NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|32564478|ref|NP_871977|]
View 

Uncharacterized protein CELE_F32A5.4 [Caenorhabditis elegans]

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
Pepsin-I3 pfam06394
Pepsin inhibitor-3-like repeated domain; Pepsin inhibitor-3 consisting of two domains, each ...
51-124 3.04e-34

Pepsin inhibitor-3-like repeated domain; Pepsin inhibitor-3 consisting of two domains, each comprising an antiparallel beta-sheet flanked by an alpha-helix. In the enzyme-inhibitor complex, the N-terminal beta-strand of PI-3 pairs with one strand of the active site flap region of pepsin. The two domains are tandem repeats of sequence, and has therefore been termed repeated domain.


:

Pssm-ID: 461895  Cd Length: 74  Bit Score: 115.34  E-value: 3.04e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32564478    51 KAPEKPSFCTAEDTTQYYFDGCMVQGNKVYVGGQYARDLSSDEISELQTFDTQQTAYQNAVQSQMQSQVQGLFG 124
Cdd:pfam06394   1 KAPEKPSFCTAEVTGQGGFDGCVVQGNKLYANGQYLRDLTSEEQSELATYDTQQTAYKNALQSSLQERRKGLFG 74
 
Name Accession Description Interval E-value
Pepsin-I3 pfam06394
Pepsin inhibitor-3-like repeated domain; Pepsin inhibitor-3 consisting of two domains, each ...
51-124 3.04e-34

Pepsin inhibitor-3-like repeated domain; Pepsin inhibitor-3 consisting of two domains, each comprising an antiparallel beta-sheet flanked by an alpha-helix. In the enzyme-inhibitor complex, the N-terminal beta-strand of PI-3 pairs with one strand of the active site flap region of pepsin. The two domains are tandem repeats of sequence, and has therefore been termed repeated domain.


Pssm-ID: 461895  Cd Length: 74  Bit Score: 115.34  E-value: 3.04e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32564478    51 KAPEKPSFCTAEDTTQYYFDGCMVQGNKVYVGGQYARDLSSDEISELQTFDTQQTAYQNAVQSQMQSQVQGLFG 124
Cdd:pfam06394   1 KAPEKPSFCTAEVTGQGGFDGCVVQGNKLYANGQYLRDLTSEEQSELATYDTQQTAYKNALQSSLQERRKGLFG 74
API3 cd00225
Ascaris pepsin inhibitor-3 (API3); protein inhibitor that reversibly inhibits aspartic ...
49-108 1.58e-33

Ascaris pepsin inhibitor-3 (API3); protein inhibitor that reversibly inhibits aspartic proteinase cathepsin E, and gastric enzymes pepsin and gastricsin.


Pssm-ID: 119406 [Multi-domain]  Cd Length: 159  Bit Score: 116.21  E-value: 1.58e-33
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564478  49 IPKAPEKPSFCTAEDTTQYYFDGCMVQGNKVYVGGQYARDLSSDEISELQTFDTQQTAYQ 108
Cdd:cd00225  83 LPKAPKKPSFCSPDDTTQFYFDGCMVQNNKVYVGNTYARDLTPKEIAELKTFEKKQTAYQ 142
 
Name Accession Description Interval E-value
Pepsin-I3 pfam06394
Pepsin inhibitor-3-like repeated domain; Pepsin inhibitor-3 consisting of two domains, each ...
51-124 3.04e-34

Pepsin inhibitor-3-like repeated domain; Pepsin inhibitor-3 consisting of two domains, each comprising an antiparallel beta-sheet flanked by an alpha-helix. In the enzyme-inhibitor complex, the N-terminal beta-strand of PI-3 pairs with one strand of the active site flap region of pepsin. The two domains are tandem repeats of sequence, and has therefore been termed repeated domain.


Pssm-ID: 461895  Cd Length: 74  Bit Score: 115.34  E-value: 3.04e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32564478    51 KAPEKPSFCTAEDTTQYYFDGCMVQGNKVYVGGQYARDLSSDEISELQTFDTQQTAYQNAVQSQMQSQVQGLFG 124
Cdd:pfam06394   1 KAPEKPSFCTAEVTGQGGFDGCVVQGNKLYANGQYLRDLTSEEQSELATYDTQQTAYKNALQSSLQERRKGLFG 74
API3 cd00225
Ascaris pepsin inhibitor-3 (API3); protein inhibitor that reversibly inhibits aspartic ...
49-108 1.58e-33

Ascaris pepsin inhibitor-3 (API3); protein inhibitor that reversibly inhibits aspartic proteinase cathepsin E, and gastric enzymes pepsin and gastricsin.


Pssm-ID: 119406 [Multi-domain]  Cd Length: 159  Bit Score: 116.21  E-value: 1.58e-33
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564478  49 IPKAPEKPSFCTAEDTTQYYFDGCMVQGNKVYVGGQYARDLSSDEISELQTFDTQQTAYQ 108
Cdd:cd00225  83 LPKAPKKPSFCSPDDTTQFYFDGCMVQNNKVYVGNTYARDLTPKEIAELKTFEKKQTAYQ 142
API3 cd00225
Ascaris pepsin inhibitor-3 (API3); protein inhibitor that reversibly inhibits aspartic ...
71-172 1.40e-04

Ascaris pepsin inhibitor-3 (API3); protein inhibitor that reversibly inhibits aspartic proteinase cathepsin E, and gastric enzymes pepsin and gastricsin.


Pssm-ID: 119406 [Multi-domain]  Cd Length: 159  Bit Score: 40.32  E-value: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564478  71 GCMVQGNKVYVGGQYARDLSSDEISELQTFDTQQTAYQNAVQSQMQSQVQGLfggsdflsalfggdrfnqqQQRQQPSST 150
Cdd:cd00225  13 GCVVTDNVLFANGFPLRELTPDEQQELAQYVEDVADYKEEVKQALKERQEGL-------------------KLRRAGKKK 73
                        90       100
                ....*....|....*....|..
gi 32564478 151 TPASTSSTTLPPKPTVPQFCTA 172
Cdd:cd00225  74 KAVTLAEEKLPKAPKKPSFCSP 95
 
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