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Conserved domains on  [gi|1734340282|ref|NP_001360666|]
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Calponin-homology (CH) domain-containing protein [Caenorhabditis elegans]

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 ...
 124-228 8.34e-64

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: 212.63  E-value: 8.34e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  124 KIPPKKLVMAWIQSALPELKLTNFRTNWNDGIALSALLEYCQPGLCPEWRNLDPSEARENCHRALLLAERYLEVPPIISS 203
Cdd:cd21229      1 KIPPKKLMLAWLQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSP 80

                           90       100
                   ....*....|....*....|....*
gi 1734340282  204 DHLSSPHLDELSCLTYLSYFITKGA 228
Cdd:cd21229     81 EDLSSPHLDELSGMTYLSYFMKEDG 105
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 12-119 1.27e-57

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: 195.20  E-value: 1.27e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   12 WIDIQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYyGKVYDQDPTEIQKLMNVQMALDALREDGVK 89
Cdd:cd21227      1 WVEIQKNTFTNWVNEQLKptGMSVEDLATDLEDGVKLIALVEILQGRKL-GRVIKKPLNQHQKLENVTLALKAMAEDGIK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 1734340282   90 TVNIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21227     80 LVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 3063-3157 2.44e-29

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 113.47  E-value: 2.44e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  3063 PSKVRVYGPGVEHGILSLfKSNFVVETRGAGAGQLTVRVRGPKGAfNVEMQREKKNERTIHCKYEPKEPGDYQVEVKWHG 3142
Cdd:smart00557    1 ASKVKASGPGLEKGVVGE-PAEFTVDTRDAGGGELEVEVTGPSGK-KVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 1734340282  3143 EHVPGSPFLVMIVDT 3157
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 229-329 1.13e-25

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


The actual alignment was detected with superfamily member cd21185:

Pssm-ID: 469584  Cd Length: 98  Bit Score: 103.54  E-value: 1.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  229 PGYRATLKKVSMLLPDCNVDDLEHSWSDGFLLAHLVEICGGRVPELERMRFDNlndFVENVAIVLDAAADIGVGSLIGAD 308
Cdd:cd21185      1 PGYKATLRWVRQLLPDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEE---SENNIQRGLEAGKSLGVEPVLTAE 77

                           90       100
                   ....*....|....*....|.
gi 1734340282  309 DIAEPQGEHLGTMALVAALCS 329
Cdd:cd21185     78 EMADPEVEHLGIMAYAAQLQK 98
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2969-3060 2.63e-22

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.44  E-value: 2.63e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2969 ADLIDVDASTLKIGIINENIKTLIDTRRAGSGQLSALCMGP-NKPAYCELYDHRDGTYALCVRPAEIGKHTLVIKYDDEH 3047
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 1734340282  3048 VKGSPFVVHVSLP 3060
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2874-2963 4.04e-21

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 90.36  E-value: 4.04e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2874 SRIMVRGDGLHRAVLKEHNEFIIDGSDINkEGRITATLLG-SKADIPVRIQQLGHNVYKATYTPLTGGTYELHILWNGKH 2952
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAG-GGELEVEVTGpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 1734340282  2953 VKGSPFAVSAD 2963
Cdd:smart00557   81 IPGSPFTVKVG 91
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2139-2222 2.02e-19

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 85.35  E-value: 2.02e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2139 PAKIKVGA--IPKGLLDKPVYFTVDASEAGVGNLEVAVC---EGRVPSMAHALGHHKYDISFVPKEDVDHTITVRFNNEP 2213
Cdd:smart00557    1 ASKVKASGpgLEKGVVGEPAEFTVDTRDAGGGELEVEVTgpsGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80


                    ....*....
gi 1734340282  2214 VPGSPFLCQ 2222
Cdd:smart00557   81 IPGSPFTVK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1893-1986 4.71e-19

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 84.19  E-value: 4.71e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  1893 ASEIIV-GEIPNQSNLNDTVEFTVDAGRAGFGNLEMAIKDADGVIIPSHVAQLESGSakFLVTFTPATKGPHTVNITFNK 1971
Cdd:smart00557    1 ASKVKAsGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGT--YTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 1734340282  1972 EVLKNSPFEVNIVDA 1986
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1023-1107 3.14e-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: 81.88  E-value: 3.14e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  1023 KVRLEPLGGGVPKQPVQFYVDAVEAGKGQLEISV---NQGKVPNNVQMQGAGRCLVTFIPQHAGTYVIDVTFNGEQVHGC 1099
Cdd:smart00557    5 KASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGS 84


                    ....*...
gi 1734340282  1100 PIKVEILP 1107
Cdd:smart00557   85 PFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 584-672 1.30e-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: 80.34  E-value: 1.30e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   584 VSFSGLtEPCSVGSIVEVVINAhGDAVSGSVYVEAVSPSGNVHRCTVRHQ-DNSYMATFTPQEVGLWRIGILYDGEHIRG 662
Cdd:smart00557    6 ASGPGL-EKGVVGEPAEFTVDT-RDAGGGELEVEVTGPSGKKVPVEVKDNgDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83

                            90
                    ....*....|
gi 1734340282   663 SPFACQVFDS 672
Cdd:smart00557   84 SPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2050-2139 1.79e-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: 79.96  E-value: 1.79e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2050 PAKTTVSkIPSL--SRVGQPSSLVVEVS--GHDQLEIRVLDSKKSEIGTDIVEIEPGHMQINFTPAQVGDHEIDVRYGGV 2125
Cdd:smart00557    1 ASKVKAS-GPGLekGVVGEPAEFTVDTRdaGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 1734340282  2126 PVTGSPFTCRAYDP 2139
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2329-2408 6.05e-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: 78.41  E-value: 6.05e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2329 NAVVGKPATFVIDAARSGAGNMEI-IVSVDNRNVPNFVQAEGQARFKVSFTPQDAKDHTISVKFNGISVPGSPLICSVSS 2407
Cdd:smart00557   13 KGVVGEPAEFTVDTRDAGGGELEVeVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGP 92


                    .
gi 1734340282  2408 A 2408
Cdd:smart00557   93 A 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 931-1016 6.93e-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: 6.93e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   931 YSELSGPGLVRAPVNRTAQFDITGEGLELSDIQAKISGPDNREYPIRIIPRSSGKYTAEYEIEQVGEHHLTVWIAGRKVD 1010
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82


                    ....*.
gi 1734340282  1011 GSPLSV 1016
Cdd:smart00557   83 GSPFTV 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2473-2554 7.94e-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: 7.94e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2473 LNSAQIGQKKGFTIDNINK-SSDCNVIITDPKGGPLPVRCYKQQDDSYWVEFTPEHLGTHTIEVTFGDVPVPGSPFKTEV 2551
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ...
gi 1734340282  2552 IDP 2554
Cdd:smart00557   91 GPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2650-2737 4.76e-16

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 75.72  E-value: 4.76e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2650 VYGAAVDQSIkIGEPASLIFDPKKTNGG-LKIHATGPDGQKVHHNVMRRPNGTSEVVFYPEETGTYNVSIDFNNRPITGS 2728
Cdd:smart00557    6 ASGPGLEKGV-VGEPAEFTVDTRDAGGGeLEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGS 84


                    ....*....
gi 1734340282  2729 PFTVNVVDP 2737
Cdd:smart00557   85 PFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2236-2319 4.18e-15

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


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 73.02  E-value: 4.18e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2236 LERIPVDEETEIQILT-DEIDSAPEARVRDPQGNDLPVNVtRSRENETlHIATYVPKCVGNHLIDIFLQGEPIAGSPFTA 2314
Cdd:smart00557   11 LEKGVVGEPAEFTVDTrDAGGGELEVEVTGPSGKKVPVEV-KDNGDGT-YTVSYTPTEPGDYTVTVKFGGEHIPGSPFTV 88


                    ....*
gi 1734340282  2315 KAYDA 2319
Cdd:smart00557   89 KVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 838-916 9.19e-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: 9.19e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   838 IQPSKLHTDHSFEIDASAAGSGNLEIMI---NGGRVPCRVRELGSRQYMAIFTPTQSMTHTIEMRFNGEHVSGSPWKLPV 914
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ..
gi 1734340282   915 ED 916
Cdd:smart00557   91 GP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 679-762 1.06e-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: 69.17  E-value: 1.06e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   679 GLDVGLVGQELNFSVNASQAGHGNLSVTVFR-HGREIPLSIEEQGSSkVHQVSFTPDGAGQYKIHVLFNRMEIKGSPFIL 757
Cdd:smart00557   10 GLEKGVVGEPAEFTVDTRDAGGGELEVEVTGpSGKKVPVEVKDNGDG-TYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTV 88


                    ....*
gi 1734340282   758 DIADA 762
Cdd:smart00557   89 KVGPA 93
IG_FLMN super family cl42963
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2571-2644 1.73e-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: 59.92  E-value: 1.73e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1734340282  2571 ATTINVDRRNAGNGELQVEITDPTGSPLRTEMLKSPGGEDRITFLPNQTGPHKINVKVAGFQIPGYPQTILVSE 2644
Cdd:smart00557   19 PAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGP 92
IG_FLMN super family cl42963
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2756-2832 1.49e-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: 1.49e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734340282  2756 RLGHSNSFDVDATAAGPGKLRAEVRDADSSLIGngPVVEDMGQGKYRVRFNPDQPGKYSIYLYWNELPVE-SAFPVRA 2832
Cdd:smart00557   15 VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVP--VEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPgSPFTVKV 90
IG_FLMN super family cl42963
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 762-826 1.03e-08

Filamin-type immunoglobulin 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: 54.92  E-value: 1.03e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   762 ASSVSVYGENLRSASVGKTASFMVHAIGAEAKDISAHVT----------------------------GEHSVDVMLADQR 813
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTgpsgkkvpvevkdngdgtytvsytptepGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 1734340282   814 VPDAPFACNVGAP 826
Cdd:smart00557   81 IPGSPFTVKVGPA 93
PTZ00121 super family cl31754
MAEBL; Provisional
 1478-1900 1.59e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1478 KKPNVPKKRATTPEGHVEPVNDNEEKDRQAFLRTQSEKVFEPVDAPLRRSDEKESIYDLPPQERLHKYPEEPTIALGEKA 1557
Cdd:PTZ00121  1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1558 NTSAIAAYTKGRQDDI---DEVSRNASFPSAPTINYNERSDEVSNYNRTKEDHYGVVGEYPTAPKIaysdsKEAVIREHY 1634
Cdd:PTZ00121  1524 ADEAKKAEEAKKADEAkkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA-----EEARIEEVM 1598

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1635 AQAKEDPYATVGECPPAPEISLRSDKLNETKNEYRRTTDSDQQDGKagppppviEISKAEQARRTEEYLRV-------KS 1707
Cdd:PTZ00121  1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE--------EKKKAEELKKAEEENKIkaaeeakKA 1670

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1708 EDDKILAKHgfTRKPEpsiEIQEPVTEQIRDDVVETAIAPEV------------PLRPVEELPHSPAPSSRSTPATTPKL 1775
Cdd:PTZ00121  1671 EEDKKKAEE--AKKAE---EDEKKAAEALKKEAEEAKKAEELkkkeaeekkkaeELKKAEEENKIKAEEAKKEAEEDKKK 1745

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1776 SAKFRKDGKEGKPFDFGKSKFVCKHDVIKRGKEVEVKlEGIKlgKEDQLRvvvlppankaipganggpPTEVDTKVKKSS 1855
Cdd:PTZ00121  1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE-EELD--EEDEKR------------------RMEVDKKIKDIF 1804

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1734340282 1856 SKYEIsfkpTEVGTHKVFAYVNDMQHPLSPFAVRVYDASEIIVGE 1900
Cdd:PTZ00121  1805 DNFAN----IIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
 
Name Accession Description Interval E-value
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 124-228 8.34e-64

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: 212.63  E-value: 8.34e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  124 KIPPKKLVMAWIQSALPELKLTNFRTNWNDGIALSALLEYCQPGLCPEWRNLDPSEARENCHRALLLAERYLEVPPIISS 203
Cdd:cd21229      1 KIPPKKLMLAWLQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSP 80

                           90       100
                   ....*....|....*....|....*
gi 1734340282  204 DHLSSPHLDELSCLTYLSYFITKGA 228
Cdd:cd21229     81 EDLSSPHLDELSGMTYLSYFMKEDG 105
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 12-119 1.27e-57

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: 195.20  E-value: 1.27e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   12 WIDIQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYyGKVYDQDPTEIQKLMNVQMALDALREDGVK 89
Cdd:cd21227      1 WVEIQKNTFTNWVNEQLKptGMSVEDLATDLEDGVKLIALVEILQGRKL-GRVIKKPLNQHQKLENVTLALKAMAEDGIK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 1734340282   90 TVNIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21227     80 LVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 3063-3157 2.44e-29

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 113.47  E-value: 2.44e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  3063 PSKVRVYGPGVEHGILSLfKSNFVVETRGAGAGQLTVRVRGPKGAfNVEMQREKKNERTIHCKYEPKEPGDYQVEVKWHG 3142
Cdd:smart00557    1 ASKVKASGPGLEKGVVGE-PAEFTVDTRDAGGGELEVEVTGPSGK-KVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 1734340282  3143 EHVPGSPFLVMIVDT 3157
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
11-242 9.44e-27

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 118.89  E-value: 9.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   11 KWIDIQLHTFTNWINEQLQGNV---IRDLTQDLSDGVNLIKLVEILQGRryyGKV-YDQDP-TEIQKLMNVQMALDALRE 85
Cdd:COG5069      5 KWQKVQKKTFTKWTNEKLISGGqkeFGDLDTDLKDGVKLAQLLEALQKD---NAGeYNETPeTRIHVMENVSGRLEFIKG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   86 DGVKTVNIGSHDIVDGNEKLILGLIWCLVQRYQIAcktKIPPKKLVMAWIQSAL----------PELKLTNFRTNWNDGI 155
Cdd:COG5069     82 KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIA---TINEEGELTKHINLLLwcdedtggykPEVDTFDFFRSWRDGL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  156 ALSALLEYCQP-GLCPEWRNLDPSEARENCHRALLLAERYLEVPPIISSDHLSSPHL-DELSCLTYLSYFITKgapgyRA 233
Cdd:COG5069    159 AFSALIHDSRPdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSWYIIR-----FG 233


                   ....*....
gi 1734340282  234 TLKKVSMLL 242
Cdd:COG5069    234 LLEKIDIAL 242
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 229-329 1.13e-25

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: 103.54  E-value: 1.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  229 PGYRATLKKVSMLLPDCNVDDLEHSWSDGFLLAHLVEICGGRVPELERMRFDNlndFVENVAIVLDAAADIGVGSLIGAD 308
Cdd:cd21185      1 PGYKATLRWVRQLLPDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEE---SENNIQRGLEAGKSLGVEPVLTAE 77

                           90       100
                   ....*....|....*....|.
gi 1734340282  309 DIAEPQGEHLGTMALVAALCS 329
Cdd:cd21185     78 EMADPEVEHLGIMAYAAQLQK 98
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 18-116 4.01e-25

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 102.01  E-value: 4.01e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282    18 HTFTNWINEQLQGN---VIRDLTQDLSDGVNLIKLVEILQGRRYYGKVYDQDPTEIQKLMNVQMALDALREDGVKTVNIG 94
Cdd:smart00033    1 KTLLRWVNSLLAEYdkpPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 1734340282    95 SHDIVDGNeKLILGLIWCLVQR 116
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
Filamin pfam00630
Filamin/ABP280 repeat;
3060-3150 3.24e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.20  E-value: 3.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 3060 PPDPSKVRVYGPGVEHGILSLfKSNFVVETRGAGaGQLTVRVRGPKGAFnVEMQREKKNERTIHCKYEPKEPGDYQVEVK 3139
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGK-PAEFTVDTRDAG-GEGEVEVTGPDGSP-VPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 1734340282 3140 WHGEHVPGSPF 3150
Cdd:pfam00630   78 FNGQHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2969-3060 2.63e-22

