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Conserved domains on  [gi|578837832|ref|XP_006724532|]
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dystrophin isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
3117-3278 2.06e-113

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). 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. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


:

Pssm-ID: 320004  Cd Length: 162  Bit Score: 357.03  E-value: 2.06e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3117 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3196
Cdd:cd16246     1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3197 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3276
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                  ..
gi 578837832 3277 MR 3278
Cdd:cd16246   161 MR 162
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
128-238 6.62e-69

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: 227.50  E-value: 6.62e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21233     1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832  208 EDVDTTYPDKKSILMYITSLFQVLPQQVSIE 238
Cdd:cd21233    81 EDVATAHPDKKSILMYVTSLFQVLPQQVSIE 111
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
3-113 1.26e-66

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: 220.95  E-value: 1.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3303-3351 6.21e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


:

Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.99  E-value: 6.21e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578837832 3303 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 3351
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
333-550 7.93e-27

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: 111.00  E-value: 7.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  333 LDRYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEV 412
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  413 QEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQ-NQKLKELNDWLTKTEERtrkMEEEPLGPDLEDLKRQVQQHKVLQED 491
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQfFRDADDLEQWLEEKEAA---LASEDLGKDLESVEELLKKHKELEEE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832  492 LEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDIL 550
Cdd:cd00176   155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2097-2312 1.87e-23

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: 101.37  E-value: 1.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2097 KWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAK-YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQE 2175
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2176 KLGSLNLRWQEVCKQLSDRKKRLEEQKNiLSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLR 2255
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 2256 QGILKQLNETGGPVLVSAPisPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQI 2312
Cdd:cd00176   159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2682-2925 1.19e-20

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: 93.28  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2682 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 2761
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2762 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 2841
Cdd:cd00176    72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2842 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 2921
Cdd:cd00176   150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                  ....
gi 578837832 2922 DETL 2925
Cdd:cd00176   210 EEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2464-2680 2.39e-20

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: 92.12  E-value: 2.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2464 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 2543
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2544 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 2623
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 2624 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 2680
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1041-1255 3.39e-16

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: 80.18  E-value: 3.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1041 KLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLE 1120
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1121 TELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQkDLSEMHEWMTQAEEEyLERDFEYKTPDELQKAVEEMKRAKEEAQ 1200
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA-LASEDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578837832 1201 QKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEE 1255
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
235kDa-fam super family cl31124
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
755-1930 8.86e-15

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


The actual alignment was detected with superfamily member TIGR01612:

Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 82.02  E-value: 8.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   755 VNAIEREKAEKFRKLQDASRSAQALVE-QMVNEGVNA-------DSIKQASEQLNSRWIEFCQLLSErLNWLeYQNNIIA 826
Cdd:TIGR01612  598 INKLKLELKEKIKNISDKNEYIKKAIDlKKIIENNNAyidelakISPYQVPEHLKNKDKIYSTIKSE-LSKI-YEDDIDA 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   827 FYNQLQ---------------QLEQMTTTAEN-WLKIQPTtpsEPTAIKSQLKICKDEVNRLSDLQPQIERL-------- 882
Cdd:TIGR01612  676 LYNELSsivkenaidntedkaKLDDLKSKIDKeYDKIQNM---ETATVELHLSNIENKKNELLDIIVEIKKHihgeinkd 752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   883 ---KIQSIALKEKGQGPMFLD-ADFVAFTNHFKQVFSDVQAR---EKELQTIFDTLPPMRYQETMSAIRTW-VQQSETKL 954
Cdd:TIGR01612  753 lnkILEDFKNKEKELSNKINDyAKEKDELNKYKSKISEIKNHyndQINIDNIKDEDAKQNYDKSKEYIKTIsIKEDEIFK 832
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   955 SIPQLSVTDYEIMeQRLGELQALQSSLQEQQSGLYylsTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQK 1034
Cdd:TIGR01612  833 IINEMKFMKDDFL-NKVDKFINFENNCKEKIDSEH---EQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEE 908
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1035 LEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEwpalgdsEILKKQLKQcrllvsDIQTIQPSlnsvneggqkikNEAEPE 1114
Cdd:TIGR01612  909 EYQNINTLKKVDEYIKICENTKESIEKFHNKQ-------NILKEILNK------NIDTIKES------------NLIEKS 963
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1115 FASRLETELKELNTQWDHMCQQVyarkeALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFeyktpDELQKAVEEMKR 1194
Cdd:TIGR01612  964 YKDKFDNTLIDKINELDKAFKDA-----SLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQF-----DEKEKATNDIEQ 1033
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1195 AKEEAQQKEAKVKL--------LTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNgkcktleevwacWHELLSY 1266
Cdd:TIGR01612 1034 KIEDANKNIPNIEIaihtsiynIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLK------------HYNFDDF 1101
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1267 LEKAN-KWLNEVEfklKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDggVMDELINEEletfnsrwre 1345
Cdd:TIGR01612 1102 GKEENiKYADEIN---KIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED--VADKAISND---------- 1166
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1346 lheeavrrqklleqsiqSAQETEKSlhlIQESLTFIDKQlaAYIADKVDaaQMPQEAQKIQSDLTSheisLEEMKKHNQ- 1424
Cdd:TIGR01612 1167 -----------------DPEEIEKK---IENIVTKIDKK--KNIYDEIK--KLLNEIAEIEKDKTS----LEEVKGINLs 1218
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1425 -GKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPanfeqrlqeskmiLDEVKMHLPALETKSVEQEVVQSQLNhcvNLYKS 1503
Cdd:TIGR01612 1219 yGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIED-------------LDEIKEKSPEIENEMGIEMDIKAEME---TFNIS 1282
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1504 LSEVKSevemviktgRQIVQKKQTENPKELDERvtALKL-HYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAat 1582
Cdd:TIGR01612 1283 HDDDKD---------HHIISKKHDENISDIREK--SLKIiEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIA-- 1349
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1583 dmeltkrsavegmpsNLDSEVAWGKaTQKEIEKQKVHLKSITEVGEALKTVLGKKETLVedKLSLLNSNWIAVTSRAEEW 1662
Cdd:TIGR01612 1350 ---------------NIYNILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--KKIKDDINLEECKSKIEST 1411
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1663 LNllleyQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKaelndirpKVDSTRDQAANLMANRGDHCR 1742
Cdd:TIGR01612 1412 LD-----DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFK--------NIEMADNKSQHILKIKKDNAT 1478
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1743 KLVEPQISELNHRFAAiSHRIKT-----GKASIPLKEL-EQFNSDIQKLLEPL-EAEIQQGVNLKEEDFNKDMNEDNEGT 1815
Cdd:TIGR01612 1479 NDHDFNINELKEHIDK-SKGCKDeadknAKAIEKNKELfEQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAH 1557
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1816 VKELLQRGDNLQQriTDERKREEIKIKQQLLQT-KHN-ALKDLRSQRR---KKALEISHqwyqYKRQADDLLKCLDDIEK 1890
Cdd:TIGR01612 1558 KKFILEAEKSEQK--IKEIKKEKFRIEDDAAKNdKSNkAAIDIQLSLEnfeNKFLKISD----IKKKINDCLKETESIEK 1631
                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|
gi 578837832  1891 KLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSE 1930
Cdd:TIGR01612 1632 KISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIED 1671
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2926-3032 1.35e-11

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 characteristic 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: 63.49  E-value: 1.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2926 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 3005
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837832  3006 LSTLEDLNTRWKLLQVAVEDRVRQLHE 3032
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
3051-3080 7.62e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


:

Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.30  E-value: 7.62e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 578837832 3051 GPWERAISPNKVPYYINHETQTTCWDHPKM 3080
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2313-2571 4.11e-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: 53.60  E-value: 4.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2313 KDLGQLEKKLEDLEEQLNHLLL--WLSPIRNQLEiynqpnqegpfDVKETEIAVQAKQPDVEEILSKGQHLYKEKP-ATQ 2389
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDYgdDLESVEALLK-----------KHEALEAELAAHEERVEALNELGEQLIEEGHpDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2390 PVKRKLEDLSSEWKAVNRLLQELRAKqpdlapglttigasptqtvtlvtqpvvtketaisklempsslMLEVPALADFNR 2469
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQR------------------------------------------LEEALDLQQFFR 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2470 AWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKtSNQEARTIITDRIERI 2549
Cdd:cd00176   114 DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE-GHPDADEEIEEKLEEL 191
                         250       260
                  ....*....|....*....|..
gi 578837832 2550 QNQWDEVQEHLQNRRQQLNEML 2571
Cdd:cd00176   192 NERWEELLELAEERQKKLEEAL 213
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1870-2094 2.13e-05

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: 48.60  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1870 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 1942
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1943 Q--LSKRWREIESKFAQFRRLnfaqihtvreetmmvmtedmpLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCaKDF 2020
Cdd:cd00176    81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578837832 2021 EDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRS 2094
Cdd:cd00176   139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
552-819 4.21e-03

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: 41.66  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  552 KWQRLTEEQCLFSAWLSEKEDAVNKIHTTgfKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSvtQK 631
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA--EE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  632 TEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLtqttvmetvttvttreqilvkhaqeelpppppqkkrqitvdse 711
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR------------------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  712 irkrldvDITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEgvNAD 791
Cdd:cd00176   114 -------DADDLEQWLEEKEAALASEDLG--KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD--ADE 182
                         250       260
                  ....*....|....*....|....*...
gi 578837832  792 SIKQASEQLNSRWIEFCQLLSERLNWLE 819
Cdd:cd00176   183 EIEEKLEELNERWEELLELAEERQKKLE 210
 
Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
3117-3278 2.06e-113

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). 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. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


Pssm-ID: 320004  Cd Length: 162  Bit Score: 357.03  E-value: 2.06e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3117 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3196
Cdd:cd16246     1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3197 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3276
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                  ..
gi 578837832 3277 MR 3278
Cdd:cd16246   161 MR 162
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
128-238 6.62e-69

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: 227.50  E-value: 6.62e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21233     1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832  208 EDVDTTYPDKKSILMYITSLFQVLPQQVSIE 238
Cdd:cd21233    81 EDVATAHPDKKSILMYVTSLFQVLPQQVSIE 111
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
3-113 1.26e-66

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: 220.95  E-value: 1.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
3081-3199 3.68e-57

EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilisation of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 430392  Cd Length: 123  Bit Score: 194.28  E-value: 3.68e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  3081 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHN 3158
Cdd:pfam09068    1 TELMQELQDFNNIRFSAYRTAMKLRALQKRLCLDLVDLWNLIEAFDEHGLNslENDLLLDVSELETLLSSIYFALNKRKP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 578837832  3159 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 3199
Cdd:pfam09068   81 TthQVNVPLSVDLLLNWLLNVYDPQRTGKIRVLSFKVALVLLC 123
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
2-224 3.48e-34

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 142.00  E-value: 3.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    2 EDEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNN 79
Cdd:COG5069     3 AKKWQKVQKKTFTKWTNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   80 NVDLVNIGSTDIVDGNHKLTLGLIWNIILhwqvKNVMKNIMAGLQQTNSEKILLsWVRQSTRNY-PQVNVINFTTSWSDG 158
Cdd:COG5069    83 GVKLFNIGPQDIVDGNPKLILGLIWSLIS----RLTIATINEEGELTKHINLLL-WCDEDTGGYkPEVDTFDFFRSWRDG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578837832  159 LALNALIHSHRPDLFDWNSVVCQQSATQ-RLEHAFNIARYQLGIEKLLDPEDV-DTTYPDKKSILMYI 224
Cdd:COG5069   158 LAFSALIHDSRPDTLDPNVLDLQKKNKAlNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3303-3351 6.21e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.99  E-value: 6.21e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578837832 3303 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 3351
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
333-550 7.93e-27

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: 111.00  E-value: 7.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  333 LDRYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEV 412
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  413 QEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQ-NQKLKELNDWLTKTEERtrkMEEEPLGPDLEDLKRQVQQHKVLQED 491
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQfFRDADDLEQWLEEKEAA---LASEDLGKDLESVEELLKKHKELEEE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832  492 LEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDIL 550
Cdd:cd00176   155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2097-2312 1.87e-23

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: 101.37  E-value: 1.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2097 KWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAK-YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQE 2175
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2176 KLGSLNLRWQEVCKQLSDRKKRLEEQKNiLSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLR 2255
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 2256 QGILKQLNETGGPVLVSAPisPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQI 2312
Cdd:cd00176   159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
11-109 3.09e-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: 90.84  E-value: 3.09e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832     11 KTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEK---GSTRVHALNNVNKALRVLQNNNVDLVNIG 87
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 578837832     88 STDIVDGNhKLTLGLIWNIILH 109
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
130-227 3.64e-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: 90.84  E-value: 3.64e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    130 KILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQ---QSATQRLEHAFNIARYQLGIEKLLD 206
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 578837832    207 PEDVDTTYPDKKSILMYITSL 227
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2682-2925 1.19e-20

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: 93.28  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2682 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 2761
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2762 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 2841
Cdd:cd00176    72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2842 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 2921
Cdd:cd00176   150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                  ....
gi 578837832 2922 DETL 2925
Cdd:cd00176   210 EEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
128-232 2.32e-20

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  Cd Length: 109  Bit Score: 88.88  E-value: 2.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   128 SEKILLSWVRQSTRNY-PQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQS-ATQRLEHAFNIARYQLGIEK-L 204
Cdd:pfam00307    3 LEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFdKLENINLALDVAEKKLGVPKvL 82
                           90       100
                   ....*....|....*....|....*...
gi 578837832   205 LDPEDVDTtyPDKKSILMYITSLFQVLP 232
Cdd:pfam00307   83 IEPEDLVE--GDNKSVLTYLASLFRRFQ 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2464-2680 2.39e-20

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: 92.12  E-value: 2.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2464 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 2543
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2544 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 2623
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 2624 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 2680
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
7-111 4.24e-20

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  Cd Length: 109  Bit Score: 88.11  E-value: 4.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832     7 DVQKKTFTKWVNAQFSK-FGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEK-GSTRVHALNNVNKALRVLQNN-NVDL 83
Cdd:pfam00307    1 LELEKELLRWINSHLAEyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*...
gi 578837832    84 VNIGSTDIVDGNHKLTLGLIWNIILHWQ 111
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
3299-3344 9.34e-17

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 76.37  E-value: 9.34e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 578837832  3299 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 3344
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1041-1255 3.39e-16

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: 80.18  E-value: 3.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1041 KLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLE 1120
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1121 TELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQkDLSEMHEWMTQAEEEyLERDFEYKTPDELQKAVEEMKRAKEEAQ 1200
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA-LASEDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578837832 1201 QKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEE 1255
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
755-1930 8.86e-15

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 82.02  E-value: 8.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   755 VNAIEREKAEKFRKLQDASRSAQALVE-QMVNEGVNA-------DSIKQASEQLNSRWIEFCQLLSErLNWLeYQNNIIA 826
Cdd:TIGR01612  598 INKLKLELKEKIKNISDKNEYIKKAIDlKKIIENNNAyidelakISPYQVPEHLKNKDKIYSTIKSE-LSKI-YEDDIDA 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   827 FYNQLQ---------------QLEQMTTTAEN-WLKIQPTtpsEPTAIKSQLKICKDEVNRLSDLQPQIERL-------- 882
Cdd:TIGR01612  676 LYNELSsivkenaidntedkaKLDDLKSKIDKeYDKIQNM---ETATVELHLSNIENKKNELLDIIVEIKKHihgeinkd 752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   883 ---KIQSIALKEKGQGPMFLD-ADFVAFTNHFKQVFSDVQAR---EKELQTIFDTLPPMRYQETMSAIRTW-VQQSETKL 954
Cdd:TIGR01612  753 lnkILEDFKNKEKELSNKINDyAKEKDELNKYKSKISEIKNHyndQINIDNIKDEDAKQNYDKSKEYIKTIsIKEDEIFK 832
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   955 SIPQLSVTDYEIMeQRLGELQALQSSLQEQQSGLYylsTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQK 1034
Cdd:TIGR01612  833 IINEMKFMKDDFL-NKVDKFINFENNCKEKIDSEH---EQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEE 908
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1035 LEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEwpalgdsEILKKQLKQcrllvsDIQTIQPSlnsvneggqkikNEAEPE 1114
Cdd:TIGR01612  909 EYQNINTLKKVDEYIKICENTKESIEKFHNKQ-------NILKEILNK------NIDTIKES------------NLIEKS 963
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1115 FASRLETELKELNTQWDHMCQQVyarkeALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFeyktpDELQKAVEEMKR 1194
Cdd:TIGR01612  964 YKDKFDNTLIDKINELDKAFKDA-----SLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQF-----DEKEKATNDIEQ 1033
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1195 AKEEAQQKEAKVKL--------LTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNgkcktleevwacWHELLSY 1266
Cdd:TIGR01612 1034 KIEDANKNIPNIEIaihtsiynIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLK------------HYNFDDF 1101
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1267 LEKAN-KWLNEVEfklKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDggVMDELINEEletfnsrwre 1345
Cdd:TIGR01612 1102 GKEENiKYADEIN---KIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED--VADKAISND---------- 1166
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1346 lheeavrrqklleqsiqSAQETEKSlhlIQESLTFIDKQlaAYIADKVDaaQMPQEAQKIQSDLTSheisLEEMKKHNQ- 1424
Cdd:TIGR01612 1167 -----------------DPEEIEKK---IENIVTKIDKK--KNIYDEIK--KLLNEIAEIEKDKTS----LEEVKGINLs 1218
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1425 -GKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPanfeqrlqeskmiLDEVKMHLPALETKSVEQEVVQSQLNhcvNLYKS 1503
Cdd:TIGR01612 1219 yGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIED-------------LDEIKEKSPEIENEMGIEMDIKAEME---TFNIS 1282
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1504 LSEVKSevemviktgRQIVQKKQTENPKELDERvtALKL-HYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAat 1582
Cdd:TIGR01612 1283 HDDDKD---------HHIISKKHDENISDIREK--SLKIiEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIA-- 1349
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1583 dmeltkrsavegmpsNLDSEVAWGKaTQKEIEKQKVHLKSITEVGEALKTVLGKKETLVedKLSLLNSNWIAVTSRAEEW 1662
Cdd:TIGR01612 1350 ---------------NIYNILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--KKIKDDINLEECKSKIEST 1411
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1663 LNllleyQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKaelndirpKVDSTRDQAANLMANRGDHCR 1742
Cdd:TIGR01612 1412 LD-----DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFK--------NIEMADNKSQHILKIKKDNAT 1478
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1743 KLVEPQISELNHRFAAiSHRIKT-----GKASIPLKEL-EQFNSDIQKLLEPL-EAEIQQGVNLKEEDFNKDMNEDNEGT 1815
Cdd:TIGR01612 1479 NDHDFNINELKEHIDK-SKGCKDeadknAKAIEKNKELfEQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAH 1557
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1816 VKELLQRGDNLQQriTDERKREEIKIKQQLLQT-KHN-ALKDLRSQRR---KKALEISHqwyqYKRQADDLLKCLDDIEK 1890
Cdd:TIGR01612 1558 KKFILEAEKSEQK--IKEIKKEKFRIEDDAAKNdKSNkAAIDIQLSLEnfeNKFLKISD----IKKKINDCLKETESIEK 1631
                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|
gi 578837832  1891 KLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSE 1930
Cdd:TIGR01612 1632 KISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIED 1671
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
3300-3343 2.26e-14

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 69.39  E-value: 2.26e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 578837832   3300 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 3343
Cdd:smart00291    2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2115-2810 3.98e-14

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 79.33  E-value: 3.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2115 AEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQtvvRTLNATGEEIiqQSSKTDASILQEKLGSLNLRWQEVCKQLSDR 2194
Cdd:TIGR02168  212 AERYKELKAELRELELALLVLRLEELREELEELQ---EELKEAEEEL--EELTAELQELEEKLEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2195 KKRLEEQKNILSEFQRDLNEFVLWLEEADNI-----ASIPLEPGKEQQLKEKLEQVKLLVEEL-PLRQGILKQLNEtggp 2268
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQleeleAQLEELESKLDELAEELAELEEKLEELkEELESLEAELEE---- 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2269 vlvsapiSPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 2348
Cdd:TIGR02168  363 -------LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2349 PNQEGPFDVKETEIA-VQAKQPDVEEILSKGQHLYKEKP-ATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLApGLTTI 2426
Cdd:TIGR02168  436 KELQAELEELEEELEeLQEELERLEEALEELREELEEAEqALDAAERELAQLQARLDSLERLQENLEGFSEGVK-ALLKN 514
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2427 GASPTQTVTLVTQPVVTK---ETAISKLEMPSSLMLEVPALADFNRA-----WTELTDWLSLLDQVIKSQRVMVGDLEDI 2498
Cdd:TIGR02168  515 QSGLSGILGVLSELISVDegyEAAIEAALGGRLQAVVVENLNAAKKAiaflkQNELGRVTFLPLDSIKGTEIQGNDREIL 594
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2499 NEmIIKQKATMQDLEQRRPQLEELI-------------TAAQNLKNKTsNQEARTIITD--------------------- 2544
Cdd:TIGR02168  595 KN-IEGFLGVAKDLVKFDPKLRKALsyllggvlvvddlDNALELAKKL-RPGYRIVTLDgdlvrpggvitggsaktnssi 672
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2545 -----RIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLA 2619
Cdd:TIGR02168  673 lerrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2620 KDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINA---SWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAW 2696
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2697 LTEAETTANVLQDatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDvyHNLDENSQKILRSLEGSDDAVLLQRRLDNMNF 2776
Cdd:TIGR02168  833 IAATERRLEDLEE--QIEELSEDIESLAAEIEELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELES 908
                          730       740       750
                   ....*....|....*....|....*....|....
gi 578837832  2777 KWSELRKKSLNIRSHLEASSDQWKRLHLSLQELL 2810
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
719-925 1.17e-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: 69.78  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  719 DITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 798
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE---GHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  799 QLNSRWIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSePTAIKSQLKICKDEVNRLSDLQPQ 878
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578837832  879 IERLKIQSIALKEKGQ--GPMFLDADFVAFTNHFKQVFSDVQAREKELQ 925
Cdd:cd00176   162 LKSLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1040-1144 4.82e-12

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 characteristic 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: 65.03  E-value: 4.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1040 NKLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEaEPEFASRL 1119
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 578837832  1120 ETELKELNTQWDHMCQQVYARKEAL 1144
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2926-3032 1.35e-11

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 characteristic 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: 63.49  E-value: 1.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2926 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 3005
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837832  3006 LSTLEDLNTRWKLLQVAVEDRVRQLHE 3032
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
441-548 1.96e-11

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 characteristic 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: 63.11  E-value: 1.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   441 LMDLQNQKLKELNDWLTKTEErtrKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVdESSGDHATAA 520
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEA---LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 578837832   521 LEEQLKVLGDRWANICRWTEDRWVLLQD 548
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2099-2199 3.98e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 62.35  E-value: 3.98e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2099 RRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKW-YLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQEKL 2177
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLkKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 578837832   2178 GSLNLRWQEVCKQLSDRKKRLE 2199
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1117-1920 5.60e-11

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 68.97  E-value: 5.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1117 SRLETELKELNTQWDHMcqqvyaRKEALKggLEKTVSLQKDLSEMHEWMTQAEEEYLERdfeyktpdELQKAVEEMKRAK 1196
Cdd:COG1196   189 ERLEDLLEELEKQLEKL------ERQAEK--AERYQELKAELRELELALLLAKLKELRK--------ELEELEEELSRLE 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1197 EEAQQKEAKVKLLTESVnsviaqappvaqEALKKELETLTTNYQWLCTRLNGKCKTLEEVWAcwhELLSYLEKANKWLNE 1276
Cdd:COG1196   253 EELEELQEELEEAEKEI------------EELKSELEELREELEELQEELLELKEEIEELEG---EISLLRERLEELENE 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1277 VEFKLKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDggvMDELINEELETFNSRWRELHEEAVRRQKL 1356
Cdd:COG1196   318 LEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEE---KLSALLEELEELFEALREELAELEAELAE 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1357 LEQSIQSAQETEKSLhliQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEmkKHNQGKEAAQRVLSQI 1436
Cdd:COG1196   395 IRNELEELKREIESL---EERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEE--QLEELRDRLKELEREL 469
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1437 DVAQKKLQDVSMKFRlfqkpaNFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVN------------LYKSL 1504
Cdd:COG1196   470 AELQEELQRLEKELS------SLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIKvkekyetaleaaLGNRL 543
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1505 SEVKSEVEMVIKTGRQIVQKKQTENPKEL-DERVTALKLHYNELGAKVTERKQQLEKCL-KLSRKMRkemNVLTEWLAAT 1582
Cdd:COG1196   544 QAVVVENEEVAKKAIEFLKENKAGRATFLpLDRIKPLRSLKSDAAPGFLGLASDLIDFDpKYEPAVR---FVLGDTLVVD 620
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1583 DMELTKRSA-----------VEG--------------MPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKK 1637
Cdd:COG1196   621 DLEQARRLArklrikyrivtLDGdlvepsgsitggsrNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSL 700
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1638 ETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMEtfdqNVDHITKWIIQADTLLDESEKKKPQQKEDvLKRLKAELN 1717
Cdd:COG1196   701 EDLLEELRRQLEELERQLEELKRELAALEEELEQLQS----RLEELEEELEELEEELEELQERLEELEEE-LESLEEALA 775
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1718 DIRPKVDSTRDQAANLMANRGDHcrklvEPQISELNHRFAAISHRIKTGKAsiPLKELEQFNSDIQKLLEPLEAEIQQGV 1797
Cdd:COG1196   776 KLKEEIEELEEKRQALQEELEEL-----EEELEEAERRLDALERELESLEQ--RRERLEQEIEELEEEIEELEEKLDELE 848
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1798 nlKEEDFNKDMNEDNEGTVKELLQRGDNLQQRItdERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEIShqwyqykRQ 1877
Cdd:COG1196   849 --EELEELEKELEELKEELEELEAEKEELEDEL--KELEEEKEELEEELRELESELAELKEEIEKLRERLE-------EL 917
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|...
gi 578837832 1878 ADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNA 1920
Cdd:COG1196   918 EAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEIEA 960
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2927-3037 1.29e-10

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: 64.00  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2927 RLRELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL 3006
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832 3007 STLEDLNTRWKLLQVAVEDRVRQLHEAHRDF 3037
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
SPEC smart00150
Spectrin repeats;
335-437 2.39e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.04  E-value: 2.39e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    335 RYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEVQE 414
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI---EEGHPDAEEIEE 77
                            90       100
                    ....*....|....*....|...
gi 578837832    415 QMNLLNSRWECLRVASMEKQSNL 437
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2096-2200 2.76e-10

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 characteristic 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: 60.02  E-value: 2.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2096 EKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEH--AKYKWYlKELQDGIGQRQTVVRTLNATGEEIIQqSSKTDASIL 2173
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESvqALLKKH-KALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837832  2174 QEKLGSLNLRWQEVCKQLSDRKKRLEE 2200
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2467-2568 2.82e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 2.82e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2467 FNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 2546
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 578837832   2547 ERIQNQWDEVQEHLQNRRQQLN 2568
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2562-2678 2.46e-09

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 characteristic 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: 57.33  E-value: 2.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2562 NRRQQLNEMLKDSTQWLEakeEAEQVLgqarakleSWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLr 2641
Cdd:pfam00435    1 LLLQQFFRDADDLESWIE---EKEALL--------SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI- 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 578837832  2642 DYSADDTRKVHMITENINASWRSIHKRVSEREAALEE 2678
Cdd:pfam00435   69 DEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
PTZ00121 PTZ00121
MAEBL; Provisional
1349-1956 5.13e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 5.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1349 EAVRRQKLLEQSIQSAQETEKsLHLIQESLTFIDKQLAAYI----ADKVDAAQMPQEAQKIQSDLTSHEI-SLEEMKKHN 1423
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEE-ERNNEEIRKFEEARMAHFArrqaAIKAEEARKADELKKAEEKKKADEAkKAEEKKKAD 1305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1424 QGKEAAQRVlSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKM-HLPALETKSVEQEVVQSQLNhcvnlyK 1502
Cdd:PTZ00121 1306 EAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAdEAEAAEEKAEAAEKKKEEAK------K 1378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1503 SLSEVKSEVEMVIKTGRqiVQKKQTENPKELDE--RVTALKLHYNELGAKvTERKQQLEKCLKLSRKMRKEMNVLTEWLA 1580
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADE--AKKKAEEDKKKADElkKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1581 ATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEvgEALKTVLGKKETLVEDKlsllnsnwiAVTSRAE 1660
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKK---------AEEAKKA 1524
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1661 EWLNLLLEYQKHMETfdQNVDHITKwiiqADTLLDESEKKKPQQKEDVLKRLKAElnDIRPKVDSTRDQAANLMANRGDH 1740
Cdd:PTZ00121 1525 DEAKKAEEAKKADEA--KKAEEKKK----ADELKKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEE 1596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1741 CRKLVEPQISELNHRF-AAISHRIKTGKasipLKELEQFNSDIQKLLEPLEAEIQQGVNL-KEEDFNKDMNEDNEGTVKE 1818
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAkKAEEAKIKAEE----LKKAEEEKKKVEQLKKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEE 1672
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1819 LLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEP 1898
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832 1899 RDER-KIKEIDRELQKKKEElnaVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFA 1956
Cdd:PTZ00121 1753 EEEKkKIAHLKKEEEKKAEE---IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
3051-3080 7.62e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.30  E-value: 7.62e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 578837832 3051 GPWERAISPNKVPYYINHETQTTCWDHPKM 3080
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC smart00150
Spectrin repeats;
2684-2793 1.37e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 55.03  E-value: 1.37e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2684 QQFPLDLEKFLAWLTEAETTAnvlqdatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGSDD 2763
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-------ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPD 71
                            90       100       110
                    ....*....|....*....|....*....|
gi 578837832   2764 AVLLQRRLDNMNFKWSELRKKSLNIRSHLE 2793
Cdd:smart00150   72 AEEIEERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1869-1971 2.65e-08

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 characteristic 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: 54.25  E-value: 2.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1869 HQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVE--PTQIQLSK 1946
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEghYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 578837832  1947 RWREIESKFAQFRRLNFAQIHTVRE 1971
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
3048-3080 2.86e-08

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 51.83  E-value: 2.86e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 578837832   3048 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 3080
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
SPEC smart00150
Spectrin repeats;
2929-3030 3.33e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 3.33e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2929 RELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLST 3008
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 578837832   3009 LEDLNTRWKLLQVAVEDRVRQL 3030
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
3052-3078 7.44e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 425661 [Multi-domain]  Cd Length: 30  Bit Score: 50.58  E-value: 7.44e-08
                           10        20
                   ....*....|....*....|....*..
gi 578837832  3052 PWERAISPNKVPYYINHETQTTCWDHP 3078
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2313-2571 4.11e-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: 53.60  E-value: 4.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2313 KDLGQLEKKLEDLEEQLNHLLL--WLSPIRNQLEiynqpnqegpfDVKETEIAVQAKQPDVEEILSKGQHLYKEKP-ATQ 2389
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDYgdDLESVEALLK-----------KHEALEAELAAHEERVEALNELGEQLIEEGHpDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2390 PVKRKLEDLSSEWKAVNRLLQELRAKqpdlapglttigasptqtvtlvtqpvvtketaisklempsslMLEVPALADFNR 2469
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQR------------------------------------------LEEALDLQQFFR 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2470 AWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKtSNQEARTIITDRIERI 2549
Cdd:cd00176   114 DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE-GHPDADEEIEEKLEEL 191
                         250       260
                  ....*....|....*....|..
gi 578837832 2550 QNQWDEVQEHLQNRRQQLNEML 2571
Cdd:cd00176   192 NERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
1052-1145 2.93e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.48  E-value: 2.93e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   1052 LKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLETELKELNTQWD 1131
Cdd:smart00150   10 LEAWLEEKEQLLASEDLG-KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLEELNERWE 87
                            90
                    ....*....|....
gi 578837832   1132 HMCQQVYARKEALK 1145
Cdd:smart00150   88 ELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
719-819 8.90e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.94  E-value: 8.90e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    719 DITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 798
Cdd:smart00150    6 DADELEAWLEEKEQLLASEDLG--KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE---GHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 578837832    799 QLNSRWIEFCQLLSERLNWLE 819
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2152-2620 1.39e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2152 RTLNATGEEIIQQSSKTD--ASILQEKLGSLnlrwQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASI- 2228
Cdd:PRK03918  296 IKLSEFYEEYLDELREIEkrLSRLEEEINGI----EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKk 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2229 -----------PLEPGKEQQLKEKLEQVKLLVEE----LPLRQGILKQ--------LNETGG-----PVlVSAPISPEEQ 2280
Cdd:PRK03918  372 eelerlkkrltGLTPEKLEKELEELEKAKEEIEEeiskITARIGELKKeikelkkaIEELKKakgkcPV-CGRELTEEHR 450
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2281 DKLENKLKqtnlqwikvsralpEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ----PNQEGPFD 2356
Cdd:PRK03918  451 KELLEEYT--------------AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkelEEKLKKYN 516
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2357 VKETEiavqAKQPDVEEILSKGQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVtl 2436
Cdd:PRK03918  517 LEELE----KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL-- 590
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2437 vtqpvvtkETAISKLEmpsslmlevpalaDFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKAtmqDLEQRR 2516
Cdd:PRK03918  591 --------EERLKELE-------------PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK---RLEELR 646
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2517 PQLEELITA--------AQNLKNKTSNQEARtiITDRIERIQNQWDEVQEHLQNRRQQLNEMLKdstqwleAKEEAEqVL 2588
Cdd:PRK03918  647 KELEELEKKyseeeyeeLREEYLELSRELAG--LRAELEELEKRREEIKKTLEKLKEELEEREK-------AKKELE-KL 716
                         490       500       510
                  ....*....|....*....|....*....|..
gi 578837832 2589 GQARAKLEswkegpytvdAIQKKITETKQLAK 2620
Cdd:PRK03918  717 EKALERVE----------ELREKVKKYKALLK 738
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1870-2094 2.13e-05

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: 48.60  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1870 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 1942
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1943 Q--LSKRWREIESKFAQFRRLnfaqihtvreetmmvmtedmpLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCaKDF 2020
Cdd:cd00176    81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578837832 2021 EDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRS 2094
Cdd:cd00176   139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2681-2783 4.88e-05

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 characteristic 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: 45.00  E-value: 4.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2681 RLLQQFPLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILrsLEG 2760
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS-------SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI--DEG 71
                           90       100
                   ....*....|....*....|...
gi 578837832  2761 SDDAVLLQRRLDNMNFKWSELRK 2783
Cdd:pfam00435   72 HYASEEIQERLEELNERWEQLLE 94
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2478-2617 8.92e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.20  E-value: 8.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2478 LSLLDQVIKSQRVMVG-DLEDINEMIikqkatmQDLEQRRPQLEELITAAQNLKNKTsnqeartiitdriERIQNQWDEV 2556
Cdd:PRK00409  497 LGLPENIIEEAKKLIGeDKEKLNELI-------ASLEELERELEQKAEEAEALLKEA-------------EKLKEELEEK 556
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578837832 2557 QEHLQNRRQQLNEMLKDSTQWL--EAKEEAEQVLGQARaklESWKEGPYTVDAiqKKITETKQ 2617
Cdd:PRK00409  557 KEKLQEEEDKLLEEAEKEAQQAikEAKKEADEIIKELR---QLQKGGYASVKA--HELIEARK 614
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1109-1379 3.65e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1109 NEAEPEFaSRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDfeyktpDELQKA 1188
Cdd:TIGR02168  701 AELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE------ERLEEA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1189 VEEMKRAKEEAQQKEAKVKLLTESVNSVIAQappvaQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLE 1268
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREA-----LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1269 KANKWLNEVEFKLKTTENipgGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDG-----GVMDEL------------ 1331
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEE---LIEELESELEALLNERASLEEALALLRSELEELSEElreleSKRSELrreleelrekla 925
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1332 ------------INEELETFNSRWRELHEEAVRRQKLLEQSIQSAQEtekSLHLIQESLT 1379
Cdd:TIGR02168  926 qlelrleglevrIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR---RLKRLENKIK 982
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
552-819 4.21e-03

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: 41.66  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  552 KWQRLTEEQCLFSAWLSEKEDAVNKIHTTgfKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSvtQK 631
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA--EE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  632 TEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLtqttvmetvttvttreqilvkhaqeelpppppqkkrqitvdse 711
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR------------------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  712 irkrldvDITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEgvNAD 791
Cdd:cd00176   114 -------DADDLEQWLEEKEAALASEDLG--KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD--ADE 182
                         250       260
                  ....*....|....*....|....*...
gi 578837832  792 SIKQASEQLNSRWIEFCQLLSERLNWLE 819
Cdd:cd00176   183 EIEEKLEELNERWEELLELAEERQKKLE 210
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2654-3025 9.76e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 9.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2654 ITENINASWRSIHKRVSEREAALEETHRLlQQFPLDLEKFLAWLTEAETTANVLQDATRkerllEDSKGVKELMKQWQDL 2733
Cdd:TIGR02169  655 MTGGSRAPRGGILFSRSEPAELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQELS-----DASRKIGEIEKEIEQL 728
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2734 QGEIEAHTDVYHNLDENSQKILRSLEGSDDAVL-LQRRLDNMNFKWSELRKKSLNIRSHLEASsdQWKRLHLSLQELlvw 2812
Cdd:TIGR02169  729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKeLEARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELSKL--- 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2813 lqlkDDELSRQAPIGGDfpAVQKQNDVHraFKRELKTKEpviMSTLETVRIFLTEQPLEgleklyqeprelppeeraqnv 2892
Cdd:TIGR02169  804 ----EEEVSRIEARLRE--IEQKLNRLT--LEKEYLEKE---IQELQEQRIDLKEQIKS--------------------- 851
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2893 trlLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVIKG--SWQpvgdllIDSLQDHLEKV 2970
Cdd:TIGR02169  852 ---IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEelEAQ------IEKKRKRLSEL 922
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 578837832  2971 KALRGEiapLKENVSHVNDLARQlttlgIQLSPYNLSTLEDLNTRWKLLQVAVED 3025
Cdd:TIGR02169  923 KAKLEA---LEEELSEIEDPKGE-----DEEIPEEELSLEDVQAELQRVEEEIRA 969
 
Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
3117-3278 2.06e-113

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). 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. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


Pssm-ID: 320004  Cd Length: 162  Bit Score: 357.03  E-value: 2.06e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3117 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3196
Cdd:cd16246     1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3197 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3276
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                  ..
gi 578837832 3277 MR 3278
Cdd:cd16246   161 MR 162
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
3117-3278 1.06e-103

EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. 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. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils.


Pssm-ID: 320000  Cd Length: 163  Bit Score: 329.20  E-value: 1.06e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3117 SLSAACDALDQHNLK-QNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGI 3195
Cdd:cd16242     1 SLSTAIEAFDQHGLRaQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3196 ISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLD 3275
Cdd:cd16242    81 VLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSVRSCFEKAGEKPEISAAHFLD 160

                  ...
gi 578837832 3276 WMR 3278
Cdd:cd16242   161 WLK 163
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
3118-3278 5.64e-84

EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. 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.


Pssm-ID: 320005  Cd Length: 162  Bit Score: 272.93  E-value: 5.64e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3118 LSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIIS 3197
Cdd:cd16247     2 LNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLMS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3198 LCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWM 3277
Cdd:cd16247    82 LSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDWM 161

                  .
gi 578837832 3278 R 3278
Cdd:cd16247   162 R 162
EFh_DRP-2 cd16248
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ...
3117-3277 4.46e-80

EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin homologue mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. Like dystrophin, DRP-2 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 only two spectrin repeats (SRs) and a WW domain.


Pssm-ID: 320006  Cd Length: 162  Bit Score: 261.65  E-value: 4.46e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3117 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3196
Cdd:cd16248     1 TLSSATEIFTEHELQMSERVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3197 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3276
Cdd:cd16248    81 CLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVEPSVRSCFRFAPGKPVIELSQFLEW 160

                  .
gi 578837832 3277 M 3277
Cdd:cd16248   161 M 161
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
128-238 6.62e-69

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: 227.50  E-value: 6.62e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21233     1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832  208 EDVDTTYPDKKSILMYITSLFQVLPQQVSIE 238
Cdd:cd21233    81 EDVATAHPDKKSILMYVTSLFQVLPQQVSIE 111
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
3118-3277 8.89e-68

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family 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. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 226.38  E-value: 8.89e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3118 LSAACDALDQHNLKQ-NDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3196
Cdd:cd15901     2 LSTVLSVFDRHGLSGsQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIALI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3197 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3276
Cdd:cd15901    82 TLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLSW 161

                  .
gi 578837832 3277 M 3277
Cdd:cd15901   162 L 162
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
3-113 1.26e-66

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: 220.95  E-value: 1.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
7-113 1.75e-64

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: 214.55  E-value: 1.75e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    7 DVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNI 86
Cdd:cd21186     1 DVQKKTFTKWINSQLSKANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNI 80
                          90       100
                  ....*....|....*....|....*..
gi 578837832   87 GSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21186    81 SSNDIVDGNPKLTLGLVWSIILHWQVK 107
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
128-232 2.08e-59

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: 199.96  E-value: 2.08e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21187     1 LEKTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLV-KDSPESRLEHAFTVAHEHLGIEKLLDP 79
                          90       100
                  ....*....|....*....|....*
gi 578837832  208 EDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21187    80 EDVNVEQPDKKSILMYVTSLFQVLP 104
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
3081-3199 3.68e-57

EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilisation of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 430392  Cd Length: 123  Bit Score: 194.28  E-value: 3.68e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  3081 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHN 3158
Cdd:pfam09068    1 TELMQELQDFNNIRFSAYRTAMKLRALQKRLCLDLVDLWNLIEAFDEHGLNslENDLLLDVSELETLLSSIYFALNKRKP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 578837832  3159 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 3199
Cdd:pfam09068   81 TthQVNVPLSVDLLLNWLLNVYDPQRTGKIRVLSFKVALVLLC 123
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
7-113 1.15e-55

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: 189.45  E-value: 1.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    7 DVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNI 86
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 80
                          90       100
                  ....*....|....*....|....*..
gi 578837832   87 GSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21232    81 GGTDIVDGNHKLTLGLLWSIILHWQVK 107
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
128-232 1.32e-51

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: 177.84  E-value: 1.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21234     1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVV-KMSPVERLEHAFSKAKNHLGIEKLLDP 79
                          90       100
                  ....*....|....*....|....*
gi 578837832  208 EDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21234    80 EDVAVQLPDKKSIIMYLTSLFEVLP 104
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
3203-3294 6.94e-50

EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilisation of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 430393  Cd Length: 90  Bit Score: 172.48  E-value: 6.94e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  3203 LEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGsnIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQ 3282
Cdd:pfam09069    1 LVDKYRYLFSQISDSNGLLDQRKLGLLLHELLQLPRQVGEVAAFGG--IEPSVRSCFEQVGGKPKIELNHFLDWLMSEPQ 78
                           90
                   ....*....|..
gi 578837832  3283 SMVWLPVLHRVA 3294
Cdd:pfam09069   79 SLVWLPVLHRLA 90
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
127-232 9.36e-43

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: 152.55  E-value: 9.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  127 NSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLD 206
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVR-NQSNRENLENAFNVAEKEFGVTRLLD 79
                          90       100
                  ....*....|....*....|....*.
gi 578837832  207 PEDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21189    80 PEDVDVPEPDEKSIITYVSSLYDVFP 105
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
3-108 9.01e-42

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: 150.21  E-value: 9.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKFGkQHIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNNNV 81
Cdd:cd21246    11 DEREAVQKKTFTKWVNSHLARVG-CRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRV 89
                          90       100
                  ....*....|....*....|....*..
gi 578837832   82 DLVNIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21246    90 HLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
8-111 1.11e-41

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: 149.47  E-value: 1.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    8 VQKKTFTKWVNAQFSKFGKqHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIG 87
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARR-RVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNIR 81
                          90       100
                  ....*....|....*....|....
gi 578837832   88 STDIVDGNHKLTLGLIWNIILHWQ 111
Cdd:cd21188    82 AEDIVDGNPKLTLGLIWTIILHFQ 105
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
132-228 9.64e-38

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: 138.31  E-value: 9.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDVD 211
Cdd:cd21194     7 LLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLD-PNDHLGNLNNAFDVAEQELGIAKLLDAEDVD 85
                          90
                  ....*....|....*..
gi 578837832  212 TTYPDKKSILMYITSLF 228
Cdd:cd21194    86 VARPDEKSIMTYVASYY 102
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
1-108 1.12e-37

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: 138.58  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    1 MEDEREDVQKKTFTKWVNAQFSKFGkQHIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNN 79
Cdd:cd21193     9 LQEERINIQKKTFTKWINSFLEKAN-LEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFLKTK 87
                          90       100
                  ....*....|....*....|....*....
gi 578837832   80 nVDLVNIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21193    88 -VRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
132-228 1.52e-37

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: 137.53  E-value: 1.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDVD 211
Cdd:cd21248     7 LLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLS-KSNALYNLQNAFNVAEQKLGLTKLLDPEDVN 85
                          90
                  ....*....|....*..
gi 578837832  212 TTYPDKKSILMYITSLF 228
Cdd:cd21248    86 VEQPDEKSIITYVVTYY 102
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
1-108 5.58e-36

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: 134.41  E-value: 5.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    1 MEDEREDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNN 79
Cdd:cd21317    24 LADEREAVQKKTFTKWVNSHLARVTCR-IGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQ 102
                          90       100
                  ....*....|....*....|....*....
gi 578837832   80 NVDLVNIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21317   103 KVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
1-108 6.32e-36

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: 134.38  E-value: 6.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    1 MEDEREDVQKKTFTKWVNAQFSKFGkQHIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNN 79
Cdd:cd21318    31 LADEREAVQKKTFTKWVNSHLARVP-CRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQ 109
                          90       100
                  ....*....|....*....|....*....
gi 578837832   80 NVDLVNIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21318   110 RVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
124-229 6.99e-36

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: 133.21  E-value: 6.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  124 QQTNSEK-ILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIE 202
Cdd:cd21319     1 RETRSAKdALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLK-KSNARHNLEHAFNVAERQLGIT 79
                          90       100
                  ....*....|....*....|....*..
gi 578837832  203 KLLDPEDVDTTYPDKKSILMYITSLFQ 229
Cdd:cd21319    80 KLLDPEDVFTENPDEKSIITYVVAFYH 106
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
4-113 2.16e-35

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: 131.73  E-value: 2.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    4 EREDVQKKTFTKWVNAQFSKFGK-QHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGST--RVHALNNVNKALRVLQNNN 80
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPpMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837832   81 VDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21241    81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
3-115 2.53e-35

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: 132.42  E-value: 2.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKFgKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21236    12 DERDKVQKKTFTKWINQHLMKV-RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVK 90
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNV 115
Cdd:cd21236    91 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
4-113 1.08e-34

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: 129.95  E-value: 1.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    4 EREDVQKKTFTKWVNAQFSKFGKQH-IENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21242     1 EQEQTQKRTFTNWINSQLAKHSPPSvVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21242    81 LINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
2-224 3.48e-34

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 142.00  E-value: 3.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    2 EDEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNN 79
Cdd:COG5069     3 AKKWQKVQKKTFTKWTNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   80 NVDLVNIGSTDIVDGNHKLTLGLIWNIILhwqvKNVMKNIMAGLQQTNSEKILLsWVRQSTRNY-PQVNVINFTTSWSDG 158
Cdd:COG5069    83 GVKLFNIGPQDIVDGNPKLILGLIWSLIS----RLTIATINEEGELTKHINLLL-WCDEDTGGYkPEVDTFDFFRSWRDG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578837832  159 LALNALIHSHRPDLFDWNSVVCQQSATQ-RLEHAFNIARYQLGIEKLLDPEDV-DTTYPDKKSILMYI 224
Cdd:COG5069   158 LAFSALIHDSRPDTLDPNVLDLQKKNKAlNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
3-118 9.89e-34

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: 127.45  E-value: 9.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKfGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21235     1 DERDRVQKKTFTKWVNKHLIK-AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKN 118
Cdd:cd21235    80 LVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 115
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
4-113 1.10e-32

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: 124.22  E-value: 1.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    4 EREDVQKKTFTKWVNAQFSKFGKQH-IENLFSDLQDGRRLLDLLEGLTGQKLPKEKG--STRVHALNNVNKALRVLQNNN 80
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSQPIvINDLFVDIKDGTALLRLLEVLSGQKLPIESGrvLQRAHKLSNIRNALDFLTKRC 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837832   81 VDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21190    81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
6-108 3.08e-32

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: 122.50  E-value: 3.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    6 EDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNNNVDLV 84
Cdd:cd21214     3 EKQQRKTFTAWCNSHLRKAGTQ-IENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLV 81
                          90       100
                  ....*....|....*....|....
gi 578837832   85 NIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21214    82 SIGAEEIVDGNLKMTLGMIWTIIL 105
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
3-115 4.14e-31

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: 119.75  E-value: 4.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKFgKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21237     1 DERDRVQKKTFTKWVNKHLMKV-RKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVK 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNV 115
Cdd:cd21237    80 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 112
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
126-232 4.32e-31

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: 119.32  E-value: 4.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  126 TNSEKILLsWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQrLEHAFNIARyQLGIEKLL 205
Cdd:cd21239     1 SAKERLLL-WSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLAN-LEHAFYVAE-KLGVTRLL 77
                          90       100
                  ....*....|....*....|....*..
gi 578837832  206 DPEDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21239    78 DPEDVDVSSPDEKSVITYVSSLYDVFP 104
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
6-108 2.13e-30

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


Pssm-ID: 409064  Cd Length: 107  Bit Score: 117.50  E-value: 2.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    6 EDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNNNVDL 83
Cdd:cd21215     2 VDVQKKTFTKWLNTKLSSRGLS-ITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKL 80
                          90       100
                  ....*....|....*....|....*
gi 578837832   84 VNIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21215    81 TNIGAEDIVDGNLKLILGLLWTLIL 105
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
125-228 2.34e-30

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: 117.27  E-value: 2.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  125 QTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKL 204
Cdd:cd21249     2 LRSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLR-PDRPLYNLANAFLVAEQELGISQL 80
                          90       100
                  ....*....|....*....|....
gi 578837832  205 LDPEDVDTTYPDKKSILMYItSLF 228
Cdd:cd21249    81 LDPEDVAVPHPDERSIMTYV-SLY 103
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
124-229 3.28e-30

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: 117.47  E-value: 3.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  124 QQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEK 203
Cdd:cd21321     2 EKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLK-KSNAHYNLQNAFNVAEKELGLTK 80
                          90       100
                  ....*....|....*....|....*.
gi 578837832  204 LLDPEDVDTTYPDKKSILMYITSLFQ 229
Cdd:cd21321    81 LLDPEDVNVDQPDEKSIITYVATYYH 106
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
124-229 3.43e-30

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: 117.85  E-value: 3.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  124 QQTNSEK-ILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIE 202
Cdd:cd21322    13 RETRSAKdALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLT-KSNATYNLQQAFNTAEQHLGLT 91
                          90       100
                  ....*....|....*....|....*..
gi 578837832  203 KLLDPEDVDTTYPDKKSILMYITSLFQ 229
Cdd:cd21322    92 KLLDPEDVNMEAPDEKSIITYVVSFYH 118
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3303-3351 6.21e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.99  E-value: 6.21e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578837832 3303 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 3351
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
125-232 7.13e-30

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: 115.88  E-value: 7.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  125 QTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKL 204
Cdd:cd21243     3 KGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLK-RRSNRENLETAFTVAEKELGIPRL 81
                          90       100
                  ....*....|....*....|....*...
gi 578837832  205 LDPEDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21243    82 LDPEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
4-113 1.66e-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: 114.98  E-value: 1.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    4 EREDVQKKTFTKWVNAQFSKFGKQ-HIENLFSDLQDGRRLLDLLEGLTGQKLPKE--KGSTRVHALNNVNKALRVLQNNN 80
Cdd:cd21191     1 ERENVQKRTFTRWINLHLEKCNPPlEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837832   81 VDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21191    81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 113
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
1-108 1.75e-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: 116.68  E-value: 1.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    1 MEDEREDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNN 79
Cdd:cd21316    46 LADEREAVQKKTFTKWVNSHLARVSCR-ITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQ 124
                          90       100
                  ....*....|....*....|....*....
gi 578837832   80 NVDLVNIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21316   125 RVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
7-112 2.67e-28

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: 111.23  E-value: 2.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    7 DVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNNNVDLV 84
Cdd:cd21227     3 EIQKNTFTNWVNEQLKPTGMS-VEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLV 81
                          90       100
                  ....*....|....*....|....*...
gi 578837832   85 NIGSTDIVDGNHKLTLGLIWNIILHWQV 112
Cdd:cd21227    82 NIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
126-232 8.01e-28

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: 110.11  E-value: 8.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  126 TNSEKILLsWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLL 205
Cdd:cd21238     2 TAKEKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLL 79
                          90       100
                  ....*....|....*....|....*..
gi 578837832  206 DPEDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21238    80 DPEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
124-230 2.34e-27

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: 108.99  E-value: 2.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  124 QQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEK 203
Cdd:cd21216     7 EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLR-KDDPRENLNLAFDVAEKHLDIPK 85
                          90       100
                  ....*....|....*....|....*...
gi 578837832  204 LLDPED-VDTTYPDKKSILMYITSLFQV 230
Cdd:cd21216    86 MLDAEDiVNTPRPDERSVMTYVSCYYHA 113
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
127-229 3.40e-27

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: 108.26  E-value: 3.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  127 NSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLD 206
Cdd:cd21320     2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLK-KSNAHYNLQNAFNLAEQHLGLTKLLD 80
                          90       100
                  ....*....|....*....|...
gi 578837832  207 PEDVDTTYPDKKSILMYITSLFQ 229
Cdd:cd21320    81 PEDISVDHPDEKSIITYVVTYYH 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
333-550 7.93e-27

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: 111.00  E-value: 7.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  333 LDRYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEV 412
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  413 QEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQ-NQKLKELNDWLTKTEERtrkMEEEPLGPDLEDLKRQVQQHKVLQED 491
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQfFRDADDLEQWLEEKEAA---LASEDLGKDLESVEELLKKHKELEEE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832  492 LEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDIL 550
Cdd:cd00176   155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
129-232 1.10e-25

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: 103.97  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  129 EKILLsWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARyQLGIEKLLDPE 208
Cdd:cd21240     7 EKLLL-WTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQ-IQSNRENLEQAFEVAE-RLGVTRLLDAE 83
                          90       100
                  ....*....|....*....|....
gi 578837832  209 DVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21240    84 DVDVPSPDEKSVITYVSSIYDAFP 107
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
125-232 1.59e-25

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: 103.27  E-value: 1.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  125 QTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKL 204
Cdd:cd21192     1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVK-NRSPRDNLELAFRIAEQHLNIPRL 79
                          90       100
                  ....*....|....*....|....*...
gi 578837832  205 LDPEDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21192    80 LEVEDVLVDKPDERSIMTYVSQFLRMFP 107
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
8-112 1.81e-25

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: 104.07  E-value: 1.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    8 VQKKTFTKWVNAQFSKFGKqHIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNN-NVDLV 84
Cdd:cd21311    15 IQQNTFTRWANEHLKTANK-HIADLETDLSDGLRLIALVEVLSGKKFPKfnKRPTFRSQKLENVSVALKFLEEDeGIKIV 93
                          90       100
                  ....*....|....*....|....*...
gi 578837832   85 NIGSTDIVDGNHKLTLGLIWNIILHWQV 112
Cdd:cd21311    94 NIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
128-228 2.23e-25

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: 102.93  E-value: 2.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDwNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21226     1 SEDGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFK-QAAIEQMDAEARLNLAFDFAEKKLGIPKLLEA 79
                          90       100
                  ....*....|....*....|.
gi 578837832  208 EDVDTTYPDKKSILMYiTSLF 228
Cdd:cd21226    80 EDVMTGNPDERSIVLY-TSLF 99
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
130-231 1.23e-24

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: 100.88  E-value: 1.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  130 KILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVvcqqSATQRLEH---AFNIARYQLGIEKLLD 206
Cdd:cd21253     4 KALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSL----SKENVYENnklAFTVAEKELGIPALLD 79
                          90       100
                  ....*....|....*....|....*.
gi 578837832  207 PED-VDTTYPDKKSILMYITSLFQVL 231
Cdd:cd21253    80 AEDmVALKVPDKLSILTYVSQYYNYF 105
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
132-228 4.43e-24

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: 99.52  E-value: 4.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDV- 210
Cdd:cd21291    15 LLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLD-KKDHRGNMQLAFDIASKEIGIPQLLDVEDVc 93
                          90
                  ....*....|....*...
gi 578837832  211 DTTYPDKKSILMYITSLF 228
Cdd:cd21291    94 DVAKPDERSIMTYVAYYF 111
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
1-112 1.04e-23

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: 99.06  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    1 MEDEREDVQKKTFTKWVNAQFSKFGKQ-HIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQN 78
Cdd:cd21247    13 LQEQRMTMQKKTFTKWMNNVFSKNGAKiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKT 92