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Conserved domains on  [gi|1720361273|ref|XP_030100928|]
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utrophin isoform X9 [Mus musculus]

Protein Classification

WW domain-containing protein( domain architecture ID 11523295)

WW domain-containing protein; the WW domain mediates protein-protein interaction via proline-rich motifs, such as PPxY

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 ...
 367-528 7.15e-113

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: 342.65  E-value: 7.15e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 367 ELNTTNEVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 446
Cdd:cd16247     1 DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 447 SLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 526
Cdd:cd16247    81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDW 160


                  ..
gi 1720361273 527 MH 528
Cdd:cd16247   161 MR 162
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 553-601 7.51e-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: 112.06  E-value: 7.51e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720361273 553 AKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEY 601
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 7-175 1.44e-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: 76.72  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273   7 NSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWnRLLASLEELIKWLNMKDEELkKQMPIGGDVPALQLQYDH 86
Cdd:cd00176    70 GHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKK 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  87 CKVLRRELKEKEYSVLNAVDQARVFLADQPIEAPEEprrnpqskteltpeeraqkiakaMRKQSSEVREKWENLNAVTSN 166
Cdd:cd00176   148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDADEE-----------------------IEEKLEELNERWEELLELAEE 204


                  ....*....
gi 1720361273 167 WQKQVGKAL 175
Cdd:cd00176   205 RQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 177-293 2.67e-10

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 61.31  E-value: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 177 KLRDLQGAMDDLDADMKEVEAVRNGWKPVGDLliDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSLKMS 256
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720361273 257 RQLDDLNMRWKLLQVSVDDRLKQLQEAHRDFGPSSQH 293
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA 115
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 302-330 5.01e-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: 5.01e-07
                          10        20
                  ....*....|....*....|....*....
gi 1720361273 302 PWQRSISHNKVPYYINHQTQTTCWDHPKM 330
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 ...
 367-528 7.15e-113

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: 342.65  E-value: 7.15e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 367 ELNTTNEVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 446
Cdd:cd16247     1 DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 447 SLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 526
Cdd:cd16247    81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDW 160


                  ..
gi 1720361273 527 MH 528
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. ...
 331-449 6.63e-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: 183.12  E-value: 6.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 331 TELFQSLADLNNVRFSAYRTAIKIRRLQKALCLDLLELNTTNEVFKQHKLN--QNDQLLSVPDVINCLTTTYDGLEQLHK 408
Cdd:pfam09068   1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720361273 409 D--LVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLS 449
Cdd:pfam09068  81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 553-601 7.51e-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: 112.06  E-value: 7.51e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720361273 553 AKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEY 601
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 7-175 1.44e-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: 76.72  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273   7 NSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWnRLLASLEELIKWLNMKDEELkKQMPIGGDVPALQLQYDH 86
Cdd:cd00176    70 GHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKK 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  87 CKVLRRELKEKEYSVLNAVDQARVFLADQPIEAPEEprrnpqskteltpeeraqkiakaMRKQSSEVREKWENLNAVTSN 166
Cdd:cd00176   148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDADEE-----------------------IEEKLEELNERWEELLELAEE 204


                  ....*....
gi 1720361273 167 WQKQVGKAL 175
Cdd:cd00176   205 RQKKLEEAL 213
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 549-593 3.31e-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: 3.31e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1720361273 549 AKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSgRTAKGHK 593
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQ 44
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 550-593 6.53e-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: 6.53e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1720361273  550 KHQAKCNICKEcPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHK 593
Cdd:smart00291   2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 177-293 2.67e-10

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 61.31  E-value: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 177 KLRDLQGAMDDLDADMKEVEAVRNGWKPVGDLliDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSLKMS 256
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720361273 257 RQLDDLNMRWKLLQVSVDDRLKQLQEAHRDFGPSSQH 293
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA 115
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 302-330 5.01e-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: 5.01e-07
                          10        20
                  ....*....|....*....|....*....
gi 1720361273 302 PWQRSISHNKVPYYINHQTQTTCWDHPKM 330
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC smart00150
Spectrin repeats;
48-170 1.12e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 47.71  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273   48 RLLASLEELIKWLNMKdEELKKQMPIGGDVPALQLQYDHCKVLRRELKEKEYSVLNAVDQARVFLADQPIEAPEeprrnp 127
Cdd:smart00150   2 QFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE------ 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720361273  128 qskteltpeeraqkiakaMRKQSSEVREKWENLNAVTSNWQKQ 170
Cdd:smart00150  75 ------------------IEERLEELNERWEELKELAEERRQK 99
SPEC smart00150
Spectrin repeats;
181-281 1.15e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 47.71  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  181 LQGAMDDLDADMKEVEAVRNGWKPVGDLliDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSLKMSRQLD 260
Cdd:smart00150   3 FLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                           90       100
                   ....*....|....*....|.
gi 1720361273  261 DLNMRWKLLQVSVDDRLKQLQ 281
Cdd:smart00150  81 ELNERWEELKELAEERRQKLE 101
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 298-330 4.18e-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: 4.18e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1720361273  298 SVQLPWQRSISHNKVPYYINHQTQTTCWDHPKM 330
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 302-328 1.10e-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: 1.10e-05
                          10        20
                  ....*....|....*....|....*..
gi 1720361273 302 PWQRSISHNKVPYYINHQTQTTCWDHP 328
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 176-282 1.40e-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: 44.62  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 176 EKLRDLQGAMDDLDADMKEVEAVrNGWKPVGDLLiDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSLKM 255
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEAL-LSSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78

                          90       100
                  ....*....|....*....|....*..
gi 1720361273 256 SRQLDDLNMRWKLLQVSVDDRLKQLQE 282
Cdd:pfam00435  79 QERLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 8-284 1.01e-04

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: 46.21  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273    8 SEEATMLQHRLDDMNQRWNDLKAKSASIRAH------------------------LEASAEKWNRLLASLEELIKWLNMK 63
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRldelsqelsdasrkigeiekeieqLEQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273   64 DEELKKQMP-IGGDVPALQLQ-----------YDHCKVLRRELKEKEYSVLNAVdQARVFLADQPIEAPEEPRrnpQSKT 131
Cdd:TIGR02169  753 IENVKSELKeLEARIEELEEDlhkleealndlEARLSHSRIPEIQAELSKLEEE-VSRIEARLREIEQKLNRL---TLEK 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  132 ELTPEERAQKIAK--AMRKQSSEVREKWENLN-------AVTSNWQKQVGKALEKLRDLQGAMDDLDADMKEVEAVRNGW 202
Cdd:TIGR02169  829 EYLEKEIQELQEQriDLKEQIKSIEKEIENLNgkkeeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  203 KPVGDLLIDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLdlhPSLKMSRQ--------LDDLNMRWKLLQVSVD 274
Cdd:TIGR02169  909 EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL---EDVQAELQrveeeiraLEPVNMLAIQEYEEVL 985

                          330
                   ....*....|
gi 1720361273  275 DRLKQLQEAH 284
Cdd:TIGR02169  986 KRLDELKEKR 995
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
39-183 3.02e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  39 LEASAEKWNRLLASLEELIKWLNMKDEELKKqmpiggdvpalqlqydhckvLRRELKE--KEYSVLnavdQARVFLADQP 116
Cdd:PRK03918  312 IEKRLSRLEEEINGIEERIKELEEKEERLEE--------------------LKKKLKEleKRLEEL----EERHELYEEA 367

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 117 IEAPEEPRRNPQSKTELTPEERAQKIaKAMRKQSSEVREKWENLNAVTSNWQKQVG---KALEKLRDLQG 183
Cdd:PRK03918  368 KAKKEELERLKKRLTGLTPEKLEKEL-EELEKAKEEIEEEISKITARIGELKKEIKelkKAIEELKKAKG 436
 
Name Accession Description Interval E-value
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
 367-528 7.15e-113

