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Conserved domains on  [gi|1789991031|emb|CAH04741|]
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Spectrin beta chain [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
38-142 4.64e-64

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: 213.42  E-value: 4.64e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   38 DNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKLVNI 117
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
                           90       100
                   ....*....|....*....|....*
gi 1789991031  118 RPEDIVEGNGKLTLGLIWTIILNFQ 142
Cdd:cd21188     81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
180-286 6.24e-60

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: 201.47  E-value: 6.24e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLL 259
Cdd:cd21189      1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQ--SNRENLENAFNVAEKEFGVTRLL 78
                           90       100
                   ....*....|....*....|....*..
gi 1789991031  260 DAEDVDTNNPDEKSIITYVSSLYNALP 286
Cdd:cd21189     79 DPEDVDVPEPDEKSIITYVSSLYDVFP 105
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
695-759 3.51e-26

SH3 domain; This entry represents an SH3 domain.


:

Pssm-ID: 407754  Cd Length: 65  Bit Score: 103.50  E-value: 3.51e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1789991031  695 PLWQRGERIPHPIKVTALCDYSDENVTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPSVVFRIP 759
Cdd:pfam17902    1 PLKQRRSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
520-693 1.13e-21

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 95.98  E-value: 1.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  520 LIAFVRAAQLELIWVSERESIEVTRNWSDIKQlDLPMLTNYYKQLLHEMELREKQYNDVHNQGAALLNQGHPAIRVIEVY 599
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  600 LRQMQSQWDWLLALSKCLEEHLRDALNLKSFMEEASDAEAWIQEQSVRLENNYNRTDfsLEEGERFLRELDEIKEILNKY 679
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD--LESVEELLKKHKELEEELEAH 158
                          170
                   ....*....|....
gi 1789991031  680 HQVLMALTERCASI 693
Cdd:cd00176    159 EPRLKSLNELAEEL 172
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
875-1089 9.01e-11

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 64.39  E-value: 9.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  875 QYDQKMAELLKKLEEAWRELNDAVgkpISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQL--PNPTPTQRVNH- 951
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieEGHPDAEEIQEr 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  952 -DRLNGLWDDLWDLSRMYVERIKVLESVLNGMVEVADI---VRQHEITLNSfDDLPAALDKLRGHHSQLLEINMVLKQQQ 1027
Cdd:cd00176     81 lEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLeqwLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789991031 1028 TVIDQLNRNVALLrqhvsrtrINEGHHPDVDAIEDEVQKLNVRWENVNSQIASRLLAVESAL 1089
Cdd:cd00176    160 PRLKSLNELAEEL--------LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1000-1228 4.92e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 53.22  E-value: 4.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031 1000 DDLPAALDKLRGHHsqllEINMVLKQQQTVIDQLNRNVallrqhvsrTRINEGHHPDVDAIEDEVQKLNVRWENVNSQIA 1079
Cdd:cd00176     30 DDLESVEALLKKHE----ALEAELAAHEERVEALNELG---------EQLIEEGHPDAEEIQERLEELNQRWEELRELAE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031 1080 SRLLAVESALQIQMVYRSEYETEmSWLDTVEETINRLRKPEELrpEQYQQQLDMLIAEYTNLQEHTQAIEHVNKEGGRFI 1159
Cdd:cd00176     97 ERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDLGKDL--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELL 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1789991031 1160 HEakifdaklgqysdgivgihgpgiksefrrtkpQPKNGSQIVTEELELLNRRFAQLSSLILERRNTMQ 1228
Cdd:cd00176    174 EE--------------------------------GHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
424-518 3.48e-05

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.01  E-value: 3.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   424 FSRVEECIEWVRVRMEKLTTMEFLEDLETLEHVFEQHKFDNRDIQDFRQNVDECIARQAEVSAEDTYEYCEL---LRVLE 500
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIeerLEELN 83
                            90
                    ....*....|....*...
gi 1789991031   501 SEYQQLRDLSAGRMLDLD 518
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
1465-1502 5.16e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.85  E-value: 5.16e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1789991031  1465 QDLPTVLNTTWGIHHPETRQPITLSEAIRIGLYDSNIR 1502
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2463-2497 9.74e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 9.74e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1789991031  2463 NYVDRSSVSVRDPSSGQQYSYQEAVDRRIVDADRG 2497
Cdd:smart00250    4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2780-2817 3.50e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 3.50e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1789991031  2780 LKPVYQAIASEGVFDPTKGHHVPVTTALNDGLINASTG 2817
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2723-2763 4.02e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 4.02e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1789991031  2723 QGLVDVTLSEvlpKGIIHPGTGERIDIKRGIELRIIDAATG 2763
Cdd:smart00250    1 QRLLEAQSAI---GGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2201-2237 9.84e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 36.31  E-value: 9.84e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1789991031  2201 TQSWEFDTQQGVFVDNLTGEKLSLERALATGKVAPED 2237
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
 
Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
38-142 4.64e-64

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: 213.42  E-value: 4.64e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   38 DNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKLVNI 117
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
                           90       100
                   ....*....|....*....|....*
gi 1789991031  118 RPEDIVEGNGKLTLGLIWTIILNFQ 142
Cdd:cd21188     81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
180-286 6.24e-60

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: 201.47  E-value: 6.24e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLL 259
Cdd:cd21189      1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQ--SNRENLENAFNVAEKEFGVTRLL 78
                           90       100
                   ....*....|....*....|....*..
gi 1789991031  260 DAEDVDTNNPDEKSIITYVSSLYNALP 286
Cdd:cd21189     79 DPEDVDVPEPDEKSIITYVSSLYDVFP 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
40-284 5.69e-42

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 165.88  E-value: 5.69e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   40 VQKKTFTKWVNKHLSKTD-HKIDDLFVDLRDGYALIALLEALTGERIQK--ENGYTRFHRIQNVQYCLDFLKKKNIKLVN 116
Cdd:COG5069      9 VQKKTFTKWTNEKLISGGqKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLFN 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  117 IRPEDIVEGNGKLTLGLIWTIILNFQVSvirqrlllessqheqmsakhtTTNSQVSLhgsdatSARDALLQWARRVTAGY 196
Cdd:COG5069     89 IGPQDIVDGNPKLILGLIWSLISRLTIA---------------------TINEEGEL------TKHINLLLWCDEDTGGY 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  197 -PRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKIssDSVSNTERLNN--AFAAADREFGVERLLDAEDV-DTNNPDEK 272
Cdd:COG5069    142 kPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVL--DLQKKNKALNNfqAFENANKVIGIARLIGVEDIvNVSIPDER 219
                          250
                   ....*....|..
gi 1789991031  273 SIITYVSSLYNA 284
Cdd:COG5069    220 SIMTYVSWYIIR 231
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
695-759 3.51e-26

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 103.50  E-value: 3.51e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1789991031  695 PLWQRGERIPHPIKVTALCDYSDENVTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPSVVFRIP 759
Cdd:pfam17902    1 PLKQRRSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
180-286 4.41e-26

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: 105.06  E-value: 4.41e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGY-PRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLNNAFAAADREFGVER- 257
Cdd:pfam00307    2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPKv 81
                           90       100
                   ....*....|....*....|....*....
gi 1789991031  258 LLDAEDVdtNNPDEKSIITYVSSLYNALP 286
Cdd:pfam00307   82 LIEPEDL--VEGDNKSVLTYLASLFRRFQ 108
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
39-142 8.79e-25

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: 101.21  E-value: 8.79e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   39 NVQKKTFTKWVNKHLSKTDHK--IDDLFVDLRDGYALIALLEALTGERIQKEN-GYTRFHRIQNVQYCLDFLKKK-NIKL 114
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*...
gi 1789991031  115 VNIRPEDIVEGNGKLTLGLIWTIILNFQ 142
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
43-139 1.21e-24

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: 100.47  E-value: 1.21e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031    43 KTFTKWVNKHLSKTDH-KIDDLFVDLRDGYALIALLEALTGERIQKEN---GYTRFHRIQNVQYCLDFLKKKNIKLVNIR 118
Cdd:smart00033    1 KTLLRWVNSLLAEYDKpPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 1789991031   119 PEDIVEGNgKLTLGLIWTIIL 139
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLIS 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
520-693 1.13e-21

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 95.98  E-value: 1.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  520 LIAFVRAAQLELIWVSERESIEVTRNWSDIKQlDLPMLTNYYKQLLHEMELREKQYNDVHNQGAALLNQGHPAIRVIEVY 599
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  600 LRQMQSQWDWLLALSKCLEEHLRDALNLKSFMEEASDAEAWIQEQSVRLENNYNRTDfsLEEGERFLRELDEIKEILNKY 679
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD--LESVEELLKKHKELEEELEAH 158
                          170
                   ....*....|....
gi 1789991031  680 HQVLMALTERCASI 693
Cdd:cd00176    159 EPRLKSLNELAEEL 172
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
183-281 7.55e-21

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: 89.68  E-value: 7.55e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   183 DALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISS--DSVSNTERLNNAFAAADREFGVERLLD 260
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 1789991031   261 AEDVDTNNPDEKSIITYVSSL 281
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
875-1089 9.01e-11

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 64.39  E-value: 9.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  875 QYDQKMAELLKKLEEAWRELNDAVgkpISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQL--PNPTPTQRVNH- 951
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieEGHPDAEEIQEr 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  952 -DRLNGLWDDLWDLSRMYVERIKVLESVLNGMVEVADI---VRQHEITLNSfDDLPAALDKLRGHHSQLLEINMVLKQQQ 1027
Cdd:cd00176     81 lEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLeqwLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789991031 1028 TVIDQLNRNVALLrqhvsrtrINEGHHPDVDAIEDEVQKLNVRWENVNSQIASRLLAVESAL 1089
Cdd:cd00176    160 PRLKSLNELAEEL--------LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
523-621 3.32e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.27  E-value: 3.32e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   523 FVRAAQLELIWVSERESIEVTRNWSDIKQlDLPMLTNYYKQLLHEMELREKQYNDVHNQGAALLNQGHPAIRVIEVYLRQ 602
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLGKDLE-SVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81
                            90
                    ....*....|....*....
gi 1789991031   603 MQSQWDWLLALSKCLEEHL 621
Cdd:smart00150   82 LNERWEELKELAEERRQKL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1000-1228 4.92e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 53.22  E-value: 4.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031 1000 DDLPAALDKLRGHHsqllEINMVLKQQQTVIDQLNRNVallrqhvsrTRINEGHHPDVDAIEDEVQKLNVRWENVNSQIA 1079
Cdd:cd00176     30 DDLESVEALLKKHE----ALEAELAAHEERVEALNELG---------EQLIEEGHPDAEEIQERLEELNQRWEELRELAE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031 1080 SRLLAVESALQIQMVYRSEYETEmSWLDTVEETINRLRKPEELrpEQYQQQLDMLIAEYTNLQEHTQAIEHVNKEGGRFI 1159
Cdd:cd00176     97 ERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDLGKDL--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELL 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1789991031 1160 HEakifdaklgqysdgivgihgpgiksefrrtkpQPKNGSQIVTEELELLNRRFAQLSSLILERRNTMQ 1228
Cdd:cd00176    174 EE--------------------------------GHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
424-518 3.48e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.01  E-value: 3.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   424 FSRVEECIEWVRVRMEKLTTMEFLEDLETLEHVFEQHKFDNRDIQDFRQNVDECIARQAEVSAEDTYEYCEL---LRVLE 500
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIeerLEELN 83
                            90
                    ....*....|....*...
gi 1789991031   501 SEYQQLRDLSAGRMLDLD 518
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
1465-1502 5.16e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.85  E-value: 5.16e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1789991031  1465 QDLPTVLNTTWGIHHPETRQPITLSEAIRIGLYDSNIR 1502
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SPEC smart00150
Spectrin repeats;
875-965 1.28e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.47  E-value: 1.28e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   875 QYDQKMAELLKKLEEAWRELNDavgKPISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQL----PNPTPTQRVN 950
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLAS---EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieegHPDAEEIEER 78
                            90
                    ....*....|....*
gi 1789991031   951 HDRLNGLWDDLWDLS 965
Cdd:smart00150   79 LEELNERWEELKELA 93
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
311-519 4.35e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 44.36  E-value: 4.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  311 NEKLDLILKRIEDVEARV-DTSPPAAVE------RTVSEIVDDLNALESPIARFFEDVEELKSMQHPEANDFYKQVYGLH 383
Cdd:cd00176      6 LRDADELEAWLSEKEELLsSTDYGDDLEsveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  384 QRRTTYLDRLtnqilvrlgvrtdslhKENQQRLENMRK--TSFSRVEECIEWVRVRMEKLTTMEFLEDLETLEHVFEQHK 461
Cdd:cd00176     86 QRWEELRELA----------------EERRQRLEEALDlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHK 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789991031  462 FDNRDIQDFRQNVDECIARQAEV----SAEDTYEYCELLRVLESEYQQLRDLSAGRMLDLDS 519
Cdd:cd00176    150 ELEEELEAHEPRLKSLNELAEELleegHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
875-976 6.67e-04

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 41.54  E-value: 6.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  875 QYDQKMAELLKKLEEAWRELNDavgKPISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQL-PNPTPTQRVNHDR 953
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSS---EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLiDEGHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 1789991031  954 LNGLwDDLWD-LSRMYVERIKVLE 976
Cdd:pfam00435   82 LEEL-NERWEqLLELAAERKQKLE 104
SH3_ITK cd11908
Src Homology 3 domain of Interleukin-2-inducible T-cell Kinase; ITK (also known as Tsk or Emt) ...
709-753 7.63e-04

Src Homology 3 domain of Interleukin-2-inducible T-cell Kinase; ITK (also known as Tsk or Emt) is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. ITK is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, ITK plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, ITK is crucial for the development of T-helper(Th)2 effector responses. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212841 [Multi-domain]  Cd Length: 56  Bit Score: 40.00  E-value: 7.63e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1789991031  709 VTALCDYSDEN---VTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPS 753
Cdd:cd11908      3 VIALYDYQTNDpqeLALRYNEEYHLLDSSEIHWWRVQDKNGHEGYVPS 50
PLEC smart00250
Plectin repeat;
2463-2497 9.74e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 9.74e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1789991031  2463 NYVDRSSVSVRDPSSGQQYSYQEAVDRRIVDADRG 2497
Cdd:smart00250    4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2780-2817 3.50e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 3.50e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1789991031  2780 LKPVYQAIASEGVFDPTKGHHVPVTTALNDGLINASTG 2817
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2723-2763 4.02e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 4.02e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1789991031  2723 QGLVDVTLSEvlpKGIIHPGTGERIDIKRGIELRIIDAATG 2763
Cdd:smart00250    1 QRLLEAQSAI---GGIIDPETGQKLSVEEALRRGLIDPETG 38
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
424-517 7.28e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 38.84  E-value: 7.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  424 FSRVEECIEWVRVRMEKLTTMEFLEDLETLEHVFEQHKFDNRDIQDFRQNVDECIARQAEVSAEDTYEYCEL---LRVLE 500
Cdd:pfam00435    7 FRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIqerLEELN 86
                           90
                   ....*....|....*..
gi 1789991031  501 SEYQQLRDLSAGRMLDL 517
Cdd:pfam00435   87 ERWEQLLELAAERKQKL 103
PLEC smart00250
Plectin repeat;
2201-2237 9.84e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 36.31  E-value: 9.84e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1789991031  2201 TQSWEFDTQQGVFVDNLTGEKLSLERALATGKVAPED 2237
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
 
Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
38-142 4.64e-64

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: 213.42  E-value: 4.64e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   38 DNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKLVNI 117
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
                           90       100
                   ....*....|....*....|....*
gi 1789991031  118 RPEDIVEGNGKLTLGLIWTIILNFQ 142
Cdd:cd21188     81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
180-286 6.24e-60

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: 201.47  E-value: 6.24e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLL 259
Cdd:cd21189      1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQ--SNRENLENAFNVAEKEFGVTRLL 78
                           90       100
                   ....*....|....*....|....*..
gi 1789991031  260 DAEDVDTNNPDEKSIITYVSSLYNALP 286
Cdd:cd21189     79 DPEDVDVPEPDEKSIITYVSSLYDVFP 105
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
31-146 6.18e-48

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: 168.24  E-value: 6.18e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   31 EKYNDERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKK 110
Cdd:cd21236      8 ERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRR 87
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1789991031  111 NIKLVNIRPEDIVEGNGKLTLGLIWTIILNFQVSVI 146
Cdd:cd21236     88 QVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
35-147 1.69e-44

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: 157.88  E-value: 1.69e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   35 DERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKL 114
Cdd:cd21235      1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1789991031  115 VNIRPEDIVEGNGKLTLGLIWTIILNFQVSVIR 147
Cdd:cd21235     81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQ 113
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
180-282 6.29e-44

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: 155.63  E-value: 6.29e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLL 259
Cdd:cd21248      2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKS--NALYNLQNAFNVAEQKLGLTKLL 79
                           90       100
                   ....*....|....*....|...
gi 1789991031  260 DAEDVDTNNPDEKSIITYVSSLY 282
Cdd:cd21248     80 DPEDVNVEQPDEKSIITYVVTYY 102
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
180-283 2.09e-43

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: 154.49  E-value: 2.09e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKIS-SDSVSNterLNNAFAAADREFGVERL 258
Cdd:cd21194      2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDpNDHLGN---LNNAFDVAEQELGIAKL 78
                           90       100
                   ....*....|....*....|....*
gi 1789991031  259 LDAEDVDTNNPDEKSIITYVSSLYN 283
Cdd:cd21194     79 LDAEDVDVARPDEKSIMTYVASYYH 103
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
35-139 2.85e-43

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: 154.45  E-value: 2.85e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   35 DERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKEN-GYTRFHRIQNVQYCLDFLKKKNIK 113
Cdd:cd21246     11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTkGKMRIHCLENVDKALQFLKEQRVH 90
                           90       100
                   ....*....|....*....|....*.
gi 1789991031  114 LVNIRPEDIVEGNGKLTLGLIWTIIL 139
Cdd:cd21246     91 LENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
39-143 5.43e-42

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: 150.22  E-value: 5.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   39 NVQKKTFTKWVNKHLSKTDHK-IDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKLVNI 117
Cdd:cd21186      1 DVQKKTFTKWINSQLSKANKPpIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNI 80
                           90       100
                   ....*....|....*....|....*.
gi 1789991031  118 RPEDIVEGNGKLTLGLIWTIILNFQV 143
Cdd:cd21186     81 SSNDIVDGNPKLTLGLVWSIILHWQV 106
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
40-284 5.69e-42

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 165.88  E-value: 5.69e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   40 VQKKTFTKWVNKHLSKTD-HKIDDLFVDLRDGYALIALLEALTGERIQK--ENGYTRFHRIQNVQYCLDFLKKKNIKLVN 116
Cdd:COG5069      9 VQKKTFTKWTNEKLISGGqKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLFN 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  117 IRPEDIVEGNGKLTLGLIWTIILNFQVSvirqrlllessqheqmsakhtTTNSQVSLhgsdatSARDALLQWARRVTAGY 196
Cdd:COG5069     89 IGPQDIVDGNPKLILGLIWSLISRLTIA---------------------TINEEGEL------TKHINLLLWCDEDTGGY 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  197 -PRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKIssDSVSNTERLNN--AFAAADREFGVERLLDAEDV-DTNNPDEK 272
Cdd:COG5069    142 kPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVL--DLQKKNKALNNfqAFENANKVIGIARLIGVEDIvNVSIPDER 219
                          250
                   ....*....|..
gi 1789991031  273 SIITYVSSLYNA 284
Cdd:COG5069    220 SIMTYVSWYIIR 231
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
35-146 1.54e-41

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: 149.41  E-value: 1.54e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   35 DERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKL 114
Cdd:cd21237      1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1789991031  115 VNIRPEDIVEGNGKLTLGLIWTIILNFQVSVI 146
Cdd:cd21237     81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDI 112
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
26-139 8.85e-41

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: 147.06  E-value: 8.85e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   26 YELNR-EKYNDERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKEN-GYTRFHRIQNVQYC 103
Cdd:cd21193      1 FEKGRiRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNrGRLRVQKIENVNKA 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1789991031  104 LDFLKKKnIKLVNIRPEDIVEGNGKLTLGLIWTIIL 139
Cdd:cd21193     81 LAFLKTK-VRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
36-143 1.47e-39

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: 143.67  E-value: 1.47e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   36 ERDNVQKKTFTKWVNKHLSKTDH--KIDDLFVDLRDGYALIALLEALTGERIQKENG--YTRFHRIQNVQYCLDFLKKKN 111
Cdd:cd21241      1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGrrLKRVHFLSNINTALKFLESKK 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1789991031  112 IKLVNIRPEDIVEGNGKLTLGLIWTIILNFQV 143
Cdd:cd21241     81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
176-283 1.44e-38

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: 140.91  E-value: 1.44e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  176 SDATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSdsvSN-TERLNNAFAAADREFG 254
Cdd:cd21319      1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKK---SNaRHNLEHAFNVAERQLG 77
                           90       100
                   ....*....|....*....|....*....
gi 1789991031  255 VERLLDAEDVDTNNPDEKSIITYVSSLYN 283
Cdd:cd21319     78 ITKLLDPEDVFTENPDEKSIITYVVAFYH 106
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
185-286 1.95e-38

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: 140.26  E-value: 1.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  185 LLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLLDAEDV 264
Cdd:cd21187      5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKD--SPESRLEHAFTVAHEHLGIEKLLDPEDV 82
                           90       100
                   ....*....|....*....|..
gi 1789991031  265 DTNNPDEKSIITYVSSLYNALP 286
Cdd:cd21187     83 NVEQPDKKSILMYVTSLFQVLP 104
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
35-143 1.46e-37

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: 137.75  E-value: 1.46e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   35 DERDNVQKKTFTKWVNKHLSKT-DHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIK 113
Cdd:cd21231      1 YEREDVQKKTFTKWINAQFAKFgKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1789991031  114 LVNIRPEDIVEGNGKLTLGLIWTIILNFQV 143
Cdd:cd21231     81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
41-139 1.68e-37

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: 137.52  E-value: 1.68e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   41 QKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQK-ENGYTRFHRIQNVQYCLDFLKKKNIKLVNIRP 119
Cdd:cd21214      6 QRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVSIGA 85
                           90       100
                   ....*....|....*....|
gi 1789991031  120 EDIVEGNGKLTLGLIWTIIL 139
Cdd:cd21214     86 EEIVDGNLKMTLGMIWTIIL 105
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
26-139 7.12e-37

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: 137.08  E-value: 7.12e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   26 YELNREK-YNDERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKEN-GYTRFHRIQNVQYC 103
Cdd:cd21318     23 FECSRIKaLADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTrGRMRIHSLENVDKA 102
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1789991031  104 LDFLKKKNIKLVNIRPEDIVEGNGKLTLGLIWTIIL 139
Cdd:cd21318    103 LQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
177-284 1.64e-36

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: 135.18  E-value: 1.64e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  177 DATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVE 256
Cdd:cd21216      7 EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKD--DPRENLNLAFDVAEKHLDIP 84
                           90       100
                   ....*....|....*....|....*....
gi 1789991031  257 RLLDAED-VDTNNPDEKSIITYVSSLYNA 284
Cdd:cd21216     85 KMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
176-283 1.25e-35

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: 132.87  E-value: 1.25e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  176 SDATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTerLNNAFAAADREFGV 255
Cdd:cd21321      1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYN--LQNAFNVAEKELGL 78
                           90       100
                   ....*....|....*....|....*...
gi 1789991031  256 ERLLDAEDVDTNNPDEKSIITYVSSLYN 283
Cdd:cd21321     79 TKLLDPEDVNVDQPDEKSIITYVATYYH 106
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
180-286 3.15e-35

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


Pssm-ID: 409088  Cd Length: 104  Bit Score: 130.88  E-value: 3.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADReFGVERLL 259
Cdd:cd21239      1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQ--SNLANLEHAFYVAEK-LGVTRLL 77
                           90       100
                   ....*....|....*....|....*..
gi 1789991031  260 DAEDVDTNNPDEKSIITYVSSLYNALP 286
Cdd:cd21239     78 DPEDVDVSSPDEKSVITYVSSLYDVFP 104
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
180-286 3.72e-35

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: 130.91  E-value: 3.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSvsNTERLNNAFAAADREFGVERLL 259
Cdd:cd21238      2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQT--NLENLDQAFSVAERDLGVTRLL 79
                           90       100
                   ....*....|....*....|....*..
gi 1789991031  260 DAEDVDTNNPDEKSIITYVSSLYNALP 286
Cdd:cd21238     80 DPEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
180-283 6.47e-35

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: 130.37  E-value: 6.47e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKI-SSDSVSNterLNNAFAAADREFGVERL 258
Cdd:cd21249      4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLrPDRPLYN---LANAFLVAEQELGISQL 80
                           90       100
                   ....*....|....*....|....*
gi 1789991031  259 LDAEDVDTNNPDEKSIITYVSSLYN 283
Cdd:cd21249     81 LDPEDVAVPHPDERSIMTYVSLYYH 105
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
180-286 6.77e-35

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: 130.16  E-value: 6.77e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADReFGVERLL 259
Cdd:cd21240      4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQ--SNRENLEQAFEVAER-LGVTRLL 80
                           90       100
                   ....*....|....*....|....*..
gi 1789991031  260 DAEDVDTNNPDEKSIITYVSSLYNALP 286
Cdd:cd21240     81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
185-288 9.33e-35

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: 130.05  E-value: 9.33e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  185 LLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSvSNTERLNNAFAAADREFGVERLLDAEDV 264
Cdd:cd21233      5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQ-SATERLDHAFNIARQHLGIEKLLDPEDV 83
                           90       100
                   ....*....|....*....|....
gi 1789991031  265 DTNNPDEKSIITYVSSLYNALPHE 288
Cdd:cd21233     84 ATAHPDKKSILMYVTSLFQVLPQQ 107
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
35-139 4.28e-34

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: 129.02  E-value: 4.28e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   35 DERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQK-ENGYTRFHRIQNVQYCLDFLKKKNIK 113
Cdd:cd21317     26 DEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQKVH 105
                           90       100
                   ....*....|....*....|....*.
gi 1789991031  114 LVNIRPEDIVEGNGKLTLGLIWTIIL 139
Cdd:cd21317    106 LENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
179-286 4.64e-34

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: 127.82  E-value: 4.64e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  179 TSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSvsNTERLNNAFAAADREFGVERL 258
Cdd:cd21243      4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRS--NRENLETAFTVAEKELGIPRL 81
                           90       100
                   ....*....|....*....|....*...
gi 1789991031  259 LDAEDVDTNNPDEKSIITYVSSLYNALP 286
Cdd:cd21243     82 LDPEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
36-143 5.68e-34

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: 127.69  E-value: 5.68e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   36 ERDNVQKKTFTKWVNKHLSKTDHK--IDDLFVDLRDGYALIALLEALTGERIQKENGYT--RFHRIQNVQYCLDFLKKKN 111
Cdd:cd21190      1 EQERVQKKTFTNWINSHLAKLSQPivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1789991031  112 IKLVNIRPEDIVEGNGKLTLGLIWTIILNFQV 143
Cdd:cd21190     81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
177-283 6.29e-34

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: 128.25  E-value: 6.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  177 DATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVsnTERLNNAFAAADREFGVE 256
Cdd:cd21322     14 ETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNA--TYNLQQAFNTAEQHLGLT 91
                           90       100
                   ....*....|....*....|....*..
gi 1789991031  257 RLLDAEDVDTNNPDEKSIITYVSSLYN 283
Cdd:cd21322     92 KLLDPEDVNMEAPDEKSIITYVVSFYH 118
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
40-141 1.38e-33

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: 126.36  E-value: 1.38e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   40 VQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGY--TRFHRIQNVQYCLDFLKKKNIKLVNI 117
Cdd:cd21215      4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNpkMRVQKLENVNKALEFIKSRGVKLTNI 83
                           90       100
                   ....*....|....*....|....
gi 1789991031  118 RPEDIVEGNGKLTLGLIWTIILNF 141
Cdd:cd21215     84 GAEDIVDGNLKLILGLLWTLILRF 107
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
36-143 9.02e-33

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: 124.17  E-value: 9.02e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   36 ERDNVQKKTFTKWVNKHLSK--TDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIK 113
Cdd:cd21242      1 EQEQTQKRTFTNWINSQLAKhsPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1789991031  114 LVNIRPEDIVEGNGKLTLGLIWTIILNFQV 143
Cdd:cd21242     81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
184-285 1.16e-32

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: 123.61  E-value: 1.16e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  184 ALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGVERLLDAED 263
Cdd:cd21253      5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKL--AFTVAEKELGIPALLDAED 82
                           90       100
                   ....*....|....*....|...
gi 1789991031  264 -VDTNNPDEKSIITYVSSLYNAL 285
Cdd:cd21253     83 mVALKVPDKLSILTYVSQYYNYF 105
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
185-286 3.43e-32

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: 122.37  E-value: 3.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  185 LLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISsdSVSNTERLNNAFAAADREFGVERLLDAEDV 264
Cdd:cd21234      5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVV--KMSPVERLEHAFSKAKNHLGIEKLLDPEDV 82
                           90       100
                   ....*....|....*....|..
gi 1789991031  265 DTNNPDEKSIITYVSSLYNALP 286
Cdd:cd21234     83 AVQLPDKKSIIMYLTSLFEVLP 104
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
39-143 4.67e-32

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: 122.04  E-value: 4.67e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   39 NVQKKTFTKWVNKHLSKTDH-KIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKLVNI 117
Cdd:cd21232      1 DVQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 80
                           90       100
                   ....*....|....*....|....*.
gi 1789991031  118 RPEDIVEGNGKLTLGLIWTIILNFQV 143
Cdd:cd21232     81 GGTDIVDGNHKLTLGLLWSIILHWQV 106
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
40-143 2.48e-31

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: 120.08  E-value: 2.48e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   40 VQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQK--ENGYTRFHRIQNVQYCLDFLKKKNIKLVNI 117
Cdd:cd21227      4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
                           90       100
                   ....*....|....*....|....*.
gi 1789991031  118 RPEDIVEGNGKLTLGLIWTIILNFQV 143
Cdd:cd21227     84 GNEDIVNGNLKLILGLIWHLILRYQI 109
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
180-283 2.89e-30

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: 117.12  E-value: 2.89e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTerLNNAFAAADREFGVERLL 259
Cdd:cd21320      2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYN--LQNAFNLAEQHLGLTKLL 79
                           90       100
                   ....*....|....*....|....
gi 1789991031  260 DAEDVDTNNPDEKSIITYVSSLYN 283
Cdd:cd21320     80 DPEDISVDHPDEKSIITYVVTYYH 103
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
181-283 1.14e-29

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


Pssm-ID: 409046  Cd Length: 105  Bit Score: 114.94  E-value: 1.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  181 ARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGVERLLD 260
Cdd:cd21197      1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRL--AFRVAETSLGIPALLD 78
                           90       100
                   ....*....|....*....|....
gi 1789991031  261 AED-VDTNNPDEKSIITYVSSLYN 283
Cdd:cd21197     79 AEDmVTMHVPDRLSIITYVSQYYN 102
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
35-139 1.92e-29

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: 116.30  E-value: 1.92e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   35 DERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQK-ENGYTRFHRIQNVQYCLDFLKKKNIK 113
Cdd:cd21316     48 DEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 127
                           90       100
                   ....*....|....*....|....*.
gi 1789991031  114 LVNIRPEDIVEGNGKLTLGLIWTIIL 139
Cdd:cd21316    128 LENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
36-143 2.60e-29

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: 114.60  E-value: 2.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   36 ERDNVQKKTFTKWVNKHLSKTDH--KIDDLFVDLRDGYALIALLEALTGERIQKENGYT--RFHRIQNVQYCLDFLKKKN 111
Cdd:cd21191      1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSshRIFRLNNIAKALKFLEDSN 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1789991031  112 IKLVNIRPEDIVEGNGKLTLGLIWTIILNFQV 143
Cdd:cd21191     81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQI 112
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
180-279 5.92e-29

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: 113.39  E-value: 5.92e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSvsNTERLNNAFAAADREFGVERLL 259
Cdd:cd21244      5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRS--NRENLEEAFRIAEQELKIPRLL 82
                           90       100
                   ....*....|....*....|
gi 1789991031  260 DAEDVDTNNPDEKSIITYVS 279
Cdd:cd21244     83 EPEDVDVVNPDEKSIMTYVA 102
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
177-285 3.36e-28

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: 111.72  E-value: 3.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  177 DATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDS-VSNterLNNAFAAADREFGV 255
Cdd:cd21290     10 EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDpVTN---LNNAFEVAEKYLDI 86
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1789991031  256 ERLLDAED-VDTNNPDEKSIITYVSSLYNAL 285
Cdd:cd21290     87 PKMLDAEDiVNTARPDEKAIMTYVSSFYHAF 117
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
183-284 7.56e-28

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: 109.86  E-value: 7.56e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  183 DALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSsaiDWNKISSDSVSNTE-RLNNAFAAADREFGVERLLDA 261
Cdd:cd21226      3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDP---ELFKQAAIEQMDAEaRLNLAFDFAEKKLGIPKLLEA 79
                           90       100
                   ....*....|....*....|...
gi 1789991031  262 EDVDTNNPDEKSIITYVSSLYNA 284
Cdd:cd21226     80 EDVMTGNPDERSIVLYTSLFYHA 102
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
181-283 2.01e-27

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


Pssm-ID: 409101  Cd Length: 107  Bit Score: 108.80  E-value: 2.01e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  181 ARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGVERLLD 260
Cdd:cd21252      1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRL--AFEVAERELGIPALLD 78
                           90       100
                   ....*....|....*....|....
gi 1789991031  261 AED-VDTNNPDEKSIITYVSSLYN 283
Cdd:cd21252     79 PEDmVSMKVPDCLSIMTYVSQYYN 102
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
183-285 3.01e-27

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: 108.14  E-value: 3.01e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  183 DALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGVERLLDAE 262
Cdd:cd22198      3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQL--AFDVAEQELGIPPVMTGQ 80
                           90       100
                   ....*....|....*....|....
gi 1789991031  263 D-VDTNNPDEKSIITYVSSLYNAL 285
Cdd:cd22198     81 EmASLAVPDKLSMVSYLSQFYEAF 104
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
180-284 3.66e-27

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: 108.38  E-value: 3.66e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKIS-SDSVSNTERlnnAFAAADREFGVERL 258
Cdd:cd21291     10 TAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDkKDHRGNMQL---AFDIASKEIGIPQL 86
                           90       100
                   ....*....|....*....|....*..
gi 1789991031  259 LDAEDV-DTNNPDEKSIITYVSSLYNA 284
Cdd:cd21291     87 LDVEDVcDVAKPDERSIMTYVAYYFHA 113
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
179-279 4.37e-27

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: 107.89  E-value: 4.37e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  179 TSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERL 258
Cdd:cd21192      2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNR--SPRDNLELAFRIAEQHLNIPRL 79
                           90       100
                   ....*....|....*....|.
gi 1789991031  259 LDAEDVDTNNPDEKSIITYVS 279
Cdd:cd21192     80 LEVEDVLVDKPDERSIMTYVS 100
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
40-144 5.18e-27

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: 108.31  E-value: 5.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   40 VQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRF--HRIQNVQYCLDFLKK-KNIKLVN 116
Cdd:cd21311     15 IQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFrsQKLENVSVALKFLEEdEGIKIVN 94
                           90       100
                   ....*....|....*....|....*...
gi 1789991031  117 IRPEDIVEGNGKLTLGLIWTIILNFQVS 144
Cdd:cd21311     95 IDSSDIVDGKLKLILGLIWTLILHYSIS 122
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
180-285 6.07e-27

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: 107.43  E-value: 6.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNkissdSVSNTERLNN---AFAAADREFGVE 256
Cdd:cd21200      1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYS-----SLDPKNRRKNfelAFSTAEELADIA 75
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1789991031  257 RLLDAED--VDTNNPDEKSIITYVSSLYNAL 285
Cdd:cd21200     76 PLLEVEDmvRMGNRPDWKCVFTYVQSLYRHL 106
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
695-759 3.51e-26

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 103.50  E-value: 3.51e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1789991031  695 PLWQRGERIPHPIKVTALCDYSDENVTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPSVVFRIP 759
Cdd:pfam17902    1 PLKQRRSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
180-286 4.41e-26

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: 105.06  E-value: 4.41e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGY-PRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLNNAFAAADREFGVER- 257
Cdd:pfam00307    2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPKv 81
                           90       100
                   ....*....|....*....|....*....
gi 1789991031  258 LLDAEDVdtNNPDEKSIITYVSSLYNALP 286
Cdd:pfam00307   82 LIEPEDL--VEGDNKSVLTYLASLFRRFQ 108
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
40-141 4.50e-26

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: 104.87  E-value: 4.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   40 VQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQ-KENGYTRF--HRIQNVQYCLDFLKKKNIKLVN 116
Cdd:cd21183      4 IQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKrSYNRRPAFqqHYLENVSTALKFIEADHIKLVN 83
                           90       100
                   ....*....|....*....|....*
gi 1789991031  117 IRPEDIVEGNGKLTLGLIWTIILNF 141
Cdd:cd21183     84 IGSGDIVNGNIKLILGLIWTLILHY 108
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
177-285 7.09e-26

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: 105.17  E-value: 7.09e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  177 DATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDS-VSNterLNNAFAAADREFGV 255
Cdd:cd21287      7 EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDpLTN---LNTAFDVAEKYLDI 83
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1789991031  256 ERLLDAED-VDTNNPDEKSIITYVSSLYNAL 285
Cdd:cd21287     84 PKMLDAEDiVGTARPDEKAIMTYVSSFYHAF 114
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
177-285 3.14e-25

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: 103.27  E-value: 3.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  177 DATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDS-VSNterLNNAFAAADREFGV 255
Cdd:cd21289      7 EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDpIGN---LNTAFEVAEKYLDI 83
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1789991031  256 ERLLDAED-VDTNNPDEKSIITYVSSLYNAL 285
Cdd:cd21289     84 PKMLDAEDiVNTPKPDEKAIMTYVSCFYHAF 114
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
39-142 8.79e-25

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: 101.21  E-value: 8.79e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   39 NVQKKTFTKWVNKHLSKTDHK--IDDLFVDLRDGYALIALLEALTGERIQKEN-GYTRFHRIQNVQYCLDFLKKK-NIKL 114
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*...
gi 1789991031  115 VNIRPEDIVEGNGKLTLGLIWTIILNFQ 142
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
43-139 1.21e-24

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: 100.47  E-value: 1.21e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031    43 KTFTKWVNKHLSKTDH-KIDDLFVDLRDGYALIALLEALTGERIQKEN---GYTRFHRIQNVQYCLDFLKKKNIKLVNIR 118
Cdd:smart00033    1 KTLLRWVNSLLAEYDKpPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 1789991031   119 PEDIVEGNgKLTLGLIWTIIL 139
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLIS 100
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
40-141 1.79e-24

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: 100.26  E-value: 1.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   40 VQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYT---RFHRIQNVQYCLDFLKKKNIKLVN 116
Cdd:cd21228      4 IQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRptfRQMKLENVSVALEFLERESIKLVS 83
                           90       100
                   ....*....|....*....|....*
gi 1789991031  117 IRPEDIVEGNGKLTLGLIWTIILNF 141
Cdd:cd21228     84 IDSSAIVDGNLKLILGLIWTLILHY 108
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
185-283 5.23e-24

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: 99.04  E-value: 5.23e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  185 LLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADrEFGVERLLDAED- 263
Cdd:cd21198      6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKL--AFDAAA-KLGIPRLLDPADm 82
                           90       100
                   ....*....|....*....|
gi 1789991031  264 VDTNNPDEKSIITYVSSLYN 283
Cdd:cd21198     83 VLLSVPDKLSVMTYLHQIRA 102
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
32-143 6.31e-24

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: 99.45  E-value: 6.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   32 KYNDERDNVQKKTFTKWVNKHLSKTDHKID--DLFVDLRDGYALIALLEALTGERIQKEN-GYTRFHRIQNVQYCLDFLK 108
Cdd:cd21247     12 KLQEQRMTMQKKTFTKWMNNVFSKNGAKIEitDIYTELKDGIHLLRLLELISGEQLPRPSrGKMRVHFLENNSKAITFLK 91
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1789991031  109 KKnIKLVNIRPEDIVEGNGKLTLGLIWTIILNFQV 143
Cdd:cd21247     92 TK-VPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
40-145 7.19e-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: 99.33  E-value: 7.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   40 VQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIqkengYTRFH--------RIQNVQYCLDFLKKKN 111
Cdd:cd21310     16 IQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKM-----YRKYHprpnfrqmKLENVSVALEFLDREH 90
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1789991031  112 IKLVNIRPEDIVEGNGKLTLGLIWTIILNFQVSV 145
Cdd:cd21310     91 IKLVSIDSKAIVDGNLKLILGLIWTLILHYSISM 124
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
180-282 2.48e-23

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: 97.43  E-value: 2.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADrEFGVERLL 259
Cdd:cd21199      8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTL--AFKAAE-SVGIPTTL 84
                           90       100
                   ....*....|....*....|....
gi 1789991031  260 DAED-VDTNNPDEKSIITYVSSLY 282
Cdd:cd21199     85 TIDEmVSMERPDWQSVMSYVTAIY 108
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
177-285 3.85e-23

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: 97.07  E-value: 3.85e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  177 DATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDS-VSNterLNNAFAAADREFGV 255
Cdd:cd21288      7 EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDpIGN---INLAMEIAEKHLDI 83
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1789991031  256 ERLLDAED-VDTNNPDEKSIITYVSSLYNAL 285
Cdd:cd21288     84 PKMLDAEDiVNTPKPDERAIMTYVSCFYHAF 114
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
41-137 6.82e-23

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: 95.73  E-value: 6.82e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   41 QKKTFTKWVNKHLSKTDHK--IDDLFVDLRDGYALIALLEALTGERIQK--ENGYTRFHRIQNVQYCLDFLKKKNIKLVN 116
Cdd:cd21212      1 EIEIYTDWANHYLEKGGHKriITDLQKDLGDGLTLVNLIEAVAGEKVPGihSRPKTRAQKLENIQACLQFLAALGVDVQG 80
                           90       100
                   ....*....|....*....|.
gi 1789991031  117 IRPEDIVEGNGKLTLGLIWTI 137
Cdd:cd21212     81 ITAEDIVDGNLKAILGLFFSL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
520-693 1.13e-21

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 95.98  E-value: 1.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  520 LIAFVRAAQLELIWVSERESIEVTRNWSDIKQlDLPMLTNYYKQLLHEMELREKQYNDVHNQGAALLNQGHPAIRVIEVY 599
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  600 LRQMQSQWDWLLALSKCLEEHLRDALNLKSFMEEASDAEAWIQEQSVRLENNYNRTDfsLEEGERFLRELDEIKEILNKY 679
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD--LESVEELLKKHKELEEELEAH 158
                          170
                   ....*....|....
gi 1789991031  680 HQVLMALTERCASI 693
Cdd:cd00176    159 EPRLKSLNELAEEL 172
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
184-286 1.45e-21

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: 92.16  E-value: 1.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  184 ALLQWARRVTAGYPrVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKisSDSVSNTERLNNAFAAADREFGVERLLDAED 263
Cdd:cd21245      7 ALLNWVQRRTRKYG-VAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQ--ALEKSPRENLEDAFRIAQESLGIPPLLEPED 83
                           90       100
                   ....*....|....*....|...
gi 1789991031  264 VDTNNPDEKSIITYVSSLYNALP 286
Cdd:cd21245     84 VMVDSPDEQSIMTYVAQFLEHFP 106
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
180-281 1.63e-21

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: 91.77  E-value: 1.63e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISS-DSVSNTERLNNAFAAadreFGVERL 258
Cdd:cd21255      1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPlDIKENNKKAFEAFAS----LGVPRL 76
                           90       100
                   ....*....|....*....|....
gi 1789991031  259 LDAED-VDTNNPDEKSIITYVSSL 281
Cdd:cd21255     77 LEPADmVLLPIPDKLIVMTYLCQL 100
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
40-145 4.00e-21

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: 91.68  E-value: 4.00e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   40 VQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIqkengYTRFHR--------IQNVQYCLDFLKKKN 111
Cdd:cd21309     17 IQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRM-----YRKYHQrptfrqmqLENVSVALEFLDRES 91
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1789991031  112 IKLVNIRPEDIVEGNGKLTLGLIWTIILNFQVSV 145
Cdd:cd21309     92 IKLVSIDSKAIVDGNLKLILGLVWTLILHYSISM 125
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
40-145 5.43e-21

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: 91.30  E-value: 5.43e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   40 VQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERI-QKENGYTRFHRIQ--NVQYCLDFLKKKNIKLVN 116
Cdd:cd21308     20 IQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQleNVSVALEFLDRESIKLVS 99
                           90       100
                   ....*....|....*....|....*....
gi 1789991031  117 IRPEDIVEGNGKLTLGLIWTIILNFQVSV 145
Cdd:cd21308    100 IDSKAIVDGNLKLILGLIWTLILHYSISM 128
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
183-281 7.55e-21

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: 89.68  E-value: 7.55e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   183 DALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISS--DSVSNTERLNNAFAAADREFGVERLLD 260
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 1789991031   261 AEDVDTNNPDEKSIITYVSSL 281
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
180-285 3.79e-20

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: 88.10  E-value: 3.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWnkissDSVSNTERLNN---AFAAADREFGVE 256
Cdd:cd21261      1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDY-----DSLSPSNRKHNfelAFSMAEKLANCD 75
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1789991031  257 RLLDAED--VDTNNPDEKSIITYVSSLYNAL 285
Cdd:cd21261     76 RLIEVEDmmVMGRKPDPMCVFTYVQSLYNHL 106
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
180-282 6.37e-20

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: 87.78  E-value: 6.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADrEFGVERLL 259
Cdd:cd21257      8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQ--DKKRNLLLAFQAAE-SVGIKPSL 84
                           90       100
                   ....*....|....*....|....
gi 1789991031  260 DAED-VDTNNPDEKSIITYVSSLY 282
Cdd:cd21257     85 ELSEmMYTDRPDWQSVMQYVAQIY 108
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
180-282 2.60e-19

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: 86.28  E-value: 2.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADrEFGVERLL 259
Cdd:cd21256     14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTL--AFQAAE-SVGIKSTL 90
                           90       100
                   ....*....|....*....|....
gi 1789991031  260 DAED-VDTNNPDEKSIITYVSSLY 282
Cdd:cd21256     91 DINEmVRTERPDWQSVMTYVTAIY 114
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
42-139 2.64e-19

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: 85.47  E-value: 2.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   42 KKTFTKWVNKHLSKTDH-KIDDLFVDLRDGYALIALLEALTGERIQKENGY--TRFHRIQNVQYCLDFLKKKNI-KLVNI 117
Cdd:cd00014      1 EEELLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIPKINKKpkSPFKKRENINLFLNACKKLGLpELDLF 80
                           90       100
                   ....*....|....*....|...
gi 1789991031  118 RPEDIVE-GNGKLTLGLIWTIIL 139
Cdd:cd00014     81 EPEDLYEkGNLKKVLGTLWALAL 103
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
182-285 2.71e-19

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


Pssm-ID: 409109  Cd Length: 116  Bit Score: 85.91  E-value: 2.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  182 RDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKIssDSVSNTERLNNAFAAADREFGVERLLDA 261
Cdd:cd21260      3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAEL--DPANRRHNFTLAFSTAEKHADCAPLLEV 80
                           90       100
                   ....*....|....*....|....*
gi 1789991031  262 ED-VDTNNPDEKSIITYVSSLYNAL 285
Cdd:cd21260     81 EDmVRMSVPDSKCVYTYIQELYRSL 105
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
176-294 3.05e-19

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: 85.48  E-value: 3.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  176 SDATSARdaLLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGV 255
Cdd:cd21195      2 GDIRPSK--LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQL--AFDVAEREFGI 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1789991031  256 ERLLDAEDV-DTNNPDEKSIITYVSSLYnalphepEMSRG 294
Cdd:cd21195     78 PPVTTGKEMaSAQEPDKLSMVMYLSKFY-------ELFRG 110
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
180-285 4.35e-19

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: 85.04  E-value: 4.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLL 259
Cdd:cd21259      1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQ--NRRHNFEVAFSSAEKHADCPQLL 78
                           90       100
                   ....*....|....*....|....*..
gi 1789991031  260 DAED-VDTNNPDEKSIITYVSSLYNAL 285
Cdd:cd21259     79 DVEDmVRMREPDWKCVYTYIQEFYRCL 105
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
180-285 8.09e-19

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


Pssm-ID: 409107  Cd Length: 111  Bit Score: 84.33  E-value: 8.09e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLL 259
Cdd:cd21258      1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQ--NRRQNFEVAFSAAEMLADCVPLV 78
                           90       100
                   ....*....|....*....|....*...
gi 1789991031  260 DAED--VDTNNPDEKSIITYVSSLYNAL 285
Cdd:cd21258     79 EVEDmmIMGKKPDSKCVFTYVQSLYNHL 106
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
176-282 1.24e-18

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: 83.84  E-value: 1.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  176 SDATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGV 255
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQL--AFDIAEKEFGI 78
                           90       100
                   ....*....|....*....|....*...
gi 1789991031  256 ERLLDAEDVDT-NNPDEKSIITYVSSLY 282
Cdd:cd21251     79 SPIMTGKEMASvGEPDKLSMVMYLTQFY 106
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
180-281 2.47e-18

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: 82.98  E-value: 2.47e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADrEFGVERLL 259
Cdd:cd21254      1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKK--AYDGFA-SLGISRLL 77
                           90       100
                   ....*....|....*....|...
gi 1789991031  260 DAED-VDTNNPDEKSIITYVSSL 281
Cdd:cd21254     78 EPSDmVLLAVPDKLTVMTYLYQI 100
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
185-294 1.29e-17

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: 81.08  E-value: 1.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  185 LLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGVERLLDAEDV 264
Cdd:cd21250      9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQL--AFDVAEREFGIPPVTTGKEM 86
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1789991031  265 D-TNNPDEKSIITYVSSLYnalphepEMSRG 294
Cdd:cd21250     87 AsAEEPDKLSMVMYLSKFY-------ELFRG 110
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
180-284 2.53e-16

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: 76.89  E-value: 2.53e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDwNKISSDSVSNTERLNNAFAAADREFGVERLL 259
Cdd:cd21184      1 SGKSLLLEW---VNSKIPEYKVKNFTTDWNDGKALAALVDALKPGLIP-DNESLDKENPLENATKAMDIAEEELGIPKII 76
                           90       100
                   ....*....|....*....|....*
gi 1789991031  260 DAEDVDTNNPDEKSIITYVSSLYNA 284
Cdd:cd21184     77 TPEDMVSPNVDELSVMTYLSYFRNA 101
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
40-137 7.35e-16

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: 76.03  E-value: 7.35e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   40 VQKKTFTKWVNKHLSKTD-HKIDDLFVDLRDGYALIALLEALTGERIQKENGY---TRFHRIQNVQYCLDFLKKK-NIKL 114
Cdd:cd21225      4 VQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLepkNRIQMIQNLHLAMLFIEEDlKIRV 83
                           90       100
                   ....*....|....*....|...
gi 1789991031  115 VNIRPEDIVEGNGKLTLGLIWTI 137
Cdd:cd21225     84 QGIGAEDFVDNNKKLILGLLWTL 106
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
42-138 9.85e-15

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: 72.61  E-value: 9.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   42 KKTFTKWVNKHLSKTDH---------KIDDLFVDLRDGYALIALLE-ALTG----ERIQKENGYTRFHRIQNVQYCLDFL 107
Cdd:cd21217      3 KEAFVEHINSLLADDPDlkhllpidpDGDDLFEALRDGVLLCKLINkIVPGtideRKLNKKKPKNIFEATENLNLALNAA 82
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1789991031  108 KKKNIKLVNIRPEDIVEGNGKLTLGLIWTII 138
Cdd:cd21217     83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
182-283 4.25e-14

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: 70.45  E-value: 4.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  182 RDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSN-TERLNNAFAAADREF-GVERLL 259
Cdd:cd00014      1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKkRENINLFLNACKKLGlPELDLF 80
                           90       100
                   ....*....|....*....|....
gi 1789991031  260 DAEDVdTNNPDEKSIITYVSSLYN 283
Cdd:cd00014     81 EPEDL-YEKGNLKKVLGTLWALAL 103
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
41-141 1.19e-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: 69.63  E-value: 1.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   41 QKKTFTKWVNKHLSK--TDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFH--RIQNVQYCLDFLKKKNIKLVN 116
Cdd:cd21213      1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDaeRKENVEKVLQFMASKRIRMHQ 80
                           90       100
                   ....*....|....*....|....*
gi 1789991031  117 IRPEDIVEGNGKLTLGLIWTIILNF 141
Cdd:cd21213     81 TSAKDIVDGNLKAIMRLILALAAHF 105
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
34-135 2.11e-13

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 68.85  E-value: 2.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   34 NDERDnvqKKTFTKWVNKHLskTDHKIDDLFVDLRDGYALIALLEAL-----TGERIQKENGYTRFHRIQNVQYCLDFLK 108
Cdd:cd21219      1 EGSRE---ERAFRMWLNSLG--LDPLINNLYEDLRDGLVLLQVLDKIqpgcvNWKKVNKPKPLNKFKKVENCNYAVDLAK 75
                           90       100
                   ....*....|....*....|....*..
gi 1789991031  109 KKNIKLVNIRPEDIVEGNGKLTLGLIW 135
Cdd:cd21219     76 KLGFSLVGIGGKDIADGNRKLTLALVW 102
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
33-141 1.43e-12

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: 66.84  E-value: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   33 YNDERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGY----TRFHRIQNVQYCLDFLK 108
Cdd:cd21222      9 EAPEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHltpsTDDEKLHNVKLALELME 88
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1789991031  109 KKNIKLVNIRPEDIVEGNGKLTLGLIWTIILNF 141
Cdd:cd21222     89 DAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
424-625 2.15e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 69.01  E-value: 2.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  424 FSRVEECIEWVRVRMEKLTTMEFLEDLETLEHVFEQHKFDNRDIQDFRQNVDECIARQAEVSAEDTYEYCEL---LRVLE 500
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIqerLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  501 SEYQQLRDLSAGRMLDLDSLIA---FVRAAQLELIWVSERESIEVTRNWSDIKQlDLPMLTNYYKQLLHEMELREKQYND 577
Cdd:cd00176     86 QRWEELRELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEELEAHEPRLKS 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1789991031  578 VHNQGAALLNQGHP-AIRVIEVYLRQMQSQWDWLLALSKCLEEHLRDAL 625
Cdd:cd00176    165 LNELAEELLEEGHPdADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
43-137 2.44e-12

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: 65.82  E-value: 2.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   43 KTFTKWVNKHLSKTDHK--IDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHR--IQNVQYCLDFLKKKNIKLVNIR 118
Cdd:cd21286      3 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSqmIENVDVCLSFLAARGVNVQGLS 82
                           90
                   ....*....|....*....
gi 1789991031  119 PEDIVEGNGKLTLGLIWTI 137
Cdd:cd21286     83 AEEIRNGNLKAILGLFFSL 101
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
38-137 2.93e-12

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: 66.14  E-value: 2.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   38 DNVQKKTFTKWVNKHLSKTDHK--IDDLFVDLRDGYALIALLEALTGERIQKENG--YTRFHRIQNVQYCLDFLKKKNIK 113
Cdd:cd21285      8 NGFDKQIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
                           90       100
                   ....*....|....*....|....
gi 1789991031  114 LVNIRPEDIVEGNGKLTLGLIWTI 137
Cdd:cd21285     88 IQGLSAEEIRNGNLKAILGLFFSL 111
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
57-138 1.05e-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: 64.15  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   57 DHKIDDLFVDLRDGYALIALLEALTGER----IQKENGYTRFHRIQNVQYCLDFLKKKNI----KLVNIRPEDIVEGNGK 128
Cdd:cd21223     23 DFAVTNLAVDLRDGVRLCRLVELLTGDWsllsKLRVPAISRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHRE 102
                           90
                   ....*....|
gi 1789991031  129 LTLGLIWTII 138
Cdd:cd21223    103 KTLALLWRII 112
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
178-285 1.27e-11

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


Pssm-ID: 409045  Cd Length: 106  Bit Score: 63.53  E-value: 1.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  178 ATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISsdSVSNTERLNNAFAAADREFGVER 257
Cdd:cd21196      1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQ--GLGALEATAWALKVAENELGITP 78
                           90       100
                   ....*....|....*....|....*...
gi 1789991031  258 LLDAEDVDTNNpDEKSIITYVSSLYNAL 285
Cdd:cd21196     79 VVSAQAVVAGS-DPLGLIAYLSHFHSAF 105
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
183-285 2.41e-11

second 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 CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409073 [Multi-domain]  Cd Length: 138  Bit Score: 63.86  E-value: 2.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  183 DALLQWARRVTAGYpRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKI---------------------SSDSVSNTER 241
Cdd:cd21224      3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIrqpttqtvdraqdeaedfwvaEFSPSTGDSG 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1789991031  242 LNNAFAAADRE-F-----------GVERLLDAEDVDTNNPDEKSIITYVSSLYNAL 285
Cdd:cd21224     82 LSSELLANEKRnFklvqqavaelgGVPALLRASDMSNTIPDEKVVILFLSYLCARL 137
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
185-279 8.35e-11

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: 61.25  E-value: 8.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  185 LLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAI-DWNKIS-SDSVSNTERlnnAFAAADREFGVERLLDAE 262
Cdd:cd21229      8 MLAW---LQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDpSNSLENCRR---AMDLAKREFNIPMVLSPE 81
                           90
                   ....*....|....*..
gi 1789991031  263 DVDTNNPDEKSIITYVS 279
Cdd:cd21229     82 DLSSPHLDELSGMTYLS 98
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
875-1089 9.01e-11

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 64.39  E-value: 9.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  875 QYDQKMAELLKKLEEAWRELNDAVgkpISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQL--PNPTPTQRVNH- 951
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieEGHPDAEEIQEr 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  952 -DRLNGLWDDLWDLSRMYVERIKVLESVLNGMVEVADI---VRQHEITLNSfDDLPAALDKLRGHHSQLLEINMVLKQQQ 1027
Cdd:cd00176     81 lEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLeqwLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789991031 1028 TVIDQLNRNVALLrqhvsrtrINEGHHPDVDAIEDEVQKLNVRWENVNSQIASRLLAVESAL 1089
Cdd:cd00176    160 PRLKSLNELAEEL--------LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
523-621 3.32e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.27  E-value: 3.32e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   523 FVRAAQLELIWVSERESIEVTRNWSDIKQlDLPMLTNYYKQLLHEMELREKQYNDVHNQGAALLNQGHPAIRVIEVYLRQ 602
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLGKDLE-SVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81
                            90
                    ....*....|....*....
gi 1789991031   603 MQSQWDWLLALSKCLEEHL 621
Cdd:smart00150   82 LNERWEELKELAEERRQKL 100
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
180-284 3.83e-10

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: 59.32  E-value: 3.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAI----DWNKisSDSVSNTERlnnAFAAADREFGV 255
Cdd:cd21230      1 TPKQRLLGW---IQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDP--NDALENATE---AMQLAEDWLGV 72
                           90       100
                   ....*....|....*....|....*....
gi 1789991031  256 ERLLDAEDVDTNNPDEKSIITYVSSLYNA 284
Cdd:cd21230     73 PQLITPEEIINPNVDEMSVMTYLSQFPKA 101
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
41-138 5.53e-10

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: 59.44  E-value: 5.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   41 QKKTFTKWVNKHlsKTDHKIDDLFVDLRDGYALIALLEALTG-----ERIQKENGYTRFHRIQNVQYCLDFLKKKNIKLV 115
Cdd:cd21299      5 EERCFRLWINSL--GIDTYVNNVFEDVRDGWVLLEVLDKVSPgsvnwKHANKPPIKMPFKKVENCNQVVKIGKQLKFSLV 82
                           90       100
                   ....*....|....*....|...
gi 1789991031  116 NIRPEDIVEGNGKLTLGLIWTII 138
Cdd:cd21299     83 NVAGNDIVQGNKKLILALLWQLM 105
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
183-281 8.84e-10

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: 58.08  E-value: 8.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  183 DALLQWARRVTagyPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSD-SVSNTERlnnAFAAAdREFGVERLLDA 261
Cdd:cd21185      4 KATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEeSENNIQR---GLEAG-KSLGVEPVLTA 76
                           90       100
                   ....*....|....*....|
gi 1789991031  262 EDVDTNNPDEKSIITYVSSL 281
Cdd:cd21185     77 EEMADPEVEHLGIMAYAAQL 96
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
43-135 9.98e-10

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: 58.59  E-value: 9.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   43 KTFTKWVNKhlSKTDHKIDDLFVDLRDGYALIALLEALT-GE----RIQKE---NGYTRFHRIQNVQYCLDFLKKKNIKL 114
Cdd:cd21300     10 RVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIpGSvnwkKVNKApasAEISRFKAVENTNYAVELGKQLGFSL 87
                           90       100
                   ....*....|....*....|.
gi 1789991031  115 VNIRPEDIVEGNGKLTLGLIW 135
Cdd:cd21300     88 VGIQGADITDGSRTLTLALVW 108
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
43-137 1.75e-09

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 58.02  E-value: 1.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   43 KTFTKWVNKhLSKTDHkIDDLFVDLRDGYALIALLEaltgeRIQ-------------KENGyTRFHRIQNVQYCLDFLKK 109
Cdd:cd21298      9 KTYRNWMNS-LGVNPF-VNHLYSDLRDGLVLLQLYD-----KIKpgvvdwsrvnkpfKKLG-ANMKKIENCNYAVELGKK 80
                           90       100
                   ....*....|....*....|....*...
gi 1789991031  110 KNIKLVNIRPEDIVEGNGKLTLGLIWTI 137
Cdd:cd21298     81 LKFSLVGIGGKDIYDGNRTLTLALVWQL 108
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
47-137 4.79e-08

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 53.84  E-value: 4.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   47 KWVNKHLSKTDHK---IDDLFVDLRDGYALIALLEALTGERIQKE---NGYTRFHRIQNVQYCLDFLKKKNIKLVnIRPE 120
Cdd:cd21218     17 RWVNYHLKKAGPTkkrVTNFSSDLKDGEVYALLLHSLAPELCDKElvlEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPE 95
                           90
                   ....*....|....*..
gi 1789991031  121 DIVEGNGKLTLGLIWTI 137
Cdd:cd21218     96 DIVSGNPRLNLAFVATL 112
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
39-141 4.25e-07

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


Pssm-ID: 409155  Cd Length: 121  Bit Score: 51.26  E-value: 4.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   39 NVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGY---TRF-HRIQNVQYCLDFLKKKNIKL 114
Cdd:cd21306     15 NVVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHltpTSFeQKVHNVQFAFELMQDAGLPK 94
                           90       100
                   ....*....|....*....|....*..
gi 1789991031  115 VNIRPEDIVEGNGKLTLGLIWTIILNF 141
Cdd:cd21306     95 PKARPEDIVNLDLKSTLRVLYNLFTKY 121
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1000-1228 4.92e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 53.22  E-value: 4.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031 1000 DDLPAALDKLRGHHsqllEINMVLKQQQTVIDQLNRNVallrqhvsrTRINEGHHPDVDAIEDEVQKLNVRWENVNSQIA 1079
Cdd:cd00176     30 DDLESVEALLKKHE----ALEAELAAHEERVEALNELG---------EQLIEEGHPDAEEIQERLEELNQRWEELRELAE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031 1080 SRLLAVESALQIQMVYRSEYETEmSWLDTVEETINRLRKPEELrpEQYQQQLDMLIAEYTNLQEHTQAIEHVNKEGGRFI 1159
Cdd:cd00176     97 ERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDLGKDL--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELL 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1789991031 1160 HEakifdaklgqysdgivgihgpgiksefrrtkpQPKNGSQIVTEELELLNRRFAQLSSLILERRNTMQ 1228
Cdd:cd00176    174 EE--------------------------------GHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
39-142 1.09e-06

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


Pssm-ID: 409186  Cd Length: 129  Bit Score: 50.38  E-value: 1.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   39 NVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGY----TRFHRIQNVQYCLDFLKKKNIKL 114
Cdd:cd21337     19 NVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFltpdSFEQKVLNVSFAFELMQDGGLEK 98
                           90       100
                   ....*....|....*....|....*...
gi 1789991031  115 VNIRPEDIVEGNGKLTLGLIWTIILNFQ 142
Cdd:cd21337     99 PKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
39-142 3.14e-06

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


Pssm-ID: 409187  Cd Length: 130  Bit Score: 49.20  E-value: 3.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   39 NVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTR----FHRIQNVQYCLDFLKKKNIKL 114
Cdd:cd21338     20 SVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTpesfDQKVHNVSFAFELMQDGGLKK 99
                           90       100
                   ....*....|....*....|....*...
gi 1789991031  115 VNIRPEDIVEGNGKLTLGLIWTIILNFQ 142
Cdd:cd21338    100 PKARPEDVVNLDLKSTLRVLYNLFTKYK 127
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
180-284 4.25e-06

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: 48.14  E-value: 4.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAI-DWNkiSSDSVSNTERLNNAFAAADREFGVERL 258
Cdd:cd21314     11 TPKQRLLGW---IQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCpDWE--SWDPNQPVQNAREAMQQADDWLGVPQV 85
                           90       100
                   ....*....|....*....|....*.
gi 1789991031  259 LDAEDVDTNNPDEKSIITYVSSLYNA 284
Cdd:cd21314     86 IAPEEIVDPNVDEHSVMTYLSQFPKA 111
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
27-138 1.00e-05

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 48.12  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   27 ELNREKYNDErdnvQKKTFTKWVNK---------HLSKTDHKIDDLFVDLRDGYAL---IALLEALT-GERIQKENGYTR 93
Cdd:cd21323     15 EGTQHSYSEE----EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLckmINLSQPDTiDERAINKKKLTP 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1789991031   94 FHRIQNVQYCLDFLKKKNIKLVNIRPEDIVEGNGKLTLGLIWTII 138
Cdd:cd21323     91 FTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
41-138 1.56e-05

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


Pssm-ID: 409142  Cd Length: 116  Bit Score: 46.75  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   41 QKKTFTKWVNKHLSK---------TDHKIDDLFVDLRDGYALIALLE-ALTG---ER-IQKENGYTRFHRIQNVQYCLDF 106
Cdd:cd21293      2 EKGSYVDHINRYLGDdpflkqflpIDPSTNDLFDLVKDGVLLCKLINvAVPGtidERaINTKKVLNPWERNENHTLCLNS 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1789991031  107 LKKKNIKLVNIRPEDIVEGNGKLTLGLIWTII 138
Cdd:cd21293     82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
36-146 1.90e-05

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 46.52  E-value: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   36 ERDNVQKKTFTKWVNKhlSKTDHKIDDLFVDLRDGYALIALLE----ALTGERIQKE-----NGYTRfhRIQNVQYCLDF 106
Cdd:cd21329      2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEmtrvPVDWGHVNKPpypalGGNMK--KIENCNYAVEL 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1789991031  107 LKKK-NIKLVNIRPEDIVEGNGKLTLGLIWTIILNFQVSVI 146
Cdd:cd21329     78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
27-138 2.58e-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: 46.97  E-value: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   27 ELNREKYNDERDNVQKKTFTKWVNK---------HLSKTDHKIDDLFVDLRDGYALIALLEA----LTGERIQKENGYTR 93
Cdd:cd21325     11 ELSSEGTQHSYSEEEKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLsvpdTIDERAINKKKLTP 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1789991031   94 FHRIQNVQYCLDFLKKKNIKLVNIRPEDIVEGNGKLTLGLIWTII 138
Cdd:cd21325     91 FIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
SPEC smart00150
Spectrin repeats;
424-518 3.48e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.01  E-value: 3.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   424 FSRVEECIEWVRVRMEKLTTMEFLEDLETLEHVFEQHKFDNRDIQDFRQNVDECIARQAEVSAEDTYEYCEL---LRVLE 500
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIeerLEELN 83
                            90
                    ....*....|....*...
gi 1789991031   501 SEYQQLRDLSAGRMLDLD 518
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
1465-1502 5.16e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.85  E-value: 5.16e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1789991031  1465 QDLPTVLNTTWGIHHPETRQPITLSEAIRIGLYDSNIR 1502
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
10-135 7.19e-05

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 48.40  E-value: 7.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   10 HAVDPSDAQEKevLDHYELNREKYNDERDNVQKKTFTKWVNKHLskTDHKIDDLFVDLRDGYALIALLEALTGE------ 83
Cdd:COG5069    351 HLFNTHPGQEP--LEEEEKPEIEEFDAEGEFEARVFTFWLNSLD--VSPEITNLFGDLRDQLILLQALSKKLMPmtvthk 426
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1789991031   84 --RIQKENG--YTRFHRIQNVQYCLDFLKKKNIKLVNIRPEDIVEGNgKLTLGLIW 135
Cdd:COG5069    427 lvKKQPASGieENRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVW 481
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
41-138 9.35e-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: 45.00  E-value: 9.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   41 QKKTFTKWVNK---------HLSKTDHKIDDLFVDLRDGYALIALLE----ALTGERIQKENGYTRFHRIQNVQYCLDFL 107
Cdd:cd21324     25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINfsvpDTIDERTINKKKLTPFTIQENLNLALNSA 104
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1789991031  108 KKKNIKLVNIRPEDIVEGNGKLTLGLIWTII 138
Cdd:cd21324    105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
36-146 1.23e-04

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 44.61  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   36 ERDNVQKKTFTKWVNKhLSKTDHkIDDLFVDLRDGYALIALLEALT----GERIQKENgYTRF----HRIQNVQYCLDFL 107
Cdd:cd21331     18 EGETREERTFRNWMNS-LGVNPH-VNHLYGDLQDALVILQLYEKIKvpvdWNKVNKPP-YPKLganmKKLENCNYAVELG 94
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1789991031  108 KKK-NIKLVNIRPEDIVEGNGKLTLGLIWTIILNFQVSVI 146
Cdd:cd21331     95 KHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTLNVL 134
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
185-284 1.25e-04

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: 44.00  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  185 LLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILhryrsSAI---------DWNkiSSDSVSNTERlnnAFAAADREFGV 255
Cdd:cd21315     21 LLGW---IQSKVPDLPITNFTNDWNDGKAIGALV-----DALapglcpdweDWD--PKDAVKNAKE---AMDLAEDWLDV 87
                           90       100
                   ....*....|....*....|....*....
gi 1789991031  256 ERLLDAEDVDTNNPDEKSIITYVSSLYNA 284
Cdd:cd21315     88 PQLIKPEEMVNPKVDELSMMTYLSQFPNA 116
SPEC smart00150
Spectrin repeats;
875-965 1.28e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.47  E-value: 1.28e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   875 QYDQKMAELLKKLEEAWRELNDavgKPISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQL----PNPTPTQRVN 950
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLAS---EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieegHPDAEEIEER 78
                            90
                    ....*....|....*
gi 1789991031   951 HDRLNGLWDDLWDLS 965
Cdd:smart00150   79 LEELNERWEELKELA 93
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
21-131 1.31e-04

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


Pssm-ID: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 44.26  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   21 EVLDH-YELNREKYNDerdnvQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGY----TRFH 95
Cdd:cd21307      1 DAIDElFKLGPDKVNT-----VKKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHLSEFFltpsSTSE 75
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1789991031   96 RIQNVQYCLDFLKKKNIKLVNIRPEDIVEGNGKLTL 131
Cdd:cd21307     76 MLHNVTLALELLKEGGLLNFPVNPEDIVNGDSKATI 111
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
36-146 1.44e-04

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 44.21  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   36 ERDNVQKKTFTKWVNKhlSKTDHKIDDLFVDLRDGYALIALLEALT----GERIQKENgYTRF----HRIQNVQYCLDFL 107
Cdd:cd21330      9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPP-YPKLgenmKKLENCNYAVELG 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1789991031  108 KKK-NIKLVNIRPEDIVEGNGKLTLGLIWTIILNFQVSVI 146
Cdd:cd21330     86 KNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLNIL 125
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
33-138 1.62e-04

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


Pssm-ID: 409141  Cd Length: 145  Bit Score: 44.58  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   33 YNDErdnvQKKTFTKWVN---------KHLSKTDHKIDDLFVDLRDGYAL---IALLEALT-GER-IQKENgYTRFHRIQ 98
Cdd:cd21292     21 YSEE----EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLckmINLSVPDTiDERaINKKK-LTVFTIHE 95
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1789991031   99 NVQYCLDFLKKKNIKLVNIRPEDIVEGNGKLTLGLIWTII 138
Cdd:cd21292     96 NLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
180-283 2.07e-04

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 43.44  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWA----RRvtAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDwNKISSDSVSNTERLNNA---FAAAdRE 252
Cdd:cd21218     10 PPEEILLRWVnyhlKK--AGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCD-KELVLEVLSEEDLEKRAekvLQAA-EK 85
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1789991031  253 FGVERLLDAEDVDTNNPDEksIITYVSSLYN 283
Cdd:cd21218     86 LGCKYFLTPEDIVSGNPRL--NLAFVATLFN 114
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
816-979 2.39e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 45.13  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  816 DQRDAIMKALNDDANKLLSELDPNDPL------ALRLR-EELRRTNEHFWNLLNASQKppepdwASQYDQKMAELLKKLE 888
Cdd:cd00176     50 AAHEERVEALNELGEQLIEEGHPDAEEiqerleELNQRwEELRELAEERRQRLEEALD------LQQFFRDADDLEQWLE 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  889 EAWRELNDAvgkPISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQLPNPTPTQRVNH-----DRLNGLWDDLWD 963
Cdd:cd00176    124 EKEAALASE---DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEieeklEELNERWEELLE 200
                          170
                   ....*....|....*.
gi 1789991031  964 LSRmyvERIKVLESVL 979
Cdd:cd00176    201 LAE---ERQKKLEEAL 213
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
180-284 2.85e-04

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: 42.77  E-value: 2.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAI-DWNkiSSDSVSNTERLNNAFAAADREFGVERL 258
Cdd:cd21313      8 TPKQRLLGW---IQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWE--SWDPQKPVDNAREAMQQADDWLGVPQV 82
                           90       100
                   ....*....|....*....|....*.
gi 1789991031  259 LDAEDVDTNNPDEKSIITYVSSLYNA 284
Cdd:cd21313     83 ITPEEIIHPDVDEHSVMTYLSQFPKA 108
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
180-284 3.36e-04

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: 42.87  E-value: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  180 SARDALLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAI-DWNkiSSDSVSNTERLNNAFAAADREFGVERL 258
Cdd:cd21312     12 TPKQRLLGW---IQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWD--SWDASKPVTNAREAMQQADDWLGIPQV 86
                           90       100
                   ....*....|....*....|....*.
gi 1789991031  259 LDAEDVDTNNPDEKSIITYVSSLYNA 284
Cdd:cd21312     87 ITPEEIVDPNVDEHSVMTYLSQFPKA 112
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
311-519 4.35e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 44.36  E-value: 4.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  311 NEKLDLILKRIEDVEARV-DTSPPAAVE------RTVSEIVDDLNALESPIARFFEDVEELKSMQHPEANDFYKQVYGLH 383
Cdd:cd00176      6 LRDADELEAWLSEKEELLsSTDYGDDLEsveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  384 QRRTTYLDRLtnqilvrlgvrtdslhKENQQRLENMRK--TSFSRVEECIEWVRVRMEKLTTMEFLEDLETLEHVFEQHK 461
Cdd:cd00176     86 QRWEELRELA----------------EERRQRLEEALDlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHK 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789991031  462 FDNRDIQDFRQNVDECIARQAEV----SAEDTYEYCELLRVLESEYQQLRDLSAGRMLDLDS 519
Cdd:cd00176    150 ELEEELEAHEPRLKSLNELAEELleegHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
875-976 6.67e-04

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 41.54  E-value: 6.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  875 QYDQKMAELLKKLEEAWRELNDavgKPISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQL-PNPTPTQRVNHDR 953
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSS---EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLiDEGHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 1789991031  954 LNGLwDDLWD-LSRMYVERIKVLE 976
Cdd:pfam00435   82 LEEL-NERWEqLLELAAERKQKLE 104
SH3_ITK cd11908
Src Homology 3 domain of Interleukin-2-inducible T-cell Kinase; ITK (also known as Tsk or Emt) ...
709-753 7.63e-04

Src Homology 3 domain of Interleukin-2-inducible T-cell Kinase; ITK (also known as Tsk or Emt) is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. ITK is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, ITK plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, ITK is crucial for the development of T-helper(Th)2 effector responses. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212841 [Multi-domain]  Cd Length: 56  Bit Score: 40.00  E-value: 7.63e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1789991031  709 VTALCDYSDEN---VTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPS 753
Cdd:cd11908      3 VIALYDYQTNDpqeLALRYNEEYHLLDSSEIHWWRVQDKNGHEGYVPS 50
PLEC smart00250
Plectin repeat;
2463-2497 9.74e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 9.74e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1789991031  2463 NYVDRSSVSVRDPSSGQQYSYQEAVDRRIVDADRG 2497
Cdd:smart00250    4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
61-138 2.35e-03

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: 40.51  E-value: 2.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   61 DDLFVDLRDGYALIALL---------EALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKLVNIRPEDIVEGNGKLTL 131
Cdd:cd21294     36 FQLFDECKDGLVLSKLIndsvpdtidERVLNKPPRKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLIL 115

                   ....*..
gi 1789991031  132 GLIWTII 138
Cdd:cd21294    116 GLIWQII 122
PLEC smart00250
Plectin repeat;
2780-2817 3.50e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 3.50e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1789991031  2780 LKPVYQAIASEGVFDPTKGHHVPVTTALNDGLINASTG 2817
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2723-2763 4.02e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 4.02e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1789991031  2723 QGLVDVTLSEvlpKGIIHPGTGERIDIKRGIELRIIDAATG 2763
Cdd:smart00250    1 QRLLEAQSAI---GGIIDPETGQKLSVEEALRRGLIDPETG 38
SH3_Tec_like cd11768
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ...
708-753 4.87e-03

Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212702 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 4.87e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1789991031  708 KVTALCDY---SDENVTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPS 753
Cdd:cd11768      1 IVVALYDFqpiEPGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
42-107 6.32e-03

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: 38.79  E-value: 6.32e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   42 KKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKE----NGYTRFHRIQNVQYCLDFL 107
Cdd:cd21221      3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPevaqSEEGQKQKLAVVLACVNFL 72
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
424-517 7.28e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 38.84  E-value: 7.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031  424 FSRVEECIEWVRVRMEKLTTMEFLEDLETLEHVFEQHKFDNRDIQDFRQNVDECIARQAEVSAEDTYEYCEL---LRVLE 500
Cdd:pfam00435    7 FRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIqerLEELN 86
                           90
                   ....*....|....*..
gi 1789991031  501 SEYQQLRDLSAGRMLDL 517
Cdd:pfam00435   87 ERWEQLLELAAERKQKL 103
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
42-134 8.23e-03

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


Pssm-ID: 409145  Cd Length: 109  Bit Score: 38.65  E-value: 8.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789991031   42 KKTFTKWVNKHLSKTDHK--IDDLFVDLRDGYALIALLEALTGER-----IQKENGYTRFHRIqnvqycLDFLKKKNIKL 114
Cdd:cd21296     12 EKVLLKWMNFHLKKAGYKktVTNFSSDVKDAEAYAYLLNVLAPEHcdpatLEAKDPLERAKLV------LEQAEKMNCKR 85
                           90       100
                   ....*....|....*....|
gi 1789991031  115 VnIRPEDIVEGNGKLTLGLI 134
Cdd:cd21296     86 Y-LTAKDIVEGSANLNLAFV 104
PLEC smart00250
Plectin repeat;
2201-2237 9.84e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 36.31  E-value: 9.84e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1789991031  2201 TQSWEFDTQQGVFVDNLTGEKLSLERALATGKVAPED 2237
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
 
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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