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Conserved domains on  [gi|14916515|ref|NP_116763|]
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dystrobrevin alpha isoform 8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05431 super family cl35319
seryl-tRNA synthetase; Provisional
 98-168 3.14e-05

seryl-tRNA synthetase; Provisional


The actual alignment was detected with superfamily member PRK05431:

Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 43.52  E-value: 3.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14916515   98 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 168
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
 
Name Accession Description Interval E-value
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 98-168 3.14e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 43.52  E-value: 3.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14916515   98 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 168
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
92-182 1.65e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916515  92 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 170
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

                        90
                ....*....|..
gi 14916515 171 LMKLLKEEELKQ 182
Cdd:COG4717 232 LENELEAAALEE 243
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 47-184 2.17e-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: 38.13  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916515     47 ESSNRLDEEHRLIARYAARLAAESSSSQPPQQrsapdisFTIDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPT 126
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKE-------YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 14916515    127 PEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEELKQGV 184
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 136-180 5.62e-03

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


Pssm-ID: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 35.54  E-value: 5.62e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 14916515 136 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEGLMKLLKEEEL 180
Cdd:cd23160   5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKLKEGTEI 52
 
Name Accession Description Interval E-value
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 98-168 3.14e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 43.52  E-value: 3.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14916515   98 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 168
Cdd:PRK05431  30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
92-182 1.65e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916515  92 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEG 170
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

                        90
                ....*....|..
gi 14916515 171 LMKLLKEEELKQ 182
Cdd:COG4717 232 LENELEAAALEE 243
PRK12704 PRK12704
phosphodiesterase; Provisional
 89-182 2.50e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916515   89 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQES 160
Cdd:PRK12704  35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                         90       100
                 ....*....|....*....|..
gi 14916515  161 RRELMVQLEGLMKLLKEEELKQ 182
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKE 130
PRK12704 PRK12704
phosphodiesterase; Provisional
 88-178 1.21e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916515   88 IDANKQQRQLIAELENKNREILQEIQ----RLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRE 163
Cdd:PRK12704  60 LEAKEEIHKLRNEFEKELRERRNELQklekRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139

                         90
                 ....*....|....*
gi 14916515  164 LMVQLEGLMKLLKEE 178
Cdd:PRK12704 140 QLQELERISGLTAEE 154
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 47-184 2.17e-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: 38.13  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916515     47 ESSNRLDEEHRLIARYAARLAAESSSSQPPQQrsapdisFTIDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPT 126
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKE-------YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 14916515    127 PEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEELKQGV 184
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 91-162 3.98e-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: 36.52  E-value: 3.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14916515    91 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRR 162
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-182 4.01e-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: 37.34  E-value: 4.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916515     50 NRLDEEHRLIARY---AARLAAESSSSQPPQQRSAPDISFTIDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPT 126
Cdd:TIGR02168  232 LRLEELREELEELqeeLKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 14916515    127 PEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEELKQ 182
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-182 5.59e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 36.84  E-value: 5.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916515  92 KQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGL 171
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                        90
                ....*....|.
gi 14916515 172 MKLLKEEELKQ 182
Cdd:COG1196 322 EEELAELEEEL 332
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 136-180 5.62e-03

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


Pssm-ID: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 35.54  E-value: 5.62e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 14916515 136 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEGLMKLLKEEEL 180
Cdd:cd23160   5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKLKEGTEI 52
 
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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