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Conserved domains on  [gi|578812961|ref|XP_006715623|]
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utrophin isoform X10 [Homo sapiens]

Protein Classification

EFh_UTRO and ZZ_dystrophin domain-containing protein( domain architecture ID 11523295)

protein containing domains SPEC, WW, EFh_UTRO, and ZZ_dystrophin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
 406-567 4.50e-114

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: 346.88  E-value: 4.50e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 406 ELSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 485
Cdd:cd16247    1 DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 486 SLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 565
Cdd:cd16247   81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDW 160


                 ..
gi 578812961 566 MH 567
Cdd:cd16247  161 MR 162
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 592-640 9.24e-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: 111.68  E-value: 9.24e-30
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 578812961 592 AKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEY 640
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 7-214 1.10e-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: 91.35  E-value: 1.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961   7 NLRELLTKFEkDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWN 86
Cdd:cd00176   34 SVEALLKKHE-ALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQ 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  87 RLLMsLEELIKWLNMKDEELkKQMPIGGDVPALQLQYDHCKALRRELKEKEYSVLNAVDQARVFLADQPIEAPEEPRRNL 166
Cdd:cd00176  111 FFRD-ADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKL 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 578812961 167 QskteltpeeraqkiakamrkqssEVKEKWESLNAVTSNWQKQVDKAL 214
Cdd:cd00176  189 E-----------------------ELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 216-332 7.53e-13

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: 68.63  E-value: 7.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 216 KLRDLQGAMDDLDADMKEAESVRNGWKPVGDLliDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKMS 295
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 578812961 296 RQLDDLNMRWKLLQVSVDDRLKQLQEAHRDFGPSSQH 332
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA 115
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 341-369 5.23e-07

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: 46.75  E-value: 5.23e-07
                         10        20
                 ....*....|....*....|....*....
gi 578812961 341 PWQRSISHNKVPYYINHQTQTTCWDHPKM 369
Cdd:cd00201    3 GWEERWDPDGRVYYYNHNTKETQWEDPRE 31
 
Name Accession Description Interval E-value
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
 406-567 4.50e-114

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: 346.88  E-value: 4.50e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 406 ELSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 485
Cdd:cd16247    1 DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 486 SLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 565
Cdd:cd16247   81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDW 160


                 ..
gi 578812961 566 MH 567
Cdd:cd16247  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. ...
 370-488 9.37e-54

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: 182.74  E-value: 9.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  370 TELFQSLADLNNVRFSAYRTAIKIRRLQKALCLDLLELSTTNEIFKQHKLN--QNDQLLSVPDVINCLTTTYDGLEQMHK 447
Cdd:pfam09068   1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 578812961  448 D--LVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLS 488
Cdd:pfam09068  81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 592-640 9.24e-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: 111.68  E-value: 9.24e-30
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 578812961 592 AKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEY 640
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 7-214 1.10e-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: 91.35  E-value: 1.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961   7 NLRELLTKFEkDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWN 86
Cdd:cd00176   34 SVEALLKKHE-ALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQ 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  87 RLLMsLEELIKWLNMKDEELkKQMPIGGDVPALQLQYDHCKALRRELKEKEYSVLNAVDQARVFLADQPIEAPEEPRRNL 166
Cdd:cd00176  111 FFRD-ADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKL 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 578812961 167 QskteltpeeraqkiakamrkqssEVKEKWESLNAVTSNWQKQVDKAL 214
Cdd:cd00176  189 E-----------------------ELNERWEELLELAEERQKKLEEAL 213
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 588-632 3.19e-15

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: 70.20  E-value: 3.19e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578812961  588 AKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSgRTAKGHK 632
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQ 44
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 589-632 6.82e-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: 6.82e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 578812961   589 KHQAKCNICKEcPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHK 632
Cdd:smart00291   2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 216-332 7.53e-13

