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Conserved domains on  [gi|2004852585|ref|NP_001380730|]
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dystrobrevin beta [Rattus norvegicus]

Protein Classification

EFh_DTN and ZZ_dystrophin domain-containing protein( domain architecture ID 11610980)

EFh_DTN and ZZ_dystrophin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 54-214 6.37e-111

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: 328.81  E-value: 6.37e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  54 DIWNMIEAFRDNGLNTLDHATEISVSRLETVISSIYYQLNKRLPSTHQINVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16244     1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTM 213
Cdd:cd16244    81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                  .
gi 2004852585 214 M 214
Cdd:cd16244   161 M 161
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 241-288 6.44e-25

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: 97.43  E-value: 6.44e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2004852585 241 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKE 288
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKE 48
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
434-521 4.15e-06

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 434 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 512
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                  ....*....
gi 2004852585 513 LMKLLKAQA 521
Cdd:COG4717   232 LENELEAAA 240
 
Name Accession Description Interval E-value
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 54-214 6.37e-111

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: 328.81  E-value: 6.37e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  54 DIWNMIEAFRDNGLNTLDHATEISVSRLETVISSIYYQLNKRLPSTHQINVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16244     1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTM 213
Cdd:cd16244    81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                  .
gi 2004852585 214 M 214
Cdd:cd16244   161 M 161
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 16-140 7.27e-63

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: 203.15  E-value: 7.27e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  16 RQLFIEMraQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHATEISVSRLETVISSIYYQLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2004852585  96 LPSTHQINVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATMC 140
Cdd:pfam09068  79 KPTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 241-288 6.44e-25

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: 97.43  E-value: 6.44e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2004852585 241 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKE 288
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKE 48
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 237-281 3.18e-16

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: 72.47  E-value: 3.18e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2004852585  237 VFHPVECSYCHCEsMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHS 281
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 239-280 3.54e-07

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: 47.09  E-value: 3.54e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2004852585 239 HPVECSYCHCESMMGFRYRCQQCHNYQLCQNCFwRGHAGGPH 280
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF-QTHKGGNH 43
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
434-521 4.15e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 434 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 512
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                  ....*....
gi 2004852585 513 LMKLLKAQA 521
Cdd:COG4717   232 LENELEAAA 240
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 440-510 9.37e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.06  E-value: 9.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004852585 440 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 510
Cdd:PRK05431   30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 433-504 3.81e-04

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 41.92  E-value: 3.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2004852585 433 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRR 504
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 405-541 1.82e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.90  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 405 IARYAARLAAEAGNMTRPPTDASFNFDANKQQRQliaELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRL 484
Cdd:pfam09787  77 LQELEAQQQEEAESSREQLQELEEQLATERSARR---EAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRN 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 485 LRQRK-------DELEQRMSALQES--------------RRELMVQLEGLMKLLK-AQATGSPHTS------PTHGGGRS 536
Cdd:pfam09787 154 QLTSKsqssssqSELENRLHQLTETliqkqtmlealsteKNSLVLQLERMEQQIKeLQGEGSNGTSinmegiSDGEGTRL 233


                  ....*
gi 2004852585 537 MPMPV 541
Cdd:pfam09787 234 RNVPG 238
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 478-513 6.88e-03

Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 37.08  E-value: 6.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2004852585 478 LLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 513
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRAKETL 40
 
Name Accession Description Interval E-value
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 54-214 6.37e-111

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: 328.81  E-value: 6.37e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  54 DIWNMIEAFRDNGLNTLDHATEISVSRLETVISSIYYQLNKRLPSTHQINVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16244     1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTM 213
Cdd:cd16244    81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                  .
gi 2004852585 214 M 214
Cdd:cd16244   161 M 161
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
 54-214 1.99e-107

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: 320.05  E-value: 1.99e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  54 DIWNMIEAFRDNGLNTLDHATEISVSRLETVISSIYYQLNKRLPSTHQINVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16250     1 DIWNMIEAFRDNGLNTLDHSTEISVSRLETIISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGHGKLTVFSVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTM 213
Cdd:cd16250    81 AMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHSVRTCFPQQKKIMLNMFLDTM 160


                  .
gi 2004852585 214 M 214
Cdd:cd16250   161 M 161
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
 54-214 3.91e-94

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: 285.64  E-value: 3.91e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  54 DIWNMIEAFRDNGLNTLDHATEISVSRLETVISSIYYQLNKRLPSTHQINVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16249     1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTM 213
Cdd:cd16249    81 MALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 160


                  .
gi 2004852585 214 M 214
Cdd:cd16249   161 M 161
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 16-140 7.27e-63

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: 203.15  E-value: 7.27e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  16 RQLFIEMraQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHATEISVSRLETVISSIYYQLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2004852585  96 LPSTHQINVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATMC 140
Cdd:pfam09068  79 KPTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 54-214 6.38e-52

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: 175.54  E-value: 6.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  54 DIWNMIEAFRDNGLNTlDHATEISVSRLETVISSIYYQLNKRLPstHQINVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd15901     1 DLSTVLSVFDRHGLSG-SQDSVLDCEELETILTELYIKLNKRRP--DLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFG--YTEHAVRTCFPQQKKIM---LNM 208
Cdd:cd15901    78 IALITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGghNVEAAVESCFQLARSRVgvsEDT 157


                  ....*.
gi 2004852585 209 FLDTMM 214
Cdd:cd15901   158 FLSWLL 163
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 144-232 8.85e-44

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: 150.91  E-value: 8.85e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 144 MLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQ---QKKIMLNMFLDTMMADppPQ 220
Cdd:pfam09069   1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGGIEPSVRSCFEQvggKPKITLNHFLDWLMSE--PQ 78

                          90
                  ....*....|..
gi 2004852585 221 CLVWLPLMHRLA 232
Cdd:pfam09069  79 SLVWLPVLHRLA 90
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 241-288 6.44e-25

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: 97.43  E-value: 6.44e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2004852585 241 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKE 288
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKE 48
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
 67-198 7.32e-22

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


Pssm-ID: 320003 [Multi-domain]  Cd Length: 164  Bit Score: 92.74  E-value: 7.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  67 LNTLDHATEISVSRLETVISSIYYQLNKRLPSThqINVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATMCGGKMLD 146
Cdd:cd16245    14 LSNSENNLCLPPDELEAVLHDIYFAAEKLGNFN--IDVDLATELLANLFLNVFDPERKKSISVLELKVFLTLLCGSSLQE 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2004852585 147 KLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFG--YTEHAVRTCF 198
Cdd:cd16245    92 KYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGshLIELAVEQCF 145
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
 54-213 1.81e-21

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: 91.53  E-value: 1.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  54 DIWNMIEAFRDNGLNTLDHATeISVSRLETVISSIYYQLNKRLPstHQINVEQSISLLLNFMIAAYDSEGRGKLTVFSVK 133
Cdd:cd16242     1 SLSTAIEAFDQHGLRAQNDKL-IDVPDMITCLTTIYEALEEEHP--TLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYT--EHAVRTCFPQ---QKKIMLNM 208
Cdd:cd16242    78 VGLVLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSniEPSVRSCFEKageKPEISAAH 157


                  ....*
gi 2004852585 209 FLDTM 213
Cdd:cd16242   158 FLDWL 162
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 237-281 3.18e-16

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: 72.47  E-value: 3.18e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2004852585  237 VFHPVECSYCHCEsMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHS 281
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
EFh_DRP-2 cd16248
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ...
 60-213 1.81e-14

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: 71.37  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  60 EAFRDNGLNTLDHAteISVSRLETVISSIYYQLNKRlpSTHQINVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATM 139
Cdd:cd16248     7 EIFTEHELQMSERV--MDVVEVIHCLTALYERLEEE--RGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIVCL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004852585 140 CGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYT--EHAVRTCF---PQQKKIMLNMFLDTM 213
Cdd:cd16248    83 CNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSnvEPSVRSCFrfaPGKPVIELSQFLEWM 161
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
 60-213 7.52e-14

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: 69.68  E-value: 7.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  60 EAFRDNGLNTLDHATEISvsRLETVISSIYyqlnKRLPSTHQ--INVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLA 137
Cdd:cd16246     7 EALDQHNLKQNDQPMDIL--QIINCLTTIY----DRLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 138 TMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYT--EHAVRTCFP---QQKKIMLNMFLDT 212
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSniEPSVRSCFQfanNKPEIEAALFLDW 160


                  .
gi 2004852585 213 M 213
Cdd:cd16246   161 M 161
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
 60-213 2.24e-12

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: 65.30  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  60 EAFRDNGLNTLDHAteISVSRLETVISSIYYQLNKRlpstHQ--INVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLA 137
Cdd:cd16247     7 SVFKQHKLTQNDQL--LSVPDVINCLTTIYDGLEQK----HKdlVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 138 TMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYT--EHAVRTCFPQ---QKKIMLNMFLDT 212
Cdd:cd16247    81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQHannKPEIDVKQFIDW 160


                  .
gi 2004852585 213 M 213
Cdd:cd16247   161 M 161
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 243-289 2.19e-08

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: 50.67  E-value: 2.19e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2004852585 243 CSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKEL 289
Cdd:cd02345     3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYEL 49
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 243-284 3.08e-08

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 49.98  E-value: 3.08e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2004852585 243 CSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQH 284
Cdd:cd02335     3 CDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
EFh_DYTN cd16243
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ...
 105-198 4.66e-08

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: 52.77  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 105 EQSISLLLnfmiAAYDSEGRGKLTVFSVKAMLATMCGGKMLDKLRYIF----SQMSDSNGLMMFGKLDQFLKEALKLPTA 180
Cdd:cd16243    52 EQTCRLLF----RLYDREQTGFVSLRSVEAALIALSGDTLSAKYRALFqlyeSGQGGSSGSITRSGLRVLLQDLSQIPAV 127

                          90
                  ....*....|....*...
gi 2004852585 181 VFEGPSFGYTEHAVRTCF 198
Cdd:cd16243   128 VQESHVFGNVETAVRSCF 145
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 241-287 3.25e-07

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: 46.96  E-value: 3.25e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2004852585 241 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMK 287
Cdd:cd02338     1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQ 47
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 239-280 3.54e-07

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: 47.09  E-value: 3.54e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2004852585 239 HPVECSYCHCESMMGFRYRCQQCHNYQLCQNCFwRGHAGGPH 280
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF-QTHKGGNH 43
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 246-289 7.97e-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: 45.89  E-value: 7.97e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2004852585 246 CHCESM--MGFRYRCQQCHNYQLCQNCFWRGHagGPHSNQHQMKEL 289
Cdd:cd02249     3 CDGCLKpiVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 241-286 3.07e-06

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: 44.17  E-value: 3.07e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2004852585 241 VECsyCHCES-MMGFRYRCQQCHNYQLCQNCfwrgHAGGPHSNqHQM 286
Cdd:cd02340     1 VIC--DGCQGpIVGVRYKCLVCPDYDLCESC----EAKGVHPE-HAM 40
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
434-521 4.15e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 434 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 512
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                  ....*....
gi 2004852585 513 LMKLLKAQA 521
Cdd:COG4717   232 LENELEAAA 240
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 243-284 3.52e-05

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: 41.29  E-value: 3.52e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2004852585 243 CSYCHCESMMGFRYRCQQCHNYQLCQNCFwrghaggpHSNQH 284
Cdd:cd02339     3 CDTCRKQGIIGIRWKCAECPNYDLCTTCY--------HGDKH 36
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 241-271 3.86e-05

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 41.03  E-value: 3.86e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2004852585 241 VECSYCHCESMMGFRYRCQQCHNYQLCQNCF 271
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCF 31
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 440-510 9.37e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.06  E-value: 9.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004852585 440 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 510
Cdd:PRK05431   30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
431-519 2.79e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 431 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNptllAELRLLRQRKDELEQRMSALQESRRELMVQL 510
Cdd:COG4372    56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----EELESLQEEAEELQEELEELQKERQDLEQQR 131


                  ....*....
gi 2004852585 511 EGLMKLLKA 519
Cdd:COG4372   132 KQLEAQIAE 140
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 248-286 3.42e-04

Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239083  Cd Length: 48  Bit Score: 38.45  E-value: 3.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2004852585 248 CESMMGF-RYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQM 286
Cdd:cd02343     6 CDEIAPWhRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
410-515 3.60e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 410 ARLAAEAGNMTRP----PTDasfNFDANKQQRQLIAELENKNREILQEIQRL-RLEHEQAsqptpEKAQQNPTLLAELRL 484
Cdd:COG4717    49 ERLEKEADELFKPqgrkPEL---NLKELKELEEELKEAEEKEEEYAELQEELeELEEELE-----ELEAELEELREELEK 120

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2004852585 485 LRQRKD--ELEQRMSALQESRRELMVQLEGLMK 515
Cdd:COG4717   121 LEKLLQllPLYQELEALEAELAELPERLEELEE 153
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 433-504 3.81e-04

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 41.92  E-value: 3.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2004852585 433 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRR 504
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 396-521 4.25e-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: 43.52  E-value: 4.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  396 SRLDEEHRliaRYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 475
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2004852585  476 PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL---MKLLKAQA 521
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrkrLSELKAKL 926
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 434-513 4.48e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 434 KQQRQLIAELENKNREILQEIQRLRLEHEQASqptpEKAQQnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 513
Cdd:COG1196   249 EELEAELEELEAELAELEAELEELRLELEELE----LELEE---AQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
434-515 7.82e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 7.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 513
Cdd:COG4372    97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176


                  ..
gi 2004852585 514 MK 515
Cdd:COG4372   177 SE 178
PRK12704 PRK12704
phosphodiesterase; Provisional
 431-518 1.12e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 431 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQES 502
Cdd:PRK12704   35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                          90
                  ....*....|....*.
gi 2004852585 503 RRELMVQLEGLMKLLK 518
Cdd:PRK12704  109 EEELEKKEKELEQKQQ 124
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 436-520 1.14e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 436 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 515
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97


                  ....*
gi 2004852585 516 LLKAQ 520
Cdd:COG4942    98 ELEAQ 102
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 405-541 1.82e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.90  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 405 IARYAARLAAEAGNMTRPPTDASFNFDANKQQRQliaELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRL 484
Cdd:pfam09787  77 LQELEAQQQEEAESSREQLQELEEQLATERSARR---EAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRN 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 485 LRQRK-------DELEQRMSALQES--------------RRELMVQLEGLMKLLK-AQATGSPHTS------PTHGGGRS 536
Cdd:pfam09787 154 QLTSKsqssssqSELENRLHQLTETliqkqtmlealsteKNSLVLQLERMEQQIKeLQGEGSNGTSinmegiSDGEGTRL 233


                  ....*
gi 2004852585 537 MPMPV 541
Cdd:pfam09787 234 RNVPG 238
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
440-520 1.89e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.66  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 440 IAELENKNREILQEIQRLRLE----HEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 512
Cdd:COG1340    10 LEELEEKIEELREEIEELKEKrdelNEELKELAEKRDELNaqvKELREEAQELREKRDELNEKVKELKEERDELNEKLNE 89


                  ....*...
gi 2004852585 513 LMKLLKAQ 520
Cdd:COG1340    90 LREELDEL 97
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 434-520 2.89e-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: 40.13  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQptpekaqqnptllaELRLLRQRKDELEQRMSALQESRRELMVQLEGL 513
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALAR--------------RIRALEQELAALEAELAELEKEIAELRAELEAQ 102


                  ....*..
gi 2004852585 514 MKLLKAQ 520
Cdd:COG4942   103 KEELAEL 109
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 241-286 2.90e-03

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 35.87  E-value: 2.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2004852585 241 VECSYCHCESMMGFRYRCQQCHN--YQLCQNCFwrgHAGGPHSNQHQM 286
Cdd:cd02341     1 FKCDSCGIEPIPGTRYHCSECDDgdFDLCQDCV---VKGESHQEDHWL 45
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
431-512 3.66e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 3.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  431 DANKQQRQL--IAELENKNREILQEIQRLR-----LEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESR 503
Cdd:COG4913    246 DAREQIELLepIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325


                   ....*....
gi 2004852585  504 RELMVQLEG 512
Cdd:COG4913    326 DELEAQIRG 334
PRK12704 PRK12704
phosphodiesterase; Provisional
 430-521 3.89e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 430 FDANKQQRQLIAELENKNREILQEIQRL---------RLEHEQASQptpEKAQQNptLLAELRLLRQRKDELEQRMSALQ 500
Cdd:PRK12704   60 LEAKEEIHKLRNEFEKELRERRNELQKLekrllqkeeNLDRKLELL---EKREEE--LEKKEKELEQKQQELEKKEEELE 134

                          90       100
                  ....*....|....*....|.
gi 2004852585 501 ESRRELMVQLEGLMKLLKAQA 521
Cdd:PRK12704  135 ELIEEQLQELERISGLTAEEA 155
mukB PRK04863
chromosome partition protein MukB;
434-513 4.17e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 4.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  434 KQQRQLIAELENKNREILQEIQRLrleHEQASQ-----------PTPEkaqqnptllAELRLLRQRKDELEQRMSALQES 502
Cdd:PRK04863   792 RAEREELAERYATLSFDVQKLQRL---HQAFSRfigshlavafeADPE---------AELRQLNRRRVELERALADHESQ 859

                           90
                   ....*....|.
gi 2004852585  503 RRELMVQLEGL 513
Cdd:PRK04863   860 EQQQRSQLEQA 870
DASH_Spc19 pfam08287
Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle ...
 433-499 4.48e-03

Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle pole body and is important for spindle and kinetochore integrity during cell division.


Pssm-ID: 429900 [Multi-domain]  Cd Length: 148  Bit Score: 38.00  E-value: 4.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004852585 433 NKQQRQLiAELENKNreilqEIQRLRLEH------------EQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSAL 499
Cdd:pfam08287  76 EKLERRE-ETLKAKL-----ELNEGRLSNaessardeegsqESDEEVNSSEGDATNEELERLRALRQKKERLKYSLERL 148
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 358-521 5.21e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 5.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  358 TKRLQYGQ------------DMPNLLADEHA-LIASYVARLQHCTRvldspSRLDEEHRL-IARYAARLAAEAGNMTR-- 421
Cdd:COG3096    410 TRAIQYQQavqalekaralcGLPDLTPENAEdYLAAFRAKEQQATE-----EVLELEQKLsVADAARRQFEKAYELVCki 484

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  422 -PPTDASFNFDANKQQ-----------------RQLIAELENKNREiLQEIQRLRLEHEQASQPTPEKAQQNPTLLAELR 483
Cdd:COG3096    485 aGEVERSQAWQTARELlrryrsqqalaqrlqqlRAQLAELEQRLRQ-QQNAERLLEEFCQRIGQQLDAAEELEELLAELE 563

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2004852585  484 llrQRKDELEQRMSALQESRREL---MVQLEGLMKLLKAQA 521
Cdd:COG3096    564 ---AQLEELEEQAAEAVEQRSELrqqLEQLRARIKELAARA 601
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
376-515 5.93e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 376 ALIASYVARLQHCTRVLDSPSRLDEEHRLIARYAAR--LAAEAGnmTRPPTDASFNFDANKQQRQLIAELENKNREILQE 453
Cdd:COG4717   337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIaaLLAEAG--VEDEEELRAALEQAEEYQELKEELEELEEQLEEL 414

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2004852585 454 iqrLRLEHEQASQPTPEkaqqnpTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 515
Cdd:COG4717   415 ---LGELEELLEALDEE------ELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 478-513 6.88e-03

Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 37.08  E-value: 6.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2004852585 478 LLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 513
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRAKETL 40
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 438-506 7.07e-03

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 37.59  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 438 QLIAELEN------KNREILQEIQRLRLEHEQ-ASQPTPEKAQQnptLLAELRLL------RQRKDELEQRMSALQESRR 504
Cdd:pfam09744  30 KVVNVLELleslasRNQEHNVELEELREDNEQlETQYEREKALR---KRAEEELEeiedqwEQETKDLLSQVESLEEENR 106


                  ..
gi 2004852585 505 EL 506
Cdd:pfam09744 107 RL 108
Bbox1 cd19757
B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of ...
 256-289 7.18e-03

B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain, in functionally unrelated proteins, most likely mediating protein-protein interactions. Based on different consensus sequences and the spacing of the 7-8 zinc-binding residues, the B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). This family corresponds to the type 1 B-box (Bbox1).


Pssm-ID: 380815 [Multi-domain]  Cd Length: 44  Bit Score: 34.78  E-value: 7.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2004852585 256 YRCQQCHNYqLCQNCFWRGHAGGPHSNQHQMKEL 289
Cdd:cd19757    12 VYCLECEEF-LCDDCSDAIHRRGKLTRSHKLVPL 44
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 431-521 7.51e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 431 DANKQQRQLIAELEnknrEILQEIQRLRLEHEQASQptpEKAQqnptLLAELRLLRQRKDELEQRMSALQESRRELMVQL 510
Cdd:COG1196   285 EAQAEEYELLAELA----RLEQDIARLEERRRELEE---RLEE----LEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90
                  ....*....|.
gi 2004852585 511 EGLMKLLKAQA 521
Cdd:COG1196   354 EEAEAELAEAE 364
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 440-514 7.68e-03

Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.


Pssm-ID: 426757 [Multi-domain]  Cd Length: 108  Bit Score: 36.41  E-value: 7.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2004852585 440 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPtllaELRLLRQRKDELEQRMSALQESRRELMVQLEGLM 514
Cdd:pfam02403  31 LLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE----DADALIAEVKELKDELKALEAELKELEAELDKLL 101
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 377-542 7.95e-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: 38.98  E-value: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 377 LIASYVARLQHCTRVL---DSPSRLDEEHRLIARYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQE 453
Cdd:COG4942   110 LRALYRLGRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585 454 IQRLRLEHEQASQptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRElmvqleglmkllkaQATGSPHTSPTHGG 533
Cdd:COG4942   190 LEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAA--------------AAERTPAAGFAALK 252


                  ....*....
gi 2004852585 534 GRsMPMPVR 542
Cdd:COG4942   253 GK-LPWPVS 260
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
431-514 8.09e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  431 DANKQQRQL---IAELENKNREILQEIQRLRLEHEQAsqptPEKAQQNPTLLAELRLLRQRKDELEQRMS--------AL 499
Cdd:COG4913    703 ELEEELDELkgeIGRLEKELEQAEEELDELQDRLEAA----EDLARLELRALLEERFAAALGDAVERELRenleeridAL 778

                           90
                   ....*....|....*
gi 2004852585  500 QESRRELMVQLEGLM 514
Cdd:COG4913    779 RARLNRAEEELERAM 793
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 371-513 8.28e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 8.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  371 LADEHALIASYVARLQHCTRVLDSPSR-LDEEHRLIARYAARLAAEAGNMtrpptdASFNFDANKQQRQLiAELENKNRE 449
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERrLEDLEEQIEELSEDIESLAAEI------EELEELIEELESEL-EALLNERAS 884

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004852585  450 ILQEIQRLRLEHEQASqptpekaqqnptllAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 513
Cdd:TIGR02168  885 LEEALALLRSELEELS--------------EELRELESKRSELRRELEELREKLAQLELRLEGL 934
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
434-513 8.51e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 8.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004852585  434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLL-AELRLLRQRKDELEQRMSALQESRRELMVQLEG 512
Cdd:COG4913    248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLeAELEELRAELARLEAELERLEARLDALREELDE 327


                   .
gi 2004852585  513 L 513
Cdd:COG4913    328 L 328
 
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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