21187    84 VEQPDKKSILMYVTSL 99
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 152-248 1.11e-10

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: 60.63  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  152 PKQKLLNWIRNR---LPGMPISNFTSDWNDGVALGALVNSMAPgALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAP 228
Cdd:cd21197     1 KIQALLRWCRRQcegYPGVNITNLTSSFRDGLAFCAILHRHRP-ELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDA 79

                          90       100
                  ....*....|....*....|.
gi 392898139  229 AEMIHPEI-DEMSVMTYLSQF 248
Cdd:cd21197    80 EDMVTMHVpDRLSIITYVSQY 100
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 153-248 1.14e-10

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: 60.77  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNRLPG---MPISNFTSDWNDGVALGALVNSMAPGALeDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPA 229
Cdd:cd21259     3 KQMLLDWCRAKTRGyenVDIQNFSSSWSDGMAFCALVHNFFPEAF-DYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVE 81

                          90       100
                  ....*....|....*....|
gi 392898139  230 EMIH-PEIDEMSVMTYLSQF 248
Cdd:cd21259    82 DMVRmREPDWKCVYTYIQEF 101
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 153-248 1.27e-10

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: 60.26  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNRLPG---MPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPA 229
Cdd:cd21249     6 KEALLIWCQRKTAGytnVNVQDFSRSWRDGLAFNALIHAHRPD-LIDYGSLRPDRPLYNLANAFLVAEQELGISQLLDPE 84

                          90
                  ....*....|....*....
gi 392898139  230 EMIHPEIDEMSVMTYLSQF 248
Cdd:cd21249    85 DVAVPHPDERSIMTYVSLY 103
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
 153-248 1.67e-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: 60.23  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNRLPG---MPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPA 229
Cdd:cd21244     7 RKALLLWAQEQCAKvgsISVTDFKSSWRNGLAFLAIIHALRPG-LVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEPE 85

                          90
                  ....*....|....*....
gi 392898139  230 EMIHPEIDEMSVMTYLSQF 248
Cdd:cd21244    86 DVDVVNPDEKSIMTYVAQF 104
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
 153-245 2.26e-10

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: 59.59  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNRLPG---MPISNFTSDWNDGVALGALVNSMAPGALeDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPA 229
Cdd:cd21261     3 KQILLEWCRSKTIGyknIDLQNFSSSWSDGMAFCALVHSFFPEAF-DYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVE 81

                          90
                  ....*....|....*...
gi 392898139  230 EMI--HPEIDEMSVMTYL 245
Cdd:cd21261    82 DMMvmGRKPDPMCVFTYV 99
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 151-253 1.00e-09

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


Pssm-ID: 409087  Cd Length: 106  Bit Score: 57.72  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  151 TPKQKLLNWIRNRL---PGMPISNFTSDWNDGVALGALVNSMAPgALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIA 227
Cdd:cd21238     2 TAKEKLLLWSQRMVegyQGLRCDNFTSSWRDGRLFNAIIHRHKP-MLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80

                          90       100
                  ....*....|....*....|....*.
gi 392898139  228 PAEMIHPEIDEMSVMTYLSQFPATKP 253
Cdd:cd21238    81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 36-131 1.07e-09

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: 57.98  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   36 VKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNV--GKFNKKVAFRSQKLENVSLALNFFQNEENIKiINIDSTHIV 113
Cdd:cd21222    25 VNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVplHEYHLTPSTDDEKLHNVKLALELMEDAGIST-PKIRPEDIV 103

                          90
                  ....*....|....*...
gi 392898139  114 DHNKKLILGLVWTLILHY 131
Cdd:cd21222   104 NGDLKSILRVLYSLFSKY 121
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 154-248 2.51e-09

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: 56.59  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  154 QKLLNWIRNRLPGMP---ISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAE 230
Cdd:cd21253     4 KALQQWCRQQTEGYRdvkVTNMTTSWRDGLAFCAIIHRFRPD-LIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAED 82

                          90
                  ....*....|....*....
gi 392898139  231 MIHPEI-DEMSVMTYLSQF 248
Cdd:cd21253    83 MVALKVpDKLSILTYVSQY 101
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
 153-248 7.36e-09

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: 55.48  E-value: 7.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  153 KQKLLNWIRNRLPG---MPISNFTSDWNDGVALGALVNSMAPGALeDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPA 229
Cdd:cd21260     3 KNMLLEWCRAKTRGyehVDIQNFSSSWSSGMAFCALIHKFFPDAF-DYAELDPANRRHNFTLAFSTAEKHADCAPLLEVE 81

                          90       100
                  ....*....|....*....|
gi 392898139  230 EMIHPEI-DEMSVMTYLSQF 248
Cdd:cd21260    82 DMVRMSVpDSKCVYTYIQEL 101
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 156-246 9.49e-09

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: 55.32  E-value: 9.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  156 LLNWIRNRL---PGMPISNFTSDWNDGVALGALVNSMAPGaLEDWEN-WSPNDALENTEKAMKSAQDLLKVAPLIAPAEM 231
Cdd:cd21233     5 LLSWVRQSTrnyPQVNVINFTSSWSDGLAFNALIHSHRPD-LFDWNSvVSQQSATERLDHAFNIARQHLGIEKLLDPEDV 83

                          90
                  ....*....|....*..
gi 392898139  232 --IHPeiDEMSVMTYLS 246
Cdd:cd21233    84 atAHP--DKKSILMYVT 98
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
 156-247 1.46e-08

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


Pssm-ID: 409048  Cd Length: 112  Bit Score: 54.67  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  156 LLNWIRNRL---PGMPISNFTSDWNDGVALGALVNSMAPGALEdWENWSPNDALENTEKAMKSAQDlLKVAPLIAPAEMI 232
Cdd:cd21199    13 LLKWCQEKTqgyKGIDITNFSSSWNDGLAFCALLHSYLPDKIP-YSELNPQDKRRNFTLAFKAAES-VGIPTTLTIDEMV 90

                          90
                  ....*....|....*.
gi 392898139  233 HPE-IDEMSVMTYLSQ 247
Cdd:cd21199    91 SMErPDWQSVMSYVTA 106
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 148-248 1.81e-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: 54.68  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  148 KEETPKQKLLNWIRNRLPGMP---ISNFTSDWNDGVALGALVNSMAPGALeDWENWSPNDALENTEKAMKSAQDLLKVAP 224
Cdd:cd21321     2 EKKSAKDALLLWCQMKTAGYPnvnVHNFTTSWRDGLAFNAIVHKHRPDLI-DFETLKKSNAHYNLQNAFNVAEKELGLTK 80

                          90       100
                  ....*....|....*....|....
gi 392898139  225 LIAPAEMIHPEIDEMSVMTYLSQF 248
Cdd:cd21321    81 LLDPEDVNVDQPDEKSIITYVATY 104
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 44-131 2.07e-08

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 54.21  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   44 GETIESLETDFSDGLkliALAQVLSHKNVGKFNKKVAFRS------QKLENVSLALNFFQnEENIKIINIDSTHIVDHNK 117
Cdd:cd21219    19 DPLINNLYEDLRDGL---VLLQVLDKIQPGCVNWKKVNKPkplnkfKKVENCNYAVDLAK-KLGFSLVGIGGKDIADGNR 94

                          90
                  ....*....|....
gi 392898139  118 KLILGLVWTLILHY 131
Cdd:cd21219    95 KLTLALVWQLMRYH 108
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
 155-248 2.77e-08

calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409044 [Multi-domain]  Cd Length: 110  Bit Score: 53.89  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  155 KLLNWIRNRLPG---MPISNFTSDWNDGVALGALVNSMAPgALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEM 231
Cdd:cd21195     8 KLLTWCQQQTEGyqhVNVTDLTTSWRSGLALCAIIHRFRP-ELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEM 86

                          90
                  ....*....|....*...
gi 392898139  232 IHP-EIDEMSVMTYLSQF 248
Cdd:cd21195    87 ASAqEPDKLSMVMYLSKF 104
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
 152-248 3.41e-08

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: 53.33  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  152 PKQKLLNWIRNR---LPGMPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAP 228
Cdd:cd21252     1 ARRALQAWCRRQcegYPGVEIRDLSSSFRDGLAFCAILHRHRPD-LIDFDSLSKDNVYENNRLAFEVAERELGIPALLDP 79

                          90       100
                  ....*....|....*....|.
gi 392898139  229 AEMIHPEI-DEMSVMTYLSQF 248
Cdd:cd21252    80 EDMVSMKVpDCLSIMTYVSQY 100
Filamin pfam00630
Filamin/ABP280 repeat;
1734-1787 3.45e-08

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 52.68  E-value: 3.45e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392898139  1734 DITARLMDPKGHTDDIEMRDLGQQYYQLKFTPKMEGIHTLSVMYKDAHVNGSPF 1787
Cdd:pfam00630   35 EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 32-127 3.77e-08

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: 53.81  E-value: 3.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   32 FTRWVKNHLQKAGET--IESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQnEENIKIINIDS 109
Cdd:cd21285    15 YTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLA-AKGINIQGLSA 93

                          90
                  ....*....|....*...
gi 392898139  110 THIVDHNKKLILGLVWTL 127
Cdd:cd21285    94 EEIRNGNLKAILGLFFSL 111
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 142-247 4.87e-08

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: 53.11  E-value: 4.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  142 REDGDNKeetpKQKLLNWIRNRLPGMP---ISNFTSDWNDGVALGALVNSMAPGALEdWENWSPNDALENTEKAMKSAQD 218
Cdd:cd21257     3 REYGGSK----RNALLKWCQKKTEGYPnidITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQDKKRNLLLAFQAAES 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 392898139  219 lLKVAPLIAPAEMIHPE-IDEMSVMTYLSQ 247
Cdd:cd21257    78 -VGIKPSLELSEMMYTDrPDWQSVMQYVAQ 106
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
 155-248 6.41e-08

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


Pssm-ID: 409100 [Multi-domain]  Cd Length: 111  Bit Score: 52.64  E-value: 6.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  155 KLLNWIRNRL---PGMPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEM 231
Cdd:cd21251     9 KLLGWCQRQTegyAGVNVTDLTMSWKSGLALCAIIHRYRPD-LIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEM 87

                          90
                  ....*....|....*...
gi 392898139  232 IH-PEIDEMSVMTYLSQF 248
Cdd:cd21251    88 ASvGEPDKLSMVMYLTQF 105
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 46-128 6.42e-08

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: 52.98  E-value: 6.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   46 TIESLETDFSDGLKLIALAQVLSHKNvgKFNKKVAF----RSQKLENVSLALNFFQN---EENIKIINIDSTHIVDHNKK 118
Cdd:cd21223    25 AVTNLAVDLRDGVRLCRLVELLTGDW--SLLSKLRVpaisRLQKLHNVEVALKALKEagvLRGGDGGGITAKDIVDGHRE 102

                          90
                  ....*....|
gi 392898139  119 LILGLVWTLI 128
Cdd:cd21223   103 KTLALLWRII 112
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
 155-248 7.95e-08

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


Pssm-ID: 409099 [Multi-domain]  Cd Length: 110  Bit Score: 52.58  E-value: 7.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  155 KLLNWIRNRLPG---MPISNFTSDWNDGVALGALVNSMAPgALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEM 231
Cdd:cd21250     8 KLLTWCQKQTEGyqnVNVTDLTTSWKSGLALCAIIHRFRP-ELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEM 86

                          90
                  ....*....|....*...
gi 392898139  232 IH-PEIDEMSVMTYLSQF 248
Cdd:cd21250    87 ASaEEPDKLSMVMYLSKF 104
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 32-127 9.06e-08

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: 52.34  E-value: 9.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   32 FTRWVKNHLQKAG--ETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFqNEENIKIINIDS 109
Cdd:cd21286     5 YTDWANHYLAKSGhkRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFL-AARGVNVQGLSA 83

                          90
                  ....*....|....*...
gi 392898139  110 THIVDHNKKLILGLVWTL 127
Cdd:cd21286    84 EEIRNGNLKAILGLFFSL 101
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 151-249 1.58e-07

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


Pssm-ID: 409089  Cd Length: 107  Bit Score: 51.58  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  151 TPKQKLLNW---IRNRLPGMPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQdLLKVAPLIA 227
Cdd:cd21240     4 SAKEKLLLWtqkVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPD-LVDMERVQIQSNRENLEQAFEVAE-RLGVTRLLD 81

                          90       100
                  ....*....|....*....|....*.
gi 392898139  228 PAEMIHPEIDEMSVMTYLSQ----FP 249
Cdd:cd21240    82 AEDVDVPSPDEKSVITYVSSiydaFP 107
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 150-248 2.46e-07

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


Pssm-ID: 409169  Cd Length: 108  Bit Score: 50.87  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  150 ETPKQKLLNWIRNRLPGMP---ISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDLLKVAPLI 226
Cdd:cd21320     1 KSAKDALLLWCQMKTAGYPnvnIHNFTTSWRDGMAFNALIHKHRPD-LIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLL 79

                          90       100
                  ....*....|....*....|..
gi 392898139  227 APAEMIHPEIDEMSVMTYLSQF 248
Cdd:cd21320    80 DPEDISVDHPDEKSIITYVVTY 101
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
 143-248 3.22e-07

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: 51.23  E-value: 3.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  143 EDGDNKEETPKQKLLNWIRNRLP---GMPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDL 219
Cdd:cd21288     2 QDISVEETSAKEGLLLWCQRKTApyrNVNIQNFHTSWKDGLGLCALIHRHRPD-LIDYSKLNKDDPIGNINLAMEIAEKH 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 392898139  220 LKVAPLIAPAEMIH-PEIDEMSVMTYLSQF 248
Cdd:cd21288    81 LDIPKMLDAEDIVNtPKPDERAIMTYVSCF 110
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 143-248 4.85e-07

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: 50.88  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  143 EDGDNKEETPKQKLLNWIRNRLP---GMPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDL 219
Cdd:cd21289     2 QDISVEETSAKEGLLLWCQRKTApyrNVNVQNFHTSWKDGLALCALIHRHRPD-LIDYAKLRKDDPIGNLNTAFEVAEKY 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 392898139  220 LKVAPLIAPAEMIH-PEIDEMSVMTYLSQF 248
Cdd:cd21289    81 LDIPKMLDAEDIVNtPKPDEKAIMTYVSCF 110
Filamin pfam00630
Filamin/ABP280 repeat;
1506-1595 5.46e-07

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 49.21  E-value: 5.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  1506 SPFRVLVMGEGQKRShlSVGSTSEVALpITQQELKGISASIKSPGGIEEPCFVRLLDGGRLGVSFTPREAGEHLITVKRD 1585
Cdd:pfam00630    3 DASKVKASGPGLEPG--VVGKPAEFTV-DTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 392898139  1586 GKLVPKAPFK 1595
Cdd:pfam00630   80 GQHIPGSPFK 89
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 47-135 8.00e-07

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: 49.93  E-value: 8.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   47 IESLETDFSDGLKLIALAQ------VLSHKNVGKFNKKVAFRsQKLENVSLALNFFQNEeNIKIINIDSTHIVDHNKKLI 120
Cdd:cd21298    24 VNHLYSDLRDGLVLLQLYDkikpgvVDWSRVNKPFKKLGANM-KKIENCNYAVELGKKL-KFSLVGIGGKDIYDGNRTLT 101

