NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|984093767|ref|XP_015337931|]
View 

dystrobrevin alpha isoform X25 [Marmota marmota marmota]

Protein Classification

EFh_DTNA and ZZ_dystrophin domain-containing protein( domain architecture ID 11611107)

protein containing domains EFh_DTNA, ZZ_dystrophin, and GBP_C

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
 54-214 3.75e-117

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: 349.20  E-value: 3.75e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  54 DIWNVIEALRENALNNLDPNIELNVARLEAVLSTIFYQLNKRMPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVK 133
Cdd:cd16249    1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 134 MALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 213
Cdd:cd16249   81 MALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 160


                 .
gi 984093767 214 M 214
Cdd:cd16249  161 M 161
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 241-289 1.06e-27

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: 105.52  E-value: 1.06e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 984093767 241 VECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMKEY 289
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
467-546 2.24e-05

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: 47.84  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 467 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 545
Cdd:COG4717  152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                 .
gi 984093767 546 L 546
Cdd:COG4717  232 L 232
 
Name Accession Description Interval E-value
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
 54-214 3.75e-117

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: 349.20  E-value: 3.75e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  54 DIWNVIEALRENALNNLDPNIELNVARLEAVLSTIFYQLNKRMPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVK 133
Cdd:cd16249    1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 134 MALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 213
Cdd:cd16249   81 MALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 160


                 .
gi 984093767 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 1.25e-50

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: 172.34  E-value: 1.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767   16 RQLFAEMraQDLDRIRLSTYRTACKLRFVQKKCNLHLVDIWNVIEALRENALNNLDPNIELNVARLEAVLSTIFYQLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 984093767   96 MPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLC 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 1.06e-27

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: 105.52  E-value: 1.06e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 984093767 241 VECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMKEY 289
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 237-281 4.75e-17

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: 75.17  E-value: 4.75e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 984093767   237 VFHPVECSYCHSEsMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHS 281
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 239-286 1.68e-07

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 48.25  E-value: 1.68e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 984093767  239 HPVECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGshsnqHQM 286
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGN-----HQM 45
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
467-546 2.24e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 467 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 545
Cdd:COG4717  152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                 .
gi 984093767 546 L 546
Cdd:COG4717  232 L 232
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 473-543 1.37e-04

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.06  E-value: 1.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984093767 473 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 543
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 422-555 3.56e-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: 44.29  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767   422 ESSNRLDEEHRLIARYAARLAAESSSSQPTQQRSAPDIsftidANKQQRqlIAELENKNREILQEIQRLRLEHEQASQPT 501
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI-----QELQEQ--RIDLKEQIKSIEKEIENLNGKKEELEEEL 870

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 984093767   502 PEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKTQGA 555
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 421-534 3.14e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 39.98  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  421 LESSNRLDEEHRLIARYAARLAAESSSSQPTQQRsapdisftIDANKQQRQLIAELENKNR---EILQEIQRLRLEHEQA 497
Cdd:pfam12795  88 LQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQ--------LSEARQRLQQIRNRLNGPAppgEPLSEAQRWALQAELA 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 984093767  498 SQPTP----EKAQQNPTLLAEL-----RLLRQRKDELEQRMSALQE 534
Cdd:pfam12795 160 ALKAQidmlEQELLSNNNRQDLlkarrDLLTLRIQRLEQQLQALQE 205
 
Name Accession Description Interval E-value
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
 54-214 3.75e-117

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: 349.20  E-value: 3.75e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  54 DIWNVIEALRENALNNLDPNIELNVARLEAVLSTIFYQLNKRMPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVK 133
Cdd:cd16249    1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 134 MALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 213
Cdd:cd16249   81 MALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 160


                 .
gi 984093767 214 M 214
Cdd:cd16249  161 M 161
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 54-214 3.44e-95

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: 292.22  E-value: 3.44e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  54 DIWNVIEALRENALNNLDPNIELNVARLEAVLSTIFYQLNKRMPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVK 133
Cdd:cd16244    1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 134 MALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 213
Cdd:cd16244   81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                 .
gi 984093767 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 1.05e-75

