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Conserved domains on  [gi|568977480|ref|XP_006515023|]
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dystrobrevin beta isoform X6 [Mus musculus]

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 4.11e-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: 4.11e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  54 DIWNMIEAFRDNGLNTLDHSTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSVK 133
Cdd:cd16244    1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTM 213
Cdd:cd16244   81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                 .
gi 568977480 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 ...
 241-289 9.04e-26

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: 99.74  E-value: 9.04e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568977480 241 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEH 289
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
434-528 1.55e-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: 50.92  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 434 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 512
Cdd:COG4717  152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

                         90
                 ....*....|....*..
gi 568977480 513 L-MKLLKEEEQKQAAQA 528
Cdd:COG4717  232 LeNELEAAALEERLKEA 248
 
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 4.11e-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: 4.11e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  54 DIWNMIEAFRDNGLNTLDHSTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSVK 133
Cdd:cd16244    1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTM 213
Cdd:cd16244   81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                 .
gi 568977480 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 2.54e-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: 203.92  E-value: 2.54e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480   16 RQLFIEMraQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHSTEISVSRLETVISSIYYQLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568977480   96 LPSTHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSVKAMLATMC 140
Cdd:pfam09068  79 KPTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 241-289 9.04e-26

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: 99.74  E-value: 9.04e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568977480 241 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEH 289
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 237-281 1.82e-15

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 70.55  E-value: 1.82e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568977480   237 VFHPVECSYCHCEsMMGFRYRCQQCHNYQLCQNCFWRGHASGAHS 281
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 239-271 1.23e-06

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: 45.55  E-value: 1.23e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568977480  239 HPVECSYCHCESMMGFRYRCQQCHNYQLCQNCF 271
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF 35
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
434-528 1.55e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 434 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 512
Cdd:COG4717  152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

                         90
                 ....*....|....*..
gi 568977480 513 L-MKLLKEEEQKQAAQA 528
Cdd:COG4717  232 LeNELEAAALEERLKEA 248
PRK12704 PRK12704
phosphodiesterase; Provisional
 431-525 3.21e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 431 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPMLLAELRLLRQRKDELEQRMSALQES 502
Cdd:PRK12704  35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                         90       100
                 ....*....|....*....|...
gi 568977480 503 RRELMVQLEGLMKLLKEEEQKQA 525
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEE 131
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 374-531 6.57e-05

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: 46.20  E-value: 6.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480   374 EHALIASYVARLQhctrvlDSPSRLDEEHRLIARYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQE 453
Cdd:TIGR02168  223 RELELALLVLRLE------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568977480   454 IQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQATGS 531
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 478-521 3.10e-04

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: 40.93  E-value: 3.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568977480 478 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEGLMKLLKEEE 521
Cdd:cd23160    5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKLKEGTE 51
Caldesmon pfam02029
Caldesmon;
465-527 1.32e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568977480  465 SQPTPEKAQQNPMLLAELRL--LRQRKDELE-QRMSALQESRRELMVQLEGLM-------KLLKEEEQKQAAQ 527
Cdd:pfam02029 231 SQSQEREEEAEVFLEAEQKLeeLRRRRQEKEsEEFEKLRQKQQEAELELEELKkkreerrKLLEEEEQRRKQE 303
 
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 4.11e-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: 4.11e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  54 DIWNMIEAFRDNGLNTLDHSTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSVK 133
Cdd:cd16244    1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTM 213
Cdd:cd16244   81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                 .
gi 568977480 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 1.07e-108

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: 322.75  E-value: 1.07e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  54 DIWNMIEAFRDNGLNTLDHSTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSVK 133
Cdd:cd16250    1 DIWNMIEAFRDNGLNTLDHSTEISVSRLETIISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGHGKLTVFSVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTM 213
Cdd:cd16250   81 AMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHSVRTCFPQQKKIMLNMFLDTM 160


                 .
gi 568977480 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 8.04e-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: 284.48  E-value: 8.04e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  54 DIWNMIEAFRDNGLNTLDHSTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSVK 133
Cdd:cd16249    1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTM 213
Cdd:cd16249   81 MALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 160


                 .
gi 568977480 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 2.54e-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: 203.92  E-value: 2.54e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480   16 RQLFIEMraQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHSTEISVSRLETVISSIYYQLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568977480   96 LPSTHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSVKAMLATMC 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 1.16e-51

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: 174.38  E-value: 1.16e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  54 DIWNMIEAFRDNGLNTlDHSTEISVSRLETVISSIYYQLNKRLPstHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSVK 133
Cdd:cd15901    1 DLSTVLSVFDRHGLSG-SQDSVLDCEELETILTELYIKLNKRRP--DLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 134 AMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFG--YTEHAVRTCFPQQKKIM---LNM 208
Cdd:cd15901   78 IALITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGghNVEAAVESCFQLARSRVgvsEDT 157


                 ....*.
gi 568977480 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 1.81e-43

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: 150.14  E-value: 1.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  144 MLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQ---QKKIMLNMFLDTMMADppPQ 220
Cdd:pfam09069   1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGGIEPSVRSCFEQvggKPKITLNHFLDWLMSE--PQ 78

                          90
                  ....*....|..
gi 568977480  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 ...
 241-289 9.04e-26

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: 99.74  E-value: 9.04e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568977480 241 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEH 289
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
 67-198 3.09e-21

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: 90.82  E-value: 3.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  67 LNTLDHSTEISVSRLETVISSIYYQLNKRLPSThqISVEQSISLLLNFMVAAYDSEGRGKLTVFSVKAMLATMCGGKMLD 146
Cdd:cd16245   14 LSNSENNLCLPPDELEAVLHDIYFAAEKLGNFN--IDVDLATELLANLFLNVFDPERKKSISVLELKVFLTLLCGSSLQE 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568977480 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 5.25e-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: 89.99  E-value: 5.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  54 DIWNMIEAFRDNGLNtlDHSTE-ISVSRLETVISSIYYQLNKRLPstHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSV 132
Cdd:cd16242    1 SLSTAIEAFDQHGLR--AQNDKlIDVPDMITCLTTIYEALEEEHP--TLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 133 KAMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYT--EHAVRTCFPQ---QKKIMLN 207
Cdd:cd16242   77 KVGLVLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSniEPSVRSCFEKageKPEISAA 156


                 ....*.
gi 568977480 208 MFLDTM 213
Cdd:cd16242  157 HFLDWL 162
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 237-281 1.82e-15

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 70.55  E-value: 1.82e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568977480   237 VFHPVECSYCHCEsMMGFRYRCQQCHNYQLCQNCFWRGHASGAHS 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 5.86e-13

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: 67.13  E-value: 5.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  60 EAFRDNGLNTLDHSteISVSRLETVISSIYYQLNKRlpSTHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSVKAMLATM 139
Cdd:cd16248    7 EIFTEHELQMSERV--MDVVEVIHCLTALYERLEEE--RGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIVCL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568977480 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 6.15e-13

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: 66.98  E-value: 6.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  60 EAFRDNGLNTLDHSTEISvsRLETVISSIYyqlnKRLPSTHQ--ISVEQSISLLLNFMVAAYDSEGRGKLTVFSVKAMLA 137
Cdd:cd16246    7 EALDQHNLKQNDQPMDIL--QIINCLTTIY----DRLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 138 TMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYT--EHAVRTCFP---QQKKIMLNMFLDT 212
Cdd:cd16246   81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSniEPSVRSCFQfanNKPEIEAALFLDW 160


                 .
gi 568977480 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 2.21e-11

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: 62.22  E-value: 2.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  60 EAFRDNGLNtlDHSTEISVSRLETVISSIYYQLNKRlpstHQ--ISVEQSISLLLNFMVAAYDSEGRGKLTVFSVKAMLA 137
Cdd:cd16247    7 SVFKQHKLT--QNDQLLSVPDVINCLTTIYDGLEQK----HKdlVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 138 TMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYT--EHAVRTCFPQ---QKKIMLNMFLDT 212
Cdd:cd16247   81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQHannKPEIDVKQFIDW 160


                 .
gi 568977480 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 ...
 243-288 3.03e-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: 49.90  E-value: 3.03e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568977480 243 CSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKE 288
Cdd:cd02345    3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 243-284 3.75e-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: 49.60  E-value: 3.75e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568977480 243 CSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQH 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 6.11e-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: 52.39  E-value: 6.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 105 EQSISLLLnfmvAAYDSEGRGKLTVFSVKAMLATMCGGKMLDKLRYIF----SQMSDSNGLMMFGKLDQFLKEALKLPTA 180
Cdd:cd16243   52 EQTCRLLF----RLYDREQTGFVSLRSVEAALIALSGDTLSAKYRALFqlyeSGQGGSSGSITRSGLRVLLQDLSQIPAV 127

                         90
                 ....*....|....*...
gi 568977480 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 6.20e-08

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: 49.27  E-value: 6.20e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568977480 241 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMK 287
Cdd:cd02338    1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQ 47
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 246-289 9.80e-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: 45.50  E-value: 9.80e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568977480 246 CHCESM--MGFRYRCQQCHNYQLCQNCFWRGHasGAHSNQHQMKEH 289
Cdd:cd02249    3 CDGCLKpiVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 239-271 1.23e-06

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: 45.55  E-value: 1.23e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568977480  239 HPVECSYCHCESMMGFRYRCQQCHNYQLCQNCF 271
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF 35
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
434-528 1.55e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 434 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 512
Cdd:COG4717  152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

                         90
                 ....*....|....*..
gi 568977480 513 L-MKLLKEEEQKQAAQA 528
Cdd:COG4717  232 LeNELEAAALEERLKEA 248
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 241-286 6.34e-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: 43.40  E-value: 6.34e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568977480 241 VECsyCHCES-MMGFRYRCQQCHNYQLCQNCfwrgHASGAHSNqHQM 286
Cdd:cd02340    1 VIC--DGCQGpIVGVRYKCLVCPDYDLCESC----EAKGVHPE-HAM 40
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 434-529 6.89e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 6.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 434 KQQRQLIAELENKNREILQEIQRLRLEHEQASqptpEKAQQnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 513
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELE----LELEE---AQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                         90
                 ....*....|....*.
gi 568977480 514 MKLLKEEEQKQAAQAT 529
Cdd:COG1196  322 EEELAELEEELEELEE 337
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 243-289 1.84e-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: 42.06  E-value: 1.84e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568977480 243 CSYCHCESMMGFRYRCQQCHNYQLCQNCFwrghasgaHSNQHQMkEH 289
Cdd:cd02339    3 CDTCRKQGIIGIRWKCAECPNYDLCTTCY--------HGDKHDL-EH 40
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
431-527 2.42e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 431 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNpmllAELRLLRQRKDELEQRMSALQESRRELMVQL 510
Cdd:COG4372   56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----EELESLQEEAEELQEELEELQKERQDLEQQR 131

                         90
                 ....*....|....*..
gi 568977480 511 EGLMKLLKEEEQKQAAQ 527
Cdd:COG4372  132 KQLEAQIAELQSEIAER 148
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 241-281 3.17e-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: 41.42  E-value: 3.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568977480 241 VECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHS 281
Cdd:cd02344    1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHT 41
PRK12704 PRK12704
phosphodiesterase; Provisional
 431-525 3.21e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 431 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPMLLAELRLLRQRKDELEQRMSALQES 502
Cdd:PRK12704  35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                         90       100
                 ....*....|....*....|...
gi 568977480 503 RRELMVQLEGLMKLLKEEEQKQA 525
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEE 131
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
410-528 5.84e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 5.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 410 ARLAAEAGNMTRP----PTDasfNFDANKQQRQLIAELENKNREILQEIQRL-RLEHEQAsqptpEKAQQNPMLLAELRL 484
Cdd:COG4717   49 ERLEKEADELFKPqgrkPEL---NLKELKELEEELKEAEEKEEEYAELQEELeELEEELE-----ELEAELEELREELEK 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568977480 485 LRQRKD--ELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQA 528
Cdd:COG4717  121 LEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 374-531 6.57e-05

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: 46.20  E-value: 6.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480   374 EHALIASYVARLQhctrvlDSPSRLDEEHRLIARYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQE 453
Cdd:TIGR02168  223 RELELALLVLRLE------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568977480   454 IQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQATGS 531
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 248-286 1.18e-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: 39.99  E-value: 1.18e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568977480 248 CESMMGF-RYRCQQCHNYQLCQNCFWRGHASGAHSNQHQM 286
Cdd:cd02343    6 CDEIAPWhRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 440-510 1.34e-04

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 44.67  E-value: 1.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568977480 440 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PMLLAELRLLRQRKDELEQRMSALQESRRELMVQL 510
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 431-528 1.49e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 431 DANKQQRQLIAELEnknrEILQEIQRLRLEHEQASQptpEKAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQL 510
Cdd:COG1196  285 EAQAEEYELLAELA----RLEQDIARLEERRRELEE---RLEE----LEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         90
                 ....*....|....*...
gi 568977480 511 EGLMKLLKEEEQKQAAQA 528
Cdd:COG1196  354 EEAEAELAEAEEALLEAE 371
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 436-529 2.30e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 436 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 515
Cdd:COG1196  307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                         90
                 ....*....|....
gi 568977480 516 LLKEEEQKQAAQAT 529
Cdd:COG1196  387 ELLEALRAAAELAA 400
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 478-521 3.10e-04

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: 40.93  E-value: 3.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568977480 478 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEGLMKLLKEEE 521
Cdd:cd23160    5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKLKEGTE 51
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 396-527 3.59e-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: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480   396 SRLDEEHRliaRYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 475
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568977480   476 PMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKE-EEQKQAAQ 527
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSElKAKLEALE 930
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 436-527 5.13e-04

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: 42.44  E-value: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 436 QRQLIAELENKNREILQEIQRLRLEHEQASQptpEKAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 515
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKK---EEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                         90
                 ....*....|..
gi 568977480 516 LLKEEEQKQAAQ 527
Cdd:COG4942   91 EIAELRAELEAQ 102
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
437-534 5.26e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.21  E-value: 5.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 437 RQLIAELENKNREILQEIQRLRLEHEQASQPTPEkaqqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKL 516
Cdd:COG1340   21 REEIEELKEKRDELNEELKELAEKRDELNAQVKE-------LREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93

                         90       100
                 ....*....|....*....|
gi 568977480 517 LKE--EEQKQAAQATGSPHT 534
Cdd:COG1340   94 LDElrKELAELNKAGGSIDK 113
PRK12704 PRK12704
phosphodiesterase; Provisional
 430-520 7.92e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 7.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 430 FDANKQQRQLIAELENKNREILQEIQRL---------RLEHEQASQptpEKAQQNpmLLAELRLLRQRKDELEQRMSALQ 500
Cdd:PRK12704  60 LEAKEEIHKLRNEFEKELRERRNELQKLekrllqkeeNLDRKLELL---EKREEE--LEKKEKELEQKQQELEKKEEELE 134

                         90       100
                 ....*....|....*....|
gi 568977480 501 ESRRELMVQLEGLMKLLKEE 520
Cdd:PRK12704 135 ELIEEQLQELERISGLTAEE 154
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
434-528 1.10e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 513
Cdd:COG4372   97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176

                         90
                 ....*....|....*
gi 568977480 514 MKLLKEEEQKQAAQA 528
Cdd:COG4372  177 SEAEAEQALDELLKE 191
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 431-528 1.19e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 431 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQL 510
Cdd:COG1196  278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         90
                 ....*....|....*...
gi 568977480 511 EglmkLLKEEEQKQAAQA 528
Cdd:COG1196  354 E----EAEAELAEAEEAL 367
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 431-585 1.20e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 431 DANKQQRQLIAELENKNREILQEIQRLRLEHEQAsqptpEKAQQNpmllaelrlLRQRKDELEQRMSALQESRRELMVQL 510
Cdd:COG3883  133 DLLEELKADKAELEAKKAELEAKLAELEALKAEL-----EAAKAE---------LEAQQAEQEALLAQLSAEEAAAEAQL 198

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568977480 511 EGLMKLLKEEEQKQAAQATGSPHTSPTHGGGRPMPMPVRSTSAGSTPTHGPQDSLSGVGGDVQEAFAQGEVTPVS 585
Cdd:COG3883  199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
Caldesmon pfam02029
Caldesmon;
465-527 1.32e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568977480  465 SQPTPEKAQQNPMLLAELRL--LRQRKDELE-QRMSALQESRRELMVQLEGLM-------KLLKEEEQKQAAQ 527
Cdd:pfam02029 231 SQSQEREEEAEVFLEAEQKLeeLRRRRQEKEsEEFEKLRQKQQEAELELEELKkkreerrKLLEEEEQRRKQE 303
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 433-504 1.40e-03

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: 40.38  E-value: 1.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568977480  433 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRR 504
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
434-528 1.49e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 434 KQQRQLIAELENKNREILQEIQRLrlEHEQASQPTPEKAQQNPMLLAEL-----RLLRQRKD--ELEQRMSALQESRREL 506
Cdd:COG4717   98 EELEEELEELEAELEELREELEKL--EKLLQLLPLYQELEALEAELAELperleELEERLEElrELEEELEELEAELAEL 175

                         90       100
                 ....*....|....*....|..
gi 568977480 507 MVQLEGLMKLLKEEEQKQAAQA 528
Cdd:COG4717  176 QEELEELLEQLSLATEEELQDL 197
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 434-531 1.85e-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: 40.90  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQptpekaqqnpmllaELRLLRQRKDELEQRMSALQESRRELMVQLEGL 513
Cdd:COG4942   37 AELEKELAALKKEEKALLKQLAALERRIAALAR--------------RIRALEQELAALEAELAELEKEIAELRAELEAQ 102

                         90
                 ....*....|....*...
gi 568977480 514 MKLLKeeEQKQAAQATGS 531
Cdd:COG4942  103 KEELA--ELLRALYRLGR 118
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 433-523 1.86e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  433 NKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 512
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486

                          90
                  ....*....|.
gi 568977480  513 LMKLLKEEEQK 523
Cdd:TIGR04523 487 KQKELKSKEKE 497
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
376-525 2.00e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 376 ALIASYVARLQHCTRVLDSPSRLDEEHRLIARYAAR--LAAEAGnmTRPPTDASFNFDANKQQRQLIAELENKNREILQE 453
Cdd:COG4717  337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIaaLLAEAG--VEDEEELRAALEQAEEYQELKEELEELEEQLEEL 414

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568977480 454 iqrLRLEHEQASQPTPEKaqqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL------MKLLKEEEQKQA 525
Cdd:COG4717  415 ---LGELEELLEALDEEE------LEEELEELEEELEELEEELEELREELAELEAELEQLeedgelAELLQELEELKA 483
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 405-535 2.02e-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: 40.51  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  405 IARYAARLAAEAGNMTRPPTDASFNFDANKQQRQliaELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRL 484
Cdd:pfam09787  77 LQELEAQQQEEAESSREQLQELEEQLATERSARR---EAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRN 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568977480  485 LRQRK-------DELEQRMSALQESRRELMVQLEGL--------MKLLKEEEQKQAAQATGSPHTS 535
Cdd:pfam09787 154 QLTSKsqssssqSELENRLHQLTETLIQKQTMLEALsteknslvLQLERMEQQIKELQGEGSNGTS 219
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 358-528 2.09e-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: 41.09  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  358 TKRLQYSQ------------DMPNLLADEHA-LIASYVARLQHCTRvldspSRLDEEHRL-IARYAARLAAEAGNMTR-- 421
Cdd:COG3096   410 TRAIQYQQavqalekaralcGLPDLTPENAEdYLAAFRAKEQQATE-----EVLELEQKLsVADAARRQFEKAYELVCki 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  422 -PPTDASFNFDANKQQ-----------------RQLIAELENKNREiLQEIQRLRLEHEQASQPTPEKAQQNPMLLAELR 483
Cdd:COG3096   485 aGEVERSQAWQTARELlrryrsqqalaqrlqqlRAQLAELEQRLRQ-QQNAERLLEEFCQRIGQQLDAAEELEELLAELE 563

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568977480  484 llrQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQ----AAQA 528
Cdd:COG3096   564 ---AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlAAQD 609
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
373-533 2.52e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  373 DEHALIASYV------ARLQHCTRVLDspsRLDEEHRLIARYAARLAAEAgnmtrpptdasfnfDANKQQRQLIAELENK 446
Cdd:COG4913   594 DRRRIRSRYVlgfdnrAKLAALEAELA---ELEEELAEAEERLEALEAEL--------------DALQERREALQRLAEY 656

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  447 NREIL------QEIQRLRLEHEQASQPTPEKAQqnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKE- 519
Cdd:COG4913   657 SWDEIdvasaeREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEl 732

                         170
                  ....*....|....
gi 568977480  520 EEQKQAAQATGSPH 533
Cdd:COG4913   733 QDRLEAAEDLARLE 746
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 438-529 2.65e-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: 38.75  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  438 QLIAELEN------KNREILQEIQRLRLEHEQ-ASQPTPEKAQQnpmLLAELRLL------RQRKDELEQRMSALQESRR 504
Cdd:pfam09744  30 KVVNVLELleslasRNQEHNVELEELREDNEQlETQYEREKALR---KRAEEELEeiedqwEQETKDLLSQVESLEEENR 106

                          90       100
                  ....*....|....*....|....*
gi 568977480  505 ELMVQLEGLMKLLKEEEQKQAAQAT 529
Cdd:pfam09744 107 RLEADHVSRLEEKEAELKKEYSKLH 131
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 430-523 2.79e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480   430 FDANKQQ--------RQLIAELENKNREILQEIQRLRLEHEQAS-----QPTPEKAQQNpMLLAELRLLRQRKDELEQRM 496
Cdd:TIGR02169  168 FDRKKEKaleeleevEENIERLDLIIDEKRQQLERLRREREKAEryqalLKEKREYEGY-ELLKEKEALERQKEAIERQL 246

                           90       100
                   ....*....|....*....|....*..
gi 568977480   497 SALQESRRELMVQLEGLMKLLKEEEQK 523
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQL 273
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
434-529 2.87e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  434 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLL--------AELRLLRQRKDELEQRMSALQESRRE 505
Cdd:COG4913   248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLeaeleelrAELARLEAELERLEARLDALREELDE 327

                          90       100
                  ....*....|....*....|....*....
gi 568977480  506 LMVQLEG-----LMKLLKEEEQKQAAQAT 529
Cdd:COG4913   328 LEAQIRGnggdrLEQLEREIERLERELEE 356
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
431-526 3.69e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 431 DANKQQRQLIAELENKNREILQ---EIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELM 507
Cdd:COG4372   42 KLQEELEQLREELEQAREELEQleeELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121

                         90
                 ....*....|....*....
gi 568977480 508 VQLEGLMKLLKEEEQKQAA 526
Cdd:COG4372  122 KERQDLEQQRKQLEAQIAE 140
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
439-523 3.78e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 439 LIAELENKNREILQEIQRLRLEHEQASQPTpEKAQQNPMLLAELRL----LRQRKDELEQRMSALQESRRELMVQLEGLM 514
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEeieeLEKELESLEGSKRKLEEKIRELEERIEELK 272


                 ....*....
gi 568977480 515 KLLKEEEQK 523
Cdd:PRK03918 273 KEIEELEEK 281
DASH_Spc19 pfam08287
Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle ...
 433-499 3.98e-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: 3.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568977480  433 NKQQRQLiAELENKNreilqEIQRLRLEH------------EQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSAL 499
Cdd:pfam08287  76 EKLERRE-ETLKAKL-----ELNEGRLSNaessardeegsqESDEEVNSSEGDATNEELERLRALRQKKERLKYSLERL 148
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 434-528 4.06e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.93  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  434 KQQR--QLIAELENKNREILQEIqRLR---LEHEQASQPTPEKAQQNPMLLAELR--------------LLRQRKDELEQ 494
Cdd:pfam15709 367 QLERaeKMREELELEQQRRFEEI-RLRkqrLEEERQRQEEEERKQRLQLQAAQERarqqqeefrrklqeLQRKKQQEEAE 445

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568977480  495 RMSALQESRRELMVQLEGLMKLL---KEEE------QKQAAQA 528
Cdd:pfam15709 446 RAEAEKQRQKELEMQLAEEQKRLmemAEEErleyqrQKQEAEE 488
mukB PRK04863
chromosome partition protein MukB;
434-519 4.84e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  434 KQQRQLIAELENKNREILQEIQRLrleHEQASQ-----------PTPEkaqqnpmllAELRLLRQRKDELEQRMSALQE- 501
Cdd:PRK04863  792 RAEREELAERYATLSFDVQKLQRL---HQAFSRfigshlavafeADPE---------AELRQLNRRRVELERALADHESq 859

                          90       100
                  ....*....|....*....|
gi 568977480  502 --SRRELMVQLEGLMKLLKE 519
Cdd:PRK04863  860 eqQQRSQLEQAKEGLSALNR 879
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
397-528 6.28e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 397 RLDEEHRLIARYAARLAA--EAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEkAQQ 474
Cdd:COG3206  183 QLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE-LLQ 261

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568977480 475 NPM---LLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQA 528
Cdd:COG3206  262 SPViqqLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL 318
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 408-502 6.44e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 38.82  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480  408 YAARLAAEAGNMTRppTDASFNFDANKQQRQLIAELENKNREILQEIQRL--RLEHEQASQPTPEKAQQNPMLLAELRLL 485
Cdd:pfam03961 131 KAKELGSPAGTKTE--IEVGVDFPELKEKLEELEKELEELEEELEKLKKRlkKLPKKARGQLPPEKREQLEKLLETKNKL 208

                          90
                  ....*....|....*..
gi 568977480  486 RQRKDELEQRMSALQES 502
Cdd:pfam03961 209 SEELEELEEELKELKEE 225
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 435-523 6.96e-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: 39.65  E-value: 6.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480   435 QQRQLIAELENKNREILQEIQRL-----RLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQ 509
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLearleRLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462

                           90
                   ....*....|....
gi 568977480   510 LEGLMKLLKEEEQK 523
Cdd:TIGR02168  463 LEELREELEEAEQA 476
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 435-519 7.31e-03

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 38.01  E-value: 7.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 435 QQRQLIAELENKNREI----------LQEIQRLRLEHEQASQptpekaQQNPMLLAELRLLRQRKDELEQRMSA----LQ 500
Cdd:cd16855   12 ELRQRTQETENDLRNLqqkqesfviqYQESQKIQAQLQQLQQ------QPQNERIELEQQLQQQKEQLEQLLNAkaqeLL 85

                         90
                 ....*....|....*....
gi 568977480 501 ESRRELMVQLEGLMKLLKE 519
Cdd:cd16855   86 QLRMELADKFKKTIQLLSK 104
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 440-514 7.38e-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: 7.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568977480  440 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPmllaELRLLRQRKDELEQRMSALQESRRELMVQLEGLM 514
Cdd:pfam02403  31 LLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE----DADALIAEVKELKDELKALEAELKELEAELDKLL 101
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
437-532 8.63e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 8.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 437 RQLIAELENKNREILQEIQRLRLEHEQASQptpekaqqnpMLLAELRLLRQRKDELEQRMSALQESRRELM-------VQ 509
Cdd:COG3206  294 IALRAQIAALRAQLQQEAQRILASLEAELE----------ALQAREASLQAQLAQLEARLAELPELEAELRrlereveVA 363

                         90       100
                 ....*....|....*....|...
gi 568977480 510 LEGLMKLLKEEEQKQAAQATGSP 532
Cdd:COG3206  364 RELYESLLQRLEEARLAEALTVG 386
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 431-529 9.05e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.98  E-value: 9.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480 431 DANKQQRQLIAELENKNREILQ---EIQRLRLEHEQASQPTpEKAQQNPMLLA---ELRLLRQRKDELEQRMSALQESRR 504
Cdd:COG1579   35 ELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARI-KKYEEQLGNVRnnkEYEALQKEIESLKRRISDLEDEIL 113

                         90       100
                 ....*....|....*....|....*
gi 568977480 505 ELMVQLEGLMKLLKEEEQKQAAQAT 529
Cdd:COG1579  114 ELMERIEELEEELAELEAELAELEA 138
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 450-528 9.09e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 38.33  E-value: 9.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568977480 450 ILQEIQRLrLEHEQASQPTPEKAQQnpmLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEEQKQAAQA 528
Cdd:cd16269  186 ILQADQAL-TEKEKEIEAERAKAEA---AEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERA 260
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 478-529 9.13e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 9.13e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568977480   478 LLAELRLLRQRKDELEQRMSALQESRRELMVQLEglmkLLKEEEQKQAAQAT 529
Cdd:TIGR02169  693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIE----QLEQEEEKLKERLE 740
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 435-528 9.36e-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: 39.18  E-value: 9.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977480   435 QQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQqnpMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLM 514
Cdd:TIGR00618  779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED---ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE 855

                           90
                   ....*....|....
gi 568977480   515 KLLKEEEQKQAAQA 528
Cdd:TIGR00618  856 ECSKQLAQLTQEQA 869
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 241-286 9.38e-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: 34.33  E-value: 9.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568977480 241 VECSYCHCESMMGFRYRCQQCHN--YQLCQNCFwrgHASGAHSNQHQM 286
Cdd:cd02341    1 FKCDSCGIEPIPGTRYHCSECDDgdFDLCQDCV---VKGESHQEDHWL 45
 
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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