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Conserved domains on  [gi|767904631|ref|XP_011539880|]
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peroxisomal membrane protein PEX14 isoform X2 [Homo sapiens]

Protein Classification

peroxisomal membrane protein PEX14( domain architecture ID 10520091)

peroxisomal membrane protein PEX14 is a receptor-docking protein which is located on the cytoplasmic surface of the peroxisomal membrane and binds peroxisomal targeting signal (PTS) receptors carrying proteins bound for the peroxisomal matrix.

CATH:  1.10.10.10
Gene Ontology:  GO:0005778|GO:0016560|GO:0005515|GO:0008320
SCOP:  4005026
TCDB:  3.A.20

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pex14_N pfam04695
Pex14 N-terminal domain; Family of peroxisomal membrane anchor proteins which bind the PTS1 ...
 9-49 4.14e-13

Pex14 N-terminal domain; Family of peroxisomal membrane anchor proteins which bind the PTS1 (peroxisomal targeting signal) receptor and are required for the import of PTS1-containing proteins into peroxisomes. Loss of functional Pex14p results in defects in both the PTS1 and PTS2-dependent import pathways. Deletion analysis of this conserved region implicates it in selective peroxisome degradation. In the majority of members this region is situated at the N-terminus of the protein.


:

Pssm-ID: 461395 [Multi-domain]  Cd Length: 46  Bit Score: 62.96  E-value: 4.14e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767904631    9 MIATAVKFLQNSRVRQSPLATRRAFLKKKGLTDEEIDMAFQ 49
Cdd:pfam04695   5 LLEQARKFLQDPSVRNAPREKKVAFLKSKGLSDEEIEELLG 45
 
Name Accession Description Interval E-value
Pex14_N pfam04695
Pex14 N-terminal domain; Family of peroxisomal membrane anchor proteins which bind the PTS1 ...
 9-49 4.14e-13

Pex14 N-terminal domain; Family of peroxisomal membrane anchor proteins which bind the PTS1 (peroxisomal targeting signal) receptor and are required for the import of PTS1-containing proteins into peroxisomes. Loss of functional Pex14p results in defects in both the PTS1 and PTS2-dependent import pathways. Deletion analysis of this conserved region implicates it in selective peroxisome degradation. In the majority of members this region is situated at the N-terminus of the protein.


Pssm-ID: 461395 [Multi-domain]  Cd Length: 46  Bit Score: 62.96  E-value: 4.14e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767904631    9 MIATAVKFLQNSRVRQSPLATRRAFLKKKGLTDEEIDMAFQ 49
Cdd:pfam04695   5 LLEQARKFLQDPSVRNAPREKKVAFLKSKGLSDEEIEELLG 45
 
Name Accession Description Interval E-value
Pex14_N pfam04695
Pex14 N-terminal domain; Family of peroxisomal membrane anchor proteins which bind the PTS1 ...
 9-49 4.14e-13

Pex14 N-terminal domain; Family of peroxisomal membrane anchor proteins which bind the PTS1 (peroxisomal targeting signal) receptor and are required for the import of PTS1-containing proteins into peroxisomes. Loss of functional Pex14p results in defects in both the PTS1 and PTS2-dependent import pathways. Deletion analysis of this conserved region implicates it in selective peroxisome degradation. In the majority of members this region is situated at the N-terminus of the protein.


Pssm-ID: 461395 [Multi-domain]  Cd Length: 46  Bit Score: 62.96  E-value: 4.14e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767904631    9 MIATAVKFLQNSRVRQSPLATRRAFLKKKGLTDEEIDMAFQ 49
Cdd:pfam04695   5 LLEQARKFLQDPSVRNAPREKKVAFLKSKGLSDEEIEELLG 45
 
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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