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: 68.63  E-value: 7.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 216 KLRDLQGAMDDLDADMKEAESVRNGWKPVGDLliDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKMS 295
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 578812961 296 RQLDDLNMRWKLLQVSVDDRLKQLQEAHRDFGPSSQH 332
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA 115
SPEC smart00150
Spectrin repeats;
220-320 4.40e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 4.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961   220 LQGAMDDLDADMKEAESVRNGWKPVGDLliDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKMSRQLD 299
Cdd:smart00150   3 FLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                           90       100
                   ....*....|....*....|.
gi 578812961   300 DLNMRWKLLQVSVDDRLKQLQ 320
Cdd:smart00150  81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
7-79 3.50e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 49.25  E-value: 3.50e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578812961     7 NLRELLTKFeKDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLE 79
Cdd:smart00150  32 SVEALLKKH-EAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEIEERLEELNERWEELKELAEERRQKLE 101
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 341-369 5.23e-07

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: 46.75  E-value: 5.23e-07
                         10        20
                 ....*....|....*....|....*....
gi 578812961 341 PWQRSISHNKVPYYINHQTQTTCWDHPKM 369
Cdd:cd00201    3 GWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 337-369 3.99e-06

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: 44.13  E-value: 3.99e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 578812961   337 SVQLPWQRSISHNKVPYYINHQTQTTCWDHPKM 369
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 341-367 1.15e-05

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: 42.88  E-value: 1.15e-05
                          10        20
                  ....*....|....*....|....*..
gi 578812961  341 PWQRSISHNKVPYYINHQTQTTCWDHP 367
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 215-321 2.63e-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 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: 44.23  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  215 EKLRDLQGAMDDLDADMKEAEsVRNGWKPVGDLLiDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKM 294
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKE-ALLSSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78

                          90       100
                  ....*....|....*....|....*..
gi 578812961  295 SRQLDDLNMRWKLLQVSVDDRLKQLQE 321
Cdd:pfam00435  79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 7-80 2.76e-04

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 41.15  E-value: 2.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578812961    7 NLRELLTKFeKDIQAEIDAHNDIFKSIDGNRQKMVKALGNSEEAtmLQHRLDDMNQRWNDLKAKSASIRAHLEA 80
Cdd:pfam00435  35 SVQALLKKH-KALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQERLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-233 4.41e-04

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: 44.28  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961     1 MIGLNFNLRELLTKFEKdIQAEIDAHNDIFKSIDGNRQKMVKALGNseeatmLQHRLDDMNQRWNDLKAKSASIRAHLEA 80
Cdd:TIGR02168  854 IESLAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEE------LSEELRELESKRSELRRELEELREKLAQ 926

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961    81 SAEKWNRLLMSLEELIKWLN----MKDEELKKQMPigGDVPALQLQYDHCKALRRELKEkeysvLNAVDqarvfladqpI 156
Cdd:TIGR02168  927 LELRLEGLEVRIDNLQERLSeeysLTLEEAEALEN--KIEDDEEEARRRLKRLENKIKE-----LGPVN----------L 989

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578812961   157 EAPEEPRrnlqskteltpeeraqkiakamrkqssEVKEKWESLNavtsnwqKQVDKALEKLRDLQGAMDDLDADMKE 233
Cdd:TIGR02168  990 AAIEEYE---------------------------ELKERYDFLT-------AQKEDLTEAKETLEEAIEEIDREARE 1032
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 17-236 1.82e-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: 41.67  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  17 KDIQAEIDAHNDIFKSIDGNRQKmvkalgnseeatmLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLMSLEELI 96
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKA-------------LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  97 KWLNMKDEELKKQMPI---GGDVPALQL---QYDHCKALRRelkekeYSVLNAVDQARVFLADQPIEAPEEPRRNLQS-- 168
Cdd:COG4942   97 AELEAQKEELAELLRAlyrLGRQPPLALllsPEDFLDAVRR------LQYLKYLAPARREQAEELRADLAELAALRAEle 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578812961 169 --KTELTPEERAQKIAKA-MRKQSSEVKEKWESLNAVTSNWQKQVDKALEKLRDLQGAMDDLDADMKEAES 236
Cdd:COG4942  171 aeRAELEALLAELEEERAaLEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK01156 PRK01156
chromosome segregation protein; Provisional
 70-325 2.58e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.81  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  70 KSASIRAHLEASAEKWNRLLMSLEELIKWLNMKDEELKKQMPI--GGDVPALQLQYDHCKALRRELKEKEysvlnaVDQA 147
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYleSEEINKSINEYNKIESARADLEDIK------IKIN 539

