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Conserved domains on  [gi|312147274|ref|NP_001185871|]
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dystrobrevin alpha isoform 14 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
125-258 5.13e-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: 45.53  E-value: 5.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147274 125 LRNNPSCMLESSNRLDEEHRLIARYAARLAAESSSSQPPQQrsapdisftIDANKQQRQLIAELENKNREILQEIQRLRL 204
Cdd:COG4717  107 LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER---------LEELEERLEELRELEEELEELEAELAELQE 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 312147274 205 EHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 258
Cdd:COG4717  178 ELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
125-258 5.13e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 5.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147274 125 LRNNPSCMLESSNRLDEEHRLIARYAARLAAESSSSQPPQQrsapdisftIDANKQQRQLIAELENKNREILQEIQRLRL 204
Cdd:COG4717  107 LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER---------LEELEERLEELRELEEELEELEAELAELQE 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 312147274 205 EHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 258
Cdd:COG4717  178 ELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 185-255 1.06e-04

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 44.29  E-value: 1.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312147274 185 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 255
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 134-267 1.25e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147274   134 ESSNRLDEEHRLIARYAARLAAESSSSQPPQQrsapdisFTIDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPT 213
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKE-------YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 312147274   214 PEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKTQGA 267
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
125-258 5.13e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 5.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147274 125 LRNNPSCMLESSNRLDEEHRLIARYAARLAAESSSSQPPQQrsapdisftIDANKQQRQLIAELENKNREILQEIQRLRL 204
Cdd:COG4717  107 LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER---------LEELEERLEELRELEEELEELEAELAELQE 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 312147274 205 EHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 258
Cdd:COG4717  178 ELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 185-255 1.06e-04

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 44.29  E-value: 1.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312147274 185 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 255
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 134-267 1.25e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147274   134 ESSNRLDEEHRLIARYAARLAAESSSSQPPQQrsapdisFTIDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPT 213
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKE-------YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 312147274   214 PEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKTQGA 267
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 178-249 2.63e-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: 38.84  E-value: 2.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312147274  178 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRR 249
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
PRK12704 PRK12704
phosphodiesterase; Provisional
 176-264 3.70e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147274 176 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQES 247
Cdd:PRK12704  35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                         90
                 ....*....|....*..
gi 312147274 248 RRELMVQLEGLMKLLKT 264
Cdd:PRK12704 109 EEELEKKEKELEQKQQE 125
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-258 5.94e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 5.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147274 179 KQQRQLIAELENKNREILQEIQRLRLEHEQASqptpEKAQQnptLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 258
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELE----LELEE---AQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
 
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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