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.44  E-value: 2.63e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2969 ADLIDVDASTLKIGIINENIKTLIDTRRAGSGQLSALCMGP-NKPAYCELYDHRDGTYALCVRPAEIGKHTLVIKYDDEH 3047
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 1734340282  3048 VKGSPFVVHVSLP 3060
Cdd:smart00557   81 IPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2874-2963 4.04e-21

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 90.36  E-value: 4.04e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2874 SRIMVRGDGLHRAVLKEHNEFIIDGSDINkEGRITATLLG-SKADIPVRIQQLGHNVYKATYTPLTGGTYELHILWNGKH 2952
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAG-GGELEVEVTGpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 1734340282  2953 VKGSPFAVSAD 2963
Cdd:smart00557   81 IPGSPFTVKVG 91
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 18-119 5.42e-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: 5.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   18 HTFTNWINEQLQGN----VIRDLTQDLSDGVNLIKLVEILQ-GRRYYGKVYdqdPTEIQKLMNVQMALDALRED-GVKTV 91
Cdd:pfam00307    5 KELLRWINSHLAEYgpgvRVTNFTTDLRDGLALCALLNKLApGLVDKKKLN---KSEFDKLENINLALDVAEKKlGVPKV 81

                           90       100
                   ....*....|....*....|....*...
gi 1734340282   92 NIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:pfam00307   82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2139-2222 2.02e-19

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 85.35  E-value: 2.02e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2139 PAKIKVGA--IPKGLLDKPVYFTVDASEAGVGNLEVAVC---EGRVPSMAHALGHHKYDISFVPKEDVDHTITVRFNNEP 2213
Cdd:smart00557    1 ASKVKASGpgLEKGVVGEPAEFTVDTRDAGGGELEVEVTgpsGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80


                    ....*....
gi 1734340282  2214 VPGSPFLCQ 2222
Cdd:smart00557   81 IPGSPFTVK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1893-1986 4.71e-19

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 84.19  E-value: 4.71e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  1893 ASEIIV-GEIPNQSNLNDTVEFTVDAGRAGFGNLEMAIKDADGVIIPSHVAQLESGSakFLVTFTPATKGPHTVNITFNK 1971
Cdd:smart00557    1 ASKVKAsGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGT--YTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 1734340282  1972 EVLKNSPFEVNIVDA 1986
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1023-1107 3.14e-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: 81.88  E-value: 3.14e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  1023 KVRLEPLGGGVPKQPVQFYVDAVEAGKGQLEISV---NQGKVPNNVQMQGAGRCLVTFIPQHAGTYVIDVTFNGEQVHGC 1099
Cdd:smart00557    5 KASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGS 84


                    ....*...
gi 1734340282  1100 PIKVEILP 1107
Cdd:smart00557   85 PFTVKVGP 92
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 584-672 1.30e-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: 80.34  E-value: 1.30e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   584 VSFSGLtEPCSVGSIVEVVINAhGDAVSGSVYVEAVSPSGNVHRCTVRHQ-DNSYMATFTPQEVGLWRIGILYDGEHIRG 662
Cdd:smart00557    6 ASGPGL-EKGVVGEPAEFTVDT-RDAGGGELEVEVTGPSGKKVPVEVKDNgDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83

                            90
                    ....*....|
gi 1734340282   663 SPFACQVFDS 672
Cdd:smart00557   84 SPFTVKVGPA 93
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 129-223 1.66e-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: 80.05  E-value: 1.66e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   129 KLVMAWIQSALPE---LKLTNFRTNWNDGIALSALLEYCQPGLCPEW---RNLDPSEARENCHRALLLAERYLEVPPIIS 202
Cdd:smart00033    1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGLVDKKkvaASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|.
gi 1734340282   203 SDHLSSPHLDELSCLTYLSYF 223
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2050-2139 1.79e-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: 79.96  E-value: 1.79e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2050 PAKTTVSkIPSL--SRVGQPSSLVVEVS--GHDQLEIRVLDSKKSEIGTDIVEIEPGHMQINFTPAQVGDHEIDVRYGGV 2125
Cdd:smart00557    1 ASKVKAS-GPGLekGVVGEPAEFTVDTRdaGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 1734340282  2126 PVTGSPFTCRAYDP 2139
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2329-2408 6.05e-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: 78.41  E-value: 6.05e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2329 NAVVGKPATFVIDAARSGAGNMEI-IVSVDNRNVPNFVQAEGQARFKVSFTPQDAKDHTISVKFNGISVPGSPLICSVSS 2407
Cdd:smart00557   13 KGVVGEPAEFTVDTRDAGGGELEVeVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGP 92


                    .
gi 1734340282  2408 A 2408
Cdd:smart00557   93 A 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 931-1016 6.93e-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: 6.93e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   931 YSELSGPGLVRAPVNRTAQFDITGEGLELSDIQAKISGPDNREYPIRIIPRSSGKYTAEYEIEQVGEHHLTVWIAGRKVD 1010
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82


                    ....*.
gi 1734340282  1011 GSPLSV 1016
Cdd:smart00557   83 GSPFTV 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2473-2554 7.94e-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: 7.94e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2473 LNSAQIGQKKGFTIDNINK-SSDCNVIITDPKGGPLPVRCYKQQDDSYWVEFTPEHLGTHTIEVTFGDVPVPGSPFKTEV 2551
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ...
gi 1734340282  2552 IDP 2554
Cdd:smart00557   91 GPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2473-2548 1.22e-16

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 77.33  E-value: 1.22e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1734340282 2473 LNSAQIGQKKGFTIDNINKSSDCNVIITDPKGGPLPVRCYKQQDDSYWVEFTPEHLGTHTIEVTFGDVPVPGSPFK 2548
Cdd:pfam00630   14 LEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2650-2737 4.76e-16

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 75.72  E-value: 4.76e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2650 VYGAAVDQSIkIGEPASLIFDPKKTNGG-LKIHATGPDGQKVHHNVMRRPNGTSEVVFYPEETGTYNVSIDFNNRPITGS 2728
Cdd:smart00557    6 ASGPGLEKGV-VGEPAEFTVDTRDAGGGeLEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGS 84


                    ....*....
gi 1734340282  2729 PFTVNVVDP 2737
Cdd:smart00557   85 PFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2236-2319 4.18e-15

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 73.02  E-value: 4.18e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2236 LERIPVDEETEIQILT-DEIDSAPEARVRDPQGNDLPVNVtRSRENETlHIATYVPKCVGNHLIDIFLQGEPIAGSPFTA 2314
Cdd:smart00557   11 LEKGVVGEPAEFTVDTrDAGGGELEVEVTGPSGKKVPVEV-KDNGDGT-YTVSYTPTEPGDYTVTVKFGGEHIPGSPFTV 88


                    ....*
gi 1734340282  2315 KAYDA 2319
Cdd:smart00557   89 KVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 838-916 9.19e-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: 9.19e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   838 IQPSKLHTDHSFEIDASAAGSGNLEIMI---NGGRVPCRVRELGSRQYMAIFTPTQSMTHTIEMRFNGEHVSGSPWKLPV 914
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ..
gi 1734340282   915 ED 916
Cdd:smart00557   91 GP 92
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 126-227 1.14e-14

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: 72.32  E-value: 1.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  126 PPKKLVMAWIQSAL----PELKLTNFRTNWNDGIALSALLEYCQPGLCPEWR-NLDPSEARENCHRALLLAERYLEVPPI 200
Cdd:pfam00307    2 ELEKELLRWINSHLaeygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKLGVPKV 81

                           90       100
                   ....*....|....*....|....*...
gi 1734340282  201 -ISSDHLSSPhlDELSCLTYLSYFITKG 227
Cdd:pfam00307   82 lIEPEDLVEG--DNKSVLTYLASLFRRF 107
Filamin pfam00630
Filamin/ABP280 repeat;
2650-2731 2.15e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.78  E-value: 2.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2650 VYGAAVDQSiKIGEPASLIFDPKKTNGGLKIHATGPDGQKVHHNVMRRPNGTSEVVFYPEETGTYNVSIDFNNRPITGSP 2729
Cdd:pfam00630    9 ASGPGLEPG-VVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSP 87


                   ..
gi 1734340282 2730 FT 2731
Cdd:pfam00630   88 FK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2316-2400 4.46e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.01  E-value: 4.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2316 AYDARKTVLVPPA--NAVVGKPATFVIDAARSGaGNMEI-IVSVDNRNVPNFVQAEGQARFKVSFTPQDAKDHTISVKFN 2392
Cdd:pfam00630    1 AADASKVKASGPGlePGVVGKPAEFTVDTRDAG-GEGEVeVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*...
gi 1734340282 2393 GISVPGSP 2400
Cdd:pfam00630   80 GQHIPGSP 87
Filamin pfam00630
Filamin/ABP280 repeat;
2874-2958 5.86e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 69.63  E-value: 5.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2874 SRIMVRGDGLHRAVLKEHNEFIIDGSDinKEGRITATLLGSK-ADIPVRIQQLGHNVYKATYTPLTGGTYELHILWNGKH 2952
Cdd:pfam00630    5 SKVKASGPGLEPGVVGKPAEFTVDTRD--AGGEGEVEVTGPDgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQH 82


                   ....*.
gi 1734340282 2953 VKGSPF 2958
Cdd:pfam00630   83 IPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
2136-2219 9.82e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 68.85  E-value: 9.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2136 AYDPAKIKVG--AIPKGLLDKPVYFTVDASEAGvGNLEVAVCE---GRVPSMAHALGHHKYDISFVPKEDVDHTITVRFN 2210
Cdd:pfam00630    1 AADASKVKASgpGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGpdgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*....
gi 1734340282 2211 NEPVPGSPF 2219
Cdd:pfam00630   80 GQHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 679-762 1.06e-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: 69.17  E-value: 1.06e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   679 GLDVGLVGQELNFSVNASQAGHGNLSVTVFR-HGREIPLSIEEQGSSkVHQVSFTPDGAGQYKIHVLFNRMEIKGSPFIL 757
Cdd:smart00557   10 GLEKGVVGEPAEFTVDTRDAGGGELEVEVTGpSGKKVPVEVKDNGDG-TYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTV 88


                    ....*
gi 1734340282   758 DIADA 762
Cdd:smart00557   89 KVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
1022-1102 1.07e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 66.16  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1022 EKVRLEPLG--GGVPKQPVQFYVDAVEA-GKGQLEISVNQGK-VPNNVQMQGAGRCLVTFIPQHAGTYVIDVTFNGEQVH 1097
Cdd:pfam00630    5 SKVKASGPGlePGVVGKPAEFTVDTRDAgGEGEVEVTGPDGSpVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIP 84


                   ....*
gi 1734340282 1098 GCPIK 1102
Cdd:pfam00630   85 GSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
669-756 3.95e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 64.62  E-value: 3.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  669 VFDSGLVNVYGLDV--GLVGQELNFSVNASQAGhGNLSVTVF-RHGREIPLSIEEQGSSKvHQVSFTPDGAGQYKIHVLF 745
Cdd:pfam00630    1 AADASKVKASGPGLepGVVGKPAEFTVDTRDAG-GEGEVEVTgPDGSPVPVEVTDNGDGT-YTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 1734340282  746 NRMEIKGSPFI 756
Cdd:pfam00630   79 NGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
932-1013 4.03e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 64.62  E-value: 4.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  932 SELSGPGLVRAPVNRTAQFDITGEGlELSDIQAKISGPDNREYPIRIIPRSSGKYTAEYEIEQVGEHHLTVWIAGRKVDG 1011
Cdd:pfam00630    7 VKASGPGLEPGVVGKPAEFTVDTRD-AGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPG 85


                   ..
gi 1734340282 1012 SP 1013
Cdd:pfam00630   86 SP 87
Filamin pfam00630
Filamin/ABP280 repeat;
1890-1980 6.82e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 63.85  E-value: 6.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1890 VYDASEIIV-GEIPNQSNLNDTVEFTVDAGRAGfGNLEMAIKDADGVIIPSHVAQLESGSakFLVTFTPATKGPHTVNIT 1968
Cdd:pfam00630    1 AADASKVKAsGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGT--YTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 1734340282 1969 FNKEVLKNSPFE 1980
Cdd:pfam00630   78 FNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
578-665 2.72e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 61.92  E-value: 2.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  578 SPDVGLVSFSGL-TEPCSVGSIVEVVINAHGdaVSGSVYVEAVSPSGNVHRCTVR-HQDNSYMATFTPQEVGLWRIGILY 655
Cdd:pfam00630    1 AADASKVKASGPgLEPGVVGKPAEFTVDTRD--AGGEGEVEVTGPDGSPVPVEVTdNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|
gi 1734340282  656 DGEHIRGSPF 665
Cdd:pfam00630   79 NGQHIPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
2049-2133 5.23e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 61.15  E-value: 5.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2049 FPAKTTVSKiPSLS--RVGQPSSLVVEVSGHD-QLEIRVLDSKKSEIGTDIVEIEPGHMQINFTPAQVGDHEIDVRYGGV 2125
Cdd:pfam00630    3 DASKVKASG-PGLEpgVVGKPAEFTVDTRDAGgEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQ 81


                   ....*...
gi 1734340282 2126 PVTGSPFT 2133
Cdd:pfam00630   82 HIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2236-2313 1.10e-10

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 60.38  E-value: 1.10e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734340282 2236 LERIPVDEETEIQILTDEIDSAPEARVRDPQGNDLPVNVTrSRENETlHIATYVPKCVGNHLIDIFLQGEPIAGSPFT 2313
Cdd:pfam00630   14 LEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVT-DNGDGT-YTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2571-2644 1.73e-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: 59.92  E-value: 1.73e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1734340282  2571 ATTINVDRRNAGNGELQVEITDPTGSPLRTEMLKSPGGEDRITFLPNQTGPHKINVKVAGFQIPGYPQTILVSE 2644
Cdd:smart00557   19 PAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
2979-3054 2.05e-10

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 59.61  E-value: 2.05e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734340282 2979 LKIGIINENIKTLIDTRRAGsGQLSALCMGPN-KPAYCELYDHRDGTYALCVRPAEIGKHTLVIKYDDEHVKGSPFV 3054
Cdd:pfam00630   14 LEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
2551-2637 4.14e-10

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 58.84  E-value: 4.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2551 VIDPKNVEIRGLS-DQVLLRHATTINVDRRNAGnGELQVEITDPTGSPLRTEMLKSPGGEDRITFLPNQTGPHKINVKVA 2629
Cdd:pfam00630    1 AADASKVKASGPGlEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*...
gi 1734340282 2630 GFQIPGYP 2637
Cdd:pfam00630   80 GQHIPGSP 87
Filamin pfam00630
Filamin/ABP280 repeat;
838-911 1.03e-09

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 57.68  E-value: 1.03e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1734340282  838 IQPSKLHTDHSFEIDAS-AAGSGNLEIMI-NGGRVPCRVRELGSRQYMAIFTPTQSMTHTIEMRFNGEHVSGSPWK 911
Cdd:pfam00630   14 LEPGVVGKPAEFTVDTRdAGGEGEVEVTGpDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2756-2832 1.49e-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: 1.49e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734340282  2756 RLGHSNSFDVDATAAGPGKLRAEVRDADSSLIGngPVVEDMGQGKYRVRFNPDQPGKYSIYLYWNELPVE-SAFPVRA 2832
Cdd:smart00557   15 VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVP--VEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPgSPFTVKV 90
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 762-826 1.03e-08

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 54.92  E-value: 1.03e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   762 ASSVSVYGENLRSASVGKTASFMVHAIGAEAKDISAHVT----------------------------GEHSVDVMLADQR 813
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTgpsgkkvpvevkdngdgtytvsytptepGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 1734340282   814 VPDAPFACNVGAP 826
Cdd:smart00557   81 IPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2734-2824 1.03e-08

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 54.60  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2734 VVDPTKVIVNDLDMDRDgtlllRLGHSNSFDVDATAAGpGKLRAEVRDADSSLIGngPVVEDMGQGKYRVRFNPDQPGKY 2813
Cdd:pfam00630    1 AADASKVKASGPGLEPG-----VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVP--VEVTDNGDGTYTVSYTPTEPGDY 72

                           90
                   ....*....|.
gi 1734340282 2814 SIYLYWNELPV 2824
Cdd:pfam00630   73 TVSVKFNGQHI 83
Filamin pfam00630
Filamin/ABP280 repeat;
760-819 2.73e-06

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 48.05  E-value: 2.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  760 ADASSVSVYGENLRSASVGKTASFMVHA-----------IGAEAKDISAHVT----------------GEHSVDVMLADQ 812
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTrdaggegevevTGPDGSPVPVEVTdngdgtytvsytptepGDYTVSVKFNGQ 81


                   ....*..
gi 1734340282  813 RVPDAPF 819
Cdd:pfam00630   82 HIPGSPF 88
PTZ00121 PTZ00121
MAEBL; Provisional
 1478-1900 1.59e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1478 KKPNVPKKRATTPEGHVEPVNDNEEKDRQAFLRTQSEKVFEPVDAPLRRSDEKESIYDLPPQERLHKYPEEPTIALGEKA 1557
Cdd:PTZ00121  1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1558 NTSAIAAYTKGRQDDI---DEVSRNASFPSAPTINYNERSDEVSNYNRTKEDHYGVVGEYPTAPKIaysdsKEAVIREHY 1634
Cdd:PTZ00121  1524 ADEAKKAEEAKKADEAkkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA-----EEARIEEVM 1598

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1635 AQAKEDPYATVGECPPAPEISLRSDKLNETKNEYRRTTDSDQQDGKagppppviEISKAEQARRTEEYLRV-------KS 1707
Cdd:PTZ00121  1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE--------EKKKAEELKKAEEENKIkaaeeakKA 1670

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1708 EDDKILAKHgfTRKPEpsiEIQEPVTEQIRDDVVETAIAPEV------------PLRPVEELPHSPAPSSRSTPATTPKL 1775
Cdd:PTZ00121  1671 EEDKKKAEE--AKKAE---EDEKKAAEALKKEAEEAKKAEELkkkeaeekkkaeELKKAEEENKIKAEEAKKEAEEDKKK 1745

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1776 SAKFRKDGKEGKPFDFGKSKFVCKHDVIKRGKEVEVKlEGIKlgKEDQLRvvvlppankaipganggpPTEVDTKVKKSS 1855
Cdd:PTZ00121  1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE-EELD--EEDEKR------------------RMEVDKKIKDIF 1804

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1734340282 1856 SKYEIsfkpTEVGTHKVFAYVNDMQHPLSPFAVRVYDASEIIVGE 1900
Cdd:PTZ00121  1805 DNFAN----IIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1806-1893 2.37e-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: 45.29  E-value: 2.37e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  1806 GKEVEVKLEGIKLGkEDQLRVVVLPPANKaipganggpptEVDTKVK-KSSSKYEISFKPTEVGTHKVFAYVNDMQHPLS 1884
Cdd:smart00557   17 GEPAEFTVDTRDAG-GGELEVEVTGPSGK-----------KVPVEVKdNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGS 84


                    ....*....
gi 1734340282  1885 PFAVRVYDA 1893
Cdd:smart00557   85 PFTVKVGPA 93
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 242-327 4.80e-05

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: 44.97  E-value: 4.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  242 LPDCNVDDLEHSWSDGFLLAHLVEICggrVPELERMRFDNLNDF--VENVAIVLDAAA-DIGV-GSLIGADDIAEPQgeH 317
Cdd:pfam00307   19 GPGVRVTNFTTDLRDGLALCALLNKL---APGLVDKKKLNKSEFdkLENINLALDVAEkKLGVpKVLIEPEDLVEGD--N 93

                           90
                   ....*....|
gi 1734340282  318 LGTMALVAAL 327
Cdd:pfam00307   94 KSVLTYLASL 103
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 246-327 1.86e-04

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: 43.07  E-value: 1.86e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   246 NVDDLEHSWSDGFLLAHLVEI-----CGGRVPELERMRFDNLndfvENVAIVLDAAADIGV-GSLIGADDIAEpqGEHLg 319
Cdd:smart00033   18 PVTNFSSDLKDGVALCALLNSlspglVDKKKVAASLSRFKKI----ENINLALSFAEKLGGkVVLFEPEDLVE--GPKL- 90


                    ....*...
gi 1734340282   320 TMALVAAL 327
Cdd:smart00033   91 ILGVIWTL 98
Filamin pfam00630
Filamin/ABP280 repeat;
1836-1886 3.41e-04

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 41.89  E-value: 3.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1734340282 1836 IPGANGGP-PTEVdtkVKKSSSKYEISFKPTEVGTHKVFAYVNDMQHPLSPF 1886
Cdd:pfam00630   40 VTGPDGSPvPVEV---TDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
 
Name Accession Description Interval E-value
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 124-228 8.34e-64

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: 212.63  E-value: 8.34e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  124 KIPPKKLVMAWIQSALPELKLTNFRTNWNDGIALSALLEYCQPGLCPEWRNLDPSEARENCHRALLLAERYLEVPPIISS 203
Cdd:cd21229      1 KIPPKKLMLAWLQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSP 80

                           90       100
                   ....*....|....*....|....*
gi 1734340282  204 DHLSSPHLDELSCLTYLSYFITKGA 228
Cdd:cd21229     81 EDLSSPHLDELSGMTYLSYFMKEDG 105
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 12-119 1.27e-57

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: 195.20  E-value: 1.27e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   12 WIDIQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYyGKVYDQDPTEIQKLMNVQMALDALREDGVK 89
Cdd:cd21227      1 WVEIQKNTFTNWVNEQLKptGMSVEDLATDLEDGVKLIALVEILQGRKL-GRVIKKPLNQHQKLENVTLALKAMAEDGIK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 1734340282   90 TVNIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21227     80 LVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 126-223 8.88e-39

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: 140.83  E-value: 8.88e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  126 PPKKLVMAWIQSALPELKLTNFRTNWNDGIALSALLEYCQPGLCPEWRNLDPSEARENCHRALLLAERYLEVPPIISSDH 205
Cdd:cd21184      1 SGKSLLLEWVNSKIPEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMDIAEEELGIPKIITPED 80

                           90
                   ....*....|....*...
gi 1734340282  206 LSSPHLDELSCLTYLSYF 223
Cdd:cd21184     81 MVSPNVDELSVMTYLSYF 98
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 126-223 8.55e-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: 135.20  E-value: 8.55e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  126 PPKKLVMAWIQSALPELKLTNFRTNWNDGIALSALLEYCQPGLCPEWRNLDPSEARENCHRALLLAERYLEVPPIISSDH 205
Cdd:cd21230      1 TPKQRLLGWIQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALENATEAMQLAEDWLGVPQLITPEE 80

                           90
                   ....*....|....*...
gi 1734340282  206 LSSPHLDELSCLTYLSYF 223
Cdd:cd21230     81 IINPNVDEMSVMTYLSQF 98
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 12-117 7.15e-32

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: 121.35  E-value: 7.15e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   12 WIDIQLHTFTNWINEQLQGN--VIRDLTQDLSDGVNLIKLVEILqGRRYYGKvYDQDPT-EIQKLMNVQMALDALREDGV 88
Cdd:cd21215      1 WVDVQKKTFTKWLNTKLSSRglSITDLVTDLSDGVRLIQLLEII-GDESLGR-YNKNPKmRVQKLENVNKALEFIKSRGV 78

                           90       100
                   ....*....|....*....|....*....
gi 1734340282   89 KTVNIGSHDIVDGNEKLILGLIWCLVQRY 117
Cdd:cd21215     79 KLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 12-117 8.39e-32

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: 121.43  E-value: 8.39e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   12 WIDIQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYYGKvYDQDPT-EIQKLMNVQMALDALREDGV 88
Cdd:cd21183      1 WKRIQANTFTRWCNEHLKerGMQIHDLATDFSDGLCLIALLENLSTRPLKRS-YNRRPAfQQHYLENVSTALKFIEADHI 79

                           90       100
                   ....*....|....*....|....*....
gi 1734340282   89 KTVNIGSHDIVDGNEKLILGLIWCLVQRY 117
Cdd:cd21183     80 KLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 127-223 1.54e-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: 1.54e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  127 PKKLVMAWIQSALPELKLTNFRTNWNDGIALSALLEYCQPGLCPEWRNLDPSEARENCHRALLLAERYLEVPPIISSDHL 206
Cdd:cd21315     17 PKQRLLGWIQSKVPDLPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIKPEEM 96

                           90
                   ....*....|....*..
gi 1734340282  207 SSPHLDELSCLTYLSYF 223
Cdd:cd21315     97 VNPKVDELSMMTYLSQF 113
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
 124-223 1.43e-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: 1.43e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  124 KIPPKKLVMAWIQSALPELKLTNFRTNWNDGIALSALLEYCQPGLCPEWRNLDPSEARENCHRALLLAERYLEVPPIISS 203
Cdd:cd21314      9 KQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPVQNAREAMQQADDWLGVPQVIAP 88

                           90       100
                   ....*....|....*....|
gi 1734340282  204 DHLSSPHLDELSCLTYLSYF 223
Cdd:cd21314     89 EEIVDPNVDEHSVMTYLSQF 108
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 3063-3157 2.44e-29

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 113.47  E-value: 2.44e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  3063 PSKVRVYGPGVEHGILSLfKSNFVVETRGAGAGQLTVRVRGPKGAfNVEMQREKKNERTIHCKYEPKEPGDYQVEVKWHG 3142
Cdd:smart00557    1 ASKVKASGPGLEKGVVGE-PAEFTVDTRDAGGGELEVEVTGPSGK-KVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 1734340282  3143 EHVPGSPFLVMIVDT 3157
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 12-120 3.99e-29

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: 114.09  E-value: 3.99e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   12 WIDIQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYygKVYDQDPT-EIQKLMNVQMALDALRED-G 87
Cdd:cd21311     12 WKRIQQNTFTRWANEHLKtaNKHIADLETDLSDGLRLIALVEVLSGKKF--PKFNKRPTfRSQKLENVSVALKFLEEDeG 89

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1734340282   88 VKTVNIGSHDIVDGNEKLILGLIWCLVQRYQIA 120
Cdd:cd21311     90 IKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 15-118 6.19e-29

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: 112.88  E-value: 6.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   15 IQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQG---RRYYGKvydqdpTEIQKLMNVQMALDALREDGVK 89
Cdd:cd21188      3 VQKKTFTKWVNKHLIkaRRRVVDLFEDLRDGHNLISLLEVLSGeslPRERGR------MRFHRLQNVQTALDFLKYRKIK 76

                           90       100
                   ....*....|....*....|....*....
gi 1734340282   90 TVNIGSHDIVDGNEKLILGLIWCLVQRYQ 118
Cdd:cd21188     77 LVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 12-117 1.49e-27

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: 109.11  E-value: 1.49e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   12 WIDIQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYYgKVYDQDPT-EIQKLMNVQMALDALREDGV 88
Cdd:cd21228      1 WKKIQQNTFTRWCNEHLKcvNKRIYNLETDLSDGLRLIALLEVLSQKRMY-KKYNKRPTfRQMKLENVSVALEFLERESI 79

                           90       100
                   ....*....|....*....|....*....
gi 1734340282   89 KTVNIGSHDIVDGNEKLILGLIWCLVQRY 117
Cdd:cd21228     80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 15-116 9.05e-27

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: 107.07  E-value: 9.05e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   15 IQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYygkvydQDPTE----IQKLMNVQMALDALREDGV 88
Cdd:cd21246     16 VQKKTFTKWVNSHLArvGCRINDLYTDLRDGRMLIKLLEVLSGERL------PKPTKgkmrIHCLENVDKALQFLKEQRV 89

                           90       100
                   ....*....|....*....|....*...
gi 1734340282   89 KTVNIGSHDIVDGNEKLILGLIWCLVQR 116
Cdd:cd21246     90 HLENMGSHDIVDGNHRLTLGLIWTIILR 117
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
11-242 9.44e-27

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 118.89  E-value: 9.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   11 KWIDIQLHTFTNWINEQLQGNV---IRDLTQDLSDGVNLIKLVEILQGRryyGKV-YDQDP-TEIQKLMNVQMALDALRE 85
Cdd:COG5069      5 KWQKVQKKTFTKWTNEKLISGGqkeFGDLDTDLKDGVKLAQLLEALQKD---NAGeYNETPeTRIHVMENVSGRLEFIKG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   86 DGVKTVNIGSHDIVDGNEKLILGLIWCLVQRYQIAcktKIPPKKLVMAWIQSAL----------PELKLTNFRTNWNDGI 155
Cdd:COG5069     82 KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIA---TINEEGELTKHINLLLwcdedtggykPEVDTFDFFRSWRDGL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  156 ALSALLEYCQP-GLCPEWRNLDPSEARENCHRALLLAERYLEVPPIISSDHLSSPHL-DELSCLTYLSYFITKgapgyRA 233
Cdd:COG5069    159 AFSALIHDSRPdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVNVSIpDERSIMTYVSWYIIR-----FG 233


                   ....*....
gi 1734340282  234 TLKKVSMLL 242
Cdd:COG5069    234 LLEKIDIAL 242
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
 127-223 1.55e-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: 1.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  127 PKKLVMAWIQSALPELKLTNFRTNWNDGIALSALLEYCQPGLCPEWRNLDPSEARENCHRALLLAERYLEVPPIISSDHL 206
Cdd:cd21313      9 PKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPQKPVDNAREAMQQADDWLGVPQVITPEEI 88

                           90
                   ....*....|....*..
gi 1734340282  207 SSPHLDELSCLTYLSYF 223
Cdd:cd21313     89 IHPDVDEHSVMTYLSQF 105
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 229-329 1.13e-25

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: 103.54  E-value: 1.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  229 PGYRATLKKVSMLLPDCNVDDLEHSWSDGFLLAHLVEICGGRVPELERMRFDNlndFVENVAIVLDAAADIGVGSLIGAD 308
Cdd:cd21185      1 PGYKATLRWVRQLLPDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEE---SENNIQRGLEAGKSLGVEPVLTAE 77

                           90       100
                   ....*....|....*....|.
gi 1734340282  309 DIAEPQGEHLGTMALVAALCS 329
Cdd:cd21185     78 EMADPEVEHLGIMAYAAQLQK 98
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 6-116 2.08e-25

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: 103.14  E-value: 2.08e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282    6 EEARQKWIDIQLHTFTNWINEQLQGN--VIRDLTQDLSDGVNLIKLVEILQGRRYyGKvydqdPTE----IQKLMNVQMA 79
Cdd:cd21193      7 RALQEERINIQKKTFTKWINSFLEKAnlEIGDLFTDLSDGKLLLKLLEIISGEKL-GK-----PNRgrlrVQKIENVNKA 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1734340282   80 LDALREDgVKTVNIGSHDIVDGNEKLILGLIWCLVQR 116
Cdd:cd21193     81 LAFLKTK-VRLENIGAEDIVDGNPRLILGLIWTIILR 116
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 14-119 2.22e-25

