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Conserved domains on  [gi|1239962638|ref|XP_013962960|]
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pulmonary surfactant-associated protein C isoform X2 [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SF_P super family cl30965
Pulmonary surfactant proteins; Pulmonary surfactant associated proteins promote alveolar ...
 10-147 1.44e-81

Pulmonary surfactant proteins; Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-C, a component of surfactant, is a highly hydrophobic peptide of 35 amino acid residues which is processed from a larger precursor protein. SP-C is post-translationally modified by the covalent attachment of two palmitoyl groups on two adjacent cysteines


The actual alignment was detected with superfamily member smart00019:

Pssm-ID: 128335 [Multi-domain]  Cd Length: 191  Bit Score: 238.34  E-value: 1.44e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239962638   10 MDVGSKEVLIESPP-----------------------------------------------------VLEMSMGGPEAQQ 36
Cdd:smart00019   1 MDVGSKEVLMESPPdysaaprgrfgipccpvhlkrllivvvvvvlvvvvivgallmglhmsqkhtemVLEMSIGAPEAQQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239962638   37 RLALQERVGTTATFSIGSTGIVVYDYQRLLIAYKPAPGTCCYIMKMTPENIPSLEALTRKFQDFQVKPAVSTSKLGQEEG 116
Cdd:smart00019  81 RLALSERAGTTATFSIGSTGIVVYDYQRLLIAYKPAPGTCCYIMKMAPESIPSLEALARKVQNFQAKPAVPTSKLGQEEG 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1239962638  117 HDAGSASPGDPLDFLGTTVSTLCGEVPLFYI 147
Cdd:smart00019 161 HDAGSASSGGDLAFLGMAVSTLCGEVPLYYI 191
 
Name Accession Description Interval E-value
SF_P smart00019
Pulmonary surfactant proteins; Pulmonary surfactant associated proteins promote alveolar ...
 10-147 1.44e-81

Pulmonary surfactant proteins; Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-C, a component of surfactant, is a highly hydrophobic peptide of 35 amino acid residues which is processed from a larger precursor protein. SP-C is post-translationally modified by the covalent attachment of two palmitoyl groups on two adjacent cysteines


Pssm-ID: 128335 [Multi-domain]  Cd Length: 191  Bit Score: 238.34  E-value: 1.44e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239962638   10 MDVGSKEVLIESPP-----------------------------------------------------VLEMSMGGPEAQQ 36
Cdd:smart00019   1 MDVGSKEVLMESPPdysaaprgrfgipccpvhlkrllivvvvvvlvvvvivgallmglhmsqkhtemVLEMSIGAPEAQQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239962638   37 RLALQERVGTTATFSIGSTGIVVYDYQRLLIAYKPAPGTCCYIMKMTPENIPSLEALTRKFQDFQVKPAVSTSKLGQEEG 116
Cdd:smart00019  81 RLALSERAGTTATFSIGSTGIVVYDYQRLLIAYKPAPGTCCYIMKMAPESIPSLEALARKVQNFQAKPAVPTSKLGQEEG 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1239962638  117 HDAGSASPGDPLDFLGTTVSTLCGEVPLFYI 147
Cdd:smart00019 161 HDAGSASSGGDLAFLGMAVSTLCGEVPLYYI 191
BRICHOS pfam04089
BRICHOS domain; The BRICHOS domain is about 100 amino acids long. It is found in a variety of ...
 52-146 1.38e-23

BRICHOS domain; The BRICHOS domain is about 100 amino acids long. It is found in a variety of proteins implicated in dementia, respiratory distress and cancer. Its exact function is unknown; roles that have been proposed for it include (a) in targeting of the protein to the secretory pathway, (b) intramolecular chaperone-like function, and (c) assisting the specialized intracellular protease processing system. This C-terminal domain is embedded in the endoplasmic reticulum lumen, and binds to the N-terminal, transmembrane, SP_C, pfam08999, provided that it is in non-helical conformation. Thus the Brichos domain of proSP-C is a chaperone that induces alpha-helix formation of an aggregation-prone TM region.


Pssm-ID: 461168  Cd Length: 91  Bit Score: 87.75  E-value: 1.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239962638  52 IGSTGIVVYDYQRLLIAYKPAPGTCCYIMKMTPENIPSLEALTRKFQDFQVKPAVSTSKLGQEEGHDagsaSPGDPLDFL 131
Cdd:pfam04089   1 GNDSATVIHDFKNGLTAYRDLSLKKCYIMKMDKSDVPPLQELLRLLENKEEGEGPPPESLGVYVPQT----RPVKDLSFL 76

                          90
                  ....*....|....*
gi 1239962638 132 GTTVSTLCGEVPLFY 146
Cdd:pfam04089  77 GSPIQELCRGLPTYW 91
 
Name Accession Description Interval E-value
SF_P smart00019
Pulmonary surfactant proteins; Pulmonary surfactant associated proteins promote alveolar ...
 10-147 1.44e-81

Pulmonary surfactant proteins; Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-C, a component of surfactant, is a highly hydrophobic peptide of 35 amino acid residues which is processed from a larger precursor protein. SP-C is post-translationally modified by the covalent attachment of two palmitoyl groups on two adjacent cysteines


Pssm-ID: 128335 [Multi-domain]  Cd Length: 191  Bit Score: 238.34  E-value: 1.44e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239962638   10 MDVGSKEVLIESPP-----------------------------------------------------VLEMSMGGPEAQQ 36
Cdd:smart00019   1 MDVGSKEVLMESPPdysaaprgrfgipccpvhlkrllivvvvvvlvvvvivgallmglhmsqkhtemVLEMSIGAPEAQQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239962638   37 RLALQERVGTTATFSIGSTGIVVYDYQRLLIAYKPAPGTCCYIMKMTPENIPSLEALTRKFQDFQVKPAVSTSKLGQEEG 116
Cdd:smart00019  81 RLALSERAGTTATFSIGSTGIVVYDYQRLLIAYKPAPGTCCYIMKMAPESIPSLEALARKVQNFQAKPAVPTSKLGQEEG 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1239962638  117 HDAGSASPGDPLDFLGTTVSTLCGEVPLFYI 147
Cdd:smart00019 161 HDAGSASSGGDLAFLGMAVSTLCGEVPLYYI 191
BRICHOS smart01039
The BRICHOS domain is found in a variety of proteins implicated in dementia, respiratory ...
 50-147 6.52e-25

The BRICHOS domain is found in a variety of proteins implicated in dementia, respiratory distress and cancer; Its exact function is unknown; roles that have been proposed for the domain, which is about 100 amino acids long, include (a) targeting of the protein to the secretory pathway, (b) intramolecular chaperone-like function, and (c) assisting the specialised intracellular protease processing system. This C-terminal domain is embedded in the endoplasmic reticulum lumen, and binds to the N-terminal, transmembrane, SP_C, pfam08999 provided that it is in non-helical conformation. Thus the Brichos domain of proSP-C is a chaperone that induces alpha-helix formation of an aggregation-prone TM region.


Pssm-ID: 198107  Cd Length: 96  Bit Score: 91.18  E-value: 6.52e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239962638   50 FSIGSTGIVVYDYQRLLIAYKPAPGTCCYIMKMTPENIPSLEALTRKFQDfqvKPAVSTSKLGQEE-GHDAGSASPGDPL 128
Cdd:smart01039   1 FSGSDSWTVIHDFKNGLTAYRPLGKKKCYIKKMNKEVIPSLQSLLELLEN---KKMPGGPYPKQTYyVVEPVVGEKIKDL 77

                           90
                   ....*....|....*....
gi 1239962638  129 DFLGTTVSTLCGEVPLFYI 147
Cdd:smart01039  78 SFLGSPIAELCKGVPTYWL 96
BRICHOS pfam04089
BRICHOS domain; The BRICHOS domain is about 100 amino acids long. It is found in a variety of ...
 52-146 1.38e-23

BRICHOS domain; The BRICHOS domain is about 100 amino acids long. It is found in a variety of proteins implicated in dementia, respiratory distress and cancer. Its exact function is unknown; roles that have been proposed for it include (a) in targeting of the protein to the secretory pathway, (b) intramolecular chaperone-like function, and (c) assisting the specialized intracellular protease processing system. This C-terminal domain is embedded in the endoplasmic reticulum lumen, and binds to the N-terminal, transmembrane, SP_C, pfam08999, provided that it is in non-helical conformation. Thus the Brichos domain of proSP-C is a chaperone that induces alpha-helix formation of an aggregation-prone TM region.


Pssm-ID: 461168  Cd Length: 91  Bit Score: 87.75  E-value: 1.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239962638  52 IGSTGIVVYDYQRLLIAYKPAPGTCCYIMKMTPENIPSLEALTRKFQDFQVKPAVSTSKLGQEEGHDagsaSPGDPLDFL 131
Cdd:pfam04089   1 GNDSATVIHDFKNGLTAYRDLSLKKCYIMKMDKSDVPPLQELLRLLENKEEGEGPPPESLGVYVPQT----RPVKDLSFL 76

                          90
                  ....*....|....*
gi 1239962638 132 GTTVSTLCGEVPLFY 146
Cdd:pfam04089  77 GSPIQELCRGLPTYW 91
SP_C-Propep pfam08999
Surfactant protein C, N terminal propeptide; The N-terminal propeptide of surfactant protein C ...
 24-49 9.04e-07

Surfactant protein C, N terminal propeptide; The N-terminal propeptide of surfactant protein C adopts an alpha-helical structure, with turn and extended regions. It's main function is the stabilization of metastable surfactant protein C (SP-C), since the latter can irreversibly transform from its native alpha-helical structure to beta-sheet aggregates and form amyloid-like fibrils. The correct intracellular trafficking of proSP-C has also been reported to depend on the propeptide.


Pssm-ID: 286135  Cd Length: 96  Bit Score: 44.66  E-value: 9.04e-07
                          10        20
                  ....*....|....*....|....*.
gi 1239962638  24 VLEMSMGGPEAQQRLALQERVGTTAT 49
Cdd:pfam08999  71 ILEMSIGAPDVQQRLALSEHAGTIAT 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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