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Conserved domains on  [gi|12060841|gb|AAG48262|]
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serologically defined breast cancer antigen NY-BR-73, partial [Homo sapiens]

Protein Classification

COP-gamma_platf and Coatomer_g_Cpla domain-containing protein( domain architecture ID 13568584)

COP-gamma_platf and Coatomer_g_Cpla domain-containing protein

Graphical summary

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List of domain hits

 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 ...
 75-187 8.42e-53

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: 164.31  E-value: 8.42e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12060841    75 SDHIQKVLKPNFAAAWEEVGDTFEKEETFALSSTKTLEEAVNNIITFLGMQPCERSDKVPENKNSHSLYLAGIFRGGYDL 154
Cdd:pfam16381   1 GDYIQPVFVGNFAAAWDELPSEGEASETFALSSVKSLQEAVDKLIELLGMQPLEGSDVVPENASSHTLKLSGKFVGGGKV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 12060841   155 LVRSRLALAD-GVTMQVTVRSKERTPVDVILASV 187
Cdd:pfam16381  81 LVRARLAISSgGVTMKLTVRSESEEVCELVLSAV 114
COP-gamma_platf super family cl37786
Coatomer gamma subunit appendage platform subdomain; COPI-coated vesicles function in ...
 1-73 1.27e-33

Coatomer gamma subunit appendage platform subdomain; COPI-coated vesicles function in retrograde transport from the Golgi to the ER, and in intra-Golgi transport. This is the platform subdomain of the coatomer gamma subunit appendage domain. It carries a protein-protein interaction site at UniProt:P53620, residue W776, which in yeast binds to the ARFGAP Glo3p, and in mammalian gamma-COP binds to a Glo3p orthologue, ARFGAP2.


The actual alignment was detected with superfamily member pfam08752:

Pssm-ID: 462588  Cd Length: 149  Bit Score: 116.87  E-value: 1.27e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12060841     1 YEVLSCIPAPSLPYNQPGICYTLVRLPD-DDPTAVAGSFSCTMKFTVRDCDPNTGVPDEDGYDDEYVLEDLEVT 73
Cdd:pfam08752  76 FEDVFIIPIPSLPPNEPGSVYVSFERPDpEEEYLVSGTFSNTLKFTVKEIDPSTGEPEEEGYEDEYQLEDLELT 149
 
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 ...
 75-187 8.42e-53

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: 164.31  E-value: 8.42e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12060841    75 SDHIQKVLKPNFAAAWEEVGDTFEKEETFALSSTKTLEEAVNNIITFLGMQPCERSDKVPENKNSHSLYLAGIFRGGYDL 154
Cdd:pfam16381   1 GDYIQPVFVGNFAAAWDELPSEGEASETFALSSVKSLQEAVDKLIELLGMQPLEGSDVVPENASSHTLKLSGKFVGGGKV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 12060841   155 LVRSRLALAD-GVTMQVTVRSKERTPVDVILASV 187
Cdd:pfam16381  81 LVRARLAISSgGVTMKLTVRSESEEVCELVLSAV 114
COP-gamma_platf pfam08752
Coatomer gamma subunit appendage platform subdomain; COPI-coated vesicles function in ...
 1-73 1.27e-33

Coatomer gamma subunit appendage platform subdomain; COPI-coated vesicles function in retrograde transport from the Golgi to the ER, and in intra-Golgi transport. This is the platform subdomain of the coatomer gamma subunit appendage domain. It carries a protein-protein interaction site at UniProt:P53620, residue W776, which in yeast binds to the ARFGAP Glo3p, and in mammalian gamma-COP binds to a Glo3p orthologue, ARFGAP2.


Pssm-ID: 462588  Cd Length: 149  Bit Score: 116.87  E-value: 1.27e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12060841     1 YEVLSCIPAPSLPYNQPGICYTLVRLPD-DDPTAVAGSFSCTMKFTVRDCDPNTGVPDEDGYDDEYVLEDLEVT 73
Cdd:pfam08752  76 FEDVFIIPIPSLPPNEPGSVYVSFERPDpEEEYLVSGTFSNTLKFTVKEIDPSTGEPEEEGYEDEYQLEDLELT 149
SEC21 COG5240
Vesicle coat complex COPI, gamma subunit [Intracellular trafficking and secretion];
2-183 6.60e-15

Vesicle coat complex COPI, gamma subunit [Intracellular trafficking and secretion];


Pssm-ID: 227565 [Multi-domain]  Cd Length: 898  Bit Score: 71.95  E-value: 6.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12060841   2 EVLSCIPAPSLPYNQPGICYTLVRLPDDDPtaVAGSFSCTMKFTVRDCDPNTGVPDEDGYDDEYVLEDLEVTVSDHIQKV 81
Cdd:COG5240 715 KKEESIKVDQIDSSEGTLSIVRFKKLDWDI--EEGYVVNGLFFTTKEIEGDTSEPEDEGFQDEYSIDPFQITAGDFVRPV 792

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12060841  82 LKPNFAAAWeevgDTFEKEETFAL--SSTKTLEEAVNNIITFLGMQPCErSDKVPENKNSHSLYLAGIFRGGYDLLVRSR 159
Cdd:COG5240 793 RIKNFPATF----DRLKREITFVLqgDIYASGKKILDKILLNSMKIPTE-ETETPNDSNTHVMKLNGKAYHGTKVSIRVK 867

                       170       180
                ....*....|....*....|....*.
gi 12060841 160 LA--LADGVTMQVTVRSKERTPVDVI 183
Cdd:COG5240 868 MVysMACGCTVKVYCDGESLYVTQLV 893
ASKHA_NBD_HSP70_HSPA12 cd10229
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ...
 63-148 5.93e-03

nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B.


Pssm-ID: 466827 [Multi-domain]  Cd Length: 372  Bit Score: 36.49  E-value: 5.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12060841  63 DEYVLEDLEVTVSDHIQKVLKPNFAAAWEEVGDTFE-KEETFALSSTKTL-----EEAVNNIITFLGMQPCErsdkvPEN 136
Cdd:cd10229 248 DEEFEELLEEIFGDDFMEAFKQKYPSDYLDLLQAFErKKRSFKLRLSPELmkslfDPVVKKIIEHIKELLEK-----PEL 322

                        90
                ....*....|..
gi 12060841 137 KNSHSLYLAGIF 148
Cdd:cd10229 323 KGVDYIFLVGGF 334
 
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 ...
 75-187 8.42e-53

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: 164.31  E-value: 8.42e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12060841    75 SDHIQKVLKPNFAAAWEEVGDTFEKEETFALSSTKTLEEAVNNIITFLGMQPCERSDKVPENKNSHSLYLAGIFRGGYDL 154
Cdd:pfam16381   1 GDYIQPVFVGNFAAAWDELPSEGEASETFALSSVKSLQEAVDKLIELLGMQPLEGSDVVPENASSHTLKLSGKFVGGGKV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 12060841   155 LVRSRLALAD-GVTMQVTVRSKERTPVDVILASV 187
Cdd:pfam16381  81 LVRARLAISSgGVTMKLTVRSESEEVCELVLSAV 114
COP-gamma_platf pfam08752
Coatomer gamma subunit appendage platform subdomain; COPI-coated vesicles function in ...
 1-73 1.27e-33

Coatomer gamma subunit appendage platform subdomain; COPI-coated vesicles function in retrograde transport from the Golgi to the ER, and in intra-Golgi transport. This is the platform subdomain of the coatomer gamma subunit appendage domain. It carries a protein-protein interaction site at UniProt:P53620, residue W776, which in yeast binds to the ARFGAP Glo3p, and in mammalian gamma-COP binds to a Glo3p orthologue, ARFGAP2.


Pssm-ID: 462588  Cd Length: 149  Bit Score: 116.87  E-value: 1.27e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12060841     1 YEVLSCIPAPSLPYNQPGICYTLVRLPD-DDPTAVAGSFSCTMKFTVRDCDPNTGVPDEDGYDDEYVLEDLEVT 73
Cdd:pfam08752  76 FEDVFIIPIPSLPPNEPGSVYVSFERPDpEEEYLVSGTFSNTLKFTVKEIDPSTGEPEEEGYEDEYQLEDLELT 149
SEC21 COG5240
Vesicle coat complex COPI, gamma subunit [Intracellular trafficking and secretion];
2-183 6.60e-15

Vesicle coat complex COPI, gamma subunit [Intracellular trafficking and secretion];


Pssm-ID: 227565 [Multi-domain]  Cd Length: 898  Bit Score: 71.95  E-value: 6.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12060841   2 EVLSCIPAPSLPYNQPGICYTLVRLPDDDPtaVAGSFSCTMKFTVRDCDPNTGVPDEDGYDDEYVLEDLEVTVSDHIQKV 81
Cdd:COG5240 715 KKEESIKVDQIDSSEGTLSIVRFKKLDWDI--EEGYVVNGLFFTTKEIEGDTSEPEDEGFQDEYSIDPFQITAGDFVRPV 792

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12060841  82 LKPNFAAAWeevgDTFEKEETFAL--SSTKTLEEAVNNIITFLGMQPCErSDKVPENKNSHSLYLAGIFRGGYDLLVRSR 159
Cdd:COG5240 793 RIKNFPATF----DRLKREITFVLqgDIYASGKKILDKILLNSMKIPTE-ETETPNDSNTHVMKLNGKAYHGTKVSIRVK 867

                       170       180
                ....*....|....*....|....*.
gi 12060841 160 LA--LADGVTMQVTVRSKERTPVDVI 183
Cdd:COG5240 868 MVysMACGCTVKVYCDGESLYVTQLV 893
ASKHA_NBD_HSP70_HSPA12 cd10229
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ...
 63-148 5.93e-03

nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B.


Pssm-ID: 466827 [Multi-domain]  Cd Length: 372  Bit Score: 36.49  E-value: 5.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12060841  63 DEYVLEDLEVTVSDHIQKVLKPNFAAAWEEVGDTFE-KEETFALSSTKTL-----EEAVNNIITFLGMQPCErsdkvPEN 136
Cdd:cd10229 248 DEEFEELLEEIFGDDFMEAFKQKYPSDYLDLLQAFErKKRSFKLRLSPELmkslfDPVVKKIIEHIKELLEK-----PEL 322

                        90
                ....*....|..
gi 12060841 137 KNSHSLYLAGIF 148
Cdd:cd10229 323 KGVDYIFLVGGF 334
 
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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