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Conserved domains on  [gi|119570583|gb|EAW50198|]
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adaptor-related protein complex 1, sigma 1 subunit, isoform CRA_a [Homo sapiens]

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

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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 ...
 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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583   3 RFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELITLE 82
Cdd:cd14831    1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRDLKIVYKRYASLYFVCCVDKDDNELITLE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119570583  83 LIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTS 127
Cdd:cd14831   81 IIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLGGELQETS 125
 
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583   3 RFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELITLE 82
Cdd:cd14831    1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRDLKIVYKRYASLYFVCCVDKDDNELITLE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119570583  83 LIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTS 127
Cdd:cd14831   81 IIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLGGELQETS 125
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583    1 MMRFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELIT 80
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELII 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 119570583   81 LELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTS 127
Cdd:pfam01217  81 LELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETS 127
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583   1 MMRFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELIT 80
Cdd:COG5030    1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEGKNEKIVYRRYATLYFVFGVDNDDNELII 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 119570583  81 LELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTSNF 129
Cdd:COG5030   81 LELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKN 129
 
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583   3 RFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELITLE 82
Cdd:cd14831    1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRDLKIVYKRYASLYFVCCVDKDDNELITLE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119570583  83 LIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTS 127
Cdd:cd14831   81 IIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLGGELQETS 125
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583    1 MMRFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELIT 80
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELII 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 119570583   81 LELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTS 127
Cdd:pfam01217  81 LELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETS 127
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583   3 RFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELITLE 82
Cdd:cd14827    1 RFILLFNRQGKTRLAKWYMQFDDDERQKLIEEIVQVVLSRDAKHCNFVEFRNYKLIYRRYASLYFCICVDSNDNELAILE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119570583  83 LIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTS 127
Cdd:cd14827   81 AIHNFVETLDKYFENVCELDLIFNFEKVYFIVDEMVLGGEIRETS 125
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583   1 MMRFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELIT 80
Cdd:COG5030    1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEGKNEKIVYRRYATLYFVFGVDNDDNELII 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 119570583  81 LELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTSNF 129
Cdd:COG5030   81 LELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKN 129
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583   1 MMRFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELIT 80
Cdd:cd14833    1 MIRFILIQNRQGKTRLAKWYVPYDDDEKQKLEEEVHRLVTSRDKKHTNFVEFRNYKLVYRRYAGLFFCICVDVNDNELAY 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 119570583  81 LELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTS 127
Cdd:cd14833   81 LEAIHLFVEVLDEYFGNVCELDLVFNFYKVYAILDEMFLAGEIQETS 127
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583   3 RFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELITLE 82
Cdd:cd14832    1 KFILMVNKQGQTRLAQYYEFLSIEERVALEGEIIRKCLSRSEKQCSFLEYRGYKLVYRRYASLYFIVGVDEDENELAILE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119570583  83 LIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTS 127
Cdd:cd14832   81 FIHNLVETLDKYFENVCELDIMFNLEKAHFILDEMVMNGCIVETN 125
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583   1 MMRFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLE------WRDLKVVYKRYASLYFCCAIEGQ 74
Cdd:cd14834    1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEggsligGSDTKLIYRHYATLYFVFCVDSS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119570583  75 DNELITLELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTS 127
Cdd:cd14834   81 ESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETN 133
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583   4 FMLLFSRQGKLRLQKWYLATSDkERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELITLEL 83
Cdd:cd14823    2 AILVLDNDGKRLFAKYYDDTYP-SVKEQKAFEKNIFNKKHRTDSEIVLLEGLRVVYKSSIDLYFVVIGSKNENELLLLEV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119570583  84 IHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTS 127
Cdd:cd14823   81 LNCLVDVLSEYFRKVEERAILENFEGLYFALDEIVDGGYIQETD 124
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
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119570583  64 SLYFCCAIEGQDNELITLELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGG 121
Cdd:cd14837   61 NLYFLAVVTSEVPPLLVIEFLHRIVDVLEDYFGSLSESTIKENFVVVYQLLEEMLDNG 118
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
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583  58 VYKRYASLYFCCAIEGQDNELITLELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTS 127
Cdd:cd14836   56 FHVRHGNLYLVAVTRSNVNAAMVFEFLYKLVQLFKSYFGKFNEDSIKNNFVLIYELLDEILDFGYPQNTE 125
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
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119570583  58 VYKRYASLYFCCAIEGQDNELITLELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDE 116
Cdd:cd14835   55 IYIKHNNLYLLAVTKKNANAAMVLSFLYKLVEVFKEYFKELEEESIRDNFVIIYELLDE 113
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
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570583  58 VYKRYASLYFCCAIEGQDNELITLELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTS 127
Cdd:cd14838   53 LHVKRNGLYFVATTRFNVSPSYVLELLNRIAKLIKDYCGVLNEESIRKNFVLIYELLDEILDFGYPQTTS 122
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
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 119570583   75 DNELITLELIHRY-VELLDKYfgsVCELDIIFNFEKAYFILDEFLMGGDVQ 124
Cdd:pfam17999  32 GDEKIPLSIKEKEeLEEEVKY---ICKSEGPLELGKEYWVYDEHGNKTDLQ 79
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
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119570583  58 VYKRYASLYFCCAIEGQDNELITLELIHRYVELLDKYFGsVCELD---IIFNFEKAYFILDEFLMGGDVQDT 126
Cdd:cd14828   55 IYIKRDDLYFVSVTQTNVNLMSVLVFLDQFYDLLKDYFG-VKKLDknsIIDNFVLIYELIDESIDFGIIQLT 125
 
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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