NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|388597723|gb|AFK76017|]
View 

dipeptidyl peptidase 1 isoform a preproprotein, partial [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CathepsinC_exc super family cl07399
Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological ...
 1-32 3.66e-15

Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor.


The actual alignment was detected with superfamily member pfam08773:

Pssm-ID: 462598 [Multi-domain]  Cd Length: 118  Bit Score: 63.45  E-value: 3.66e-15
                          10        20        30
                  ....*....|....*....|....*....|..
gi 388597723    1 YKEEGSKVTTYCNETMTGWVHDVLGRNWACFT 32
Cdd:pfam08773  87 YKKNGSNVTSYCNETLPGWYHDVLGKNWACFR 118
 
Name Accession Description Interval E-value
CathepsinC_exc pfam08773
Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological ...
 1-32 3.66e-15

Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor.


Pssm-ID: 462598 [Multi-domain]  Cd Length: 118  Bit Score: 63.45  E-value: 3.66e-15
                          10        20        30
                  ....*....|....*....|....*....|..
gi 388597723    1 YKEEGSKVTTYCNETMTGWVHDVLGRNWACFT 32
Cdd:pfam08773  87 YKKNGSNVTSYCNETLPGWYHDVLGKNWACFR 118
 
Name Accession Description Interval E-value
CathepsinC_exc pfam08773
Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological ...
 1-32 3.66e-15

Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor.


Pssm-ID: 462598 [Multi-domain]  Cd Length: 118  Bit Score: 63.45  E-value: 3.66e-15
                          10        20        30
                  ....*....|....*....|....*....|..
gi 388597723    1 YKEEGSKVTTYCNETMTGWVHDVLGRNWACFT 32
Cdd:pfam08773  87 YKKNGSNVTSYCNETLPGWYHDVLGKNWACFR 118
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH