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Conserved domains on  [gi|767994952|ref|XP_011523176|]
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coatomer subunit zeta-2 isoform X4 [Homo sapiens]

Protein Classification

longin-like domain-containing protein( domain architecture ID 1000061)

longin-like domain-containing protein; 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
longin-like super family cl38905
Longin-like domains; Longin-like domains are small protein domains present in a variety of ...
 47-152 2.99e-50

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).


The actual alignment was detected with superfamily member cd14829:

Pssm-ID: 365781  Cd Length: 132  Bit Score: 158.48  E-value: 2.99e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952  47 KAVFILDNDGRRLLAKYYDDTFPSMKEQMVFEKNVFNKTSRTESEIAFFGGMTIVYKNSIDLFLYVVGSSYENELMLMSV 126
Cdd:cd14829    1 KAILILDNDGKRVLAKYYDDTFPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSSDENELILASV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767994952 127 LTCLFESLNHML--------------------------SVILESDPQQVIQK 152
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 ...
 47-152 2.99e-50

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: 158.48  E-value: 2.99e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952  47 KAVFILDNDGRRLLAKYYDDTFPSMKEQMVFEKNVFNKTSRTESEIAFFGGMTIVYKNSIDLFLYVVGSSYENELMLMSV 126
Cdd:cd14829    1 KAILILDNDGKRVLAKYYDDTFPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSSDENELILASV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767994952 127 LTCLFESLNHML--------------------------SVILESDPQQVIQK 152
Cdd:cd14829   81 LNCLYDALSLLLrknvekrallenldlvllaldeivdgGIILETDPTAIASR 132
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
45-173 3.66e-26

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 97.43  E-value: 3.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952   45 TIKAVFILDNDGRRLLAKYYDdTFPSMKEQMVFEKNVFNKTSRT--ESEIAFFGGMTIVYKNSIDLFLYVVGSSYENELM 122
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYT-PYSDPEQQKLIEQIYALISARKpkMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767994952  123 LMSVLTCLFESLNHMLSVILESDPQQVIQKVNFRAD---DGGLT-EQSVAQVLQS 173
Cdd:pfam01217  80 ILELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDemvMGGEIlETSKNEVLHR 134
RET3 COG5541
Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, ...
 42-184 4.87e-19

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


Pssm-ID: 227828  Cd Length: 187  Bit Score: 79.99  E-value: 4.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952  42 SLYTIKAVFILDNDGRRLLAKYYDDT---------FPSMKEQMVFEKNVFNKTSRTESEIAFFGGMTIVYKNSIDLFLYV 112
Cdd:COG5541    4 SLYDVEALLILDSQGERIYRKYYQPPhrseghqlvFNSVKKEKEFEKKLAEKTAKDRESILMFYDRLVMCKRLDDVLLYI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952 113 VGSSYENELMLMSVLTCLFESLNHMLS--------------------------VILESDPQQVIQKV----NFRADDGGL 162
Cdd:COG5541   84 VSPMEENEPFLGQVFDEIRAALILIVKtptdkrnvwenydqivllvdetidegVILETKSDEIADRVpkppNFEGQDGMK 163

                        170       180
                 ....*....|....*....|..
gi 767994952 163 TEQSVAQVLQSAKEQIKWSLLK 184
Cdd:COG5541  164 VPRGFASFLHKATKKLSERSNK 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 ...
 47-152 2.99e-50

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: 158.48  E-value: 2.99e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952  47 KAVFILDNDGRRLLAKYYDDTFPSMKEQMVFEKNVFNKTSRTESEIAFFGGMTIVYKNSIDLFLYVVGSSYENELMLMSV 126
Cdd:cd14829    1 KAILILDNDGKRVLAKYYDDTFPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSSDENELILASV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767994952 127 LTCLFESLNHML--------------------------SVILESDPQQVIQK 152
Cdd:cd14829   81 LNCLYDALSLLLrknvekrallenldlvllaldeivdgGIILETDPTAIASR 132
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
 47-174 1.60e-28

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: 102.98  E-value: 1.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952  47 KAVFILDNDGRRLLAKYYDDTFPSMKEQMVFEKNVFNKTSRTESEIAFFGGMTIVYKNSIDLFLYVVGSSYENELMLMSV 126
Cdd:cd14823    1 KAILVLDNDGKRLFAKYYDDTYPSVKEQKAFEKNIFNKKHRTDSEIVLLEGLRVVYKSSIDLYFVVIGSKNENELLLLEV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767994952 127 LTCLFESLNHMLSVILESDPQQVIQKVNFRAD---DGGLTEQSVAQVLQSA 174
Cdd:cd14823   81 LNCLVDVLSEYFRKVEERAILENFEGLYFALDeivDGGYIQETDPKQVVHF 131
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
45-173 3.66e-26

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 97.43  E-value: 3.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952   45 TIKAVFILDNDGRRLLAKYYDdTFPSMKEQMVFEKNVFNKTSRT--ESEIAFFGGMTIVYKNSIDLFLYVVGSSYENELM 122
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYT-PYSDPEQQKLIEQIYALISARKpkMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767994952  123 LMSVLTCLFESLNHMLSVILESDPQQVIQKVNFRAD---DGGLT-EQSVAQVLQS 173
Cdd:pfam01217  80 ILELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDemvMGGEIlETSKNEVLHR 134
longin-like cd14818
Longin-like domains; Longin-like domains are small protein domains present in a variety of ...
 47-138 2.05e-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: 79.11  E-value: 2.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952  47 KAVFILDNDGRRLLAKYYDDTFPSMKEQMVFEKNVFNKTSRTE--SEIAFFGGMTIVYKNSIDLFLYVVGSSYENELMLM 124
Cdd:cd14818    1 LQLAVFDPQGQVLAASNWLGKKPSVKFSLIQIKSFFSKLITSGfdFLTLTIGSYTFHYYLNKGLYFVVITDEQELRQELF 80

                         90
                 ....*....|....
gi 767994952 125 SVLTCLFESLNHML 138
Cdd:cd14818   81 QTLNLLLKEFNSLH 94
RET3 COG5541
Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, ...
 42-184 4.87e-19

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


Pssm-ID: 227828  Cd Length: 187  Bit Score: 79.99  E-value: 4.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952  42 SLYTIKAVFILDNDGRRLLAKYYDDT---------FPSMKEQMVFEKNVFNKTSRTESEIAFFGGMTIVYKNSIDLFLYV 112
Cdd:COG5541    4 SLYDVEALLILDSQGERIYRKYYQPPhrseghqlvFNSVKKEKEFEKKLAEKTAKDRESILMFYDRLVMCKRLDDVLLYI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952 113 VGSSYENELMLMSVLTCLFESLNHMLS--------------------------VILESDPQQVIQKV----NFRADDGGL 162
Cdd:COG5541   84 VSPMEENEPFLGQVFDEIRAALILIVKtptdkrnvwenydqivllvdetidegVILETKSDEIADRVpkppNFEGQDGMK 163

                        170       180
                 ....*....|....*....|..
gi 767994952 163 TEQSVAQVLQSAKEQIKWSLLK 184
Cdd:COG5541  164 VPRGFASFLHKATKKLSERSNK 185
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
 46-179 3.59e-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: 47.22  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952  46 IKAVFILDNDGRRLLAKYYDDTFPSMKEQMVfeKNVFNKTS-RTESEIAF------FGG--MTIVYKNSIDL-FLYVVGS 115
Cdd:cd14834    2 IKAILIFNNHGKPRLSKFYQHYSEEKQQQII--RETFQLVSkRDDNVCNFleggslIGGsdTKLIYRHYATLyFVFCVDS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767994952 116 SyENELMLMSVLTCLFESLNHMLSVILESDPQQVIQKVNFRADD---GGLT-EQSVAQVLQSAKEQIK 179
Cdd:cd14834   80 S-ESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEivmGGMVlETNMTEILTAIEEQNK 146
AP_sigma cd14827
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ...
 47-179 4.50e-06

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: 44.35  E-value: 4.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952  47 KAVFILDNDGRRLLAKYYDdTFPSmKEQMVFEKNVFNK-TSRTESEIAF--FGGMTIVYKNSIDLFLYVVGSSYENELML 123
Cdd:cd14827    1 RFILLFNRQGKTRLAKWYM-QFDD-DERQKLIEEIVQVvLSRDAKHCNFveFRNYKLIYRRYASLYFCICVDSNDNELAI 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952 124 MSVLTCLFESLNHMLSVILESDPQQVIQKVNFRADD----GGLTEQSVAQVLQSAKEQIK 179
Cdd:cd14827   79 LEAIHNFVETLDKYFENVCELDLIFNFEKVYFIVDEmvlgGEIRETSQTKILKQIEMLDK 138
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
 50-155 6.73e-06

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: 43.76  E-value: 6.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952  50 FIL--DNDGRRLLAKYYDdtFPSMKEQMVFEKNVFNKT-SRTESEIAF--FGGMTIVYKNSIDLFLYVVGSSYENELMLM 124
Cdd:cd14832    2 FILmvNKQGQTRLAQYYE--FLSIEERVALEGEIIRKClSRSEKQCSFleYRGYKLVYRRYASLYFIVGVDEDENELAIL 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767994952 125 SVLTCLFESLNHMLSVILESDPQQVIQKVNF 155
Cdd:cd14832   80 EFIHNLVETLDKYFENVCELDIMFNLEKAHF 110
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
46-135 2.11e-03

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 37.01  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994952  46 IKAVFILDNDGRRLLAKYYddTFPSMKEQMVFEKNVFNKTS---RTESEIAFFGGMTIVYKNSIDLFLYVVGSSYENELM 122
Cdd:COG5030    2 IKFVLIFNRQGKPRLVKWY--TPVSDPEQAKLIADIYELISarkPKESNFIEGKNEKIVYRRYATLYFVFGVDNDDNELI 79

                         90
                 ....*....|...
gi 767994952 123 LMSVLTCLFESLN 135
Cdd:COG5030   80 ILELIHNFVEILD 92
 
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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