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: 102.85  E-value: 2.22e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   14 DIQLHTFTNWINEQL---QGNVIRDLTQDLSDGVNLIKLVEILQGRRYYGkvyDQDPTEIQKLMNVQMALDALREDGVKT 90
Cdd:cd21186      1 DVQKKTFTKWINSQLskaNKPPIKDLFEDLRDGTRLLALLEVLTGKKLKP---EKGRMRVHHLNNVNRALQVLEQNNVKL 77

                           90       100
                   ....*....|....*....|....*....
gi 1734340282   91 VNIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21186     78 VNISSNDIVDGNPKLTLGLVWSIILHWQV 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 18-116 4.01e-25

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 102.01  E-value: 4.01e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282    18 HTFTNWINEQLQGN---VIRDLTQDLSDGVNLIKLVEILQGRRYYGKVYDQDPTEIQKLMNVQMALDALREDGVKTVNIG 94
Cdd:smart00033    1 KTLLRWVNSLLAEYdkpPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 1734340282    95 SHDIVDGNeKLILGLIWCLVQR 116
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 12-120 1.95e-24

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: 100.88  E-value: 1.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   12 WIDIQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYYGKVYDQDPTEIQKLMNVQMALDALREDGVK 89
Cdd:cd21310     13 WKKIQQNTFTRWCNEHLKcvQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQMKLENVSVALEFLDREHIK 92

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1734340282   90 TVNIGSHDIVDGNEKLILGLIWCLVQRYQIA 120
Cdd:cd21310     93 LVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
 124-223 1.21e-23

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: 98.34  E-value: 1.21e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  124 KIPPKKLVMAWIQSALPELKLTNFRTNWNDGIALSALLEYCQPGLCPEWRNLDPSEARENCHRALLLAERYLEVPPIISS 203
Cdd:cd21312     10 KQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITP 89

                           90       100
                   ....*....|....*....|
gi 1734340282  204 DHLSSPHLDELSCLTYLSYF 223
Cdd:cd21312     90 EEIVDPNVDEHSVMTYLSQF 109
Filamin pfam00630
Filamin/ABP280 repeat;
3060-3150 3.24e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 96.20  E-value: 3.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 3060 PPDPSKVRVYGPGVEHGILSLfKSNFVVETRGAGaGQLTVRVRGPKGAFnVEMQREKKNERTIHCKYEPKEPGDYQVEVK 3139
Cdd:pfam00630    1 AADASKVKASGPGLEPGVVGK-PAEFTVDTRDAG-GEGEVEVTGPDGSP-VPVEVTDNGDGTYTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|.
gi 1734340282 3140 WHGEHVPGSPF 3150
Cdd:pfam00630   78 FNGQHIPGSPF 88
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 12-114 6.67e-23

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: 95.92  E-value: 6.67e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   12 WIDIQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYYGKvyDQDPTEIQKLMNVQMALDALREDGVK 89
Cdd:cd21214      2 WEKQQRKTFTAWCNSHLRkaGTQIENIEEDFRDGLKLMLLLEVISGERLPKP--ERGKMRFHKIANVNKALDFIASKGVK 79

                           90       100
                   ....*....|....*....|....*
gi 1734340282   90 TVNIGSHDIVDGNEKLILGLIWCLV 114
Cdd:cd21214     80 LVSIGAEEIVDGNLKMTLGMIWTII 104
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 12-120 1.06e-22

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: 96.31  E-value: 1.06e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   12 WIDIQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYYGKvYDQDPTEIQ-KLMNVQMALDALREDGV 88
Cdd:cd21308     17 WKKIQQNTFTRWCNEHLKcvSKRIANLQTDLSDGLRLIALLEVLSQKKMHRK-HNQRPTFRQmQLENVSVALEFLDRESI 95

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1734340282   89 KTVNIGSHDIVDGNEKLILGLIWCLVQRYQIA 120
Cdd:cd21308     96 KLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 12-120 1.40e-22

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: 95.92  E-value: 1.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   12 WIDIQLHTFTNWINEQLQG--NVIRDLTQDLSDGVNLIKLVEILQGRRYYGKvYDQDPTEIQ-KLMNVQMALDALREDGV 88
Cdd:cd21309     14 WKKIQQNTFTRWCNEHLKCvnKRIGNLQTDLSDGLRLIALLEVLSQKRMYRK-YHQRPTFRQmQLENVSVALEFLDRESI 92

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1734340282   89 KTVNIGSHDIVDGNEKLILGLIWCLVQRYQIA 120
Cdd:cd21309     93 KLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 14-119 1.72e-22

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: 94.94  E-value: 1.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   14 DIQLHTFTNWINEQLQGN----VIRDLTQDLSDGVNLIKLVEILQGrryygkvyDQDPTE-------IQKLMNVQMALDA 82
Cdd:cd21190      4 RVQKKTFTNWINSHLAKLsqpiVINDLFVDIKDGTALLRLLEVLSG--------QKLPIEsgrvlqrAHKLSNIRNALDF 75

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1734340282   83 LREDGVKTVNIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21190     76 LTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2969-3060 2.63e-22

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.44  E-value: 2.63e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2969 ADLIDVDASTLKIGIINENIKTLIDTRRAGSGQLSALCMGP-NKPAYCELYDHRDGTYALCVRPAEIGKHTLVIKYDDEH 3047
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPsGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 1734340282  3048 VKGSPFVVHVSLP 3060
Cdd:smart00557   81 IPGSPFTVKVGPA 93
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 15-120 3.94e-22

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


Pssm-ID: 409085  Cd Length: 128  Bit Score: 94.28  E-value: 3.94e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   15 IQLHTFTNWINEQLQG--NVIRDLTQDLSDGVNLIKLVEILQGR---RYYGKVydqdptEIQKLMNVQMALDALREDGVK 89
Cdd:cd21236     17 VQKKTFTKWINQHLMKvrKHVNDLYEDLRDGHNLISLLEVLSGDtlpREKGRM------RFHRLQNVQIALDYLKRRQVK 90

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1734340282   90 TVNIGSHDIVDGNEKLILGLIWCLVQRYQIA 120
Cdd:cd21236     91 LVNIRNDDITDGNPKLTLGLIWTIILHFQIS 121
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 14-119 4.54e-22

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


Pssm-ID: 409080  Cd Length: 111  Bit Score: 93.45  E-value: 4.54e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   14 DIQLHTFTNWINEQLQG---NVIRDLTQDLSDGVNLIKLVEILQGRRYygkVYDQDPTEIQKLMNVQMALDALREDGVKT 90
Cdd:cd21231      5 DVQKKTFTKWINAQFAKfgkPPIEDLFTDLQDGRRLLELLEGLTGQKL---VKEKGSTRVHALNNVNKALQVLQKNNVDL 81

                           90       100
                   ....*....|....*....|....*....
gi 1734340282   91 VNIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21231     82 VNIGSADIVDGNHKLTLGLIWSIILHWQV 110
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2874-2963 4.04e-21

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 90.36  E-value: 4.04e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2874 SRIMVRGDGLHRAVLKEHNEFIIDGSDINkEGRITATLLG-SKADIPVRIQQLGHNVYKATYTPLTGGTYELHILWNGKH 2952
Cdd:smart00557    2 SKVKASGPGLEKGVVGEPAEFTVDTRDAG-GGELEVEVTGpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80

                            90
                    ....*....|.
gi 1734340282  2953 VKGSPFAVSAD 2963
Cdd:smart00557   81 IPGSPFTVKVG 91
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 18-119 5.42e-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: 5.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   18 HTFTNWINEQLQGN----VIRDLTQDLSDGVNLIKLVEILQ-GRRYYGKVYdqdPTEIQKLMNVQMALDALRED-GVKTV 91
Cdd:pfam00307    5 KELLRWINSHLAEYgpgvRVTNFTTDLRDGLALCALLNKLApGLVDKKKLN---KSEFDKLENINLALDVAEKKlGVPKV 81

                           90       100
                   ....*....|....*....|....*...
gi 1734340282   92 NIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:pfam00307   82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 15-120 1.05e-20

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: 90.08  E-value: 1.05e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   15 IQLHTFTNWINEQL--QGNVIRDLTQDLSDGVNLIKLVEILQGR---RYYGKVydqdptEIQKLMNVQMALDALREDGVK 89
Cdd:cd21235      6 VQKKTFTKWVNKHLikAQRHISDLYEDLRDGHNLISLLEVLSGDslpREKGRM------RFHKLQNVQIALDYLRHRQVK 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1734340282   90 TVNIGSHDIVDGNEKLILGLIWCLVQRYQIA 120
Cdd:cd21235     80 LVNIRNDDIADGNPKLTLGLIWTIILHFQIS 110
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 12-118 1.21e-20

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: 89.51  E-value: 1.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   12 WIDIQLHTFTNWINEQLQ---GNVIRDLTQDLSDGVNLIKLVEILQGRRyYGKVYDQDP-TEIQKLMNVQMALDALRED- 86
Cdd:cd21225      1 WEKVQIKAFTAWVNSVLEkrgIPKISDLATDLSDGVRLIFFLELVSGKK-FPKKFDLEPkNRIQMIQNLHLAMLFIEEDl 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1734340282   87 GVKTVNIGSHDIVDGNEKLILGLIWCLVQRYQ 118
Cdd:cd21225     80 KIRVQGIGAEDFVDNNKKLILGLLWTLYRKYR 111
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 15-116 1.53e-20

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: 90.11  E-value: 1.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   15 IQLHTFTNWINEQLQGNVIR--DLTQDLSDGVNLIKLVEILQGRRYygkvydQDPTE----IQKLMNVQMALDALREDGV 88
Cdd:cd21317     31 VQKKTFTKWVNSHLARVTCRigDLYTDLRDGRMLIRLLEVLSGEQL------PKPTKgrmrIHCLENVDKALQFLKEQKV 104

                           90       100
                   ....*....|....*....|....*...
gi 1734340282   89 KTVNIGSHDIVDGNEKLILGLIWCLVQR 116
Cdd:cd21317    105 HLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 126-224 3.65e-20

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


Pssm-ID: 409034  Cd Length: 98  Bit Score: 87.74  E-value: 3.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  126 PPKKLVMAWIQSALPELKLTNFRTNWNDGIALSALLEYCQpGLCPEWRNLDPSEARENCHRALLLAERyLEVPPIISSDH 205
Cdd:cd21185      1 PGYKATLRWVRQLLPDVDVNNFTTDWNDGRLLCGLVNALG-GSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEE 78

                           90
                   ....*....|....*....
gi 1734340282  206 LSSPHLDELSCLTYLSYFI 224
Cdd:cd21185     79 MADPEVEHLGIMAYAAQLQ 97
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 15-120 6.51e-20

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


Pssm-ID: 409086  Cd Length: 118  Bit Score: 87.78  E-value: 6.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   15 IQLHTFTNWINEQLQG--NVIRDLTQDLSDGVNLIKLVEILQGRRYygkVYDQDPTEIQKLMNVQMALDALREDGVKTVN 92
Cdd:cd21237      6 VQKKTFTKWVNKHLMKvrKHINDLYEDLRDGHNLISLLEVLSGVKL---PREKGRMRFHRLQNVQIALDFLKQRQVKLVN 82

                           90       100
                   ....*....|....*....|....*...
gi 1734340282   93 IGSHDIVDGNEKLILGLIWCLVQRYQIA 120
Cdd:cd21237     83 IRNDDITDGNPKLTLGLIWTIILHFQIS 110
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 15-116 1.36e-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: 87.77  E-value: 1.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   15 IQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYygkvydQDPTE----IQKLMNVQMALDALREDGV 88
Cdd:cd21318     38 VQKKTFTKWVNSHLArvPCRINDLYTDLRDGYVLTRLLEVLSGEQL------PKPTRgrmrIHSLENVDKALQFLKEQRV 111

                           90       100
                   ....*....|....*....|....*...
gi 1734340282   89 KTVNIGSHDIVDGNEKLILGLIWCLVQR 116
Cdd:cd21318    112 HLENVGSHDIVDGNHRLTLGLIWTIILR 139
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2139-2222 2.02e-19

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 85.35  E-value: 2.02e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2139 PAKIKVGA--IPKGLLDKPVYFTVDASEAGVGNLEVAVC---EGRVPSMAHALGHHKYDISFVPKEDVDHTITVRFNNEP 2213
Cdd:smart00557    1 ASKVKASGpgLEKGVVGEPAEFTVDTRDAGGGELEVEVTgpsGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEH 80


                    ....*....
gi 1734340282  2214 VPGSPFLCQ 2222
Cdd:smart00557   81 IPGSPFTVK 89
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 14-119 3.83e-19

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


Pssm-ID: 409091  Cd Length: 111  Bit Score: 85.27  E-value: 3.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   14 DIQLHTFTNWINEQLQGN----VIRDLTQDLSDGVNLIKLVEILQGRRYygkvydqdPTE-----IQKLMNVQMALDALR 84
Cdd:cd21242      4 QTQKRTFTNWINSQLAKHsppsVVSDLFTDIQDGHRLLDLLEVLSGQQL--------PREkghnvFQCRSNIETALSFLK 75

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1734340282   85 EDGVKTVNIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21242     76 NKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 15-119 4.50e-19

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: 85.12  E-value: 4.50e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   15 IQLHTFTNWINEQLQGN----VIRDLTQDLSDGVNLIKLVEILQGRRY---YGKVYDQdpteIQKLMNVQMALDALREDG 87
Cdd:cd21241      5 VQKKTFTNWINSYLAKRkppmKVEDLFEDIKDGTKLLALLEVLSGEKLpceKGRRLKR----VHFLSNINTALKFLESKK 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1734340282   88 VKTVNIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21241     81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1893-1986 4.71e-19

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 84.19  E-value: 4.71e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  1893 ASEIIV-GEIPNQSNLNDTVEFTVDAGRAGFGNLEMAIKDADGVIIPSHVAQLESGSakFLVTFTPATKGPHTVNITFNK 1971
Cdd:smart00557    1 ASKVKAsGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGT--YTVSYTPTEPGDYTVTVKFGG 78

                            90
                    ....*....|....*
gi 1734340282  1972 EVLKNSPFEVNIVDA 1986
Cdd:smart00557   79 EHIPGSPFTVKVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1023-1107 3.14e-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: 81.88  E-value: 3.14e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  1023 KVRLEPLGGGVPKQPVQFYVDAVEAGKGQLEISV---NQGKVPNNVQMQGAGRCLVTFIPQHAGTYVIDVTFNGEQVHGC 1099
Cdd:smart00557    5 KASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGS 84


                    ....*...
gi 1734340282  1100 PIKVEILP 1107
Cdd:smart00557   85 PFTVKVGP 92
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 15-116 1.16e-17

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: 82.40  E-value: 1.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   15 IQLHTFTNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYygkvydQDPTE----IQKLMNVQMALDALREDGV 88
Cdd:cd21316     53 VQKKTFTKWVNSHLArvSCRITDLYMDLRDGRMLIKLLEVLSGERL------PKPTKgrmrIHCLENVDKALQFLKEQRV 126

                           90       100
                   ....*....|....*....|....*...
gi 1734340282   89 KTVNIGSHDIVDGNEKLILGLIWCLVQR 116
Cdd:cd21316    127 HLENMGSHDIVDGNHRLTLGLIWTIILR 154
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 14-119 1.26e-17

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


Pssm-ID: 409081  Cd Length: 107  Bit Score: 80.82  E-value: 1.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   14 DIQLHTFTNWINEQLQGN---VIRDLTQDLSDGVNLIKLVEILQGRRYygkVYDQDPTEIQKLMNVQMALDALREDGVKT 90
Cdd:cd21232      1 DVQKKTFTKWINARFSKSgkpPIKDMFTDLRDGRKLLDLLEGLTGKSL---PKERGSTRVHALNNVNRVLQVLHQNNVEL 77

                           90       100
                   ....*....|....*....|....*....
gi 1734340282   91 VNIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21232     78 VNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 584-672 1.30e-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: 80.34  E-value: 1.30e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   584 VSFSGLtEPCSVGSIVEVVINAhGDAVSGSVYVEAVSPSGNVHRCTVRHQ-DNSYMATFTPQEVGLWRIGILYDGEHIRG 662
Cdd:smart00557    6 ASGPGL-EKGVVGEPAEFTVDT-RDAGGGELEVEVTGPSGKKVPVEVKDNgDGTYTVSYTPTEPGDYTVTVKFGGEHIPG 83

                            90
                    ....*....|
gi 1734340282   663 SPFACQVFDS 672
Cdd:smart00557   84 SPFTVKVGPA 93
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 129-223 1.66e-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: 80.05  E-value: 1.66e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   129 KLVMAWIQSALPE---LKLTNFRTNWNDGIALSALLEYCQPGLCPEW---RNLDPSEARENCHRALLLAERYLEVPPIIS 202
Cdd:smart00033    1 KTLLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGLVDKKkvaASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|.
gi 1734340282   203 SDHLSSPHLDELSCLTYLSYF 223
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2050-2139 1.79e-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: 79.96  E-value: 1.79e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2050 PAKTTVSkIPSL--SRVGQPSSLVVEVS--GHDQLEIRVLDSKKSEIGTDIVEIEPGHMQINFTPAQVGDHEIDVRYGGV 2125
Cdd:smart00557    1 ASKVKAS-GPGLekGVVGEPAEFTVDTRdaGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGE 79

                            90
                    ....*....|....
gi 1734340282  2126 PVTGSPFTCRAYDP 2139
Cdd:smart00557   80 HIPGSPFTVKVGPA 93
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 20-117 2.61e-17

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


Pssm-ID: 409061  Cd Length: 105  Bit Score: 79.93  E-value: 2.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   20 FTNWINEQLQ----GNVIRDLTQDLSDGVNLIKLVEILQGRRYyGKVYDQDPTEIQKLMNVQMALDALREDGVKTVNIGS 95
Cdd:cd21212      5 YTDWANHYLEkgghKRIITDLQKDLGDGLTLVNLIEAVAGEKV-PGIHSRPKTRAQKLENIQACLQFLAALGVDVQGITA 83

                           90       100
                   ....*....|....*....|..
gi 1734340282   96 HDIVDGNEKLILGLIWCLVQRY 117
Cdd:cd21212     84 EDIVDGNLKAILGLFFSLSRYK 105
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2329-2408 6.05e-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: 78.41  E-value: 6.05e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2329 NAVVGKPATFVIDAARSGAGNMEI-IVSVDNRNVPNFVQAEGQARFKVSFTPQDAKDHTISVKFNGISVPGSPLICSVSS 2407
Cdd:smart00557   13 KGVVGEPAEFTVDTRDAGGGELEVeVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGP 92


                    .
gi 1734340282  2408 A 2408
Cdd:smart00557   93 A 93
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 14-119 6.40e-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: 79.16  E-value: 6.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   14 DIQLHTFTNWINEQLQGN----VIRDLTQDLSDGVNLIKLVEILQGRRYYGKvYDQDPTEIQKLMNVQMALDALREDGVK 89
Cdd:cd21191      4 NVQKRTFTRWINLHLEKCnpplEVKDLFVDIQDGKILMALLEVLSGQNLLQE-YKPSSHRIFRLNNIAKALKFLEDSNVK 82

                           90       100       110
                   ....*....|....*....|....*....|
gi 1734340282   90 TVNIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21191     83 LVSIDAAEIADGNPSLVLGLIWNIILFFQI 112
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 931-1016 6.93e-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: 6.93e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   931 YSELSGPGLVRAPVNRTAQFDITGEGLELSDIQAKISGPDNREYPIRIIPRSSGKYTAEYEIEQVGEHHLTVWIAGRKVD 1010
Cdd:smart00557    3 KVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIP 82


                    ....*.
gi 1734340282  1011 GSPLSV 1016
Cdd:smart00557   83 GSPFTV 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2473-2554 7.94e-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: 7.94e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2473 LNSAQIGQKKGFTIDNINK-SSDCNVIITDPKGGPLPVRCYKQQDDSYWVEFTPEHLGTHTIEVTFGDVPVPGSPFKTEV 2551
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAgGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ...
gi 1734340282  2552 IDP 2554
Cdd:smart00557   91 GPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2473-2548 1.22e-16

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 77.33  E-value: 1.22e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1734340282 2473 LNSAQIGQKKGFTIDNINKSSDCNVIITDPKGGPLPVRCYKQQDDSYWVEFTPEHLGTHTIEVTFGDVPVPGSPFK 2548
Cdd:pfam00630   14 LEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 19-117 2.68e-16

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: 77.32  E-value: 2.68e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   19 TFTNWINEQLQGNVIRDLTQDLSDGVNLIKLVEILQ-GRRYYGKVYDQDP-TEIQKLMNVQMALDALREDGVKTVNIGSH 96
Cdd:cd21219      8 AFRMWLNSLGLDPLINNLYEDLRDGLVLLQVLDKIQpGCVNWKKVNKPKPlNKFKKVENCNYAVDLAKKLGFSLVGIGGK 87

                           90       100
                   ....*....|....*....|.
gi 1734340282   97 DIVDGNEKLILGLIWCLVQRY 117
Cdd:cd21219     88 DIADGNRKLTLALVWQLMRYH 108
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 17-113 4.54e-16

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 76.22  E-value: 4.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   17 LHTFTNWINEQLQGN---VIRDLTQDLSDGVNLIKLVEILQGRRyYGKVYDQDPTEIQKLMNVQMALDALREDGV-KTVN 92
Cdd:cd00014      1 EEELLKWINEVLGEElpvSITDLFESLRDGVLLCKLINKLSPGS-IPKINKKPKSPFKKRENINLFLNACKKLGLpELDL 79

                           90       100
                   ....*....|....*....|..
gi 1734340282   93 IGSHDIV-DGNEKLILGLIWCL 113
Cdd:cd00014     80 FEPEDLYeKGNLKKVLGTLWAL 101
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2650-2737 4.76e-16

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 75.72  E-value: 4.76e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2650 VYGAAVDQSIkIGEPASLIFDPKKTNGG-LKIHATGPDGQKVHHNVMRRPNGTSEVVFYPEETGTYNVSIDFNNRPITGS 2728
Cdd:smart00557    6 ASGPGLEKGV-VGEPAEFTVDTRDAGGGeLEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGS 84


                    ....*....
gi 1734340282  2729 PFTVNVVDP 2737
Cdd:smart00557   85 PFTVKVGPA 93
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 1-119 3.30e-15

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: 74.41  E-value: 3.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282    1 MGKQGEEAR-----QKWIDIQLHTFTNWINEQLQGN----VIRDLTQDLSDGVNLIKLVEILQGrryygkvyDQDPTEIQ 71
Cdd:cd21247      1 MDTEYEKGHirklqEQRMTMQKKTFTKWMNNVFSKNgakiEITDIYTELKDGIHLLRLLELISG--------EQLPRPSR 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1734340282   72 KLMNVQM------ALDALREDgVKTVNIGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21247     73 GKMRVHFlennskAITFLKTK-VPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2236-2319 4.18e-15

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 73.02  E-value: 4.18e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  2236 LERIPVDEETEIQILT-DEIDSAPEARVRDPQGNDLPVNVtRSRENETlHIATYVPKCVGNHLIDIFLQGEPIAGSPFTA 2314
Cdd:smart00557   11 LEKGVVGEPAEFTVDTrDAGGGELEVEVTGPSGKKVPVEV-KDNGDGT-YTVSYTPTEPGDYTVTVKFGGEHIPGSPFTV 88


                    ....*
gi 1734340282  2315 KAYDA 2319
Cdd:smart00557   89 KVGPA 93
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 838-916 9.19e-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: 9.19e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   838 IQPSKLHTDHSFEIDASAAGSGNLEIMI---NGGRVPCRVRELGSRQYMAIFTPTQSMTHTIEMRFNGEHVSGSPWKLPV 914
Cdd:smart00557   11 LEKGVVGEPAEFTVDTRDAGGGELEVEVtgpSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKV 90


                    ..
gi 1734340282   915 ED 916
Cdd:smart00557   91 GP 92
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 126-227 1.14e-14

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: 72.32  E-value: 1.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  126 PPKKLVMAWIQSAL----PELKLTNFRTNWNDGIALSALLEYCQPGLCPEWR-NLDPSEARENCHRALLLAERYLEVPPI 200
Cdd:pfam00307    2 ELEKELLRWINSHLaeygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKLGVPKV 81

                           90       100
                   ....*....|....*....|....*...
gi 1734340282  201 -ISSDHLSSPhlDELSCLTYLSYFITKG 227
Cdd:pfam00307   82 lIEPEDLVEG--DNKSVLTYLASLFRRF 107
Filamin pfam00630
Filamin/ABP280 repeat;
2650-2731 2.15e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.78  E-value: 2.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2650 VYGAAVDQSiKIGEPASLIFDPKKTNGGLKIHATGPDGQKVHHNVMRRPNGTSEVVFYPEETGTYNVSIDFNNRPITGSP 2729
Cdd:pfam00630    9 ASGPGLEPG-VVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSP 87


                   ..
gi 1734340282 2730 FT 2731
Cdd:pfam00630   88 FK 89
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 21-117 2.44e-14

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


Pssm-ID: 409071  Cd Length: 121  Bit Score: 71.85  E-value: 2.44e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   21 TNWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGrrYY--GKVYDQDP-TEIQKLMNVQMALDALREDGVKTVNIGS 95
Cdd:cd21222     22 LQFVNKHLAklNIEVTDLATQFHDGVYLILLIGLLEG--FFvpLHEYHLTPsTDDEKLHNVKLALELMEDAGISTPKIRP 99

                           90       100
                   ....*....|....*....|..
gi 1734340282   96 HDIVDGNEKLILGLIWCLVQRY 117
Cdd:cd21222    100 EDIVNGDLKSILRVLYSLFSKY 121
Filamin pfam00630
Filamin/ABP280 repeat;
2316-2400 4.46e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 70.01  E-value: 4.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2316 AYDARKTVLVPPA--NAVVGKPATFVIDAARSGaGNMEI-IVSVDNRNVPNFVQAEGQARFKVSFTPQDAKDHTISVKFN 2392
Cdd:pfam00630    1 AADASKVKASGPGlePGVVGKPAEFTVDTRDAG-GEGEVeVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*...
gi 1734340282 2393 GISVPGSP 2400
Cdd:pfam00630   80 GQHIPGSP 87
Filamin pfam00630
Filamin/ABP280 repeat;
2874-2958 5.86e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 69.63  E-value: 5.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2874 SRIMVRGDGLHRAVLKEHNEFIIDGSDinKEGRITATLLGSK-ADIPVRIQQLGHNVYKATYTPLTGGTYELHILWNGKH 2952
Cdd:pfam00630    5 SKVKASGPGLEPGVVGKPAEFTVDTRD--AGGEGEVEVTGPDgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQH 82


                   ....*.
gi 1734340282 2953 VKGSPF 2958
Cdd:pfam00630   83 IPGSPF 88
Filamin pfam00630
Filamin/ABP280 repeat;
2136-2219 9.82e-14

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 68.85  E-value: 9.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2136 AYDPAKIKVG--AIPKGLLDKPVYFTVDASEAGvGNLEVAVCE---GRVPSMAHALGHHKYDISFVPKEDVDHTITVRFN 2210
Cdd:pfam00630    1 AADASKVKASgpGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGpdgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*....
gi 1734340282 2211 NEPVPGSPF 2219
Cdd:pfam00630   80 GQHIPGSPF 88
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 679-762 1.06e-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: 69.17  E-value: 1.06e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   679 GLDVGLVGQELNFSVNASQAGHGNLSVTVFR-HGREIPLSIEEQGSSkVHQVSFTPDGAGQYKIHVLFNRMEIKGSPFIL 757
Cdd:smart00557   10 GLEKGVVGEPAEFTVDTRDAGGGELEVEVTGpSGKKVPVEVKDNGDG-TYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTV 88


                    ....*
gi 1734340282   758 DIADA 762
Cdd:smart00557   89 KVGPA 93
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 16-117 8.91e-13

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: 66.94  E-value: 8.91e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   16 QLHTFTNWINEQLQGNV----IRDLTQDLSDGVNLIKLVEILQGRRYYGKVYdqDPTEIQ-KLMNVQMALDALREDGVKT 90
Cdd:cd21213      1 QLQAYVAWVNSQLKKRPgirpVQDLRRDLRDGVALAQLIEILAGEKLPGIDW--NPTTDAeRKENVEKVLQFMASKRIRM 78

                           90       100
                   ....*....|....*....|....*..
gi 1734340282   91 VNIGSHDIVDGNEKLILGLIWCLVQRY 117
Cdd:cd21213     79 HQTSAKDIVDGNLKAIMRLILALAAHF 105
Filamin pfam00630
Filamin/ABP280 repeat;
1022-1102 1.07e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 66.16  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1022 EKVRLEPLG--GGVPKQPVQFYVDAVEA-GKGQLEISVNQGK-VPNNVQMQGAGRCLVTFIPQHAGTYVIDVTFNGEQVH 1097
Cdd:pfam00630    5 SKVKASGPGlePGVVGKPAEFTVDTRDAgGEGEVEVTGPDGSpVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIP 84


                   ....*
gi 1734340282 1098 GCPIK 1102
Cdd:pfam00630   85 GSPFK 89
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 20-114 1.50e-12

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: 66.44  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   20 FTNWINEQLQGN-------VIRDLTQDL----SDGVNLIKLVEILQgrryYGKV------YDQDPTEIQKLMNVQMALDA 82
Cdd:cd21217      6 FVEHINSLLADDpdlkhllPIDPDGDDLfealRDGVLLCKLINKIV----PGTIderklnKKKPKNIFEATENLNLALNA 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1734340282   83 LREDGVKTVNIGSHDIVDGNEKLILGLIWCLV 114
Cdd:cd21217     82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 19-120 2.66e-12

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: 66.10  E-value: 2.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   19 TFTNWINEQLQGNVIRDLTQDLSDGVNLIKLVEILQ-GRRYYGKV---YDQDPTEIQKLMNVQMALDALREDGVKTVNIG 94
Cdd:cd21298     10 TYRNWMNSLGVNPFVNHLYSDLRDGLVLLQLYDKIKpGVVDWSRVnkpFKKLGANMKKIENCNYAVELGKKLKFSLVGIG 89

                           90       100
                   ....*....|....*....|....*.
gi 1734340282   95 SHDIVDGNEKLILGLIWCLVQRYQIA 120
Cdd:cd21298     90 GKDIYDGNRTLTLALVWQLMRAYTLS 115
Filamin pfam00630
Filamin/ABP280 repeat;
669-756 3.95e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 64.62  E-value: 3.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  669 VFDSGLVNVYGLDV--GLVGQELNFSVNASQAGhGNLSVTVF-RHGREIPLSIEEQGSSKvHQVSFTPDGAGQYKIHVLF 745
Cdd:pfam00630    1 AADASKVKASGPGLepGVVGKPAEFTVDTRDAG-GEGEVEVTgPDGSPVPVEVTDNGDGT-YTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|.
gi 1734340282  746 NRMEIKGSPFI 756
Cdd:pfam00630   79 NGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
932-1013 4.03e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 64.62  E-value: 4.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  932 SELSGPGLVRAPVNRTAQFDITGEGlELSDIQAKISGPDNREYPIRIIPRSSGKYTAEYEIEQVGEHHLTVWIAGRKVDG 1011
Cdd:pfam00630    7 VKASGPGLEPGVVGKPAEFTVDTRD-AGGEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPG 85


                   ..
gi 1734340282 1012 SP 1013
Cdd:pfam00630   86 SP 87
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
 127-223 4.15e-12

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


Pssm-ID: 409188  Cd Length: 105  Bit Score: 65.00  E-value: 4.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  127 PKKLvMAWIQSAL---PELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIIS- 202
Cdd:cd22198      2 PEEL-LSWCQEQTegyRGVKVTDLTSSWRSGLALCAIIHRFRPDLI-DFSSLDPENIAENNQLAFDVAEQELGIPPVMTg 79

                           90       100
                   ....*....|....*....|.
gi 1734340282  203 SDHLSSPHLDELSCLTYLSYF 223
Cdd:cd22198     80 QEMASLAVPDKLSMVSYLSQF 100
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 109-223 4.49e-12

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: 64.74  E-value: 4.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  109 LIWClvQRyqiacKTkippkklvmawiqSALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRAL 188
Cdd:cd21194      8 LLWC--QR-----KT-------------AGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLI-DYNRLDPNDHLGNLNNAF 66

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1734340282  189 LLAERYLEVPPIISSDHLSSPHLDELSCLTYL-SYF 223
Cdd:cd21194     67 DVAEQELGIAKLLDAEDVDVARPDEKSIMTYVaSYY 102
Filamin pfam00630
Filamin/ABP280 repeat;
1890-1980 6.82e-12

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 63.85  E-value: 6.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1890 VYDASEIIV-GEIPNQSNLNDTVEFTVDAGRAGfGNLEMAIKDADGVIIPSHVAQLESGSakFLVTFTPATKGPHTVNIT 1968
Cdd:pfam00630    1 AADASKVKAsGPGLEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGT--YTVSYTPTEPGDYTVSVK 77

                           90
                   ....*....|..
gi 1734340282 1969 FNKEVLKNSPFE 1980
Cdd:pfam00630   78 FNGQHIPGSPFK 89
Filamin pfam00630
Filamin/ABP280 repeat;
578-665 2.72e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 61.92  E-value: 2.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  578 SPDVGLVSFSGL-TEPCSVGSIVEVVINAHGdaVSGSVYVEAVSPSGNVHRCTVR-HQDNSYMATFTPQEVGLWRIGILY 655
Cdd:pfam00630    1 AADASKVKASGPgLEPGVVGKPAEFTVDTRD--AGGEGEVEVTGPDGSPVPVEVTdNGDGTYTVSYTPTEPGDYTVSVKF 78

                           90
                   ....*....|
gi 1734340282  656 DGEHIRGSPF 665
Cdd:pfam00630   79 NGQHIPGSPF 88
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
 128-223 2.99e-11

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


Pssm-ID: 409168  Cd Length: 112  Bit Score: 62.72  E-value: 2.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIISSD 204
Cdd:cd21319      7 KDALLLWCQmktAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLV-DFGKLKKSNARHNLEHAFNVAERQLGITKLLDPE 85

                           90
                   ....*....|....*....
gi 1734340282  205 HLSSPHLDELSCLTYLSYF 223
Cdd:cd21319     86 DVFTENPDEKSIITYVVAF 104
Filamin pfam00630
Filamin/ABP280 repeat;
2049-2133 5.23e-11

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 61.15  E-value: 5.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2049 FPAKTTVSKiPSLS--RVGQPSSLVVEVSGHD-QLEIRVLDSKKSEIGTDIVEIEPGHMQINFTPAQVGDHEIDVRYGGV 2125
Cdd:pfam00630    3 DASKVKASG-PGLEpgVVGKPAEFTVDTRDAGgEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQ 81


                   ....*...
gi 1734340282 2126 PVTGSPFT 2133
Cdd:pfam00630   82 HIPGSPFK 89
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 32-115 5.35e-11

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: 62.22  E-value: 5.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   32 VIRDLTQDLSDGVNLIKLVEILQGRRyYGKVYDQDPTE--IQKLMNVQMALDALREDGVKTVNIGSH----DIVDGNEKL 105
Cdd:cd21223     25 AVTNLAVDLRDGVRLCRLVELLTGDW-SLLSKLRVPAIsrLQKLHNVEVALKALKEAGVLRGGDGGGitakDIVDGHREK 103

                           90
                   ....*....|
gi 1734340282  106 ILGLIWCLVQ 115
Cdd:cd21223    104 TLALLWRIIF 113
Filamin pfam00630
Filamin/ABP280 repeat;
2236-2313 1.10e-10

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 60.38  E-value: 1.10e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734340282 2236 LERIPVDEETEIQILTDEIDSAPEARVRDPQGNDLPVNVTrSRENETlHIATYVPKCVGNHLIDIFLQGEPIAGSPFT 2313
Cdd:pfam00630   14 LEPGVVGKPAEFTVDTRDAGGEGEVEVTGPDGSPVPVEVT-DNGDGT-YTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2571-2644 1.73e-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: 59.92  E-value: 1.73e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1734340282  2571 ATTINVDRRNAGNGELQVEITDPTGSPLRTEMLKSPGGEDRITFLPNQTGPHKINVKVAGFQIPGYPQTILVSE 2644
Cdd:smart00557   19 PAEFTVDTRDAGGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGSPFTVKVGP 92
Filamin pfam00630
Filamin/ABP280 repeat;
2979-3054 2.05e-10

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 59.61  E-value: 2.05e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734340282 2979 LKIGIINENIKTLIDTRRAGsGQLSALCMGPN-KPAYCELYDHRDGTYALCVRPAEIGKHTLVIKYDDEHVKGSPFV 3054
Cdd:pfam00630   14 LEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDgSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 127-221 2.21e-10

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: 60.10  E-value: 2.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  127 PKKLVMAWIQSAL---PELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIISS 203
Cdd:cd21189      2 AKEALLLWARRTTegyPGVRVTNFTSSWRDGLAFNAIIHRNRPDLI-DFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80

                           90
                   ....*....|....*...
gi 1734340282  204 DHLSSPHLDELSCLTYLS 221
Cdd:cd21189     81 EDVDVPEPDEKSIITYVS 98
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
 109-223 2.75e-10

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


Pssm-ID: 409065  Cd Length: 115  Bit Score: 60.07  E-value: 2.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  109 LIWClvQRyqiacKTKipPKKLVmawiqsalpelKLTNFRTNWNDGIALSALLEYCQPGLCPeWRNLDPSEARENCHRAL 188
Cdd:cd21216     16 LLWC--QR-----KTA--PYKNV-----------NVQNFHTSWKDGLAFCALIHRHRPDLLD-YDKLRKDDPRENLNLAF 74

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1734340282  189 LLAERYLEVPPII-SSDHLSSPHLDELSCLTYLSYF 223
Cdd:cd21216     75 DVAEKHLDIPKMLdAEDIVNTPRPDERSVMTYVSCY 110
Filamin pfam00630
Filamin/ABP280 repeat;
2551-2637 4.14e-10

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 58.84  E-value: 4.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2551 VIDPKNVEIRGLS-DQVLLRHATTINVDRRNAGnGELQVEITDPTGSPLRTEMLKSPGGEDRITFLPNQTGPHKINVKVA 2629
Cdd:pfam00630    1 AADASKVKASGPGlEPGVVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFN 79


                   ....*...
gi 1734340282 2630 GFQIPGYP 2637
Cdd:pfam00630   80 GQHIPGSP 87
Filamin pfam00630
Filamin/ABP280 repeat;
838-911 1.03e-09

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 57.68  E-value: 1.03e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1734340282  838 IQPSKLHTDHSFEIDAS-AAGSGNLEIMI-NGGRVPCRVRELGSRQYMAIFTPTQSMTHTIEMRFNGEHVSGSPWK 911
Cdd:pfam00630   14 LEPGVVGKPAEFTVDTRdAGGEGEVEVTGpDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPFK 89
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 2756-2832 1.49e-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: 1.49e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734340282  2756 RLGHSNSFDVDATAAGPGKLRAEVRDADSSLIGngPVVEDMGQGKYRVRFNPDQPGKYSIYLYWNELPVE-SAFPVRA 2832
Cdd:smart00557   15 VVGEPAEFTVDTRDAGGGELEVEVTGPSGKKVP--VEVKDNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPgSPFTVKV 90
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 128-223 2.45e-09

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: 57.76  E-value: 2.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIISSD 204
Cdd:cd21322     19 KDALLLWCQmktAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLI-DFSKLTKSNATYNLQQAFNTAEQHLGLTKLLDPE 97

                           90
                   ....*....|....*....
gi 1734340282  205 HLSSPHLDELSCLTYLSYF 223
Cdd:cd21322     98 DVNMEAPDEKSIITYVVSF 116
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
 131-223 3.86e-09

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: 56.59  E-value: 3.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  131 VMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLcpewrnLDPSE-----ARENCHRALLLAERYLEVPPIIS 202
Cdd:cd21196      8 LLRWCQeqtAGYPGVHVSDLSSSWADGLALCALVYRLQPGL------LEPSElqglgALEATAWALKVAENELGITPVVS 81

                           90       100
                   ....*....|....*....|.
gi 1734340282  203 SDHLSSPHlDELSCLTYLSYF 223
Cdd:cd21196     82 AQAVVAGS-DPLGLIAYLSHF 101
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
 122-224 6.22e-09

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: 56.00  E-value: 6.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  122 KTKIPPKKLVMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVP 198
Cdd:cd21244      1 RWKMSARKALLLWAQeqcAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLV-DMEKLKGRSNRENLEEAFRIAEQELKIP 79

                           90       100
                   ....*....|....*....|....*.
gi 1734340282  199 PIISSDHLSSPHLDELSCLTYLSYFI 224
Cdd:cd21244     80 RLLEPEDVDVVNPDEKSIMTYVAQFL 105
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 128-224 9.66e-09

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 55.42  E-value: 9.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQSALPE---LKLTNFRTNWNDGIALSALLEYCQPGLCPEWRN--LDPSEARENCHRALLLAERY-LEVPPII 201
Cdd:cd00014      1 EEELLKWINEVLGEelpVSITDLFESLRDGVLLCKLINKLSPGSIPKINKkpKSPFKKRENINLFLNACKKLgLPELDLF 80

                           90       100
                   ....*....|....*....|...
gi 1734340282  202 SSDHLSSPHlDELSCLTYLSYFI 224
Cdd:cd00014     81 EPEDLYEKG-NLKKVLGTLWALA 102
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 762-826 1.03e-08

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


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 54.92  E-value: 1.03e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   762 ASSVSVYGENLRSASVGKTASFMVHAIGAEAKDISAHVT----------------------------GEHSVDVMLADQR 813
Cdd:smart00557    1 ASKVKASGPGLEKGVVGEPAEFTVDTRDAGGGELEVEVTgpsgkkvpvevkdngdgtytvsytptepGDYTVTVKFGGEH 80

                            90
                    ....*....|...
gi 1734340282   814 VPDAPFACNVGAP 826
Cdd:smart00557   81 IPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
2734-2824 1.03e-08

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 54.60  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 2734 VVDPTKVIVNDLDMDRDgtlllRLGHSNSFDVDATAAGpGKLRAEVRDADSSLIGngPVVEDMGQGKYRVRFNPDQPGKY 2813
Cdd:pfam00630    1 AADASKVKASGPGLEPG-----VVGKPAEFTVDTRDAG-GEGEVEVTGPDGSPVP--VEVTDNGDGTYTVSYTPTEPGDY 72

                           90
                   ....*....|.
gi 1734340282 2814 SIYLYWNELPV 2824
Cdd:pfam00630   73 TVSVKFNGQHI 83
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 20-118 1.54e-08

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


Pssm-ID: 409135  Cd Length: 105  Bit Score: 55.04  E-value: 1.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   20 FTNWINEQLQGN----VIRDLTQDLSDGVNLIKLVEILQGRRYYgKVYDQDPTEIQKLMNVQMALDALREDGVKTVNIGS 95
Cdd:cd21286      5 YTDWANHYLAKSghkrLIKDLQQDIADGVLLAEIIQIIANEKVE-DINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 83

                           90       100
                   ....*....|....*....|...
gi 1734340282   96 HDIVDGNEKLILGLIWCLvQRYQ 118
Cdd:cd21286     84 EEIRNGNLKAILGLFFSL-SRYK 105
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 128-223 2.83e-08

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


Pssm-ID: 409097  Cd Length: 105  Bit Score: 53.94  E-value: 2.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIISSD 204
Cdd:cd21248      4 KDALLLWCQmktAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLI-DYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPE 82

                           90       100
                   ....*....|....*....|
gi 1734340282  205 HLSSPHLDELSCLTYL-SYF 223
Cdd:cd21248     83 DVNVEQPDEKSIITYVvTYY 102
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 128-220 6.20e-08

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


Pssm-ID: 409169  Cd Length: 108  Bit Score: 53.18  E-value: 6.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIISSD 204
Cdd:cd21320      4 KDALLLWCQmktAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLI-DFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPE 82

                           90
                   ....*....|....*.
gi 1734340282  205 HLSSPHLDELSCLTYL 220
Cdd:cd21320     83 DISVDHPDEKSIITYV 98
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
 122-226 6.92e-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: 53.09  E-value: 6.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  122 KTKIPPKKLVMAWIQSALPE---LKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVP 198
Cdd:cd21243      1 KFKGGAKKALLKWVQNAAAKrfgIEVKDFGPSWRDGVAFNAIIHSIRPDLV-DMESLKRRSNRENLETAFTVAEKELGIP 79

                           90       100
                   ....*....|....*....|....*...
gi 1734340282  199 PIISSDHLSSPHLDELSCLTYLSYFITK 226
Cdd:cd21243     80 RLLDPEDVDVDKPDEKSIMTYVAQFLKK 107
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 229-330 7.41e-08

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: 52.62  E-value: 7.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  229 PGYRATLKKVSMLLPDCNVDDLEHSWSDGFLLAHLVE-ICGGRVPELERMrfdNLNDFVENVAIVLDAAAD-IGVGSLIG 306
Cdd:cd21184      1 SGKSLLLEWVNSKIPEYKVKNFTTDWNDGKALAALVDaLKPGLIPDNESL---DKENPLENATKAMDIAEEeLGIPKIIT 77

                           90       100
                   ....*....|....*....|....
gi 1734340282  307 ADDIAEPQGEHLGTMALVAALCSV 330
Cdd:cd21184     78 PEDMVSPNVDELSVMTYLSYFRNA 101
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 19-119 9.33e-08

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: 53.47  E-value: 9.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   19 TFTNWINEQLQGNVIRDLTQDLSDGVNLIKLVEILQGRRYYGKV----YDQDPTEIQKLMNVQMALDaLREDGVK--TVN 92
Cdd:cd21331     26 TFRNWMNSLGVNPHVNHLYGDLQDALVILQLYEKIKVPVDWNKVnkppYPKLGANMKKLENCNYAVE-LGKHPAKfsLVG 104

                           90       100
                   ....*....|....*....|....*..
gi 1734340282   93 IGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21331    105 IGGQDLNDGNPTLTLALVWQLMRRYTL 131
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 128-223 9.97e-08

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: 52.92  E-value: 9.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIISSD 204
Cdd:cd21291     12 KEGLLLWCQrktAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLI-DYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVE 90

                           90       100
                   ....*....|....*....|..
gi 1734340282  205 HL---SSPhlDELSCLTYLSYF 223
Cdd:cd21291     91 DVcdvAKP--DERSIMTYVAYY 110
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
 125-223 1.23e-07

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: 52.35  E-value: 1.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  125 IPPKKLvMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPII 201
Cdd:cd21195      4 IRPSKL-LTWCQqqtEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELI-NFDSLNEDDAVENNQLAFDVAEREFGIPPVT 81

                           90       100
                   ....*....|....*....|...
gi 1734340282  202 SSDHLSSP-HLDELSCLTYLSYF 223
Cdd:cd21195     82 TGKEMASAqEPDKLSMVMYLSKF 104
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 128-223 1.32e-07

