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Conserved domains on  [gi|597801925|ref|XP_007242303|]
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dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit dad1 [Astyanax mexicanus]

Protein Classification

DAD/OST2 family dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit( domain architecture ID 10489298)

DAD/OST2 family dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit is part of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DAD pfam02109
DAD family; Members of this family are thought to be integral membrane proteins. Some members ...
7-113 3.63e-51

DAD family; Members of this family are thought to be integral membrane proteins. Some members of this family have been shown to cause apoptosis if mutated, these proteins are known as DAD for defender against death. The family also includes the epsilon subunit of the oligosaccharyltransferase that is involved in N-linked glycosylation.


:

Pssm-ID: 460448  Cd Length: 108  Bit Score: 156.90  E-value: 3.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597801925    7 SVLTRFVEEYRNRTSSKLKVIDAYLLYILLTGAFQFLYCLLVGTFPFNSFLSGFISSVGSFILAVCLRIQINPQNKGEFL 86
Cdd:pfam02109   2 SILSTLWKSYSKQTPQRLKLIDAFLLFLVLTGILQFVYCLLVGTFPFNAFLSGFISCVGQFVLTVSLRLQLNPENKSEFK 81
                          90       100
                  ....*....|....*....|....*..
gi 597801925   87 SVSPERAFADFLFAHTVLHLVVVNFIG 113
Cdd:pfam02109  82 GISPERAFADFVFASLVLHFFVINFIG 108
 
Name Accession Description Interval E-value
DAD pfam02109
DAD family; Members of this family are thought to be integral membrane proteins. Some members ...
7-113 3.63e-51

DAD family; Members of this family are thought to be integral membrane proteins. Some members of this family have been shown to cause apoptosis if mutated, these proteins are known as DAD for defender against death. The family also includes the epsilon subunit of the oligosaccharyltransferase that is involved in N-linked glycosylation.


Pssm-ID: 460448  Cd Length: 108  Bit Score: 156.90  E-value: 3.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597801925    7 SVLTRFVEEYRNRTSSKLKVIDAYLLYILLTGAFQFLYCLLVGTFPFNSFLSGFISSVGSFILAVCLRIQINPQNKGEFL 86
Cdd:pfam02109   2 SILSTLWKSYSKQTPQRLKLIDAFLLFLVLTGILQFVYCLLVGTFPFNAFLSGFISCVGQFVLTVSLRLQLNPENKSEFK 81
                          90       100
                  ....*....|....*....|....*..
gi 597801925   87 SVSPERAFADFLFAHTVLHLVVVNFIG 113
Cdd:pfam02109  82 GISPERAFADFVFASLVLHFFVINFIG 108
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
43-98 8.44e-03

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 34.07  E-value: 8.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 597801925  43 LYCLLVGTFPFNsflsgfissvGSFILAVCLRIQINPQNKGEFLSVSPEraFADFL 98
Cdd:cd14008  201 LYCLVFGRLPFN----------GDNILELYEAIQNQNDEFPIPPELSPE--LKDLL 244
 
Name Accession Description Interval E-value
DAD pfam02109
DAD family; Members of this family are thought to be integral membrane proteins. Some members ...
7-113 3.63e-51

DAD family; Members of this family are thought to be integral membrane proteins. Some members of this family have been shown to cause apoptosis if mutated, these proteins are known as DAD for defender against death. The family also includes the epsilon subunit of the oligosaccharyltransferase that is involved in N-linked glycosylation.


Pssm-ID: 460448  Cd Length: 108  Bit Score: 156.90  E-value: 3.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597801925    7 SVLTRFVEEYRNRTSSKLKVIDAYLLYILLTGAFQFLYCLLVGTFPFNSFLSGFISSVGSFILAVCLRIQINPQNKGEFL 86
Cdd:pfam02109   2 SILSTLWKSYSKQTPQRLKLIDAFLLFLVLTGILQFVYCLLVGTFPFNAFLSGFISCVGQFVLTVSLRLQLNPENKSEFK 81
                          90       100
                  ....*....|....*....|....*..
gi 597801925   87 SVSPERAFADFLFAHTVLHLVVVNFIG 113
Cdd:pfam02109  82 GISPERAFADFVFASLVLHFFVINFIG 108
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
43-98 8.44e-03

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 34.07  E-value: 8.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 597801925  43 LYCLLVGTFPFNsflsgfissvGSFILAVCLRIQINPQNKGEFLSVSPEraFADFL 98
Cdd:cd14008  201 LYCLVFGRLPFN----------GDNILELYEAIQNQNDEFPIPPELSPE--LKDLL 244
 
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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