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: 241.47  E-value: 1.05e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  54 DIWNVIEALRENALNNLDPNIELNVARLEAVLSTIFYQLNKRMPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVK 133
Cdd:cd16250    1 DIWNMIEAFRDNGLNTLDHSTEISVSRLETIISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGHGKLTVFSVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 134 MALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 213
Cdd:cd16250   81 AMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHSVRTCFPQQKKIMLNMFLDTM 160


                 .
gi 984093767 214 M 214
Cdd:cd16250  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 1.25e-50

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: 172.34  E-value: 1.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767   16 RQLFAEMraQDLDRIRLSTYRTACKLRFVQKKCNLHLVDIWNVIEALRENALNNLDPNIELNVARLEAVLSTIFYQLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 984093767   96 MPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLC 140
Cdd:pfam09068  79 KPTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 144-232 4.93e-42

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: 147.45  E-value: 4.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  144 IMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQ---QKKVTLNGFLDTLMSDppPQ 220
Cdd:pfam09069   1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGGIEPSVRSCFEQvggKPKITLNHFLDWLMSE--PQ 78

                          90
                  ....*....|..
gi 984093767  221 CLVWLPLLHRLA 232
Cdd:pfam09069  79 SLVWLPVLHRLA 90
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 54-214 2.47e-32

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: 122.77  E-value: 2.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  54 DIWNVIEALRENALNNLDPNiELNVARLEAVLSTIFYQLNKRMPttHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVK 133
Cdd:cd15901    1 DLSTVLSVFDRHGLSGSQDS-VLDCEELETILTELYIKLNKRRP--DLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 134 MALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFG--YTEQSARSCFSQQKK---VTLNG 208
Cdd:cd15901   78 IALITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGghNVEAAVESCFQLARSrvgVSEDT 157


                 ....*.
gi 984093767 209 FLDTLM 214
Cdd:cd15901  158 FLSWLL 163
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 241-289 1.06e-27

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: 105.52  E-value: 1.06e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 984093767 241 VECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMKEY 289
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 237-281 4.75e-17

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: 75.17  E-value: 4.75e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 984093767   237 VFHPVECSYCHSEsMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHS 281
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
 67-200 7.48e-13

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: 66.94  E-value: 7.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  67 LNNLDPNIELNVARLEAVLSTIFYQLNKRMPTThqIHVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMD 146
Cdd:cd16245   14 LSNSENNLCLPPDELEAVLHDIYFAAEKLGNFN--IDVDLATELLANLFLNVFDPERKKSISVLELKVFLTLLCGSSLQE 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 984093767 147 KLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFG--YTEQSARSCFSQ 200
Cdd:cd16245   92 KYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGshLIELAVEQCFEN 147
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
 120-213 1.89e-11

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: 63.02  E-value: 1.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 120 DPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSC 197
Cdd:cd16242   64 DSGRSGKIRVLSFKVGLVLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSniEPSVRSC 143

                         90
                 ....*....|....*....
gi 984093767 198 FSQ---QKKVTLNGFLDTL 213
Cdd:cd16242  144 FEKageKPEISAAHFLDWL 162
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 243-288 3.65e-09

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: 52.98  E-value: 3.65e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 984093767 243 CSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMKE 288
Cdd:cd02345    3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 241-287 4.91e-09

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: 52.73  E-value: 4.91e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 984093767 241 VECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMK 287
Cdd:cd02338    1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQ 47
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 241-289 2.79e-08

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


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 50.51  E-value: 2.79e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 984093767 241 VECSYCHSESMmGFRYRCQQCHNYQLCQDCFWRGHagGSHSNQHQMKEY 289
Cdd:cd02249    1 YSCDGCLKPIV-GVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 243-284 8.99e-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: 48.83  E-value: 8.99e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 984093767 243 CSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQH 284
Cdd:cd02335    3 CDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 239-286 1.68e-07

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 48.25  E-value: 1.68e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 984093767  239 HPVECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGshsnqHQM 286
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGN-----HQM 45
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
 125-198 4.68e-07

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: 50.42  E-value: 4.68e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 984093767 125 GKISVFAVKMALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCF 198
Cdd:cd16246   68 GRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSniEPSVRSCF 143
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 241-286 1.01e-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: 45.71  E-value: 1.01e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 984093767 241 VECSYCHSEsMMGFRYRCQQCHNYQLCQDCfwrgHAGGSHSNqHQM 286
Cdd:cd02340    1 VICDGCQGP-IVGVRYKCLVCPDYDLCESC----EAKGVHPE-HAM 40
EFh_DYTN cd16243
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ...
 120-200 1.18e-06

