NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|159164348|pdb|2E9G|A]
View 

Chain A, AP-1 complex subunit gamma-2

Protein Classification

Alpha_adaptinC2 domain-containing protein( domain architecture ID 10655447)

Alpha_adaptinC2 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
18-126 1.89e-29

Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Gamma-adaptin is a subunit of the golgi adaptor. Alpha adaptin is a heterotetramer that regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This Ig-fold domain is found in alpha, beta and gamma adaptins and consists of a beta-sandwich containing 7 strands in 2 beta-sheets in a greek-key topology.. The adaptor appendage contains an additional N-terminal strand.


:

Pssm-ID: 197886 [Multi-domain]  Cd Length: 104  Bit Score: 102.32  E-value: 1.89e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E9G_A          18 VFEREGVQLNLSFIRPPENpalLLITITATNFSEGDVTHFICQAAVPKSLQLQLQAPSGNTVPARGglPITQLFRILNPN 97
Cdd:smart00809   1 AYEKNGLQIGFKFERRPGL---IRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPGG--QITQVLKVENPG 75
                           90       100
                   ....*....|....*....|....*....
2E9G_A          98 KAPLRLKLRLTYDHFHQSVQEIFEVNNLP 126
Cdd:smart00809  76 KFPLRLRLRLSYLLGGSAVTEQGDVLKFP 104
 
Name Accession Description Interval E-value
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
18-126 1.89e-29

Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Gamma-adaptin is a subunit of the golgi adaptor. Alpha adaptin is a heterotetramer that regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This Ig-fold domain is found in alpha, beta and gamma adaptins and consists of a beta-sandwich containing 7 strands in 2 beta-sheets in a greek-key topology.. The adaptor appendage contains an additional N-terminal strand.


Pssm-ID: 197886 [Multi-domain]  Cd Length: 104  Bit Score: 102.32  E-value: 1.89e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E9G_A          18 VFEREGVQLNLSFIRPPENpalLLITITATNFSEGDVTHFICQAAVPKSLQLQLQAPSGNTVPARGglPITQLFRILNPN 97
Cdd:smart00809   1 AYEKNGLQIGFKFERRPGL---IRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPGG--QITQVLKVENPG 75
                           90       100
                   ....*....|....*....|....*....
2E9G_A          98 KAPLRLKLRLTYDHFHQSVQEIFEVNNLP 126
Cdd:smart00809  76 KFPLRLRLRLSYLLGGSAVTEQGDVLKFP 104
Alpha_adaptinC2 pfam02883
Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud ...
14-126 2.74e-27

Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This ig-fold domain is found in alpha, beta and gamma adaptins.


Pssm-ID: 460735  Cd Length: 111  Bit Score: 97.39  E-value: 2.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E9G_A         14 PDLKVFEREGVQLNLSFIRPpENPALLLITITATNFSEGDVTHFICQAAVPKSLQLQLQAPSGNTVPARGGLPITQLFRI 93
Cdd:pfam02883   1 PPVVLYESDGLQIGFSFERS-RRPGQIRITLTFTNKSSSPISNFSFQAAVPKSLKLQLQPPSSNVLPPNPGGQITQVLLI 79
                          90       100       110
                  ....*....|....*....|....*....|...
2E9G_A         94 LNPNKAPLRLKLRLTYdHFHQSVQEIFEVNNLP 126
Cdd:pfam02883  80 ENPGKKPLRMRLKISY-LNGGAVQEQGDVLKFP 111
 
Name Accession Description Interval E-value
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
18-126 1.89e-29

Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Gamma-adaptin is a subunit of the golgi adaptor. Alpha adaptin is a heterotetramer that regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This Ig-fold domain is found in alpha, beta and gamma adaptins and consists of a beta-sandwich containing 7 strands in 2 beta-sheets in a greek-key topology.. The adaptor appendage contains an additional N-terminal strand.


Pssm-ID: 197886 [Multi-domain]  Cd Length: 104  Bit Score: 102.32  E-value: 1.89e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E9G_A          18 VFEREGVQLNLSFIRPPENpalLLITITATNFSEGDVTHFICQAAVPKSLQLQLQAPSGNTVPARGglPITQLFRILNPN 97
Cdd:smart00809   1 AYEKNGLQIGFKFERRPGL---IRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSSPTLPPGG--QITQVLKVENPG 75
                           90       100
                   ....*....|....*....|....*....
2E9G_A          98 KAPLRLKLRLTYDHFHQSVQEIFEVNNLP 126
Cdd:smart00809  76 KFPLRLRLRLSYLLGGSAVTEQGDVLKFP 104
Alpha_adaptinC2 pfam02883
Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud ...
14-126 2.74e-27

Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud formation. The carboxyl-terminal appendage of the alpha subunit regulates translocation of endocytic accessory proteins to the bud site. This ig-fold domain is found in alpha, beta and gamma adaptins.


Pssm-ID: 460735  Cd Length: 111  Bit Score: 97.39  E-value: 2.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E9G_A         14 PDLKVFEREGVQLNLSFIRPpENPALLLITITATNFSEGDVTHFICQAAVPKSLQLQLQAPSGNTVPARGGLPITQLFRI 93
Cdd:pfam02883   1 PPVVLYESDGLQIGFSFERS-RRPGQIRITLTFTNKSSSPISNFSFQAAVPKSLKLQLQPPSSNVLPPNPGGQITQVLLI 79
                          90       100       110
                  ....*....|....*....|....*....|...
2E9G_A         94 LNPNKAPLRLKLRLTYdHFHQSVQEIFEVNNLP 126
Cdd:pfam02883  80 ENPGKKPLRMRLKISY-LNGGAVQEQGDVLKFP 111
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH