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Conserved domains on  [gi|268834371|ref|NP_001161374|]
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pyroglutamyl-peptidase 1-like protein isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C15 super family cl00237
Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: ...
 5-98 2.23e-18

Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: Enzymes responsible for cleaving pyroglutamate (pGlu) from the N-terminal end of specialized proteins. The N-terminal pGlu protects these proteins from proteolysis by other proteases until the pGlu is removed by a PGP. PGPs are cysteine proteases with a Cys-His-Glu/Asp catalytic triad. Type I PGPs are found in a wide variety of prokaryotes and eukaryotes. It is not clear whether the functional form is a monomer, a homodimer, or a homotetramer.


The actual alignment was detected with superfamily member cd00501:

Pssm-ID: 444776  Cd Length: 194  Bit Score: 76.92  E-value: 2.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268834371   5 AKAIILEQSGKNQGY-RDADIRSFWPEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLH- 82
Cdd:cd00501   73 RSTITIERVAINIDDaRIPDNEGNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPARVSNDAGTYLCNHVYYGSLHe 152

                         90       100
                 ....*....|....*....|
gi 268834371  83 -HGKGC---AALIHVPPLSR 98
Cdd:cd00501  153 sATRGPfirAGFIHVPYSPE 172
 
Name Accession Description Interval E-value
Peptidase_C15 cd00501
Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: ...
 5-98 2.23e-18

Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: Enzymes responsible for cleaving pyroglutamate (pGlu) from the N-terminal end of specialized proteins. The N-terminal pGlu protects these proteins from proteolysis by other proteases until the pGlu is removed by a PGP. PGPs are cysteine proteases with a Cys-His-Glu/Asp catalytic triad. Type I PGPs are found in a wide variety of prokaryotes and eukaryotes. It is not clear whether the functional form is a monomer, a homodimer, or a homotetramer.


Pssm-ID: 238279  Cd Length: 194  Bit Score: 76.92  E-value: 2.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268834371   5 AKAIILEQSGKNQGY-RDADIRSFWPEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLH- 82
Cdd:cd00501   73 RSTITIERVAINIDDaRIPDNEGNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPARVSNDAGTYLCNHVYYGSLHe 152

                         90       100
                 ....*....|....*....|
gi 268834371  83 -HGKGC---AALIHVPPLSR 98
Cdd:cd00501  153 sATRGPfirAGFIHVPYSPE 172
Pcp COG2039
Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational ...
 36-119 1.21e-09

Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441642  Cd Length: 203  Bit Score: 54.04  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268834371  36 PGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHH----GKGCAAL-IHVPPLSR---------GLP 101
Cdd:COG2039  105 ADGPAAYFSTLPIKAIVAALRAAGIPASVSNTAGTYVCNHVMYRLLHLlatkGPPIRAGfIHVPYLPEqaaakpgtpSMS 184

                         90
                 ....*....|....*...
gi 268834371 102 ASLLGRALRVIIQEMLEE 119
Cdd:COG2039  185 LEDIVRALEAAIEAALEA 202
Peptidase_C15 pfam01470
Pyroglutamyl peptidase;
20-94 6.10e-06

Pyroglutamyl peptidase;


Pssm-ID: 426276  Cd Length: 203  Bit Score: 43.65  E-value: 6.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268834371   20 RDADIRSFWPEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHH--GKGC---AALIHVP 94
Cdd:pfam01470  88 RIPDNEGRQPIDEPIDPDGPVAYFSTLPVKAMTLKMREAGIPAAVSNSAGTFVCNHLMYGLLHHlaQKGPpvrAGFIHVP 167
PRK13194 PRK13194
pyrrolidone-carboxylate peptidase; Provisional
 29-94 3.72e-05

pyrrolidone-carboxylate peptidase; Provisional


Pssm-ID: 183887  Cd Length: 208  Bit Score: 41.79  E-value: 3.72e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268834371  29 PEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHHG--KG---CAALIHVP 94
Cdd:PRK13194  98 PEDEPIVEGAPAAYFATLPTREIVEELKKNGIPAVLSYSAGTYLCNYVMYLTLHHSatKGypkMAGFIHVP 168
pyro_pdase TIGR00504
pyroglutamyl-peptidase I; Alternate names include pyroglutamate aminopeptidase, ...
 36-94 4.22e-05

pyroglutamyl-peptidase I; Alternate names include pyroglutamate aminopeptidase, pyrrolidone-carboxylate peptidase, and 5-oxoprolyl-peptidase. It removes pyroglutamate (pyrrolidone-carboxylate, a modified glutamine) that can otherwise block hydrolysis of a polypeptide at the amino end, and so can be extremely useful in the biochemical studies of proteins. The biological role in the various species in which it is found is not fully understood. The enzyme appears to be a homodimer. It does not closely resemble any other peptidases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 129595  Cd Length: 212  Bit Score: 41.37  E-value: 4.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268834371   36 PGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHH--GKGC---AALIHVP 94
Cdd:TIGR00504 103 PDGPAAYFATLPVRAMVLAMKKAGIPADVSYTAGTFVCNHLMYGLLHHlaQKGLpvrAGFIHVP 166
 
Name Accession Description Interval E-value
Peptidase_C15 cd00501
Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: ...
 5-98 2.23e-18

Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: Enzymes responsible for cleaving pyroglutamate (pGlu) from the N-terminal end of specialized proteins. The N-terminal pGlu protects these proteins from proteolysis by other proteases until the pGlu is removed by a PGP. PGPs are cysteine proteases with a Cys-His-Glu/Asp catalytic triad. Type I PGPs are found in a wide variety of prokaryotes and eukaryotes. It is not clear whether the functional form is a monomer, a homodimer, or a homotetramer.


Pssm-ID: 238279  Cd Length: 194  Bit Score: 76.92  E-value: 2.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268834371   5 AKAIILEQSGKNQGY-RDADIRSFWPEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLH- 82
Cdd:cd00501   73 RSTITIERVAINIDDaRIPDNEGNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPARVSNDAGTYLCNHVYYGSLHe 152

                         90       100
                 ....*....|....*....|
gi 268834371  83 -HGKGC---AALIHVPPLSR 98
Cdd:cd00501  153 sATRGPfirAGFIHVPYSPE 172
Pcp COG2039
Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational ...
 36-119 1.21e-09

Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441642  Cd Length: 203  Bit Score: 54.04  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268834371  36 PGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHH----GKGCAAL-IHVPPLSR---------GLP 101
Cdd:COG2039  105 ADGPAAYFSTLPIKAIVAALRAAGIPASVSNTAGTYVCNHVMYRLLHLlatkGPPIRAGfIHVPYLPEqaaakpgtpSMS 184

                         90
                 ....*....|....*...
gi 268834371 102 ASLLGRALRVIIQEMLEE 119
Cdd:COG2039  185 LEDIVRALEAAIEAALEA 202
Peptidase_C15 pfam01470
Pyroglutamyl peptidase;
20-94 6.10e-06

Pyroglutamyl peptidase;


Pssm-ID: 426276  Cd Length: 203  Bit Score: 43.65  E-value: 6.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268834371   20 RDADIRSFWPEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHH--GKGC---AALIHVP 94
Cdd:pfam01470  88 RIPDNEGRQPIDEPIDPDGPVAYFSTLPVKAMTLKMREAGIPAAVSNSAGTFVCNHLMYGLLHHlaQKGPpvrAGFIHVP 167
PRK13194 PRK13194
pyrrolidone-carboxylate peptidase; Provisional
 29-94 3.72e-05

pyrrolidone-carboxylate peptidase; Provisional


Pssm-ID: 183887  Cd Length: 208  Bit Score: 41.79  E-value: 3.72e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268834371  29 PEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHHG--KG---CAALIHVP 94
Cdd:PRK13194  98 PEDEPIVEGAPAAYFATLPTREIVEELKKNGIPAVLSYSAGTYLCNYVMYLTLHHSatKGypkMAGFIHVP 168
pyro_pdase TIGR00504
pyroglutamyl-peptidase I; Alternate names include pyroglutamate aminopeptidase, ...
 36-94 4.22e-05

pyroglutamyl-peptidase I; Alternate names include pyroglutamate aminopeptidase, pyrrolidone-carboxylate peptidase, and 5-oxoprolyl-peptidase. It removes pyroglutamate (pyrrolidone-carboxylate, a modified glutamine) that can otherwise block hydrolysis of a polypeptide at the amino end, and so can be extremely useful in the biochemical studies of proteins. The biological role in the various species in which it is found is not fully understood. The enzyme appears to be a homodimer. It does not closely resemble any other peptidases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 129595  Cd Length: 212  Bit Score: 41.37  E-value: 4.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268834371   36 PGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHH--GKGC---AALIHVP 94
Cdd:TIGR00504 103 PDGPAAYFATLPVRAMVLAMKKAGIPADVSYTAGTFVCNHLMYGLLHHlaQKGLpvrAGFIHVP 166
 
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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