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Conserved domains on  [gi|414144872|ref|NP_001258664|]
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coatomer subunit zeta-1 isoform 3 [Homo sapiens]

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 ...
 14-145 1.24e-81

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: 236.67  E-value: 1.24e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872  14 KAILILDNDGDRLFAKYYDDTYPSVKEQKAFEKNIFNKTHRTDSEIALLEGLTVVYKSSIDLYFYVIGSSYENELMLMAV 93
Cdd:cd14829    1 KAILILDNDGKRVLAKYYDDTFPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSSDENELILASV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 414144872  94 LNCLFDSLSQMLRKNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHR 145
Cdd:cd14829   81 LNCLYDALSLLLRKNVEKRALLENLDLVLLALDEIVDGGIILETDPTAIASR 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 ...
 14-145 1.24e-81

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: 236.67  E-value: 1.24e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872  14 KAILILDNDGDRLFAKYYDDTYPSVKEQKAFEKNIFNKTHRTDSEIALLEGLTVVYKSSIDLYFYVIGSSYENELMLMAV 93
Cdd:cd14829    1 KAILILDNDGKRVLAKYYDDTFPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSSDENELILASV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 414144872  94 LNCLFDSLSQMLRKNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHR 145
Cdd:cd14829   81 LNCLYDALSLLLRKNVEKRALLENLDLVLLALDEIVDGGIILETDPTAIASR 132
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
12-148 1.77e-51

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 160.99  E-value: 1.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872   12 TVKAILILDNDGDRLFAKYYDdTYPSVKEQKAFEKNIFNKTHRT--DSEIALLEGLTVVYKSSIDLYFYVIGSSYENELM 89
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYT-PYSDPEQQKLIEQIYALISARKpkMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 414144872   90 LMAVLNCLFDSLSQMLRkNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHRVLQ 148
Cdd:pfam01217  80 ILELIHRFVESLDRYFG-NVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVAL 137
RET3 COG5541
Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, ...
 9-146 7.96e-34

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


Pssm-ID: 227828  Cd Length: 187  Bit Score: 117.35  E-value: 7.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872   9 SLYTVKAILILDNDGDRLFAKYYDDT---------YPSVKEQKAFEKNIFNKTHRTDSEIALLEGLTVVYKSSIDLYFYV 79
Cdd:COG5541    4 SLYDVEALLILDSQGERIYRKYYQPPhrseghqlvFNSVKKEKEFEKKLAEKTAKDRESILMFYDRLVMCKRLDDVLLYI 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 414144872  80 IGSSYENELMLMAVLNCLFDSLSQMLRKNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHRV 146
Cdd:COG5541   84 VSPMEENEPFLGQVFDEIRAALILIVKTPTDKRNVWENYDQIVLLVDETIDEGVILETKSDEIADRV 150
 
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 ...
 14-145 1.24e-81

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: 236.67  E-value: 1.24e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872  14 KAILILDNDGDRLFAKYYDDTYPSVKEQKAFEKNIFNKTHRTDSEIALLEGLTVVYKSSIDLYFYVIGSSYENELMLMAV 93
Cdd:cd14829    1 KAILILDNDGKRVLAKYYDDTFPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSSDENELILASV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 414144872  94 LNCLFDSLSQMLRKNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHR 145
Cdd:cd14829   81 LNCLYDALSLLLRKNVEKRALLENLDLVLLALDEIVDGGIILETDPTAIASR 132
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
 14-145 5.14e-56

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: 171.93  E-value: 5.14e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872  14 KAILILDNDGDRLFAKYYDDTYPSVKEQKAFEKNIFNKTHRTDSEIALLEGLTVVYKSSIDLYFYVIGSSYENELMLMAV 93
Cdd:cd14823    1 KAILVLDNDGKRLFAKYYDDTYPSVKEQKAFEKNIFNKKHRTDSEIVLLEGLRVVYKSSIDLYFVVIGSKNENELLLLEV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 414144872  94 LNCLFDSLSQMLRkNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHR 145
Cdd:cd14823   81 LNCLVDVLSEYFR-KVEERAILENFEGLYFALDEIVDGGYIQETDPKQVVHF 131
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
12-148 1.77e-51

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 160.99  E-value: 1.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872   12 TVKAILILDNDGDRLFAKYYDdTYPSVKEQKAFEKNIFNKTHRT--DSEIALLEGLTVVYKSSIDLYFYVIGSSYENELM 89
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYT-PYSDPEQQKLIEQIYALISARKpkMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 414144872   90 LMAVLNCLFDSLSQMLRkNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHRVLQ 148
Cdd:pfam01217  80 ILELIHRFVESLDRYFG-NVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVAL 137
longin-like cd14818
Longin-like domains; Longin-like domains are small protein domains present in a variety of ...
 14-128 1.14e-38

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: 127.64  E-value: 1.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872  14 KAILILDNDGDRLFAKYYDDTYPSVKEQKAFEKNIFNKTHR--TDSEIALLEGLTVVYKSSIDLYFYVIGSSYENELMLM 91
Cdd:cd14818    1 LQLAVFDPQGQVLAASNWLGKKPSVKFSLIQIKSFFSKLITsgFDFLTLTIGSYTFHYYLNKGLYFVVITDEQELRQELF 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 414144872  92 AVLNCLFDSLSQMLRKNVEKRALLENMEGLFLAVDEI 128
Cdd:cd14818   81 QTLNLLLKEFNSLHGSEVITKNIEDDLEEFESYLDIK 117
RET3 COG5541
Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, ...
 9-146 7.96e-34

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


Pssm-ID: 227828  Cd Length: 187  Bit Score: 117.35  E-value: 7.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872   9 SLYTVKAILILDNDGDRLFAKYYDDT---------YPSVKEQKAFEKNIFNKTHRTDSEIALLEGLTVVYKSSIDLYFYV 79
Cdd:COG5541    4 SLYDVEALLILDSQGERIYRKYYQPPhrseghqlvFNSVKKEKEFEKKLAEKTAKDRESILMFYDRLVMCKRLDDVLLYI 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 414144872  80 IGSSYENELMLMAVLNCLFDSLSQMLRKNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHRV 146
Cdd:COG5541   84 VSPMEENEPFLGQVFDEIRAALILIVKTPTDKRNVWENYDQIVLLVDETIDEGVILETKSDEIADRV 150
AP_sigma cd14827
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ...
 14-151 7.60e-10

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: 53.98  E-value: 7.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872  14 KAILILDNDGDRLFAKYYddTYPSVKEQKAFEKNIFNK-THRTDSEIALLE--GLTVVYKSSIDLYFYVIGSSYENELML 90
Cdd:cd14827    1 RFILLFNRQGKTRLAKWY--MQFDDDERQKLIEEIVQVvLSRDAKHCNFVEfrNYKLIYRRYASLYFCICVDSNDNELAI 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 414144872  91 MAVLNCLFDSLSQMLrKNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHRVLQSAK 151
Cdd:cd14827   79 LEAIHNFVETLDKYF-ENVCELDLIFNFEKVYFIVDEMVLGGEIRETSQTKILKQIEMLDK 138
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
13-152 3.56e-08

Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];


Pssm-ID: 227363  Cd Length: 152  Bit Score: 49.72  E-value: 3.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872  13 VKAILILDNDGDRLFAKYYddTYPSVKEQKAFEKNIFNK-THRTDSEIALLEG--LTVVYKSSIDLYFYVIGSSYENELM 89
Cdd:COG5030    2 IKFVLIFNRQGKPRLVKWY--TPVSDPEQAKLIADIYELiSARKPKESNFIEGknEKIVYRRYATLYFVFGVDNDDNELI 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 414144872  90 LMAVLNCLFDSLSQMLrKNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHRVLQSAKE 152
Cdd:COG5030   80 ILELIHNFVEILDRFF-GNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAE 141
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
 13-146 1.22e-07

AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, 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. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341438  Cd Length: 146  Bit Score: 47.99  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872  13 VKAILILDNDGDRLFAKYYDDtYPSVKEQKAFEKNIFNKTHRTDSEIALLEG--------LTVVYKSSIDLYFYVIGSSY 84
Cdd:cd14834    2 IKAILIFNNHGKPRLSKFYQH-YSEEKQQQIIRETFQLVSKRDDNVCNFLEGgsliggsdTKLIYRHYATLYFVFCVDSS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 414144872  85 ENELMLMAVLNCLFDSLSQMLrKNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHRV 146
Cdd:cd14834   81 ESELGILDLIQVFVETLDKCF-ENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTAI 141
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
 14-147 6.99e-07

AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large epsilon-, 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. AP-4 does not bind the coat protein clathrin, it is associated with nonclathrin coats. Its phospholipid binding partner is unknown and it is localized in the trans-Golgi network (TGN). The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341436  Cd Length: 138  Bit Score: 46.07  E-value: 6.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872  14 KAILILDNDGDRLFAKYYDdtYPSVKEQKAFEKNIFNKT-HRTDSEIALLE--GLTVVYKSSIDLYFYVIGSSYENELML 90
Cdd:cd14832    1 KFILMVNKQGQTRLAQYYE--FLSIEERVALEGEIIRKClSRSEKQCSFLEyrGYKLVYRRYASLYFIVGVDEDENELAI 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 414144872  91 MAVLNCLFDSLSQMLrKNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHRVL 147
Cdd:cd14832   79 LEFIHNLVETLDKYF-ENVCELDIMFNLEKAHFILDEMVMNGCIVETNKSNILAPIL 134
AP2_Mu_N cd14836
AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the ...
 15-148 4.28e-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: 35.58  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414144872  15 AILILDNDGDRLFAKYY-DDTYPSVKEqkAFEKNIFNKTHRTDSEIALLEGLTVVYKSSIDLYFYVIGSSYENELMLMAV 93
Cdd:cd14836    4 ALFIYNLKGDVLISRTYrDDVKRSVAD--AFRVQVINAKEQVRSPVLTIGSTSFFHVRHGNLYLVAVTRSNVNAAMVFEF 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 414144872  94 LNCLFDSLSQMLRKNVEKrALLENMEGLFLAVDEIVDGGVILESDPQQVVHRVLQ 148
Cdd:cd14836   82 LYKLVQLFKSYFGKFNED-SIKNNFVLIYELLDEILDFGYPQNTEPEALKTYITQ 135
 
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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