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Conserved domains on  [gi|145579725]
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Chain B, Ap-2 Complex Subunit Beta-2

Protein Classification

Alpha_adaptinC2 and B2-adapt-app_C domain-containing protein( domain architecture ID 10655463)

Alpha_adaptinC2 and B2-adapt-app_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
B2-adapt-app_C smart01020
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
 127-237 3.38e-52

Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure consisting of a 5 stranded beta-sheet, flanked by one alpha helix on the outer side, and by two alpha helices on the inner side. This domain is required for binding to clathrin, and its subsequent polymerisation. Furthermore, a hydrophobic patch present in the domain also binds to a subset of D-phi-F/W motif-containing proteins that are bound by the alpha-adaptin appendage domain (epsin, AP180, eps15).


:

Pssm-ID: 198088  Cd Length: 111  Bit Score: 164.79  E-value: 3.38e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145579725   127 FVEDGKMERQVFLATWKDIPNENELQFQIKECHLNADTVSSKLQNNNVYTIAKRNVEGQDMLYQSLKLTNGIWILAELRI 206
Cdd:smart01020   1 FVEDGQMEREVFLKTWKSLPESNEQQFQLQPNNLNPDTIIKKLQSNNIFTIAKRNVGNQDKLYLSAKLTNGIWILIELTI 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 145579725   207 QPGNPNYTLSLKCRAPEVSQYIYQVYDSILK 237
Cdd:smart01020  81 NPGTPNVTLSVKCDSPEVIQLFTQVFEKILS 111
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
 18-118 1.98e-21

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: 85.37  E-value: 1.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145579725    18 AVKAKGLEISGTFTHRQGHIYMEMNFTNKALQHMTDFAIQFNKNSFGVIPSTPLAIhTPLMPNQSIDVSLPLNTLGP--- 94
Cdd:smart00809   1 AYEKNGLQIGFKFERRPGLIRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSS-PTLPPGGQITQVLKVENPGKfpl 79

                           90       100
                   ....*....|....*....|....*
gi 145579725    95 VMKMEPLNNLQV-AVKNNIDVFYFS 118
Cdd:smart00809  80 RLRLRLSYLLGGsAVTEQGDVLKFP 104
 
Name Accession Description Interval E-value
B2-adapt-app_C smart01020
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
 127-237 3.38e-52

Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure consisting of a 5 stranded beta-sheet, flanked by one alpha helix on the outer side, and by two alpha helices on the inner side. This domain is required for binding to clathrin, and its subsequent polymerisation. Furthermore, a hydrophobic patch present in the domain also binds to a subset of D-phi-F/W motif-containing proteins that are bound by the alpha-adaptin appendage domain (epsin, AP180, eps15).


Pssm-ID: 198088  Cd Length: 111  Bit Score: 164.79  E-value: 3.38e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145579725   127 FVEDGKMERQVFLATWKDIPNENELQFQIKECHLNADTVSSKLQNNNVYTIAKRNVEGQDMLYQSLKLTNGIWILAELRI 206
Cdd:smart01020   1 FVEDGQMEREVFLKTWKSLPESNEQQFQLQPNNLNPDTIIKKLQSNNIFTIAKRNVGNQDKLYLSAKLTNGIWILIELTI 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 145579725   207 QPGNPNYTLSLKCRAPEVSQYIYQVYDSILK 237
Cdd:smart01020  81 NPGTPNVTLSVKCDSPEVIQLFTQVFEKILS 111
B2-adapt-app_C pfam09066
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
 128-236 4.43e-45

Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure consisting of a 5 stranded beta-sheet, flanked by one alpha helix on the outer side, and by two alpha helices on the inner side. This domain is required for binding to clathrin, and its subsequent polymerization. Furthermore, a hydrophobic patch present in the domain also binds to a subset of D-phi-F/W motif-containing proteins that are bound by the alpha-adaptin appendage domain (epsin, AP180, eps15).


Pssm-ID: 462667  Cd Length: 111  Bit Score: 146.64  E-value: 4.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145579725  128 VEDGKMERQVFLATWKDIPNENELQFQIKE-CHLNADTVSSKLQNNNVYTIAKRNVEG-QDMLYQSLKLTNGIWILAELR 205
Cdd:pfam09066   1 VEDGKLDREVFLETWKSLPDSNELSLTLQNlASVSPDAIEQKLQANNIFTIAKRGVEGpQEKLYFSAKLTNGILFLVELT 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 145579725  206 IQPGNPNYTLSLKCRAPEVSQYIYQVYDSIL 236
Cdd:pfam09066  81 INTPGSNVKLSVKSEDPEVAPLFLQLFESIL 111
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
 18-118 1.98e-21

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: 85.37  E-value: 1.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145579725    18 AVKAKGLEISGTFTHRQGHIYMEMNFTNKALQHMTDFAIQFNKNSFGVIPSTPLAIhTPLMPNQSIDVSLPLNTLGP--- 94
Cdd:smart00809   1 AYEKNGLQIGFKFERRPGLIRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSS-PTLPPGGQITQVLKVENPGKfpl 79

                           90       100
                   ....*....|....*....|....*
gi 145579725    95 VMKMEPLNNLQV-AVKNNIDVFYFS 118
Cdd:smart00809  80 RLRLRLSYLLGGsAVTEQGDVLKFP 104
Alpha_adaptinC2 pfam02883
Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud ...
 12-118 2.06e-13

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: 64.27  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145579725   12 KAVWLPAVKAKGLEISGTFTHRQGHIYMEMNFTNKALQHMTDFAIQFNKNSFGVIPSTPLAIHT-PLMPNQSIDVSLPLN 90
Cdd:pfam02883   1 PPVVLYESDGLQIGFSFERSRRPGQIRITLTFTNKSSSPISNFSFQAAVPKSLKLQLQPPSSNVlPPNPGGQITQVLLIE 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 145579725   91 TLG---PVMKMEPLNNLQVAVKNNIDVFYFS 118
Cdd:pfam02883  81 NPGkkpLRMRLKISYLNGGAVQEQGDVLKFP 111
 
Name Accession Description Interval E-value
B2-adapt-app_C smart01020
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
 127-237 3.38e-52

Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure consisting of a 5 stranded beta-sheet, flanked by one alpha helix on the outer side, and by two alpha helices on the inner side. This domain is required for binding to clathrin, and its subsequent polymerisation. Furthermore, a hydrophobic patch present in the domain also binds to a subset of D-phi-F/W motif-containing proteins that are bound by the alpha-adaptin appendage domain (epsin, AP180, eps15).


Pssm-ID: 198088  Cd Length: 111  Bit Score: 164.79  E-value: 3.38e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145579725   127 FVEDGKMERQVFLATWKDIPNENELQFQIKECHLNADTVSSKLQNNNVYTIAKRNVEGQDMLYQSLKLTNGIWILAELRI 206
Cdd:smart01020   1 FVEDGQMEREVFLKTWKSLPESNEQQFQLQPNNLNPDTIIKKLQSNNIFTIAKRNVGNQDKLYLSAKLTNGIWILIELTI 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 145579725   207 QPGNPNYTLSLKCRAPEVSQYIYQVYDSILK 237
Cdd:smart01020  81 NPGTPNVTLSVKCDSPEVIQLFTQVFEKILS 111
B2-adapt-app_C pfam09066
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
 128-236 4.43e-45

Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure consisting of a 5 stranded beta-sheet, flanked by one alpha helix on the outer side, and by two alpha helices on the inner side. This domain is required for binding to clathrin, and its subsequent polymerization. Furthermore, a hydrophobic patch present in the domain also binds to a subset of D-phi-F/W motif-containing proteins that are bound by the alpha-adaptin appendage domain (epsin, AP180, eps15).


Pssm-ID: 462667  Cd Length: 111  Bit Score: 146.64  E-value: 4.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145579725  128 VEDGKMERQVFLATWKDIPNENELQFQIKE-CHLNADTVSSKLQNNNVYTIAKRNVEG-QDMLYQSLKLTNGIWILAELR 205
Cdd:pfam09066   1 VEDGKLDREVFLETWKSLPDSNELSLTLQNlASVSPDAIEQKLQANNIFTIAKRGVEGpQEKLYFSAKLTNGILFLVELT 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 145579725  206 IQPGNPNYTLSLKCRAPEVSQYIYQVYDSIL 236
Cdd:pfam09066  81 INTPGSNVKLSVKSEDPEVAPLFLQLFESIL 111
Alpha_adaptinC2 smart00809
Adaptin C-terminal domain; Adaptins are components of the adaptor complexes which link ...
 18-118 1.98e-21

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: 85.37  E-value: 1.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145579725    18 AVKAKGLEISGTFTHRQGHIYMEMNFTNKALQHMTDFAIQFNKNSFGVIPSTPLAIhTPLMPNQSIDVSLPLNTLGP--- 94
Cdd:smart00809   1 AYEKNGLQIGFKFERRPGLIRITLTFTNKSPSPITNFSFQAAVPKSLKLQLQPPSS-PTLPPGGQITQVLKVENPGKfpl 79

                           90       100
                   ....*....|....*....|....*
gi 145579725    95 VMKMEPLNNLQV-AVKNNIDVFYFS 118
Cdd:smart00809  80 RLRLRLSYLLGGsAVTEQGDVLKFP 104
Alpha_adaptinC2 pfam02883
Adaptin C-terminal domain; Alpha adaptin is a heterotetramer which regulates clathrin-bud ...
 12-118 2.06e-13

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: 64.27  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145579725   12 KAVWLPAVKAKGLEISGTFTHRQGHIYMEMNFTNKALQHMTDFAIQFNKNSFGVIPSTPLAIHT-PLMPNQSIDVSLPLN 90
Cdd:pfam02883   1 PPVVLYESDGLQIGFSFERSRRPGQIRITLTFTNKSSSPISNFSFQAAVPKSLKLQLQPPSSNVlPPNPGGQITQVLLIE 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 145579725   91 TLG---PVMKMEPLNNLQVAVKNNIDVFYFS 118
Cdd:pfam02883  81 NPGkkpLRMRLKISYLNGGAVQEQGDVLKFP 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.
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