                          90
                  ....*....|....*
gi 392898139  121 LGLVWTLILHYSISM 135
Cdd:cd21298   102 LALVWQLMRAYTLSI 116
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
 142-246 1.47e-06

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: 49.30  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  142 REDGDNKeetpKQKLLNWIRNRLPGMP---ISNFTSDWNDGVALGALVNSMAPGALEdWENWSPNDALENTEKAMKSAQD 218
Cdd:cd21256     9 REYGGSK----RNALLKWCQKKTEGYQnidITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKRRNFTLAFQAAES 83

                          90       100
                  ....*....|....*....|....*....
gi 392898139  219 lLKVAPLIAPAEMIHPE-IDEMSVMTYLS 246
Cdd:cd21256    84 -VGIKSTLDINEMVRTErPDWQSVMTYVT 111
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 365-444 2.01e-06

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: 47.98  E-value: 2.01e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    365 KTAKVGDDVKFAV--VDAIEGPVEAIVVDPTGKEHRMVILDgTSPGEHSFEYKIPCIGLHSVNVFHKKLPLTGSPFPLRG 442
Cdd:smart00557   12 EKGVVGEPAEFTVdtRDAGGGELEVEVTGPSGKKVPVEVKD-NGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ..
gi 392898139    443 KP 444
Cdd:smart00557   91 GP 92
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 145-239 2.54e-06

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 48.45  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  145 GDNKEETPKQKLLNWI-----RNRLPGMPISNFTSDWNDGVALGALVNSMAPG---ALEDWENWSPNDALENTEKAMKSA 216
Cdd:cd21218     4 ESLLYLPPEEILLRWVnyhlkKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPElcdKELVLEVLSEEDLEKRAEKVLQAA 83

                          90       100
                  ....*....|....*....|...
gi 392898139  217 QDlLKVAPLIAPAEMIHPEIDEM 239
Cdd:cd21218    84 EK-LGCKYFLTPEDIVSGNPRLN 105
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 156-253 2.91e-06

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: 48.03  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  156 LLNWIRNR---LPGMPISNFTSDWNDGVALGALVNSMAPGALEdWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEMI 232
Cdd:cd21234     5 LLSWVRQStrpYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFS-WDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVA 83

                          90       100
                  ....*....|....*....|.
gi 392898139  233 HPEIDEMSVMTYLSQFPATKP 253
Cdd:cd21234    84 VQLPDKKSIIMYLTSLFEVLP 104
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 146-248 3.57e-06

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: 47.91  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  146 DNKEE--TPKQKLLNWIRNRLPG---MPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDLL 220
Cdd:cd21291     3 DINEEglTAKEGLLLWCQRKTAGydeVDVQDFTTSWTDGLAFCALIHRHRPD-LIDYDKLDKKDHRGNMQLAFDIASKEI 81

                          90       100
                  ....*....|....*....|....*....
gi 392898139  221 KVAPLIAPAEMIHPEI-DEMSVMTYLSQF 248
Cdd:cd21291    82 GIPQLLDVEDVCDVAKpDERSIMTYVAYY 110
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
 143-248 3.92e-06

second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409139  Cd Length: 125  Bit Score: 48.16  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  143 EDGDNKEETPKQKLLNWIRNRLP---GMPISNFTSDWNDGVALGALVNSMAPgALEDWENWSPNDALENTEKAMKSAQDL 219
Cdd:cd21290     5 QDISVEETSAKEGLLLWCQRKTApykNVNVQNFHISWKDGLAFNALIHRHRP-ELIEYDKLRKDDPVTNLNNAFEVAEKY 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 392898139  220 LKVAPLIAPAEMIH-PEIDEMSVMTYLSQF 248
Cdd:cd21290    84 LDIPKMLDAEDIVNtARPDEKAIMTYVSSF 113
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 151-249 5.75e-06

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


Pssm-ID: 409088  Cd Length: 104  Bit Score: 46.90  E-value: 5.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  151 TPKQKLLNWIRNRLPG---MPISNFTSDWNDGVALGALVNSMAPGaLEDWENWSPNDALENTEKAMKSAQDlLKVAPLIA 227
Cdd:cd21239     1 SAKERLLLWSQQMTEGytgIRCENFTTCWRDGRLFNAIIHKYRPD-LIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLD 78

                          90       100
                  ....*....|....*....|....*.
gi 392898139  228 PAEMIHPEIDEMSVMTYLSQ----FP 249
Cdd:cd21239    79 PEDVDVSSPDEKSVITYVSSlydvFP 104
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 152-248 1.24e-05

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: 45.92  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  152 PKQKLLNWIRNRLPG---MPISNFTSDWNDGVALGALVNSMAPGALEDWEnWSPNDALENTEKAMKSAQDLLKVAPLIAP 228
Cdd:cd21226     1 SEDGLLAWCRQTTEGydgVNITSFKSSFNDGRAFLALLHAYDPELFKQAA-IEQMDAEARLNLAFDFAEKKLGIPKLLEA 79

                          90       100
                  ....*....|....*....|
gi 392898139  229 AEMIHPEIDEMSVMTYLSQF 248
Cdd:cd21226    80 EDVMTGNPDERSIVLYTSLF 99
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 28-131 1.36e-05

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: 46.14  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   28 QQNTFTRWVKNHLQKAGET--IESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQNEEnIKII 105
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIrpVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKR-IRMH 79

                          90       100
                  ....*....|....*....|....*.
gi 392898139  106 NIDSTHIVDHNKKLILGLVWTLILHY 131
Cdd:cd21213    80 QTSAKDIVDGNLKAIMRLILALAAHF 105
Filamin pfam00630
Filamin/ABP280 repeat;
641-728 1.45e-05

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 45.36  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   641 PSATRVTGIDESKVYnVGEKIPFRVDTRlcGVDLVPKVEILDPELNPISYGAREITPGLFEYTLIPDAPIKHKIDVSVAG 720
Cdd:pfam00630    4 ASKVKASGPGLEPGV-VGKPAEFTVDTR--DAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 392898139   721 VSVPGAPF 728
Cdd:pfam00630   81 QHIPGSPF 88
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
 143-248 3.50e-05

second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409136  Cd Length: 124  Bit Score: 45.46  E-value: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139  143 EDGDNKEETPKQKLLNWIRNRLP---GMPISNFTSDWNDGVALGALVNSMAPgALEDWENWSPNDALENTEKAMKSAQDL 219
Cdd:cd21287     2 QDISVEETSAKEGLLLWCQRKTApykNVNIQNFHISWKDGLGFCALIHRHRP-ELIDYGKLRKDDPLTNLNTAFDVAEKY 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 392898139  220 LKVAPLIAPAEMI-HPEIDEMSVMTYLSQF 248
Cdd:cd21287    81 LDIPKMLDAEDIVgTARPDEKAIMTYVSSF 110
Filamin pfam00630
Filamin/ABP280 repeat;
1363-1417 1.03e-04

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 43.05  E-value: 1.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392898139  1363 DLEAIVMPPTQKKEVAEIIDNLDGTILVKYTPKVHGSHELSILQNGAQLQGTPIK 1417
Cdd:pfam00630   35 EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 34-127 1.24e-04

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: 43.44  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   34 RWVKNHLQKAGET---IESLETDFSDGLKLIAL-AQVLSHKNVGKFNKKVAFRSQKLENVSLALNffqneeNIKIIN--- 106
Cdd:cd21218    17 RWVNYHLKKAGPTkkrVTNFSSDLKDGEVYALLlHSLAPELCDKELVLEVLSEEDLEKRAEKVLQ------AAEKLGcky 90

                          90       100
                  ....*....|....*....|..
gi 392898139  107 -IDSTHIVDHNKKLILGLVWTL 127
Cdd:cd21218    91 fLTPEDIVSGNPRLNLAFVATL 112
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 36-131 2.99e-04

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


Pssm-ID: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 42.72  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   36 VKNHLQKAGETIESLETDFSDGLKLIALAQVLS--HKNVGKFNKKVAFRSQKLENVSLALNFFQnEENIKIINIDSTHIV 113
Cdd:cd21307    25 VNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEgfFIHLSEFFLTPSSTSEMLHNVTLALELLK-EGGLLNFPVNPEDIV 103

                          90
                  ....*....|....*...
gi 392898139  114 DHNKKLILGLVWTLILHY 131
Cdd:cd21307   104 NGDSKATIRVLYCLFSKY 121
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 32-128 3.56e-04

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 42.18  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   32 FTRWVKNHLQK----AGETIESLETD-----FSDGL---KLIALAQVLS--HKNVGKFNKKVAFrsQKLENVSLALNFfQ 97
Cdd:cd21217     6 FVEHINSLLADdpdlKHLLPIDPDGDdlfeaLRDGVllcKLINKIVPGTidERKLNKKKPKNIF--EATENLNLALNA-A 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 392898139   98 NEENIKIINIDSTHIVDHNKKLILGLVWTLI 128
Cdd:cd21217    83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 21-135 4.65e-04

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 42.28  E-value: 4.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   21 DAEWKIIQ-----QNTFTRWVkNHLqKAGETIESLETDFSDGLKLIALAQVLSHK-NVGKFNK----KVAFRSQKLENVS 90
Cdd:cd21330     2 DIDWSSIEgetreERTFRNWM-NSL-GVNPRVNHLYSDLSDALVIFQLYEKIKVPvDWNRVNKppypKLGENMKKLENCN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 392898139   91 LALNFFQNEENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISM 135
Cdd:cd21330    80 YAVELGKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNI 124
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 15-135 4.72e-04

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 42.29  E-value: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   15 PAIR---HDDAEWKIIQ-----QNTFTRWVKNhlQKAGETIESLETDFSDGLKLIALAQVLSHK-NVGKFNK----KVAF 81
Cdd:cd21331     2 PALTkpeNQDIDWTLLEgetreERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIKVPvDWNKVNKppypKLGA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392898139   82 RSQKLENVSLALNFFQNEENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISM 135
Cdd:cd21331    80 NMKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNV 133
Filamin pfam00630
Filamin/ABP280 repeat;
365-438 8.00e-04

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 40.35  E-value: 8.00e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392898139   365 KTAKVGDDVKFAV--VDAiEGPVEAIVVDPTGKEHRMVILDgTSPGEHSFEYKIPCIGLHSVNVFHKKLPLTGSPF 438
Cdd:pfam00630   15 EPGVVGKPAEFTVdtRDA-GGEGEVEVTGPDGSPVPVEVTD-NGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 28-135 2.00e-03

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 39.97  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139   28 QQNTFTRWVkNHLqKAGETIESLETDFSDGLKLIALAQVLSHK-NVGKFNKK----VAFRSQKLENVSLALNFFQNEENI 102
Cdd:cd21329     7 EERTFRNWM-NSL-GVNPYVNHLYSDLCDALVIFQLYEMTRVPvDWGHVNKPpypaLGGNMKKIENCNYAVELGKNKAKF 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 392898139  103 KIINIDSTHIVDHNKKLILGLVWTLILHYSISM 135
Cdd:cd21329    85 SLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNV 117
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 259-356 5.06e-03

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: 38.35  E-value: 5.06e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898139    259 KVQATISNLDKIlQVNDPREFDLKLSRDGF-KPKVSIRDEDGQDIHLSLKKVEDkeNAYKVKFTPTKIGFIHVDVAANDV 337
Cdd:smart00557    3 KVKASGPGLEKG-VVGEPAEFTVDTRDAGGgELEVEVTGPSGKKVPVEVKDNGD--GTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....*....
gi 392898139    338 HtfetqtIPEASVICQVVP 356
Cdd:smart00557   80 H------IPGSPFTVKVGP 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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