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Conserved domains on  [gi|12654705|gb|AAH01192|]
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C19orf56 protein, partial [Homo sapiens]

Protein Classification

protein Asterix( domain architecture ID 10508479)

protein Asterix

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASTER pfam03669
PAT complex subunit Asterix; This family represents Asterix proteins which are a component of ...
3-101 1.86e-53

PAT complex subunit Asterix; This family represents Asterix proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. Asterix is the substrate-interacting subunit of the PAT complex and associates with the first TMD of the nascent chain. The PAT complex favors the binding to TMDs with exposed hydrophilic amino acids within the lipid bilayer and provides a membrane-embedded partially hydrophilic environment in which TMD1 binds.


:

Pssm-ID: 461012  Cd Length: 96  Bit Score: 161.72  E-value: 1.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12654705     3 NMSDPRRPNKVLRYKPPPSECNpalDDPTPDYMNLLGMIFSMCGLMLKLKWCAWVAVYCSFISFANSRSSEDTKQMMSSF 82
Cdd:pfam03669   1 NNSDPRRPDKAHRYKPPQLSPQ---EDLPPDYMNFLGMIFSMCGLMMRLKWCAWIALYCCCISFANMKSSDDLKQILSSF 77
                          90
                  ....*....|....*....
gi 12654705    83 MLSISAVVMSYLQNPQPMT 101
Cdd:pfam03669  78 MLSVSALVMSYLQNPRPMT 96
 
Name Accession Description Interval E-value
ASTER pfam03669
PAT complex subunit Asterix; This family represents Asterix proteins which are a component of ...
3-101 1.86e-53

PAT complex subunit Asterix; This family represents Asterix proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. Asterix is the substrate-interacting subunit of the PAT complex and associates with the first TMD of the nascent chain. The PAT complex favors the binding to TMDs with exposed hydrophilic amino acids within the lipid bilayer and provides a membrane-embedded partially hydrophilic environment in which TMD1 binds.


Pssm-ID: 461012  Cd Length: 96  Bit Score: 161.72  E-value: 1.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12654705     3 NMSDPRRPNKVLRYKPPPSECNpalDDPTPDYMNLLGMIFSMCGLMLKLKWCAWVAVYCSFISFANSRSSEDTKQMMSSF 82
Cdd:pfam03669   1 NNSDPRRPDKAHRYKPPQLSPQ---EDLPPDYMNFLGMIFSMCGLMMRLKWCAWIALYCCCISFANMKSSDDLKQILSSF 77
                          90
                  ....*....|....*....
gi 12654705    83 MLSISAVVMSYLQNPQPMT 101
Cdd:pfam03669  78 MLSVSALVMSYLQNPRPMT 96
 
Name Accession Description Interval E-value
ASTER pfam03669
PAT complex subunit Asterix; This family represents Asterix proteins which are a component of ...
3-101 1.86e-53

PAT complex subunit Asterix; This family represents Asterix proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. Asterix is the substrate-interacting subunit of the PAT complex and associates with the first TMD of the nascent chain. The PAT complex favors the binding to TMDs with exposed hydrophilic amino acids within the lipid bilayer and provides a membrane-embedded partially hydrophilic environment in which TMD1 binds.


Pssm-ID: 461012  Cd Length: 96  Bit Score: 161.72  E-value: 1.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12654705     3 NMSDPRRPNKVLRYKPPPSECNpalDDPTPDYMNLLGMIFSMCGLMLKLKWCAWVAVYCSFISFANSRSSEDTKQMMSSF 82
Cdd:pfam03669   1 NNSDPRRPDKAHRYKPPQLSPQ---EDLPPDYMNFLGMIFSMCGLMMRLKWCAWIALYCCCISFANMKSSDDLKQILSSF 77
                          90
                  ....*....|....*....
gi 12654705    83 MLSISAVVMSYLQNPQPMT 101
Cdd:pfam03669  78 MLSVSALVMSYLQNPRPMT 96
 
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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