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Conserved domains on  [gi|272432643|gb|AAF46895|]
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jitterbug, isoform F [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 170-274 2.51e-68

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: 225.34  E-value: 2.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  170 KFPPRKLMLAWLQAALPDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEP 249
Cdd:cd21229     1 KIPPKKLMLAWLQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSP 80

                          90       100
                  ....*....|....*....|....*
gi 272432643  250 EYLASPWLDELSGMTYLSYFMKPGG 274
Cdd:cd21229    81 EDLSSPHLDELSGMTYLSYFMKEDG 105
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 57-166 1.08e-64

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: 215.23  E-value: 1.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   57 WVEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKPSwNRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21227     1 WVEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRV-IKKPLNQHQKLENVTLALKAMAEDGIK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21227    80 LVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 275-373 1.57e-48

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: 168.64  E-value: 1.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  275 PGYNATMRWVNTQVKD-PVKNFTTDWNDGRVMCEIIKGLGGSAPAPEKLstDPFHYENNIRKAVDAGARLGVQPILTAKD 353
Cdd:cd21185     1 PGYKATLRWVRQLLPDvDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNL--DPEESENNIQRGLEAGKSLGVEPVLTAEE 78

                          90       100
                  ....*....|....*....|
gi 272432643  354 MANPEVEHLGIMAYAAHLQW 373
Cdd:cd21185    79 MADPEVEHLGIMAYAAQLQK 98
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2850-2944 2.53e-27

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 107.69  E-value: 2.53e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2850 ASKVRVYGPGIEHGVLATFQSrFICDTRGAGAGQLTVRVRGPKGAfRVEMQRESQKDRTILCKYDPTEPGDYRVEVKWAG 2929
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAE-FTVDTRDAGGGELEVEVTGPSGK-KVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 272432643   2930 EFVPGSPFPVMIFDT 2944
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2756-2847 2.76e-27

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 107.69  E-value: 2.76e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2756 ASKVIVSGEGLRHGIVGKDIKSWIDTRRAGPGELTAHCAGVR-KVAYCELYDHGDATFTLNIKPQESGRHILTIKYGGQN 2834
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 272432643   2835 VPGSPFALKVAGA 2847
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1480-1569 3.51e-22

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.05  E-value: 3.51e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1480 ASKVVVG--SVSRGTMGRPVQFTVDAGDAGEGNLEITI-SAKGQNIPTQVHPQGSARFSVSFVPTESCEHTINVSFNKMP 1556
Cdd:smart00557    1 ASKVKASgpGLEKGVVGEPAEFTVDTRDAGGGELEVEVtGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 272432643   1557 VPGCPITVSISGG 1569
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2285-2375 1.13e-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: 91.51  E-value: 1.13e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2285 EISVSGLGLYQSRVGKTTSFAIDTVKRPAREFDVVVSGPGGQALPVRCYQTKNGHLQAEFTINKPGQCVIEVLHQSKPLP 2364
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|.
gi 272432643   2365 GSPFTCESFDS 2375
Cdd:smart00557   83 GSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1837-1926 5.30e-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: 89.59  E-value: 5.30e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1837 AEKVIVT--DIRAGVVNKSVSFGINASQAGAGNLEI-IVAVNGKNVPNFVQSEGNARFKVNFKPTEAATHSLSVRFNGHP 1913
Cdd:smart00557    1 ASKVKASgpGLEKGVVGEPAEFTVDTRDAGGGELEVeVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 272432643   1914 VPGSPFSCHIAAA 1926
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2376-2465 6.75e-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: 89.59  E-value: 6.75e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2376 SKVSTQGVTKEPLALHSPNSFTVRTDNAGTAELEAFAISPSNQSIPVLISEQSDGVYNVEFVPSQPGNYKLTLMYGGETI 2455
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|
gi 272432643   2456 PSSPLNFTAS 2465
Cdd:smart00557   82 PGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1661-1747 1.99e-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: 88.04  E-value: 1.99e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1661 SAIKVK--NVSSGTVGKAVTFLVETSQAGPGNLEVTV---NGGRVPTSAQAQGQHTYAISFTPREAESHTVELRFNSQDV 1735
Cdd:smart00557    2 SKVKASgpGLEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|..
gi 272432643   1736 PGSPFTCRVAAA 1747
Cdd:smart00557   82 PGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1936-2023 8.98e-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: 86.12  E-value: 8.98e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1936 RAMAMGECLKQAAVKMDNTFELEGFD--GVEPQIFVTSPSGDNEHCQLSQHDGGSYSASFRPTTVGRHLISVTANDQHIN 2013
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDagGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|
gi 272432643   2014 GSPFSCNVFD 2023
Cdd:smart00557   83 GSPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1310-1389 2.08e-18

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 82.27  E-value: 2.08e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1310 VNGGVVGQACQFRVDASAAGEGQLEISI---NEGEVPNHVQVVGGGRCLVSFTPEQAKSHLIDIKFNGETVRGCPFVCAV 1386
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ...
gi 272432643   1387 ADT 1389
Cdd:smart00557   91 GPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1575-1659 6.09e-17

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 78.03  E-value: 6.09e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1575 VSLGGPG----PVHQTNSFVINHNGGRLEDIEVNVEGPAGQSVPAQVHQSADGVFKAEFVPRVVGEHRVNVTVNGLPTAG 1650
Cdd:smart00557    4 VKASGPGlekgVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83


                    ....*....
gi 272432643   1651 SPYAAKVYD 1659
Cdd:smart00557   84 SPFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 560-648 1.01e-15

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 74.56  E-value: 1.01e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643    560 ASGVSVH--GLDGAMPLRAHTFEVDARGVGvSGELHVDIVH-DKHSLVCSVEKIVENKYRVTFMPRQNGKYRVYIYFNGY 636
Cdd:smart00557    1 ASKVKASgpGLEKGVVGEPAEFTVDTRDAG-GGELEVEVTGpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|..
gi 272432643    637 DVKGSPFIMRVG 648
Cdd:smart00557   80 HIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1399-1480 1.35e-15

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 74.18  E-value: 1.35e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1399 LELIPVNRPSSFHITVSGGGAAELAVSVRGPQG-ELPVRVTgDIHAG-FTAEFTPTTVGGHSINVEYNGFAVQGTPFLAK 1476
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGkKVPVEVK-DNGDGtYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVK 89


                    ....
gi 272432643   1477 SYDA 1480
Cdd:smart00557   90 VGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2021-2111 5.99e-15

Filamin/ABP280 repeat;


:

Pssm-ID: 395505  Cd Length: 89  Bit Score: 72.32  E-value: 5.99e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2021 VFDVSRVSISG--LEqqygPANLGVPVTFSVDAAGA-GEGTLElVVSTDSSTVKAEVVACARGLYDVTFVPQSTEPHYVN 2097
Cdd:pfam00630    1 AADASKVKASGpgLE----PGVVGKPAEFTVDTRDAgGEGEVE-VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVS 75

                           90
                   ....*....|....
gi 272432643  2098 ITFNEVAVDGSPFR 2111
Cdd:pfam00630   76 VKFNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1119-1198 7.48e-15

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 72.25  E-value: 7.48e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1119 ARAIRVQ--DIPNGSIGRPVEFEIDGSRAGSGNLEILV---NGGRVTSSVRSLGGQRFIASFTPHEHGTHTVQITFNGET 1193
Cdd:smart00557    1 ASKVKASgpGLEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80


                    ....*
gi 272432643   1194 VPGSP 1198
Cdd:smart00557   81 IPGSP 85
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2657-2751 2.49e-13

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 68.01  E-value: 2.49e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2657 ADKVQLMGRGLAAAQAGEAAHFTIDASNAPAGRPEVILTSQDNTSLPVSLaQPRPsENIWLASYTPLKSttGTLNLSVKW 2736
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEV-KDNG-DGTYTVSYTPTEP--GDYTVTVKF 76

                            90
                    ....*....|....*
gi 272432643   2737 NGRLVKGCPLTVAVG 2751
Cdd:smart00557   77 GGEHIPGSPFTVKVG 91
IG_FLMN super family cl42963
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1757-1837 4.10e-10

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


The actual alignment was detected with superfamily member smart00557:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 58.77  E-value: 4.10e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1757 DKVSVGRLFEFVVESDT----KPTVEVLGPARRSVPVKIDALGSSTlgYNVKFEPMEVGDHSVEVRLpGGGHVEGSPFLL 1832
Cdd:smart00557   12 EKGVVGEPAEFTVDTRDagggELEVEVTGPSGKKVPVEVKDNGDGT--YTVSYTPTEPGDYTVTVKF-GGEHIPGSPFTV 88


                    ....*
gi 272432643   1833 KAYSA 1837
Cdd:smart00557   89 KVGPA 93
IG_FLMN super family cl42963
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 468-560 1.54e-09

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


The actual alignment was detected with superfamily member smart00557:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 57.23  E-value: 1.54e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643    468 PRLLQVAPPGMAPCALGSLVEVLVNATGAPkTEDILVTAVSPTGISHNCPLKKIDEGHSAI-FKPDEAGIWEIAITYQGR 546
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAG-GGELEVEVTGPSGKKVPVEVKDNGDGTYTVsYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 272432643    547 HIQGGPFTCAVFDA 560
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2474-2555 1.06e-06

Filamin/ABP280 repeat;


:

Pssm-ID: 395505  Cd Length: 89  Bit Score: 48.82  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2474 RAAGHGLEVCHRNKEASFVVYCPIAPNV-QIERLDEYGERIEPKIKALGNNEWRISYTILSVGKYEIRASCPNRgSLPGS 2552
Cdd:pfam00630    8 KASGPGLEPGVVGKPAEFTVDTRDAGGEgEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQ-HIPGS 86


                   ...
gi 272432643  2553 PWH 2555
Cdd:pfam00630   87 PFK 89
IG_FLMN super family cl42963
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2198-2280 1.51e-06

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


The actual alignment was detected with superfamily member smart00557:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 48.75  E-value: 1.51e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2198 VSEAFCHRPASIGVSLNEAGQGDLSALVRCGA-TEVPHTIRgPSKTGVYEIVYQPTRVAPHKISILFNEVPISLKPLEIN 2276
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgKKVPVEVK-DNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVK 89


                    ....
gi 272432643   2277 VLPA 2280
Cdd:smart00557   90 VGPA 93
IG_FLMN super family cl42963
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1220-1302 5.43e-05

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


The actual alignment was detected with superfamily member smart00557:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 44.13  E-value: 5.43e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1220 PANTPAVFEILpppGQSLSKGECVATVLTPSKSKLNARVtHEAANGAARIEFVPTEVGTHVIDASINGTKIAGGPLIAKV 1299
Cdd:smart00557   15 VVGEPAEFTVD---TRDAGGGELEVEVTGPSGKKVPVEV-KDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ...
gi 272432643   1300 YDS 1302
Cdd:smart00557   91 GPA 93
 
Name Accession Description Interval E-value
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 170-274 2.51e-68

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: 225.34  E-value: 2.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  170 KFPPRKLMLAWLQAALPDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEP 249
Cdd:cd21229     1 KIPPKKLMLAWLQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSP 80

                          90       100
                  ....*....|....*....|....*
gi 272432643  250 EYLASPWLDELSGMTYLSYFMKPGG 274
Cdd:cd21229    81 EDLSSPHLDELSGMTYLSYFMKEDG 105
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 57-166 1.08e-64

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: 215.23  E-value: 1.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   57 WVEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKPSwNRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21227     1 WVEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRV-IKKPLNQHQKLENVTLALKAMAEDGIK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21227    80 LVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 275-373 1.57e-48

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: 168.64  E-value: 1.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  275 PGYNATMRWVNTQVKD-PVKNFTTDWNDGRVMCEIIKGLGGSAPAPEKLstDPFHYENNIRKAVDAGARLGVQPILTAKD 353
Cdd:cd21185     1 PGYKATLRWVRQLLPDvDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNL--DPEESENNIQRGLEAGKSLGVEPVLTAEE 78

                          90       100
                  ....*....|....*....|
gi 272432643  354 MANPEVEHLGIMAYAAHLQW 373
Cdd:cd21185    79 MADPEVEHLGIMAYAAQLQK 98
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2850-2944 2.53e-27

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 107.69  E-value: 2.53e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2850 ASKVRVYGPGIEHGVLATFQSrFICDTRGAGAGQLTVRVRGPKGAfRVEMQRESQKDRTILCKYDPTEPGDYRVEVKWAG 2929
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAE-FTVDTRDAGGGELEVEVTGPSGK-KVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 272432643   2930 EFVPGSPFPVMIFDT 2944
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2756-2847 2.76e-27

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 107.69  E-value: 2.76e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2756 ASKVIVSGEGLRHGIVGKDIKSWIDTRRAGPGELTAHCAGVR-KVAYCELYDHGDATFTLNIKPQESGRHILTIKYGGQN 2834
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 272432643   2835 VPGSPFALKVAGA 2847
Cdd:smart00557   81 IPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2847-2937 2.17e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.59  E-value: 2.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2847 APDASKVRVYGPGIEHGVlATFQSRFICDTRGAGaGQLTVRVRGPKGaFRVEMQRESQKDRTILCKYDPTEPGDYRVEVK 2926
Cdd:pfam00630    1 AADASKVKASGPGLEPGV-VGKPAEFTVDTRDAG-GEGEVEVTGPDG-SPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 272432643  2927 WAGEFVPGSPF 2937
Cdd:pfam00630   78 FNGQHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1480-1569 3.51e-22