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: 52.17  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIISSD 204
Cdd:cd21249      6 KEALLIWCQrktAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLI-DYGSLRPDRPLYNLANAFLVAEQELGISQLLDPE 84

                           90
                   ....*....|....*....
gi 1734340282  205 HLSSPHLDELSCLTYLSYF 223
Cdd:cd21249     85 DVAVPHPDERSIMTYVSLY 103
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 20-115 1.49e-07

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: 53.12  E-value: 1.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   20 FTNWINEQLQGN-----VI------RDLTQDLSDGVNLIKLVEILQGRRYYGKVYDQD---PTEIQKlmNVQMALDALRE 85
Cdd:cd21323     29 FVNWINKALEGDpdckhVVpmnptdESLFKSLADGILLCKMINLSQPDTIDERAINKKkltPFTISE--NLNLALNSASA 106

                           90       100       110
                   ....*....|....*....|....*....|
gi 1734340282   86 DGVKTVNIGSHDIVDGNEKLILGLIWCLVQ 115
Cdd:cd21323    107 IGCTVVNIGSLDLKEGKPHLVLGLLWQIIK 136
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 22-118 2.01e-07

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: 51.97  E-value: 2.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   22 NWINEQLQ--GNVIRDLTQDLSDGVNLIKLVEILQGRRYYGKVYDQDP-TEIQKLMNVQMALDALREDGVKTVNIGSHDI 98
Cdd:cd21307     23 HFVNKHLGnlGLNVKDLDSQFADGVILLLLIGQLEGFFIHLSEFFLTPsSTSEMLHNVTLALELLKEGGLLNFPVNPEDI 102

                           90       100
                   ....*....|....*....|
gi 1734340282   99 VDGNEKLILGLIWCLVQRYQ 118
Cdd:cd21307    103 VNGDSKATIRVLYCLFSKYK 122
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
 140-223 2.27e-07

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


Pssm-ID: 409102  Cd Length: 106  Bit Score: 51.58  E-value: 2.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  140 PELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPII-SSDHLSSPHLDELSCLT 218
Cdd:cd21253     18 RDVKVTNMTTSWRDGLAFCAIIHRFRPDLI-DFDSLSKENVYENNKLAFTVAEKELGIPALLdAEDMVALKVPDKLSILT 96


                   ....*
gi 1734340282  219 YLSYF 223
Cdd:cd21253     97 YVSQY 101
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
 126-220 3.18e-07

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: 50.89  E-value: 3.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  126 PPKKLVMAWIQSA---LPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERyLEVP-PII 201
Cdd:cd21198      1 SSGQDLLEWCQEVtkgYRGVKITNLTTSWRNGLAFCAILHHFRPDLI-DFSSLSPHDIKENCKLAFDAAAK-LGIPrLLD 78

                           90
                   ....*....|....*....
gi 1734340282  202 SSDHLSSPHLDELSCLTYL 220
Cdd:cd21198     79 PADMVLLSVPDKLSVMTYL 97
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
 128-223 3.83e-07

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


Pssm-ID: 409138  Cd Length: 124  Bit Score: 51.65  E-value: 3.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPII-SS 203
Cdd:cd21289     12 KEGLLLWCQrktAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLI-DYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLdAE 90

                           90       100
                   ....*....|....*....|
gi 1734340282  204 DHLSSPHLDELSCLTYLSYF 223
Cdd:cd21289     91 DIVNTPKPDEKAIMTYVSCF 110
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 122-223 4.45e-07

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: 51.21  E-value: 4.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  122 KTKIPPKKLVMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVP 198
Cdd:cd21321      1 KEKKSAKDALLLWCQmktAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLI-DFETLKKSNAHYNLQNAFNVAEKELGLT 79

                           90       100
                   ....*....|....*....|....*
gi 1734340282  199 PIISSDHLSSPHLDELSCLTYLSYF 223
Cdd:cd21321     80 KLLDPEDVNVDQPDEKSIITYVATY 104
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
 124-224 4.53e-07

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: 50.88  E-value: 4.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  124 KIPPKKLVMAWIQSALPEL---KLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPI 200
Cdd:cd21192      1 QGSAEKALLKWVQAEIGKYygiRVTDFDKSWRDGVAFLALIHAIRPDLV-DMKTVKNRSPRDNLELAFRIAEQHLNIPRL 79

                           90       100
                   ....*....|....*....|....
gi 1734340282  201 ISSDHLSSPHLDELSCLTYLSYFI 224
Cdd:cd21192     80 LEVEDVLVDKPDERSIMTYVSQFL 103
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 246-327 6.17e-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: 50.03  E-value: 6.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  246 NVDDLEHSWSDGFLLAHLVE-ICGGRVPE---LERMRFDNLndfvENVAIVLDAAADIGVGS--LIGADDIAEPQGEHLg 319
Cdd:cd00014     19 SITDLFESLRDGVLLCKLINkLSPGSIPKinkKPKSPFKKR----ENINLFLNACKKLGLPEldLFEPEDLYEKGNLKK- 93


                   ....*...
gi 1734340282  320 TMALVAAL 327
Cdd:cd00014     94 VLGTLWAL 101
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 124-214 8.92e-07

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 49.99  E-value: 8.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  124 KIPPKKLVMAWIQSAL-----PELKLTNFRTNWNDGIALSALLEYCQPGLCPEWRNLDPSEARENCHRA--LLLAERYLE 196
Cdd:cd21218      8 YLPPEEILLRWVNYHLkkagpTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKRAekVLQAAEKLG 87

                           90
                   ....*....|....*...
gi 1734340282  197 VPPIISSDHLSSPHLDEL 214
Cdd:cd21218     88 CKYFLTPEDIVSGNPRLN 105
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
 128-223 9.11e-07

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


Pssm-ID: 409137  Cd Length: 124  Bit Score: 50.46  E-value: 9.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPII-SS 203
Cdd:cd21288     12 KEGLLLWCQrktAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLI-DYSKLNKDDPIGNINLAMEIAEKHLDIPKMLdAE 90

                           90       100
                   ....*....|....*....|
gi 1734340282  204 DHLSSPHLDELSCLTYLSYF 223
Cdd:cd21288     91 DIVNTPKPDERAIMTYVSCF 110
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
 20-119 1.03e-06

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: 49.81  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   20 FTNWINEQLQGNVIRDLTQDLSDGVNLIKLVEILQGRRYYGKVYDQDPTEI--QKLMNVQMALDALREDGVKTVNIGSHD 97
Cdd:cd21299      9 FRLWINSLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMpfKKVENCNQVVKIGKQLKFSLVNVAGND 88

                           90       100
                   ....*....|....*....|..
gi 1734340282   98 IVDGNEKLILGLIWCLVqRYQI 119
Cdd:cd21299     89 IVQGNKKLILALLWQLM-RYHM 109
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
 131-221 1.17e-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: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  131 VMAWIQS---ALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERyLEVPPIIS-SDHL 206
Cdd:cd21255      6 LLEWCQEvtaGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLV-DYESLDPLDIKENNKKAFEAFAS-LGVPRLLEpADMV 83

                           90
                   ....*....|....*
gi 1734340282  207 SSPHLDELSCLTYLS 221
Cdd:cd21255     84 LLPIPDKLIVMTYLC 98
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 128-221 2.13e-06

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


Pssm-ID: 409082  Cd Length: 111  Bit Score: 48.77  E-value: 2.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQSAL---PELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSE-ARENCHRALLLAERYLEVPPIISS 203
Cdd:cd21233      2 EKILLSWVRQSTrnyPQVNVINFTSSWSDGLAFNALIHSHRPDLF-DWNSVVSQQsATERLDHAFNIARQHLGIEKLLDP 80

                           90
                   ....*....|....*...
gi 1734340282  204 DHLSSPHLDELSCLTYLS 221
Cdd:cd21233     81 EDVATAHPDKKSILMYVT 98
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 129-224 2.56e-06

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: 48.63  E-value: 2.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  129 KLVMAWIQSALPE--LKLTNFRTNWNDGIALSALLEYCQPGLCPEWRNLDpSEARENCHRALLLAERYLEVPPIISSDHL 206
Cdd:cd21245      6 KALLNWVQRRTRKygVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALE-KSPRENLEDAFRIAQESLGIPPLLEPEDV 84

                           90
                   ....*....|....*...
gi 1734340282  207 SSPHLDELSCLTYLSYFI 224
Cdd:cd21245     85 MVDSPDEQSIMTYVAQFL 102
Filamin pfam00630
Filamin/ABP280 repeat;
760-819 2.73e-06

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 48.05  E-value: 2.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  760 ADASSVSVYGENLRSASVGKTASFMVHA-----------IGAEAKDISAHVT----------------GEHSVDVMLADQ 812
Cdd:pfam00630    2 ADASKVKASGPGLEPGVVGKPAEFTVDTrdaggegevevTGPDGSPVPVEVTdngdgtytvsytptepGDYTVSVKFNGQ 81


                   ....*..
gi 1734340282  813 RVPDAPF 819
Cdd:pfam00630   82 HIPGSPF 88
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
 128-223 3.06e-06

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


Pssm-ID: 409139  Cd Length: 125  Bit Score: 48.93  E-value: 3.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQSALPELK---LTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPII-SS 203
Cdd:cd21290     15 KEGLLLWCQRKTAPYKnvnVQNFHISWKDGLAFNALIHRHRPELI-EYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLdAE 93

                           90       100
                   ....*....|....*....|
gi 1734340282  204 DHLSSPHLDELSCLTYLSYF 223
Cdd:cd21290     94 DIVNTARPDEKAIMTYVSSF 113
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
 19-119 3.26e-06

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 48.44  E-value: 3.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   19 TFTNWINEQLQGNVIRDLTQDLSDGVNLIKLVEILQGRRYYGKV----YDQDPTEIQKLMNVQMALD-ALREDGVKTVNI 93
Cdd:cd21329     10 TFRNWMNSLGVNPYVNHLYSDLCDALVIFQLYEMTRVPVDWGHVnkppYPALGGNMKKIENCNYAVElGKNKAKFSLVGI 89

                           90       100
                   ....*....|....*....|....*.
gi 1734340282   94 GSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21329     90 AGSDLNEGNKTLTLALIWQLMRRYTL 115
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 128-221 3.88e-06

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


Pssm-ID: 409089  Cd Length: 107  Bit Score: 48.11  E-value: 3.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERyLEVPPIISSD 204
Cdd:cd21240      6 KEKLLLWTQkvtAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLV-DMERVQIQSNRENLEQAFEVAER-LGVTRLLDAE 83

                           90
                   ....*....|....*..
gi 1734340282  205 HLSSPHLDELSCLTYLS 221
Cdd:cd21240     84 DVDVPSPDEKSVITYVS 100
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 20-118 4.27e-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: 48.42  E-value: 4.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   20 FTNWINEQL----QGNVIRDLTQDLSDGVNLIKLVEILQGRryygKVYDQD---PTEIQKLMNVQMALDALREDGVKTVN 92
Cdd:cd21285     15 YTDWANHYLaksgHKRLIKDLQQDVTDGVLLAEIIQVVANE----KIEDINgcpKNRSQMIENIDACLSFLAAKGINIQG 90

                           90       100
                   ....*....|....*....|....*.
gi 1734340282   93 IGSHDIVDGNEKLILGLIWCLvQRYQ 118
Cdd:cd21285     91 LSAEEIRNGNLKAILGLFFSL-SRYK 115
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 20-116 5.46e-06

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: 48.21  E-value: 5.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   20 FTNWINEQLQGNviRDLTQDL-------------SDGVNLIKLVEILQGRRYYGKVYDQDPTEIQKLMNVQM------AL 80
Cdd:cd21294     11 FTKHINAVLAGD--PDVGSRLpfptdtfqlfdecKDGLVLSKLINDSVPDTIDERVLNKPPRKNKPLNNFQMiennniVI 88

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1734340282   81 DALREDGVKTVNIGSHDIVDGNEKLILGLIWCLVQR 116
Cdd:cd21294     89 NSAKAIGCSVVNIGAGDIIEGREHLILGLIWQIIRR 124
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
 122-223 5.89e-06

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: 47.57  E-value: 5.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  122 KTKIPPKKLvMAWIQSALPELK---LTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVP 198
Cdd:cd21250      1 ESDIRPNKL-LTWCQKQTEGYQnvnVTDLTTSWKSGLALCAIIHRFRPELI-DFDSLNEDDAVKNNQLAFDVAEREFGIP 78

                           90       100
                   ....*....|....*....|....*.
gi 1734340282  199 PIISSDHLSSPH-LDELSCLTYLSYF 223
Cdd:cd21250     79 PVTTGKEMASAEePDKLSMVMYLSKF 104
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
 131-223 8.66e-06

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: 47.25  E-value: 8.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  131 VMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIISSDHLS 207
Cdd:cd21251     10 LLGWCQrqtEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLI-DFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEMA 88

                           90
                   ....*....|....*..
gi 1734340282  208 S-PHLDELSCLTYLSYF 223
Cdd:cd21251     89 SvGEPDKLSMVMYLTQF 105
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 19-119 1.11e-05

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 47.29  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   19 TFTNWINEQLQGNVIRDLTQDLSDGVNLIKLVEILQGRRYYGKV----YDQDPTEIQKLMNVQMALDaLREDGVK--TVN 92
Cdd:cd21330     17 TFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVnkppYPKLGENMKKLENCNYAVE-LGKNKAKfsLVG 95

                           90       100
                   ....*....|....*....|....*..
gi 1734340282   93 IGSHDIVDGNEKLILGLIWCLVQRYQI 119
Cdd:cd21330     96 IAGQDLNEGNRTLTLALIWQLMRRYTL 122
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 22-107 1.58e-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: 46.52  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   22 NWINEQLQG-----NVIRDLTQDLSDGVNLIKLVEILQGRRYYGKVYDQDPTEIQKLMNVQMALDALREDGVKTVnIGSH 96
Cdd:cd21218     17 RWVNYHLKKagptkKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPE 95

                           90
                   ....*....|.
gi 1734340282   97 DIVDGNEKLIL 107
Cdd:cd21218     96 DIVSGNPRLNL 106
PTZ00121 PTZ00121
MAEBL; Provisional
 1478-1900 1.59e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1478 KKPNVPKKRATTPEGHVEPVNDNEEKDRQAFLRTQSEKVFEPVDAPLRRSDEKESIYDLPPQERLHKYPEEPTIALGEKA 1557
Cdd:PTZ00121  1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1558 NTSAIAAYTKGRQDDI---DEVSRNASFPSAPTINYNERSDEVSNYNRTKEDHYGVVGEYPTAPKIaysdsKEAVIREHY 1634
Cdd:PTZ00121  1524 ADEAKKAEEAKKADEAkkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA-----EEARIEEVM 1598

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1635 AQAKEDPYATVGECPPAPEISLRSDKLNETKNEYRRTTDSDQQDGKagppppviEISKAEQARRTEEYLRV-------KS 1707
Cdd:PTZ00121  1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE--------EKKKAEELKKAEEENKIkaaeeakKA 1670

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1708 EDDKILAKHgfTRKPEpsiEIQEPVTEQIRDDVVETAIAPEV------------PLRPVEELPHSPAPSSRSTPATTPKL 1775
Cdd:PTZ00121  1671 EEDKKKAEE--AKKAE---EDEKKAAEALKKEAEEAKKAEELkkkeaeekkkaeELKKAEEENKIKAEEAKKEAEEDKKK 1745

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282 1776 SAKFRKDGKEGKPFDFGKSKFVCKHDVIKRGKEVEVKlEGIKlgKEDQLRvvvlppankaipganggpPTEVDTKVKKSS 1855
Cdd:PTZ00121  1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE-EELD--EEDEKR------------------RMEVDKKIKDIF 1804

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1734340282 1856 SKYEIsfkpTEVGTHKVFAYVNDMQHPLSPFAVRVYDASEIIVGE 1900
Cdd:PTZ00121  1805 DNFAN----IIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 128-221 2.23e-05

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: 45.78  E-value: 2.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQSAL---PELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIISSD 204
Cdd:cd21238      4 KEKLLLWSQRMVegyQGLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 82

                           90
                   ....*....|....*..
gi 1734340282  205 HLSSPHLDELSCLTYLS 221
Cdd:cd21238     83 DVDVPQPDEKSIITYVS 99
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 1806-1893 2.37e-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: 45.29  E-value: 2.37e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  1806 GKEVEVKLEGIKLGkEDQLRVVVLPPANKaipganggpptEVDTKVK-KSSSKYEISFKPTEVGTHKVFAYVNDMQHPLS 1884
Cdd:smart00557   17 GEPAEFTVDTRDAG-GGELEVEVTGPSGK-----------KVPVEVKdNGDGTYTVSYTPTEPGDYTVTVKFGGEHIPGS 84


                    ....*....
gi 1734340282  1885 PFAVRVYDA 1893
Cdd:smart00557   85 PFTVKVGPA 93
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
 4-116 2.66e-05

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


Pssm-ID: 409149  Cd Length: 119  Bit Score: 45.88  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282    4 QGE-EARqkwidiqlhTFTNWINeQLQGNV-IRDLTQDLSDGVNLIKLVE-ILQGRRYYGKVYDQDPTEI----QKLMNV 76
Cdd:cd21300      4 EGErEAR---------VFTLWLN-SLDVEPaVNDLFEDLRDGLILLQAYDkVIPGSVNWKKVNKAPASAEisrfKAVENT 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1734340282   77 QMALDALREDGVKTVNIGSHDIVDGNEKLILGLIWCLVQR 116
Cdd:cd21300     74 NYAVELGKQLGFSLVGIQGADITDGSRTLTLALVWQLMRF 113
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
 128-223 2.69e-05

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


Pssm-ID: 409136  Cd Length: 124  Bit Score: 46.23  E-value: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQSALPELK---LTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPII-SS 203
Cdd:cd21287     12 KEGLLLWCQRKTAPYKnvnIQNFHISWKDGLGFCALIHRHRPELI-DYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLdAE 90

                           90       100
                   ....*....|....*....|
gi 1734340282  204 DHLSSPHLDELSCLTYLSYF 223
Cdd:cd21287     91 DIVGTARPDEKAIMTYVSSF 110
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 248-327 3.26e-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: 45.75  E-value: 3.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  248 DDLehswSDGFLLAHLVE-ICGGRVPELERMRFDNLNDFVENVAIVLDAAADIGVGSLIGADDIAEPQgEHLgTMALVAA 326
Cdd:cd21218     38 SDL----KDGEVYALLLHsLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCKYFLTPEDIVSGN-PRL-NLAFVAT 111


                   .
gi 1734340282  327 L 327
Cdd:cd21218    112 L 112
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 6-115 3.87e-05

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: 46.20  E-value: 3.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282    6 EEARQKWIDIQLHTFTNWINEQLQGN-----VI------RDLTQDLSDGVNLIKLVEILQGRRYYGKVYDQD---PTEIQ 71
Cdd:cd21325     15 EGTQHSYSEEEKYAFVNWINKALENDpdcrhVIpmnpntDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKkltPFIIQ 94

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1734340282   72 KlmNVQMALDALREDGVKTVNIGSHDIVDGNEKLILGLIWCLVQ 115
Cdd:cd21325     95 E--NLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIK 136
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
 134-208 3.91e-05

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


Pssm-ID: 409048  Cd Length: 112  Bit Score: 45.43  E-value: 3.91e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734340282  134 WIQS---ALPELKLTNFRTNWNDGIALSALLEYCQPGLCPeWRNLDPSEARENCHRALLLAERYlEVPPIISSDHLSS 208
Cdd:cd21199     16 WCQEktqGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIP-YSELNPQDKRRNFTLAFKAAESV-GIPTTLTIDEMVS 91
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
 142-220 3.98e-05

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: 45.23  E-value: 3.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  142 LKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERyLEVPPIIS-SDH--LSSPhlDELSCLT 218
Cdd:cd21254     20 VKITNFTTSWRNGLAFCAILHHFRPDLI-DYKSLNPHDIKENNKKAYDGFAS-LGISRLLEpSDMvlLAVP--DKLTVMT 95


                   ..
gi 1734340282  219 YL 220
Cdd:cd21254     96 YL 97
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 20-111 4.03e-05

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


Pssm-ID: 409141  Cd Length: 145  Bit Score: 46.12  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   20 FTNWINEQLQGNV-----------IRDLTQDLSDGVNLIKLVEILQ----GRRYYGKvydQDPTEIQKLMNVQMALDALR 84
Cdd:cd21292     29 FVNWINKNLGDDPdckhllpmdpnTDDLFEKVKDGILLCKMINLSVpdtiDERAINK---KKLTVFTIHENLTLALNSAS 105

                           90       100
                   ....*....|....*....|....*..
gi 1734340282   85 EDGVKTVNIGSHDIVDGNEKLILGLIW 111
Cdd:cd21292    106 AIGCNVVNIGAEDLKEGKPHLVLGLLW 132
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 242-327 4.80e-05

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: 44.97  E-value: 4.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  242 LPDCNVDDLEHSWSDGFLLAHLVEICggrVPELERMRFDNLNDF--VENVAIVLDAAA-DIGV-GSLIGADDIAEPQgeH 317
Cdd:pfam00307   19 GPGVRVTNFTTDLRDGLALCALLNKL---APGLVDKKKLNKSEFdkLENINLALDVAEkKLGVpKVLIEPEDLVEGD--N 93

                           90
                   ....*....|
gi 1734340282  318 LGTMALVAAL 327
Cdd:pfam00307   94 KSVLTYLASL 103
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 128-221 5.55e-05

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: 44.56  E-value: 5.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWI-QSALP--ELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIISSD 204
Cdd:cd21234      2 EKILLSWVrQSTRPysQVNVLNFTTSWTDGLAFNAVLHRHKPDLF-SWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPE 80

                           90
                   ....*....|....*..
gi 1734340282  205 HLSSPHLDELSCLTYLS 221
Cdd:cd21234     81 DVAVQLPDKKSIIMYLT 97
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 18-115 7.90e-05

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: 45.39  E-value: 7.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   18 HTFTNWINEQLQGN-----VI------RDLTQDLSDGVNLIKLVEILQGRRYYGKVYDQD---PTEIQKlmNVQMALDAL 83
Cdd:cd21324     27 YAFVNWINKALENDpdckhVIpmnpntDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKkltPFTIQE--NLNLALNSA 104

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1734340282   84 REDGVKTVNIGSHDIVDGNEKLILGLIWCLVQ 115
Cdd:cd21324    105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIK 136
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 246-327 1.86e-04

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: 43.07  E-value: 1.86e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   246 NVDDLEHSWSDGFLLAHLVEI-----CGGRVPELERMRFDNLndfvENVAIVLDAAADIGV-GSLIGADDIAEpqGEHLg 319
Cdd:smart00033   18 PVTNFSSDLKDGVALCALLNSlspglVDKKKVAASLSRFKKI----ENINLALSFAEKLGGkVVLFEPEDLVE--GPKL- 90


                    ....*...
gi 1734340282   320 TMALVAAL 327
Cdd:smart00033   91 ILGVIWTL 98
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 129-223 1.92e-04

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


Pssm-ID: 409036  Cd Length: 104  Bit Score: 43.19  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  129 KLVMAWIQSA---LPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIISSDH 205
Cdd:cd21187      3 KTLLAWCRQStrgYEQVDVKNFTTSWRDGLAFNALIHRHRPDLF-DFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81

                           90
                   ....*....|....*...
gi 1734340282  206 LSSPHLDELSCLTYLSYF 223
Cdd:cd21187     82 VNVEQPDKKSILMYVTSL 99
Filamin pfam00630
Filamin/ABP280 repeat;
1836-1886 3.41e-04

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 41.89  E-value: 3.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1734340282 1836 IPGANGGP-PTEVdtkVKKSSSKYEISFKPTEVGTHKVFAYVNDMQHPLSPF 1886
Cdd:pfam00630   40 VTGPDGSPvPVEV---TDNGDGTYTVSYTPTEPGDYTVSVKFNGQHIPGSPF 88
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
 128-204 5.56e-04

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


Pssm-ID: 409049  Cd Length: 107  Bit Score: 41.94  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQS---ALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAERYLEVPPIISSD 204
Cdd:cd21200      3 KQMLLEWCQAktrGYEHVDITNFSSSWSDGMAFCALIHHFFPDAF-DYSSLDPKNRRKNFELAFSTAEELADIAPLLEVE 81
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 242-325 6.67e-04

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: 41.60  E-value: 6.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  242 LPDCNVDDLEHSWSDGFLLAHLVEICG-GRVPELERMrfdNLNDFVENVAIVLDAAAD-IGVGSLIGADDIAEPQGEHLG 319
Cdd:cd21230     14 IPQLPITNFTTDWNDGRALGALVDSCApGLCPDWETW---DPNDALENATEAMQLAEDwLGVPQLITPEEIINPNVDEMS 90


                   ....*.
gi 1734340282  320 TMALVA 325
Cdd:cd21230     91 VMTYLS 96
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 21-85 8.17e-04

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


Pssm-ID: 409070  Cd Length: 106  Bit Score: 41.49  E-value: 8.17e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734340282   21 TNWINEQLQGN--VIRDLTQDLSDGVNLIKLVEILQGRRY-YGKVYDQDPTEIQKLMNVqmaLDALRE 85
Cdd:cd21221      7 TEWINEELADDriVVRDLEEDLFDGQVLQALLEKLANEKLeVPEVAQSEEGQKQKLAVV---LACVNF 71
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
 128-237 9.78e-04

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


Pssm-ID: 409108  Cd Length: 112  Bit Score: 41.51  E-value: 9.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  128 KKLVMAWIQS---ALPELKLTNFRTNWNDGIALSALLEycqpGLCPE---WRNLDPSEARENCHRALLLAERYLEVPPII 201
Cdd:cd21259      3 KQMLLDWCRAktrGYENVDIQNFSSSWSDGMAFCALVH----NFFPEafdYSQLSPQNRRHNFEVAFSSAEKHADCPQLL 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1734340282  202 SSDHLSSPHLDELSCL-TYLSYFitkgapgYRATLKK 237
Cdd:cd21259     79 DVEDMVRMREPDWKCVyTYIQEF-------YRCLVQK 108
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 127-223 1.62e-03

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


Pssm-ID: 409075  Cd Length: 103  Bit Score: 40.53  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  127 PKKLVMAWIQS-----ALPELklTNFRTNWNDGIALSALLEYCQP--GLCPEWRNLDPsEARenCHRALLLAERYLEVPP 199
Cdd:cd21226      1 SEDGLLAWCRQttegyDGVNI--TSFKSSFNDGRAFLALLHAYDPelFKQAAIEQMDA-EAR--LNLAFDFAEKKLGIPK 75

                           90       100
                   ....*....|....*....|....
gi 1734340282  200 IISSDHLSSPHLDELSCLTYLSYF 223
Cdd:cd21226     76 LLEAEDVMTGNPDERSIVLYTSLF 99
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
 131-223 1.65e-03

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


Pssm-ID: 409106  Cd Length: 112  Bit Score: 40.78  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  131 VMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCPeWRNLDPSEARENCHRALLLAERYLEVPPIISSDHLS 207
Cdd:cd21257     13 LLKWCQkktEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQDKKRNLLLAFQAAESVGIKPSLELSEMMY 91

                           90       100
                   ....*....|....*....|
gi 1734340282  208 SPHLDELSCLTYLS----YF 223
Cdd:cd21257     92 TDRPDWQSVMQYVAqiykYF 111
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
 128-192 2.74e-03

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


Pssm-ID: 409105  Cd Length: 119  Bit Score: 40.44  E-value: 2.74e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734340282  128 KKLVMAWIQ---SALPELKLTNFRTNWNDGIALSALLEYCQPGLCPeWRNLDPSEARENCHRALLLAE 192
Cdd:cd21256     16 RNALLKWCQkktEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKRRNFTLAFQAAE 82
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 256-323 3.11e-03

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: 39.88  E-value: 3.11e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1734340282  256 DGFLLAHLVEICGGRVPELERMRFDNLNDF--VENVAIVLDAAADIGVGSLIG-----ADDIAEPQGEHlgTMAL 323
Cdd:cd21223     35 DGVRLCRLVELLTGDWSLLSKLRVPAISRLqkLHNVEVALKALKEAGVLRGGDgggitAKDIVDGHREK--TLAL 107
CH_PARVA_rpt1 cd21335
first calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, ...
 17-85 4.50e-03

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


Pssm-ID: 409184  Cd Length: 115  Bit Score: 39.63  E-value: 4.50e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1734340282   17 LHTFTNWINEQLQGN--VIRDLTQDLSDGVNLIKLVEILQGRRYygKVYDQDPTEIQKLMNVQMALDALRE 85
Cdd:cd21335      8 MKVLIDWINDVLVGEriIVKDLAEDLYDGQVLQKLFEKLEGEKL--NVAEVTQSEIAQKQKLQTVLEKINE 76
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 239-312 5.91e-03

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: 39.09  E-value: 5.91e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734340282  239 SMLLPDCNVDDLEHSWSDGFLLAHLVE-ICGGRVPELERMRFDNLNDF--VENVAIVLDAAADIGVGSL-IGADDIAE 312
Cdd:cd21217     22 HLLPIDPDGDDLFEALRDGVLLCKLINkIVPGTIDERKLNKKKPKNIFeaTENLNLALNAAKKIGCKVVnIGPQDILD 99
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
 128-193 6.71e-03

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


Pssm-ID: 409110  Cd Length: 107  Bit Score: 38.79  E-value: 6.71e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1734340282  128 KKLVMAWIQS---ALPELKLTNFRTNWNDGIALSALLEYCQPGLCpEWRNLDPSEARENCHRALLLAER 193
Cdd:cd21261      3 KQILLEWCRSktiGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAF-DYDSLSPSNRKHNFELAFSMAEK 70
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 22-57 8.30e-03

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


Pssm-ID: 409153  Cd Length: 107  Bit Score: 38.45  E-value: 8.30e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1734340282   22 NWINEQLQGN--VIRDLTQDLSDGVNLIKLVEILQGRR 57
Cdd:cd21304      8 EWINDELAEQriIVKDIEEDLYDGQVLQKLLEKLTGVK 45
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 22-102 8.79e-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: 38.05  E-value: 8.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282   22 NWINEQLQGNVIRDLTQDLSDGVNLIKLVEILQGRryYGKVYDQDPTEiqKLMNVQMALDALREDGVKTVnIGSHDIVDG 101
Cdd:cd21185      8 RWVRQLLPDVDVNNFTTDWNDGRLLCGLVNALGGS--VPGWPNLDPEE--SENNIQRGLEAGKSLGVEPV-LTAEEMADP 82


                   .
gi 1734340282  102 N 102
Cdd:cd21185     83 E 83
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 235-312 9.13e-03

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: 38.52  E-value: 9.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734340282  235 LKKVSMllpdcNVDDLEHSWSDGFLLAHLVE-ICGGRVPELER--MRFDNLNdfveNVAIVLDAAADIGVGSL-IGADDI 310
Cdd:cd21214     18 LRKAGT-----QIENIEEDFRDGLKLMLLLEvISGERLPKPERgkMRFHKIA----NVNKALDFIASKGVKLVsIGAEEI 88


                   ..
gi 1734340282  311 AE 312
Cdd:cd21214     89 VD 90
 
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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