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Conserved domains on  [gi|666637993|ref|NP_001288005|]
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AP-2 complex subunit sigma isoform 3 [Homo sapiens]

Protein Classification

AP-2 complex subunit sigma( domain architecture ID 13000710)

AP-2 complex subunit sigma is a component of the adaptor protein complex 2 (AP-2) that functions in protein transport via transport vesicles in different membrane traffic pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AP2_sigma cd14833
AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor ...
 18-157 5.05e-92

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: 263.28  E-value: 5.05e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  18 IRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYL 97
Cdd:cd14833    2 IRFILIQNRQGKTRLAKWYVPYDDDEKQKLEEEVHRLVTSRDKKHTNFVEFRNYKLVYRRYAGLFFCICVDVNDNELAYL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  98 EAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLMLQSL 157
Cdd:cd14833   82 EAIHLFVEVLDEYFGNVCELDLVFNFYKVYAILDEMFLAGEIQETSKKVILERLKELDKL 141
 
Name Accession Description Interval E-value
AP2_sigma cd14833
AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor ...
 18-157 5.05e-92

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: 263.28  E-value: 5.05e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  18 IRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYL 97
Cdd:cd14833    2 IRFILIQNRQGKTRLAKWYVPYDDDEKQKLEEEVHRLVTSRDKKHTNFVEFRNYKLVYRRYAGLFFCICVDVNDNELAYL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  98 EAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLMLQSL 157
Cdd:cd14833   82 EAIHLFVEVLDEYFGNVCELDLVFNFYKVYAILDEMFLAGEIQETSKKVILERLKELDKL 141
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
18-158 1.06e-71

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 211.83  E-value: 1.06e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993   18 IRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYL 97
Cdd:pfam01217   2 IKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELIIL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 666637993   98 EAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLMLQSLE 158
Cdd:pfam01217  82 ELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
18-158 1.07e-57

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 176.83  E-value: 1.07e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  18 IRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYL 97
Cdd:COG5030    2 IKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEGKNEKIVYRRYATLYFVFGVDNDDNELIIL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 666637993  98 EAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLMLQSLE 158
Cdd:COG5030   82 ELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAES 142
 
Name Accession Description Interval E-value
AP2_sigma cd14833
AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor ...
 18-157 5.05e-92

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: 263.28  E-value: 5.05e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  18 IRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYL 97
Cdd:cd14833    2 IRFILIQNRQGKTRLAKWYVPYDDDEKQKLEEEVHRLVTSRDKKHTNFVEFRNYKLVYRRYAGLFFCICVDVNDNELAYL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  98 EAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLMLQSL 157
Cdd:cd14833   82 EAIHLFVEVLDEYFGNVCELDLVFNFYKVYAILDEMFLAGEIQETSKKVILERLKELDKL 141
AP_sigma cd14827
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ...
 19-156 6.05e-75

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: 220.00  E-value: 6.05e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  19 RFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYLE 98
Cdd:cd14827    1 RFILLFNRQGKTRLAKWYMQFDDDERQKLIEEIVQVVLSRDAKHCNFVEFRNYKLIYRRYASLYFCICVDSNDNELAILE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 666637993  99 AIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLMLQS 156
Cdd:cd14827   81 AIHNFVETLDKYFENVCELDLIFNFEKVYFIVDEMVLGGEIRETSQTKILKQIEMLDK 138
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
18-158 1.06e-71

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 211.83  E-value: 1.06e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993   18 IRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYL 97
Cdd:pfam01217   2 IKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELIIL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 666637993   98 EAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLMLQSLE 158
Cdd:pfam01217  82 ELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
AP1_sigma cd14831
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ...
 19-151 4.46e-59

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: 180.06  E-value: 4.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  19 RFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYLE 98
Cdd:cd14831    1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRDLKIVYKRYASLYFVCCVDKDDNELITLE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 666637993  99 AIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQL 151
Cdd:cd14831   81 IIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLGGELQETSKKNVLRAI 133
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
18-158 1.07e-57

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 176.83  E-value: 1.07e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  18 IRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYL 97
Cdd:COG5030    2 IKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEGKNEKIVYRRYATLYFVFGVDNDDNELIIL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 666637993  98 EAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLMLQSLE 158
Cdd:COG5030   82 ELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAES 142
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
 19-154 2.63e-44

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: 142.37  E-value: 2.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  19 RFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYLE 98
Cdd:cd14832    1 KFILMVNKQGQTRLAQYYEFLSIEERVALEGEIIRKCLSRSEKQCSFLEYRGYKLVYRRYASLYFIVGVDEDENELAILE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 666637993  99 AIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLML 154
Cdd:cd14832   81 FIHNLVETLDKYFENVCELDIMFNLEKAHFILDEMVMNGCIVETNKSNILAPILLM 136
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
 18-150 1.20e-39

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: 130.81  E-value: 1.20e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  18 IRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEF------RNFKIIYRRYAGLYFCICVDVND 91
Cdd:cd14834    2 IKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGgsliggSDTKLIYRHYATLYFVFCVDSSE 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 666637993  92 NNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQ 150
Cdd:cd14834   82 SELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTA 140
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
 20-149 1.11e-22

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: 87.19  E-value: 1.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  20 FILIQNRAGKTRLAKWYMQfDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYLEA 99
Cdd:cd14823    2 AILVLDNDGKRLFAKYYDD-TYPSVKEQKAFEKNIFNKKHRTDSEIVLLEGLRVVYKSSIDLYFVVIGSKNENELLLLEV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 666637993 100 IHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLK 149
Cdd:cd14823   81 LNCLVDVLSEYFRKVEERAILENFEGLYFALDEIVDGGYIQETDPKQVVH 130
AP1_Mu_N cd14835
AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the ...
 74-150 5.45e-07

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: 46.39  E-value: 5.45e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 666637993  74 IYRRYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGeIRETSQTKVLKQ 150
Cdd:cd14835   55 IYIKHNNLYLLAVTKKNANAAMVLSFLYKLVEVFKEYFKELEEESIRDNFVIIYELLDEMMDFG-YPQTTESKILQE 130
AP3_Mu_N cd14837
AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the ...
 74-158 1.89e-03

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: 36.34  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  74 IYRryAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGeIRETSQTKVLKQLLM 153
Cdd:cd14837   57 ILR--NNLYFLAVVTSEVPPLLVIEFLHRIVDVLEDYFGSLSESTIKENFVVVYQLLEEMLDNG-FPLTTEPNALKELVP 133


                 ....*
gi 666637993 154 LQSLE 158
Cdd:cd14837  134 PPSLL 138
AP_Mu_N cd14828
AP complex subunit mu N-terminal domain; AP complex mu subunits are part of the ...
 53-149 2.50e-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: 36.02  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666637993  53 AVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFH-NVCELDLVF-NFYKVYTVV 130
Cdd:cd14828   34 AYKKLNPEERPPIISSNGWNFIYIKRDDLYFVSVTQTNVNLMSVLVFLDQFYDLLKDYFGvKKLDKNSIIdNFVLIYELI 113

                         90
                 ....*....|....*....
gi 666637993 131 DEMFLAGeIRETSQTKVLK 149
Cdd:cd14828  114 DESIDFG-IIQLTDYNILK 131
 
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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