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Conserved domains on  [gi|24665461|ref|NP_730188|]
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coat protein (coatomer) zeta, isoform C [Drosophila melanogaster]

Protein Classification

coatomer subunit zeta( domain architecture ID 13000590)

coatomer subunit zeta is a component of the coatomer, a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Zeta-COP cd14829
zeta subunit of the F-COPI complex; Zeta subunit of the heterotetrameric F-COPI complex, which ...
 1-131 1.99e-74

zeta subunit of the F-COPI complex; Zeta 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: 341433  Cd Length: 132  Bit Score: 218.57  E-value: 1.99e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461   1 MCIMDNDGNRILAKYYDKNiLSTLKEQKAFEKNLFNKTHRSNTEIIMLDGLTCVYKSNVDLFFYVMGNAYENELILLSVL 80
Cdd:cd14829   3 ILILDNDGKRVLAKYYDDT-FPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSSDENELILASVL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 24665461  81 NCLYDSISLILKKNVEKRLVLENLEIIMLAFDEICDGGIILDADPSSVVKR 131
Cdd:cd14829  82 NCLYDALSLLLRKNVEKRALLENLDLVLLALDEIVDGGIILETDPTAIASR 132
 
Name Accession Description Interval E-value
Zeta-COP cd14829
zeta subunit of the F-COPI complex; Zeta subunit of the heterotetrameric F-COPI complex, which ...
 1-131 1.99e-74

zeta subunit of the F-COPI complex; Zeta 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: 341433  Cd Length: 132  Bit Score: 218.57  E-value: 1.99e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461   1 MCIMDNDGNRILAKYYDKNiLSTLKEQKAFEKNLFNKTHRSNTEIIMLDGLTCVYKSNVDLFFYVMGNAYENELILLSVL 80
Cdd:cd14829   3 ILILDNDGKRVLAKYYDDT-FPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSSDENELILASVL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 24665461  81 NCLYDSISLILKKNVEKRLVLENLEIIMLAFDEICDGGIILDADPSSVVKR 131
Cdd:cd14829  82 NCLYDALSLLLRKNVEKRALLENLDLVLLALDEIVDGGIILETDPTAIASR 132
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-138 4.19e-28

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 101.66  E-value: 4.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461     1 MCIMDNDGNRILAKYYDKniLSTLKEQKAFEKNLFNKTHRS--NTEIIMLDGLTCVYKSNVDLFFYVMGNAYENELILLS 78
Cdd:pfam01217   5 ILIFNRQGKPRLAKWYTP--YSDPEQQKLIEQIYALISARKpkMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELIILE 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461    79 VLNCLYDSISLILkKNVEKRLVLENLEIIMLAFDEICDGGIILDADPSSVVKRVDLRNDD 138
Cdd:pfam01217  83 LIHRFVESLDRYF-GNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDEL 141
RET3 COG5541
Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, ...
 3-163 3.60e-26

Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227828  Cd Length: 187  Bit Score: 97.71  E-value: 3.60e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461   3 IMDNDGNRILAKYY--------DKNILSTLKEQKAFEKNLFNKTHRSNTEIIMLDGLTCVYKSNVDLFFYVMGNAYENEL 74
Cdd:COG5541  13 ILDSQGERIYRKYYqpphrsegHQLVFNSVKKEKEFEKKLAEKTAKDRESILMFYDRLVMCKRLDDVLLYIVSPMEENEP 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461  75 ILLSVLNCLYDSISLILKKNVEKRLVLENLEIIMLAFDEICDGGIILDADPSSVVKRVDLRNDDIPIA----EQTVAQVL 150
Cdd:COG5541  93 FLGQVFDEIRAALILIVKTPTDKRNVWENYDQIVLLVDETIDEGVILETKSDEIADRVPKPPNFEGQDgmkvPRGFASFL 172

                       170
                ....*....|...
gi 24665461 151 QSAREQLKWSILK 163
Cdd:COG5541 173 HKATKKLSERSNK 185
 
Name Accession Description Interval E-value
Zeta-COP cd14829
zeta subunit of the F-COPI complex; Zeta subunit of the heterotetrameric F-COPI complex, which ...
 1-131 1.99e-74

zeta subunit of the F-COPI complex; Zeta 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: 341433  Cd Length: 132  Bit Score: 218.57  E-value: 1.99e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461   1 MCIMDNDGNRILAKYYDKNiLSTLKEQKAFEKNLFNKTHRSNTEIIMLDGLTCVYKSNVDLFFYVMGNAYENELILLSVL 80
Cdd:cd14829   3 ILILDNDGKRVLAKYYDDT-FPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSSDENELILASVL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 24665461  81 NCLYDSISLILKKNVEKRLVLENLEIIMLAFDEICDGGIILDADPSSVVKR 131
Cdd:cd14829  82 NCLYDALSLLLRKNVEKRALLENLDLVLLALDEIVDGGIILETDPTAIASR 132
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
 3-131 3.64e-31

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: 109.14  E-value: 3.64e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461   3 IMDNDGNRILAKYYDKNILSTlKEQKAFEKNLFNKTHRSNTEIIMLDGLTCVYKSNVDLFFYVMGNAYENELILLSVLNC 82
Cdd:cd14823   5 VLDNDGKRLFAKYYDDTYPSV-KEQKAFEKNIFNKKHRTDSEIVLLEGLRVVYKSSIDLYFVVIGSKNENELLLLEVLNC 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 24665461  83 LYDSISLILkKNVEKRLVLENLEIIMLAFDEICDGGIILDADPSSVVKR 131
Cdd:cd14823  84 LVDVLSEYF-RKVEERAILENFEGLYFALDEIVDGGYIQETDPKQVVHF 131
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-138 4.19e-28

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 101.66  E-value: 4.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461     1 MCIMDNDGNRILAKYYDKniLSTLKEQKAFEKNLFNKTHRS--NTEIIMLDGLTCVYKSNVDLFFYVMGNAYENELILLS 78
Cdd:pfam01217   5 ILIFNRQGKPRLAKWYTP--YSDPEQQKLIEQIYALISARKpkMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELIILE 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461    79 VLNCLYDSISLILkKNVEKRLVLENLEIIMLAFDEICDGGIILDADPSSVVKRVDLRNDD 138
Cdd:pfam01217  83 LIHRFVESLDRYF-GNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDEL 141
RET3 COG5541
Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, ...
 3-163 3.60e-26

Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227828  Cd Length: 187  Bit Score: 97.71  E-value: 3.60e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461   3 IMDNDGNRILAKYY--------DKNILSTLKEQKAFEKNLFNKTHRSNTEIIMLDGLTCVYKSNVDLFFYVMGNAYENEL 74
Cdd:COG5541  13 ILDSQGERIYRKYYqpphrsegHQLVFNSVKKEKEFEKKLAEKTAKDRESILMFYDRLVMCKRLDDVLLYIVSPMEENEP 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461  75 ILLSVLNCLYDSISLILKKNVEKRLVLENLEIIMLAFDEICDGGIILDADPSSVVKRVDLRNDDIPIA----EQTVAQVL 150
Cdd:COG5541  93 FLGQVFDEIRAALILIVKTPTDKRNVWENYDQIVLLVDETIDEGVILETKSDEIADRVPKPPNFEGQDgmkvPRGFASFL 172

                       170
                ....*....|...
gi 24665461 151 QSAREQLKWSILK 163
Cdd:COG5541 173 HKATKKLSERSNK 185
longin-like cd14818
Longin-like domains; Longin-like domains are small protein domains present in a variety of ...
 3-114 7.44e-19

Longin-like domains; Longin-like domains are small protein domains present in a variety of proteins and members of protein complexes involved in or required for different steps during the transport of proteins from the ribosome to the ER to the plasma membrane, via the Golgi apparatus. Examples are mu and sigma subunits of the heterotetrameric adaptor protein (AP) complex, zeta and delta subunits of the heterotetrameric F-COPI complex, a subgroup of R-SNARE proteins, a subfamily of the transport protein particle (TRAPP), and the signal recognition particle receptor subunit alpha (SR-alpha).


Pssm-ID: 341426  Cd Length: 117  Bit Score: 77.18  E-value: 7.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461   3 IMDNDGNRILAKYYDKNiLSTLKEQKAFEKNLFNKTHRS--NTEIIMLDGLTCVYKSNVDLFFYVMGNAYENELILLSVL 80
Cdd:cd14818   5 VFDPQGQVLAASNWLGK-KPSVKFSLIQIKSFFSKLITSgfDFLTLTIGSYTFHYYLNKGLYFVVITDEQELRQELFQTL 83

                        90       100       110
                ....*....|....*....|....*....|....
gi 24665461  81 NCLYDSISLILKKNVEKRLVLENLEIIMLAFDEI 114
Cdd:cd14818  84 NLLLKEFNSLHGSEVITKNIEDDLEEFESYLDIK 117
AP_Mu_N cd14828
AP complex subunit mu N-terminal domain; AP complex mu subunits are part of the ...
 2-126 8.42e-04

AP complex subunit mu N-terminal domain; AP complex mu 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 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: 341432  Cd Length: 136  Bit Score: 37.56  E-value: 8.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461   2 CIMDNDGNRILAKYYdKNILSTLKEQKAFEKNLFNKTHRSNTEIIMLDGLTCVYKSNVDLFFYVMGNAYENELILLSVLN 81
Cdd:cd14828   4 YILDENLEPLISRNY-RADINLQSVVQDFFKAYKKLNPEERPPIISSNGWNFIYIKRDDLYFVSVTQTNVNLMSVLVFLD 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24665461  82 CLYDSISLILK-KNVEKRLVLENLEIIMLAFDEICDGGIILDADPS 126
Cdd:cd14828  83 QFYDLLKDYFGvKKLDKNSIIDNFVLIYELIDESIDFGIIQLTDYN 128
AP_sigma cd14827
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ...
 3-136 5.15e-03

AP complex subunit sigma; 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: 341431  Cd Length: 138  Bit Score: 35.49  E-value: 5.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665461   3 IMDNDGNRILAKYYdknILSTLKEQKAFEKNLFNKTHRSN---TEIIMLDGLTCVYKSNVDLFFYVMGNAYENELILLSV 79
Cdd:cd14827   5 LFNRQGKTRLAKWY---MQFDDDERQKLIEEIVQVVLSRDakhCNFVEFRNYKLIYRRYASLYFCICVDSNDNELAILEA 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24665461  80 LNCLYDSISLILKKNVEKRLVLeNLEIIMLAFDEICDGGIILDADPSSVVKRVDLRN 136
Cdd:cd14827  82 IHNFVETLDKYFENVCELDLIF-NFEKVYFIVDEMVLGGEIRETSQTKILKQIEMLD 137
 
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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