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Conserved domains on  [gi|677425256|gb|KFQ27627|]
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Coatomer subunit delta, partial [Merops nubicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Delta_COP_N cd14830
delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric ...
 4-133 8.09e-94

delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric F-COPI complex, which consists of one beta-, one gamma-, one delta-, and one zeta subunit, where beta- and gamma- subunits are related to the large adaptor protein (AP) complex subunits, and delta- and zeta- subunits are related to the medium and small AP subunits, respectively. F-COPI forms a coatomer together with the B-COPI subcomplex, which assembles with a small GTPase, ADP-ribosylation factor 1 (ARF1), playing an important role in the formation of COPI complex-coated vesicles. COPI complex-coated vesicles function in the early secretory pathway mediating the retrograde transport from the Golgi to the ER, and intra-Golgi transport.


:

Pssm-ID: 341434  Cd Length: 130  Bit Score: 272.09  E-value: 8.09e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677425256   4 LAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETL 83
Cdd:cd14830    1 LSAAICTKGGKILVSRQFVEISRSRIEGLLAAFPKLVGSGSQHTYVETENVRYVYQPLEDLYLVLITTKNSNILEDLETL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 677425256  84 RLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTF 133
Cdd:cd14830   81 RLLSRVVPEYCPSVDEEEILKNAFDLIFAFDEVISLGYRENVTLSQIKTF 130
 
Name Accession Description Interval E-value
Delta_COP_N cd14830
delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric ...
 4-133 8.09e-94

delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric F-COPI complex, which consists of one beta-, one gamma-, one delta-, and one zeta subunit, where beta- and gamma- subunits are related to the large adaptor protein (AP) complex subunits, and delta- and zeta- subunits are related to the medium and small AP subunits, respectively. F-COPI forms a coatomer together with the B-COPI subcomplex, which assembles with a small GTPase, ADP-ribosylation factor 1 (ARF1), playing an important role in the formation of COPI complex-coated vesicles. COPI complex-coated vesicles function in the early secretory pathway mediating the retrograde transport from the Golgi to the ER, and intra-Golgi transport.


Pssm-ID: 341434  Cd Length: 130  Bit Score: 272.09  E-value: 8.09e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677425256   4 LAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETL 83
Cdd:cd14830    1 LSAAICTKGGKILVSRQFVEISRSRIEGLLAAFPKLVGSGSQHTYVETENVRYVYQPLEDLYLVLITTKNSNILEDLETL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 677425256  84 RLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTF 133
Cdd:cd14830   81 RLLSRVVPEYCPSVDEEEILKNAFDLIFAFDEVISLGYRENVTLSQIKTF 130
 
Name Accession Description Interval E-value
Delta_COP_N cd14830
delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric ...
 4-133 8.09e-94

delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric F-COPI complex, which consists of one beta-, one gamma-, one delta-, and one zeta subunit, where beta- and gamma- subunits are related to the large adaptor protein (AP) complex subunits, and delta- and zeta- subunits are related to the medium and small AP subunits, respectively. F-COPI forms a coatomer together with the B-COPI subcomplex, which assembles with a small GTPase, ADP-ribosylation factor 1 (ARF1), playing an important role in the formation of COPI complex-coated vesicles. COPI complex-coated vesicles function in the early secretory pathway mediating the retrograde transport from the Golgi to the ER, and intra-Golgi transport.


Pssm-ID: 341434  Cd Length: 130  Bit Score: 272.09  E-value: 8.09e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677425256   4 LAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETL 83
Cdd:cd14830    1 LSAAICTKGGKILVSRQFVEISRSRIEGLLAAFPKLVGSGSQHTYVETENVRYVYQPLEDLYLVLITTKNSNILEDLETL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 677425256  84 RLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTF 133
Cdd:cd14830   81 RLLSRVVPEYCPSVDEEEILKNAFDLIFAFDEVISLGYRENVTLSQIKTF 130
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
 4-133 1.08e-57

Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341427  Cd Length: 131  Bit Score: 180.41  E-value: 1.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677425256   4 LAAAVCTKAGKAIVSRQFVEMTRtrIEGLLAAFPKLMNTGK---QHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDL 80
Cdd:cd14823    1 KAILVLDNDGKRLFAKYYDDTYP--SVKEQKAFEKNIFNKKhrtDSEIVLLEGLRVVYKSSIDLYFVVIGSKNENELLLL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 677425256  81 ETLRLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTF 133
Cdd:cd14823   79 EVLNCLVDVLSEYFRKVEERAILENFEGLYFALDEIVDGGYIQETDPKQVVHF 131
AP1_Mu_N cd14835
AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the ...
 13-121 1.89e-04

AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large gamma-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-1 the coat protein is clathrin. AP-1 binds the phospholipid PI(4)P which plays a role in its localisation to the trans-Golgi network (TGN)/endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341439  Cd Length: 139  Bit Score: 40.61  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677425256  13 GKAIVSRQF---VEMTrtriegLLAAFPKLMN----TGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETLRL 85
Cdd:cd14835   10 GKVLISRNYrgdVPMS------VIEKFMPLLMekeeEGNLTPILTDGGVTYIYIKHNNLYLLAVTKKNANAAMVLSFLYK 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 677425256  86 FSRVIPEYCRALEENEISEHcFDLIFA-FDEIVALGY 121
Cdd:cd14835   84 LVEVFKEYFKELEEESIRDN-FVIIYElLDEMMDFGY 119
AP2_Mu_N cd14836
AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the ...
 52-133 1.94e-03

AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-2 complex which consists of one large alpha-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-2 the coat protein is clathrin. AP-2 binds the phospholipid PI(4,5)P2 which is important for its localisation to the plasma membrane. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341440  Cd Length: 140  Bit Score: 37.50  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677425256  52 ESVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRVIPEYCRALEENEISEHcFDLIFA-FDEIVALGYRENVNLAQI 130
Cdd:cd14836   51 GSTSFFHVRHGNLYLVAVTRSNVNAAMVFEFLYKLVQLFKSYFGKFNEDSIKNN-FVLIYElLDEILDFGYPQNTEPEAL 129


                 ...
gi 677425256 131 RTF 133
Cdd:cd14836  130 KTY 132
 
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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