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 148 RVFLADQPIEAPEEPRRNLQSkteltpEERAQKiakamrkqssevKEKWESLNAVTS-----NWQKQVDKALEKLRDLQG 222
Cdd:PRK01156 540 ELKDKHDKYEEIKNRYKSLKL------EDLDSK------------RTSWLNALAVISlidieTNRSRSNEIKKQLNDLES 601

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 223 AMDDLDADM---------------KEAESVRNGWKPVGDL--LIDSLQdhiEKIMAFREEIAPINFKVKTVNDLSSQLSp 285
Cdd:PRK01156 602 RLQEIEIGFpddksyidksireieNEANNLNNKYNEIQENkiLIEKLR---GKIDNYKKQIAEIDSIIPDLKEITSRIN- 677

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 578812961 286 lDLHPSLKMSR-QLDDLNM---RWKLLQVSVDDRLKQLQEAHRD 325
Cdd:PRK01156 678 -DIEDNLKKSRkALDDAKAnraRLESTIEILRTRINELSDRIND 720
 
Name Accession Description Interval E-value
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
 406-567 4.50e-114

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: 346.88  E-value: 4.50e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 406 ELSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 485
Cdd:cd16247    1 DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 486 SLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 565
Cdd:cd16247   81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDW 160


                 ..
gi 578812961 566 MH 567
Cdd:cd16247  161 MR 162
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
 406-567 3.62e-99

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: 307.63  E-value: 3.62e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 406 ELSTTNEIFKQHKLN-QNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 484
Cdd:cd16242    1 SLSTAIEAFDQHGLRaQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 485 MSLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFID 564
Cdd:cd16242   81 VLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSVRSCFEKAGEKPEISAAHFLD 160


                 ...
gi 578812961 565 WMH 567
Cdd:cd16242  161 WLK 163
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
 407-566 3.17e-84

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: 268.05  E-value: 3.17e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 407 LSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMS 486
Cdd:cd16246    2 LSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 487 LSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDWM 566
Cdd:cd16246   82 LCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWM 161
EFh_DRP-2 cd16248
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ...
 406-566 2.13e-73

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: 238.54  E-value: 2.13e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 406 ELSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 485
Cdd:cd16248    1 TLSSATEIFTEHELQMSERVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 486 SLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 565
Cdd:cd16248   81 CLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVEPSVRSCFRFAPGKPVIELSQFLEW 160


                 .
gi 578812961 566 M 566
Cdd:cd16248  161 M 161
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 406-566 1.37e-57

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: 195.18  E-value: 1.37e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 406 ELSTTNEIFKQHKLNQ-NDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 484
Cdd:cd15901    1 DLSTVLSVFDRHGLSGsQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 485 MSLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFID 564
Cdd:cd15901   81 ITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLS 160


                 ..
gi 578812961 565 WM 566
Cdd:cd15901  161 WL 162
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 370-488 9.37e-54

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: 182.74  E-value: 9.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  370 TELFQSLADLNNVRFSAYRTAIKIRRLQKALCLDLLELSTTNEIFKQHKLN--QNDQLLSVPDVINCLTTTYDGLEQMHK 447
Cdd:pfam09068   1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 578812961  448 D--LVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLS 488
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. ...
 492-583 2.67e-47

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: 163.24  E-value: 2.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  492 LEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGsnIEPSVRSCFQQNNNKPEISVKEFIDWMHLEPQ 571
Cdd:pfam09069   1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGG--IEPSVRSCFEQVGGKPKITLNHFLDWLMSEPQ 78

                          90
                  ....*....|..
gi 578812961  572 SMVWLPVLHRVA 583
Cdd:pfam09069  79 SLVWLPVLHRLA 90
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 592-640 9.24e-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: 111.68  E-value: 9.24e-30
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 578812961 592 AKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEY 640
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 7-214 1.10e-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: 91.35  E-value: 1.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961   7 NLRELLTKFEkDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWN 86
Cdd:cd00176   34 SVEALLKKHE-ALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQ 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  87 RLLMsLEELIKWLNMKDEELkKQMPIGGDVPALQLQYDHCKALRRELKEKEYSVLNAVDQARVFLADQPIEAPEEPRRNL 166
Cdd:cd00176  111 FFRD-ADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKL 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 578812961 167 QskteltpeeraqkiakamrkqssEVKEKWESLNAVTSNWQKQVDKAL 214
Cdd:cd00176  189 E-----------------------ELNERWEELLELAEERQKKLEEAL 213
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
 413-566 5.96e-20

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: 87.74  E-value: 5.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 413 IFKQHKLNQNDQLLSVP--DVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLSKG 490
Cdd:cd16245    8 VFDRHQLSNSENNLCLPpdELEAVLHDIYFAAEKLGNFNIDVDLATELLANLFLNVFDPERKKSISVLELKVFLTLLCGS 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578812961 491 LLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDWM 566
Cdd:cd16245   88 SLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPGLVGLTEYQFIGWW 163
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 412-566 1.74e-17

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: 80.74  E-value: 1.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 412 EIFKQHKLNQND--QLLSVPDVINCLTTTYDGLEQM--HKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSL 487
Cdd:cd16244    7 EAFRENGLNTLDptTELSVSRLETLLSSIYYQLNKRlpTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVKVALSTL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578812961 488 SKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQQNNnkpEISVKEFIDWM 566
Cdd:cd16244   87 CAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYN--ESAARSCFPGQS---KVTVNDFLDVM 160
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 588-632 3.19e-15

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: 70.20  E-value: 3.19e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578812961  588 AKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSgRTAKGHK 632
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQ 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 84-323 6.67e-15

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: 74.79  E-value: 6.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  84 KWNRLLMSLEELIKWLNMKDEELKkQMPIGGDVPALQLQYDHCKALRRELKEKEYSVLNAVDQARVFLADQPIEAPEepr 163
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 164 rnlqskteltpeeraqkiakaMRKQSSEVKEKWESLNAVTSNWQKQVDKALEKLRDLQgAMDDLDADMKEAESVRNGWKP 243
Cdd:cd00176   77 ---------------------IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDL 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 244 VGDLliDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQL-SPLDLHPSLKMSRQLDDLNMRWKLLQVSVDDRLKQLQEA 322
Cdd:cd00176  135 GKDL--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212


                 .
gi 578812961 323 H 323
Cdd:cd00176  213 L 213
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 589-632 6.82e-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: 6.82e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 578812961   589 KHQAKCNICKEcPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHK 632
Cdd:smart00291   2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 216-332 7.53e-13

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: 68.63  E-value: 7.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 216 KLRDLQGAMDDLDADMKEAESVRNGWKPVGDLliDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKMS 295
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 578812961 296 RQLDDLNMRWKLLQVSVDDRLKQLQEAHRDFGPSSQH 332
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA 115
EFh_DYTN cd16243
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ...
 420-566 2.78e-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: 65.87  E-value: 2.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 420 NQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCvDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLSKGLLEEKYRYL 499
Cdd:cd16243   16 IERTISLSVEEVSQALERLFQSASQEVPGQVSAEAT-EQTCRLLFRLYDREQTGFVSLRSVEAALIALSGDTLSAKYRAL 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578812961 500 FK----EVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGgsNIEPSVRSCFQQNNNkPEISVKEFIDWM 566
Cdd:cd16243   95 FQlyesGQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFG--NVETAVRSCFSGVLT-ASISEEHFLSWL 162
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
 412-564 7.31e-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: 58.76  E-value: 7.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 412 EIFKQHKLNQND--QLLSVPDVINCLTTTYdglEQMHKDL-----VNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 484
Cdd:cd16249    7 EALRENALNNLDpnTELNVARLEAVLSTIF---YQLNKRMptthqINVEQSISLLLNFLLAAFDPEGHGKISVFAVKMAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 485 MSLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQQnnnKPEISVKEFID 564
Cdd:cd16249   84 ATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCFSQ---QKKVTLNGFLD 158
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
 412-566 4.06e-08

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: 53.49  E-value: 4.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 412 EIFKQHKLNQNDQL--LSVPDVINCLTTTYdglEQMHKDL-----VNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 484
Cdd:cd16250    7 EAFRDNGLNTLDHSteISVSRLETIISSIY---YQLNKRLpsthqISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAML 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 485 MSLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQQnnnKPEISVKEFID 564
Cdd:cd16250   84 ATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYT--EHSVRTCFPQ---QKKIMLNMFLD 158


                 ..
gi 578812961 565 WM 566
Cdd:cd16250  159 TM 160
SPEC smart00150
Spectrin repeats;
220-320 4.40e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 4.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961   220 LQGAMDDLDADMKEAESVRNGWKPVGDLliDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKMSRQLD 299
Cdd:smart00150   3 FLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                           90       100
                   ....*....|....*....|.
gi 578812961   300 DLNMRWKLLQVSVDDRLKQLQ 320
Cdd:smart00150  81 ELNERWEELKELAEERRQKLE 101
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 594-640 6.63e-08

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: 49.74  E-value: 6.63e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 578812961 594 CNICKEcPIVGFRYRSLKHFNYDVCQSCFFSGRtaKGHKLHYPMVEY 640
Cdd:cd02249    3 CDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
SPEC smart00150
Spectrin repeats;
7-79 3.50e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 49.25  E-value: 3.50e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578812961     7 NLRELLTKFeKDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLE 79
Cdd:smart00150  32 SVEALLKKH-EAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEIEERLEELNERWEELKELAEERRQKLE 101
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 341-369 5.23e-07

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: 46.75  E-value: 5.23e-07
                         10        20
                 ....*....|....*....|....*....
gi 578812961 341 PWQRSISHNKVPYYINHQTQTTCWDHPKM 369
Cdd:cd00201    3 GWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC smart00150
Spectrin repeats;
92-211 2.48e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.94  E-value: 2.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961    92 LEELIKWLNMKdEELKKQMPIGGDVPALQLQYDHCKALRRELKEKEYSVLNAVDQARVFLADQPIEAPEeprrnlqskte 171
Cdd:smart00150   7 ADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE----------- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 578812961   172 ltpeeraqkiakaMRKQSSEVKEKWESLNAVTSNWQKQVD 211
Cdd:smart00150  75 -------------IEERLEELNERWEELKELAEERRQKLE 101
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 337-369 3.99e-06

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: 44.13  E-value: 3.99e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 578812961   337 SVQLPWQRSISHNKVPYYINHQTQTTCWDHPKM 369
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 341-367 1.15e-05

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: 42.88  E-value: 1.15e-05
                          10        20
                  ....*....|....*....|....*..
gi 578812961  341 PWQRSISHNKVPYYINHQTQTTCWDHP 367
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 594-637 2.18e-05

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: 42.72  E-value: 2.18e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 578812961 594 CNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPM 637
Cdd:cd02338    3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 215-321 2.63e-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 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: 44.23  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  215 EKLRDLQGAMDDLDADMKEAEsVRNGWKPVGDLLiDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKM 294
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKE-ALLSSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78

                          90       100
                  ....*....|....*....|....*..
gi 578812961  295 SRQLDDLNMRWKLLQVSVDDRLKQLQE 321
Cdd:pfam00435  79 QERLEELNERWEQLLELAAERKQKLEE 105
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 594-640 1.16e-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: 1.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 578812961 594 CNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRtakgHKLHYPMVEY 640
Cdd:cd02339    3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDK----HDLEHRFYRY 45
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 7-80 2.76e-04

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 41.15  E-value: 2.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578812961    7 NLRELLTKFeKDIQAEIDAHNDIFKSIDGNRQKMVKALGNSEEAtmLQHRLDDMNQRWNDLKAKSASIRAHLEA 80
Cdd:pfam00435  35 SVQALLKKH-KALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQERLEELNERWEQLLELAAERKQKLEE 105
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 594-639 3.55e-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: 39.11  E-value: 3.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 578812961 594 CNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVE 639
Cdd:cd02345    3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-233 4.41e-04

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: 44.28  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961     1 MIGLNFNLRELLTKFEKdIQAEIDAHNDIFKSIDGNRQKMVKALGNseeatmLQHRLDDMNQRWNDLKAKSASIRAHLEA 80
Cdd:TIGR02168  854 IESLAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEE------LSEELRELESKRSELRRELEELREKLAQ 926

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961    81 SAEKWNRLLMSLEELIKWLN----MKDEELKKQMPigGDVPALQLQYDHCKALRRELKEkeysvLNAVDqarvfladqpI 156
Cdd:TIGR02168  927 LELRLEGLEVRIDNLQERLSeeysLTLEEAEALEN--KIEDDEEEARRRLKRLENKIKE-----LGPVN----------L 989

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578812961   157 EAPEEPRrnlqskteltpeeraqkiakamrkqssEVKEKWESLNavtsnwqKQVDKALEKLRDLQGAMDDLDADMKE 233
Cdd:TIGR02168  990 AAIEEYE---------------------------ELKERYDFLT-------AQKEDLTEAKETLEEAIEEIDREARE 1032
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 17-236 1.82e-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: 41.67  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  17 KDIQAEIDAHNDIFKSIDGNRQKmvkalgnseeatmLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLMSLEELI 96
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKA-------------LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  97 KWLNMKDEELKKQMPI---GGDVPALQL---QYDHCKALRRelkekeYSVLNAVDQARVFLADQPIEAPEEPRRNLQS-- 168
Cdd:COG4942   97 AELEAQKEELAELLRAlyrLGRQPPLALllsPEDFLDAVRR------LQYLKYLAPARREQAEELRADLAELAALRAEle 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578812961 169 --KTELTPEERAQKIAKA-MRKQSSEVKEKWESLNAVTSNWQKQVDKALEKLRDLQGAMDDLDADMKEAES 236
Cdd:COG4942  171 aeRAELEALLAELEEERAaLEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK01156 PRK01156
chromosome segregation protein; Provisional
 70-325 2.58e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.81  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961  70 KSASIRAHLEASAEKWNRLLMSLEELIKWLNMKDEELKKQMPI--GGDVPALQLQYDHCKALRRELKEKEysvlnaVDQA 147
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYleSEEINKSINEYNKIESARADLEDIK------IKIN 539

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 148 RVFLADQPIEAPEEPRRNLQSkteltpEERAQKiakamrkqssevKEKWESLNAVTS-----NWQKQVDKALEKLRDLQG 222
Cdd:PRK01156 540 ELKDKHDKYEEIKNRYKSLKL------EDLDSK------------RTSWLNALAVISlidieTNRSRSNEIKKQLNDLES 601

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578812961 223 AMDDLDADM---------------KEAESVRNGWKPVGDL--LIDSLQdhiEKIMAFREEIAPINFKVKTVNDLSSQLSp 285
Cdd:PRK01156 602 RLQEIEIGFpddksyidksireieNEANNLNNKYNEIQENkiLIEKLR---GKIDNYKKQIAEIDSIIPDLKEITSRIN- 677

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 578812961 286 lDLHPSLKMSR-QLDDLNM---RWKLLQVSVDDRLKQLQEAHRD 325
Cdd:PRK01156 678 -DIEDNLKKSRkALDDAKAnraRLESTIEILRTRINELSDRIND 720
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 596-638 5.52e-03

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: 35.70  E-value: 5.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 578812961 596 ICKEC--PIVGFRYRSLKHFNYDVCQSCffsgrTAKG-HKLHyPMV 638
Cdd:cd02340    2 ICDGCqgPIVGVRYKCLVCPDYDLCESC-----EAKGvHPEH-AML 41
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
 594-626 6.26e-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: 35.37  E-value: 6.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 578812961 594 CNIC-KECPIVgfRYRSLKHFNYDVCQSCFFSGR 626
Cdd:cd02336    3 CFTCgNDCTRV--RYHNLKAKKYDLCPSCYQEGR 34
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
 593-622 9.45e-03

Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239082  Cd Length: 43  Bit Score: 34.86  E-value: 9.45e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 578812961 593 KCNICKECPIVGFRYRSLKHFNYDVCQSCF 622
Cdd:cd02342    2 QCDGCGVLPITGPRYKSKVKEDYDLCTICF 31
 
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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