NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6323200|ref|NP_013271|]
View 

Aps1p [Saccharomyces cerevisiae S288C]

Protein Classification

AP-1 complex subunit sigma( domain architecture ID 13000692)

AP-1 complex subunit sigma is a subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes

Gene Ontology:  GO:0035615|GO:0030121|GO:0016192
PubMed:  16788044|23424177

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
AP1_sigma cd14831
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ...
5-149 6.24e-83

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: 240.15  E-value: 6.24e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323200    5 KYLLLVSRQGKIRLKKWYTAMSAGEKAKIVKDLTPTILARKPKMCNIIEYNDHKVVYKRYASLYFIVGMTPDvDNELLTL 84
Cdd:cd14831   1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRDLKIVYKRYASLYFVCCVDKD-DNELITL 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323200   85 EIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMIMCdGSIAESSRKEVLHHVTVMDTMESND 149
Cdd:cd14831  80 EIIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLG-GELQETSKKNVLRAIEAQDLLQEEE 143
 
Name Accession Description Interval E-value
AP1_sigma cd14831
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ...
5-149 6.24e-83

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: 240.15  E-value: 6.24e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323200    5 KYLLLVSRQGKIRLKKWYTAMSAGEKAKIVKDLTPTILARKPKMCNIIEYNDHKVVYKRYASLYFIVGMTPDvDNELLTL 84
Cdd:cd14831   1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRDLKIVYKRYASLYFVCCVDKD-DNELITL 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323200   85 EIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMIMCdGSIAESSRKEVLHHVTVMDTMESND 149
Cdd:cd14831  80 EIIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLG-GELQETSKKNVLRAIEAQDLLQEEE 143
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
3-156 2.14e-79

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 231.92  E-value: 2.14e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323200    3 QLKYLLLVSRQGKIRLKKWYTAMSAGEKAKIVKDLTPTILARKPKMCNIIEYNDHKVVYKRYASLYFIVGMTPDvDNELL 82
Cdd:COG5030   1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEGKNEKIVYRRYATLYFVFGVDND-DNELI 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323200   83 TLEIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMIMCdGSIAESSRKEVLHHVTVMDTMESNDNLERVLS 156
Cdd:COG5030  80 ILELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILG-GEIIESSKNEVLEHVYALDAESTDDKIGRSLS 152
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
3-146 1.01e-69

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 206.82  E-value: 1.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323200      3 QLKYLLLVSRQGKIRLKKWYTAMSAGEKAKIVKDLTPTILARKPKMCNIIEYNDHKVVYKRYASLYFIVGMTpDVDNELL 82
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIEFNDLKVIYKRYATLYFVVIVD-DQDNELI 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323200     83 TLEIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMIMCdGSIAESSRKEVLHHVTVMDTME 146
Cdd:pfam01217  80 ILELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMG-GEILETSKNEVLHRVALLDELA 142
 
Name Accession Description Interval E-value
AP1_sigma cd14831
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ...
5-149 6.24e-83

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: 240.15  E-value: 6.24e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323200    5 KYLLLVSRQGKIRLKKWYTAMSAGEKAKIVKDLTPTILARKPKMCNIIEYNDHKVVYKRYASLYFIVGMTPDvDNELLTL 84
Cdd:cd14831   1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRDLKIVYKRYASLYFVCCVDKD-DNELITL 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323200   85 EIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMIMCdGSIAESSRKEVLHHVTVMDTMESND 149
Cdd:cd14831  80 EIIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLG-GELQETSKKNVLRAIEAQDLLQEEE 143
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
3-156 2.14e-79

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 231.92  E-value: 2.14e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323200    3 QLKYLLLVSRQGKIRLKKWYTAMSAGEKAKIVKDLTPTILARKPKMCNIIEYNDHKVVYKRYASLYFIVGMTPDvDNELL 82
Cdd:COG5030   1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEGKNEKIVYRRYATLYFVFGVDND-DNELI 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323200   83 TLEIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMIMCdGSIAESSRKEVLHHVTVMDTMESNDNLERVLS 156
Cdd:COG5030  80 ILELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILG-GEIIESSKNEVLEHVYALDAESTDDKIGRSLS 152
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
3-146 1.01e-69

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 206.82  E-value: 1.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323200      3 QLKYLLLVSRQGKIRLKKWYTAMSAGEKAKIVKDLTPTILARKPKMCNIIEYNDHKVVYKRYASLYFIVGMTpDVDNELL 82
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIEFNDLKVIYKRYATLYFVVIVD-DQDNELI 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323200     83 TLEIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMIMCdGSIAESSRKEVLHHVTVMDTME 146
Cdd:pfam01217  80 ILELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMG-GEILETSKNEVLHRVALLDELA 142
AP2_sigma cd14833
AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor ...
3-143 4.32e-52

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: 162.36  E-value: 4.32e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323200    3 QLKYLLLVSRQGKIRLKKWYTAMSAGEKAKIVKDLTPTILARKPKMCNIIEYNDHKVVYKRYASLYFIVGMTPDvDNELL 82
Cdd:cd14833   1 MIRFILIQNRQGKTRLAKWYVPYDDDEKQKLEEEVHRLVTSRDKKHTNFVEFRNYKLVYRRYAGLFFCICVDVN-DNELA 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323200   83 TLEIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMIMcDGSIAESSRKEVLHHVTVMD 143
Cdd:cd14833  80 YLEAIHLFVEVLDEYFGNVCELDLVFNFYKVYAILDEMFL-AGEIQETSKKVILERLKELD 139
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
5-143 2.87e-49

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: 155.08  E-value: 2.87e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323200    5 KYLLLVSRQGKIRLKKWYTAMSAGEKAKIVKDLTPTILARKPKMCNIIEYNDHKVVYKRYASLYFIVGMTPDvDNELLTL 84
Cdd:cd14832   1 KFILMVNKQGQTRLAQYYEFLSIEERVALEGEIIRKCLSRSEKQCSFLEYRGYKLVYRRYASLYFIVGVDED-ENELAIL 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6323200   85 EIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMIMCdGSIAESSRKEVLHHVTVMD 143
Cdd:cd14832  80 EFIHNLVETLDKYFENVCELDIMFNLEKAHFILDEMVMN-GCIVETNKSNILAPILLMD 137
AP_sigma cd14827
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ...
5-143 4.88e-47

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: 149.13  E-value: 4.88e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323200    5 KYLLLVSRQGKIRLKKWYTAMSAGEKAKIVKDLTPTILARKPKMCNIIEYNDHKVVYKRYASLYFIVGMTPDvDNELLTL 84
Cdd:cd14827   1 RFILLFNRQGKTRLAKWYMQFDDDERQKLIEEIVQVVLSRDAKHCNFVEFRNYKLIYRRYASLYFCICVDSN-DNELAIL 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6323200   85 EIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMIMcDGSIAESSRKEVLHHVTVMD 143
Cdd:cd14827  80 EAIHNFVETLDKYFENVCELDLIFNFEKVYFIVDEMVL-GGEIRETSQTKILKQIEMLD 137
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
5-139 3.37e-30

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: 106.54  E-value: 3.37e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323200    5 KYLLLVSRQGKIRLKKWYTAMSAGEKAKIVKDLTPTILARKPKMCNIIEY------NDHKVVYKRYASLYFIVGmTPDVD 78
Cdd:cd14834   3 KAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGgsliggSDTKLIYRHYATLYFVFC-VDSSE 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323200   79 NELLTLEIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMIMcDGSIAESSRKEVLHHV 139
Cdd:cd14834  82 SELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVM-GGMVLETNMTEILTAI 141
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
5-137 2.86e-25

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: 93.74  E-value: 2.86e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323200    5 KYLLLVSRQGKIRLKKWYTAMSAGEKaKIVKDLTPTILARKPKMCNIIEYNDHKVVYKRYASLYFIVgMTPDVDNELLTL 84
Cdd:cd14823   1 KAILVLDNDGKRLFAKYYDDTYPSVK-EQKAFEKNIFNKKHRTDSEIVLLEGLRVVYKSSIDLYFVV-IGSKNENELLLL 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 6323200   85 EIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEmIMCDGSIAESSRKEVLH 137
Cdd:cd14823  79 EVLNCLVDVLSEYFRKVEERAILENFEGLYFALDE-IVDGGYIQETDPKQVVH 130
AP3_Mu_N cd14837
AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the ...
51-121 1.13e-07

AP-3 complex subunit mu N-terminal domain; AP-3 complex mu 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 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: 341441  Cd Length: 139  Bit Score: 47.90  E-value: 1.13e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323200   51 IIEYNDHKVVYKRYASLYFIVGMTPDVDnELLTLEIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMI 121
Cdd:cd14837  46 VIYTPPYYLFHILRNNLYFLAVVTSEVP-PLLVIEFLHRIVDVLEDYFGSLSESTIKENFVVVYQLLEEML 115
AP2_Mu_N cd14836
AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the ...
60-121 8.76e-05

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: 40.20  E-value: 8.76e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323200   60 VYKRYASLYfIVGMTPDVDNELLTLEIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMI 121
Cdd:cd14836  56 FHVRHGNLY-LVAVTRSNVNAAMVFEFLYKLVQLFKSYFGKFNEDSIKNNFVLIYELLDEIL 116
AP_Mu_N cd14828
AP complex subunit mu N-terminal domain; AP complex mu subunits are part of the ...
51-121 3.32e-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: 38.33  E-value: 3.32e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323200   51 IIEYNDHKVVYKRYASLYFIVGMTPDvDNELLTLEIIHRFVETMDTYFGnVCELD---IIFNFSKVYDILNEMI 121
Cdd:cd14828  46 IISSNGWNFIYIKRDDLYFVSVTQTN-VNLMSVLVFLDQFYDLLKDYFG-VKKLDknsIIDNFVLIYELIDESI 117
AP1_Mu_N cd14835
AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the ...
51-121 3.42e-04

AP-1 complex subunit mu N-terminal domain; AP-1 complex mu 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 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: 341439  Cd Length: 139  Bit Score: 38.68  E-value: 3.42e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323200   51 IIEYNDHKVVYKRYASLYFiVGMTPDVDNELLTLEIIHRFVETMDTYFGNVCELDIIFNFSKVYDILNEMI 121
Cdd:cd14835  46 ILTDGGVTYIYIKHNNLYL-LAVTKKNANAAMVLSFLYKLVEVFKEYFKELEEESIRDNFVIIYELLDEMM 115
 
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