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: 48.92  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 120 DPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSM----ISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSAR 195
Cdd:cd16243   63 DREQTGFVSLRSVEAALIALSGDTLSAKYRALFQLyesgQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFGNVETAVR 142


                 ....*
gi 984093767 196 SCFSQ 200
Cdd:cd16243  143 SCFSG 147
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 243-284 1.74e-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: 42.45  E-value: 1.74e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 984093767 243 CSYCHSESMMGFRYRCQQCHNYQLCQDCFwrghaggsHSNQH 284
Cdd:cd02339    3 CDTCRKQGIIGIRWKCAECPNYDLCTTCY--------HGDKH 36
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
467-546 2.24e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 467 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 545
Cdd:COG4717  152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                 .
gi 984093767 546 L 546
Cdd:COG4717  232 L 232
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 241-286 2.25e-05

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: 42.04  E-value: 2.25e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 984093767 241 VECSYCHSESMMGFRYRCQQCHN--YQLCQDCFwrgHAGGSHSNQHQM 286
Cdd:cd02341    1 FKCDSCGIEPIPGTRYHCSECDDgdFDLCQDCV---VKGESHQEDHWL 45
EFh_DRP-2 cd16248
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ...
 116-198 2.74e-05

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: 45.17  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 116 LAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYT--EQS 193
Cdd:cd16248   59 LNVYDSGRNGKIRVLSFKTGIVCLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSnvEPS 138


                 ....*
gi 984093767 194 ARSCF 198
Cdd:cd16248  139 VRSCF 143
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 473-543 1.37e-04

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.06  E-value: 1.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984093767 473 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 543
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 241-281 1.43e-04

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: 39.87  E-value: 1.43e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 984093767 241 VECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHS 281
Cdd:cd02344    1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHT 41
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
 76-211 1.43e-04

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: 42.96  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  76 LNVARLEAVLSTIFYQLNKRmpttHQ--IHVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFS 153
Cdd:cd16247   21 LSVPDVINCLTTIYDGLEQK----HKdlVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLMSLSKGLLEEKYRYLFK 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984093767 154 MISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCFSQ---QKKVTLNGFLD 211
Cdd:cd16247   97 EVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQHannKPEIDVKQFID 159
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 422-555 3.56e-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: 44.29  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767   422 ESSNRLDEEHRLIARYAARLAAESSSSQPTQQRSAPDIsftidANKQQRqlIAELENKNREILQEIQRLRLEHEQASQPT 501
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI-----QELQEQ--RIDLKEQIKSIEKEIENLNGKKEELEEEL 870

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 984093767   502 PEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKTQGA 555
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 255-286 3.98e-04

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


Pssm-ID: 239083  Cd Length: 48  Bit Score: 38.84  E-value: 3.98e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 984093767 255 RYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQM 286
Cdd:cd02343   14 RYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 466-537 1.15e-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: 40.76  E-value: 1.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 984093767  466 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRR 537
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 467-546 1.43e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 467 KQQRQLIAELENKNREILQEIQRLRLEHEQASqptpEKAQQnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 546
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELE----LELEE---AQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
PRK12704 PRK12704
phosphodiesterase; Provisional
 464-552 2.36e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 464 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQES 535
Cdd:PRK12704  35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                         90
                 ....*....|....*..
gi 984093767 536 RRELMVQLEGLMKLLKT 552
Cdd:PRK12704 109 EEELEKKEKELEQKQQE 125
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 421-534 3.14e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 39.98  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  421 LESSNRLDEEHRLIARYAARLAAESSSSQPTQQRsapdisftIDANKQQRQLIAELENKNR---EILQEIQRLRLEHEQA 497
Cdd:pfam12795  88 LQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQ--------LSEARQRLQQIRNRLNGPAppgEPLSEAQRWALQAELA 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 984093767  498 SQPTP----EKAQQNPTLLAEL-----RLLRQRKDELEQRMSALQE 534
Cdd:pfam12795 160 ALKAQidmlEQELLSNNNRQDLlkarrDLLTLRIQRLEQQLQALQE 205
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 397-538 3.56e-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: 40.52  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 397 DRLADehVLIGLYVNMLRNNPSCMLESSNRLDEEHRLiaRYAARLAAESSSSQPTQQRSAPDISFTIDANKQQRQLIAEL 476
Cdd:COG4942  104 EELAE--LLRALYRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 984093767 477 ENKNREILQEIQRLRLEHEQASQptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRE 538
Cdd:COG4942  180 LAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
463-548 4.06e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 463 IDANKQQRQLIAELENKNREILQEIQRL-RLEHEQAsqptpEKAQQNPTLLAELRLLRQRKD--ELEQRMSALQESRREL 539
Cdd:COG4717   70 LKELKELEEELKEAEEKEEEYAELQEELeELEEELE-----ELEAELEELREELEKLEKLLQllPLYQELEALEAELAEL 144


