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Conserved domains on  [gi|526479822|ref|NP_001268354|]
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dynactin subunit 3 isoform 3 [Homo sapiens]

Protein Classification

Dynactin_p22 domain-containing protein( domain architecture ID 10538436)

Dynactin_p22 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dynactin_p22 pfam07426
Dynactin subunit p22; This family contains p22, the smallest subunit of dynactin, a complex ...
 10-142 5.42e-50

Dynactin subunit p22; This family contains p22, the smallest subunit of dynactin, a complex that binds to cytoplasmic dynein and is a required activator for cytoplasmic dynein-mediated vesicular transport. Dynactin localizes to the cleavage furrow and to the midbodies of dividing cells, suggesting that it may function in cytokinesis. Family members are approximately 170 residues long.


:

Pssm-ID: 462162 [Multi-domain]  Cd Length: 163  Bit Score: 157.77  E-value: 5.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479822   10 LQARVEELERWVYGPGGARG--SRKVADGLVKVQVALGNISSKRERVKILYKKIEDLIKYLDPEYIDRIAIPDASKLQFI 87
Cdd:pfam07426   1 LEERIAELEKRVYGEEKNREkdPNSIIDSLLKVQTKLSSAVSKREKIKQLFKKIPELNKYLDPQYEDSIALPDAAKLELI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479822   88 LAA----------------------------VPEHAARLQRLAQIHIQQQDQCVEITEESKALLEEYNKTTMLLSKQFVQ 139
Cdd:pfam07426  81 LASedelrstaalleqlqelkpvldsehikdVPELTEKLEKLSQIHLKQQEQANELTEEVKDLLENYNQLVLTLSKQFVQ 160


                  ...
gi 526479822  140 WDE 142
Cdd:pfam07426 161 WDE 163
 
Name Accession Description Interval E-value
Dynactin_p22 pfam07426
Dynactin subunit p22; This family contains p22, the smallest subunit of dynactin, a complex ...
 10-142 5.42e-50

Dynactin subunit p22; This family contains p22, the smallest subunit of dynactin, a complex that binds to cytoplasmic dynein and is a required activator for cytoplasmic dynein-mediated vesicular transport. Dynactin localizes to the cleavage furrow and to the midbodies of dividing cells, suggesting that it may function in cytokinesis. Family members are approximately 170 residues long.


Pssm-ID: 462162 [Multi-domain]  Cd Length: 163  Bit Score: 157.77  E-value: 5.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479822   10 LQARVEELERWVYGPGGARG--SRKVADGLVKVQVALGNISSKRERVKILYKKIEDLIKYLDPEYIDRIAIPDASKLQFI 87
Cdd:pfam07426   1 LEERIAELEKRVYGEEKNREkdPNSIIDSLLKVQTKLSSAVSKREKIKQLFKKIPELNKYLDPQYEDSIALPDAAKLELI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479822   88 LAA----------------------------VPEHAARLQRLAQIHIQQQDQCVEITEESKALLEEYNKTTMLLSKQFVQ 139
Cdd:pfam07426  81 LASedelrstaalleqlqelkpvldsehikdVPELTEKLEKLSQIHLKQQEQANELTEEVKDLLENYNQLVLTLSKQFVQ 160


                  ...
gi 526479822  140 WDE 142
Cdd:pfam07426 161 WDE 163
 
Name Accession Description Interval E-value
Dynactin_p22 pfam07426
Dynactin subunit p22; This family contains p22, the smallest subunit of dynactin, a complex ...
 10-142 5.42e-50

Dynactin subunit p22; This family contains p22, the smallest subunit of dynactin, a complex that binds to cytoplasmic dynein and is a required activator for cytoplasmic dynein-mediated vesicular transport. Dynactin localizes to the cleavage furrow and to the midbodies of dividing cells, suggesting that it may function in cytokinesis. Family members are approximately 170 residues long.


Pssm-ID: 462162 [Multi-domain]  Cd Length: 163  Bit Score: 157.77  E-value: 5.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479822   10 LQARVEELERWVYGPGGARG--SRKVADGLVKVQVALGNISSKRERVKILYKKIEDLIKYLDPEYIDRIAIPDASKLQFI 87
Cdd:pfam07426   1 LEERIAELEKRVYGEEKNREkdPNSIIDSLLKVQTKLSSAVSKREKIKQLFKKIPELNKYLDPQYEDSIALPDAAKLELI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526479822   88 LAA----------------------------VPEHAARLQRLAQIHIQQQDQCVEITEESKALLEEYNKTTMLLSKQFVQ 139
Cdd:pfam07426  81 LASedelrstaalleqlqelkpvldsehikdVPELTEKLEKLSQIHLKQQEQANELTEEVKDLLENYNQLVLTLSKQFVQ 160


                  ...
gi 526479822  140 WDE 142
Cdd:pfam07426 161 WDE 163
 
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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