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Conserved domains on  [gi|398364633|ref|NP_012510|]
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Aps3p [Saccharomyces cerevisiae S288C]

Protein Classification

APS2 family protein( domain architecture ID 10009032)

APS2 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-172 1.13e-67

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


:

Pssm-ID: 227363  Cd Length: 152  Bit Score: 203.80  E-value: 1.13e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633   1 MIHAVLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRNSDfQSSFLvtppslllsnennndevNNEDIQIIYKNY 80
Cdd:COG5030    1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPK-ESNFI-----------------EGKNEKIVYRRY 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633  81 ATLYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIVASVDELnkAA 160
Cdd:COG5030   63 ATLYFVFGVDNDDNELIILELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYAL--DA 140
                        170
                 ....*....|..
gi 398364633 161 ESTDSKIGRLTS 172
Cdd:COG5030  141 ESTDDKIGRSLS 152
 
Name Accession Description Interval E-value
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-172 1.13e-67

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 203.80  E-value: 1.13e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633   1 MIHAVLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRNSDfQSSFLvtppslllsnennndevNNEDIQIIYKNY 80
Cdd:COG5030    1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPK-ESNFI-----------------EGKNEKIVYRRY 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633  81 ATLYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIVASVDELnkAA 160
Cdd:COG5030   63 ATLYFVFGVDNDDNELIILELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYAL--DA 140
                        170
                 ....*....|..
gi 398364633 161 ESTDSKIGRLTS 172
Cdd:COG5030  141 ESTDDKIGRSLS 152
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-160 1.77e-62

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 190.26  E-value: 1.77e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633    1 MIHAVLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRNSDFqSSFLvtppslllsnennndevNNEDIQIIYKNY 80
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKM-SNFI-----------------EFNDLKVIYKRY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633   81 ATLYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIVASVDELNKAA 160
Cdd:pfam01217  63 ATLYFVVIVDDQDNELIILELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
1-158 3.48e-62

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: 189.36  E-value: 3.48e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633   1 MIHAVLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRnSDFQSSFLvTPPSLLLSNEnnndevnnedIQIIYKNY 80
Cdd:cd14834    1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKR-DDNVCNFL-EGGSLIGGSD----------TKLIYRHY 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398364633  81 ATLYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIVASVDELNK 158
Cdd:cd14834   69 ATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTAIEEQNK 146
 
Name Accession Description Interval E-value
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-172 1.13e-67

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 203.80  E-value: 1.13e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633   1 MIHAVLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRNSDfQSSFLvtppslllsnennndevNNEDIQIIYKNY 80
Cdd:COG5030    1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPK-ESNFI-----------------EGKNEKIVYRRY 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633  81 ATLYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIVASVDELnkAA 160
Cdd:COG5030   63 ATLYFVFGVDNDDNELIILELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYAL--DA 140
                        170
                 ....*....|..
gi 398364633 161 ESTDSKIGRLTS 172
Cdd:COG5030  141 ESTDDKIGRSLS 152
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-160 1.77e-62

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 190.26  E-value: 1.77e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633    1 MIHAVLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRNSDFqSSFLvtppslllsnennndevNNEDIQIIYKNY 80
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKM-SNFI-----------------EFNDLKVIYKRY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633   81 ATLYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIVASVDELNKAA 160
Cdd:pfam01217  63 ATLYFVVIVDDQDNELIILELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
1-158 3.48e-62

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: 189.36  E-value: 3.48e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633   1 MIHAVLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRnSDFQSSFLvTPPSLLLSNEnnndevnnedIQIIYKNY 80
Cdd:cd14834    1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKR-DDNVCNFL-EGGSLIGGSD----------TKLIYRHY 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398364633  81 ATLYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIVASVDELNK 158
Cdd:cd14834   69 ATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTAIEEQNK 146
AP_sigma cd14827
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ...
3-158 4.78e-35

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: 120.24  E-value: 4.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633   3 HAVLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRNSDfQSSFLvtppslllsnennndevNNEDIQIIYKNYAT 82
Cdd:cd14827    1 RFILLFNRQGKTRLAKWYMQFDDDERQKLIEEIVQVVLSRDAK-HCNFV-----------------EFRNYKLIYRRYAS 62
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364633  83 LYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIVASVDELNK 158
Cdd:cd14827   63 LYFCICVDSNDNELAILEAIHNFVETLDKYFENVCELDLIFNFEKVYFIVDEMVLGGEIRETSQTKILKQIEMLDK 138
AP2_sigma cd14833
AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor ...
1-158 1.70e-31

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: 111.12  E-value: 1.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633   1 MIHAVLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRNSdFQSSFLvtppslllsnennndevNNEDIQIIYKNY 80
Cdd:cd14833    1 MIRFILIQNRQGKTRLAKWYVPYDDDEKQKLEEEVHRLVTSRDK-KHTNFV-----------------EFRNYKLVYRRY 62
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398364633  81 ATLYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIVASVDELNK 158
Cdd:cd14833   63 AGLFFCICVDVNDNELAYLEAIHLFVEVLDEYFGNVCELDLVFNFYKVYAILDEMFLAGEIQETSKKVILERLKELDK 140
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
5-158 6.57e-26

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: 96.92  E-value: 6.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633   5 VLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRnSDFQSSFLvtppslllsnennndevNNEDIQIIYKNYATLY 84
Cdd:cd14832    3 ILMVNKQGQTRLAQYYEFLSIEERVALEGEIIRKCLSR-SEKQCSFL-----------------EYRGYKLVYRRYASLY 64
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398364633  85 FTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIVASVDELNK 158
Cdd:cd14832   65 FIVGVDEDENELAILEFIHNLVETLDKYFENVCELDIMFNLEKAHFILDEMVMNGCIVETNKSNILAPILLMDK 138
AP1_sigma cd14831
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ...
3-156 6.73e-25

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: 94.16  E-value: 6.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633   3 HAVLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRNSDFqSSFLvtppslllsnennndevNNEDIQIIYKNYAT 82
Cdd:cd14831    1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKM-CNFL-----------------EWRDLKIVYKRYAS 62
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398364633  83 LYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIET---NVNRIVASVDEL 156
Cdd:cd14831   63 LYFVCCVDKDDNELITLEIIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLGGELQETskkNVLRAIEAQDLL 139
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
3-150 1.06e-12

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: 62.15  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364633   3 HAVLIFNKKCQPRLVKFYtpVDLPKQKLLLEQVYELISQRNSDFQSSFLVTppslllsnennndevnnEDIQIIYKNYAT 82
Cdd:cd14823    1 KAILVLDNDGKRLFAKYY--DDTYPSVKEQKAFEKNIFNKKHRTDSEIVLL-----------------EGLRVVYKSSID 61
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398364633  83 LYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIV 150
Cdd:cd14823   62 LYFVVIGSKNENELLLLEVLNCLVDVLSEYFRKVEERAILENFEGLYFALDEIVDGGYIQETDPKQVV 129
Zeta-COP cd14829
zeta subunit of the F-COPI complex; Zeta subunit of the heterotetrameric F-COPI complex, which ...
75-150 7.11e-04

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: 37.91  E-value: 7.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398364633  75 IIYKNYATLYFTFIVDDQESELAILDLIQTFVESLDRCF-TEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIV 150
Cdd:cd14829   54 VVYKSNIDLTFYVVGSSDENELILASVLNCLYDALSLLLrKNVEKRALLENLDLVLLALDEIVDGGIILETDPTAIA 130
 
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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