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Conserved domains on  [gi|2327276876|ref|XP_051707968|]
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dystrobrevin alpha isoform X8 [Oryctolagus cuniculus]

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

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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 3.96e-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: 349.58  E-value: 3.96e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  54 DIWNVIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVK 133
Cdd:cd16249     1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 134 MALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 213
Cdd:cd16249    81 MALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 160


                  .
gi 2327276876 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 1.59e-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: 105.13  E-value: 1.59e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2327276876 241 VECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMKEY 289
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
398-529 6.93e-06

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 398 NRLDEEHRLIARYAARLAAESSSSPTQQRsapdisftIDANKQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPAPEK 476
Cdd:COG4717   119 EKLEKLLQLLPLYQELEALEAELAELPER--------LEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLAT 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2327276876 477 AQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEELKQ 529
Cdd:COG4717   191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
 
Name Accession Description Interval E-value
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
 54-214 3.96e-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: 349.58  E-value: 3.96e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  54 DIWNVIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVK 133
Cdd:cd16249     1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 134 MALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 213
Cdd:cd16249    81 MALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 160


                  .
gi 2327276876 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 3.20e-51

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: 174.26  E-value: 3.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  16 RQLFAEMraQDLDRIRLSTYRTACKLRFVQKKCNLHLVDIWNVIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2327276876  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 1.59e-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: 105.13  E-value: 1.59e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2327276876 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 4.88e-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: 4.88e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2327276876  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 1.92e-07

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


Pssm-ID: 395451  Cd Length: 45  Bit Score: 47.86  E-value: 1.92e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2327276876 239 HPVECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGshsnqHQM 286
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGN-----HQM 45
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
398-529 6.93e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 398 NRLDEEHRLIARYAARLAAESSSSPTQQRsapdisftIDANKQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPAPEK 476
Cdd:COG4717   119 EKLEKLLQLLPLYQELEALEAELAELPER--------LEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLAT 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2327276876 477 AQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEELKQ 529
Cdd:COG4717   191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 374-529 6.41e-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: 46.59  E-value: 6.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  374 AEEHSLIKLYVNQLD-HGARMLESSNRLDEEHRLIARYAARLAAESSssptqqrsapDISFTIDANKQQRQLIAELENKN 452
Cdd:TIGR02168  221 ELRELELALLVLRLEeLREELEELQEELKEAEEELEELTAELQELEE----------KLEELRLEVSELEEEIEELQKEL 290

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2327276876  453 REILQEIQRLRLEHEQASQPAPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEELKQ 529
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 445-515 8.93e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.44  E-value: 8.93e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2327276876 445 IAELENKNREILQEIQRLRLEHEQAS----QPAPEKAQQNPtLLAELRLLRQRKDELEQRMSALQESRRELMVQL 515
Cdd:PRK05431   30 LLELDEERRELQTELEELQAERNALSkeigQAKRKGEDAEA-LIAEVKELKEEIKALEAELDELEAELEELLLRI 103
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 483-527 6.58e-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: 40.16  E-value: 6.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2327276876 483 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEGLMKLLKEEEL 527
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKLKEGTEI 52
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 391-506 1.17e-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: 41.13  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 391 ARMLESSNRLDEEHRLIARYAARLAaESSSSPTQQRSApdisftIDANKQQRQLIAELENKNR---EILQEIQRLRLEHE 467
Cdd:pfam12795  85 QRLLQTSAQLQELQNQLAQLNSQLI-ELQTRPERAQQQ------LSEARQRLQQIRNRLNGPAppgEPLSEAQRWALQAE 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2327276876 468 QASQPAP----EKAQQNPTLLAEL-----RLLRQRKDELEQRMSALQE 506
Cdd:pfam12795 158 LAALKAQidmlEQELLSNNNRQDLlkarrDLLTLRIQRLEQQLQALQE 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 3.96e-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: 349.58  E-value: 3.96e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  54 DIWNVIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVK 133
Cdd:cd16249     1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 134 MALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 213
Cdd:cd16249    81 MALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 160


                  .
gi 2327276876 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 1.61e-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: 293.76  E-value: 1.61e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  54 DIWNVIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVK 133
Cdd:cd16244     1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 134 MALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 213
Cdd:cd16244    81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                  .
gi 2327276876 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 3.45e-76

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: 243.01  E-value: 3.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  54 DIWNVIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVK 133
Cdd:cd16250     1 DIWNMIEAFRDNGLNTLDHSTEISVSRLETIISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGHGKLTVFSVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 134 MALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 213
Cdd:cd16250    81 AMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHSVRTCFPQQKKIMLNMFLDTM 160


                  .
gi 2327276876 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 3.20e-51

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: 174.26  E-value: 3.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  16 RQLFAEMraQDLDRIRLSTYRTACKLRFVQKKCNLHLVDIWNVIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2327276876  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 1.67e-41

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: 146.29  E-value: 1.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 144 IMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQ---QKKVTLNGFLDTLMSDppPQ 220
Cdd:pfam09069   1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGGIEPSVRSCFEQvggKPKITLNHFLDWLMSE--PQ 78

                          90
                  ....*....|..
gi 2327276876 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 8.27e-33

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: 124.31  E-value: 8.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  54 DIWNVIEALRENALNNLDPnTELNVARLEAVLSTIFYQLNKRMPttHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVK 133
Cdd:cd15901     1 DLSTVLSVFDRHGLSGSQD-SVLDCEELETILTELYIKLNKRRP--DLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 134 MALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFG--YTEQSARSCFSQQKK---VTLNG 208
Cdd:cd15901    78 IALITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGghNVEAAVESCFQLARSrvgVSEDT 157


                  ....*.
gi 2327276876 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 1.59e-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: 105.13  E-value: 1.59e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2327276876 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 4.88e-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: 4.88e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2327276876  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 2.05e-12

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: 65.78  E-value: 2.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  67 LNNLDPNTELNVARLEAVLSTIFYQLNKRMPTThqIHVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMD 146
Cdd:cd16245    14 LSNSENNLCLPPDELEAVLHDIYFAAEKLGNFN--IDVDLATELLANLFLNVFDPERKKSISVLELKVFLTLLCGSSLQE 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2327276876 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 ...
 54-213 1.35e-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: 63.41  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  54 DIWNVIEALRENALNnlDPNTEL-NVARLEAVLSTIFYQLNKRMPttHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAV 132
Cdd:cd16242     1 SLSTAIEAFDQHGLR--AQNDKLiDVPDMITCLTTIYEALEEEHP--TLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 133 KMALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCFSQ---QKKVTLN 207
Cdd:cd16242    77 KVGLVLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSniEPSVRSCFEKageKPEISAA 156


                  ....*.
gi 2327276876 208 GFLDTL 213
Cdd:cd16242   157 HFLDWL 162
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 243-288 4.06e-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: 4.06e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2327276876 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 4.62e-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: 4.62e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2327276876 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 2.87e-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: 2.87e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2327276876 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 9.51e-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: 9.51e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2327276876 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 1.92e-07

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


Pssm-ID: 395451  Cd Length: 45  Bit Score: 47.86  E-value: 1.92e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2327276876 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 4.14e-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: 4.14e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2327276876 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 1.04e-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: 1.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2327276876 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 1.70e-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: 48.54  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 120 DPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSM----ISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSAR 195
Cdd:cd16243    63 DREQTGFVSLRSVEAALIALSGDTLSAKYRALFQLyesgQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFGNVETAVR 142


                  ....*
gi 2327276876 196 SCFSQ 200
Cdd:cd16243   143 SCFSG 147
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
398-529 6.93e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 398 NRLDEEHRLIARYAARLAAESSSSPTQQRsapdisftIDANKQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPAPEK 476
Cdd:COG4717   119 EKLEKLLQLLPLYQELEALEAELAELPER--------LEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLAT 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2327276876 477 AQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEELKQ 529
Cdd:COG4717   191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 243-284 1.79e-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: 1.79e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2327276876 243 CSYCHSESMMGFRYRCQQCHNYQLCQDCFwrghaggsHSNQH 284
Cdd:cd02339     3 CDTCRKQGIIGIRWKCAECPNYDLCTTCY--------HGDKH 36
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 241-286 2.31e-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: 2.31e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2327276876 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 2.83e-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: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 116 LAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYT--EQS 193
Cdd:cd16248    59 LNVYDSGRNGKIRVLSFKTGIVCLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSnvEPS 138


                  ....*
gi 2327276876 194 ARSCF 198
Cdd:cd16248   139 VRSCF 143
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 374-529 6.41e-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: 46.59  E-value: 6.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  374 AEEHSLIKLYVNQLD-HGARMLESSNRLDEEHRLIARYAARLAAESSssptqqrsapDISFTIDANKQQRQLIAELENKN 452
Cdd:TIGR02168  221 ELRELELALLVLRLEeLREELEELQEELKEAEEELEELTAELQELEE----------KLEELRLEVSELEEEIEELQKEL 290

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2327276876  453 REILQEIQRLRLEHEQASQPAPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEELKQ 529
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 445-515 8.93e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 45.44  E-value: 8.93e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2327276876 445 IAELENKNREILQEIQRLRLEHEQAS----QPAPEKAQQNPtLLAELRLLRQRKDELEQRMSALQESRRELMVQL 515
Cdd:PRK05431   30 LLELDEERRELQTELEELQAERNALSkeigQAKRKGEDAEA-LIAEVKELKEEIKALEAELDELEAELEELLLRI 103
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
 76-211 1.20e-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: 43.35  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  76 LNVARLEAVLSTIFYQLNKRmpttHQ--IHVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFS 153
Cdd:cd16247    21 LSVPDVINCLTTIYDGLEQK----HKdlVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLMSLSKGLLEEKYRYLFK 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2327276876 154 MISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCFSQ---QKKVTLNGFLD 211
Cdd:cd16247    97 EVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQHannKPEIDVKQFID 159
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 241-281 1.47e-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: 1.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2327276876 241 VECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHS 281
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHT 41
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 438-509 1.61e-04

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


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 43.46  E-value: 1.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2327276876 438 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPAPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRR 509
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
PRK12704 PRK12704
phosphodiesterase; Provisional
 436-529 1.86e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 436 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqpapEKAQQNPTLLAELRLLRQRKDELEQRMSALQES 507
Cdd:PRK12704   35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                          90       100
                  ....*....|....*....|..
gi 2327276876 508 RRELMVQLEGLMKLLKEEELKQ 529
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKE 130
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 395-532 2.18e-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: 45.06  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  395 ESSNRLDEEHRliaRYAARLAAESSSsptQQRSAPDISFTIDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPAP 474
Cdd:TIGR02169  798 AELSKLEEEVS---RIEARLREIEQK---LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2327276876  475 EKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEELKQGTQ 532
Cdd:TIGR02169  872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
439-529 3.57e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 439 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPAPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 518
Cdd:COG4372    97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176

                          90
                  ....*....|.
gi 2327276876 519 MKLLKEEELKQ 529
Cdd:COG4372   177 SEAEAEQALDE 187
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 438-550 3.67e-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: 43.60  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 438 NKQQRQLIAELENKNREILQEIQRLRLEHEQASQPAPEKAQQNPTLLAE-------LRLLRQRKDELEQRMSALQESRRe 510
Cdd:COG4942   145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAE- 223

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2327276876 511 lmvQLEGLMKLLKEEELKQGTQGASSPRSSPSHTISRPIP 550
Cdd:COG4942   224 ---ELEALIARLEAEAAAAAERTPAAGFAALKGKLPWPVS 260
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 255-286 3.74e-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: 3.74e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2327276876 255 RYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQM 286
Cdd:cd02343    14 RYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 483-527 6.58e-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: 40.16  E-value: 6.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2327276876 483 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEGLMKLLKEEEL 527
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKLKEGTEI 52
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 411-525 8.60e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.76  E-value: 8.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 411 AARLAAESSSSPTQQRsapDISFTIDANKQQRQ-LIAELENKNREILQEIQRLRLEHEQASQPAPEKAQQNPTLLAELRL 489
Cdd:COG0542   399 AARVRMEIDSKPEELD---ELERRLEQLEIEKEaLKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQE 475

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2327276876 490 LRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEE 525
Cdd:COG0542   476 LKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 375-526 1.02e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 375 EEHSLIKLYVNQLDH-GARMLESSNRLDEEHRLIARYAARLAAESSSSPTQQRSAPDISFTID-ANKQQRQLIAELEnkn 452
Cdd:COG1196   222 LKELEAELLLLKLRElEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeAQAEEYELLAELA--- 298

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2327276876 453 rEILQEIQRLRLEHEQASQPAPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEE 526
Cdd:COG1196   299 -RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 391-506 1.17e-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: 41.13  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 391 ARMLESSNRLDEEHRLIARYAARLAaESSSSPTQQRSApdisftIDANKQQRQLIAELENKNR---EILQEIQRLRLEHE 467
Cdd:pfam12795  85 QRLLQTSAQLQELQNQLAQLNSQLI-ELQTRPERAQQQ------LSEARQRLQQIRNRLNGPAppgEPLSEAQRWALQAE 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2327276876 468 QASQPAP----EKAQQNPTLLAEL-----RLLRQRKDELEQRMSALQE 506
Cdd:pfam12795 158 LAALKAQidmlEQELLSNNNRQDLlkarrDLLTLRIQRLEQQLQALQE 205
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
435-529 1.24e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 435 IDANKQQRQLIAELENKNREILQEIQRL-RLEHEQAsqpapEKAQQNPTLLAELRLLRQRKD--ELEQRMSALQESRREL 511
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEYAELQEELeELEEELE-----ELEAELEELREELEKLEKLLQllPLYQELEALEAELAEL 144

                          90
                  ....*....|....*...
gi 2327276876 512 MVQLEGLMKllKEEELKQ 529
Cdd:COG4717   145 PERLEELEE--RLEELRE 160
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
445-549 1.34e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 445 IAELENKNREILQEIQRLRLE----HEQASQPAPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 517
Cdd:COG1340    10 LEELEEKIEELREEIEELKEKrdelNEELKELAEKRDELNaqvKELREEAQELREKRDELNEKVKELKEERDELNEKLNE 89

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2327276876 518 LMKLLkeEELKQGTQGASSPRSSPsHTISRPI 549
Cdd:COG1340    90 LREEL--DELRKELAELNKAGGSI-DKLRKEI 118
PRK12704 PRK12704
phosphodiesterase; Provisional
 435-525 1.47e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 435 IDANKQQRQLIAELENKNREILQEIQRL---------RLEHEQASQpapEKAQQNptLLAELRLLRQRKDELEQRMSALQ 505
Cdd:PRK12704   60 LEAKEEIHKLRNEFEKELRERRNELQKLekrllqkeeNLDRKLELL---EKREEE--LEKKEKELEQKQQELEKKEEELE 134

                          90       100
                  ....*....|....*....|
gi 2327276876 506 ESRRELMVQLEGLMKLLKEE 525
Cdd:PRK12704  135 ELIEEQLQELERISGLTAEE 154
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 440-586 1.66e-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: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 440 QQRQLIAELENKNREILQEIQRLRLEHEQASQPAPEKAQQNPTLLAEL----RLLRQRKDELEQRMSALQESRRELMVQL 515
Cdd:COG3883   119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELeaakAELEAQQAEQEALLAQLSAEEAAAEAQL 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2327276876 516 EGLMKLLKEEELKQGTQGASSPRSSPSHTISRPipmPIRSASACSTPTHTPQDSLTGVGGDVQEAFAQSSR 586
Cdd:COG3883   199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA---AAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
436-529 1.92e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 436 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPAPEKAQQNptllAELRLLRQRKDELEQRMSALQESRRELMVQL 515
Cdd:COG4372    56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----EELESLQEEAEELQEELEELQKERQDLEQQR 131

                          90       100
                  ....*....|....*....|...
gi 2327276876 516 EGLMKLL---------KEEELKQ 529
Cdd:COG4372   132 KQLEAQIaelqseiaeREEELKE 154
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 441-526 2.39e-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: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 441 QRQLIAELENKNREILQEIQRLRLEHEQASQPAPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMK 520
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97


                  ....*.
gi 2327276876 521 LLKEEE 526
Cdd:COG4942    98 ELEAQK 103
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 436-562 2.48e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 436 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPAPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 515
Cdd:COG3883   133 DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2327276876 516 EGLMKLLKEEELKQGTQGASSPRSSPSHTISRPIPMPIRSASACSTP 562
Cdd:COG3883   213 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAA 259
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 391-516 2.69e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 41.28  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 391 ARMLESSNRLDEEHR-------LIARYAARLAAESSSSPTQQRSAP---DISFTIDANKQQR-QLIAELENKNREILQEI 459
Cdd:pfam07111 429 ARIPSLSNRLSYAVRkvhtikgLMARKVALAQLRQESCPPPPPAPPvdaDLSLELEQLREERnRLDAELQLSAHLIQQEV 508

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2327276876 460 QRLRLEHEQASQPAPEKAQQnptllaelrllrqrkdeLEQRMSALQESRRELMVQLE 516
Cdd:pfam07111 509 GRAREQGEAERQQLSEVAQQ-----------------LEQELQRAQESLASVGQQLE 548
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 385-518 3.04e-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: 41.20  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  385 NQLDHGARMLES-SNRLDEEHRLIARYAARLAAESSSSPTQQRSAPDISFTI-DANKQQRQLIAELENKNREI------L 456
Cdd:TIGR02168  796 EELKALREALDElRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIeELSEDIESLAAEIEELEELIeeleseL 875

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2327276876  457 QEIQRLRLEHEQASQPAPEKAQQnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 518
Cdd:TIGR02168  876 EALLNERASLEEALALLRSELEE---LSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
444-529 4.53e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 444 LIAELENKNREI-----------LQEIQRLRLEHEQASqpapEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELM 512
Cdd:COG4717    47 LLERLEKEADELfkpqgrkpelnLKELKELEEELKEAE----EKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122

                          90
                  ....*....|....*..
gi 2327276876 513 VQLEGLMKLLKEEELKQ 529
Cdd:COG4717   123 KLLQLLPLYQELEALEA 139
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 448-529 5.24e-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: 39.48  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 448 LENKN---REILQEIQRLrLEHEQASQPAPEKAQQnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKE 524
Cdd:cd16269   176 LQSKEaeaEAILQADQAL-TEKEKEIEAERAKAEA---AEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERE 251


                  ....*
gi 2327276876 525 EELKQ 529
Cdd:cd16269   252 NLLKE 256
Bbox1 cd19757
B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of ...
 243-288 5.43e-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: 5.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2327276876 243 CSYCHSESMmgfRYRCQQCHNYqLCQDCFWRGHAGGSHSNQHQMKE 288
Cdd:cd19757     2 CDECEEREA---TVYCLECEEF-LCDDCSDAIHRRGKLTRSHKLVP 43
mukB PRK04863
chromosome partition protein MukB;
435-529 5.63e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 5.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  435 IDANKQQRQLIAELENKNREILQEIQRLrleHEQASQ-----------PAPEkaqqnptllAELRLLRQRKDELE----- 498
Cdd:PRK04863   788 IEQLRAEREELAERYATLSFDVQKLQRL---HQAFSRfigshlavafeADPE---------AELRQLNRRRVELEralad 855

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2327276876  499 ------QRMSALQESRRELMV--QLEGLMKLLKEEELKQ 529
Cdd:PRK04863   856 hesqeqQQRSQLEQAKEGLSAlnRLLPRLNLLADETLAD 894
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
375-535 5.67e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 5.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 375 EEHSLIKLYVNQLDHGARMLESSNRLDEEHRLIARYAARLAAESSSSPTQQRSAPDI--SFTIDANKQQR-QLIAELENK 451
Cdd:COG3206   203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLaELEAELAEL 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 452 N----------REILQEIQRLRLEHEQASQPAPEKAQ-QNPTLLAELRLLRQRKDELEQRMSALQESRRELMV------- 513
Cdd:COG3206   283 SarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEaELEALQAREASLQAQLAQLEARLAELPELEAELRRlerevev 362

                         170       180
                  ....*....|....*....|....*
gi 2327276876 514 ---QLEGLMKLLKEEELKQGTQGAS 535
Cdd:COG3206   363 areLYESLLQRLEEARLAEALTVGN 387
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
436-517 5.95e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 5.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  436 DANKQQRQL--IAELENKNREILQEIQRLR-----LEHEQASQPAPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESR 508
Cdd:COG4913    246 DAREQIELLepIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325


                   ....*....
gi 2327276876  509 RELMVQLEG 517
Cdd:COG4913    326 DELEAQIRG 334
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 406-524 6.10e-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: 39.75  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 406 LIARYAARLAAESSSSPTQQRSApdISFTIdanKQQRQLIAELENKNREILQEIQRLRLEHEQASQpapekaqqnptlla 485
Cdd:COG4942     9 LLLALAAAAQADAAAEAEAELEQ--LQQEI---AELEKELAALKKEEKALLKQLAALERRIAALAR-------------- 69

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2327276876 486 ELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKE 524
Cdd:COG4942    70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 433-524 7.20e-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: 38.40  E-value: 7.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876 433 FTIDANKQQRQLIAELENKNREIlQEIQRLRLEHEQASQpapekaQQNPTLLAELRLLRQRKDELEQRMSA----LQESR 508
Cdd:cd16855    16 RTQETENDLRNLQQKQESFVIQY-QESQKIQAQLQQLQQ------QPQNERIELEQQLQQQKEQLEQLLNAkaqeLLQLR 88

                          90
                  ....*....|....*.
gi 2327276876 509 RELMVQLEGLMKLLKE 524
Cdd:cd16855    89 MELADKFKKTIQLLSK 104
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 421-541 7.84e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.95  E-value: 7.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327276876  421 SPTQQRSAPDISFTIDANKQQRQLIAELENKNREILQEIQRlRLEHEQASQPAPEKAQQNPTLLAELRLLRQ-------- 492
Cdd:TIGR00618  289 ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK-RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahevatsi 367

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2327276876  493 -----RKDELEQRMSALQESRRELMVQLEGLMKLLKEEELKQGTQGASSPRSSP 541
Cdd:TIGR00618  368 reiscQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD 421
 
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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