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Conserved domains on  [gi|2082545130|gb|QZA76294|]
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xaa-pro dipeptidyl-peptidase, partial [Limosilactobacillus fermentum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05371 super family cl47124
x-prolyl-dipeptidyl aminopeptidase; Provisional
 1-193 2.42e-63

x-prolyl-dipeptidyl aminopeptidase; Provisional


The actual alignment was detected with superfamily member PRK05371:

Pssm-ID: 481464 [Multi-domain]  Cd Length: 767  Bit Score: 208.32  E-value: 2.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082545130   1 PLEYPLLGIKRSNLPHHYheewdqAAVIDSFYLLLLTRTKNGISLLDKLTSQGMLtwtyhlPASQKPIFFNGKPVASFNP 80
Cdd:PRK05371   98 TLNDALAFMKKIGLPIVT------TDLIKALYQLLNTRTKNGQTLIDSLVSQGLL------PGDNKPHFFNGKSLPVFDT 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082545130  81 HRFIHEVVYVQTDLDTDFDGEADLVKAEVIRPADSNQGLKVPVLFTASPYNQGTNDEWGEKITHDVNVPLTHKDPDADsp 160
Cdd:PRK05371  166 SQLIREVVYVETPVDTDQDGKLDLVKVTIVRPKETASGLKVPVIMTASPYYQGTNDVANDKKLHNVDVELYAKPPRAQ-- 243

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2082545130 161 aeatFPTPAQHRDIQGVGPASERFAATPSYTLN 193
Cdd:PRK05371  244 ----FTPLKTQPRKLPVGPAEESFTHINSYSLN 272
 
Name Accession Description Interval E-value
PRK05371 PRK05371
x-prolyl-dipeptidyl aminopeptidase; Provisional
 1-193 2.42e-63

x-prolyl-dipeptidyl aminopeptidase; Provisional


Pssm-ID: 235435 [Multi-domain]  Cd Length: 767  Bit Score: 208.32  E-value: 2.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082545130   1 PLEYPLLGIKRSNLPHHYheewdqAAVIDSFYLLLLTRTKNGISLLDKLTSQGMLtwtyhlPASQKPIFFNGKPVASFNP 80
Cdd:PRK05371   98 TLNDALAFMKKIGLPIVT------TDLIKALYQLLNTRTKNGQTLIDSLVSQGLL------PGDNKPHFFNGKSLPVFDT 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082545130  81 HRFIHEVVYVQTDLDTDFDGEADLVKAEVIRPADSNQGLKVPVLFTASPYNQGTNDEWGEKITHDVNVPLTHKDPDADsp 160
Cdd:PRK05371  166 SQLIREVVYVETPVDTDQDGKLDLVKVTIVRPKETASGLKVPVIMTASPYYQGTNDVANDKKLHNVDVELYAKPPRAQ-- 243

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2082545130 161 aeatFPTPAQHRDIQGVGPASERFAATPSYTLN 193
Cdd:PRK05371  244 ----FTPLKTQPRKLPVGPAEESFTHINSYSLN 272
PepX_N pfam09168
X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal; Members of this family adopt a secondary ...
 5-53 1.86e-13

X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal; Members of this family adopt a secondary structure consisting of a helical bundle of eight alpha helices and three beta strands, the last alpha helix connecting to the first strand of the catalytic domain. The first strand of the N-terminus also forms a small parallel beta sheet with strand 5' of catalytic domain. The domain mediates dimerization of the protein, with two proline residues present in the domain being critical for interaction.


Pssm-ID: 430445  Cd Length: 157  Bit Score: 64.96  E-value: 1.86e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2082545130   5 PLLGIKRSNLPHHYHEEWDQAAVIDSFYLLLLTRTKNGISLLDKLTSQG 53
Cdd:pfam09168 108 PLAFMKKINLPVVDQEKFDTENLISAFYLLLNTRTKNGQTLIDQLVSDG 156
PepX_N smart00940
X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal; This N-terminal domain adopts a secondary ...
 5-54 6.60e-13

X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal; This N-terminal domain adopts a secondary structure consisting of a helical bundle of eight alpha helices and three beta strands, with the last alpha helix connecting to the first strand of the catalytic domain. The first strand of the N-terminus also forms a small parallel beta sheet with strand five of the catalytic domain. This domain mediates dimerisation of the protein, with two proline residues present in the domain being critical for interaction.


Pssm-ID: 198008  Cd Length: 156  Bit Score: 63.45  E-value: 6.60e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2082545130    5 PLLGIKRSNLPHHYHEEWDQAAVIDSFYLLLLTRTKNGISLLDKLTSQGM 54
Cdd:smart00940 107 PLAFMKKIGLPVVDHIIFTTENLIEALYQLLNTRTKNGQTLIDQLVSQGY 156
 
Name Accession Description Interval E-value
PRK05371 PRK05371
x-prolyl-dipeptidyl aminopeptidase; Provisional
 1-193 2.42e-63

x-prolyl-dipeptidyl aminopeptidase; Provisional


Pssm-ID: 235435 [Multi-domain]  Cd Length: 767  Bit Score: 208.32  E-value: 2.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082545130   1 PLEYPLLGIKRSNLPHHYheewdqAAVIDSFYLLLLTRTKNGISLLDKLTSQGMLtwtyhlPASQKPIFFNGKPVASFNP 80
Cdd:PRK05371   98 TLNDALAFMKKIGLPIVT------TDLIKALYQLLNTRTKNGQTLIDSLVSQGLL------PGDNKPHFFNGKSLPVFDT 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082545130  81 HRFIHEVVYVQTDLDTDFDGEADLVKAEVIRPADSNQGLKVPVLFTASPYNQGTNDEWGEKITHDVNVPLTHKDPDADsp 160
Cdd:PRK05371  166 SQLIREVVYVETPVDTDQDGKLDLVKVTIVRPKETASGLKVPVIMTASPYYQGTNDVANDKKLHNVDVELYAKPPRAQ-- 243

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2082545130 161 aeatFPTPAQHRDIQGVGPASERFAATPSYTLN 193
Cdd:PRK05371  244 ----FTPLKTQPRKLPVGPAEESFTHINSYSLN 272
PepX_N pfam09168
X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal; Members of this family adopt a secondary ...
 5-53 1.86e-13

X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal; Members of this family adopt a secondary structure consisting of a helical bundle of eight alpha helices and three beta strands, the last alpha helix connecting to the first strand of the catalytic domain. The first strand of the N-terminus also forms a small parallel beta sheet with strand 5' of catalytic domain. The domain mediates dimerization of the protein, with two proline residues present in the domain being critical for interaction.


Pssm-ID: 430445  Cd Length: 157  Bit Score: 64.96  E-value: 1.86e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2082545130   5 PLLGIKRSNLPHHYHEEWDQAAVIDSFYLLLLTRTKNGISLLDKLTSQG 53
Cdd:pfam09168 108 PLAFMKKINLPVVDQEKFDTENLISAFYLLLNTRTKNGQTLIDQLVSDG 156
PepX_N smart00940
X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal; This N-terminal domain adopts a secondary ...
 5-54 6.60e-13

X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal; This N-terminal domain adopts a secondary structure consisting of a helical bundle of eight alpha helices and three beta strands, with the last alpha helix connecting to the first strand of the catalytic domain. The first strand of the N-terminus also forms a small parallel beta sheet with strand five of the catalytic domain. This domain mediates dimerisation of the protein, with two proline residues present in the domain being critical for interaction.


Pssm-ID: 198008  Cd Length: 156  Bit Score: 63.45  E-value: 6.60e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2082545130    5 PLLGIKRSNLPHHYHEEWDQAAVIDSFYLLLLTRTKNGISLLDKLTSQGM 54
Cdd:smart00940 107 PLAFMKKIGLPVVDHIIFTTENLIEALYQLLNTRTKNGQTLIDQLVSQGY 156
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
99-150 5.27e-04

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 39.63  E-value: 5.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2082545130  99 DGeaDLVKAEVIRPADSnqGLKVPVLFTASPYNQGTNDEWgEKITHDVNVPL 150
Cdd:pfam02129   1 DG--VRLAADIYRPTKT--GGPVPALLTRSPYGARRDGAS-DLALAHPEWEF 47
 
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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