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Conserved domains on  [gi|1769047537|ref|NP_001362252|]
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utrophin isoform 2 [Homo sapiens]

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 ...
 437-598 1.38e-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: 346.11  E-value: 1.38e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 437 ELSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 516
Cdd:cd16247     1 DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 517 SLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 596
Cdd:cd16247    81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDW 160


                  ..
gi 1769047537 597 MH 598
Cdd:cd16247   161 MR 162
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 623-671 2.22e-29

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: 110.91  E-value: 2.22e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1769047537 623 AKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEY 671
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 44-245 3.61e-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: 90.20  E-value: 3.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  44 QKLCKDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLMsL 123
Cdd:cd00176    39 LKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-A 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 124 EELIKWLNMKDEELkKQMPIGGDVPALQLQYDHCKALRRELKEKEYSVLNAVDQARVFLADQPIEAPEEPRRNLQsktel 203
Cdd:cd00176   116 DDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE----- 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1769047537 204 tpeeraqkiakamrkqssEVKEKWESLNAVTSNWQKQVDKAL 245
Cdd:cd00176   190 ------------------ELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 247-363 7.66e-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: 7.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 247 KLRDLQGAMDDLDADMKEAESVRNGWKPVGDLliDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKMS 326
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1769047537 327 RQLDDLNMRWKLLQVSVDDRLKQLQEAHRDFGPSSQH 363
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA 115
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 372-400 5.40e-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: 5.40e-07
                          10        20
                  ....*....|....*....|....*....
gi 1769047537 372 PWQRSISHNKVPYYINHQTQTTCWDHPKM 400
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 ...
 437-598 1.38e-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: 346.11  E-value: 1.38e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 437 ELSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 516
Cdd:cd16247     1 DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 517 SLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 596
Cdd:cd16247    81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDW 160


                  ..
gi 1769047537 597 MH 598
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. ...
 401-519 1.49e-53

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: 182.35  E-value: 1.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 401 TELFQSLADLNNVRFSAYRTAIKIRRLQKALCLDLLELSTTNEIFKQHKLN--QNDQLLSVPDVINCLTTTYDGLEQMHK 478
Cdd:pfam09068   1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1769047537 479 D--LVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLS 519
Cdd:pfam09068  81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 623-671 2.22e-29

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: 110.91  E-value: 2.22e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1769047537 623 AKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEY 671
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 44-245 3.61e-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: 90.20  E-value: 3.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  44 QKLCKDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLMsL 123
Cdd:cd00176    39 LKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-A 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 124 EELIKWLNMKDEELkKQMPIGGDVPALQLQYDHCKALRRELKEKEYSVLNAVDQARVFLADQPIEAPEEPRRNLQsktel 203
Cdd:cd00176   116 DDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE----- 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1769047537 204 tpeeraqkiakamrkqssEVKEKWESLNAVTSNWQKQVDKAL 245
Cdd:cd00176   190 ------------------ELNERWEELLELAEERQKKLEEAL 213
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 619-663 5.91e-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: 69.43  E-value: 5.91e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1769047537 619 AKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSgRTAKGHK 663
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQ 44
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 620-663 7.04e-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: 7.04e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1769047537  620 KHQAKCNICKEcPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHK 663
Cdd:smart00291   2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 247-363 7.66e-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: 7.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 247 KLRDLQGAMDDLDADMKEAESVRNGWKPVGDLliDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKMS 326
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1769047537 327 RQLDDLNMRWKLLQVSVDDRLKQLQEAHRDFGPSSQH 363
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA 115
SPEC smart00150
Spectrin repeats;
251-351 4.59e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 4.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  251 LQGAMDDLDADMKEAESVRNGWKPVGDLliDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKMSRQLD 330
Cdd:smart00150   3 FLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                           90       100
                   ....*....|....*....|.
gi 1769047537  331 DLNMRWKLLQVSVDDRLKQLQ 351
Cdd:smart00150  81 ELNERWEELKELAEERRQKLE 101
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 372-400 5.40e-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: 5.40e-07
                          10        20
                  ....*....|....*....|....*....
gi 1769047537 372 PWQRSISHNKVPYYINHQTQTTCWDHPKM 400
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC smart00150
Spectrin repeats;
44-110 7.81e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.48  E-value: 7.81e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1769047537   44 QKLCKDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLE 110
Cdd:smart00150  37 LKKHEAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEIEERLEELNERWEELKELAEERRQKLE 101
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 368-400 4.12e-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: 4.12e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1769047537  368 SVQLPWQRSISHNKVPYYINHQTQTTCWDHPKM 400
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 372-398 1.18e-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: 1.18e-05
                          10        20
                  ....*....|....*....|....*..
gi 1769047537 372 PWQRSISHNKVPYYINHQTQTTCWDHP 398
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 246-352 2.44e-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: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 246 EKLRDLQGAMDDLDADMKEAEsVRNGWKPVGDLLiDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKM 325
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKE-ALLSSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78

                          90       100
                  ....*....|....*....|....*..
gi 1769047537 326 SRQLDDLNMRWKLLQVSVDDRLKQLQE 352
Cdd:pfam00435  79 QERLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-264 1.46e-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: 45.82  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537   24 QKVVVLLHRLQRMAVSSPRYQKLCKDIQAEIDAHNDIFKSIDGNRQKMVKALGNseeatmLQHRLDDMNQRWNDLKAKSA 103
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE------LSEELRELESKRSELRRELE 918

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  104 SIRAHLEASAEKWNRLLMSLEELIKWLN----MKDEELKKQMPigGDVPALQLQYDHCKALRRELKEkeysvLNAVDqar 179
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQERLSeeysLTLEEAEALEN--KIEDDEEEARRRLKRLENKIKE-----LGPVN--- 988

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  180 vfladqpIEAPEEPRrnlqskteltpeeraqkiakamrkqssEVKEKWESLNavtsnwqKQVDKALEKLRDLQGAMDDLD 259
Cdd:TIGR02168  989 -------LAAIEEYE---------------------------ELKERYDFLT-------AQKEDLTEAKETLEEAIEEID 1027


                   ....*
gi 1769047537  260 ADMKE 264
Cdd:TIGR02168 1028 REARE 1032
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 44-111 1.66e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 38.84  E-value: 1.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769047537  44 QKLCKDIQAEIDAHNDIFKSIDGNRQKMVKALGNSEEAtmLQHRLDDMNQRWNDLKAKSASIRAHLEA 111
Cdd:pfam00435  40 LKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQERLEELNERWEQLLELAAERKQKLEE 105
PRK01156 PRK01156
chromosome segregation protein; Provisional
 101-356 1.69e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.20  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 101 KSASIRAHLEASAEKWNRLLMSLEELIKWLNMKDEELKKQMPI--GGDVPALQLQYDHCKALRRELKEKEysvlnaVDQA 178
Cdd:PRK01156  466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYleSEEINKSINEYNKIESARADLEDIK------IKIN 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 179 RVFLADQPIEAPEEPRRNLQSkteltpEERAQKiakamrkqssevKEKWESLNAVTSN-----WQKQVDKALEKLRDLQG 253
Cdd:PRK01156  540 ELKDKHDKYEEIKNRYKSLKL------EDLDSK------------RTSWLNALAVISLidietNRSRSNEIKKQLNDLES 601

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 254 AMDDLDADM---------------KEAESVRNGWKPVGDL--LIDSLQdhiEKIMAFREEIAPINFKVKTVNDLSSQLSp 316
Cdd:PRK01156  602 RLQEIEIGFpddksyidksireieNEANNLNNKYNEIQENkiLIEKLR---GKIDNYKKQIAEIDSIIPDLKEITSRIN- 677

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1769047537 317 lDLHPSLKMSR-QLDDLNM---RWKLLQVSVDDRLKQLQEAHRD 356
Cdd:PRK01156  678 -DIEDNLKKSRkALDDAKAnraRLESTIEILRTRINELSDRIND 720
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 48-267 2.13e-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: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  48 KDIQAEIDAHNDIFKSIDGNRQKmvkalgnseeatmLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLMSLEELI 127
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKA-------------LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 128 KWLNMKDEELKKQMPI---GGDVPALQL---QYDHCKALRRelkekeYSVLNAVDQARVFLADQPIEAPEEPRRNLQS-- 199
Cdd:COG4942    97 AELEAQKEELAELLRAlyrLGRQPPLALllsPEDFLDAVRR------LQYLKYLAPARREQAEELRADLAELAALRAEle 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1769047537 200 --KTELTPEERAQKIAKA-MRKQSSEVKEKWESLNAVTSNWQKQVDKALEKLRDLQGAMDDLDADMKEAES 267
Cdd:COG4942   171 aeRAELEALLAELEEERAaLEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
 
Name Accession Description Interval E-value
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
 437-598 1.38e-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: 346.11  E-value: 1.38e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 437 ELSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 516
Cdd:cd16247     1 DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 517 SLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 596
Cdd:cd16247    81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDW 160


                  ..
gi 1769047537 597 MH 598
Cdd:cd16247   161 MR 162
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
 437-598 7.63e-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: 307.24  E-value: 7.63e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 437 ELSTTNEIFKQHKLN-QNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 515
Cdd:cd16242     1 SLSTAIEAFDQHGLRaQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 516 MSLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFID 595
Cdd:cd16242    81 VLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSVRSCFEKAGEKPEISAAHFLD 160


                  ...
gi 1769047537 596 WMH 598
Cdd:cd16242   161 WLK 163
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
 438-597 6.23e-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: 267.67  E-value: 6.23e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 438 LSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMS 517
Cdd:cd16246     2 LSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 518 LSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDWM 597
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 ...
 437-597 4.38e-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: 238.16  E-value: 4.38e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 437 ELSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 516
Cdd:cd16248     1 TLSSATEIFTEHELQMSERVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 517 SLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 596
Cdd:cd16248    81 CLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVEPSVRSCFRFAPGKPVIELSQFLEW 160


                  .
gi 1769047537 597 M 597
Cdd:cd16248   161 M 161
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 437-597 2.08e-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: 194.80  E-value: 2.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 437 ELSTTNEIFKQHKLNQ-NDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 515
Cdd:cd15901     1 DLSTVLSVFDRHGLSGsQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 516 MSLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFID 595
Cdd:cd15901    81 ITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLS 160


                  ..
gi 1769047537 596 WM 597
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. ...
 401-519 1.49e-53

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: 182.35  E-value: 1.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 401 TELFQSLADLNNVRFSAYRTAIKIRRLQKALCLDLLELSTTNEIFKQHKLN--QNDQLLSVPDVINCLTTTYDGLEQMHK 478
Cdd:pfam09068   1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1769047537 479 D--LVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLS 519
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. ...
 523-614 4.11e-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: 162.86  E-value: 4.11e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 523 LEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGsnIEPSVRSCFQQNNNKPEISVKEFIDWMHLEPQ 602
Cdd:pfam09069   1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGG--IEPSVRSCFEQVGGKPKITLNHFLDWLMSEPQ 78

                          90
                  ....*....|..
gi 1769047537 603 SMVWLPVLHRVA 614
Cdd:pfam09069  79 SLVWLPVLHRLA 90
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 623-671 2.22e-29

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: 110.91  E-value: 2.22e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1769047537 623 AKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEY 671
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 44-245 3.61e-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: 90.20  E-value: 3.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  44 QKLCKDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLMsL 123
Cdd:cd00176    39 LKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-A 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 124 EELIKWLNMKDEELkKQMPIGGDVPALQLQYDHCKALRRELKEKEYSVLNAVDQARVFLADQPIEAPEEPRRNLQsktel 203
Cdd:cd00176   116 DDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE----- 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1769047537 204 tpeeraqkiakamrkqssEVKEKWESLNAVTSNWQKQVDKAL 245
Cdd:cd00176   190 ------------------ELNERWEELLELAEERQKKLEEAL 213
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
 444-597 6.06e-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: 6.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 444 IFKQHKLNQNDQLLSVP--DVINCLTTTYDGLEQMHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLSKG 521
Cdd:cd16245     8 VFDRHQLSNSENNLCLPpdELEAVLHDIYFAAEKLGNFNIDVDLATELLANLFLNVFDPERKKSISVLELKVFLTLLCGS 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769047537 522 LLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDWM 597
Cdd:cd16245    88 SLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPGLVGLTEYQFIGWW 163
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 443-597 1.57e-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: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 443 EIFKQHKLNQND--QLLSVPDVINCLTTTYDGLEQM--HKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSL 518
Cdd:cd16244     7 EAFRENGLNTLDptTELSVSRLETLLSSIYYQLNKRlpTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVKVALSTL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1769047537 519 SKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQQNNnkpEISVKEFIDWM 597
Cdd:cd16244    87 CAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYN--ESAARSCFPGQS---KVTVNDFLDVM 160
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 619-663 5.91e-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: 69.43  E-value: 5.91e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1769047537 619 AKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSgRTAKGHK 663
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQ 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 115-354 6.73e-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: 6.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 115 KWNRLLMSLEELIKWLNMKDEELKkQMPIGGDVPALQLQYDHCKALRRELKEKEYSVLNAVDQARVFLADQPIEAPEepr 194
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 195 rnlqskteltpeeraqkiakaMRKQSSEVKEKWESLNAVTSNWQKQVDKALEKLRDLQgAMDDLDADMKEAESVRNGWKP 274
Cdd:cd00176    77 ---------------------IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 275 VGDLliDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQL-SPLDLHPSLKMSRQLDDLNMRWKLLQVSVDDRLKQLQEA 353
Cdd:cd00176   135 GKDL--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212


                  .
gi 1769047537 354 H 354
Cdd:cd00176   213 L 213
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 620-663 7.04e-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: 7.04e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1769047537  620 KHQAKCNICKEcPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHK 663
Cdd:smart00291   2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 247-363 7.66e-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: 7.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 247 KLRDLQGAMDDLDADMKEAESVRNGWKPVGDLliDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKMS 326
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1769047537 327 RQLDDLNMRWKLLQVSVDDRLKQLQEAHRDFGPSSQH 363
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA 115
EFh_DYTN cd16243
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ...
 451-597 4.06e-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: 65.10  E-value: 4.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 451 NQNDQLLSVPDVINCLTTTYDGLEQMHKDLVNVPLCvDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLSKGLLEEKYRYL 530
Cdd:cd16243    16 IERTISLSVEEVSQALERLFQSASQEVPGQVSAEAT-EQTCRLLFRLYDREQTGFVSLRSVEAALIALSGDTLSAKYRAL 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1769047537 531 FK----EVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGgsNIEPSVRSCFQQNNNkPEISVKEFIDWM 597
Cdd:cd16243    95 FQlyesGQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFG--NVETAVRSCFSGVLT-ASISEEHFLSWL 162
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
 443-595 6.37e-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: 6.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 443 EIFKQHKLNQND--QLLSVPDVINCLTTTYdglEQMHKDL-----VNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 515
Cdd:cd16249     7 EALRENALNNLDpnTELNVARLEAVLSTIF---YQLNKRMptthqINVEQSISLLLNFLLAAFDPEGHGKISVFAVKMAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 516 MSLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQQnnnKPEISVKEFID 595
Cdd:cd16249    84 ATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCFSQ---QKKVTLNGFLD 158
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
 443-597 3.97e-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: 53.88  E-value: 3.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 443 EIFKQHKLNQNDQL--LSVPDVINCLTTTYdglEQMHKDL-----VNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 515
Cdd:cd16250     7 EAFRDNGLNTLDHSteISVSRLETIISSIY---YQLNKRLpsthqISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAML 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 516 MSLSKGLLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQQnnnKPEISVKEFID 595
Cdd:cd16250    84 ATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYT--EHSVRTCFPQ---QKKIMLNMFLD 158


                  ..
gi 1769047537 596 WM 597
Cdd:cd16250   159 TM 160
SPEC smart00150
Spectrin repeats;
251-351 4.59e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 4.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  251 LQGAMDDLDADMKEAESVRNGWKPVGDLliDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKMSRQLD 330
Cdd:smart00150   3 FLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80

                           90       100
                   ....*....|....*....|.
gi 1769047537  331 DLNMRWKLLQVSVDDRLKQLQ 351
Cdd:smart00150  81 ELNERWEELKELAEERRQKLE 101
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 625-671 1.02e-07

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


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 48.97  E-value: 1.02e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1769047537 625 CNICKEcPIVGFRYRSLKHFNYDVCQSCFFSGRtaKGHKLHYPMVEY 671
Cdd:cd02249     3 CDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 372-400 5.40e-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: 5.40e-07
                          10        20
                  ....*....|....*....|....*....
gi 1769047537 372 PWQRSISHNKVPYYINHQTQTTCWDHPKM 400
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC smart00150
Spectrin repeats;
44-110 7.81e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.48  E-value: 7.81e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1769047537   44 QKLCKDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLE 110
Cdd:smart00150  37 LKKHEAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEIEERLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
123-242 2.44e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.94  E-value: 2.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  123 LEELIKWLNMKdEELKKQMPIGGDVPALQLQYDHCKALRRELKEKEYSVLNAVDQARVFLADQPIEAPEeprrnlqskte 202
Cdd:smart00150   7 ADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE----------- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1769047537  203 ltpeeraqkiakaMRKQSSEVKEKWESLNAVTSNWQKQVD 242
Cdd:smart00150  75 -------------IEERLEELNERWEELKELAEERRQKLE 101
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 368-400 4.12e-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: 4.12e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1769047537  368 SVQLPWQRSISHNKVPYYINHQTQTTCWDHPKM 400
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 372-398 1.18e-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: 1.18e-05
                          10        20
                  ....*....|....*....|....*..
gi 1769047537 372 PWQRSISHNKVPYYINHQTQTTCWDHP 398
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 246-352 2.44e-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: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 246 EKLRDLQGAMDDLDADMKEAEsVRNGWKPVGDLLiDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDLHPSLKM 325
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKE-ALLSSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78

                          90       100
                  ....*....|....*....|....*..
gi 1769047537 326 SRQLDDLNMRWKLLQVSVDDRLKQLQE 352
Cdd:pfam00435  79 QERLEELNERWEQLLELAAERKQKLEE 105
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 625-668 3.30e-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: 41.95  E-value: 3.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1769047537 625 CNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPM 668
Cdd:cd02338     3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-264 1.46e-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: 45.82  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537   24 QKVVVLLHRLQRMAVSSPRYQKLCKDIQAEIDAHNDIFKSIDGNRQKMVKALGNseeatmLQHRLDDMNQRWNDLKAKSA 103
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE------LSEELRELESKRSELRRELE 918

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  104 SIRAHLEASAEKWNRLLMSLEELIKWLN----MKDEELKKQMPigGDVPALQLQYDHCKALRRELKEkeysvLNAVDqar 179
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQERLSeeysLTLEEAEALEN--KIEDDEEEARRRLKRLENKIKE-----LGPVN--- 988

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  180 vfladqpIEAPEEPRrnlqskteltpeeraqkiakamrkqssEVKEKWESLNavtsnwqKQVDKALEKLRDLQGAMDDLD 259
Cdd:TIGR02168  989 -------LAAIEEYE---------------------------ELKERYDFLT-------AQKEDLTEAKETLEEAIEEID 1027


                   ....*
gi 1769047537  260 ADMKE 264
Cdd:TIGR02168 1028 REARE 1032
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 625-671 1.49e-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: 40.13  E-value: 1.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1769047537 625 CNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRtakgHKLHYPMVEY 671
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 ...
 625-670 5.44e-04

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


Pssm-ID: 239085  Cd Length: 49  Bit Score: 38.72  E-value: 5.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1769047537 625 CNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVE 670
Cdd:cd02345     3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 22-298 6.65e-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: 43.89  E-value: 6.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537   22 SLQKVVVLLHRLQRMAVSSPRYQKLCKDIQAEIDAhndIFKSIDGNRQKMVKAlgnSEEATMLQHRLDDMNQRWNDLKAK 101
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQE---LEEKLEELRLEVSEL---EEEIEELQKELYALANEISRLEQQ 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  102 SASIR---AHLEASAEKWN----RLLMSLEELIKWLNMKDEELKKQMPI-----------GGDVPALQLQYDHCKALRRE 163
Cdd:TIGR02168  304 KQILRerlANLERQLEELEaqleELESKLDELAEELAELEEKLEELKEElesleaeleelEAELEELESRLEELEEQLET 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  164 LKEKEYSVLNAVDQ--ARVFLADQPIEAPEEPRRNLQSKTELTPEERAQKIAKAMRKQSSEVKEKWESLNAVTSNWQKQV 241
Cdd:TIGR02168  384 LRSKVAQLELQIASlnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1769047537  242 DKALEKLRDLQGAMDDLDADMKEAESvrngwkpvgdlLIDSLQDHIEKIMAFREEIA 298
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQLQA-----------RLDSLERLQENLEGFSEGVK 509
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 44-111 1.66e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 38.84  E-value: 1.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769047537  44 QKLCKDIQAEIDAHNDIFKSIDGNRQKMVKALGNSEEAtmLQHRLDDMNQRWNDLKAKSASIRAHLEA 111
Cdd:pfam00435  40 LKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQERLEELNERWEQLLELAAERKQKLEE 105
PRK01156 PRK01156
chromosome segregation protein; Provisional
 101-356 1.69e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.20  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 101 KSASIRAHLEASAEKWNRLLMSLEELIKWLNMKDEELKKQMPI--GGDVPALQLQYDHCKALRRELKEKEysvlnaVDQA 178
Cdd:PRK01156  466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYleSEEINKSINEYNKIESARADLEDIK------IKIN 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 179 RVFLADQPIEAPEEPRRNLQSkteltpEERAQKiakamrkqssevKEKWESLNAVTSN-----WQKQVDKALEKLRDLQG 253
Cdd:PRK01156  540 ELKDKHDKYEEIKNRYKSLKL------EDLDSK------------RTSWLNALAVISLidietNRSRSNEIKKQLNDLES 601

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 254 AMDDLDADM---------------KEAESVRNGWKPVGDL--LIDSLQdhiEKIMAFREEIAPINFKVKTVNDLSSQLSp 316
Cdd:PRK01156  602 RLQEIEIGFpddksyidksireieNEANNLNNKYNEIQENkiLIEKLR---GKIDNYKKQIAEIDSIIPDLKEITSRIN- 677

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1769047537 317 lDLHPSLKMSR-QLDDLNM---RWKLLQVSVDDRLKQLQEAHRD 356
Cdd:PRK01156  678 -DIEDNLKKSRkALDDAKAnraRLESTIEILRTRINELSDRIND 720
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 48-267 2.13e-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: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  48 KDIQAEIDAHNDIFKSIDGNRQKmvkalgnseeatmLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLMSLEELI 127
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKA-------------LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 128 KWLNMKDEELKKQMPI---GGDVPALQL---QYDHCKALRRelkekeYSVLNAVDQARVFLADQPIEAPEEPRRNLQS-- 199
Cdd:COG4942    97 AELEAQKEELAELLRAlyrLGRQPPLALllsPEDFLDAVRR------LQYLKYLAPARREQAEELRADLAELAALRAEle 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1769047537 200 --KTELTPEERAQKIAKA-MRKQSSEVKEKWESLNAVTSNWQKQVDKALEKLRDLQGAMDDLDADMKEAES 267
Cdd:COG4942   171 aeRAELEALLAELEEERAaLEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
 625-657 6.53e-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: 6.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1769047537 625 CNIC-KECPIVgfRYRSLKHFNYDVCQSCFFSGR 657
Cdd:cd02336     3 CFTCgNDCTRV--RYHNLKAKKYDLCPSCYQEGR 34
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 627-669 9.15e-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: 34.93  E-value: 9.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1769047537 627 ICKEC--PIVGFRYRSLKHFNYDVCQSCffsgrTAKG-HKLHyPMV 669
Cdd:cd02340     2 ICDGCqgPIVGVRYKCLVCPDYDLCESC-----EAKGvHPEH-AML 41
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 40-393 9.47e-03

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: 39.95  E-value: 9.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537   40 SPRYQKLCKDIQAEIDAHNDIFKSIDGNRQKMVKALGN-SEEATMLQHRLDDMNQRWNDLKaksasirahleasaEKWNR 118
Cdd:TIGR00618  523 PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASlKEQMQEIQQSFSILTQCDNRSK--------------EDIPN 588

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  119 LLMSLEELIKWLNMKDEELKKQMpiggdvpalqlqydhcKALRRELKEKEYsvlnAVDQARVFLADQPIEAPEEPRRNLQ 198
Cdd:TIGR00618  589 LQNITVRLQDLTEKLSEAEDMLA----------------CEQHALLRKLQP----EQDLQDVRLHLQQCSQELALKLTAL 648

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  199 SKTELT-PEERAQKIAKAMRKQSSEVKEKWESLNAVTSNWQKQVDKALEKLRDLQGAMDDLDADMKEAESVRNGWKPVGD 277
Cdd:TIGR00618  649 HALQLTlTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASS 728

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  278 LLIDSLQD----HIEKIMAFREEiAPINFKVKTVNDL-SSQLSPLDLHPSLKMSRQLDDLNMRWKLLQVSVDDrLKQLQE 352
Cdd:TIGR00618  729 SLGSDLAAredaLNQSLKELMHQ-ARTVLKARTEAHFnNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL-LKTLEA 806

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1769047537  353 AHRDFGPSSQHFLSTSVQLPWQRSIS-HNKVPyyINHQTQTT 393
Cdd:TIGR00618  807 EIGQEIPSDEDILNLQCETLVQEEEQfLSRLE--EKSATLGE 846
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
68-356 9.71e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537  68 RQKMVKALGNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLMSLEELikwlnmkDEELKKQMPIGGDV 147
Cdd:PRK02224  331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL-------EEEIEELRERFGDA 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 148 PA--------LQLQYDHCKALRRELKEKEY---SVLNAVDQARVFLAD-------QPIE-AP--------EEPRRNLQ-- 198
Cdd:PRK02224  404 PVdlgnaedfLEELREERDELREREAELEAtlrTARERVEEAEALLEAgkcpecgQPVEgSPhvetieedRERVEELEae 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 199 -SKTELTPEERAQKI--AKAMRKQSSEV---KEKWESLNAVTSNWQKQVDKALEKLRDLQGAMDDLDADMKEAESvrngw 272
Cdd:PRK02224  484 lEDLEEEVEEVEERLerAEDLVEAEDRIerlEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKRE----- 558

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769047537 273 kpVGDLLIDSLQDHIEKIMAFREEIAPINFKVKTVNDLSSQLSPLDlhpslKMSRQLDDLNMRWKLLQVSVD---DRLKQ 349
Cdd:PRK02224  559 --AAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA-----DAEDEIERLREKREALAELNDerrERLAE 631


                  ....*..
gi 1769047537 350 LQEAHRD 356
Cdd:PRK02224  632 KRERKRE 638
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
 624-653 9.76e-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: 9.76e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1769047537 624 KCNICKECPIVGFRYRSLKHFNYDVCQSCF 653
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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