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Conserved domains on  [gi|260763941|ref|NP_001159595|]
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BBSome-interacting protein 1 [Danio rerio]

Protein Classification

BBIP10 domain-containing protein( domain architecture ID 10632203)

BBIP10 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BBIP10 pfam14777
Cilia BBSome complex subunit 10; The BBSome (so-named after the association with Bardet-Biedl ...
1-63 2.99e-21

Cilia BBSome complex subunit 10; The BBSome (so-named after the association with Bardet-Biedl syndrome) is a complex of 8 subunits that lies at the base of the flagellar microtubule structure. The precise function of the all the individual components in cilia formation is unclear, however they function to promote loading of cargo to the ciliary axoneme. BBIP10 localizes to the primary cilium, and is present exclusively in ciliated organizms. It is required for cytoplasmic microtubule polymerization and acetylation, two functions not shared with any other BBSome subunits. BBIP10 physically interacts with HDAC6. BBSome-bound BBIP10 may therefore function to couple acetylation of axonemal microtubules and ciliary membrane growth. The primary cilium, a slim microtubule-based organelle that projects from the surface of vertebrate cells has crucial roles in vertebrate development and human genetic diseases. Cilia are required for the response to developmental signals, and evidence is accumulating that the primary cilium is specialized for Hedgehog (Hh) signal transduction. Formation of cilia, in turn, is regulated by other signalling pathways, possibly including the planar cell polarity pathway. The connections between cilia and developmental signalling have begun to clarify the basis of human diseases associated with ciliary dysfunction.


:

Pssm-ID: 464310  Cd Length: 63  Bit Score: 78.26  E-value: 2.99e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260763941   1 MPEVKSMFREVLPKQGQLSMEDVPTMVLCKPKLLPLKSVTLEKLEKMQKDAQEIIRQQELALK 63
Cdd:pfam14777  1 MAEVKDMFREVLPKQGLLYSEDQPTMVLCKPKLLPLKSVTLEKLEKMQREAQETVKQQEEAEK 63
 
Name Accession Description Interval E-value
BBIP10 pfam14777
Cilia BBSome complex subunit 10; The BBSome (so-named after the association with Bardet-Biedl ...
1-63 2.99e-21

Cilia BBSome complex subunit 10; The BBSome (so-named after the association with Bardet-Biedl syndrome) is a complex of 8 subunits that lies at the base of the flagellar microtubule structure. The precise function of the all the individual components in cilia formation is unclear, however they function to promote loading of cargo to the ciliary axoneme. BBIP10 localizes to the primary cilium, and is present exclusively in ciliated organizms. It is required for cytoplasmic microtubule polymerization and acetylation, two functions not shared with any other BBSome subunits. BBIP10 physically interacts with HDAC6. BBSome-bound BBIP10 may therefore function to couple acetylation of axonemal microtubules and ciliary membrane growth. The primary cilium, a slim microtubule-based organelle that projects from the surface of vertebrate cells has crucial roles in vertebrate development and human genetic diseases. Cilia are required for the response to developmental signals, and evidence is accumulating that the primary cilium is specialized for Hedgehog (Hh) signal transduction. Formation of cilia, in turn, is regulated by other signalling pathways, possibly including the planar cell polarity pathway. The connections between cilia and developmental signalling have begun to clarify the basis of human diseases associated with ciliary dysfunction.


Pssm-ID: 464310  Cd Length: 63  Bit Score: 78.26  E-value: 2.99e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260763941   1 MPEVKSMFREVLPKQGQLSMEDVPTMVLCKPKLLPLKSVTLEKLEKMQKDAQEIIRQQELALK 63
Cdd:pfam14777  1 MAEVKDMFREVLPKQGLLYSEDQPTMVLCKPKLLPLKSVTLEKLEKMQREAQETVKQQEEAEK 63
 
Name Accession Description Interval E-value
BBIP10 pfam14777
Cilia BBSome complex subunit 10; The BBSome (so-named after the association with Bardet-Biedl ...
1-63 2.99e-21

Cilia BBSome complex subunit 10; The BBSome (so-named after the association with Bardet-Biedl syndrome) is a complex of 8 subunits that lies at the base of the flagellar microtubule structure. The precise function of the all the individual components in cilia formation is unclear, however they function to promote loading of cargo to the ciliary axoneme. BBIP10 localizes to the primary cilium, and is present exclusively in ciliated organizms. It is required for cytoplasmic microtubule polymerization and acetylation, two functions not shared with any other BBSome subunits. BBIP10 physically interacts with HDAC6. BBSome-bound BBIP10 may therefore function to couple acetylation of axonemal microtubules and ciliary membrane growth. The primary cilium, a slim microtubule-based organelle that projects from the surface of vertebrate cells has crucial roles in vertebrate development and human genetic diseases. Cilia are required for the response to developmental signals, and evidence is accumulating that the primary cilium is specialized for Hedgehog (Hh) signal transduction. Formation of cilia, in turn, is regulated by other signalling pathways, possibly including the planar cell polarity pathway. The connections between cilia and developmental signalling have begun to clarify the basis of human diseases associated with ciliary dysfunction.


Pssm-ID: 464310  Cd Length: 63  Bit Score: 78.26  E-value: 2.99e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260763941   1 MPEVKSMFREVLPKQGQLSMEDVPTMVLCKPKLLPLKSVTLEKLEKMQKDAQEIIRQQELALK 63
Cdd:pfam14777  1 MAEVKDMFREVLPKQGLLYSEDQPTMVLCKPKLLPLKSVTLEKLEKMQREAQETVKQQEEAEK 63
 
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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