NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1376904526|ref|XP_024519652|]
View 

AP-3 complex subunit sigma isoform X1 [Selaginella moellendorffii]

Protein Classification

AP-3 complex subunit sigma( domain architecture ID 13000718)

AP-3 complex subunit sigma is part of the AP-3 complex that is associated with the Golgi region as well as more peripheral structures

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
 1-145 1.04e-86

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: 249.45  E-value: 1.04e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   1 MIDAVLVMNTQGKPRLAKFYKSLSPVKQQEIVRKVYTGLSSRAEHFCNFVEADEIF-GAGTKLVYKHFATLYFVFVIDSG 79
Cdd:cd14834     1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGGSLIgGSDTKLIYRHYATLYFVFCVDSS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376904526  80 ESELGILDLIQVFVETLDSIFKNVCELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVKSVQEIFK 145
Cdd:cd14834    81 ESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTAIEEQNK 146
 
Name Accession Description Interval E-value
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
 1-145 1.04e-86

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: 249.45  E-value: 1.04e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   1 MIDAVLVMNTQGKPRLAKFYKSLSPVKQQEIVRKVYTGLSSRAEHFCNFVEADEIF-GAGTKLVYKHFATLYFVFVIDSG 79
Cdd:cd14834     1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGGSLIgGSDTKLIYRHYATLYFVFCVDSS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376904526  80 ESELGILDLIQVFVETLDSIFKNVCELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVKSVQEIFK 145
Cdd:cd14834    81 ESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTAIEEQNK 146
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-147 3.96e-52

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 162.58  E-value: 3.96e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   1 MIDAVLVMNTQGKPRLAKFYKSLSPVKQQEIVRKVYTGLSSRAEHFCNFVEadeifGAGTKLVYKHFATLYFVFVIDSGE 80
Cdd:COG5030     1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIE-----GKNEKIVYRRYATLYFVFGVDNDD 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376904526  81 SELGILDLIQVFVETLDSIFKNVCELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVKSVQEIFKLE 147
Cdd:COG5030    76 NELIILELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAES 142
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-147 4.34e-51

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 159.44  E-value: 4.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   1 MIDAVLVMNTQGKPRLAKFYKSLSPVKQQEIVRKVYTGLSSRAEHFCNFVEadeifGAGTKLVYKHFATLYFVFVIDSGE 80
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIE-----FNDLKVIYKRYATLYFVVIVDDQD 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376904526  81 SELGILDLIQVFVETLDSIFKNVCELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVKSVQEIFKLE 147
Cdd:pfam01217  76 NELIILELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
 
Name Accession Description Interval E-value
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
 1-145 1.04e-86

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: 249.45  E-value: 1.04e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   1 MIDAVLVMNTQGKPRLAKFYKSLSPVKQQEIVRKVYTGLSSRAEHFCNFVEADEIF-GAGTKLVYKHFATLYFVFVIDSG 79
Cdd:cd14834     1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGGSLIgGSDTKLIYRHYATLYFVFCVDSS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376904526  80 ESELGILDLIQVFVETLDSIFKNVCELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVKSVQEIFK 145
Cdd:cd14834    81 ESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTAIEEQNK 146
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-147 3.96e-52

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 162.58  E-value: 3.96e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   1 MIDAVLVMNTQGKPRLAKFYKSLSPVKQQEIVRKVYTGLSSRAEHFCNFVEadeifGAGTKLVYKHFATLYFVFVIDSGE 80
Cdd:COG5030     1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIE-----GKNEKIVYRRYATLYFVFGVDNDD 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376904526  81 SELGILDLIQVFVETLDSIFKNVCELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVKSVQEIFKLE 147
Cdd:COG5030    76 NELIILELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAES 142
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-147 4.34e-51

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 159.44  E-value: 4.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   1 MIDAVLVMNTQGKPRLAKFYKSLSPVKQQEIVRKVYTGLSSRAEHFCNFVEadeifGAGTKLVYKHFATLYFVFVIDSGE 80
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIE-----FNDLKVIYKRYATLYFVVIVDDQD 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376904526  81 SELGILDLIQVFVETLDSIFKNVCELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVKSVQEIFKLE 147
Cdd:pfam01217  76 NELIILELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
AP_sigma cd14827
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ...
 4-141 9.92e-48

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: 150.67  E-value: 9.92e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   4 AVLVMNTQGKPRLAKFYKSLSPVKQQEIVRKVYTGLSSRAEHFCNFVEadeifGAGTKLVYKHFATLYFVFVIDSGESEL 83
Cdd:cd14827     2 FILLFNRQGKTRLAKWYMQFDDDERQKLIEEIVQVVLSRDAKHCNFVE-----FRNYKLIYRRYASLYFCICVDSNDNEL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1376904526  84 GILDLIQVFVETLDSIFKNVCELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVKSVQ 141
Cdd:cd14827    77 AILEAIHNFVETLDKYFENVCELDLIFNFEKVYFIVDEMVLGGEIRETSQTKILKQIE 134
AP2_sigma cd14833
AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor ...
 1-146 5.54e-47

AP-2 complex subunit sigma; AP-2 complex sigma 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 sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341437  Cd Length: 141  Bit Score: 148.87  E-value: 5.54e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   1 MIDAVLVMNTQGKPRLAKFYKSLSPVKQQEIVRKVYTGLSSRAEHFCNFVEADeifgaGTKLVYKHFATLYFVFVIDSGE 80
Cdd:cd14833     1 MIRFILIQNRQGKTRLAKWYVPYDDDEKQKLEEEVHRLVTSRDKKHTNFVEFR-----NYKLVYRRYAGLFFCICVDVND 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376904526  81 SELGILDLIQVFVETLDSIFKNVCELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVKSVQEIFKL 146
Cdd:cd14833    76 NELAYLEAIHLFVEVLDEYFGNVCELDLVFNFYKVYAILDEMFLAGEIQETSKKVILERLKELDKL 141
AP1_sigma cd14831
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ...
 5-140 3.11e-44

AP-1 complex subunit sigma; AP-1 complex sigma 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 sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341435  Cd Length: 143  Bit Score: 141.93  E-value: 3.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   5 VLVMNTQGKPRLAKFYKSLSPVKQQEIVRKVYTGLSSRAEHFCNFVEADEifgagTKLVYKHFATLYFVFVIDSGESELG 84
Cdd:cd14831     3 LLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRD-----LKIVYKRYASLYFVCCVDKDDNELI 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1376904526  85 ILDLIQVFVETLDSIFKNVCELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVKSV 140
Cdd:cd14831    78 TLEIIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLGGELQETSKKNVLRAI 133
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
 5-141 1.07e-38

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: 127.73  E-value: 1.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   5 VLVMNTQGKPRLAKFYKSLSPVKQQ----EIVRKVYtglsSRAEHFCNFVEAdeifgAGTKLVYKHFATLYFVFVIDSGE 80
Cdd:cd14832     3 ILMVNKQGQTRLAQYYEFLSIEERValegEIIRKCL----SRSEKQCSFLEY-----RGYKLVYRRYASLYFIVGVDEDE 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1376904526  81 SELGILDLIQVFVETLDSIFKNVCELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVKSVQ 141
Cdd:cd14832    74 NELAILEFIHNLVETLDKYFENVCELDIMFNLEKAHFILDEMVMNGCIVETNKSNILAPIL 134
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
 4-138 5.46e-19

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: 77.17  E-value: 5.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   4 AVLVMNTQGKPRLAKFYKSLSPVkQQEIVRKVYTGLSSRAEHFCNFVEADEIfgagtKLVYKHFATLYFVFVIDSGESEL 83
Cdd:cd14823     2 AILVLDNDGKRLFAKYYDDTYPS-VKEQKAFEKNIFNKKHRTDSEIVLLEGL-----RVVYKSSIDLYFVVIGSKNENEL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1376904526  84 GILDLIQVFVETLDSIFKNVCELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVK 138
Cdd:cd14823    76 LLLEVLNCLVDVLSEYFRKVEERAILENFEGLYFALDEIVDGGYIQETDPKQVVH 130
Zeta-COP cd14829
zeta subunit of the F-COPI complex; Zeta subunit of the heterotetrameric F-COPI complex, which ...
 4-137 3.10e-09

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: 51.78  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   4 AVLVMNTQGKPRLAKFY-KSLSPVKQQEIVRKVYTGLSSRAEhfcnfveADEIFGAGTKLVYKHFATLYFVFVIDSGESE 82
Cdd:cd14829     2 AILILDNDGKRVLAKYYdDTFPTVKEQKAFEKKLFDKTHKAN-------AEIILLDGLTVVYKSNIDLTFYVVGSSDENE 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1376904526  83 LGILDLIQVFVETLDSIFKNVCE----LDivfNFNKVNTVLDEIVMGGQVVETNSTEIV 137
Cdd:cd14829    75 LILASVLNCLYDALSLLLRKNVEkralLE---NLDLVLLALDEIVDGGIILETDPTAIA 130
RET3 COG5541
Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, ...
 2-149 1.05e-03

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


Pssm-ID: 227828  Cd Length: 187  Bit Score: 37.61  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526   2 IDAVLVMNTQGKPRLAKFYKSL-----------SPVKQQEIVRKVYTGLSSRAEHFCNFveadeifgAGTKLVYKHFATL 70
Cdd:COG5541     8 VEALLILDSQGERIYRKYYQPPhrseghqlvfnSVKKEKEFEKKLAEKTAKDRESILMF--------YDRLVMCKRLDDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376904526  71 YFVFVIDSGESELGILDLIQVFVETLDSIFKNVC-ELDIVFNFNKVNTVLDEIVMGGQVVETNSTEIVKSV--------Q 141
Cdd:COG5541    80 LLYIVSPMEENEPFLGQVFDEIRAALILIVKTPTdKRNVWENYDQIVLLVDETIDEGVILETKSDEIADRVpkppnfegQ 159


                  ....*...
gi 1376904526 142 EIFKLERG 149
Cdd:COG5541   160 DGMKVPRG 167
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH