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Conserved domains on  [gi|15226705|ref|NP_179216|]
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structural molecule [Arabidopsis thaliana]

Protein Classification

Coatomer_g_Cpla superfamily-containing protein( domain architecture ID 585247)

Coatomer_g_Cpla superfamily-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Coatomer_g_Cpla super family cl24825
Coatomer subunit gamma-1 C-terminal appendage platform; Coatomer_g_Cpla is the very C-terminal ...
 1-66 5.22e-19

Coatomer subunit gamma-1 C-terminal appendage platform; Coatomer_g_Cpla is the very C-terminal domain of the eukaryotic Coatomer subunit gamma-1 proteins. It acts as a platform domain to the C-terminal appendage. It carries one single protein/protein interaction site, which is the binding site for ARFGAP2 or ADP-ribosylation factor GTPase-activating protein. COPI-coated vesicles mediate retrograde transport from the Golgi back to the ER and intra-Golgi transport. The gamma-COPI is part of one of two subcomplexes that make up the heptameric coatomer complex along with the beta, delta and zeta subunits.


The actual alignment was detected with superfamily member pfam16381:

Pssm-ID: 406717  Cd Length: 114  Bit Score: 73.78  E-value: 5.22e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226705     1 MQSCKGTETVASNARSHTCLPSGLYIGNVKVLVKAQFGMdSSKEIVMKLAVRAEDPSVSDAIHALV 66
Cdd:pfam16381  50 MQPLEGSDVVPENASSHTLKLSGKFVGGGKVLVRARLAI-SSGGVTMKLTVRSESEEVCELVLSAV 114
 
Name Accession Description Interval E-value
Coatomer_g_Cpla pfam16381
Coatomer subunit gamma-1 C-terminal appendage platform; Coatomer_g_Cpla is the very C-terminal ...
 1-66 5.22e-19

Coatomer subunit gamma-1 C-terminal appendage platform; Coatomer_g_Cpla is the very C-terminal domain of the eukaryotic Coatomer subunit gamma-1 proteins. It acts as a platform domain to the C-terminal appendage. It carries one single protein/protein interaction site, which is the binding site for ARFGAP2 or ADP-ribosylation factor GTPase-activating protein. COPI-coated vesicles mediate retrograde transport from the Golgi back to the ER and intra-Golgi transport. The gamma-COPI is part of one of two subcomplexes that make up the heptameric coatomer complex along with the beta, delta and zeta subunits.


Pssm-ID: 406717  Cd Length: 114  Bit Score: 73.78  E-value: 5.22e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226705     1 MQSCKGTETVASNARSHTCLPSGLYIGNVKVLVKAQFGMdSSKEIVMKLAVRAEDPSVSDAIHALV 66
Cdd:pfam16381  50 MQPLEGSDVVPENASSHTLKLSGKFVGGGKVLVRARLAI-SSGGVTMKLTVRSESEEVCELVLSAV 114
 
Name Accession Description Interval E-value
Coatomer_g_Cpla pfam16381
Coatomer subunit gamma-1 C-terminal appendage platform; Coatomer_g_Cpla is the very C-terminal ...
 1-66 5.22e-19

Coatomer subunit gamma-1 C-terminal appendage platform; Coatomer_g_Cpla is the very C-terminal domain of the eukaryotic Coatomer subunit gamma-1 proteins. It acts as a platform domain to the C-terminal appendage. It carries one single protein/protein interaction site, which is the binding site for ARFGAP2 or ADP-ribosylation factor GTPase-activating protein. COPI-coated vesicles mediate retrograde transport from the Golgi back to the ER and intra-Golgi transport. The gamma-COPI is part of one of two subcomplexes that make up the heptameric coatomer complex along with the beta, delta and zeta subunits.


Pssm-ID: 406717  Cd Length: 114  Bit Score: 73.78  E-value: 5.22e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226705     1 MQSCKGTETVASNARSHTCLPSGLYIGNVKVLVKAQFGMdSSKEIVMKLAVRAEDPSVSDAIHALV 66
Cdd:pfam16381  50 MQPLEGSDVVPENASSHTLKLSGKFVGGGKVLVRARLAI-SSGGVTMKLTVRSESEEVCELVLSAV 114
 
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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