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Conserved domains on  [gi|51093836|ref|NP_653297|]
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axonemal dynein light chain domain-containing protein 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ax_dynein_light super family cl23860
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
 261-357 1.80e-05

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


The actual alignment was detected with superfamily member pfam10211:

Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 46.41  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51093836    261 IYNMIFHELIRQVSVDCADRGELLSKVRERYvqmldqiaRQMIDFYKDLVTQRV----------------MDQRI---LE 321
Cdd:pfam10211   62 LYSQCFDELIRQVTINCPERGLLLLRVRDEL--------RMTIAAYQTLYESSVafgmrkalqaeqgkaeLEKKIadlEE 133

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 51093836    322 ELYNFKHVIEELTRELCLVRAHDVKLTKETEKAHKD 357
Cdd:pfam10211  134 EKEELEKQVAELKAKCEAIEKREEERRQAEEKKHAE 169
 
Name Accession Description Interval E-value
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
 261-357 1.80e-05

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 46.41  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51093836    261 IYNMIFHELIRQVSVDCADRGELLSKVRERYvqmldqiaRQMIDFYKDLVTQRV----------------MDQRI---LE 321
Cdd:pfam10211   62 LYSQCFDELIRQVTINCPERGLLLLRVRDEL--------RMTIAAYQTLYESSVafgmrkalqaeqgkaeLEKKIadlEE 133

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 51093836    322 ELYNFKHVIEELTRELCLVRAHDVKLTKETEKAHKD 357
Cdd:pfam10211  134 EKEELEKQVAELKAKCEAIEKREEERRQAEEKKHAE 169
 
Name Accession Description Interval E-value
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
 261-357 1.80e-05

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 46.41  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51093836    261 IYNMIFHELIRQVSVDCADRGELLSKVRERYvqmldqiaRQMIDFYKDLVTQRV----------------MDQRI---LE 321
Cdd:pfam10211   62 LYSQCFDELIRQVTINCPERGLLLLRVRDEL--------RMTIAAYQTLYESSVafgmrkalqaeqgkaeLEKKIadlEE 133

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 51093836    322 ELYNFKHVIEELTRELCLVRAHDVKLTKETEKAHKD 357
Cdd:pfam10211  134 EKEELEKQVAELKAKCEAIEKREEERRQAEEKKHAE 169
 
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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