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Conserved domains on  [gi|161078018|ref|NP_649475|]
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sterile affecting ciliogenesis [Drosophila melanogaster]

Protein Classification

dynein heavy chain( domain architecture ID 10552002)

dynein heavy chain is part of the cytoplasmic dynein that acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules; similar to portion of Homo sapiens axonemal dynein heavy chain 11

Gene Ontology:  GO:0008569|GO:0045505|GO:0051959|GO:0007018|GO:0030286
PubMed:  15661525

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHC_N2 pfam08393
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ...
 901-1042 4.58e-13

Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic cells, as they can convert energy derived from the hydrolysis of ATP to force and movement along cytoskeletal polymers, such as microtubules. This region is found C-terminal to the dynein heavy chain N-terminal region 1 (pfam08385) in many members of this family. No functions seem to have been attributed specifically to this region.


:

Pssm-ID: 462462 [Multi-domain]  Cd Length: 402  Bit Score: 72.29  E-value: 4.58e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078018   901 LESIIASFTPYKNLWYGCANFLKLEDATLGNPIAQLDLEDVWNNLMRLRDELNESMKIFHEkveiMDVAKTFIAKIDDFV 980
Cdd:pfam08393    1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD----WDVAEELKKKIDDFK 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161078018   981 PVYNSIKDIRNENWMYIHWQELSAITGQEI-KYSVAMNYQYLIRKGILDVLPEVHIISEKANN 1042
Cdd:pfam08393   77 KSLPLIEDLRNPALRERHWKQLSEILGFDFdPLSEFFTLGDLLDLNLHKYEEEIEEISEQASK 139
 
Name Accession Description Interval E-value
DHC_N2 pfam08393
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ...
 901-1042 4.58e-13

Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic cells, as they can convert energy derived from the hydrolysis of ATP to force and movement along cytoskeletal polymers, such as microtubules. This region is found C-terminal to the dynein heavy chain N-terminal region 1 (pfam08385) in many members of this family. No functions seem to have been attributed specifically to this region.


Pssm-ID: 462462 [Multi-domain]  Cd Length: 402  Bit Score: 72.29  E-value: 4.58e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078018   901 LESIIASFTPYKNLWYGCANFLKLEDATLGNPIAQLDLEDVWNNLMRLRDELNESMKIFHEkveiMDVAKTFIAKIDDFV 980
Cdd:pfam08393    1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD----WDVAEELKKKIDDFK 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161078018   981 PVYNSIKDIRNENWMYIHWQELSAITGQEI-KYSVAMNYQYLIRKGILDVLPEVHIISEKANN 1042
Cdd:pfam08393   77 KSLPLIEDLRNPALRERHWKQLSEILGFDFdPLSEFFTLGDLLDLNLHKYEEEIEEISEQASK 139
 
Name Accession Description Interval E-value
DHC_N2 pfam08393
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ...
 901-1042 4.58e-13

Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic cells, as they can convert energy derived from the hydrolysis of ATP to force and movement along cytoskeletal polymers, such as microtubules. This region is found C-terminal to the dynein heavy chain N-terminal region 1 (pfam08385) in many members of this family. No functions seem to have been attributed specifically to this region.


Pssm-ID: 462462 [Multi-domain]  Cd Length: 402  Bit Score: 72.29  E-value: 4.58e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078018   901 LESIIASFTPYKNLWYGCANFLKLEDATLGNPIAQLDLEDVWNNLMRLRDELNESMKIFHEkveiMDVAKTFIAKIDDFV 980
Cdd:pfam08393    1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD----WDVAEELKKKIDDFK 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161078018   981 PVYNSIKDIRNENWMYIHWQELSAITGQEI-KYSVAMNYQYLIRKGILDVLPEVHIISEKANN 1042
Cdd:pfam08393   77 KSLPLIEDLRNPALRERHWKQLSEILGFDFdPLSEFFTLGDLLDLNLHKYEEEIEEISEQASK 139
 
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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