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Conserved domains on  [gi|190192186|dbj|BAG48307|]
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filamin A [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 129-242 1.93e-80

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: 260.51  E-value: 1.93e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  129 DEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDW 208
Cdd:cd21312     1 DEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDW 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 190192186  209 LGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKL 242
Cdd:cd21312    81 LGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKL 114
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 1-126 1.28e-79

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: 258.48  E-value: 1.28e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    1 MPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENV 80
Cdd:cd21308     4 MPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 190192186   81 SVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 126
Cdd:cd21308    84 SVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 129
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1421-1515 9.69e-33

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 123.10  E-value: 9.69e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1421 ASKVKCSGPGLSPGMVraNLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVLYGD 1500
Cdd:smart00557    1 ASKVKASGPGLEKGVV--GEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 190192186   1501 EEVPRSPFKVKVLPT 1515
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2012-2101 1.70e-32

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 122.33  E-value: 1.70e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2012 ASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPS--KVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQH 2089
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 190192186   2090 VPGSPFSVKVTG 2101
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1833-1919 8.37e-32

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 120.40  E-value: 8.37e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1833 VTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPS--KAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPG 1910
Cdd:smart00557    4 VKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83


                    ....*....
gi 190192186   1911 SPFTARVTG 1919
Cdd:smart00557   84 SPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 645-739 1.61e-31

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 119.63  E-value: 1.61e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    645 PDRVKARGPGLEKTgvAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGG 724
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 190192186    725 VSIPNSPFRVNVGAG 739
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2203-2293 8.45e-31

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 117.70  E-value: 8.45e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2203 AHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPS--KAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEH 2280
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 190192186   2281 IPDSPFVVPVASP 2293
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1133-1225 2.85e-30

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 116.16  E-value: 2.85e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1133 ASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQP 1212
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 190192186   1213 VPNFPSKLQVEPA 1225
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1615-1708 3.92e-29

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 112.70  E-value: 3.92e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1615 ASKCTVTGAGIGPTIqIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGE 1694
Cdd:smart00557    1 ASKVKASGPGLEKGV-VGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 190192186   1695 HVPNSPFQVTALAG 1708
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 354-450 5.05e-29

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 112.31  E-value: 5.05e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    354 ASKVTAQGPGLEPSgnIANKTTYFEIFTAGAGTGEVEVVIQDPMGQKgtVEPQLEARGDSTYRCSYQPTMEGVHTVHVTF 433
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 190192186    434 AGVPIPRSPYTVTVGQA 450
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1040-1129 5.56e-29

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 112.31  E-value: 5.56e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1040 PSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLTVEGP--CEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTH 1117
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 190192186   1118 IPGSPFKAHVVP 1129
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1518-1612 2.76e-28

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 110.39  E-value: 2.76e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1518 ASKVKASGPGLNttGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGG 1597
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 190192186   1598 DEIPFSPYRVRAVPT 1612
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 453-544 4.86e-28

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 109.62  E-value: 4.86e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    453 PSACRAVGRGLQPKgvRVKETADFKVYTKGAGSGELKVTVKGPKG-EERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGG 531
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|...
gi 190192186    532 QNIGRSPFEVKVG 544
Cdd:smart00557   79 EHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2394-2484 3.74e-26

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 104.22  E-value: 3.74e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2394 PGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAGALSVTIDGPS--KVKMDCQECPEG-YRVTYTPMAPGSYLISIKYGGpY 2470
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGG-E 79

                            90
                    ....*....|....
gi 190192186   2471 HIGGSPFKAKVTGP 2484
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2522-2611 1.03e-25

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 103.07  E-value: 1.03e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2522 ASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEH 2601
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 190192186   2602 IPGSPYRVVV 2611
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 254-348 2.44e-25

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 101.91  E-value: 2.44e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    254 PKKARAYGPGIEPTgnMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDknRTFSVWYVPEVTGTHKVTVLF 333
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGD--GTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*
gi 190192186    334 AGQHIAKSPFEVYVD 348
Cdd:smart00557   77 GGEHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1229-1325 1.36e-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: 1.36e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1229 SGVQCYGPGIEGQGVFReaTTEFSVDARaltQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSVDVTY 1308
Cdd:smart00557    2 SKVKASGPGLEKGVVGE--PAEFTVDTR---DAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 190192186   1309 DGSPVPSSPFQVPVTEG 1325
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 845-941 1.49e-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: 99.60  E-value: 1.49e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    845 ASKVKAEGPGLSRTGVelGKPTHFTVNAKAAGKGKLDVQFSGLTKGDAvrDVDIIDHHDNTYTVKYTPVQQGPVGVNVTY 924
Cdd:smart00557    1 ASKVKASGPGLEKGVV--GEPAEFTVDTRDAGGGELEVEVTGPSGKKV--PVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 190192186    925 GGDPIPKSPFSVAVSPS 941
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1328-1415 1.46e-23

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 96.90  E-value: 1.46e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1328 PSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPS--EAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQ 1405
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 190192186   1406 VPGSPFKVPV 1415
Cdd:smart00557   81 IPGSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 550-632 6.67e-23

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 94.98  E-value: 6.67e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    550 QKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECD--DKGDGSCDVRYWPQEAGEYAVHVLCNSEDI 627
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEvkDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81


                    ....*
gi 190192186    628 RLSPF 632
Cdd:smart00557   82 PGSPF 86
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 742-842 4.36e-22

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 92.67  E-value: 4.36e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    742 PNKVKVYGPGVAKTglKAHEPTYFTVDCAEAGQGDVSIGikcapgVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTI 821
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVE------VTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTV 72

                            90       100
                    ....*....|....*....|.
gi 190192186    822 MVLFADQATPTSPIRVKVEPS 842
Cdd:smart00557   73 TVKFGGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 945-1037 2.87e-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: 2.87e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    945 SKIKVSGLG-EKVDVGKDQEFTVKSKGAGGqGKVASKIVGPSGAAVPCKVEPgLGADNSVVRFLPREEGPYEVEVTYDGV 1023
Cdd:smart00557    2 SKVKASGPGlEKGVVGEPAEFTVDTRDAGG-GELEVEVTGPSGKKVPVEVKD-NGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 190192186   1024 PVPGSPFPLEAVAP 1037
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2297-2388 1.04e-20

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 88.81  E-value: 1.04e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2297 ARRLTVSSLQESGLKVNQPASFAVSLNGA-KGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTH 2375
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 190192186   2376 IPGSPFKIRVGEP 2388
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1762-1826 9.05e-16

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 74.56  E-value: 9.05e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1762 FTIK-----KGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYVD 1826
Cdd:smart00557   22 FTVDtrdagGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
 
Name Accession Description Interval E-value
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 129-242 1.93e-80

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: 260.51  E-value: 1.93e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  129 DEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDW 208
Cdd:cd21312     1 DEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDW 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 190192186  209 LGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKL 242
Cdd:cd21312    81 LGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKL 114
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 1-126 1.28e-79

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: 258.48  E-value: 1.28e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    1 MPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENV 80
Cdd:cd21308     4 MPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 190192186   81 SVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 126
Cdd:cd21308    84 SVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 129
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1421-1515 9.69e-33

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 123.10  E-value: 9.69e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1421 ASKVKCSGPGLSPGMVraNLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVLYGD 1500
Cdd:smart00557    1 ASKVKASGPGLEKGVV--GEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 190192186   1501 EEVPRSPFKVKVLPT 1515
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2012-2101 1.70e-32

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 122.33  E-value: 1.70e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2012 ASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPS--KVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQH 2089
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 190192186   2090 VPGSPFSVKVTG 2101
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1833-1919 8.37e-32

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 120.40  E-value: 8.37e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1833 VTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPS--KAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPG 1910
Cdd:smart00557    4 VKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83


                    ....*....
gi 190192186   1911 SPFTARVTG 1919
Cdd:smart00557   84 SPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 645-739 1.61e-31

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 119.63  E-value: 1.61e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    645 PDRVKARGPGLEKTgvAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGG 724
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 190192186    725 VSIPNSPFRVNVGAG 739
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
14-240 2.11e-31

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 133.14  E-value: 2.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   14 WKKIQQNTFTRWCNEHL-KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkHNQRPTFRQMQLENVSVALEFLDRESI 92
Cdd:COG5069     6 WQKVQKKTFTKWTNEKLiSGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGE-YNETPETRIHVMENVSGRLEFIKGKGV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   93 KLVSIDSKAIVDGNLKLILGLIWTLILHYSISmpmwdeeEDEEAKKQTPKQRLLGW----IQNKLPQLPITNFSRDWQSG 168
Cdd:COG5069    85 KLFNIGPQDIVDGNPKLILGLIWSLISRLTIA-------TINEEGELTKHINLLLWcdedTGGYKPEVDTFDFFRSWRDG 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190192186  169 RALGALVDSCAP-GLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVDPNV-DEHSVMTYLSQFPKA 240
Cdd:COG5069   158 LAFSALIHDSRPdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSWYIIR 231
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2203-2293 8.45e-31

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 117.70  E-value: 8.45e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2203 AHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPS--KAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEH 2280
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 190192186   2281 IPDSPFVVPVASP 2293
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1133-1225 2.85e-30

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 116.16  E-value: 2.85e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1133 ASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQP 1212
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 190192186   1213 VPNFPSKLQVEPA 1225
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1615-1708 3.92e-29

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 112.70  E-value: 3.92e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1615 ASKCTVTGAGIGPTIqIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGE 1694
Cdd:smart00557    1 ASKVKASGPGLEKGV-VGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 190192186   1695 HVPNSPFQVTALAG 1708
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 354-450 5.05e-29

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 112.31  E-value: 5.05e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    354 ASKVTAQGPGLEPSgnIANKTTYFEIFTAGAGTGEVEVVIQDPMGQKgtVEPQLEARGDSTYRCSYQPTMEGVHTVHVTF 433
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 190192186    434 AGVPIPRSPYTVTVGQA 450
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1040-1129 5.56e-29

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 112.31  E-value: 5.56e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1040 PSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLTVEGP--CEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTH 1117
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 190192186   1118 IPGSPFKAHVVP 1129
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1518-1612 2.76e-28

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 110.39  E-value: 2.76e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1518 ASKVKASGPGLNttGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGG 1597
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 190192186   1598 DEIPFSPYRVRAVPT 1612
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 453-544 4.86e-28

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 109.62  E-value: 4.86e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    453 PSACRAVGRGLQPKgvRVKETADFKVYTKGAGSGELKVTVKGPKG-EERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGG 531
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|...
gi 190192186    532 QNIGRSPFEVKVG 544
Cdd:smart00557   79 EHIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2394-2484 3.74e-26

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 104.22  E-value: 3.74e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2394 PGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAGALSVTIDGPS--KVKMDCQECPEG-YRVTYTPMAPGSYLISIKYGGpY 2470
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGG-E 79

                            90
                    ....*....|....
gi 190192186   2471 HIGGSPFKAKVTGP 2484
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1418-1509 8.85e-26

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 103.14  E-value: 8.85e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1418 VTDASKVKCSGPGLSPGmvRANLPQSFQVDTSKAGvAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVL 1497
Cdd:pfam00630    1 AADASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 190192186  1498 YGDEEVPRSPFK 1509
Cdd:pfam00630   78 FNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2522-2611 1.03e-25

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 103.07  E-value: 1.03e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2522 ASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEH 2601
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 190192186   2602 IPGSPYRVVV 2611
Cdd:smart00557   81 IPGSPFTVKV 90
Filamin pfam00630
Filamin/ABP280 repeat;
1833-1914 1.60e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 102.37  E-value: 1.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1833 VTAYGPGLTHGVVNKPATFTVNTKDAGeGGLSLAIEGPS--KAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPG 1910
Cdd:pfam00630    7 VKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPG 85


                   ....
gi 190192186  1911 SPFT 1914
Cdd:pfam00630   86 SPFK 89
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 20-120 2.26e-25

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: 102.39  E-value: 2.26e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186     20 NTFTRWCNEHLKC-VSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSID 98
Cdd:smart00033    1 KTLLRWVNSLLAEyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 190192186     99 SKAIVDGNlKLILGLIWTLILH 120
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 254-348 2.44e-25

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 101.91  E-value: 2.44e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    254 PKKARAYGPGIEPTgnMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDknRTFSVWYVPEVTGTHKVTVLF 333
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGD--GTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*
gi 190192186    334 AGQHIAKSPFEVYVD 348
Cdd:smart00557   77 GGEHIPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
2010-2095 9.39e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 100.06  E-value: 9.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  2010 GDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGyGGLSLSIEGPS--KVDINTEDLEDGTCRVTYCPTEPGNYIINIKFAD 2087
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 190192186  2088 QHVPGSPF 2095
Cdd:pfam00630   81 QHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1229-1325 1.36e-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: 1.36e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1229 SGVQCYGPGIEGQGVFReaTTEFSVDARaltQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSVDVTY 1308
Cdd:smart00557    2 SKVKASGPGLEKGVVGE--PAEFTVDTR---DAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 190192186   1309 DGSPVPSSPFQVPVTEG 1325
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 845-941 1.49e-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: 99.60  E-value: 1.49e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    845 ASKVKAEGPGLSRTGVelGKPTHFTVNAKAAGKGKLDVQFSGLTKGDAvrDVDIIDHHDNTYTVKYTPVQQGPVGVNVTY 924
Cdd:smart00557    1 ASKVKASGPGLEKGVV--GEPAEFTVDTRDAGGGELEVEVTGPSGKKV--PVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 190192186    925 GGDPIPKSPFSVAVSPS 941
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1131-1217 5.73e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 97.74  E-value: 5.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1131 FDASKVKCSGPGLERATAGEVGQFQVDCSSAGSaELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGG 1210
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*..
gi 190192186  1211 QPVPNFP 1217
Cdd:pfam00630   81 QHIPGSP 87
Filamin pfam00630
Filamin/ABP280 repeat;
1517-1606 7.38e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 97.74  E-value: 7.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1517 DASKVKASGPGLNttGVPASLPVEFTIDAKDAGeGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYG 1596
Cdd:pfam00630    3 DASKVKASGPGLE--PGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 190192186  1597 GDEIPFSPYR 1606
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
352-444 1.14e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.97  E-value: 1.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   352 GDASKVTAQGPGLEPSgnIANKTTYFEIFTAGAGtGEVEVVIQDPMGQKgtVEPQLEARGDSTYRCSYQPTMEGVHTVHV 431
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSP--VPVEVTDNGDGTYTVSYTPTEPGDYTVSV 76

                           90
                   ....*....|...
gi 190192186   432 TFAGVPIPRSPYT 444
Cdd:pfam00630   77 KFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1037-1124 1.28e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.97  E-value: 1.28e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1037 PTKPSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLtVEGP--CEAQLECLDNGDGTCSVSYVPTEPGDYNINILFA 1114
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVE-VTGPdgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 190192186  1115 DTHIPGSPFK 1124
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1328-1415 1.46e-23

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 96.90  E-value: 1.46e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1328 PSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPS--EAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQ 1405
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 190192186   1406 VPGSPFKVPV 1415
Cdd:smart00557   81 IPGSPFTVKV 90
Filamin pfam00630
Filamin/ABP280 repeat;
1613-1701 1.62e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.59  E-value: 1.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1613 GDASKCTVTGAGIGPTiQIGEETVITVDTKAAGkGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFG 1692
Cdd:pfam00630    2 ADASKVKASGPGLEPG-VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*....
gi 190192186  1693 GEHVPNSPF 1701
Cdd:pfam00630   80 GQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
643-733 1.84e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.59  E-value: 1.84e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   643 FHPDRVKARGPGLEktGVAVNKPAEFTVDAKhGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSW 722
Cdd:pfam00630    2 ADASKVKASGPGLE--PGVVGKPAEFTVDTR-DAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 190192186   723 GGVSIPNSPFR 733
Cdd:pfam00630   79 NGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2201-2287 1.86e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.59  E-value: 1.86e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  2201 GGAHKVRAGGPGLERAEAGVPAEFSIWTREAGaGGLAIAVEGPS--KAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNE 2278
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 190192186  2279 EHIPDSPFV 2287
Cdd:pfam00630   81 QHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 550-632 6.67e-23

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 94.98  E-value: 6.67e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    550 QKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECD--DKGDGSCDVRYWPQEAGEYAVHVLCNSEDI 627
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEvkDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81


                    ....*
gi 190192186    628 RLSPF 632
Cdd:smart00557   82 PGSPF 86
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 742-842 4.36e-22

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 92.67  E-value: 4.36e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    742 PNKVKVYGPGVAKTglKAHEPTYFTVDCAEAGQGDVSIGikcapgVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTI 821
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVE------VTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTV 72

                            90       100
                    ....*....|....*....|.
gi 190192186    822 MVLFADQATPTSPIRVKVEPS 842
Cdd:smart00557   73 TVKFGGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 945-1037 2.87e-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: 2.87e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    945 SKIKVSGLG-EKVDVGKDQEFTVKSKGAGGqGKVASKIVGPSGAAVPCKVEPgLGADNSVVRFLPREEGPYEVEVTYDGV 1023
Cdd:smart00557    2 SKVKASGPGlEKGVVGEPAEFTVDTRDAGG-GELEVEVTGPSGKKVPVEVKD-NGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 190192186   1024 PVPGSPFPLEAVAP 1037
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 16-123 3.85e-21

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: 90.42  E-value: 3.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    16 KIQQNTFTRWCNEHLKC--VSKRIANLQTDLSDGLRLIALLEVLSQKKmhRKHNQRPTFRQMQLENVSVALEFLDRE-SI 92
Cdd:pfam00307    1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGL--VDKKKLNKSEFDKLENINLALDVAEKKlGV 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 190192186    93 KLVSIDSKAIVDGNLKLILGLIWTLILHYSI 123
Cdd:pfam00307   79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2297-2388 1.04e-20

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 88.81  E-value: 1.04e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2297 ARRLTVSSLQESGLKVNQPASFAVSLNGA-KGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTH 2375
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 190192186   2376 IPGSPFKIRVGEP 2388
Cdd:smart00557   81 IPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
941-1030 1.97e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 87.73  E-value: 1.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   941 SLDLSKIKVSGLG-EKVDVGKDQEFTVKSKGAGGQGKVasKIVGPSGAAVPCKVEPgLGADNSVVRFLPREEGPYEVEVT 1019
Cdd:pfam00630    1 AADASKVKASGPGlEPGVVGKPAEFTVDTRDAGGEGEV--EVTGPDGSPVPVEVTD-NGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 190192186  1020 YDGVPVPGSPF 1030
Cdd:pfam00630   78 FNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
844-934 3.70e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.96  E-value: 3.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   844 DASKVKAEGPGLSRtgVELGKPTHFTVNAKAAGkGKLDVQFSGlTKGDAVrDVDIIDHHDNTYTVKYTPVQQGPVGVNVT 923
Cdd:pfam00630    3 DASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTG-PDGSPV-PVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 190192186   924 YGGDPIPKSPF 934
Cdd:pfam00630   78 FNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
253-344 4.96e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.57  E-value: 4.96e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   253 NPKKARAYGPGIEPTgnMVKKRAEFTVETRSAGqGEVLVYVEDPAGHQEEAKVTANNDknRTFSVWYVPEVTGTHKVTVL 332
Cdd:pfam00630    3 DASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGD--GTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 190192186   333 FAGQHIAKSPFE 344
Cdd:pfam00630   78 FNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
450-540 1.76e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.03  E-value: 1.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   450 ACNPSACRAVGRGLQPkgVRVKETADFKVYTKGAGsGELKVTVKGPKG-EERVKQKDLGDGVYGFEYYPMVPGTYIVTIT 528
Cdd:pfam00630    1 AADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 190192186   529 WGGQNIGRSPFE 540
Cdd:pfam00630   78 FNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2392-2478 1.96e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.03  E-value: 1.96e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  2392 GDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGaGALSVTIDGPS--KVKMDCQECPEG-YRVTYTPMAPGSYLISIKYGG 2468
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFNG 80

                           90
                   ....*....|
gi 190192186  2469 pYHIGGSPFK 2478
Cdd:pfam00630   81 -QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
550-632 2.03e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.03  E-value: 2.03e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   550 QKVRAWGPGLEGGVVGKSADFVVEAiGDDVGTLGFSVEGPS--QAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDI 627
Cdd:pfam00630    5 SKVKASGPGLEPGVVGKPAEFTVDT-RDAGGEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHI 83


                   ....*
gi 190192186   628 RLSPF 632
Cdd:pfam00630   84 PGSPF 88
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 145-237 5.51e-19

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 84.29  E-value: 5.51e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    145 LLGWIQNKL---PQLPITNFSRDWQSGRALGALVDSCAPGLCPDWD---SWDASKPVTNAREAMQQADDWLGIPQVITPE 218
Cdd:smart00033    3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90
                    ....*....|....*....
gi 190192186    219 EIVDPNVDEHSVMTYLSQF 237
Cdd:smart00033   83 DLVEGPKLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
2519-2608 6.54e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 83.49  E-value: 6.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  2519 PADASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNmLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWG 2598
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGE-GEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 190192186  2599 DEHIPGSPYR 2608
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2294-2382 1.41e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 82.72  E-value: 1.41e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  2294 SGDARRLTVSSLQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNG 2373
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 190192186  2374 THIPGSPFK 2382
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1326-1412 2.19e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 81.95  E-value: 2.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1326 CDPSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLaVEGPSEAKMSCM--DNKDGSCSVEYIPYEAGTYSLNVTYGG 1403
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVE-VTGPDGSPVPVEvtDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 190192186  1404 HQVPGSPFK 1412
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1225-1318 2.87e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 81.57  E-value: 2.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1225 AVDTSGVQCYGPGIEGQGVFREAttEFSVDARalTQTGGPHVKarVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSV 1304
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPA--EFTVDTR--DAGGEGEVE--VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTV 74

                           90
                   ....*....|....
gi 190192186  1305 DVTYDGSPVPSSPF 1318
Cdd:pfam00630   75 SVKFNGQHIPGSPF 88
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 139-237 7.54e-17

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: 78.48  E-value: 7.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   139 QTPKQRLLGWIQNKL----PQLPITNFSRDWQSGRALGALVDSCAPGLCPDWD-SWDASKPVTNAREAMQQADDWLGIPQ 213
Cdd:pfam00307    1 LELEKELLRWINSHLaeygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKLGVPK 80

                           90       100
                   ....*....|....*....|....*
gi 190192186   214 V-ITPEEIVDPnvDEHSVMTYLSQF 237
Cdd:pfam00307   81 VlIEPEDLVEG--DNKSVLTYLASL 103
Filamin pfam00630
Filamin/ABP280 repeat;
740-836 6.20e-16

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 75.02  E-value: 6.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   740 SHPNKVKVYGPGVAKTglKAHEPTYFTVDCAEA-GQGDVSIgikcapgvVGPAEADIDFDIIRNDNDTFTVKYTPRGAGS 818
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAgGEGEVEV--------TGPDGSPVPVEVTDNGDGTYTVSYTPTEPGD 71