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: 342.65  E-value: 7.15e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 367 ELNTTNEVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 446
Cdd:cd16247     1 DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 447 SLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 526
Cdd:cd16247    81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDW 160


                  ..
gi 1720361273 527 MH 528
Cdd:cd16247   161 MR 162
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
 367-528 2.42e-96

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: 299.54  E-value: 2.42e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 367 ELNTTNEVFKQHKLN-QNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 445
Cdd:cd16242     1 SLSTAIEAFDQHGLRaQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 446 MSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFID 525
Cdd:cd16242    81 VLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSVRSCFEKAGEKPEISAAHFLD 160


                  ...
gi 1720361273 526 WMH 528
Cdd:cd16242   161 WLK 163
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
 373-527 1.18e-82

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: 263.05  E-value: 1.18e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 373 EVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLSKGL 452
Cdd:cd16246     7 EALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAH 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720361273 453 LEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDWM 527
Cdd:cd16246    87 LEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWM 161
EFh_DRP-2 cd16248
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ...
 367-527 4.98e-71

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: 231.61  E-value: 4.98e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 367 ELNTTNEVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 446
Cdd:cd16248     1 TLSSATEIFTEHELQMSERVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 447 SLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 526
Cdd:cd16248    81 CLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVEPSVRSCFRFAPGKPVIELSQFLEW 160


                  .
gi 1720361273 527 M 527
Cdd:cd16248   161 M 161
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 367-527 2.30e-55

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: 188.63  E-value: 2.30e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 367 ELNTTNEVFKQHKLNQ-NDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 445
Cdd:cd15901     1 DLSTVLSVFDRHGLSGsQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 446 MSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFID 525
Cdd:cd15901    81 ITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLS 160


                  ..
gi 1720361273 526 WM 527
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. ...
 331-449 6.63e-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: 183.12  E-value: 6.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 331 TELFQSLADLNNVRFSAYRTAIKIRRLQKALCLDLLELNTTNEVFKQHKLN--QNDQLLSVPDVINCLTTTYDGLEQLHK 408
Cdd:pfam09068   1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720361273 409 D--LVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLS 449
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. ...
 453-544 1.42e-45

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: 158.23  E-value: 1.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 453 LEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGsnIEPSVRSCFQQNNNKPEISVKEFIDWMHLEPQ 532
Cdd:pfam09069   1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGG--IEPSVRSCFEQVGGKPKITLNHFLDWLMSEPQ 78

                          90
                  ....*....|..
gi 1720361273 533 SMVWLPVLHRVA 544
Cdd:pfam09069  79 SLVWLPVLHRLA 90
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 553-601 7.51e-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: 112.06  E-value: 7.51e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720361273 553 AKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEY 601
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
 368-527 1.32e-19

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: 86.58  E-value: 1.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 368 LNTTNEVFKQHKLNQNDQLLSVP--DVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 445
Cdd:cd16245     2 LKLIMGVFDRHQLSNSENNLCLPpdELEAVLHDIYFAAEKLGNFNIDVDLATELLANLFLNVFDPERKKSISVLELKVFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 446 MSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFID 525
Cdd:cd16245    82 TLLCGSSLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPGLVGLTEYQFIG 161


                  ..
gi 1720361273 526 WM 527
Cdd:cd16245   162 WW 163
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 373-527 1.27e-15

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: 75.35  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 373 EVFKQHKLNQND--QLLSVPDVINCLTTTYdglEQLHKDL-----VNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 445
Cdd:cd16244     7 EAFRENGLNTLDptTELSVSRLETLLSSIY---YQLNKRLptthqIDVDQSISLLLNWLLAAYDPEATGRLTVFSVKVAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 446 MSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQQNNnkpEISVKEFID 525
Cdd:cd16244    84 STLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYN--ESAARSCFPGQS---KVTVNDFLD 158


                  ..
gi 1720361273 526 WM 527
Cdd:cd16244   159 VM 160
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 7-175 1.44e-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: 76.72  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273   7 NSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWnRLLASLEELIKWLNMKDEELkKQMPIGGDVPALQLQYDH 86
Cdd:cd00176    70 GHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKK 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  87 CKVLRRELKEKEYSVLNAVDQARVFLADQPIEAPEEprrnpqskteltpeeraqkiakaMRKQSSEVREKWENLNAVTSN 166
Cdd:cd00176   148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDADEE-----------------------IEEKLEELNERWEELLELAEE 204


                  ....*....
gi 1720361273 167 WQKQVGKAL 175
Cdd:cd00176   205 RQKKLEEAL 213
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 549-593 3.31e-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: 3.31e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1720361273 549 AKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSgRTAKGHK 593
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQ 44
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 550-593 6.53e-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: 6.53e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1720361273  550 KHQAKCNICKEcPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHK 593
Cdd:smart00291   2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 45-284 8.27e-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: 74.40  E-value: 8.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  45 KWNRLLASLEELIKWLNMKDEELKkQMPIGGDVPALQLQYDHCKVLRRELKEKEYSVLNAVDQARVFLADQPIEAPEepr 124
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 125 rnpqskteltpeeraqkiakaMRKQSSEVREKWENLNAVTSNWQKQVGKALEKLRDLQgAMDDLDADMKEVEAVRNGWKP 204
Cdd:cd00176    77 ---------------------IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 205 VGDLliDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQL-SPLDLHPSLKMSRQLDDLNMRWKLLQVSVDDRLKQLQEA 283
Cdd:cd00176   135 GKDL--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212


                  .
gi 1720361273 284 H 284
Cdd:cd00176   213 L 213
EFh_DYTN cd16243
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ...
 424-527 3.21e-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: 65.49  E-value: 3.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 424 LLNVYDTGRTGKIRVQSLKIGLMSLSKGLLEEKYRCLFK----EVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGgs 499
Cdd:cd16243    58 LFRLYDREQTGFVSLRSVEAALIALSGDTLSAKYRALFQlyesGQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFG-- 135

                          90       100
                  ....*....|....*....|....*...
gi 1720361273 500 NIEPSVRSCFQQNNNkPEISVKEFIDWM 527
Cdd:cd16243   136 NVETAVRSCFSGVLT-ASISEEHFLSWL 162
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 177-293 2.67e-10

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 61.31  E-value: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 177 KLRDLQGAMDDLDADMKEVEAVRNGWKPVGDLliDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSLKMS 256
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720361273 257 RQLDDLNMRWKLLQVSVDDRLKQLQEAHRDFGPSSQH 293
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA 115
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
 373-525 3.11e-09

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: 56.83  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 373 EVFKQHKLNQND--QLLSVPDVINCLTTTYdglEQLHKDL-----VNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 445
Cdd:cd16249     7 EALRENALNNLDpnTELNVARLEAVLSTIF---YQLNKRMptthqINVEQSISLLLNFLLAAFDPEGHGKISVFAVKMAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 446 MSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQQnnnKPEISVKEFID 525
Cdd:cd16249    84 ATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCFSQ---QKKVTLNGFLD 158
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 555-601 6.11e-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: 6.11e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720361273 555 CNICKEcPIVGFRYRSLKHFNYDVCQSCFFSGRtaKGHKLHYPMVEY 601
Cdd:cd02249     3 CDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
 373-527 2.22e-07

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: 51.56  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 373 EVFKQHKLNQNDQL--LSVPDVINCLTTTYdglEQLHKDL-----VNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 445
Cdd:cd16250     7 EAFRDNGLNTLDHSteISVSRLETIISSIY---YQLNKRLpsthqISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAML 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 446 MSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQQnnnKPEISVKEFID 525
Cdd:cd16250    84 ATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYT--EHSVRTCFPQ---QKKIMLNMFLD 158


                  ..
gi 1720361273 526 WM 527
Cdd:cd16250   159 TM 160
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 302-330 5.01e-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: 5.01e-07
                          10        20
                  ....*....|....*....|....*....
gi 1720361273 302 PWQRSISHNKVPYYINHQTQTTCWDHPKM 330
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC smart00150
Spectrin repeats;
48-170 1.12e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 47.71  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273   48 RLLASLEELIKWLNMKdEELKKQMPIGGDVPALQLQYDHCKVLRRELKEKEYSVLNAVDQARVFLADQPIEAPEeprrnp 127
Cdd:smart00150   2 QFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE------ 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720361273  128 qskteltpeeraqkiakaMRKQSSEVREKWENLNAVTSNWQKQ 170
Cdd:smart00150  75 ------------------IEERLEELNERWEELKELAEERRQK 99
SPEC smart00150
Spectrin repeats;
181-281 1.15e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 47.71  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  181 LQGAMDDLDADMKEVEAVRNGWKPVGDLliDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSLKMSRQLD 260
Cdd:smart00150   3 FLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                           90       100
                   ....*....|....*....|.
gi 1720361273  261 DLNMRWKLLQVSVDDRLKQLQ 281
Cdd:smart00150  81 ELNERWEELKELAEERRQKLE 101
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 298-330 4.18e-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: 4.18e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1720361273  298 SVQLPWQRSISHNKVPYYINHQTQTTCWDHPKM 330
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 302-328 1.10e-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: 1.10e-05
                          10        20
                  ....*....|....*....|....*..
gi 1720361273 302 PWQRSISHNKVPYYINHQTQTTCWDHP 328
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 176-282 1.40e-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: 44.62  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 176 EKLRDLQGAMDDLDADMKEVEAVrNGWKPVGDLLiDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSLKM 255
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEAL-LSSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78

                          90       100
                  ....*....|....*....|....*..
gi 1720361273 256 SRQLDDLNMRWKLLQVSVDDRLKQLQE 282
Cdd:pfam00435  79 QERLEELNERWEQLLELAAERKQKLEE 105
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 555-598 2.17e-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: 42.33  E-value: 2.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720361273 555 CNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPM 598
Cdd:cd02338     3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 8-284 1.01e-04

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: 46.21  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273    8 SEEATMLQHRLDDMNQRWNDLKAKSASIRAH------------------------LEASAEKWNRLLASLEELIKWLNMK 63
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRldelsqelsdasrkigeiekeieqLEQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273   64 DEELKKQMP-IGGDVPALQLQ-----------YDHCKVLRRELKEKEYSVLNAVdQARVFLADQPIEAPEEPRrnpQSKT 131
Cdd:TIGR02169  753 IENVKSELKeLEARIEELEEDlhkleealndlEARLSHSRIPEIQAELSKLEEE-VSRIEARLREIEQKLNRL---TLEK 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  132 ELTPEERAQKIAK--AMRKQSSEVREKWENLN-------AVTSNWQKQVGKALEKLRDLQGAMDDLDADMKEVEAVRNGW 202
Cdd:TIGR02169  829 EYLEKEIQELQEQriDLKEQIKSIEKEIENLNgkkeeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  203 KPVGDLLIDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLdlhPSLKMSRQ--------LDDLNMRWKLLQVSVD 274
Cdd:TIGR02169  909 EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL---EDVQAELQrveeeiraLEPVNMLAIQEYEEVL 985

                          330
                   ....*....|
gi 1720361273  275 DRLKQLQEAH 284
Cdd:TIGR02169  986 KRLDELKEKR 995
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 555-601 1.11e-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: 1.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720361273 555 CNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRtakgHKLHYPMVEY 601
Cdd:cd02339     3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDK----HDLEHRFYRY 45
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 555-600 3.51e-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: 3.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720361273 555 CNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVE 600
Cdd:cd02345     3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 8-323 8.84e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 8.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273    8 SEEATMLQHRLDDMNQRWNDLKaksasirahleasaEKWNRLLASLEELIKWLNMKDEELKKQMpiggdvpalqlqydhc 87
Cdd:TIGR00618  562 KEQMQEIQQSFSILTQCDNRSK--------------EDIPNLQNITVRLQDLTEKLSEAEDMLA---------------- 611

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273   88 KVLRRELKEKEYsvlnAVDQARVFLADQPIEAPEEPRRNPQSKTELT-PEERAQKIAKAMRKQSSEVREKWENLNAVTSN 166
Cdd:TIGR00618  612 CEQHALLRKLQP----EQDLQDVRLHLQQCSQELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQLALQKMQS 687

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  167 WQKQVGKALEKLRDLQGAMDDLDADMKEVEAVRNGWKPVGDLLIDSLQ---DHIEKTLAFREEIAPINLKVKTMNDL-SS 242
Cdd:TIGR00618  688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAareDALNQSLKELMHQARTVLKARTEAHFnNN 767

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  243 QLSPLDLHPSLKMSRQLDDLNMRWKLLQVSVDDrLKQLQEAHRDFGPSSQHFLSTSVQLPWQRSIS-HNKVPyyINHQTQ 321
Cdd:TIGR00618  768 EEVTAALQTGAELSHLAAEIQFFNRLREEDTHL-LKTLEAEIGQEIPSDEDILNLQCETLVQEEEQfLSRLE--EKSATL 844


                   ..
gi 1720361273  322 TT 323
Cdd:TIGR00618  845 GE 846
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
39-183 3.02e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  39 LEASAEKWNRLLASLEELIKWLNMKDEELKKqmpiggdvpalqlqydhckvLRRELKE--KEYSVLnavdQARVFLADQP 116
Cdd:PRK03918  312 IEKRLSRLEEEINGIEERIKELEEKEERLEE--------------------LKKKLKEleKRLEEL----EERHELYEEA 367

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 117 IEAPEEPRRNPQSKTELTPEERAQKIaKAMRKQSSEVREKWENLNAVTSNWQKQVG---KALEKLRDLQG 183
Cdd:PRK03918  368 KAKKEELERLKKRLTGLTPEKLEKEL-EELEKAKEEIEEEISKITARIGELKKEIKelkKAIEELKKAKG 436
PRK01156 PRK01156
chromosome segregation protein; Provisional
 31-286 3.22e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.43  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273  31 KSASIRAHLEASAEKWNRLLASLEELIKWLNMKDEELKKQMPI--GGDVPALQLQYDHCKVLRRELKEKEysvlnaVDQA 108
Cdd:PRK01156  466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYleSEEINKSINEYNKIESARADLEDIK------IKIN 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 109 RvfLADQPIEApeeprrnpqskTELTPEERAQKIAKAMRKqssevREKWENLNAVTS-----NWQKQVGKALEKLRDLQG 183
Cdd:PRK01156  540 E--LKDKHDKY-----------EEIKNRYKSLKLEDLDSK-----RTSWLNALAVISlidieTNRSRSNEIKKQLNDLES 601

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361273 184 AMDDLDADM---------------KEVEAVRNGWKPVGDL--LIDSLQDHIEKtlaFREEIAPINLKVKTMNDLSSQLSp 246
Cdd:PRK01156  602 RLQEIEIGFpddksyidksireieNEANNLNNKYNEIQENkiLIEKLRGKIDN---YKKQIAEIDSIIPDLKEITSRIN- 677

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1720361273 247 lDLHPSLKMSR-QLDDLNM---RWKLLQVSVDDRLKQLQEAHRD 286
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 ...
 557-599 5.29e-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: 5.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720361273 557 ICKEC--PIVGFRYRSLKHFNYDVCQSCffsgrTAKG-HKLHyPMV 599
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 ...
 555-587 6.00e-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: 6.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720361273 555 CNIC-KECPIVgfRYRSLKHFNYDVCQSCFFSGR 587
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 ...
 554-583 9.06e-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: 9.06e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720361273 554 KCNICKECPIVGFRYRSLKHFNYDVCQSCF 583
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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