                 ....*....
gi 984093767 540 MVQLEGLMK 548
Cdd:COG4717  145 PERLEELEE 153
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 469-553 4.43e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 469 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 548
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97


                 ....*
gi 984093767 549 LLKTQ 553
Cdd:COG4942   98 ELEAQ 102
Bbox1 cd19757
B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of ...
 243-288 4.52e-03

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


Pssm-ID: 380815 [Multi-domain]  Cd Length: 44  Bit Score: 35.55  E-value: 4.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 984093767 243 CSYCHSESMmgfRYRCQQCHNYqLCQDCFWRGHAGGSHSNQHQMKE 288
Cdd:cd19757    2 CDECEEREA---TVYCLECEEF-LCDDCSDAIHRRGKLTRSHKLVP 43
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 467-546 4.74e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 467 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 546
Cdd:COG1196  256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
464-552 4.95e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 464 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNptllAELRLLRQRKDELEQRMSALQESRRELMVQL 543
Cdd:COG4372   56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----EELESLQEEAEELQEELEELQKERQDLEQQR 131


                 ....*....
gi 984093767 544 EGLMKLLKT 552
Cdd:COG4372  132 KQLEAQIAE 140
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 425-552 5.24e-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: 40.43  E-value: 5.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767   425 NRLDEEHRLIARY---AARLAAESSSSQPTQQRSAPDISFTIDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPT 501
Cdd:TIGR02168  232 LRLEELREELEELqeeLKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 984093767   502 PEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKT 552
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 467-557 5.97e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 5.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 467 KQQRQLIAELENKNREILQEIQRLRLEHEQASqptpEKAQQnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 546
Cdd:COG3883   19 QAKQKELSELQAELEAAQAELDALQAELEELN----EEYNE---LQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91

                         90
                 ....*....|.
gi 984093767 547 MKLLKTQGAGS 557
Cdd:COG3883   92 ARALYRSGGSV 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 422-532 6.67e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767 422 ESSNRLDEEHRLIARYAARLAAESSSSQPTQQRSAPDISFTIDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPT 501
Cdd:COG1196  669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748

                         90       100       110
                 ....*....|....*....|....*....|.
gi 984093767 502 PEKAQQNPTLLAELRLLRQRKDELEQRMSAL 532
Cdd:COG1196  749 EEEALEELPEPPDLEELERELERLEREIEAL 779
mukB PRK04863
chromosome partition protein MukB;
463-546 8.18e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 8.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  463 IDANKQQRQLIAELENKNREILQEIQRLrleHEQASQ-----------PTPEkaqqnptllAELRLLRQRKDELEQRMSA 531
Cdd:PRK04863  788 IEQLRAEREELAERYATLSFDVQKLQRL---HQAFSRfigshlavafeADPE---------AELRQLNRRRVELERALAD 855

                          90
                  ....*....|....*
gi 984093767  532 LQESRRELMVQLEGL 546
Cdd:PRK04863  856 HESQEQQQRSQLEQA 870
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
467-545 8.73e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984093767  467 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLL--------AELRLLRQRKDELEQRMSALQESRRE 538
Cdd:COG4913   248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLeaeleelrAELARLEAELERLEARLDALREELDE 327


                  ....*..
gi 984093767  539 LMVQLEG 545
Cdd:COG4913   328 LEAQIRG 334
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH