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Conserved domains on  [gi|1890275301|ref|NP_004005|]
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dystrophin isoform Dp116 [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 ...
 396-557 1.27e-117

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: 356.26  E-value: 1.27e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 396 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 475
Cdd:cd16246     1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 476 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 555
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160


                  ..
gi 1890275301 556 MR 557
Cdd:cd16246   161 MR 162
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 582-630 3.36e-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: 113.22  E-value: 3.36e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1890275301 582 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 630
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 10-204 1.43e-18

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: 85.19  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  10 KDLQGEIEAHTDVYHNLDENSQKILRslEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELL 89
Cdd:cd00176    43 EALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  90 VWLQLKDDELSRQaPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraq 169
Cdd:cd00176   120 QWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------- 183

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1890275301 170 nvtrlLRKQAEEVNTEWEKLNLHSADWQRKIDETL 204
Cdd:cd00176   184 -----IEEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 205-311 6.29e-15

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


:

Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 71.58  E-value: 6.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 205 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 284
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78

                          90       100
                  ....*....|....*....|....*..
gi 1890275301 285 LSTLEDLNTRWKLLQVAVEDRVRQLHE 311
Cdd:pfam00435  79 QERLEELNERWEQLLELAAERKQKLEE 105
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 330-359 1.90e-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: 53.69  E-value: 1.90e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 1890275301 330 GPWERAISPNKVPYYINHETQTTCWDHPKM 359
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
GumC super family cl34566
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
766-870 2.69e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG3206:

Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 766 LISLESEERGELERI------LADLEEENRNLQAEYDRLKQQhehkglspLPSPPEMMPTSPQSPRDAELIAEAKLLRQH 839
Cdd:COG3206   207 LVDLSEEAKLLLQQLselesqLAEARAELAEAEARLAALRAQ--------LGSGPDALPELLQSPVIQQLRAQLAELEAE 278

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1890275301 840 KGRLEARMQilEDHN--KQLESQLHRLRQLLEQ 870
Cdd:COG3206   279 LAELSARYT--PNHPdvIALRAQIAALRAQLQQ 309
 
Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
 396-557 1.27e-117

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: 356.26  E-value: 1.27e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 396 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 475
Cdd:cd16246     1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 476 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 555
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160


                  ..
gi 1890275301 556 MR 557
Cdd:cd16246   161 MR 162
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 360-478 8.56e-58

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: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462668  Cd Length: 123  Bit Score: 193.91  E-value: 8.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 360 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHN 437
Cdd:pfam09068   1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1890275301 438 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 478
Cdd:pfam09068  81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 582-630 3.36e-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: 113.22  E-value: 3.36e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1890275301 582 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 630
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 10-204 1.43e-18

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: 85.19  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  10 KDLQGEIEAHTDVYHNLDENSQKILRslEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELL 89
Cdd:cd00176    43 EALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  90 VWLQLKDDELSRQaPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraq 169
Cdd:cd00176   120 QWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------- 183

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1890275301 170 nvtrlLRKQAEEVNTEWEKLNLHSADWQRKIDETL 204
Cdd:cd00176   184 -----IEEKLEELNERWEELLELAEERQKKLEEAL 213
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 578-623 3.16e-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: 75.98  E-value: 3.16e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1890275301 578 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 623
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 579-622 6.12e-15

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: 6.12e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1890275301  579 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 622
Cdd:smart00291   2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 205-311 6.29e-15

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 71.58  E-value: 6.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 205 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 284
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78

                          90       100
                  ....*....|....*....|....*..
gi 1890275301 285 LSTLEDLNTRWKLLQVAVEDRVRQLHE 311
Cdd:pfam00435  79 QERLEELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 206-316 5.92e-14

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: 71.71  E-value: 5.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 206 RLRELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL 285
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1890275301 286 STLEDLNTRWKLLQVAVEDRVRQLHEAHRDF 316
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
SPEC smart00150
Spectrin repeats;
208-309 4.91e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.42  E-value: 4.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  208 RELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLST 287
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78

                           90       100
                   ....*....|....*....|..
gi 1890275301  288 LEDLNTRWKLLQVAVEDRVRQL 309
Cdd:smart00150  79 LEELNERWEELKELAEERRQKL 100
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 330-359 1.90e-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: 53.69  E-value: 1.90e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 1890275301 330 GPWERAISPNKVPYYINHETQTTCWDHPKM 359
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 327-359 6.34e-09

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: 52.22  E-value: 6.34e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1890275301  327 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 359
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 331-357 2.47e-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: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 50.20  E-value: 2.47e-08
                          10        20
                  ....*....|....*....|....*..
gi 1890275301 331 PWERAISPNKVPYYINHETQTTCWDHP 357
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
SPEC smart00150
Spectrin repeats;
80-201 6.43e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 6.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301   80 RLHLSLQELLVWLQLKDDELSrQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEklyqep 159
Cdd:smart00150   2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE------ 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1890275301  160 relppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKID 201
Cdd:smart00150  75 ---------------IEERLEELNERWEELKELAEERRQKLE 101
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
149-312 5.39e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 149 LEGLEKLYQEPRELPPEERAQNVTRLlrKQAEEVNTEWEKLnlhsadwQRKIDETLERLRELQEATDELDLKLRQAEVIK 228
Cdd:COG4717    55 ADELFKPQGRKPELNLKELKELEEEL--KEAEEKEEEYAEL-------QEELEELEEELEELEAELEELREELEKLEKLL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 229 GSWQPVGDL--LIDSLQDHLEKVKALRGEIAPLKENV-------SHVNDLARQLTTLGIQLSPYNLSTLEDLNTRWKLLQ 299
Cdd:COG4717   126 QLLPLYQELeaLEAELAELPERLEELEERLEELRELEeeleeleAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205

                         170
                  ....*....|...
gi 1890275301 300 VAVEDRVRQLHEA 312
Cdd:COG4717   206 QRLAELEEELEEA 218
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
766-870 2.69e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 766 LISLESEERGELERI------LADLEEENRNLQAEYDRLKQQhehkglspLPSPPEMMPTSPQSPRDAELIAEAKLLRQH 839
Cdd:COG3206   207 LVDLSEEAKLLLQQLselesqLAEARAELAEAEARLAALRAQ--------LGSGPDALPELLQSPVIQQLRAQLAELEAE 278

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1890275301 840 KGRLEARMQilEDHN--KQLESQLHRLRQLLEQ 870
Cdd:COG3206   279 LAELSARYT--PNHPdvIALRAQIAALRAQLQQ 309
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-318 5.69e-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: 40.82  E-value: 5.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301   33 ILRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAV 112
Cdd:TIGR02169  666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  113 QKQNDVHR-AFKRELKTKEPVI--------------------------------MSTLETV--RIFLTEQPLEG-LEKLY 156
Cdd:TIGR02169  746 LSSLEQEIeNVKSELKELEARIeeleedlhkleealndlearlshsripeiqaeLSKLEEEvsRIEARLREIEQkLNRLT 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  157 QEpRELPPEERAQNVTRL---------LRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVI 227
Cdd:TIGR02169  826 LE-KEYLEKEIQELQEQRidlkeqiksIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  228 KG--SWQpvgdllIDSLQDHLEKVKALRGEiapLKENVSHVNDLARQlttlgIQLSPYNLSTLEDlntrwkllqvaVEDR 305
Cdd:TIGR02169  905 IEelEAQ------IEKKRKRLSELKAKLEA---LEEELSEIEDPKGE-----DEEIPEEELSLED-----------VQAE 959

                          330
                   ....*....|...
gi 1890275301  306 VRQLHEAHRDFGP 318
Cdd:TIGR02169  960 LQRVEEEIRALEP 972
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 10-225 9.61e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  10 KDLQGEIEAHTDVYHNLDENSQKILRSLEGSDDAV-LLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQEL 88
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  89 LVWLQLkddeLSRQAPI-----GGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVrifltEQPLEGLEKLYQEPRELp 163
Cdd:COG4942   110 LRALYR----LGRQPPLalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL-----AALRAELEAERAELEAL- 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890275301 164 pEERAQNVTRLLRKQAEEVNTEWEKLnlhsadwQRKIDETLERLRELQEATDELDLKLRQAE 225
Cdd:COG4942   180 -LAELEEERAALEALKAERQKLLARL-------EKELAELAAELAELQQEAEELEALIARLE 233
 
Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
 396-557 1.27e-117

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: 356.26  E-value: 1.27e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 396 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 475
Cdd:cd16246     1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 476 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 555
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160


                  ..
gi 1890275301 556 MR 557
Cdd:cd16246   161 MR 162
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
 396-557 1.74e-106

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: 326.89  E-value: 1.74e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 396 SLSAACDALDQHNLK-QNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGI 474
Cdd:cd16242     1 SLSTAIEAFDQHGLRaQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 475 ISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLD 554
Cdd:cd16242    81 VLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSVRSCFEKAGEKPEISAAHFLD 160


                  ...
gi 1890275301 555 WMR 557
Cdd:cd16242   161 WLK 163
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
 397-557 2.31e-87

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: 276.39  E-value: 2.31e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 397 LSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIIS 476
Cdd:cd16247     2 LNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLMS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 477 LCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWM 556
Cdd:cd16247    82 LSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDWM 161


                  .
gi 1890275301 557 R 557
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 ...
 396-556 3.54e-82

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: 262.42  E-value: 3.54e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 396 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 475
Cdd:cd16248     1 TLSSATEIFTEHELQMSERVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 476 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 555
Cdd:cd16248    81 CLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVEPSVRSCFRFAPGKPVIELSQFLEW 160


                  .
gi 1890275301 556 M 556
Cdd:cd16248   161 M 161
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 397-556 1.37e-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: 225.61  E-value: 1.37e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 397 LSAACDALDQHNLKQ-NDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 475
Cdd:cd15901     2 LSTVLSVFDRHGLSGsQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIALI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 476 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 555
Cdd:cd15901    82 TLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLSW 161


                  .
gi 1890275301 556 M 556
Cdd:cd15901   162 L 162
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 360-478 8.56e-58

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: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462668  Cd Length: 123  Bit Score: 193.91  E-value: 8.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 360 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHN 437
Cdd:pfam09068   1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1890275301 438 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 478
Cdd:pfam09068  81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 482-573 4.52e-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: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462669  Cd Length: 90  Bit Score: 170.95  E-value: 4.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 482 LEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGsnIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQ 561
Cdd:pfam09069   1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGG--IEPSVRSCFEQVGGKPKITLNHFLDWLMSEPQ 78

                          90
                  ....*....|..
gi 1890275301 562 SMVWLPVLHRVA 573
Cdd:pfam09069  79 SLVWLPVLHRLA 90
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 582-630 3.36e-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: 113.22  E-value: 3.36e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1890275301 582 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 630
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
 396-556 6.07e-22

EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and similar proteins; DAH, the product of the dah (discontinuous actin hexagon) gene, is a Drosophila homolog to vertebrate dystrotelin. It is tightly membrane-associated and highly phosphorylated in a time-dependent fashion. DAH plays an essential role in the process of cellularization, and is associated with vesicles that convene at the cleavage furrow. The absence of DAH leads the severe disruption of the cleavage furrows around the nuclei and development stalls. DAH contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils.


Pssm-ID: 320003 [Multi-domain]  Cd Length: 164  Bit Score: 93.51  E-value: 6.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 396 SLSAACDALDQHNLKQND-----QPMDILQIINcltTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSF 470
Cdd:cd16245     1 PLKLIMGVFDRHQLSNSEnnlclPPDELEAVLH---DIYFAAEKLGNFNIDVDLATELLANLFLNVFDPERKKSISVLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 471 KTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAA 550
Cdd:cd16245    78 KVFLTLLCGSSLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPGLVGLTEY 157


                  ....*.
gi 1890275301 551 LFLDWM 556
Cdd:cd16245   158 QFIGWW 163
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 415-556 2.71e-19

EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the dystrophin-glycoprotein complex (DGC). They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. The family includes two paralogs dystrobrevins, alpha- and beta-dystrobrevin, both of which are cytoplasmic components of the dystrophin-associated protein complex that function as scaffold proteins in signal transduction and intracellular transport. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. The dystrobrevins 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, dystrobrevins contain one or two syntrophin binding sites (SBSs).


Pssm-ID: 320002 [Multi-domain]  Cd Length: 161  Bit Score: 85.75  E-value: 2.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 415 PMDILQIINCLTTIY----DRLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLF 490
Cdd:cd16244    22 ELSVSRLETLLSSIYyqlnKRLPTTHQ--IDVDQSISLLLNWLLAAYDPEATGRLTVFSVKVALSTLCAGKLVDKLRYIF 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890275301 491 KQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSniEPSVRSCFQfANNKPEIEAalFLDWM 556
Cdd:cd16244   100 SQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYN--ESAARSCFP-GQSKVTVND--FLDVM 160
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 10-204 1.43e-18

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: 85.19  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  10 KDLQGEIEAHTDVYHNLDENSQKILRslEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELL 89
Cdd:cd00176    43 EALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  90 VWLQLKDDELSRQaPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraq 169
Cdd:cd00176   120 QWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------- 183

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1890275301 170 nvtrlLRKQAEEVNTEWEKLNLHSADWQRKIDETL 204
Cdd:cd00176   184 -----IEEKLEELNERWEELLELAEERQKKLEEAL 213
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 578-623 3.16e-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: 75.98  E-value: 3.16e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1890275301 578 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 623
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 77-313 1.44e-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: 79.41  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  77 QWKRLHLSLQELLVWLQLKDDELSRQAPiGGDFPAVQKQNDVHRAFKRELKTKEPVImstletvriflteqplEGLEKLY 156
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERV----------------EALNELG 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 157 QEPRELPPEERAQnvtrlLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEAtDELDLKLRQAEVIKGSWQPVGD 236
Cdd:cd00176    64 EQLIEEGHPDAEE-----IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGKD 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890275301 237 LliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL-STLEDLNTRWKLLQVAVEDRVRQLHEAH 313
Cdd:cd00176   138 L--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIeEKLEELNERWEELLELAEERQKKLEEAL 213
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 579-622 6.12e-15

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: 6.12e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1890275301  579 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 622
Cdd:smart00291   2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 205-311 6.29e-15

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 71.58  E-value: 6.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 205 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 284
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78

                          90       100
                  ....*....|....*....|....*..
gi 1890275301 285 LSTLEDLNTRWKLLQVAVEDRVRQLHE 311
Cdd:pfam00435  79 QERLEELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 206-316 5.92e-14

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: 71.71  E-value: 5.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 206 RLRELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL 285
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1890275301 286 STLEDLNTRWKLLQVAVEDRVRQLHEAHRDF 316
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
EFh_DYTN cd16243
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ...
 425-557 1.68e-12

EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains 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. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 320001  Cd Length: 163  Bit Score: 66.26  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 425 LTTIYDRLEQEHNNLVNVPLCvDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFkQVA-----SSTGF 499
Cdd:cd16243    31 LERLFQSASQEVPGQVSAEAT-EQTCRLLFRLYDREQTGFVSLRSVEAALIALSGDTLSAKYRALF-QLYesgqgGSSGS 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1890275301 500 CDQRRLGLLLHDSIQIPRQLGEVASFGgsNIEPSVRSCFQFANNkPEIEAALFLDWMR 557
Cdd:cd16243   109 ITRSGLRVLLQDLSQIPAVVQESHVFG--NVETAVRSCFSGVLT-ASISEEHFLSWLQ 163
SPEC smart00150
Spectrin repeats;
208-309 4.91e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.42  E-value: 4.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  208 RELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLST 287
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78

                           90       100
                   ....*....|....*....|..
gi 1890275301  288 LEDLNTRWKLLQVAVEDRVRQL 309
Cdd:smart00150  79 LEELNERWEELKELAEERRQKL 100
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
 431-556 1.05e-10

EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin 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, beta-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320008  Cd Length: 161  Bit Score: 61.19  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 431 RLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLH 510
Cdd:cd16250    42 RLPSTHQ--ISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLR 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1890275301 511 DSIQIPRQLGEVASFGGSniEPSVRSCFQfanNKPEIEAALFLDWM 556
Cdd:cd16250   120 EVLKLPTAVFEGPSFGYT--EHSVRTCFP---QQKKIMLNMFLDTM 160
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
 425-538 1.11e-10

EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin alpha (DTN-A), or dystrophin-related protein 3 (DRP-3), is the mammalian ortholog of the Torpedo 87 kDa postsynaptic protein that tightly associates with dystrophin. It is a cytoplasmic protein expressed predominantly in skeletal muscle, heart, lung, and brain. Alpha-dystrobrevin has been implicated in the regulation of acetylcholine receptor (AChR) aggregate density and patterning. It is also essential in the pathogenesis of dystrophin-dependent muscular dystrophies. It plays a critical role in the full functionality of dystrophin through increasing dystrophin's binding to the dystrophin-glycoprotein complex (DGC), and provides protection during cardiac stress. Alpha-dystrobrevin binds to the intermediate filament proteins syncoilin and beta-synemin, thereby linking the dystrophin-associated protein complex (DAPC) to the intermediate filament network. Moreover, alpha-dystrobrevin involves in cell signaling via interaction with other proteins such as syntrophin, a modular adaptor protein that coordinates the assembly of the signaling proteins nitric oxide synthase, stress-activated protein kinase-3, and Grb2 to the DAPC. Furthermore, alpha-dystrobrevin plays an important role in muscle function, as well as in nuclear morphology maintenance through specific interaction with the nuclear lamina component lamin B1. In addition, alpha-dystrobrevin is required in dystrophin-associated protein scaffolding in brain. Absence of glial alpha-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. Alpha-dystrobrevin 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, alpha-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320007  Cd Length: 161  Bit Score: 61.07  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 425 LTTIY----DRLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFC 500
Cdd:cd16249    32 LSTIFyqlnKRMPTTHQ--INVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSNGVM 109

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1890275301 501 DQRRLGLLLHDSIQIPRQLGEVASFGGSniEPSVRSCF 538
Cdd:cd16249   110 VYGRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCF 145
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 330-359 1.90e-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: 53.69  E-value: 1.90e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 1890275301 330 GPWERAISPNKVPYYINHETQTTCWDHPKM 359
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 327-359 6.34e-09

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: 52.22  E-value: 6.34e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1890275301  327 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 359
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 331-357 2.47e-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: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 50.20  E-value: 2.47e-08
                          10        20
                  ....*....|....*....|....*..
gi 1890275301 331 PWERAISPNKVPYYINHETQTTCWDHP 357
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 584-630 1.00e-07

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 48.97  E-value: 1.00e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1890275301 584 CNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRvaKGHKMHYPMVEY 630
Cdd:cd02249     3 CDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 584-627 2.61e-06

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 45.03  E-value: 2.61e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1890275301 584 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPM 627
Cdd:cd02338     3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
SPEC smart00150
Spectrin repeats;
80-201 6.43e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 6.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301   80 RLHLSLQELLVWLQLKDDELSrQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEklyqep 159
Cdd:smart00150   2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE------ 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1890275301  160 relppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKID 201
Cdd:smart00150  75 ---------------IEERLEELNERWEELKELAEERRQKLE 101
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 584-630 1.04e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 40.52  E-value: 1.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1890275301 584 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRvakgHKMHYPMVEY 630
Cdd:cd02339     3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDK----HDLEHRFYRY 45
SPEC smart00150
Spectrin repeats;
10-72 1.48e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.93  E-value: 1.48e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890275301   10 KDLQGEIEAHTDVYHNLDENSQKILRslEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLE 72
Cdd:smart00150  41 EAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERLEELNERWEELKELAEERRQKLE 101
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 584-629 2.44e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 39.50  E-value: 2.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1890275301 584 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVE 629
Cdd:cd02345     3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
149-312 5.39e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 149 LEGLEKLYQEPRELPPEERAQNVTRLlrKQAEEVNTEWEKLnlhsadwQRKIDETLERLRELQEATDELDLKLRQAEVIK 228
Cdd:COG4717    55 ADELFKPQGRKPELNLKELKELEEEL--KEAEEKEEEYAEL-------QEELEELEEELEELEAELEELREELEKLEKLL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 229 GSWQPVGDL--LIDSLQDHLEKVKALRGEIAPLKENV-------SHVNDLARQLTTLGIQLSPYNLSTLEDLNTRWKLLQ 299
Cdd:COG4717   126 QLLPLYQELeaLEAELAELPERLEELEERLEELRELEeeleeleAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205

                         170
                  ....*....|...
gi 1890275301 300 VAVEDRVRQLHEA 312
Cdd:COG4717   206 QRLAELEEELEEA 218
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 586-628 7.32e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 38.01  E-value: 7.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1890275301 586 ICKEC--PIIGFRYRSLKHFNYDICQSCffsgrVAKG-HKMHyPMV 628
Cdd:cd02340     2 ICDGCqgPIVGVRYKCLVCPDYDLCESC-----EAKGvHPEH-AML 41
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
166-315 1.37e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  166 ERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDlkLRQAEVIKGswqpvgdlLIDSLQDH 245
Cdd:COG4913    284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG--GDRLEQLER--------EIERLERE 353

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  246 LEKVKALRGEiaplkenvshvndLARQLTTLGIQLsPYNLSTLEDLNTRWKLLQVAVEDRVRQLHEAHRD 315
Cdd:COG4913    354 LEERERRRAR-------------LEALLAALGLPL-PASAEEFAALRAEAAALLEALEEELEALEEALAE 409
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
766-870 2.69e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301 766 LISLESEERGELERI------LADLEEENRNLQAEYDRLKQQhehkglspLPSPPEMMPTSPQSPRDAELIAEAKLLRQH 839
Cdd:COG3206   207 LVDLSEEAKLLLQQLselesqLAEARAELAEAEARLAALRAQ--------LGSGPDALPELLQSPVIQQLRAQLAELEAE 278

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1890275301 840 KGRLEARMQilEDHN--KQLESQLHRLRQLLEQ 870
Cdd:COG3206   279 LAELSARYT--PNHPdvIALRAQIAALRAQLQQ 309
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
 584-616 4.43e-03

Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of the RSC complex, which is closely related to the SWI/SNF complex and is involved in remodeling chromatin structure. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239076  Cd Length: 45  Bit Score: 35.76  E-value: 4.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1890275301 584 CNIC-KECpiIGFRYRSLKHFNYDICQSCFFSGR 616
Cdd:cd02336     3 CFTCgNDC--TRVRYHNLKAKKYDLCPSCYQEGR 34
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-318 5.69e-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: 40.82  E-value: 5.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301   33 ILRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAV 112
Cdd:TIGR02169  666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  113 QKQNDVHR-AFKRELKTKEPVI--------------------------------MSTLETV--RIFLTEQPLEG-LEKLY 156
Cdd:TIGR02169  746 LSSLEQEIeNVKSELKELEARIeeleedlhkleealndlearlshsripeiqaeLSKLEEEvsRIEARLREIEQkLNRLT 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  157 QEpRELPPEERAQNVTRL---------LRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVI 227
Cdd:TIGR02169  826 LE-KEYLEKEIQELQEQRidlkeqiksIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  228 KG--SWQpvgdllIDSLQDHLEKVKALRGEiapLKENVSHVNDLARQlttlgIQLSPYNLSTLEDlntrwkllqvaVEDR 305
Cdd:TIGR02169  905 IEelEAQ------IEKKRKRLSELKAKLEA---LEEELSEIEDPKGE-----DEEIPEEELSLED-----------VQAE 959

                          330
                   ....*....|...
gi 1890275301  306 VRQLHEAHRDFGP 318
Cdd:TIGR02169  960 LQRVEEEIRALEP 972
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 26-330 5.83e-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: 40.44  E-value: 5.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301   26 LDENSQKILRSLEGsddavlLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQellvwLQLKDDELSRQAPI 105
Cdd:TIGR02169  235 LERQKEAIERQLAS------LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVKEKIGELEAEI 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  106 GGDFPAVQ-KQNDVHRAFKRELKTKEPV--IMSTLETVRIFLTEQPLEgLEKLYQEPRELppeeraQNVTRLLRKQAEEV 182
Cdd:TIGR02169  304 ASLERSIAeKERELEDAEERLAKLEAEIdkLLAEIEELEREIEEERKR-RDKLTEEYAEL------KEELEDLRAELEEV 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  183 NTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEV--------IKGSWQPVGDlLIDSLQDHLEKVKALRG 254
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEeladlnaaIAGIEAKINE-LEEEKEDKALEIKKQEW 455

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1890275301  255 EIAPLKENVSHVNDLARQLTtlgiqlspynlSTLEDLNTRWKLLQ---VAVEDRVRQLHEAHRDFGPASQhFLSTSVQG 330
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLK-----------EEYDRVEKELSKLQrelAEAEAQARASEERVRGGRAVEE-VLKASIQG 522
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 10-225 9.61e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  10 KDLQGEIEAHTDVYHNLDENSQKILRSLEGSDDAV-LLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQEL 88
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890275301  89 LVWLQLkddeLSRQAPI-----GGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVrifltEQPLEGLEKLYQEPRELp 163
Cdd:COG4942   110 LRALYR----LGRQPPLalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL-----AALRAELEAERAELEAL- 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890275301 164 pEERAQNVTRLLRKQAEEVNTEWEKLnlhsadwQRKIDETLERLRELQEATDELDLKLRQAE 225
Cdd:COG4942   180 -LAELEEERAALEALKAERQKLLARL-------EKELAELAAELAELQQEAEELEALIARLE 233
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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