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adaptor-related protein complex 1, sigma 1 subunit, isoform CRA_a [Homo sapiens]
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
List of domain hits
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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 ... |
3-127 | 5.48e-91 | |||
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: 259.80 E-value: 5.48e-91
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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 ... |
3-127 | 5.48e-91 | |||
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: 259.80 E-value: 5.48e-91
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Clat_adaptor_s | pfam01217 | Clathrin adaptor complex small chain; |
1-127 | 5.86e-68 | |||
Clathrin adaptor complex small chain; Pssm-ID: 460115 Cd Length: 142 Bit Score: 201.43 E-value: 5.86e-68
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APS2 | COG5030 | Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion]; |
1-129 | 1.33e-59 | |||
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion]; Pssm-ID: 227363 Cd Length: 152 Bit Score: 180.68 E-value: 1.33e-59
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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 ... |
3-127 | 5.48e-91 | |||
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: 259.80 E-value: 5.48e-91
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Clat_adaptor_s | pfam01217 | Clathrin adaptor complex small chain; |
1-127 | 5.86e-68 | |||
Clathrin adaptor complex small chain; Pssm-ID: 460115 Cd Length: 142 Bit Score: 201.43 E-value: 5.86e-68
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AP_sigma | cd14827 | AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ... |
3-127 | 5.27e-61 | |||
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: 183.79 E-value: 5.27e-61
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APS2 | COG5030 | Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion]; |
1-129 | 1.33e-59 | |||
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion]; Pssm-ID: 227363 Cd Length: 152 Bit Score: 180.68 E-value: 1.33e-59
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AP2_sigma | cd14833 | AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor ... |
1-127 | 2.31e-56 | |||
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: 171.99 E-value: 2.31e-56
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AP4_sigma | cd14832 | AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ... |
3-127 | 8.22e-47 | |||
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: 147.76 E-value: 8.22e-47
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AP3_sigma | cd14834 | AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ... |
1-127 | 5.76e-41 | |||
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: 133.12 E-value: 5.76e-41
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AP_longin-like | cd14823 | Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ... |
4-127 | 6.45e-41 | |||
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: 132.64 E-value: 6.45e-41
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AP3_Mu_N | cd14837 | AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the ... |
64-121 | 1.34e-05 | |||
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: 41.74 E-value: 1.34e-05
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AP2_Mu_N | cd14836 | AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the ... |
58-127 | 7.24e-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: 39.81 E-value: 7.24e-05
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AP1_Mu_N | cd14835 | AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the ... |
58-116 | 2.70e-03 | |||
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: 35.60 E-value: 2.70e-03
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AP4_Mu_N | cd14838 | AP-4 complex subunit mu N-terminal domain; AP-4 complex mu subunit is part of the ... |
58-127 | 4.88e-03 | |||
AP-4 complex subunit mu N-terminal domain; AP-4 complex mu 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 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: 341442 Cd Length: 137 Bit Score: 34.83 E-value: 4.88e-03
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PulA_N1 | pfam17999 | Pullulanase N1-terminal domain; This is the N-terminal domain found in debranching enzyme such ... |
75-124 | 6.89e-03 | |||
Pullulanase N1-terminal domain; This is the N-terminal domain found in debranching enzyme such as Pullulanase (PulA)from Anoxybacillus sp. LM18-11. The PulA structure comprises four domains (N1, N2, A, and C). This is the N1 domain which has been identified as a carbohydrate-binding motif. Two maltotriose or maltotetraose molecules were found between the N1 domain and a loop of the A domain in the PulA-maltotriose or PulA-maltotetraose structures. These carbohydrates are bound in a parallel binding mode close to each other and form hydrogen bonds. The sugar moieties bound to the N1 domain are not immediately adjacent to the active site, but the enzyme might use N1 binding to attract and grab the substrate. Functional analysis indicate that N1 is important for catalytic activity and thermostability in addition to assisting substrate binding. The structure of the N1 domain reveals a classic distorted beta-jelly roll fold consisting of two anti-parallel beta-sheets, forming a concave and a convex surface. On the concave side of N1 domain there is a cleft to accommodate two molecules of maltotriose or maltotetraose. Pssm-ID: 436198 Cd Length: 85 Bit Score: 33.69 E-value: 6.89e-03
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AP_Mu_N | cd14828 | AP complex subunit mu N-terminal domain; AP complex mu subunits are part of the ... |
58-126 | 9.87e-03 | |||
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: 34.09 E-value: 9.87e-03
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