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.05  E-value: 3.51e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1480 ASKVVVG--SVSRGTMGRPVQFTVDAGDAGEGNLEITI-SAKGQNIPTQVHPQGSARFSVSFVPTESCEHTINVSFNKMP 1556
Cdd:smart00557    1 ASKVKASgpGLEKGVVGEPAEFTVDTRDAGGGELEVEVtGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 272432643   1557 VPGCPITVSISGG 1569
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2285-2375 1.13e-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: 91.51  E-value: 1.13e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2285 EISVSGLGLYQSRVGKTTSFAIDTVKRPAREFDVVVSGPGGQALPVRCYQTKNGHLQAEFTINKPGQCVIEVLHQSKPLP 2364
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|.
gi 272432643   2365 GSPFTCESFDS 2375
Cdd:smart00557   83 GSPFTVKVGPA 93
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 59-166 5.15e-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: 5.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643    59 EIQANTFRNWVNEHLRE--TGMQVHDWATDFCDGTCLCALVENLqtRPLKPSWNRRPANQHHYLENATTALKSIEAD-HI 135
Cdd:pfam00307    1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKL--APGLVDKKKLNKSEFDKLENINLALDVAEKKlGV 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 272432643   136 KLVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:pfam00307   79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1837-1926 5.30e-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: 89.59  E-value: 5.30e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1837 AEKVIVT--DIRAGVVNKSVSFGINASQAGAGNLEI-IVAVNGKNVPNFVQSEGNARFKVNFKPTEAATHSLSVRFNGHP 1913
Cdd:smart00557    1 ASKVKASgpGLEKGVVGEPAEFTVDTRDAGGGELEVeVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 272432643   1914 VPGSPFSCHIAAA 1926
Cdd:smart00557   81 IPGSPFTVKVGPA 93
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
53-271 5.50e-21

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 100.40  E-value: 5.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   53 NEDLWVEIQANTFRNWVNEHL-RETGMQVHDWATDFCDGTCLCALVENLQtRPLKPSWNRRPANQHHYLENATTALKSIE 131
Cdd:COG5069     2 EAKKWQKVQKKTFTKWTNEKLiSGGQKEFGDLDTDLKDGVKLAQLLEALQ-KDNAGEYNETPETRIHVMENVSGRLEFIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  132 ADHIKLVNIGNVDIVNGNIKLILGLIWSLIVRYQIGR----SKFPPRKLMLAWLQ----AALPDCRITNLTTDWNSGVNL 203
Cdd:COG5069    81 GKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATineeGELTKHINLLLWCDedtgGYKPEVDTFDFFRSWRDGLAF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 272432643  204 AALLDYCQPGLF-PHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEYL---ASPwlDELSGMTYLSYFMK 271
Cdd:COG5069   161 SALIHDSRPDTLdPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIvnvSIP--DERSIMTYVSWYII 230
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2376-2465 6.75e-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: 89.59  E-value: 6.75e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2376 SKVSTQGVTKEPLALHSPNSFTVRTDNAGTAELEAFAISPSNQSIPVLISEQSDGVYNVEFVPSQPGNYKLTLMYGGETI 2455
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|
gi 272432643   2456 PSSPLNFTAS 2465
Cdd:smart00557   82 PGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1661-1747 1.99e-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: 88.04  E-value: 1.99e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1661 SAIKVK--NVSSGTVGKAVTFLVETSQAGPGNLEVTV---NGGRVPTSAQAQGQHTYAISFTPREAESHTVELRFNSQDV 1735
Cdd:smart00557    2 SKVKASgpGLEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|..
gi 272432643   1736 PGSPFTCRVAAA 1747
Cdd:smart00557   82 PGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1936-2023 8.98e-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: 86.12  E-value: 8.98e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1936 RAMAMGECLKQAAVKMDNTFELEGFD--GVEPQIFVTSPSGDNEHCQLSQHDGGSYSASFRPTTVGRHLISVTANDQHIN 2013
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDagGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|
gi 272432643   2014 GSPFSCNVFD 2023
Cdd:smart00557   83 GSPFTVKVGP 92
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 172-271 1.19e-18

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 83.49  E-value: 1.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   172 PPRKLMLAWLQAAL----PDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWR-SLDPSQSVRNCTQAMDLAQREFGVPKV 246
Cdd:pfam00307    2 ELEKELLRWINSHLaeygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKLGVPKV 81

                           90       100
                   ....*....|....*....|....*.
gi 272432643   247 L-EPEYLASPwlDELSGMTYLSYFMK 271
Cdd:pfam00307   82 LiEPEDLVEG--DNKSVLTYLASLFR 105
Filamin pfam00630
Filamin/ABP280 repeat;
2755-2840 1.96e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 82.34  E-value: 1.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2755 DASKVIVSGEGLRHGIVGKDIKSWIDTRRAGpGELTAHCAGV-RKVAYCELYDHGDATFTLNIKPQESGRHILTIKYGGQ 2833
Cdd:pfam00630    3 DASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPdGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQ 81


                   ....*..
gi 272432643  2834 NVPGSPF 2840
Cdd:pfam00630   82 HIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1310-1389 2.08e-18

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 82.27  E-value: 2.08e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1310 VNGGVVGQACQFRVDASAAGEGQLEISI---NEGEVPNHVQVVGGGRCLVSFTPEQAKSHLIDIKFNGETVRGCPFVCAV 1386
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ...
gi 272432643   1387 ADT 1389
Cdd:smart00557   91 GPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1477-1563 2.89e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 81.95  E-value: 2.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1477 SYDASKVVVG--SVSRGTMGRPVQFTVDAGDA-GEGNLEITiSAKGQNIPTQVHPQGSARFSVSFVPTESCEHTINVSFN 1553
Cdd:pfam00630    1 AADASKVKASgpGLEPGVVGKPAEFTVDTRDAgGEGEVEVT-GPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 272432643  1554 KMPVPGCPIT 1563
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2279-2369 5.61e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 81.18  E-value: 5.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2279 PASAGKeISVSGLGLYQSRVGKTTSFAIDTvKRPAREFDVVVSGPGGQALPVRCYQTKNGHLQAEFTINKPGQCVIEVLH 2358
Cdd:pfam00630    1 AADASK-VKASGPGLEPGVVGKPAEFTVDT-RDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 272432643  2359 QSKPLPGSPFT 2369
Cdd:pfam00630   79 NGQHIPGSPFK 89
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 63-161 3.40e-17

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: 79.28  E-value: 3.40e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643     63 NTFRNWVNEHLRETGMQVH-DWATDFCDGTCLCALVENLQTRPLKPSWNRRPANQHHYLENATTALKSIEADHIKLVNIG 141
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVtNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|
gi 272432643    142 NVDIVNGNiKLILGLIWSLI 161
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLI 99
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1575-1659 6.09e-17

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 78.03  E-value: 6.09e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1575 VSLGGPG----PVHQTNSFVINHNGGRLEDIEVNVEGPAGQSVPAQVHQSADGVFKAEFVPRVVGEHRVNVTVNGLPTAG 1650
Cdd:smart00557    4 VKASGPGlekgVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83


                    ....*....
gi 272432643   1651 SPYAAKVYD 1659
Cdd:smart00557   84 SPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
2372-2459 2.18e-16

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 76.56  E-value: 2.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2372 SFDSSKVSTQGVTKEPLALHSPNSFTVRTDNAGtAELEAFAISPSNQSIPVLISEQSDGVYNVEFVPSQPGNYKLTLMYG 2451
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*...
gi 272432643  2452 GETIPSSP 2459
Cdd:pfam00630   80 GQHIPGSP 87
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 560-648 1.01e-15

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 74.56  E-value: 1.01e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643    560 ASGVSVH--GLDGAMPLRAHTFEVDARGVGvSGELHVDIVH-DKHSLVCSVEKIVENKYRVTFMPRQNGKYRVYIYFNGY 636
Cdd:smart00557    1 ASKVKASgpGLEKGVVGEPAEFTVDTRDAG-GGELEVEVTGpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|..
gi 272432643    637 DVKGSPFIMRVG 648
Cdd:smart00557   80 HIPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1399-1480 1.35e-15

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 74.18  E-value: 1.35e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1399 LELIPVNRPSSFHITVSGGGAAELAVSVRGPQG-ELPVRVTgDIHAG-FTAEFTPTTVGGHSINVEYNGFAVQGTPFLAK 1476
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGkKVPVEVK-DNGDGtYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVK 89


                    ....
gi 272432643   1477 SYDA 1480
Cdd:smart00557   90 VGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2021-2111 5.99e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 72.32  E-value: 5.99e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2021 VFDVSRVSISG--LEqqygPANLGVPVTFSVDAAGA-GEGTLElVVSTDSSTVKAEVVACARGLYDVTFVPQSTEPHYVN 2097
Cdd:pfam00630    1 AADASKVKASGpgLE----PGVVGKPAEFTVDTRDAgGEGEVE-VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVS 75

                           90
                   ....*....|....
gi 272432643  2098 ITFNEVAVDGSPFR 2111
Cdd:pfam00630   76 VKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1834-1919 6.66e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 72.32  E-value: 6.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1834 AYSAEKVIVT--DIRAGVVNKSVSFGINASQAGaGNLEI-IVAVNGKNVPNFVQSEGNARFKVNFKPTEAATHSLSVRFN 1910
Cdd:pfam00630    1 AADASKVKASgpGLEPGVVGKPAEFTVDTRDAG-GEGEVeVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*....
gi 272432643  1911 GHPVPGSPF 1919
Cdd:pfam00630   80 GQHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1119-1198 7.48e-15

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 72.25  E-value: 7.48e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1119 ARAIRVQ--DIPNGSIGRPVEFEIDGSRAGSGNLEILV---NGGRVTSSVRSLGGQRFIASFTPHEHGTHTVQITFNGET 1193
Cdd:smart00557    1 ASKVKASgpGLEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80


                    ....*
gi 272432643   1194 VPGSP 1198
Cdd:smart00557   81 IPGSP 85
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2025-2114 8.48e-15

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 72.25  E-value: 8.48e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2025 SRVSISGLEqqygPANLGVPVTFSVDAAGAGEGTLELVVSTDSST-VKAEVVACARGLYDVTFVPQSTEPHYVNITFNEV 2103
Cdd:smart00557    4 VKASGPGLE----KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKkVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|.
gi 272432643   2104 AVDGSPFRVDI 2114
Cdd:smart00557   80 HIPGSPFTVKV 90
Filamin pfam00630
Filamin/ABP280 repeat;
1939-2017 2.27e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.78  E-value: 2.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1939 AMGECLKQAAVKMDNTFELEGFD-GVEPQIFVTSPSGDNEHCQLSQHDGGSYSASFRPTTVGRHLISVTANDQHINGSPF 2017
Cdd:pfam00630    9 ASGPGLEPGVVGKPAEFTVDTRDaGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
1116-1200 3.52e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.01  E-value: 3.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1116 ATGARAIRVQ--DIPNGSIGRPVEFEIDGSRAGsGNLEILV---NGGRVTSSVRSLGGQRFIASFTPHEHGTHTVQITFN 1190
Cdd:pfam00630    1 AADASKVKASgpGLEPGVVGKPAEFTVDTRDAG-GEGEVEVtgpDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 272432643  1191 GETVPGSPWH 1200
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1299-1383 4.45e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.01  E-value: 4.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1299 VYDSSLIQVTE--VNGGVVGQACQFRVDAS-AAGEGQLEISINEG-EVPNHVQVVGGGRCLVSFTPEQAKSHLIDIKFNG 1374
Cdd:pfam00630    1 AADASKVKASGpgLEPGVVGKPAEFTVDTRdAGGEGEVEVTGPDGsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 272432643  1375 ETVRGCPFV 1383
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1657-1741 4.59e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.01  E-value: 4.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1657 VYDVSAIKVK--NVSSGTVGKAVTFLVETSQAGpGNLEVTV---NGGRVPTSAQAQGQHTYAISFTPREAESHTVELRFN 1731
Cdd:pfam00630    1 AADASKVKASgpGLEPGVVGKPAEFTVDTRDAG-GEGEVEVtgpDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 272432643  1732 SQDVPGSPFT 1741
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
557-644 5.68e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 69.63  E-value: 5.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   557 VFDASGVSV--HGLDGAMPLRAHTFEVDARGVGvsGELHVDIVHDKHSLV-CSVEKIVENKYRVTFMPRQNGKYRVYIYF 633
Cdd:pfam00630    1 AADASKVKAsgPGLEPGVVGKPAEFTVDTRDAG--GEGEVEVTGPDGSPVpVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 272432643   634 NGYDVKGSPFI 644
Cdd:pfam00630   79 NGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2657-2751 2.49e-13

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 68.01  E-value: 2.49e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2657 ADKVQLMGRGLAAAQAGEAAHFTIDASNAPAGRPEVILTSQDNTSLPVSLaQPRPsENIWLASYTPLKSttGTLNLSVKW 2736
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEV-KDNG-DGTYTVSYTPTEP--GDYTVTVKF 76

                            90
                    ....*....|....*
gi 272432643   2737 NGRLVKGCPLTVAVG 2751
Cdd:smart00557   77 GGEHIPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
1580-1653 3.35e-13

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 67.31  E-value: 3.35e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 272432643  1580 PGPVHQTNSFVInHNGGRLEDIEVNVEGPAGQSVPAQVHQSADGVFKAEFVPRVVGEHRVNVTVNGLPTAGSPY 1653
Cdd:pfam00630   16 PGVVGKPAEFTV-DTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 281-377 1.38e-12

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: 66.54  E-value: 1.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   281 MRWVNTQVKDP-----VKNFTTDWNDGRVMCEIIKGLGGSAPAPEKLSTDPFHYENNIRKAVDAGAR-LGVQPIL-TAKD 353
Cdd:pfam00307    8 LRWINSHLAEYgpgvrVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKkLGVPKVLiEPED 87

                           90       100
                   ....*....|....*....|....
gi 272432643   354 MANPevEHLGIMAYAAHLQWVPPR 377
Cdd:pfam00307   88 LVEG--DNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 178-269 3.54e-11

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: 61.95  E-value: 3.54e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643    178 LAWLQAAL---PDCRITNLTTDWNSGVNLAALLDYCQPGLFPHW---RSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEY 251
Cdd:smart00033    4 LRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKkvaASLSRFKKIENINLALSFAEKLGGKVVLFEPED 83

                            90
                    ....*....|....*...
gi 272432643    252 LASPWLDELSGMTYLSYF 269
Cdd:smart00033   84 LVEGPKLILGVIWTLISL 101
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1757-1837 4.10e-10

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 58.77  E-value: 4.10e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1757 DKVSVGRLFEFVVESDT----KPTVEVLGPARRSVPVKIDALGSSTlgYNVKFEPMEVGDHSVEVRLpGGGHVEGSPFLL 1832
Cdd:smart00557   12 EKGVVGEPAEFTVDTRDagggELEVEVTGPSGKKVPVEVKDNGDGT--YTVSYTPTEPGDYTVTVKF-GGEHIPGSPFTV 88


                    ....*
gi 272432643   1833 KAYSA 1837
Cdd:smart00557   89 KVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 468-560 1.54e-09

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 57.23  E-value: 1.54e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643    468 PRLLQVAPPGMAPCALGSLVEVLVNATGAPkTEDILVTAVSPTGISHNCPLKKIDEGHSAI-FKPDEAGIWEIAITYQGR 546
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAG-GGELEVEVTGPSGKKVPVEVKDNGDGTYTVsYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 272432643    547 HIQGGPFTCAVFDA 560
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1758-1830 1.78e-09

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 56.91  E-value: 1.78e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 272432643  1758 KVSVGRLFEFVVESDT---KPTVEVLGPARRSVPVKIDALGSSTlgYNVKFEPMEVGDHSVEVRLpGGGHVEGSPF 1830
Cdd:pfam00630   16 PGVVGKPAEFTVDTRDaggEGEVEVTGPDGSPVPVEVTDNGDGT--YTVSYTPTEPGDYTVSVKF-NGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
1386-1473 2.07e-08

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 53.83  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1386 VADTSRVLLNLSNLELIPVNRPSSFHI-TVSGGGaaELAVSVRGPQG-ELPVRVTgDIHAG-FTAEFTPTTVGGHSINVE 1462
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVdTRDAGG--EGEVEVTGPDGsPVPVEVT-DNGDGtYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 272432643  1463 YNGFAVQGTPF 1473
Cdd:pfam00630   78 FNGQHIPGSPF 88
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 281-367 3.83e-07

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: 50.78  E-value: 3.83e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643    281 MRWVNTQVK----DPVKNFTTDWNDGRVMCEIIKGL-GGSAP-APEKLSTDPFHYENNIRKAVDAGARLGVQP-ILTAKD 353
Cdd:smart00033    4 LRWVNSLLAeydkPPVTNFSSDLKDGVALCALLNSLsPGLVDkKKVAASLSRFKKIENINLALSFAEKLGGKVvLFEPED 83

                            90
                    ....*....|....
gi 272432643    354 MANPEVEHLGIMAY 367
Cdd:smart00033   84 LVEGPKLILGVIWT 97
Filamin pfam00630
Filamin/ABP280 repeat;
2474-2555 1.06e-06

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 48.82  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2474 RAAGHGLEVCHRNKEASFVVYCPIAPNV-QIERLDEYGERIEPKIKALGNNEWRISYTILSVGKYEIRASCPNRgSLPGS 2552
Cdd:pfam00630    8 KASGPGLEPGVVGKPAEFTVDTRDAGGEgEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQ-HIPGS 86


                   ...
gi 272432643  2553 PWH 2555
Cdd:pfam00630   87 PFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2657-2747 1.34e-06

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 48.82  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2657 ADKVQLMGRGLAAAQAGEAAHFTIDASNApAGRPEVILTSQDNTSLPVSLAQPRPseNIWLASYTPlkSTTGTLNLSVKW 2736
Cdd:pfam00630    4 ASKVKASGPGLEPGVVGKPAEFTVDTRDA-GGEGEVEVTGPDGSPVPVEVTDNGD--GTYTVSYTP--TEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 272432643  2737 NGRLVKGCPLT 2747
Cdd:pfam00630   79 NGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2198-2280 1.51e-06

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 48.75  E-value: 1.51e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2198 VSEAFCHRPASIGVSLNEAGQGDLSALVRCGA-TEVPHTIRgPSKTGVYEIVYQPTRVAPHKISILFNEVPISLKPLEIN 2276
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgKKVPVEVK-DNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVK 89


                    ....
gi 272432643   2277 VLPA 2280
Cdd:smart00557   90 VGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1220-1302 5.43e-05

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 44.13  E-value: 5.43e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1220 PANTPAVFEILpppGQSLSKGECVATVLTPSKSKLNARVtHEAANGAARIEFVPTEVGTHVIDASINGTKIAGGPLIAKV 1299
Cdd:smart00557   15 VVGEPAEFTVD---TRDAGGGELEVEVTGPSGKKVPVEV-KDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ...
gi 272432643   1300 YDS 1302
Cdd:smart00557   91 GPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2187-2272 6.52e-05

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 43.82  E-value: 6.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2187 VFDPTLVKITE--VSEAFCHRPASIGVSLNEAGqGDLSALVRC-GATEVPHTIRgPSKTGVYEIVYQPTRVAPHKISILF 2263
Cdd:pfam00630    1 AADASKVKASGpgLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGpDGSPVPVEVT-DNGDGTYTVSYTPTEPGDYTVSVKF 78


                   ....*....
gi 272432643  2264 NEVPISLKP 2272
Cdd:pfam00630   79 NGQHIPGSP 87
Filamin pfam00630
Filamin/ABP280 repeat;
468-554 1.17e-04

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 43.05  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   468 PRLLQVAPPGMAPCALGSLVEVLVNATGAPKTEDILVTavSPTGISHNCPLKKIDEG-HSAIFKPDEAGIWEIAITYQGR 546
Cdd:pfam00630    4 ASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVT--GPDGSPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFNGQ 81


                   ....*...
gi 272432643   547 HIQGGPFT 554
Cdd:pfam00630   82 HIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1210-1294 1.61e-03

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 39.96  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1210 TALGESTRLVPANTPAVFEILPppgqSLSKGECVATVLTPSKSKLNARVTHEAaNGAARIEFVPTEVGTHVIDASINGTK 1289
Cdd:pfam00630    8 KASGPGLEPGVVGKPAEFTVDT----RDAGGEGEVEVTGPDGSPVPVEVTDNG-DGTYTVSYTPTEPGDYTVSVKFNGQH 82


                   ....*
gi 272432643  1290 IAGGP 1294
Cdd:pfam00630   83 IPGSP 87
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2474-2561 2.13e-03

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 39.51  E-value: 2.13e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2474 RAAGHGLEVCHRNKEASFVVYC--PIAPNVQIERLDEYGERIEPKIKALGNNEWRISYTILSVGKYEIRASCPNRgSLPG 2551
Cdd:smart00557    5 KASGPGLEKGVVGEPAEFTVDTrdAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE-HIPG 83

                            90
                    ....*....|
gi 272432643   2552 SPWHISCVES 2561
Cdd:smart00557   84 SPFTVKVGPA 93
 
Name Accession Description Interval E-value
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 170-274 2.51e-68

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: 225.34  E-value: 2.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  170 KFPPRKLMLAWLQAALPDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEP 249
Cdd:cd21229     1 KIPPKKLMLAWLQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSP 80

                          90       100
                  ....*....|....*....|....*
gi 272432643  250 EYLASPWLDELSGMTYLSYFMKPGG 274
Cdd:cd21229    81 EDLSSPHLDELSGMTYLSYFMKEDG 105
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 57-166 1.08e-64

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: 215.23  E-value: 1.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   57 WVEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKPSwNRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21227     1 WVEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRV-IKKPLNQHQKLENVTLALKAMAEDGIK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21227    80 LVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 57-164 9.75e-64

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: 212.34  E-value: 9.75e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   57 WVEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKPSWNRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21183     1 WKRIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYNRRPAFQQHYLENVSTALKFIEADHIK 80

                          90       100
                  ....*....|....*....|....*...
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRY 164
Cdd:cd21183    81 LVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 172-274 9.70e-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: 9.70e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  172 PPRKLMLAWLQAALPDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEY 251
Cdd:cd21184     1 SGKSLLLEWVNSKIPEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMDIAEEELGIPKIITPED 80

                          90       100
                  ....*....|....*....|...
gi 272432643  252 LASPWLDELSGMTYLSYFMKPGG 274
Cdd:cd21184    81 MVSPNVDELSVMTYLSYFRNAKV 103
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 275-373 1.57e-48

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: 168.64  E-value: 1.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  275 PGYNATMRWVNTQVKD-PVKNFTTDWNDGRVMCEIIKGLGGSAPAPEKLstDPFHYENNIRKAVDAGARLGVQPILTAKD 353
Cdd:cd21185     1 PGYKATLRWVRQLLPDvDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNL--DPEESENNIQRGLEAGKSLGVEPVLTAEE 78

                          90       100
                  ....*....|....*....|
gi 272432643  354 MANPEVEHLGIMAYAAHLQW 373
Cdd:cd21185    79 MADPEVEHLGIMAYAAQLQK 98
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 172-269 2.82e-37

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: 136.74  E-value: 2.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  172 PPRKLMLAWLQAALPDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEY 251
Cdd:cd21230     1 TPKQRLLGWIQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALENATEAMQLAEDWLGVPQLITPEE 80

                          90
                  ....*....|....*...
gi 272432643  252 LASPWLDELSGMTYLSYF 269
Cdd:cd21230    81 IINPNVDEMSVMTYLSQF 98
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 57-166 1.86e-31

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: 120.63  E-value: 1.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   57 WVEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLkPSWNRRPANQHHYLENATTALKSIEAD-HI 135
Cdd:cd21311    12 WKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKF-PKFNKRPTFRSQKLENVSVALKFLEEDeGI 90

                          90       100       110
                  ....*....|....*....|....*....|.
gi 272432643  136 KLVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21311    91 KIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 57-164 1.98e-31

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: 120.29  E-value: 1.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   57 WVEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKPSWNRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21228     1 WKKIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRPTFRQMKLENVSVALEFLERESIK 80

                          90       100
                  ....*....|....*....|....*...
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRY 164
Cdd:cd21228    81 LVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 173-269 1.69e-30

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: 117.96  E-value: 1.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  173 PRKLMLAWLQAALPDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEYL 252
Cdd:cd21315    17 PKQRLLGWIQSKVPDLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIKPEEM 96

                          90
                  ....*....|....*..
gi 272432643  253 ASPWLDELSGMTYLSYF 269
Cdd:cd21315    97 VNPKVDELSMMTYLSQF 113
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 57-164 8.55e-30

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: 115.58  E-value: 8.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   57 WVEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLkPSWNRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21215     1 WVDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESL-GRYNKNPKMRVQKLENVNKALEFIKSRGVK 79

                          90       100
                  ....*....|....*....|....*...
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRY 164
Cdd:cd21215    80 LTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 173-271 1.24e-29

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: 115.17  E-value: 1.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  173 PRKLMLAWLQAALPDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEYL 252
Cdd:cd21314    12 PKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPVQNAREAMQQADDWLGVPQVIAPEEI 91

                          90
                  ....*....|....*....
gi 272432643  253 ASPWLDELSGMTYLSYFMK 271
Cdd:cd21314    92 VDPNVDEHSVMTYLSQFPK 110
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2850-2944 2.53e-27

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 107.69  E-value: 2.53e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2850 ASKVRVYGPGIEHGVLATFQSrFICDTRGAGAGQLTVRVRGPKGAfRVEMQRESQKDRTILCKYDPTEPGDYRVEVKWAG 2929
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAE-FTVDTRDAGGGELEVEVTGPSGK-KVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 272432643   2930 EFVPGSPFPVMIFDT 2944
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2756-2847 2.76e-27

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 107.69  E-value: 2.76e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2756 ASKVIVSGEGLRHGIVGKDIKSWIDTRRAGPGELTAHCAGVR-KVAYCELYDHGDATFTLNIKPQESGRHILTIKYGGQN 2834
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 272432643   2835 VPGSPFALKVAGA 2847
Cdd:smart00557   81 IPGSPFTVKVGPA 93
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
 173-271 1.56e-26

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: 106.33  E-value: 1.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  173 PRKLMLAWLQAALPDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEYL 252
Cdd:cd21313     9 PKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPQKPVDNAREAMQQADDWLGVPQVITPEEI 88

                          90
                  ....*....|....*....
gi 272432643  253 ASPWLDELSGMTYLSYFMK 271
Cdd:cd21313    89 IHPDVDEHSVMTYLSQFPK 107
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 57-166 2.42e-26

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: 106.27  E-value: 2.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   57 WVEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKPSWNRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21310    13 WKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQMKLENVSVALEFLDREHIK 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21310    93 LVSIDSKAIVDGNLKLILGLIWTLILHYSI 122
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 57-161 4.05e-26

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: 104.78  E-value: 4.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   57 WVEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKPSwnRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21214     2 WEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKP--ERGKMRFHKIANVNKALDFIASKGVK 79

                          90       100
                  ....*....|....*....|....*
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLI 161
Cdd:cd21214    80 LVSIGAEEIVDGNLKMTLGMIWTII 104
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 170-271 2.24e-25

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: 102.96  E-value: 2.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  170 KFPPRKLMLAWLQAALPDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEP 249
Cdd:cd21312    10 KQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITP 89

                          90       100
                  ....*....|....*....|..
gi 272432643  250 EYLASPWLDELSGMTYLSYFMK 271
Cdd:cd21312    90 EEIVDPNVDEHSVMTYLSQFPK 111
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 59-165 2.78e-25

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: 102.48  E-value: 2.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   59 EIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKpswNRRPANQHHYLENATTALKSIEADHIKLV 138
Cdd:cd21188     2 AVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLP---RERGRMRFHRLQNVQTALDFLKYRKIKLV 78

                          90       100
                  ....*....|....*....|....*..
gi 272432643  139 NIGNVDIVNGNIKLILGLIWSLIVRYQ 165
Cdd:cd21188    79 NIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 59-166 4.51e-25

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: 102.07  E-value: 4.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   59 EIQANTFRNWVNEHL--RETGMQVHDWATDFCDGTCLCALVENLQTRPLkPSWNRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21241     4 RVQKKTFTNWINSYLakRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKL-PCEKGRRLKRVHFLSNINTALKFLESKKIK 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21241    83 LVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 57-166 5.97e-24

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: 99.77  E-value: 5.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   57 WVEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKPSWNRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21309    14 WKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFRQMQLENVSVALEFLDRESIK 93

                          90       100       110
                  ....*....|....*....|....*....|
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21309    94 LVSIDSKAIVDGNLKLILGLVWTLILHYSI 123
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 57-166 6.81e-24

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: 99.39  E-value: 6.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   57 WVEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKPSWNRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21308    17 WKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIK 96

                          90       100       110
                  ....*....|....*....|....*....|
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21308    97 LVSIDSKAIVDGNLKLILGLIWTLILHYSI 126
Filamin pfam00630
Filamin/ABP280 repeat;
2847-2937 2.17e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.59  E-value: 2.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2847 APDASKVRVYGPGIEHGVlATFQSRFICDTRGAGaGQLTVRVRGPKGaFRVEMQRESQKDRTILCKYDPTEPGDYRVEVK 2926
Cdd:pfam00630    1 AADASKVKASGPGLEPGV-VGKPAEFTVDTRDAG-GEGEVEVTGPDG-SPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 272432643  2927 WAGEFVPGSPF 2937
Cdd:pfam00630   78 FNGQHIPGSPF 88
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 59-166 3.29e-23

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


Pssm-ID: 409035  Cd Length: 107  Bit Score: 96.68  E-value: 3.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   59 EIQANTFRNWVNEHLRETGMQ-VHDWATDFCDGTCLCALVENLQTRPLKPswnRRPANQHHYLENATTALKSIEADHIKL 137
Cdd:cd21186     1 DVQKKTFTKWINSQLSKANKPpIKDLFEDLRDGTRLLALLEVLTGKKLKP---EKGRMRVHHLNNVNRALQVLEQNNVKL 77

                          90       100
                  ....*....|....*....|....*....
gi 272432643  138 VNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21186    78 VNISSNDIVDGNPKLTLGLVWSIILHWQV 106
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1480-1569 3.51e-22

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.05  E-value: 3.51e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1480 ASKVVVG--SVSRGTMGRPVQFTVDAGDAGEGNLEITI-SAKGQNIPTQVHPQGSARFSVSFVPTESCEHTINVSFNKMP 1556
Cdd:smart00557    1 ASKVKASgpGLEKGVVGEPAEFTVDTRDAGGGELEVEVtGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 272432643   1557 VPGCPITVSISGG 1569
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2285-2375 1.13e-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: 91.51  E-value: 1.13e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2285 EISVSGLGLYQSRVGKTTSFAIDTVKRPAREFDVVVSGPGGQALPVRCYQTKNGHLQAEFTINKPGQCVIEVLHQSKPLP 2364
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|.
gi 272432643   2365 GSPFTCESFDS 2375
Cdd:smart00557   83 GSPFTVKVGPA 93
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 59-166 5.15e-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: 5.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643    59 EIQANTFRNWVNEHLRE--TGMQVHDWATDFCDGTCLCALVENLqtRPLKPSWNRRPANQHHYLENATTALKSIEAD-HI 135
Cdd:pfam00307    1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKL--APGLVDKKKLNKSEFDKLENINLALDVAEKKlGV 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 272432643   136 KLVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:pfam00307   79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1837-1926 5.30e-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: 89.59  E-value: 5.30e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1837 AEKVIVT--DIRAGVVNKSVSFGINASQAGAGNLEI-IVAVNGKNVPNFVQSEGNARFKVNFKPTEAATHSLSVRFNGHP 1913
Cdd:smart00557    1 ASKVKASgpGLEKGVVGEPAEFTVDTRDAGGGELEVeVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 272432643   1914 VPGSPFSCHIAAA 1926
Cdd:smart00557   81 IPGSPFTVKVGPA 93
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
53-271 5.50e-21

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 100.40  E-value: 5.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   53 NEDLWVEIQANTFRNWVNEHL-RETGMQVHDWATDFCDGTCLCALVENLQtRPLKPSWNRRPANQHHYLENATTALKSIE 131
Cdd:COG5069     2 EAKKWQKVQKKTFTKWTNEKLiSGGQKEFGDLDTDLKDGVKLAQLLEALQ-KDNAGEYNETPETRIHVMENVSGRLEFIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  132 ADHIKLVNIGNVDIVNGNIKLILGLIWSLIVRYQIGR----SKFPPRKLMLAWLQ----AALPDCRITNLTTDWNSGVNL 203
Cdd:COG5069    81 GKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATineeGELTKHINLLLWCDedtgGYKPEVDTFDFFRSWRDGLAF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 272432643  204 AALLDYCQPGLF-PHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEYL---ASPwlDELSGMTYLSYFMK 271
Cdd:COG5069   161 SALIHDSRPDTLdPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIvnvSIP--DERSIMTYVSWYII 230
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2376-2465 6.75e-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: 89.59  E-value: 6.75e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2376 SKVSTQGVTKEPLALHSPNSFTVRTDNAGTAELEAFAISPSNQSIPVLISEQSDGVYNVEFVPSQPGNYKLTLMYGGETI 2455
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|
gi 272432643   2456 PSSPLNFTAS 2465
Cdd:smart00557   82 PGSPFTVKVG 91
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 275-367 8.39e-21

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: 89.60  E-value: 8.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  275 PGYNATMRWVNTQV-KDPVKNFTTDWNDGRVMCEIIKGL-GGSAPAPEKLST-DPfhyENNIRKAVDAGAR-LGVQPILT 350
Cdd:cd21184     1 SGKSLLLEWVNSKIpEYKVKNFTTDWNDGKALAALVDALkPGLIPDNESLDKeNP---LENATKAMDIAEEeLGIPKIIT 77

                          90
                  ....*....|....*..
gi 272432643  351 AKDMANPEVEHLGIMAY 367
Cdd:cd21184    78 PEDMVSPNVDELSVMTY 94
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1661-1747 1.99e-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: 88.04  E-value: 1.99e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1661 SAIKVK--NVSSGTVGKAVTFLVETSQAGPGNLEVTV---NGGRVPTSAQAQGQHTYAISFTPREAESHTVELRFNSQDV 1735
Cdd:smart00557    2 SKVKASgpGLEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHI 81

                            90
                    ....*....|..
gi 272432643   1736 PGSPFTCRVAAA 1747
Cdd:smart00557   82 PGSPFTVKVGPA 93
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 60-166 7.81e-20

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: 87.24  E-value: 7.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   60 IQANTFRNWVNEHL--RETGMQVHDWATDFCDGTCLCALVENLQTRPLkPSWNRRPANQHHYLENATTALKSIEADHIKL 137
Cdd:cd21190     5 VQKKTFTNWINSHLakLSQPIVINDLFVDIKDGTALLRLLEVLSGQKL-PIESGRVLQRAHKLSNIRNALDFLTKRCIKL 83

                          90       100
                  ....*....|....*....|....*....
gi 272432643  138 VNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21190    84 VNINSTDIVDGKPSIVLGLIWTIILYFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1936-2023 8.98e-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: 86.12  E-value: 8.98e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1936 RAMAMGECLKQAAVKMDNTFELEGFD--GVEPQIFVTSPSGDNEHCQLSQHDGGSYSASFRPTTVGRHLISVTANDQHIN 2013
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDagGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82

                            90
                    ....*....|
gi 272432643   2014 GSPFSCNVFD 2023
Cdd:smart00557   83 GSPFTVKVGP 92
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 59-166 1.30e-19

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: 86.52  E-value: 1.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   59 EIQANTFRNWVNEHLRETGMQ-VHDWATDFCDGTCLCALVENLQTRPLKpswNRRPANQHHYLENATTALKSIEADHIKL 137
Cdd:cd21231     5 DVQKKTFTKWINAQFAKFGKPpIEDLFTDLQDGRRLLELLEGLTGQKLV---KEKGSTRVHALNNVNKALQVLQKNNVDL 81

                          90       100
                  ....*....|....*....|....*....
gi 272432643  138 VNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21231    82 VNIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 60-163 1.53e-19

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: 86.65  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   60 IQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPL-KPSWNRRpanQHHYLENATTALKSIEADHIKLV 138
Cdd:cd21246    16 VQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLpKPTKGKM---RIHCLENVDKALQFLKEQRVHLE 92

                          90       100
                  ....*....|....*....|....*
gi 272432643  139 NIGNVDIVNGNIKLILGLIWSLIVR 163
Cdd:cd21246    93 NMGSHDIVDGNHRLTLGLIWTIILR 117
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 60-163 1.85e-19

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


Pssm-ID: 409167  Cd Length: 139  Bit Score: 87.00  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   60 IQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPL-KPSWNRRpanQHHYLENATTALKSIEADHIKLV 138
Cdd:cd21318    38 VQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLpKPTRGRM---RIHSLENVDKALQFLKEQRVHLE 114

                          90       100
                  ....*....|....*....|....*
gi 272432643  139 NIGNVDIVNGNIKLILGLIWSLIVR 163
Cdd:cd21318   115 NVGSHDIVDGNHRLTLGLIWTIILR 139
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 50-168 7.58e-19

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: 85.04  E-value: 7.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   50 IRGNEDLWVEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKPSWNRRpanQHHYLENATTALKS 129
Cdd:cd21236     7 LERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM---RFHRLQNVQIALDY 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 272432643  130 IEADHIKLVNIGNVDIVNGNIKLILGLIWSLIVRYQIGR 168
Cdd:cd21236    84 LKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISD 122
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 58-163 8.65e-19

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: 84.27  E-value: 8.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   58 VEIQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPL-KPSWNRRpanQHHYLENATTALKSIeADHIK 136
Cdd:cd21193    14 INIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLgKPNRGRL---RVQKIENVNKALAFL-KTKVR 89

                          90       100
                  ....*....|....*....|....*..
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVR 163
Cdd:cd21193    90 LENIGAEDIVDGNPRLILGLIWTIILR 116
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 172-271 1.19e-18

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 83.49  E-value: 1.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   172 PPRKLMLAWLQAAL----PDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWR-SLDPSQSVRNCTQAMDLAQREFGVPKV 246
Cdd:pfam00307    2 ELEKELLRWINSHLaeygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKLGVPKV 81

                           90       100
                   ....*....|....*....|....*.
gi 272432643   247 L-EPEYLASPwlDELSGMTYLSYFMK 271
Cdd:pfam00307   82 LiEPEDLVEG--DNKSVLTYLASLFR 105
Filamin pfam00630
Filamin/ABP280 repeat;
2755-2840 1.96e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 82.34  E-value: 1.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2755 DASKVIVSGEGLRHGIVGKDIKSWIDTRRAGpGELTAHCAGV-RKVAYCELYDHGDATFTLNIKPQESGRHILTIKYGGQ 2833
Cdd:pfam00630    3 DASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPdGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQ 81


                   ....*..
gi 272432643  2834 NVPGSPF 2840
Cdd:pfam00630   82 HIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1310-1389 2.08e-18

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 82.27  E-value: 2.08e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1310 VNGGVVGQACQFRVDASAAGEGQLEISI---NEGEVPNHVQVVGGGRCLVSFTPEQAKSHLIDIKFNGETVRGCPFVCAV 1386
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ...
gi 272432643   1387 ADT 1389
Cdd:smart00557   91 GPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1477-1563 2.89e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 81.95  E-value: 2.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1477 SYDASKVVVG--SVSRGTMGRPVQFTVDAGDA-GEGNLEITiSAKGQNIPTQVHPQGSARFSVSFVPTESCEHTINVSFN 1553
Cdd:pfam00630    1 AADASKVKASgpGLEPGVVGKPAEFTVDTRDAgGEGEVEVT-GPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 272432643  1554 KMPVPGCPIT 1563
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2279-2369 5.61e-18

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 81.18  E-value: 5.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2279 PASAGKeISVSGLGLYQSRVGKTTSFAIDTvKRPAREFDVVVSGPGGQALPVRCYQTKNGHLQAEFTINKPGQCVIEVLH 2358
Cdd:pfam00630    1 AADASK-VKASGPGLEPGVVGKPAEFTVDT-RDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 272432643  2359 QSKPLPGSPFT 2369
Cdd:pfam00630   79 NGQHIPGSPFK 89
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 60-166 1.12e-17

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: 81.09  E-value: 1.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   60 IQANTFRNWVNEHLR--ETGMQVHDWATDFCDGTCLCALVENLQTRPL----KPSWNRRpanqhHYLENATTALKSIEAD 133
Cdd:cd21191     5 VQKRTFTRWINLHLEkcNPPLEVKDLFVDIQDGKILMALLEVLSGQNLlqeyKPSSHRI-----FRLNNIAKALKFLEDS 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 272432643  134 HIKLVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21191    80 NVKLVSIDAAEIADGNPSLVLGLIWNIILFFQI 112
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 60-167 1.60e-17

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: 80.84  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   60 IQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKPSWNRRpanQHHYLENATTALKSIEADHIKLVN 139
Cdd:cd21235     6 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRHRQVKLVN 82

                          90       100
                  ....*....|....*....|....*...
gi 272432643  140 IGNVDIVNGNIKLILGLIWSLIVRYQIG 167
Cdd:cd21235    83 IRNDDIADGNPKLTLGLIWTIILHFQIS 110
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 57-165 1.96e-17

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: 80.27  E-value: 1.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   57 WVEIQANTFRNWVNEHLRETGM-QVHDWATDFCDGTCLCALVENLQTRPLKPSWNRRPANQHHYLENATTALKSIEAD-H 134
Cdd:cd21225     1 WEKVQIKAFTAWVNSVLEKRGIpKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQMIQNLHLAMLFIEEDlK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 272432643  135 IKLVNIGNVDIVNGNIKLILGLIWSLIVRYQ 165
Cdd:cd21225    81 IRVQGIGAEDFVDNNKKLILGLLWTLYRKYR 111
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 63-161 3.40e-17

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: 79.28  E-value: 3.40e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643     63 NTFRNWVNEHLRETGMQVH-DWATDFCDGTCLCALVENLQTRPLKPSWNRRPANQHHYLENATTALKSIEADHIKLVNIG 141
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVtNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|
gi 272432643    142 NVDIVNGNiKLILGLIWSLI 161
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLI 99
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1575-1659 6.09e-17

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 78.03  E-value: 6.09e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1575 VSLGGPG----PVHQTNSFVINHNGGRLEDIEVNVEGPAGQSVPAQVHQSADGVFKAEFVPRVVGEHRVNVTVNGLPTAG 1650
Cdd:smart00557    4 VKASGPGlekgVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83


                    ....*....
gi 272432643   1651 SPYAAKVYD 1659
Cdd:smart00557   84 SPFTVKVGP 92
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 60-163 7.70e-17

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: 79.33  E-value: 7.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   60 IQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPL-KPSWNRRpanQHHYLENATTALKSIEADHIKLV 138
Cdd:cd21317    31 VQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLpKPTKGRM---RIHCLENVDKALQFLKEQKVHLE 107

                          90       100
                  ....*....|....*....|....*
gi 272432643  139 NIGNVDIVNGNIKLILGLIWSLIVR 163
Cdd:cd21317   108 NMGSHDIVDGNHRLTLGLIWTIILR 132
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 59-166 9.37e-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: 78.13  E-value: 9.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   59 EIQANTFRNWVNEHLRETGM-QVHDWATDFCDGTCLCALVENLQTRPLKpswNRRPANQHHYLENATTALKSIEADHIKL 137
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLP---KERGSTRVHALNNVNRVLQVLHQNNVEL 77

                          90       100
                  ....*....|....*....|....*....
gi 272432643  138 VNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21232    78 VNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
Filamin pfam00630
Filamin/ABP280 repeat;
2372-2459 2.18e-16

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 76.56  E-value: 2.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2372 SFDSSKVSTQGVTKEPLALHSPNSFTVRTDNAGtAELEAFAISPSNQSIPVLISEQSDGVYNVEFVPSQPGNYKLTLMYG 2451
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*...
gi 272432643  2452 GETIPSSP 2459
Cdd:pfam00630   80 GQHIPGSP 87
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 60-166 3.43e-16

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: 77.00  E-value: 3.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   60 IQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPLKPSWNRRpanQHHYLENATTALKSIEADHIKLVN 139
Cdd:cd21237     6 VQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRM---RFHRLQNVQIALDFLKQRQVKLVN 82

                          90       100
                  ....*....|....*....|....*..
gi 272432643  140 IGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21237    83 IRNDDITDGNPKLTLGLIWTIILHFQI 109
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 560-648 1.01e-15

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 74.56  E-value: 1.01e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643    560 ASGVSVH--GLDGAMPLRAHTFEVDARGVGvSGELHVDIVH-DKHSLVCSVEKIVENKYRVTFMPRQNGKYRVYIYFNGY 636
Cdd:smart00557    1 ASKVKASgpGLEKGVVGEPAEFTVDTRDAG-GGELEVEVTGpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|..
gi 272432643    637 DVKGSPFIMRVG 648
Cdd:smart00557   80 HIPGSPFTVKVG 91
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 177-269 1.24e-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: 74.76  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  177 MLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEYLA 253
Cdd:cd21194     7 LLLWCQrktAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLI-DYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAEDVD 85

                          90
                  ....*....|....*..
gi 272432643  254 SPWLDELSGMTYL-SYF 269
Cdd:cd21194    86 VARPDEKSIMTYVaSYY 102
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1399-1480 1.35e-15

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 74.18  E-value: 1.35e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1399 LELIPVNRPSSFHITVSGGGAAELAVSVRGPQG-ELPVRVTgDIHAG-FTAEFTPTTVGGHSINVEYNGFAVQGTPFLAK 1476
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGkKVPVEVK-DNGDGtYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVK 89


                    ....
gi 272432643   1477 SYDA 1480
Cdd:smart00557   90 VGPA 93
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 60-163 2.83e-15

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: 75.47  E-value: 2.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   60 IQANTFRNWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTRPL-KPSWNRRpanQHHYLENATTALKSIEADHIKLV 138
Cdd:cd21316    53 VQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLpKPTKGRM---RIHCLENVDKALQFLKEQRVHLE 129

                          90       100
                  ....*....|....*....|....*
gi 272432643  139 NIGNVDIVNGNIKLILGLIWSLIVR 163
Cdd:cd21316   130 NMGSHDIVDGNHRLTLGLIWTIILR 154
Filamin pfam00630
Filamin/ABP280 repeat;
2021-2111 5.99e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 72.32  E-value: 5.99e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2021 VFDVSRVSISG--LEqqygPANLGVPVTFSVDAAGA-GEGTLElVVSTDSSTVKAEVVACARGLYDVTFVPQSTEPHYVN 2097
Cdd:pfam00630    1 AADASKVKASGpgLE----PGVVGKPAEFTVDTRDAgGEGEVE-VTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVS 75

                           90
                   ....*....|....
gi 272432643  2098 ITFNEVAVDGSPFR 2111
Cdd:pfam00630   76 VKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1834-1919 6.66e-15

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 72.32  E-value: 6.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1834 AYSAEKVIVT--DIRAGVVNKSVSFGINASQAGaGNLEI-IVAVNGKNVPNFVQSEGNARFKVNFKPTEAATHSLSVRFN 1910
Cdd:pfam00630    1 AADASKVKASgpGLEPGVVGKPAEFTVDTRDAG-GEGEVeVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*....
gi 272432643  1911 GHPVPGSPF 1919
Cdd:pfam00630   80 GQHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1119-1198 7.48e-15

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 72.25  E-value: 7.48e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1119 ARAIRVQ--DIPNGSIGRPVEFEIDGSRAGSGNLEILV---NGGRVTSSVRSLGGQRFIASFTPHEHGTHTVQITFNGET 1193
Cdd:smart00557    1 ASKVKASgpGLEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80


                    ....*
gi 272432643   1194 VPGSP 1198
Cdd:smart00557   81 IPGSP 85
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2025-2114 8.48e-15

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 72.25  E-value: 8.48e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2025 SRVSISGLEqqygPANLGVPVTFSVDAAGAGEGTLELVVSTDSST-VKAEVVACARGLYDVTFVPQSTEPHYVNITFNEV 2103
Cdd:smart00557    4 VKASGPGLE----KGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKkVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|.
gi 272432643   2104 AVDGSPFRVDI 2114
Cdd:smart00557   80 HIPGSPFTVKV 90
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 59-166 1.18e-14

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: 72.17  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   59 EIQANTFRNWVNEHL--RETGMQVHDWATDFCDGTCLCALVENLQTRPLKpswNRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21242     4 QTQKRTFTNWINSQLakHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLP---REKGHNVFQCRSNIETALSFLKNKSIK 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21242    81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
Filamin pfam00630
Filamin/ABP280 repeat;
1939-2017 2.27e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.78  E-value: 2.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1939 AMGECLKQAAVKMDNTFELEGFD-GVEPQIFVTSPSGDNEHCQLSQHDGGSYSASFRPTTVGRHLISVTANDQHINGSPF 2017
Cdd:pfam00630    9 ASGPGLEPGVVGKPAEFTVDTRDaGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
1116-1200 3.52e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.01  E-value: 3.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1116 ATGARAIRVQ--DIPNGSIGRPVEFEIDGSRAGsGNLEILV---NGGRVTSSVRSLGGQRFIASFTPHEHGTHTVQITFN 1190
Cdd:pfam00630    1 AADASKVKASgpGLEPGVVGKPAEFTVDTRDAG-GEGEVEVtgpDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 272432643  1191 GETVPGSPWH 1200
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1299-1383 4.45e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.01  E-value: 4.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1299 VYDSSLIQVTE--VNGGVVGQACQFRVDAS-AAGEGQLEISINEG-EVPNHVQVVGGGRCLVSFTPEQAKSHLIDIKFNG 1374
Cdd:pfam00630    1 AADASKVKASGpgLEPGVVGKPAEFTVDTRdAGGEGEVEVTGPDGsPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNG 80


                   ....*....
gi 272432643  1375 ETVRGCPFV 1383
Cdd:pfam00630   81 QHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
1657-1741 4.59e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.01  E-value: 4.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1657 VYDVSAIKVK--NVSSGTVGKAVTFLVETSQAGpGNLEVTV---NGGRVPTSAQAQGQHTYAISFTPREAESHTVELRFN 1731
Cdd:pfam00630    1 AADASKVKASgpGLEPGVVGKPAEFTVDTRDAG-GEGEVEVtgpDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79

                           90
                   ....*....|
gi 272432643  1732 SQDVPGSPFT 1741
Cdd:pfam00630   80 GQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
557-644 5.68e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 69.63  E-value: 5.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   557 VFDASGVSV--HGLDGAMPLRAHTFEVDARGVGvsGELHVDIVHDKHSLV-CSVEKIVENKYRVTFMPRQNGKYRVYIYF 633
Cdd:pfam00630    1 AADASKVKAsgPGLEPGVVGKPAEFTVDTRDAG--GEGEVEVTGPDGSPVpVEVTDNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 272432643   634 NGYDVKGSPFI 644
Cdd:pfam00630   79 NGQHIPGSPFK 89
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 173-269 1.13e-13

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: 69.24  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  173 PRKLmLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEP 249
Cdd:cd22198     2 PEEL-LSWCQeqtEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLI-DFSSLDPENIAENNQLAFDVAEQELGIPPVMTG 79

                          90       100
                  ....*....|....*....|...
gi 272432643  250 EYLAS---PwlDELSGMTYLSYF 269
Cdd:cd22198    80 QEMASlavP--DKLSMVSYLSQF 100
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 281-369 2.16e-13

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: 69.04  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  281 MRWVNTQVKD-PVKNFTTDWNDGRVMCEIIKGLG-GSAPAPEklSTDPFHYENNIRKAVDAGAR-LGVQPILTAKDMANP 357
Cdd:cd21315    22 LGWIQSKVPDlPITNFTNDWNDGKAIGALVDALApGLCPDWE--DWDPKDAVKNAKEAMDLAEDwLDVPQLIKPEEMVNP 99

                          90
                  ....*....|..
gi 272432643  358 EVEHLGIMAYAA 369
Cdd:cd21315   100 KVDELSMMTYLS 111
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2657-2751 2.49e-13

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 68.01  E-value: 2.49e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2657 ADKVQLMGRGLAAAQAGEAAHFTIDASNAPAGRPEVILTSQDNTSLPVSLaQPRPsENIWLASYTPLKSttGTLNLSVKW 2736
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEV-KDNG-DGTYTVSYTPTEP--GDYTVTVKF 76

                            90
                    ....*....|....*
gi 272432643   2737 NGRLVKGCPLTVAVG 2751
Cdd:smart00557   77 GGEHIPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
1580-1653 3.35e-13

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 67.31  E-value: 3.35e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 272432643  1580 PGPVHQTNSFVInHNGGRLEDIEVNVEGPAGQSVPAQVHQSADGVFKAEFVPRVVGEHRVNVTVNGLPTAGSPY 1653
Cdd:pfam00630   16 PGVVGKPAEFTV-DTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 63-161 9.21e-13

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: 66.59  E-value: 9.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   63 NTFRNWVNEHLRETGMQ-VHDWATDFCDGTCLCALVENLQTRpLKPSWNRRPANQHHYLENATTALKSIEADHI-KLVNI 140
Cdd:cd00014     2 EELLKWINEVLGEELPVsITDLFESLRDGVLLCKLINKLSPG-SIPKINKKPKSPFKKRENINLFLNACKKLGLpELDLF 80

                          90       100
                  ....*....|....*....|..
gi 272432643  141 GNVDIV-NGNIKLILGLIWSLI 161
Cdd:cd00014    81 EPEDLYeKGNLKKVLGTLWALA 102
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 281-377 1.38e-12

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: 66.54  E-value: 1.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   281 MRWVNTQVKDP-----VKNFTTDWNDGRVMCEIIKGLGGSAPAPEKLSTDPFHYENNIRKAVDAGAR-LGVQPIL-TAKD 353
Cdd:pfam00307    8 LRWINSHLAEYgpgvrVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKkLGVPKVLiEPED 87

                           90       100
                   ....*....|....*....|....
gi 272432643   354 MANPevEHLGIMAYAAHLQWVPPR 377
Cdd:pfam00307   88 LVEG--DNKSVLTYLASLFRRFQA 109
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 60-166 2.65e-12

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: 65.93  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   60 IQANTFRNWVNEHLRE--TGMQVHDWATDFCDGTCLCALVENLQTRPL-KPSwnrRPANQHHYLENATTALKSIEADhIK 136
Cdd:cd21247    20 MQKKTFTKWMNNVFSKngAKIEITDIYTELKDGIHLLRLLELISGEQLpRPS---RGKMRVHFLENNSKAITFLKTK-VP 95

                          90       100       110
                  ....*....|....*....|....*....|
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21247    96 VKLIGPENIVDGDRTLILGLIWIIILRFQI 125
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 278-367 6.32e-12

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: 64.33  E-value: 6.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  278 NATMRWVNTQVKD-PVKNFTTDWNDGRVMCEIIKGLggsAPA--PEKLSTDPFHYENNIRKAVD-AGARLGVQPILTAKD 353
Cdd:cd21230     4 QRLLGWIQNKIPQlPITNFTTDWNDGRALGALVDSC---APGlcPDWETWDPNDALENATEAMQlAEDWLGVPQLITPEE 80

                          90
                  ....*....|....
gi 272432643  354 MANPEVEHLGIMAY 367
Cdd:cd21230    81 IINPNVDEMSVMTY 94
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 173-267 6.83e-12

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


Pssm-ID: 409038  Cd Length: 105  Bit Score: 64.34  E-value: 6.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  173 PRKLMLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEP 249
Cdd:cd21189     2 AKEALLLWARrttEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLI-DFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80

                          90
                  ....*....|....*...
gi 272432643  250 EYLASPWLDELSGMTYLS 267
Cdd:cd21189    81 EDVDVPEPDEKSIITYVS 98
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 172-266 9.38e-12

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: 63.98  E-value: 9.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  172 PPRKLMLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQrEFGVPKVLE 248
Cdd:cd21198     1 SSGQDLLEWCQevtKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLI-DFSSLSPHDIKENCKLAFDAAA-KLGIPRLLD 78

                          90       100
                  ....*....|....*....|.
gi 272432643  249 PE---YLASPwlDELSGMTYL 266
Cdd:cd21198    79 PAdmvLLSVP--DKLSVMTYL 97
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 63-168 2.13e-11

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: 63.07  E-value: 2.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   63 NTFRNWVNEHLRETgmQVHDWATDFCDGTCLCALVENLQtrPLKPSWNR----RPANQHHYLENATTALKSIEADHIKLV 138
Cdd:cd21219     7 RAFRMWLNSLGLDP--LINNLYEDLRDGLVLLQVLDKIQ--PGCVNWKKvnkpKPLNKFKKVENCNYAVDLAKKLGFSLV 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 272432643  139 NIGNVDIVNGNIKLILGLIWSLiVRYQIGR 168
Cdd:cd21219    83 GIGGKDIADGNRKLTLALVWQL-MRYHVLQ 111
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 178-269 3.54e-11

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: 61.95  E-value: 3.54e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643    178 LAWLQAAL---PDCRITNLTTDWNSGVNLAALLDYCQPGLFPHW---RSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEY 251
Cdd:smart00033    4 LRWVNSLLaeyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKkvaASLSRFKKIENINLALSFAEKLGGKVVLFEPED 83

                            90
                    ....*....|....*...
gi 272432643    252 LASPWLDELSGMTYLSYF 269
Cdd:smart00033   84 LVEGPKLILGVIWTLISL 101
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 174-269 3.84e-11

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


Pssm-ID: 409098  Cd Length: 109  Bit Score: 62.19  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  174 RKLMLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPE 250
Cdd:cd21249     6 KEALLIWCQrktAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLI-DYGSLRPDRPLYNLANAFLVAEQELGISQLLDPE 84

                          90
                  ....*....|....*....
gi 272432643  251 YLASPWLDELSGMTYLSYF 269
Cdd:cd21249    85 DVAVPHPDERSIMTYVSLY 103
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
 173-269 1.65e-10

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: 60.44  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  173 PRKLmLAWLQA---ALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEP 249
Cdd:cd21195     6 PSKL-LTWCQQqteGYQHVNVTDLTTSWRSGLALCAIIHRFRPELI-NFDSLNEDDAVENNQLAFDVAEREFGIPPVTTG 83

                          90       100
                  ....*....|....*....|...
gi 272432643  250 EYLAS---PwlDELSGMTYLSYF 269
Cdd:cd21195    84 KEMASaqeP--DKLSMVMYLSKF 104
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 173-266 1.95e-10

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: 60.25  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  173 PRKLMLAWLQAALPDCR---ITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQrEFGVPKVLEP 249
Cdd:cd21254     2 ASQSLLAWCKEVTKGYRgvkITNFTTSWRNGLAFCAILHHFRPDLI-DYKSLNPHDIKENNKKAYDGFA-SLGISRLLEP 79

                          90       100
                  ....*....|....*....|
gi 272432643  250 E---YLASPwlDELSGMTYL 266
Cdd:cd21254    80 SdmvLLAVP--DKLTVMTYL 97
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
 169-269 2.69e-10

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: 59.89  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  169 SKFPPRKLmLAWLQAALPDCR---ITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPK 245
Cdd:cd21250     2 SDIRPNKL-LTWCQKQTEGYQnvnVTDLTTSWKSGLALCAIIHRFRPELI-DFDSLNEDDAVKNNQLAFDVAEREFGIPP 79

                          90       100
                  ....*....|....*....|....*..
gi 272432643  246 VLEPEYLAS---PwlDELSGMTYLSYF 269
Cdd:cd21250    80 VTTGKEMASaeeP--DKLSMVMYLSKF 104
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 177-269 3.97e-10

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


Pssm-ID: 409140  Cd Length: 115  Bit Score: 59.46  E-value: 3.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  177 MLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEYL- 252
Cdd:cd21291    15 LLLWCQrktAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLI-DYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVEDVc 93

                          90
                  ....*....|....*....
gi 272432643  253 --ASPwlDELSGMTYLSYF 269
Cdd:cd21291    94 dvAKP--DERSIMTYVAYY 110
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
 174-271 4.00e-10

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: 59.63  E-value: 4.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  174 RKLMLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPE 250
Cdd:cd21319     7 KDALLLWCQmktAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLV-DFGKLKKSNARHNLEHAFNVAERQLGITKLLDPE 85

                          90       100
                  ....*....|....*....|....*
gi 272432643  251 YLASPWLDELSGMTYL----SYFMK 271
Cdd:cd21319    86 DVFTENPDEKSIITYVvafyHYFSK 110
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1757-1837 4.10e-10

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 58.77  E-value: 4.10e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1757 DKVSVGRLFEFVVESDT----KPTVEVLGPARRSVPVKIDALGSSTlgYNVKFEPMEVGDHSVEVRLpGGGHVEGSPFLL 1832
Cdd:smart00557   12 EKGVVGEPAEFTVDTRDagggELEVEVTGPSGKKVPVEVKDNGDGT--YTVSYTPTEPGDYTVTVKF-GGEHIPGSPFTV 88


                    ....*
gi 272432643   1833 KAYSA 1837
Cdd:smart00557   89 KVGPA 93
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
 168-271 9.97e-10

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


Pssm-ID: 409093  Cd Length: 109  Bit Score: 58.31  E-value: 9.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  168 RSKFPPRKLMLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVP 244
Cdd:cd21244     1 RWKMSARKALLLWAQeqcAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLV-DMEKLKGRSNRENLEEAFRIAEQELKIP 79

                          90       100
                  ....*....|....*....|....*..
gi 272432643  245 KVLEPEYLASPWLDELSGMTYLSYFMK 271
Cdd:cd21244    80 RLLEPEDVDVVNPDEKSIMTYVAQFLQ 106
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 468-560 1.54e-09

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 57.23  E-value: 1.54e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643    468 PRLLQVAPPGMAPCALGSLVEVLVNATGAPkTEDILVTAVSPTGISHNCPLKKIDEGHSAI-FKPDEAGIWEIAITYQGR 546
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAG-GGELEVEVTGPSGKKVPVEVKDNGDGTYTVsYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 272432643    547 HIQGGPFTCAVFDA 560
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1758-1830 1.78e-09

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 56.91  E-value: 1.78e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 272432643  1758 KVSVGRLFEFVVESDT---KPTVEVLGPARRSVPVKIDALGSSTlgYNVKFEPMEVGDHSVEVRLpGGGHVEGSPF 1830
Cdd:pfam00630   16 PGVVGKPAEFTVDTRDaggEGEVEVTGPDGSPVPVEVTDNGDGT--YTVSYTPTEPGDYTVSVKF-NGQHIPGSPF 88
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 175-269 2.46e-09

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


Pssm-ID: 409102  Cd Length: 106  Bit Score: 56.97  E-value: 2.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  175 KLMLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFPhWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPE- 250
Cdd:cd21253     4 KALQQWCRqqtEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLID-FDSLSKENVYENNKLAFTVAEKELGIPALLDAEd 82

                          90       100
                  ....*....|....*....|.
gi 272432643  251 --YLASPwlDELSGMTYLSYF 269
Cdd:cd21253    83 mvALKVP--DKLSILTYVSQY 101
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
 173-269 2.62e-09

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


Pssm-ID: 409046  Cd Length: 105  Bit Score: 56.78  E-value: 2.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  173 PRKLMLAWLQA---ALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEP 249
Cdd:cd21197     1 KIQALLRWCRRqceGYPGVNITNLTSSFRDGLAFCAILHRHRPELI-DFHSLKKDNWLENNRLAFRVAETSLGIPALLDA 79

                          90       100
                  ....*....|....*....|.
gi 272432643  250 EYLASPWL-DELSGMTYLSYF 269
Cdd:cd21197    80 EDMVTMHVpDRLSIITYVSQY 100
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 59-164 2.71e-09

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: 56.82  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   59 EIQANTfrNWVNEHLRETG--MQVHDWATDFCDGTCLCALVENLqTRPLKPSWNRRPANQHHYLENATTALKSIEADHIK 136
Cdd:cd21212     1 EIEIYT--DWANHYLEKGGhkRIITDLQKDLGDGLTLVNLIEAV-AGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVD 77

                          90       100
                  ....*....|....*....|....*...
gi 272432643  137 LVNIGNVDIVNGNIKLILGLIWSLIVRY 164
Cdd:cd21212    78 VQGITAEDIVDGNLKAILGLFFSLSRYK 105
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 281-371 5.39e-09

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: 56.15  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  281 MRWVNTQV------KDPVKNFTTDWNDGRVMCEIIKGLGGSA--PAPEKLSTDPFHYENNIRKAVDAGARLGVQPILTAK 352
Cdd:cd21218    16 LRWVNYHLkkagptKKRVTNFSSDLKDGEVYALLLHSLAPELcdKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYFLTPE 95

                          90
                  ....*....|....*....
gi 272432643  353 DMANPEvEHLgIMAYAAHL 371
Cdd:cd21218    96 DIVSGN-PRL-NLAFVATL 112
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 177-267 7.50e-09

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: 55.56  E-value: 7.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  177 MLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDlAQREFGVPKVLEP-EYL 252
Cdd:cd21255     6 LLEWCQevtAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLV-DYESLDPLDIKENNKKAFE-AFASLGVPRLLEPaDMV 83

                          90
                  ....*....|....*
gi 272432643  253 ASPWLDELSGMTYLS 267
Cdd:cd21255    84 LLPIPDKLIVMTYLC 98
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 177-269 9.21e-09

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: 55.48  E-value: 9.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  177 MLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEYLA 253
Cdd:cd21248     7 LLLWCQmktAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLI-DYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPEDVN 85

                          90
                  ....*....|....*..
gi 272432643  254 SPWLDELSGMTYL-SYF 269
Cdd:cd21248    86 VEQPDEKSIITYVvTYY 102
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 170-271 9.71e-09

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: 55.51  E-value: 9.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  170 KFPPRKLMLAWLQAALPD---CRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKV 246
Cdd:cd21192     1 QGSAEKALLKWVQAEIGKyygIRVTDFDKSWRDGVAFLALIHAIRPDLV-DMKTVKNRSPRDNLELAFRIAEQHLNIPRL 79

                          90       100
                  ....*....|....*....|....*
gi 272432643  247 LEPEYLASPWLDELSGMTYLSYFMK 271
Cdd:cd21192    80 LEVEDVLVDKPDERSIMTYVSQFLR 104
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
 168-271 1.30e-08

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: 55.02  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  168 RSKFPPRKLMLAWLQAALP---DCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVP 244
Cdd:cd21243     1 KFKGGAKKALLKWVQNAAAkrfGIEVKDFGPSWRDGVAFNAIIHSIRPDLV-DMESLKRRSNRENLETAFTVAEKELGIP 79

                          90       100
                  ....*....|....*....|....*..
gi 272432643  245 KVLEPEYLASPWLDELSGMTYLSYFMK 271
Cdd:cd21243    80 RLLDPEDVDVDKPDEKSIMTYVAQFLK 106
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
 177-269 1.33e-08

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


Pssm-ID: 409100 [Multi-domain]  Cd Length: 111  Bit Score: 54.95  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  177 MLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEYLA 253
Cdd:cd21251    10 LLGWCQrqtEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLI-DFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEMA 88

                          90
                  ....*....|....*....
gi 272432643  254 S---PwlDELSGMTYLSYF 269
Cdd:cd21251    89 SvgeP--DKLSMVMYLTQF 105
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 278-354 1.78e-08

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: 54.27  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  278 NATMRWVNTQVK----DPVKNFTTDWNDGRVMCEIIKGL-GGSAPAPEKLSTDPFHYENNIRKAVDAGARLGVQP--ILT 350
Cdd:cd00014     2 EELLKWINEVLGeelpVSITDLFESLRDGVLLCKLINKLsPGSIPKINKKPKSPFKKRENINLFLNACKKLGLPEldLFE 81


                  ....
gi 272432643  351 AKDM 354
Cdd:cd00014    82 PEDL 85
Filamin pfam00630
Filamin/ABP280 repeat;
1386-1473 2.07e-08

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 53.83  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1386 VADTSRVLLNLSNLELIPVNRPSSFHI-TVSGGGaaELAVSVRGPQG-ELPVRVTgDIHAG-FTAEFTPTTVGGHSINVE 1462
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGKPAEFTVdTRDAGG--EGEVEVTGPDGsPVPVEVT-DNGDGtYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 272432643  1463 YNGFAVQGTPF 1473
Cdd:pfam00630   78 FNGQHIPGSPF 88
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 59-161 2.60e-08

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: 54.50  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   59 EIQAntFRNWVNEHLRET----GMQVHDWATD-----FCDGTCLCALVENLQ--TRPLKpSWNR-RPANQHHYLENATTA 126
Cdd:cd21217     2 EKEA--FVEHINSLLADDpdlkHLLPIDPDGDdlfeaLRDGVLLCKLINKIVpgTIDER-KLNKkKPKNIFEATENLNLA 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 272432643  127 LKSIEADHIKLVNIGNVDIVNGNIKLILGLIWSLI 161
Cdd:cd21217    79 LNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 86-163 4.49e-08

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 53.99  E-value: 4.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   86 DFC-DGTCLCALVEN-----LQTRPL-KPSWNRRPANQHHYLENATTALKSIEADHIKLVNIGNVDIVNGNIKLILGLIW 158
Cdd:cd21294    40 DECkDGLVLSKLINDsvpdtIDERVLnKPPRKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIW 119


                  ....*
gi 272432643  159 SLIVR 163
Cdd:cd21294   120 QIIRR 124
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 177-271 7.90e-08

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


Pssm-ID: 409170  Cd Length: 119  Bit Score: 53.14  E-value: 7.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  177 MLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEYLA 253
Cdd:cd21321    10 LLLWCQmktAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLI-DFETLKKSNAHYNLQNAFNVAEKELGLTKLLDPEDVN 88

                          90       100
                  ....*....|....*....|..
gi 272432643  254 SPWLDELSGMTYLS----YFMK 271
Cdd:cd21321    89 VDQPDEKSIITYVAtyyhYFSK 110
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 67-160 8.09e-08

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 53.07  E-value: 8.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   67 NWVNEHLRETG---MQVHDWATDFCDGTCLCALVENLQTRPLKPSWNRRPANQHHYLENATTALKSIEADHIKLVnIGNV 143
Cdd:cd21218    17 RWVNYHLKKAGptkKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPE 95

                          90
                  ....*....|....*..
gi 272432643  144 DIVNGNIKLILGLIWSL 160
Cdd:cd21218    96 DIVSGNPRLNLAFVATL 112
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 67-164 1.50e-07

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: 52.20  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   67 NWVNEHLRETGMQVHDWATDFCDGT---CLCALVENLQTrPLKpSWNRRPANQHHYLENATTALKSIEADHIKLVNIGNV 143
Cdd:cd21222    23 QFVNKHLAKLNIEVTDLATQFHDGVyliLLIGLLEGFFV-PLH-EYHLTPSTDDEKLHNVKLALELMEDAGISTPKIRPE 100

                          90       100
                  ....*....|....*....|.
gi 272432643  144 DIVNGNIKLILGLIWSLIVRY 164
Cdd:cd21222   101 DIVNGDLKSILRVLYSLFSKY 121
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 175-271 1.67e-07

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


Pssm-ID: 409036  Cd Length: 104  Bit Score: 51.66  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  175 KLMLAWLQAA---LPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEY 251
Cdd:cd21187     3 KTLLAWCRQStrgYEQVDVKNFTTSWRDGLAFNALIHRHRPDLF-DFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81

                          90       100
                  ....*....|....*....|
gi 272432643  252 LASPWLDELSGMTYLSYFMK 271
Cdd:cd21187    82 VNVEQPDKKSILMYVTSLFQ 101
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 177-269 1.80e-07

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


Pssm-ID: 409171  Cd Length: 130  Bit Score: 52.36  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  177 MLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEYLA 253
Cdd:cd21322    22 LLLWCQmktAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLI-DFSKLTKSNATYNLQQAFNTAEQHLGLTKLLDPEDVN 100

                          90
                  ....*....|....*.
gi 272432643  254 SPWLDELSGMTYLSYF 269
Cdd:cd21322   101 MEAPDEKSIITYVVSF 116
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 174-271 3.53e-07

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: 50.80  E-value: 3.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  174 RKLMLAWLQAALPD---CRITNLTTDWNSGVNLAALLDYCQPGLFP--HWRSLDPSQSVRNCTQAMDLAqREFGVPKV-- 246
Cdd:cd00014     1 EEELLKWINEVLGEelpVSITDLFESLRDGVLLCKLINKLSPGSIPkiNKKPKSPFKKRENINLFLNAC-KKLGLPELdl 79

                          90       100
                  ....*....|....*....|....*
gi 272432643  247 LEPEYLASPwLDELSGMTYLSYFMK 271
Cdd:cd00014    80 FEPEDLYEK-GNLKKVLGTLWALAL 103
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 281-367 3.83e-07

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: 50.78  E-value: 3.83e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643    281 MRWVNTQVK----DPVKNFTTDWNDGRVMCEIIKGL-GGSAP-APEKLSTDPFHYENNIRKAVDAGARLGVQP-ILTAKD 353
Cdd:smart00033    4 LRWVNSLLAeydkPPVTNFSSDLKDGVALCALLNSLsPGLVDkKKVAASLSRFKKIENINLALSFAEKLGGKVvLFEPED 83

                            90
                    ....*....|....
gi 272432643    354 MANPEVEHLGIMAY 367
Cdd:smart00033   84 LVEGPKLILGVIWT 97
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 64-166 4.51e-07

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 50.70  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   64 TFRNWVNEhlreTGMQ--VHDWATDFCDGTCLCALVENLqtRPLKPSWNRR----PANQHHY--LENATTALKSIEADHI 135
Cdd:cd21298    10 TYRNWMNS----LGVNpfVNHLYSDLRDGLVLLQLYDKI--KPGVVDWSRVnkpfKKLGANMkkIENCNYAVELGKKLKF 83

                          90       100       110
                  ....*....|....*....|....*....|.
gi 272432643  136 KLVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21298    84 SLVGIGGKDIYDGNRTLTLALVWQLMRAYTL 114
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 175-267 5.34e-07

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


Pssm-ID: 409083 [Multi-domain]  Cd Length: 104  Bit Score: 50.34  E-value: 5.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  175 KLMLAWL-QAALP--DCRITNLTTDWNSGVNLAALLDYCQPGLFPhWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEY 251
Cdd:cd21234     3 KILLSWVrQSTRPysQVNVLNFTTSWTDGLAFNAVLHRHKPDLFS-WDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81

                          90
                  ....*....|....*.
gi 272432643  252 LASPWLDELSGMTYLS 267
Cdd:cd21234    82 VAVQLPDKKSIIMYLT 97
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 175-270 5.55e-07

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: 50.17  E-value: 5.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  175 KLMLAWLQ--AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWRSLDPSqSVRNCTQAMDLAQREFGVPKVLEPEYL 252
Cdd:cd21245     6 KALLNWVQrrTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKS-PRENLEDAFRIAQESLGIPPLLEPEDV 84

                          90       100
                  ....*....|....*....|
gi 272432643  253 A--SPwlDELSGMTYLSYFM 270
Cdd:cd21245    85 MvdSP--DEQSIMTYVAQFL 102
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
 173-272 6.00e-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: 6.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  173 PRKLMLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEP 249
Cdd:cd21252     1 ARRALQAWCRrqcEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLI-DFDSLSKDNVYENNRLAFEVAERELGIPALLDP 79

                          90       100
                  ....*....|....*....|....*...
gi 272432643  250 EYLASPWL-DELSGMTYLS----YFMKP 272
Cdd:cd21252    80 EDMVSMKVpDCLSIMTYVSqyynHFSNP 107
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
 177-269 8.76e-07

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


Pssm-ID: 409045  Cd Length: 106  Bit Score: 49.66  E-value: 8.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  177 MLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLfphwrsLDPSQ-----SVRNCTQAMDLAQREFGVPKVLE 248
Cdd:cd21196     8 LLRWCQeqtAGYPGVHVSDLSSSWADGLALCALVYRLQPGL------LEPSElqglgALEATAWALKVAENELGITPVVS 81

                          90       100
                  ....*....|....*....|.
gi 272432643  249 PEYLASPwLDELSGMTYLSYF 269
Cdd:cd21196    82 AQAVVAG-SDPLGLIAYLSHF 101
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 283-378 9.19e-07

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: 50.07  E-value: 9.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  283 WVNTQVKD-PVKNFTTDWNDGRVMCEIIKglgGSAPA--PEKLSTDPFHYENNIRKAV-DAGARLGVQPILTAKDMANPE 358
Cdd:cd21314    19 WIQNKVPQlPITNFNRDWQDGKALGALVD---NCAPGlcPDWESWDPNQPVQNAREAMqQADDWLGVPQVIAPEEIVDPN 95

                          90       100
                  ....*....|....*....|
gi 272432643  359 VEHLGIMAYAAHLQWVPPRP 378
Cdd:cd21314    96 VDEHSVMTYLSQFPKAKLKP 115
Filamin pfam00630
Filamin/ABP280 repeat;
2474-2555 1.06e-06

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 48.82  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2474 RAAGHGLEVCHRNKEASFVVYCPIAPNV-QIERLDEYGERIEPKIKALGNNEWRISYTILSVGKYEIRASCPNRgSLPGS 2552
Cdd:pfam00630    8 KASGPGLEPGVVGKPAEFTVDTRDAGGEgEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQ-HIPGS 86


                   ...
gi 272432643  2553 PWH 2555
Cdd:pfam00630   87 PFK 89
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 177-271 1.15e-06

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: 49.33  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  177 MLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPEYLA 253
Cdd:cd21320     7 LLLWCQmktAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDIS 85

                          90       100
                  ....*....|....*....|..
gi 272432643  254 SPWLDELSGMTYL----SYFMK 271
Cdd:cd21320    86 VDHPDEKSIITYVvtyyHYFSK 107
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 292-372 1.21e-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: 49.40  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  292 VKNFTTDWNDGRVMCEIIKGLggsapAPEKL---STDPFHYENNIRKAVDAGARLGVQPILTAKDMANPEV-EHLGIMAY 367
Cdd:cd21255    22 VTNFTTSWRNGLAFCAILHHF-----HPDLVdyeSLDPLDIKENNKKAFEAFASLGVPRLLEPADMVLLPIpDKLIVMTY 96


                  ....*
gi 272432643  368 AAHLQ 372
Cdd:cd21255    97 LCQLR 101
Filamin pfam00630
Filamin/ABP280 repeat;
2657-2747 1.34e-06

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 48.82  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2657 ADKVQLMGRGLAAAQAGEAAHFTIDASNApAGRPEVILTSQDNTSLPVSLAQPRPseNIWLASYTPlkSTTGTLNLSVKW 2736
Cdd:pfam00630    4 ASKVKASGPGLEPGVVGKPAEFTVDTRDA-GGEGEVEVTGPDGSPVPVEVTDNGD--GTYTVSYTP--TEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 272432643  2737 NGRLVKGCPLT 2747
Cdd:pfam00630   79 NGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2198-2280 1.51e-06

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 48.75  E-value: 1.51e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2198 VSEAFCHRPASIGVSLNEAGQGDLSALVRCGA-TEVPHTIRgPSKTGVYEIVYQPTRVAPHKISILFNEVPISLKPLEIN 2276
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSgKKVPVEVK-DNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVK 89


                    ....
gi 272432643   2277 VLPA 2280
Cdd:smart00557   90 VGPA 93
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 277-371 1.79e-06

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: 48.82  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  277 YNATMRWVNTQVKD----PVKNFTTDWNDGRVMCEIIKGLggsapAPEKL---STDPFHYENNIRKAVDAGAR-LGVQPI 348
Cdd:cd22198     2 PEELLSWCQEQTEGyrgvKVTDLTSSWRSGLALCAIIHRF-----RPDLIdfsSLDPENIAENNQLAFDVAEQeLGIPPV 76

                          90       100
                  ....*....|....*....|....
gi 272432643  349 LTAKDMAN-PEVEHLGIMAYAAHL 371
Cdd:cd22198    77 MTGQEMASlAVPDKLSMVSYLSQF 100
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 79-161 2.37e-06

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: 48.74  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   79 QVHDWATDFCDGTCLCALVENLQTRPLKPSWNRRPAN---QHhyLENATTALKSI-EADHIKLVNIGNV---DIVNGNIK 151
Cdd:cd21223    25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAIsrlQK--LHNVEVALKALkEAGVLRGGDGGGItakDIVDGHRE 102

                          90
                  ....*....|
gi 272432643  152 LILGLIWSLI 161
Cdd:cd21223   103 KTLALLWRII 112
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 68-160 4.23e-06

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: 47.68  E-value: 4.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   68 WVNEHL--RETGMQVHDWATDFCDGTCLCALVENLQTRPLkPSWNRRPANQHHYLENATTALKSIEADHIKLVNIGNVDI 145
Cdd:cd21213     8 WVNSQLkkRPGIRPVQDLRRDLRDGVALAQLIEILAGEKL-PGIDWNPTTDAERKENVEKVLQFMASKRIRMHQTSAKDI 86

                          90
                  ....*....|....*
gi 272432643  146 VNGNIKLILGLIWSL 160
Cdd:cd21213    87 VDGNLKAIMRLILAL 101
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
 283-367 5.43e-06

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: 47.78  E-value: 5.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  283 WVNTQVKD-PVKNFTTDWNDGRVMCEIIKglgGSAPA--PEKLSTDPFHYENNIRKAV-DAGARLGVQPILTAKDMANPE 358
Cdd:cd21313    16 WIQNKIPYlPITNFNQNWQDGKALGALVD---SCAPGlcPDWESWDPQKPVDNAREAMqQADDWLGVPQVITPEEIIHPD 92


                  ....*....
gi 272432643  359 VEHLGIMAY 367
Cdd:cd21313    93 VDEHSVMTY 101
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 174-267 6.74e-06

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: 47.32  E-value: 6.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  174 RKLMLAWLQAAL---PDCRITNLTTDWNSGVNLAALLDYCQPGLFPHWRSLDPSqSVRNCTQAMDLAQREFGVPKVLEPE 250
Cdd:cd21238     4 KEKLLLWSQRMVegyQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQT-NLENLDQAFSVAERDLGVTRLLDPE 82

                          90
                  ....*....|....*..
gi 272432643  251 YLASPWLDELSGMTYLS 267
Cdd:cd21238    83 DVDVPQPDEKSIITYVS 99
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 65-165 8.62e-06

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: 47.27  E-value: 8.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   65 FRNWVNEHLRETGMQ--VHDWATDFCDGTCLCALVENLQTRPLKpSWNRRPANQHHYLENATTALKSIEADHIKLVNIGN 142
Cdd:cd21285    15 YTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKIE-DINGCPKNRSQMIENIDACLSFLAAKGINIQGLSA 93

                          90       100
                  ....*....|....*....|...
gi 272432643  143 VDIVNGNIKLILGLIWSLiVRYQ 165
Cdd:cd21285    94 EEIRNGNLKAILGLFFSL-SRYK 115
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 65-166 1.14e-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: 46.73  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   65 FRNWVNEHLRETgmQVHDWATDFCDGTCLCALVENLQtrPLKPSW---NRRP-ANQHHYLENATTALKSIEADHIKLVNI 140
Cdd:cd21299     9 FRLWINSLGIDT--YVNNVFEDVRDGWVLLEVLDKVS--PGSVNWkhaNKPPiKMPFKKVENCNQVVKIGKQLKFSLVNV 84

                          90       100
                  ....*....|....*....|....*.
gi 272432643  141 GNVDIVNGNIKLILGLIWSLIvRYQI 166
Cdd:cd21299    85 AGNDIVQGNKKLILALLWQLM-RYHM 109
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 61-166 1.38e-05

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 47.30  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   61 QANTFRNWVNEhlRETGMQVHDWATDFCDGTCLCALVENLQ-----TRPLKPSWNRRPANQHHyLENATTALK-SIEADH 134
Cdd:cd21331    23 EERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIKvpvdwNKVNKPPYPKLGANMKK-LENCNYAVElGKHPAK 99

                          90       100       110
                  ....*....|....*....|....*....|..
gi 272432643  135 IKLVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21331   100 FSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 65-165 2.95e-05

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: 45.41  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   65 FRNWVNEHLRETGMQ--VHDWATDFCDGTCLCALVENLQTRPLKpSWNRRPANQHHYLENATTALKSIEADHIKLVNIGN 142
Cdd:cd21286     5 YTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVE-DINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 83

                          90       100
                  ....*....|....*....|...
gi 272432643  143 VDIVNGNIKLILGLIWSLiVRYQ 165
Cdd:cd21286    84 EEIRNGNLKAILGLFFSL-SRYK 105
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 41-161 3.97e-05

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 46.19  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   41 EGTAAKG----MNIRGNEDLWVEIQANTFRNWVNEHLRETGMQVHDWATD---------FCDGTCLCALVENLQTRPL-K 106
Cdd:cd21323     1 EGITAIGgtsaISSEGTQHSYSEEEKVAFVNWINKALEGDPDCKHVVPMNptdeslfksLADGILLCKMINLSQPDTIdE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 272432643  107 PSWNRRPANQHHYLENATTALKSIEADHIKLVNIGNVDIVNGNIKLILGLIWSLI 161
Cdd:cd21323    81 RAINKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1220-1302 5.43e-05

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 44.13  E-value: 5.43e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   1220 PANTPAVFEILpppGQSLSKGECVATVLTPSKSKLNARVtHEAANGAARIEFVPTEVGTHVIDASINGTKIAGGPLIAKV 1299
Cdd:smart00557   15 VVGEPAEFTVD---TRDAGGGELEVEVTGPSGKKVPVEV-KDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ...
gi 272432643   1300 YDS 1302
Cdd:smart00557   91 GPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2187-2272 6.52e-05

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 43.82  E-value: 6.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  2187 VFDPTLVKITE--VSEAFCHRPASIGVSLNEAGqGDLSALVRC-GATEVPHTIRgPSKTGVYEIVYQPTRVAPHKISILF 2263
Cdd:pfam00630    1 AADASKVKASGpgLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGpDGSPVPVEVT-DNGDGTYTVSYTPTEPGDYTVSVKF 78


                   ....*....
gi 272432643  2264 NEVPISLKP 2272
Cdd:pfam00630   79 NGQHIPGSP 87
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 172-255 6.86e-05

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: 44.60  E-value: 6.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  172 PPRKLMLAWLQAAL-----PDCRITNLTTDWNSGVNLAALLDYCQPGLFPH---WRSLDPSQSVRNCTQAMDLAqREFGV 243
Cdd:cd21218    10 PPEEILLRWVNYHLkkagpTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKelvLEVLSEEDLEKRAEKVLQAA-EKLGC 88

                          90
                  ....*....|..
gi 272432643  244 PKVLEPEYLASP 255
Cdd:cd21218    89 KYFLTPEDIVSG 100
Filamin pfam00630
Filamin/ABP280 repeat;
468-554 1.17e-04

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 43.05  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   468 PRLLQVAPPGMAPCALGSLVEVLVNATGAPKTEDILVTavSPTGISHNCPLKKIDEG-HSAIFKPDEAGIWEIAITYQGR 546
Cdd:pfam00630    4 ASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEGEVEVT--GPDGSPVPVEVTDNGDGtYTVSYTPTEPGDYTVSVKFNGQ 81


                   ....*...
gi 272432643   547 HIQGGPFT 554
Cdd:pfam00630   82 HIPGSPFK 89
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 173-269 2.31e-04

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


Pssm-ID: 409075  Cd Length: 103  Bit Score: 42.84  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  173 PRKLMLAWLQAALPD---CRITNLTTDWNSGVNLAALLDYCQPGLFPHWRSLDPSQSVRnCTQAMDLAQREFGVPKVLEP 249
Cdd:cd21226     1 SEDGLLAWCRQTTEGydgVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEAR-LNLAFDFAEKKLGIPKLLEA 79

                          90       100
                  ....*....|....*....|
gi 272432643  250 EYLASPWLDELSGMTYLSYF 269
Cdd:cd21226    80 EDVMTGNPDERSIVLYTSLF 99
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
 162-267 2.51e-04

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: 42.73  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  162 VRYQIGRSKfppRKLMLAWLQ---AALPDCRITNLTTDWNSGVNLAALLDYCQPGLFPhWRSLDPSQSVRNCTQAMDLAQ 238
Cdd:cd21199     1 LARRYGGSK---RNALLKWCQektQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIP-YSELNPQDKRRNFTLAFKAAE 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 272432643  239 rEFGVPKVLEPEYLAS---PwlDELSGMTYLS 267
Cdd:cd21199    77 -SVGIPTTLTIDEMVSmerP--DWQSVMSYVT 105
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 292-367 2.93e-04

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: 42.41  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  292 VKNFTTDWNDGRVMCEIIKGLggsapAPEKL---STDPFHYENNIRKAVDAGARLGVQPILTAKDMANPEV-EHLGIMAY 367
Cdd:cd21198    22 ITNLTTSWRNGLAFCAILHHF-----RPDLIdfsSLSPHDIKENCKLAFDAAAKLGIPRLLDPADMVLLSVpDKLSVMTY 96
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 67-165 4.24e-04

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


Pssm-ID: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 42.34  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   67 NWVNEHLRETGMQVHDWATDFCDGTCLCALVENLQTR--PLKpSWNRRPANQHHYLENATTALKSIEADHIKLVNIGNVD 144
Cdd:cd21307    23 HFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFfiHLS-EFFLTPSSTSEMLHNVTLALELLKEGGLLNFPVNPED 101

                          90       100
                  ....*....|....*....|.
gi 272432643  145 IVNGNIKLILGLIWSLIVRYQ 165
Cdd:cd21307   102 IVNGDSKATIRVLYCLFSKYK 122
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 61-166 8.14e-04

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 41.90  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   61 QANTFRNWVNEhlRETGMQVHDWATDFCDGTCLCALVENLQT-----RPLKPSWNRRPANQHHyLENATTALkSIEADHI 135
Cdd:cd21330    14 EERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKVpvdwnRVNKPPYPKLGENMKK-LENCNYAV-ELGKNKA 89

                          90       100       110
                  ....*....|....*....|....*....|...
gi 272432643  136 K--LVNIGNVDIVNGNIKLILGLIWSLIVRYQI 166
Cdd:cd21330    90 KfsLVGIAGQDLNEGNRTLTLALIWQLMRRYTL 122
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 65-161 8.68e-04

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


Pssm-ID: 409141  Cd Length: 145  Bit Score: 42.27  E-value: 8.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   65 FRNWVNEHLRETG-------MQVHDWA--TDFCDGTCLCALV-----ENLQTRPLkpswNRRPANQHHYLENATTALKSI 130
Cdd:cd21292    29 FVNWINKNLGDDPdckhllpMDPNTDDlfEKVKDGILLCKMInlsvpDTIDERAI----NKKKLTVFTIHENLTLALNSA 104

                          90       100       110
                  ....*....|....*....|....*....|.
gi 272432643  131 EADHIKLVNIGNVDIVNGNIKLILGLIWSLI 161
Cdd:cd21292   105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 41-161 1.25e-03

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409174  Cd Length: 148  Bit Score: 41.97  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   41 EGTAAKG----MNIRGNEDLWVEIQANTFRNWVNE---------HLRETGMQVHDWATDFCDGTCLCALV-----ENLQT 102
Cdd:cd21325     1 EGICALGgtseLSSEGTQHSYSEEEKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMInlsvpDTIDE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 272432643  103 RPLkpswNRRPANQHHYLENATTALKSIEADHIKLVNIGNVDIVNGNIKLILGLIWSLI 161
Cdd:cd21325    81 RAI----NKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
Filamin pfam00630
Filamin/ABP280 repeat;
1210-1294 1.61e-03

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 39.96  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  1210 TALGESTRLVPANTPAVFEILPppgqSLSKGECVATVLTPSKSKLNARVTHEAaNGAARIEFVPTEVGTHVIDASINGTK 1289
Cdd:pfam00630    8 KASGPGLEPGVVGKPAEFTVDT----RDAGGEGEVEVTGPDGSPVPVEVTDNG-DGTYTVSYTPTEPGDYTVSVKFNGQH 82


                   ....*
gi 272432643  1290 IAGGP 1294
Cdd:pfam00630   83 IPGSP 87
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
 273-369 1.96e-03

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: 40.42  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  273 GGPGYNATMRWVNTQVKD----PVKNFTTDWNDGRVMCEIIKG-LGGSAPAPEKLSTDPFHyenNIRKAVDAGARLGVQP 347
Cdd:cd21199     6 GGSKRNALLKWCQEKTQGykgiDITNFSSSWNDGLAFCALLHSyLPDKIPYSELNPQDKRR---NFTLAFKAAESVGIPT 82

                          90       100
                  ....*....|....*....|...
gi 272432643  348 ILTAKDMANPEV-EHLGIMAYAA 369
Cdd:cd21199    83 TLTIDEMVSMERpDWQSVMSYVT 105
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2474-2561 2.13e-03

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 39.51  E-value: 2.13e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   2474 RAAGHGLEVCHRNKEASFVVYC--PIAPNVQIERLDEYGERIEPKIKALGNNEWRISYTILSVGKYEIRASCPNRgSLPG 2551
Cdd:smart00557    5 KASGPGLEKGVVGEPAEFTVDTrdAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE-HIPG 83

                            90
                    ....*....|
gi 272432643   2552 SPWHISCVES 2561
Cdd:smart00557   84 SPFTVKVGPA 93
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 274-369 2.21e-03

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: 40.10  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  274 GPGYNATMRWVNTQVKDP----VKNFTTDWNDGRVMCEIIKGLGGSAPAPEKLSTDPFHyeNNIRKAVD-AGARLGVQPI 348
Cdd:cd21192     2 GSAEKALLKWVQAEIGKYygirVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPR--DNLELAFRiAEQHLNIPRL 79

                          90       100
                  ....*....|....*....|.
gi 272432643  349 LTAKDMANPEVEHLGIMAYAA 369
Cdd:cd21192    80 LEVEDVLVDKPDERSIMTYVS 100
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 282-337 3.45e-03

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: 39.67  E-value: 3.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  282 RWVNTQV----KDPVKNFTTDWNDGRVMCEIIKGLGGSAPAPEKLSTDpFHYENNIRKAV 337
Cdd:cd21186     9 KWINSQLskanKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMR-VHHLNNVNRAL 67
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 174-250 4.10e-03

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: 39.25  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643  174 RKLMLAWLQA---ALPDCRITNLTTDWNSGVNLAALLDYCQPGLFpHWRSLDPSQSVRNCTQAMDLAQREFGVPKVLEPE 250
Cdd:cd21200     3 KQMLLEWCQAktrGYEHVDITNFSSSWSDGMAFCALIHHFFPDAF-DYSSLDPKNRRKNFELAFSTAEELADIAPLLEVE 81
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 54-160 4.32e-03

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: 39.71  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   54 EDLWVEIQANTFRNWVNEHLRETGmqVHDWATDFCDGTCLCALVENLQtrPLKPSW---NRRPANQH----HYLENATTA 126
Cdd:cd21300     1 FDAEGEREARVFTLWLNSLDVEPA--VNDLFEDLRDGLILLQAYDKVI--PGSVNWkkvNKAPASAEisrfKAVENTNYA 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 272432643  127 LKSIEADHIKLVNIGNVDIVNGNIKLILGLIWSL 160
Cdd:cd21300    77 VELGKQLGFSLVGIQGADITDGSRTLTLALVWQL 110
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 292-367 4.72e-03

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: 39.06  E-value: 4.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 272432643  292 VKNFTTDWNDGRVMCEIIKGLGGSAPAPEKLStdPFHYENNIRKAVDAGARLGVQPILTAKDMANPEV-EHLGIMAY 367
Cdd:cd21254    22 ITNFTTSWRNGLAFCAILHHFRPDLIDYKSLN--PHDIKENNKKAYDGFASLGISRLLEPSDMVLLAVpDKLTVMTY 96
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 66-150 7.65e-03

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: 38.44  E-value: 7.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   66 RNWVNEHLREtgMQVHDWATDFCDGTCLCALVENLQTRPlkPSW-NRRPANQHHYLENATTALKSIEADHIklvnIGNVD 144
Cdd:cd21185     7 LRWVRQLLPD--VDVNNFTTDWNDGRLLCGLVNALGGSV--PGWpNLDPEESENNIQRGLEAGKSLGVEPV----LTAEE 78


                  ....*.
gi 272432643  145 IVNGNI 150
Cdd:cd21185    79 MADPEV 84
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 52-161 8.55e-03

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409173  Cd Length: 145  Bit Score: 39.22  E-value: 8.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272432643   52 GNEDLWVEIQANTFRNWVNE---------HLRETGMQVHDWATDFCDGTCLCALV-----ENLQTRPLkpswNRRPANQH 117
Cdd:cd21324    16 GTQHSYSEEEKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMInfsvpDTIDERTI----NKKKLTPF 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 272432643  118 HYLENATTALKSIEADHIKLVNIGNVDIVNGNIKLILGLIWSLI 161
Cdd:cd21324    92 TIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
 
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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