                           90
                   ....*....|....*...
gi 190192186   819 YTIMVLFADQATPTSPIR 836
Cdd:pfam00630   72 YTVSVKFNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1762-1826 9.05e-16

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 74.56  E-value: 9.05e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1762 FTIK-----KGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYVD 1826
Cdd:smart00557   22 FTVDtrdagGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
1762-1820 1.15e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 63.08  E-value: 1.15e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190192186  1762 FTI----KKGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSP 1820
Cdd:pfam00630   25 FTVdtrdAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSP 87
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
22-118 4.12e-03

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 42.62  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   22 FTRWCNEHLkcVSKRIANLQTDLSDGLRliaLLEVLSQKKM-----HRKHNQRPT-----FRQMQLENVSVALEFLDRES 91
Cdd:COG5069   384 FTFWLNSLD--VSPEITNLFGDLRDQLI---LLQALSKKLMpmtvtHKLVKKQPAsgieeNRFKAFENENYAVDLGITEG 458

                          90       100
                  ....*....|....*....|....*..
gi 190192186   92 IKLVSIDSKAIVDGNlKLILGLIWTLI 118
Cdd:COG5069   459 FSLVGIKGLEILDGI-RLKLTLVWQVL 484
 
Name Accession Description Interval E-value
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 129-242 1.93e-80

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: 260.51  E-value: 1.93e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  129 DEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDW 208
Cdd:cd21312     1 DEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDW 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 190192186  209 LGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKL 242
Cdd:cd21312    81 LGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKL 114
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 1-126 1.28e-79

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: 258.48  E-value: 1.28e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    1 MPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENV 80
Cdd:cd21308     4 MPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 190192186   81 SVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 126
Cdd:cd21308    84 SVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 129
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 1-128 1.27e-78

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: 255.78  E-value: 1.27e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    1 MPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENV 80
Cdd:cd21309     1 MPVTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFRQMQLENV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 190192186   81 SVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMW 128
Cdd:cd21309    81 SVALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISMPVW 128
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 136-244 3.35e-77

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: 251.14  E-value: 3.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  136 AKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVI 215
Cdd:cd21314     7 ARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPVQNAREAMQQADDWLGVPQVI 86

                          90       100
                  ....*....|....*....|....*....
gi 190192186  216 TPEEIVDPNVDEHSVMTYLSQFPKAKLKP 244
Cdd:cd21314    87 APEEIVDPNVDEHSVMTYLSQFPKAKLKP 115
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 2-126 3.67e-77

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: 251.49  E-value: 3.67e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    2 PATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVS 81
Cdd:cd21310     1 PATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQMKLENVS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 190192186   82 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 126
Cdd:cd21310    81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 125
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 140-242 1.47e-72

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: 237.28  E-value: 1.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  140 TPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEE 219
Cdd:cd21230     1 TPKQRLLGWIQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALENATEAMQLAEDWLGVPQLITPEE 80

                          90       100
                  ....*....|....*....|...
gi 190192186  220 IVDPNVDEHSVMTYLSQFPKAKL 242
Cdd:cd21230    81 IINPNVDEMSVMTYLSQFPKAKL 103
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 14-121 1.20e-71

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


Pssm-ID: 409077  Cd Length: 108  Bit Score: 235.08  E-value: 1.20e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   14 WKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIK 93
Cdd:cd21228     1 WKKIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRPTFRQMKLENVSVALEFLERESIK 80

                          90       100
                  ....*....|....*....|....*...
gi 190192186   94 LVSIDSKAIVDGNLKLILGLIWTLILHY 121
Cdd:cd21228    81 LVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 3-126 1.19e-70

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: 232.73  E-value: 1.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    3 ATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQLENVSV 82
Cdd:cd21311     1 AAERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKF-PKFNKRPTFRSQKLENVSV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 190192186   83 ALEFL-DRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMP 126
Cdd:cd21311    80 ALKFLeEDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSISMP 124
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
 136-242 5.64e-70

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: 230.36  E-value: 5.64e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  136 AKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVI 215
Cdd:cd21313     4 AKKQTPKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPQKPVDNAREAMQQADDWLGVPQVI 83

                          90       100
                  ....*....|....*....|....*..
gi 190192186  216 TPEEIVDPNVDEHSVMTYLSQFPKAKL 242
Cdd:cd21313    84 TPEEIIHPDVDEHSVMTYLSQFPKAKL 110
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 14-121 1.40e-62

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: 208.87  E-value: 1.40e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   14 WKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIK 93
Cdd:cd21183     1 WKRIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYNRRPAFQQHYLENVSTALKFIEADHIK 80

                          90       100
                  ....*....|....*....|....*...
gi 190192186   94 LVSIDSKAIVDGNLKLILGLIWTLILHY 121
Cdd:cd21183    81 LVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 127-242 4.27e-59

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: 199.24  E-value: 4.27e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  127 MWD--EEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQ 204
Cdd:cd21315     1 MWEgeDDGPDDGKGPTPKQRLLGWIQSKVPDLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAVKNAKEAMDL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 190192186  205 ADDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKL 242
Cdd:cd21315    81 AEDWLDVPQLIKPEEMVNPKVDELSMMTYLSQFPNAKL 118
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 140-241 7.26e-49

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


Pssm-ID: 409033  Cd Length: 103  Bit Score: 169.34  E-value: 7.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  140 TPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEE 219
Cdd:cd21184     1 SGKSLLLEWVNSKIPEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMDIAEEELGIPKIITPED 80

                          90       100
                  ....*....|....*....|..
gi 190192186  220 IVDPNVDEHSVMTYLSQFPKAK 241
Cdd:cd21184    81 MVSPNVDELSVMTYLSYFRNAK 102
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 14-123 2.03e-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: 151.29  E-value: 2.03e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   14 WKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNqRPTFRQMQLENVSVALEFLDRESIK 93
Cdd:cd21227     1 WVEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIK-KPLNQHQKLENVTLALKAMAEDGIK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 190192186   94 LVSIDSKAIVDGNLKLILGLIWTLILHYSI 123
Cdd:cd21227    80 LVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 14-121 8.23e-39

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


Pssm-ID: 409064  Cd Length: 107  Bit Score: 141.00  E-value: 8.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   14 WKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkHNQRPTFRQMQLENVSVALEFLDRESIK 93
Cdd:cd21215     1 WVDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGR-YNKNPKMRVQKLENVNKALEFIKSRGVK 79

                          90       100
                  ....*....|....*....|....*...
gi 190192186   94 LVSIDSKAIVDGNLKLILGLIWTLILHY 121
Cdd:cd21215    80 LTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 16-121 3.42e-36

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


Pssm-ID: 409037  Cd Length: 105  Bit Score: 133.30  E-value: 3.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   16 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 95
Cdd:cd21188     2 AVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPR---ERGRMRFHRLQNVQTALDFLKYRKIKLV 78

                          90       100
                  ....*....|....*....|....*.
gi 190192186   96 SIDSKAIVDGNLKLILGLIWTLILHY 121
Cdd:cd21188    79 NIRAEDIVDGNPKLTLGLIWTIILHF 104
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 138-239 1.47e-35

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


Pssm-ID: 409078  Cd Length: 105  Bit Score: 131.74  E-value: 1.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  138 KQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITP 217
Cdd:cd21229     1 KIPPKKLMLAWLQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSP 80

                          90       100
                  ....*....|....*....|..
gi 190192186  218 EEIVDPNVDEHSVMTYLSQFPK 239
Cdd:cd21229    81 EDLSSPHLDELSGMTYLSYFMK 102
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 14-119 6.84e-33

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


Pssm-ID: 409063  Cd Length: 105  Bit Score: 124.04  E-value: 6.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   14 WKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKhnQRPTFRQMQLENVSVALEFLDRESIK 93
Cdd:cd21214     2 WEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKP--ERGKMRFHKIANVNKALDFIASKGVK 79

                          90       100
                  ....*....|....*....|....*.
gi 190192186   94 LVSIDSKAIVDGNLKLILGLIWTLIL 119
Cdd:cd21214    80 LVSIGAEEIVDGNLKMTLGMIWTIIL 105
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1421-1515 9.69e-33

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 123.10  E-value: 9.69e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1421 ASKVKCSGPGLSPGMVraNLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVLYGD 1500
Cdd:smart00557    1 ASKVKASGPGLEKGVV--GEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 190192186   1501 EEVPRSPFKVKVLPT 1515
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2012-2101 1.70e-32

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 122.33  E-value: 1.70e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2012 ASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPS--KVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQH 2089
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 190192186   2090 VPGSPFSVKVTG 2101
Cdd:smart00557   81 IPGSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1833-1919 8.37e-32

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 120.40  E-value: 8.37e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1833 VTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPS--KAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPG 1910
Cdd:smart00557    4 VKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83


                    ....*....
gi 190192186   1911 SPFTARVTG 1919
Cdd:smart00557   84 SPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 645-739 1.61e-31

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 119.63  E-value: 1.61e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    645 PDRVKARGPGLEKTgvAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGG 724
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 190192186    725 VSIPNSPFRVNVGAG 739
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
14-240 2.11e-31

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 133.14  E-value: 2.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   14 WKKIQQNTFTRWCNEHL-KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkHNQRPTFRQMQLENVSVALEFLDRESI 92
Cdd:COG5069     6 WQKVQKKTFTKWTNEKLiSGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGE-YNETPETRIHVMENVSGRLEFIKGKGV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   93 KLVSIDSKAIVDGNLKLILGLIWTLILHYSISmpmwdeeEDEEAKKQTPKQRLLGW----IQNKLPQLPITNFSRDWQSG 168
Cdd:COG5069    85 KLFNIGPQDIVDGNPKLILGLIWSLISRLTIA-------TINEEGELTKHINLLLWcdedTGGYKPEVDTFDFFRSWRDG 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190192186  169 RALGALVDSCAP-GLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVDPNV-DEHSVMTYLSQFPKA 240
Cdd:COG5069   158 LAFSALIHDSRPdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSWYIIR 231
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2203-2293 8.45e-31

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 117.70  E-value: 8.45e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2203 AHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPS--KAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEH 2280
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 190192186   2281 IPDSPFVVPVASP 2293
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1133-1225 2.85e-30

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 116.16  E-value: 2.85e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1133 ASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQP 1212
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 190192186   1213 VPNFPSKLQVEPA 1225
Cdd:smart00557   81 IPGSPFTVKVGPA 93
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 17-119 3.06e-30

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


Pssm-ID: 409042  Cd Length: 116  Bit Score: 117.01  E-value: 3.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   17 IQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRptFRQMQLENVSVALEFLdRESIKLVS 96
Cdd:cd21193    16 IQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRGR--LRVQKIENVNKALAFL-KTKVRLEN 92

                          90       100
                  ....*....|....*....|...
gi 190192186   97 IDSKAIVDGNLKLILGLIWTLIL 119
Cdd:cd21193    93 IGAEDIVDGNPRLILGLIWTIIL 115
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 6-119 9.17e-30

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: 115.54  E-value: 9.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    6 KDLAEDApwKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMhrkhnQRPTFRQM---QLENVSV 82
Cdd:cd21246     7 KALADER--EAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERL-----PKPTKGKMrihCLENVDK 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 190192186   83 ALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLIL 119
Cdd:cd21246    80 ALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1615-1708 3.92e-29

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 112.70  E-value: 3.92e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1615 ASKCTVTGAGIGPTIqIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGE 1694
Cdd:smart00557    1 ASKVKASGPGLEKGV-VGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 190192186   1695 HVPNSPFQVTALAG 1708
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 17-121 3.98e-29

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


Pssm-ID: 409035  Cd Length: 107  Bit Score: 113.25  E-value: 3.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   17 IQQNTFTRWCNEHL-KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 95
Cdd:cd21186     2 VQKKTFTKWINSQLsKANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKP---EKGRMRVHHLNNVNRALQVLEQNNVKLV 78

                          90       100
                  ....*....|....*....|....*.
gi 190192186   96 SIDSKAIVDGNLKLILGLIWTLILHY 121
Cdd:cd21186    79 NISSNDIVDGNPKLTLGLVWSIILHW 104
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 354-450 5.05e-29

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 112.31  E-value: 5.05e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    354 ASKVTAQGPGLEPSgnIANKTTYFEIFTAGAGTGEVEVVIQDPMGQKgtVEPQLEARGDSTYRCSYQPTMEGVHTVHVTF 433
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKK--VPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 190192186    434 AGVPIPRSPYTVTVGQA 450
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1040-1129 5.56e-29

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 112.31  E-value: 5.56e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1040 PSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLTVEGP--CEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTH 1117
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|..
gi 190192186   1118 IPGSPFKAHVVP 1129
Cdd:smart00557   81 IPGSPFTVKVGP 92
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 16-124 8.28e-29

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


Pssm-ID: 409085  Cd Length: 128  Bit Score: 113.16  E-value: 8.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   16 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 95
Cdd:cd21236    16 KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHRLQNVQIALDYLKRRQVKLV 92

                          90       100
                  ....*....|....*....|....*....
gi 190192186   96 SIDSKAIVDGNLKLILGLIWTLILHYSIS 124
Cdd:cd21236    93 NIRNDDITDGNPKLTLGLIWTIILHFQIS 121
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 16-123 1.51e-28

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: 112.08  E-value: 1.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   16 KIQQNTFTRWCNEHL-KCVSK-RIANLQTDLSDGLRLIALLEVLSQKKMH---RKHNQRPTFrqmqLENVSVALEFLDRE 90
Cdd:cd21241     4 RVQKKTFTNWINSYLaKRKPPmKVEDLFEDIKDGTKLLALLEVLSGEKLPcekGRRLKRVHF----LSNINTALKFLESK 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 190192186   91 SIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 123
Cdd:cd21241    80 KIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1518-1612 2.76e-28

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 110.39  E-value: 2.76e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1518 ASKVKASGPGLNttGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGG 1597
Cdd:smart00557    1 ASKVKASGPGLE--KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 190192186   1598 DEIPFSPYRVRAVPT 1612
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 453-544 4.86e-28

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 109.62  E-value: 4.86e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    453 PSACRAVGRGLQPKgvRVKETADFKVYTKGAGSGELKVTVKGPKG-EERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGG 531
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|...
gi 190192186    532 QNIGRSPFEVKVG 544
Cdd:smart00557   79 EHIPGSPFTVKVG 91
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 16-124 1.00e-26

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


Pssm-ID: 409086  Cd Length: 118  Bit Score: 107.04  E-value: 1.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   16 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 95
Cdd:cd21237     5 RVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPR---EKGRMRFHRLQNVQIALDFLKQRQVKLV 81

                          90       100
                  ....*....|....*....|....*....
gi 190192186   96 SIDSKAIVDGNLKLILGLIWTLILHYSIS 124
Cdd:cd21237    82 NIRNDDITDGNPKLTLGLIWTIILHFQIS 110
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 16-124 3.13e-26

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: 105.49  E-value: 3.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   16 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 95
Cdd:cd21235     5 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 81

                          90       100
                  ....*....|....*....|....*....
gi 190192186   96 SIDSKAIVDGNLKLILGLIWTLILHYSIS 124
Cdd:cd21235    82 NIRNDDIADGNPKLTLGLIWTIILHFQIS 110
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2394-2484 3.74e-26

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 104.22  E-value: 3.74e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2394 PGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAGALSVTIDGPS--KVKMDCQECPEG-YRVTYTPMAPGSYLISIKYGGpY 2470
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGtYTVSYTPTEPGDYTVTVKFGG-E 79

                            90
                    ....*....|....
gi 190192186   2471 HIGGSPFKAKVTGP 2484
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1418-1509 8.85e-26

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 103.14  E-value: 8.85e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1418 VTDASKVKCSGPGLSPGmvRANLPQSFQVDTSKAGvAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVL 1497
Cdd:pfam00630    1 AADASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 190192186  1498 YGDEEVPRSPFK 1509
Cdd:pfam00630   78 FNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2522-2611 1.03e-25

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 103.07  E-value: 1.03e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2522 ASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEH 2601
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 190192186   2602 IPGSPYRVVV 2611
Cdd:smart00557   81 IPGSPFTVKV 90
Filamin pfam00630
Filamin/ABP280 repeat;
1833-1914 1.60e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 102.37  E-value: 1.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1833 VTAYGPGLTHGVVNKPATFTVNTKDAGeGGLSLAIEGPS--KAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPG 1910
Cdd:pfam00630    7 VKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPG 85


                   ....
gi 190192186  1911 SPFT 1914
Cdd:pfam00630   86 SPFK 89
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 20-120 2.26e-25

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: 102.39  E-value: 2.26e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186     20 NTFTRWCNEHLKC-VSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSID 98
Cdd:smart00033    1 KTLLRWVNSLLAEyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 190192186     99 SKAIVDGNlKLILGLIWTLILH 120
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 254-348 2.44e-25

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 101.91  E-value: 2.44e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    254 PKKARAYGPGIEPTgnMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDknRTFSVWYVPEVTGTHKVTVLF 333
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGD--GTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*
gi 190192186    334 AGQHIAKSPFEVYVD 348
Cdd:smart00557   77 GGEHIPGSPFTVKVG 91
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 15-123 2.70e-25

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


Pssm-ID: 409039  Cd Length: 113  Bit Score: 102.65  E-value: 2.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   15 KKIQQNTFTRWCNEHLKCVSK--RIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTfRQMQLENVSVALEFLDRESI 92
Cdd:cd21190     3 ERVQKKTFTNWINSHLAKLSQpiVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQ-RAHKLSNIRNALDFLTKRCI 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 190192186   93 KLVSIDSKAIVDGNLKLILGLIWTLILHYSI 123
Cdd:cd21190    82 KLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 14-122 8.95e-25

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


Pssm-ID: 409074  Cd Length: 111  Bit Score: 101.07  E-value: 8.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   14 WKKIQQNTFTRWCNEHL-KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRE-S 91
Cdd:cd21225     1 WEKVQIKAFTAWVNSVLeKRGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQMIQNLHLAMLFIEEDlK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 190192186   92 IKLVSIDSKAIVDGNLKLILGLIWTLILHYS 122
Cdd:cd21225    81 IRVQGIGAEDFVDNNKKLILGLLWTLYRKYR 111
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 6-119 9.01e-25

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


Pssm-ID: 409166  Cd Length: 132  Bit Score: 102.05  E-value: 9.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    6 KDLAEDApwKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMhrkhnQRPTFRQMQ---LENVSV 82
Cdd:cd21317    22 KALADER--EAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQL-----PKPTKGRMRihcLENVDK 94

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 190192186   83 ALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLIL 119
Cdd:cd21317    95 ALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
Filamin pfam00630
Filamin/ABP280 repeat;
2010-2095 9.39e-25

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 100.06  E-value: 9.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  2010 GDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGyGGLSLSIEGPS--KVDINTEDLEDGTCRVTYCPTEPGNYIINIKFAD 2087
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*...
gi 190192186  2088 QHVPGSPF 2095
Cdd:pfam00630   81 QHIPGSPF 88
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 6-119 1.33e-24

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


Pssm-ID: 409167  Cd Length: 139  Bit Score: 101.64  E-value: 1.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    6 KDLAEDApwKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMhrkhnQRPTFRQMQ---LENVSV 82
Cdd:cd21318    29 KALADER--EAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQL-----PKPTRGRMRihsLENVDK 101

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 190192186   83 ALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLIL 119
Cdd:cd21318   102 ALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1229-1325 1.36e-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: 1.36e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1229 SGVQCYGPGIEGQGVFReaTTEFSVDARaltQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSVDVTY 1308
Cdd:smart00557    2 SKVKASGPGLEKGVVGE--PAEFTVDTR---DAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 190192186   1309 DGSPVPSSPFQVPVTEG 1325
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 845-941 1.49e-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: 99.60  E-value: 1.49e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    845 ASKVKAEGPGLSRTGVelGKPTHFTVNAKAAGKGKLDVQFSGLTKGDAvrDVDIIDHHDNTYTVKYTPVQQGPVGVNVTY 924
Cdd:smart00557    1 ASKVKASGPGLEKGVV--GEPAEFTVDTRDAGGGELEVEVTGPSGKKV--PVEVKDNGDGTYTVSYTPTEPGDYTVTVKF 76

                            90
                    ....*....|....*..
gi 190192186    925 GGDPIPKSPFSVAVSPS 941
Cdd:smart00557   77 GGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1131-1217 5.73e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 97.74  E-value: 5.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1131 FDASKVKCSGPGLERATAGEVGQFQVDCSSAGSaELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGG 1210
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGG-EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*..
gi 190192186  1211 QPVPNFP 1217
Cdd:pfam00630   81 QHIPGSP 87
Filamin pfam00630
Filamin/ABP280 repeat;
1517-1606 7.38e-24

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 97.74  E-value: 7.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1517 DASKVKASGPGLNttGVPASLPVEFTIDAKDAGeGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYG 1596
Cdd:pfam00630    3 DASKVKASGPGLE--PGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 190192186  1597 GDEIPFSPYR 1606
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
352-444 1.14e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.97  E-value: 1.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   352 GDASKVTAQGPGLEPSgnIANKTTYFEIFTAGAGtGEVEVVIQDPMGQKgtVEPQLEARGDSTYRCSYQPTMEGVHTVHV 431
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSP--VPVEVTDNGDGTYTVSYTPTEPGDYTVSV 76

                           90
                   ....*....|...
gi 190192186   432 TFAGVPIPRSPYT 444
Cdd:pfam00630   77 KFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1037-1124 1.28e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.97  E-value: 1.28e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1037 PTKPSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLtVEGP--CEAQLECLDNGDGTCSVSYVPTEPGDYNINILFA 1114
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVE-VTGPdgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 190192186  1115 DTHIPGSPFK 1124
Cdd:pfam00630   80 GQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1328-1415 1.46e-23

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 96.90  E-value: 1.46e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1328 PSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPS--EAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQ 1405
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgkKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|
gi 190192186   1406 VPGSPFKVPV 1415
Cdd:smart00557   81 IPGSPFTVKV 90
Filamin pfam00630
Filamin/ABP280 repeat;
1613-1701 1.62e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.59  E-value: 1.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1613 GDASKCTVTGAGIGPTiQIGEETVITVDTKAAGkGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFG 1692
Cdd:pfam00630    2 ADASKVKASGPGLEPG-VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*....
gi 190192186  1693 GEHVPNSPF 1701
Cdd:pfam00630   80 GQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
643-733 1.84e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.59  E-value: 1.84e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   643 FHPDRVKARGPGLEktGVAVNKPAEFTVDAKhGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSW 722
Cdd:pfam00630    2 ADASKVKASGPGLE--PGVVGKPAEFTVDTR-DAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 190192186   723 GGVSIPNSPFR 733
Cdd:pfam00630   79 NGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2201-2287 1.86e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.59  E-value: 1.86e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  2201 GGAHKVRAGGPGLERAEAGVPAEFSIWTREAGaGGLAIAVEGPS--KAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNE 2278
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 190192186  2279 EHIPDSPFV 2287
Cdd:pfam00630   81 QHIPGSPFK 89
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 17-123 2.40e-23

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


Pssm-ID: 409040  Cd Length: 114  Bit Score: 97.26  E-value: 2.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   17 IQQNTFTRWCNEHLKCVSKRIA--NLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTfRQMQLENVSVALEFLDRESIKL 94
Cdd:cd21191     5 VQKRTFTRWINLHLEKCNPPLEvkDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSH-RIFRLNNIAKALKFLEDSNVKL 83

                          90       100
                  ....*....|....*....|....*....
gi 190192186   95 VSIDSKAIVDGNLKLILGLIWTLILHYSI 123
Cdd:cd21191    84 VSIDAAEIADGNPSLVLGLIWNIILFFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 550-632 6.67e-23

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 94.98  E-value: 6.67e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    550 QKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECD--DKGDGSCDVRYWPQEAGEYAVHVLCNSEDI 627
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEvkDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81


                    ....*
gi 190192186    628 RLSPF 632
Cdd:smart00557   82 PGSPF 86
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 17-123 1.68e-22

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


Pssm-ID: 409080  Cd Length: 111  Bit Score: 94.60  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   17 IQQNTFTRWCNEHL-KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 95
Cdd:cd21231     6 VQKKTFTKWINAQFaKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVK---EKGSTRVHALNNVNKALQVLQKNNVDLV 82

                          90       100
                  ....*....|....*....|....*...
gi 190192186   96 SIDSKAIVDGNLKLILGLIWTLILHYSI 123
Cdd:cd21231    83 NIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 6-119 2.06e-22

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


Pssm-ID: 409165  Cd Length: 154  Bit Score: 95.88  E-value: 2.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    6 KDLAEDApwKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMhrkhnQRPTFRQMQ---LENVSV 82
Cdd:cd21316    44 KALADER--EAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERL-----PKPTKGRMRihcLENVDK 116

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 190192186   83 ALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLIL 119
Cdd:cd21316   117 ALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 17-123 2.11e-22

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: 94.13  E-value: 2.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   17 IQQNTFTRWCNEHLkcvSKR-----IANLQTDLSDGLRLIALLEVLSQKKMHRK--HNqrpTFRQMQleNVSVALEFLDR 89
Cdd:cd21242     5 TQKRTFTNWINSQL---AKHsppsvVSDLFTDIQDGHRLLDLLEVLSGQQLPREkgHN---VFQCRS--NIETALSFLKN 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 190192186   90 ESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 123
Cdd:cd21242    77 KSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 742-842 4.36e-22

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 92.67  E-value: 4.36e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    742 PNKVKVYGPGVAKTglKAHEPTYFTVDCAEAGQGDVSIGikcapgVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTI 821
Cdd:smart00557    1 ASKVKASGPGLEKG--VVGEPAEFTVDTRDAGGGELEVE------VTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTV 72

                            90       100
                    ....*....|....*....|.
gi 190192186    822 MVLFADQATPTSPIRVKVEPS 842
Cdd:smart00557   73 TVKFGGEHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 945-1037 2.87e-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: 2.87e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    945 SKIKVSGLG-EKVDVGKDQEFTVKSKGAGGqGKVASKIVGPSGAAVPCKVEPgLGADNSVVRFLPREEGPYEVEVTYDGV 1023
Cdd:smart00557    2 SKVKASGPGlEKGVVGEPAEFTVDTRDAGG-GELEVEVTGPSGKKVPVEVKD-NGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 190192186   1024 PVPGSPFPLEAVAP 1037
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 16-123 3.85e-21

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: 90.42  E-value: 3.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    16 KIQQNTFTRWCNEHLKC--VSKRIANLQTDLSDGLRLIALLEVLSQKKmhRKHNQRPTFRQMQLENVSVALEFLDRE-SI 92
Cdd:pfam00307    1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGL--VDKKKLNKSEFDKLENINLALDVAEKKlGV 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 190192186    93 KLVSIDSKAIVDGNLKLILGLIWTLILHYSI 123
Cdd:pfam00307   79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2297-2388 1.04e-20

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 88.81  E-value: 1.04e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   2297 ARRLTVSSLQESGLKVNQPASFAVSLNGA-KGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTH 2375
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 190192186   2376 IPGSPFKIRVGEP 2388
Cdd:smart00557   81 IPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
941-1030 1.97e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 87.73  E-value: 1.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   941 SLDLSKIKVSGLG-EKVDVGKDQEFTVKSKGAGGQGKVasKIVGPSGAAVPCKVEPgLGADNSVVRFLPREEGPYEVEVT 1019
Cdd:pfam00630    1 AADASKVKASGPGlEPGVVGKPAEFTVDTRDAGGEGEV--EVTGPDGSPVPVEVTD-NGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 190192186  1020 YDGVPVPGSPF 1030
Cdd:pfam00630   78 FNGQHIPGSPF 88
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 146-237 3.06e-20

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: 87.74  E-value: 3.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  146 LGWIQNKLPQLPITNFSRDWQSGRALGALVDSCApGLCPDWDSWDASKPVTNAREAMQQADDwLGIPQVITPEEIVDPNV 225
Cdd:cd21185     7 LRWVRQLLPDVDVNNFTTDWNDGRLLCGLVNALG-GSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEV 84

                          90
                  ....*....|..
gi 190192186  226 DEHSVMTYLSQF 237
Cdd:cd21185    85 EHLGIMAYAAQL 96
Filamin pfam00630
Filamin/ABP280 repeat;
844-934 3.70e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.96  E-value: 3.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   844 DASKVKAEGPGLSRtgVELGKPTHFTVNAKAAGkGKLDVQFSGlTKGDAVrDVDIIDHHDNTYTVKYTPVQQGPVGVNVT 923
Cdd:pfam00630    3 DASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTG-PDGSPV-PVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 190192186   924 YGGDPIPKSPF 934
Cdd:pfam00630   78 FNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
253-344 4.96e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.57  E-value: 4.96e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   253 NPKKARAYGPGIEPTgnMVKKRAEFTVETRSAGqGEVLVYVEDPAGHQEEAKVTANNDknRTFSVWYVPEVTGTHKVTVL 332
Cdd:pfam00630    3 DASKVKASGPGLEPG--VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGD--GTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 190192186   333 FAGQHIAKSPFE 344
Cdd:pfam00630   78 FNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
450-540 1.76e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.03  E-value: 1.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   450 ACNPSACRAVGRGLQPkgVRVKETADFKVYTKGAGsGELKVTVKGPKG-EERVKQKDLGDGVYGFEYYPMVPGTYIVTIT 528
Cdd:pfam00630    1 AADASKVKASGPGLEP--GVVGKPAEFTVDTRDAG-GEGEVEVTGPDGsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 190192186   529 WGGQNIGRSPFE 540
Cdd:pfam00630   78 FNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2392-2478 1.96e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.03  E-value: 1.96e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  2392 GDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGaGALSVTIDGPS--KVKMDCQECPEG-YRVTYTPMAPGSYLISIKYGG 2468
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgsPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFNG 80

                           90
                   ....*....|
gi 190192186  2469 pYHIGGSPFK 2478
Cdd:pfam00630   81 -QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
550-632 2.03e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 85.03  E-value: 2.03e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   550 QKVRAWGPGLEGGVVGKSADFVVEAiGDDVGTLGFSVEGPS--QAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDI 627
Cdd:pfam00630    5 SKVKASGPGLEPGVVGKPAEFTVDT-RDAGGEGEVEVTGPDgsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHI 83


                   ....*
gi 190192186   628 RLSPF 632
Cdd:pfam00630   84 PGSPF 88
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 22-121 4.93e-19

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


Pssm-ID: 409061  Cd Length: 105  Bit Score: 84.56  E-value: 4.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   22 FTRWCNEHLK--CVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHnQRPTFRQMQLENVSVALEFLDRESIKLVSIDS 99
Cdd:cd21212     5 YTDWANHYLEkgGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIH-SRPKTRAQKLENIQACLQFLAALGVDVQGITA 83

                          90       100
                  ....*....|....*....|..
gi 190192186  100 KAIVDGNLKLILGLIWTLILHY 121
Cdd:cd21212    84 EDIVDGNLKAILGLFFSLSRYK 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 145-237 5.51e-19

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 84.29  E-value: 5.51e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    145 LLGWIQNKL---PQLPITNFSRDWQSGRALGALVDSCAPGLCPDWD---SWDASKPVTNAREAMQQADDWLGIPQVITPE 218
Cdd:smart00033    3 LLRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90
                    ....*....|....*....
gi 190192186    219 EIVDPNVDEHSVMTYLSQF 237
Cdd:smart00033   83 DLVEGPKLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
2519-2608 6.54e-19

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 83.49  E-value: 6.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  2519 PADASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNmLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWG 2598
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGE-GEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 190192186  2599 DEHIPGSPYR 2608
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2294-2382 1.41e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 82.72  E-value: 1.41e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  2294 SGDARRLTVSSLQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNG 2373
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 190192186  2374 THIPGSPFK 2382
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1326-1412 2.19e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 81.95  E-value: 2.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1326 CDPSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLaVEGPSEAKMSCM--DNKDGSCSVEYIPYEAGTYSLNVTYGG 1403
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVE-VTGPDGSPVPVEvtDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 190192186  1404 HQVPGSPFK 1412
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1225-1318 2.87e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 81.57  E-value: 2.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  1225 AVDTSGVQCYGPGIEGQGVFREAttEFSVDARalTQTGGPHVKarVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSV 1304
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPA--EFTVDTR--DAGGEGEVE--VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTV 74

                           90
                   ....*....|....
gi 190192186  1305 DVTYDGSPVPSSPF 1318
Cdd:pfam00630   75 SVKFNGQHIPGSPF 88
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 17-123 1.49e-17

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


Pssm-ID: 409096  Cd Length: 125  Bit Score: 80.96  E-value: 1.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   17 IQQNTFTRWCNEHLKCVSKRI--ANLQTDLSDGLRLIALLEVLSQKKMHRKhnQRPTFRQMQLENVSVALEFLdRESIKL 94
Cdd:cd21247    20 MQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRP--SRGKMRVHFLENNSKAITFL-KTKVPV 96

                          90       100
                  ....*....|....*....|....*....
gi 190192186   95 VSIDSKAIVDGNLKLILGLIWTLILHYSI 123
Cdd:cd21247    97 KLIGPENIVDGDRTLILGLIWIIILRFQI 125
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 17-123 1.83e-17

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


Pssm-ID: 409081  Cd Length: 107  Bit Score: 80.05  E-value: 1.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   17 IQQNTFTRWCNEHLKCVSK-RIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 95
Cdd:cd21232     2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPK---ERGSTRVHALNNVNRVLQVLHQNNVELV 78

                          90       100
                  ....*....|....*....|....*...
gi 190192186   96 SIDSKAIVDGNLKLILGLIWTLILHYSI 123
Cdd:cd21232    79 NIGGTDIVDGNHKLTLGLLWSIILHWQV 106
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 139-237 7.54e-17

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: 78.48  E-value: 7.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   139 QTPKQRLLGWIQNKL----PQLPITNFSRDWQSGRALGALVDSCAPGLCPDWD-SWDASKPVTNAREAMQQADDWLGIPQ 213
Cdd:pfam00307    1 LELEKELLRWINSHLaeygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKLGVPK 80

                           90       100
                   ....*....|....*....|....*
gi 190192186   214 V-ITPEEIVDPnvDEHSVMTYLSQF 237
Cdd:pfam00307   81 VlIEPEDLVEG--DNKSVLTYLASL 103
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
 138-240 5.57e-16

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


Pssm-ID: 409092  Cd Length: 109  Bit Score: 75.82  E-value: 5.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  138 KQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQV 214
Cdd:cd21243     3 KGGAKKALLKWVQNAAAKrfgIEVKDFGPSWRDGVAFNAIIHSIRPDLV-DMESLKRRSNRENLETAFTVAEKELGIPRL 81

                          90       100
                  ....*....|....*....|....*.
gi 190192186  215 ITPEEIVDPNVDEHSVMTYLSQFPKA 240
Cdd:cd21243    82 LDPEDVDVDKPDEKSIMTYVAQFLKK 107
Filamin pfam00630
Filamin/ABP280 repeat;
740-836 6.20e-16

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 75.02  E-value: 6.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   740 SHPNKVKVYGPGVAKTglKAHEPTYFTVDCAEA-GQGDVSIgikcapgvVGPAEADIDFDIIRNDNDTFTVKYTPRGAGS 818
Cdd:pfam00630    2 ADASKVKASGPGLEPG--VVGKPAEFTVDTRDAgGEGEVEV--------TGPDGSPVPVEVTDNGDGTYTVSYTPTEPGD 71

                           90
                   ....*....|....*...
gi 190192186   819 YTIMVLFADQATPTSPIR 836
Cdd:pfam00630   72 YTVSVKFNGQHIPGSPFK 89
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 19-119 6.31e-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: 75.45  E-value: 6.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   19 QNTFTRWCNEHLKC-VSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNqRPTFRQMQLENVSVALEFLDRESI-KLVS 96
Cdd:cd00014     1 EEELLKWINEVLGEeLPVSITDLFESLRDGVLLCKLINKLSPGSIPKINK-KPKSPFKKRENINLFLNACKKLGLpELDL 79

                          90       100
                  ....*....|....*....|....
gi 190192186   97 IDSKAIV-DGNLKLILGLIWTLIL 119
Cdd:cd00014    80 FEPEDLYeKGNLKKVLGTLWALAL 103
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1762-1826 9.05e-16

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 74.56  E-value: 9.05e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   1762 FTIK-----KGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYVD 1826
Cdd:smart00557   22 FTVDtrdagGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVG 91
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 142-237 2.16e-15

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


Pssm-ID: 409043  Cd Length: 105  Bit Score: 73.99  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  142 KQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPE 218
Cdd:cd21194     4 KDALLLWCQRKtagYPGVNIQNFTTSWRDGLAFNALIHAHRPDLI-DYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAE 82

                          90
                  ....*....|....*....
gi 190192186  219 EIVDPNVDEHSVMTYLSQF 237
Cdd:cd21194    83 DVDVARPDEKSIMTYVASY 101
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 138-237 1.29e-14

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


Pssm-ID: 409098  Cd Length: 109  Bit Score: 72.20  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  138 KQTPKQRLLGWIQNKLP---QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQV 214
Cdd:cd21249     2 LRSAKEALLIWCQRKTAgytNVNVQDFSRSWRDGLAFNALIHAHRPDLI-DYGSLRPDRPLYNLANAFLVAEQELGISQL 80

                          90       100
                  ....*....|....*....|...
gi 190192186  215 ITPEEIVDPNVDEHSVMTYLSQF 237
Cdd:cd21249    81 LDPEDVAVPHPDERSIMTYVSLY 103
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 140-240 1.56e-14

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: 72.01  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  140 TPKQRLLGWIQNKLP---QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVIT 216
Cdd:cd21216    10 SAKEGLLLWCQRKTApykNVNVQNFHTSWKDGLAFCALIHRHRPDLL-DYDKLRKDDPRENLNLAFDVAEKHLDIPKMLD 88

                          90       100
                  ....*....|....*....|....*
gi 190192186  217 PEEIVD-PNVDEHSVMTYLSQFPKA 240
Cdd:cd21216    89 AEDIVNtPRPDERSVMTYVSCYYHA 113
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 18-121 8.05e-14

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


Pssm-ID: 409062  Cd Length: 107  Bit Score: 69.63  E-value: 8.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   18 QQNTFTRWCNEHLKcvsKR-----IANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQlENVSVALEFLDRESI 92
Cdd:cd21213     1 QLQAYVAWVNSQLK---KRpgirpVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERK-ENVEKVLQFMASKRI 76

                          90       100
                  ....*....|....*....|....*....
gi 190192186   93 KLVSIDSKAIVDGNLKLILGLIWTLILHY 121
Cdd:cd21213    77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 145-237 9.40e-14

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


Pssm-ID: 409094  Cd Length: 106  Bit Score: 69.43  E-value: 9.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  145 LLGWIQNKLPQ--LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVD 222
Cdd:cd21245     8 LLNWVQRRTRKygVAVQDFGSSWRSGLAFLALIKAIDPSLV-DMRQALEKSPRENLEDAFRIAQESLGIPPLLEPEDVMV 86

                          90
                  ....*....|....*
gi 190192186  223 PNVDEHSVMTYLSQF 237
Cdd:cd21245    87 DSPDEQSIMTYVAQF 101
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
 138-237 1.03e-13

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


Pssm-ID: 409093  Cd Length: 109  Bit Score: 69.48  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  138 KQTPKQRLLGWIQN---KLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQV 214
Cdd:cd21244     3 KMSARKALLLWAQEqcaKVGSISVTDFKSSWRNGLAFLAIIHALRPGLV-DMEKLKGRSNRENLEEAFRIAEQELKIPRL 81

                          90       100
                  ....*....|....*....|...
gi 190192186  215 ITPEEIVDPNVDEHSVMTYLSQF 237
Cdd:cd21244    82 LEPEDVDVVNPDEKSIMTYVAQF 104
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
 139-237 1.95e-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: 68.88  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  139 QTPKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVI 215
Cdd:cd21319     4 RSAKDALLLWCQMKtagYPNVNVTNFTSSWKDGLAFNALIHKHRPDLV-DFGKLKKSNARHNLEHAFNVAERQLGITKLL 82

                          90       100
                  ....*....|....*....|..
gi 190192186  216 TPEEIVDPNVDEHSVMTYLSQF 237
Cdd:cd21319    83 DPEDVFTENPDEKSIITYVVAF 104
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 138-237 2.74e-13

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


Pssm-ID: 409041  Cd Length: 107  Bit Score: 68.22  E-value: 2.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  138 KQTPKQRLLGWIQN---KLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQV 214
Cdd:cd21192     1 QGSAEKALLKWVQAeigKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLV-DMKTVKNRSPRDNLELAFRIAEQHLNIPRL 79

                          90       100
                  ....*....|....*....|...
gi 190192186  215 ITPEEIVDPNVDEHSVMTYLSQF 237
Cdd:cd21192    80 LEVEDVLVDKPDERSIMTYVSQF 102
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 7-121 2.86e-13

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: 68.38  E-value: 2.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    7 DLAEDAPWK--KIQQnTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQ--KKMHrKHNQRPTFRQMQLENVSV 82
Cdd:cd21222     5 DLFDEAPEKlaEVKE-LLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGffVPLH-EYHLTPSTDDEKLHNVKL 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 190192186   83 ALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHY 121
Cdd:cd21222    83 ALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 143-237 1.15e-12

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: 66.15  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  143 QRLLGWIQNKL---PQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEE 219
Cdd:cd22198     3 EELLSWCQEQTegyRGVKVTDLTSSWRSGLALCAIIHRFRPDLI-DFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQE 81

                          90
                  ....*....|....*....
gi 190192186  220 IVDPNV-DEHSVMTYLSQF 237
Cdd:cd22198    82 MASLAVpDKLSMVSYLSQF 100
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 138-228 2.09e-12

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: 65.78  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  138 KQTPKQRLLGWIQNKL-----PQLPITNFSRDWQSGRALGALVDSCAPGLCPD---WDSWDASKPVTNAREAMQQADDwL 209
Cdd:cd21218     8 YLPPEEILLRWVNYHLkkagpTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKelvLEVLSEEDLEKRAEKVLQAAEK-L 86

                          90
                  ....*....|....*....
gi 190192186  210 GIPQVITPEEIVDPNVDEH 228
Cdd:cd21218    87 GCKYFLTPEDIVSGNPRLN 105
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 140-238 3.05e-12

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


Pssm-ID: 409038  Cd Length: 105  Bit Score: 65.11  E-value: 3.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  140 TPKQRLLGWIQ---NKLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVIT 216
Cdd:cd21189     1 SAKEALLLWARrttEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLI-DFRSVRNQSNRENLENAFNVAEKEFGVTRLLD 79

                          90       100
                  ....*....|....*....|....*.
gi 190192186  217 PEEIVDPNVDEHSVMTYLSQ----FP 238
Cdd:cd21189    80 PEDVDVPEPDEKSIITYVSSlydvFP 105
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 36-118 3.48e-12

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


Pssm-ID: 409072  Cd Length: 113  Bit Score: 65.31  E-value: 3.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   36 RIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQ-LENVSVALEFLDRESI----KLVSIDSKAIVDGNLKLI 110
Cdd:cd21223    25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQkLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104


                  ....*...
gi 190192186  111 LGLIWTLI 118
Cdd:cd21223   105 LALLWRII 112
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 142-237 5.04e-12

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


Pssm-ID: 409097  Cd Length: 105  Bit Score: 64.34  E-value: 5.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  142 KQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPE 218
Cdd:cd21248     4 KDALLLWCQMKtagYPNVNVRNFTTSWRDGLAFNALIHKHRPDLI-DYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPE 82

                          90
                  ....*....|....*....
gi 190192186  219 EIVDPNVDEHSVMTYLSQF 237
Cdd:cd21248    83 DVNVEQPDEKSIITYVVTY 101
Filamin pfam00630
Filamin/ABP280 repeat;
1762-1820 1.15e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 63.08  E-value: 1.15e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190192186  1762 FTI----KKGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSP 1820
Cdd:pfam00630   25 FTVdtrdAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSP 87
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 9-117 3.03e-11

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


Pssm-ID: 409134  Cd Length: 121  Bit Score: 62.67  E-value: 3.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    9 AEDAPWKKIqqntFTRWCNEHL-KCVSKR-IANLQTDLSDGLRLIALLEVLSQKKMHrKHNQRPTFRQMQLENVSVALEF 86
Cdd:cd21285     6 AENGFDKQI----YTDWANHYLaKSGHKRlIKDLQQDVTDGVLLAEIIQVVANEKIE-DINGCPKNRSQMIENIDACLSF 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 190192186   87 LDRESIKLVSIDSKAIVDGNLKLILGLIWTL 117
Cdd:cd21285    81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 140-236 4.12e-11

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


Pssm-ID: 409047  Cd Length: 105  Bit Score: 62.06  E-value: 4.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  140 TPKQRLLGWIQN---KLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDwLGIPQVIT 216
Cdd:cd21198     1 SSGQDLLEWCQEvtkGYRGVKITNLTTSWRNGLAFCAILHHFRPDLI-DFSSLSPHDIKENCKLAFDAAAK-LGIPRLLD 78

                          90       100
                  ....*....|....*....|.
gi 190192186  217 PEEIVDPNV-DEHSVMTYLSQ 236
Cdd:cd21198    79 PADMVLLSVpDKLSVMTYLHQ 99
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 140-237 4.46e-11

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


Pssm-ID: 409140  Cd Length: 115  Bit Score: 62.16  E-value: 4.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  140 TPKQRLLGWIQNKLP---QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVIT 216
Cdd:cd21291    10 TAKEGLLLWCQRKTAgydEVDVQDFTTSWTDGLAFCALIHRHRPDLI-DYDKLDKKDHRGNMQLAFDIASKEIGIPQLLD 88

                          90       100
                  ....*....|....*....|..
gi 190192186  217 PEEIVD-PNVDEHSVMTYLSQF 237
Cdd:cd21291    89 VEDVCDvAKPDERSIMTYVAYY 110
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
 137-240 1.67e-10

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


Pssm-ID: 409139  Cd Length: 125  Bit Score: 60.87  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  137 KKQTPKQRLLGWIQNKLP---QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQ 213
Cdd:cd21290    10 EETSAKEGLLLWCQRKTApykNVNVQNFHISWKDGLAFNALIHRHRPELI-EYDKLRKDDPVTNLNNAFEVAEKYLDIPK 88

                          90       100
                  ....*....|....*....|....*...
gi 190192186  214 VITPEEIVD-PNVDEHSVMTYLSQFPKA 240
Cdd:cd21290    89 MLDAEDIVNtARPDEKAIMTYVSSFYHA 116
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 22-117 2.11e-10

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


Pssm-ID: 409135  Cd Length: 105  Bit Score: 60.04  E-value: 2.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   22 FTRWCNEHL-KCVSKR-IANLQTDLSDGLRLIALLEVLSQKKMHrKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDS 99
Cdd:cd21286     5 YTDWANHYLaKSGHKRlIKDLQQDIADGVLLAEIIQIIANEKVE-DINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 83

                          90
                  ....*....|....*...
gi 190192186  100 KAIVDGNLKLILGLIWTL 117
Cdd:cd21286    84 EEIRNGNLKAILGLFFSL 101
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 139-237 5.19e-10

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: 59.68  E-value: 5.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  139 QTPKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVI 215
Cdd:cd21322    16 RSAKDALLLWCQMKtagYPEVNIQNFTTSWRDGLAFNALIHRHRPDLI-DFSKLTKSNATYNLQQAFNTAEQHLGLTKLL 94

                          90       100
                  ....*....|....*....|..
gi 190192186  216 TPEEIVDPNVDEHSVMTYLSQF 237
Cdd:cd21322    95 DPEDVNMEAPDEKSIITYVVSF 116
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 137-240 6.39e-10

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: 58.97  E-value: 6.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  137 KKQTPKQRLLGWIQNKLP---QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQ 213
Cdd:cd21289     7 EETSAKEGLLLWCQRKTApyrNVNVQNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKYLDIPK 85

                          90       100
                  ....*....|....*....|....*...
gi 190192186  214 VITPEEIVD-PNVDEHSVMTYLSQFPKA 240
Cdd:cd21289    86 MLDAEDIVNtPKPDEKAIMTYVSCFYHA 113
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 21-125 8.08e-10

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 58.40  E-value: 8.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   21 TFTRWCNEhlKCVSKRIANLQTDLSDGLRLIALLE-----VLSQKKMHRKHNQRPTFRQMqLENVSVALEFLDRESIKLV 95
Cdd:cd21298    10 TYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDkikpgVVDWSRVNKPFKKLGANMKK-IENCNYAVELGKKLKFSLV 86

                          90       100       110
                  ....*....|....*....|....*....|
gi 190192186   96 SIDSKAIVDGNLKLILGLIWTLILHYSISM 125
Cdd:cd21298    87 GIGGKDIYDGNRTLTLALVWQLMRAYTLSI 116
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
 137-240 8.12e-10

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: 58.93  E-value: 8.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  137 KKQTPKQRLLGWIQNKLP---QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQ 213
Cdd:cd21288     7 EETSAKEGLLLWCQRKTApyrNVNIQNFHTSWKDGLGLCALIHRHRPDLI-DYSKLNKDDPIGNINLAMEIAEKHLDIPK 85

                          90       100
                  ....*....|....*....|....*...
gi 190192186  214 VITPEEIVD-PNVDEHSVMTYLSQFPKA 240
Cdd:cd21288    86 MLDAEDIVNtPKPDERAIMTYVSCFYHA 113
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 142-237 4.38e-09

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 56.19  E-value: 4.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  142 KQRLLGWIQNKL---PQLPITNFSRDWQSGRALGALVDSCAPGLCPDW--DSWDASKPVTNAREAMQQADDW-LGIPQVI 215
Cdd:cd00014     1 EEELLKWINEVLgeeLPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLgLPELDLF 80

                          90       100
                  ....*....|....*....|..
gi 190192186  216 TPEEIVDPNvDEHSVMTYLSQF 237
Cdd:cd00014    81 EPEDLYEKG-NLKKVLGTLWAL 101
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 36-121 9.16e-09

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: 55.37  E-value: 9.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   36 RIANLQTDLSDGLRLIALLEVLSQKKMH--RKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGL 113
Cdd:cd21219    21 LINNLYEDLRDGLVLLQVLDKIQPGCVNwkKVNKPKPLNKFKKVENCNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLAL 100


                  ....*...
gi 190192186  114 IWTLILHY 121
Cdd:cd21219   101 VWQLMRYH 108
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
 144-237 2.30e-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: 54.28  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  144 RLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEI 220
Cdd:cd21195     8 KLLTWCQQQtegYQHVNVTDLTTSWRSGLALCAIIHRFRPELI-NFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEM 86

                          90       100
                  ....*....|....*....|
gi 190192186  221 V---DPnvDEHSVMTYLSQF 237
Cdd:cd21195    87 AsaqEP--DKLSMVMYLSKF 104
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 141-237 2.48e-08

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: 54.08  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  141 PKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITP 217
Cdd:cd21197     1 KIQALLRWCRRQcegYPGVNITNLTSSFRDGLAFCAILHRHRPELI-DFHSLKKDNWLENNRLAFRVAETSLGIPALLDA 79

                          90       100
                  ....*....|....*....|.
gi 190192186  218 EEIVDPNV-DEHSVMTYLSQF 237
Cdd:cd21197    80 EDMVTMHVpDRLSIITYVSQY 100
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 137-237 2.59e-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: 54.29  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  137 KKQTPKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQ 213
Cdd:cd21321     2 EKKSAKDALLLWCQMKtagYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLI-DFETLKKSNAHYNLQNAFNVAEKELGLTK 80

                          90       100
                  ....*....|....*....|....
gi 190192186  214 VITPEEIVDPNVDEHSVMTYLSQF 237
Cdd:cd21321    81 LLDPEDVNVDQPDEKSIITYVATY 104
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 139-237 3.99e-08

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


Pssm-ID: 409169  Cd Length: 108  Bit Score: 53.56  E-value: 3.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  139 QTPKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVI 215
Cdd:cd21320     1 KSAKDALLLWCQMKtagYPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQHLGLTKLL 79

                          90       100
                  ....*....|....*....|..
gi 190192186  216 TPEEIVDPNVDEHSVMTYLSQF 237
Cdd:cd21320    80 DPEDISVDHPDEKSIITYVVTY 101
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 145-237 4.33e-08

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: 53.20  E-value: 4.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  145 LLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIV 221
Cdd:cd21187     5 LLAWCRQStrgYEQVDVKNFTTSWRDGLAFNALIHRHRPDLF-DFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVN 83

                          90
                  ....*....|....*.
gi 190192186  222 DPNVDEHSVMTYLSQF 237
Cdd:cd21187    84 VEQPDKKSILMYVTSL 99
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
 137-240 5.54e-08

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


Pssm-ID: 409136  Cd Length: 124  Bit Score: 53.55  E-value: 5.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  137 KKQTPKQRLLGWIQNKLP---QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQ 213
Cdd:cd21287     7 EETSAKEGLLLWCQRKTApykNVNIQNFHISWKDGLGFCALIHRHRPELI-DYGKLRKDDPLTNLNTAFDVAEKYLDIPK 85

                          90       100
                  ....*....|....*....|....*...
gi 190192186  214 VITPEEIV-DPNVDEHSVMTYLSQFPKA 240
Cdd:cd21287    86 MLDAEDIVgTARPDEKAIMTYVSSFYHA 113
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 140-235 6.21e-08

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


Pssm-ID: 409087  Cd Length: 106  Bit Score: 52.72  E-value: 6.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  140 TPKQRLLGWIQNKL---PQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVIT 216
Cdd:cd21238     2 TAKEKLLLWSQRMVegyQGLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80

                          90
                  ....*....|....*....
gi 190192186  217 PEEIVDPNVDEHSVMTYLS 235
Cdd:cd21238    81 PEDVDVPQPDEKSIITYVS 99
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 24-117 1.03e-07

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 52.30  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   24 RWCNEHLK---CVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVsIDSK 100
Cdd:cd21218    17 RWVNYHLKkagPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPE 95

                          90
                  ....*....|....*..
gi 190192186  101 AIVDGNLKLILGLIWTL 117
Cdd:cd21218    96 DIVSGNPRLNLAFVATL 112
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 140-236 2.85e-07

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: 51.01  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  140 TPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDwLGIPQVIT 216
Cdd:cd21254     1 NASQSLLAWCKEVTKGyrgVKITNFTTSWRNGLAFCAILHHFRPDLI-DYKSLNPHDIKENNKKAYDGFAS-LGISRLLE 78

                          90       100
                  ....*....|....*....|.
gi 190192186  217 PEEIVDPNV-DEHSVMTYLSQ 236
Cdd:cd21254    79 PSDMVLLAVpDKLTVMTYLYQ 99
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
 145-236 4.85e-07

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: 50.44  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  145 LLGWIQNKL---PQLPITNFSRDWQSGRALGALVDSCAPGLCPdWDSWDASKPVTNAREAMQQADDwLGIPQVITPEEIV 221
Cdd:cd21199    13 LLKWCQEKTqgyKGIDITNFSSSWNDGLAFCALLHSYLPDKIP-YSELNPQDKRRNFTLAFKAAES-VGIPTTLTIDEMV 90

                          90
                  ....*....|....*.
gi 190192186  222 -DPNVDEHSVMTYLSQ 236
Cdd:cd21199    91 sMERPDWQSVMSYVTA 106
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
 141-237 5.24e-07

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


Pssm-ID: 409101  Cd Length: 107  Bit Score: 50.25  E-value: 5.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  141 PKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITP 217
Cdd:cd21252     1 ARRALQAWCRRQcegYPGVEIRDLSSSFRDGLAFCAILHRHRPDLI-DFDSLSKDNVYENNRLAFEVAERELGIPALLDP 79

                          90       100
                  ....*....|....*....|.
gi 190192186  218 EEIVDPNV-DEHSVMTYLSQF 237
Cdd:cd21252    80 EDMVSMKVpDCLSIMTYVSQY 100
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
 144-237 6.79e-07

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: 49.95  E-value: 6.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  144 RLLGWIQNKL---PQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEE- 219
Cdd:cd21251     9 KLLGWCQRQTegyAGVNVTDLTMSWKSGLALCAIIHRYRPDLI-DFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEm 87

                          90       100
                  ....*....|....*....|
gi 190192186  220 --IVDPnvDEHSVMTYLSQF 237
Cdd:cd21251    88 asVGEP--DKLSMVMYLTQF 105
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
 144-237 7.28e-07

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: 49.88  E-value: 7.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  144 RLLGWIQNKLP---QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEI 220
Cdd:cd21250     8 KLLTWCQKQTEgyqNVNVTDLTTSWKSGLALCAIIHRFRPELI-DFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEM 86

                          90
                  ....*....|....*...
gi 190192186  221 VDPN-VDEHSVMTYLSQF 237
Cdd:cd21250    87 ASAEePDKLSMVMYLSKF 104
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 158-237 9.55e-07

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: 49.65  E-value: 9.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  158 ITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVDPNV-DEHSVMTYLSQ 236
Cdd:cd21253    22 VTNMTTSWRDGLAFCAIIHRFRPDLI-DFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDMVALKVpDKLSILTYVSQ 100


                  .
gi 190192186  237 F 237
Cdd:cd21253   101 Y 101
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 2-125 1.18e-06

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 50.00  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186    2 PATEKDLAEDAPWKKIQ-----QNTFTRWCNEhlKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNqRPTFRQM- 75
Cdd:cd21331     2 PALTKPENQDIDWTLLEgetreERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVN-KPPYPKLg 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 190192186   76 ----QLENVSVALEF-LDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 125
Cdd:cd21331    79 anmkKLENCNYAVELgKHPAKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNV 133
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 145-235 1.32e-06

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


Pssm-ID: 409082  Cd Length: 111  Bit Score: 49.16  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  145 LLGWIQNKL---PQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASK-PVTNAREAMQQADDWLGIPQVITPEEI 220
Cdd:cd21233     5 LLSWVRQSTrnyPQVNVINFTSSWSDGLAFNALIHSHRPDLF-DWNSVVSQQsATERLDHAFNIARQHLGIEKLLDPEDV 83

                          90
                  ....*....|....*
gi 190192186  221 VDPNVDEHSVMTYLS 235
Cdd:cd21233    84 ATAHPDKKSILMYVT 98
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 145-235 3.30e-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: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  145 LLGWI-QNKLP--QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIV 221
Cdd:cd21234     5 LLSWVrQSTRPysQVNVLNFTTSWTDGLAFNAVLHRHKPDLF-SWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVA 83

                          90
                  ....*....|....
gi 190192186  222 DPNVDEHSVMTYLS 235
Cdd:cd21234    84 VQLPDKKSIIMYLT 97
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 140-238 4.18e-06

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: 47.73  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  140 TPKQRLLGWIQN---KLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDwLGIPQVIT 216
Cdd:cd21240     4 SAKEKLLLWTQKvtaGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGVTRLLD 81

                          90       100
                  ....*....|....*....|....*.
gi 190192186  217 PEEIVDPNVDEHSVMTYLSQ----FP 238
Cdd:cd21240    82 AEDVDVPSPDEKSVITYVSSiydaFP 107
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 140-238 5.41e-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: 47.29  E-value: 5.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  140 TPKQRLLGWIQNKLP---QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDwLGIPQVIT 216
Cdd:cd21239     1 SAKERLLLWSQQMTEgytGIRCENFTTCWRDGRLFNAIIHKYRPDLI-DMNTVAVQSNLANLEHAFYVAEK-LGVTRLLD 78

                          90       100
                  ....*....|....*....|....*.
gi 190192186  217 PEEIVDPNVDEHSVMTYLSQ----FP 238
Cdd:cd21239    79 PEDVDVSSPDEKSVITYVSSlydvFP 104
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 143-236 7.22e-06

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: 47.09  E-value: 7.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  143 QRLLGWIQN---KLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDwLGIPQVITPEE 219
Cdd:cd21255     4 QSLLEWCQEvtaGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLV-DYESLDPLDIKENNKKAFEAFAS-LGVPRLLEPAD 81

                          90
                  ....*....|....*...
gi 190192186  220 IVDPNV-DEHSVMTYLSQ 236
Cdd:cd21255    82 MVLLPIpDKLIVMTYLCQ 99
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 10-125 1.02e-05

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 47.29  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   10 EDAPWKKIQ-----QNTFTRWCNEhlKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFR----QMQLENV 80
Cdd:cd21330     1 QDIDWSSIEgetreERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKlgenMKKLENC 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 190192186   81 SVALEF-LDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 125
Cdd:cd21330    79 NYAVELgKNKAKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNI 124
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 22-117 3.51e-05

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


Pssm-ID: 409149  Cd Length: 119  Bit Score: 45.49  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   22 FTRWCNEhLKcVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKH-NQRPTFRQMQ----LENVSVALEFLDRESIKLVS 96
Cdd:cd21300    12 FTLWLNS-LD-VEPAVNDLFEDLRDGLILLQAYDKVIPGSVNWKKvNKAPASAEISrfkaVENTNYAVELGKQLGFSLVG 89

                          90       100
                  ....*....|....*....|.
gi 190192186   97 IDSKAIVDGNLKLILGLIWTL 117
Cdd:cd21300    90 IQGADITDGSRTLTLALVWQL 110
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 142-237 4.35e-05

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


Pssm-ID: 409049  Cd Length: 107  Bit Score: 44.64  E-value: 4.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  142 KQRLLGWIQNKL---PQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPE 218
Cdd:cd21200     3 KQMLLEWCQAKTrgyEHVDITNFSSSWSDGMAFCALIHHFFPDAF-DYSSLDPKNRRKNFELAFSTAEELADIAPLLEVE 81

                          90       100
                  ....*....|....*....|.
gi 190192186  219 EIV--DPNVDEHSVMTYLSQF 237
Cdd:cd21200    82 DMVrmGNRPDWKCVFTYVQSL 102
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 145-239 5.87e-05

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


Pssm-ID: 409106  Cd Length: 112  Bit Score: 44.64  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  145 LLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCP--DWDSWDASKPVTNAREAMQQaddwLGI-PQVITPE 218
Cdd:cd21257    13 LLKWCQKKtegYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPyqELSSQDKKRNLLLAFQAAES----VGIkPSLELSE 88

                          90       100
                  ....*....|....*....|.
gi 190192186  219 EIVDPNVDEHSVMTYLSQFPK 239
Cdd:cd21257    89 MMYTDRPDWQSVMQYVAQIYK 109
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 37-125 5.96e-05

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


Pssm-ID: 409148  Cd Length: 114  Bit Score: 44.41  E-value: 5.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   37 IANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPT----FRQmqLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILG 112
Cdd:cd21299    22 VNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPikmpFKK--VENCNQVVKIGKQLKFSLVNVAGNDIVQGNKKLILA 99

                          90
                  ....*....|...
gi 190192186  113 LIWTLILHYSISM 125
Cdd:cd21299   100 LLWQLMRYHMLQL 112
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 18-125 1.05e-04

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: 44.21  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   18 QQNTFTRWCNEhlKCVSKRIANLQTDLSDGLRLIALLEvLSQKKMHRKHNQRPTFRQM-----QLENVSVALEF-LDRES 91
Cdd:cd21329     7 EERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYE-MTRVPVDWGHVNKPPYPALggnmkKIENCNYAVELgKNKAK 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 190192186   92 IKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 125
Cdd:cd21329    84 FSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNV 117
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 19-121 2.47e-04

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


Pssm-ID: 409070  Cd Length: 106  Bit Score: 42.65  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   19 QNTFTRWCNEHLkcVSKRIA--NLQTDLSDGLRLIALLEVLSQKKMHrkHNQRPTFRQMQLENVSVALEFLDREsIKLVS 96
Cdd:cd21221     3 VRVLTEWINEEL--ADDRIVvrDLEEDLFDGQVLQALLEKLANEKLE--VPEVAQSEEGQKQKLAVVLACVNFL-LGLEE 77

                          90       100
                  ....*....|....*....|....*....
gi 190192186   97 IDSKAIVDG----NLKLILGLIWTLILHY 121
Cdd:cd21221    78 DEARWTVDGiynkDLVSILHLLVALAHHY 106
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
 142-240 2.64e-04

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: 42.72  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  142 KQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPE 218
Cdd:cd21196     5 QEELLRWCQEQtagYPGVHVSDLSSSWADGLALCALVYRLQPGLL-EPSELQGLGALEATAWALKVAENELGITPVVSAQ 83

                          90       100
                  ....*....|....*....|..
gi 190192186  219 EIVdPNVDEHSVMTYLSQFPKA 240
Cdd:cd21196    84 AVV-AGSDPLGLIAYLSHFHSA 104
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 141-237 3.41e-04

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


Pssm-ID: 409075  Cd Length: 103  Bit Score: 42.07  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  141 PKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITP 217
Cdd:cd21226     1 SEDGLLAWCRQTTEGydgVNITSFKSSFNDGRAFLALLHAYDPELF-KQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEA 79

                          90       100
                  ....*....|....*....|
gi 190192186  218 EEIVDPNVDEHSVMTYLSQF 237
Cdd:cd21226    80 EDVMTGNPDERSIVLYTSLF 99
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 44-118 4.28e-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: 4.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   44 LSDGLRLIALLEVLS-----QKKMHRKHNQRPtFRQMqlENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLI 118
Cdd:cd21217    37 LRDGVLLCKLINKIVpgtidERKLNKKKPKNI-FEAT--ENLNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
 140-239 2.02e-03

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


Pssm-ID: 409105  Cd Length: 119  Bit Score: 40.44  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  140 TPKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCP--DWDSWDASKPVTNAREAMQQaddwLGIPQV 214
Cdd:cd21256    14 SKRNALLKWCQKKtegYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPyqELNSQDKRRNFTLAFQAAES----VGIKST 89

                          90       100
                  ....*....|....*....|....*.
gi 190192186  215 ITPEEIV-DPNVDEHSVMTYLSQFPK 239
Cdd:cd21256    90 LDINEMVrTERPDWQSVMTYVTAIYK 115
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 142-245 2.86e-03

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: 39.59  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  142 KQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPE 218
Cdd:cd21259     3 KQMLLDWCRAKtrgYENVDIQNFSSSWSDGMAFCALVHNFFPEAF-DYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVE 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 190192186  219 EIV---DPnvDEHSVMTYLSQFPKAKLKPG 245
Cdd:cd21259    82 DMVrmrEP--DWKCVYTYIQEFYRCLVQKG 109
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
22-118 4.12e-03

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 42.62  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   22 FTRWCNEHLkcVSKRIANLQTDLSDGLRliaLLEVLSQKKM-----HRKHNQRPT-----FRQMQLENVSVALEFLDRES 91
Cdd:COG5069   384 FTFWLNSLD--VSPEITNLFGDLRDQLI---LLQALSKKLMpmtvtHKLVKKQPAsgieeNRFKAFENENYAVDLGITEG 458

                          90       100
                  ....*....|....*....|....*..
gi 190192186   92 IKLVSIDSKAIVDGNlKLILGLIWTLI 118
Cdd:COG5069   459 FSLVGIKGLEILDGI-RLKLTLVWQVL 484
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 27-121 4.81e-03

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: 39.26  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186   27 NEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMH-RKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDG 105
Cdd:cd21307    26 NKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHlSEFFLTPSSTSEMLHNVTLALELLKEGGLLNFPVNPEDIVNG 105

                          90
                  ....*....|....*.
gi 190192186  106 NLKLILGLIWTLILHY 121
Cdd:cd21307   106 DSKATIRVLYCLFSKY 121
CH_PLS1_rpt2 cd21326
second calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 138-224 7.48e-03

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


Pssm-ID: 409175  Cd Length: 121  Bit Score: 38.71  E-value: 7.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  138 KQTPKQRLLGWIQNKLPQL---PITNFSRDWQSGRALGALVDSCAP-------GLCPDWDSWDASKPVTNAREAMQQADD 207
Cdd:cd21326    10 KLSPEELLLRWVNYHLTNAgwqNISNFSQDIKDSRAYFHLLNQIAPkgdvfdeNIEIDFSGFNEKNDLKRAEYMLQEADK 89

                          90
                  ....*....|....*..
gi 190192186  208 wLGIPQVITPEEIVDPN 224
Cdd:cd21326    90 -LGCRQFVTPADVVSGN 105
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 141-222 8.73e-03

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


Pssm-ID: 409145  Cd Length: 109  Bit Score: 38.27  E-value: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190192186  141 PKQRLLGWIQNKLPQL----PITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDwLGIPQVIT 216
Cdd:cd21296    11 PEKVLLKWMNFHLKKAgykkTVTNFSSDVKDAEAYAYLLNVLAPEHC-DPATLEAKDPLERAKLVLEQAEK-MNCKRYLT 88


                  ....*.
gi 190192186  217 PEEIVD 222
Cdd:cd21296    89 AKDIVE 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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