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Conserved domains on  [gi|545746264|ref|NP_001271147|]
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cytosolic carboxypeptidase 1 isoform 2 [Mus musculus]

Protein Classification

cytosolic carboxypeptidase N-terminal domain-containing protein( domain architecture ID 1564195)

cytosolic carboxypeptidase N-terminal domain-containing protein; this N-terminal domain may contribute to folding, might have a regulatory function and/or might be involved in binding other proteins

MEROPS:  M14
PubMed:  7674922|10493853

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pepdidase_M14_N super family cl39445
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
 704-778 1.31e-11

Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain of cytosolic carboxypeptidases. The N-terminal domain folds into a nine-stranded antiparallel beta sandwich. This domain is specific to CCP proteins and is absent in other carboxypeptidases. It has been hypothesized that the N-terminal domain might contribute to folding, might have a regulatory function and/or might be involved in binding other proteins.


The actual alignment was detected with superfamily member pfam18027:

Pssm-ID: 407865  Cd Length: 107  Bit Score: 61.92  E-value: 1.31e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545746264  704 FNSKFESGNLRKVIQIRKSEYDLILNSDINSNHyHQWFYFEVSGMRpGVAYRFNIINCEKSNSQFNYDGEETCYK 778
Cdd:pfam18027   1 ISSNFDSGNIEVVSASDPDAIRLRIRPDNGSEH-FQWFYFRVSGAR-GRPLTFVIENAGEASYPDGWTGYRVVAS 73
 
Name Accession Description Interval E-value
Pepdidase_M14_N pfam18027
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
 704-778 1.31e-11

Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain of cytosolic carboxypeptidases. The N-terminal domain folds into a nine-stranded antiparallel beta sandwich. This domain is specific to CCP proteins and is absent in other carboxypeptidases. It has been hypothesized that the N-terminal domain might contribute to folding, might have a regulatory function and/or might be involved in binding other proteins.


Pssm-ID: 407865  Cd Length: 107  Bit Score: 61.92  E-value: 1.31e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545746264  704 FNSKFESGNLRKVIQIRKSEYDLILNSDINSNHyHQWFYFEVSGMRpGVAYRFNIINCEKSNSQFNYDGEETCYK 778
Cdd:pfam18027   1 ISSNFDSGNIEVVSASDPDAIRLRIRPDNGSEH-FQWFYFRVSGAR-GRPLTFVIENAGEASYPDGWTGYRVVAS 73
 
Name Accession Description Interval E-value
Pepdidase_M14_N pfam18027
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
 704-778 1.31e-11

Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain of cytosolic carboxypeptidases. The N-terminal domain folds into a nine-stranded antiparallel beta sandwich. This domain is specific to CCP proteins and is absent in other carboxypeptidases. It has been hypothesized that the N-terminal domain might contribute to folding, might have a regulatory function and/or might be involved in binding other proteins.


Pssm-ID: 407865  Cd Length: 107  Bit Score: 61.92  E-value: 1.31e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545746264  704 FNSKFESGNLRKVIQIRKSEYDLILNSDINSNHyHQWFYFEVSGMRpGVAYRFNIINCEKSNSQFNYDGEETCYK 778
Cdd:pfam18027   1 ISSNFDSGNIEVVSASDPDAIRLRIRPDNGSEH-FQWFYFRVSGAR-GRPLTFVIENAGEASYPDGWTGYRVVAS 73
 
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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