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Conserved domains on  [gi|2306267214|ref|NP_001399058|]
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pyroglutamyl-peptidase 1-like protein isoform 3 [Homo sapiens]

Protein Classification

C15 family peptidase( domain architecture ID 1560)

C15 family peptidase contains a Cys-His-Glu/Asp catalytic triad, such as pyrrolidone-carboxylate peptidase, also called pyroglutamyl-peptidase I (PGP-I), that cleaves 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 PGP

CATH:  3.40.630.20
EC:  3.4.19.-
Gene Ontology:  GO:0008234|GO:0006508
MEROPS:  C15
PubMed:  9920379|7824521|11517925
SCOP:  4000580

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 3.38e-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: 3.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306267214   5 AKAIILEQSGKNQGY-RDADIRSFWPEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLH- 82
Cdd:cd00501    73 RSTITIERVAINIDDaRIPDNEGNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPARVSNDAGTYLCNHVYYGSLHe 152

                          90       100
                  ....*....|....*....|
gi 2306267214  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 3.38e-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: 3.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306267214   5 AKAIILEQSGKNQGY-RDADIRSFWPEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLH- 82
Cdd:cd00501    73 RSTITIERVAINIDDaRIPDNEGNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPARVSNDAGTYLCNHVYYGSLHe 152

                          90       100
                  ....*....|....*....|
gi 2306267214  83 -HGKGC---AALIHVPPLSR 98
Cdd:cd00501   153 sATRGPfirAGFIHVPYSPE 172
Pcp COG2039
Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational ...
 36-110 2.16e-06

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


Pssm-ID: 441642  Cd Length: 203  Bit Score: 45.18  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306267214  36 PGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHH----GKGCAAL-IHVPPLSR---------GLP 101
Cdd:COG2039   105 ADGPAAYFSTLPIKAIVAALRAAGIPASVSNTAGTYVCNHVMYRLLHLlatkGPPIRAGfIHVPYLPEqaaakpgtpSMS 184


                  ....*....
gi 2306267214 102 ASLLGRALR 110
Cdd:COG2039   185 LEDIVRALE 193
Peptidase_C15 pfam01470
Pyroglutamyl peptidase;
20-94 7.00e-06

Pyroglutamyl peptidase;


Pssm-ID: 426276  Cd Length: 203  Bit Score: 43.65  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306267214  20 RDADIRSFWPEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHH--GKGC---AALIHVP 94
Cdd:pfam01470  88 RIPDNEGRQPIDEPIDPDGPVAYFSTLPVKAMTLKMREAGIPAAVSNSAGTFVCNHLMYGLLHHlaQKGPpvrAGFIHVP 167
PRK13194 PRK13194
pyrrolidone-carboxylate peptidase; Provisional
 29-114 1.78e-05

pyrrolidone-carboxylate peptidase; Provisional


Pssm-ID: 183887  Cd Length: 208  Bit Score: 42.56  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306267214  29 PEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHHG--KG---CAALIHVPPlsrgLPAS 103
Cdd:PRK13194   98 PEDEPIVEGAPAAYFATLPTREIVEELKKNGIPAVLSYSAGTYLCNYVMYLTLHHSatKGypkMAGFIHVPY----TPDQ 173

                          90
                  ....*....|.
gi 2306267214 104 LLGRALRGHHP 114
Cdd:PRK13194  174 VIEKIGKGKNT 184
pyro_pdase TIGR00504
pyroglutamyl-peptidase I; Alternate names include pyroglutamate aminopeptidase, ...
 36-111 3.89e-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: 41.75  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306267214  36 PGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHH--GKGC---AALIHVPPL------SRGLPASL 104
Cdd:TIGR00504 103 PDGPAAYFATLPVRAMVLAMKKAGIPADVSYTAGTFVCNHLMYGLLHHlaQKGLpvrAGFIHVPYLpsqvalKHGVPSMS 182


                  ....*..
gi 2306267214 105 LGRALRG 111
Cdd:TIGR00504 183 LDTAVAG 189
 
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 3.38e-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: 3.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306267214   5 AKAIILEQSGKNQGY-RDADIRSFWPEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLH- 82
Cdd:cd00501    73 RSTITIERVAINIDDaRIPDNEGNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPARVSNDAGTYLCNHVYYGSLHe 152

                          90       100
                  ....*....|....*....|
gi 2306267214  83 -HGKGC---AALIHVPPLSR 98
Cdd:cd00501   153 sATRGPfirAGFIHVPYSPE 172
Pcp COG2039
Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational ...
 36-110 2.16e-06

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


Pssm-ID: 441642  Cd Length: 203  Bit Score: 45.18  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306267214  36 PGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHH----GKGCAAL-IHVPPLSR---------GLP 101
Cdd:COG2039   105 ADGPAAYFSTLPIKAIVAALRAAGIPASVSNTAGTYVCNHVMYRLLHLlatkGPPIRAGfIHVPYLPEqaaakpgtpSMS 184


                  ....*....
gi 2306267214 102 ASLLGRALR 110
Cdd:COG2039   185 LEDIVRALE 193
Peptidase_C15 pfam01470
Pyroglutamyl peptidase;
20-94 7.00e-06

Pyroglutamyl peptidase;


Pssm-ID: 426276  Cd Length: 203  Bit Score: 43.65  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306267214  20 RDADIRSFWPEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHH--GKGC---AALIHVP 94
Cdd:pfam01470  88 RIPDNEGRQPIDEPIDPDGPVAYFSTLPVKAMTLKMREAGIPAAVSNSAGTFVCNHLMYGLLHHlaQKGPpvrAGFIHVP 167
PRK13194 PRK13194
pyrrolidone-carboxylate peptidase; Provisional
 29-114 1.78e-05

pyrrolidone-carboxylate peptidase; Provisional


Pssm-ID: 183887  Cd Length: 208  Bit Score: 42.56  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306267214  29 PEGGVCLPGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHHG--KG---CAALIHVPPlsrgLPAS 103
Cdd:PRK13194   98 PEDEPIVEGAPAAYFATLPTREIVEELKKNGIPAVLSYSAGTYLCNYVMYLTLHHSatKGypkMAGFIHVPY----TPDQ 173

                          90
                  ....*....|.
gi 2306267214 104 LLGRALRGHHP 114
Cdd:PRK13194  174 VIEKIGKGKNT 184
pyro_pdase TIGR00504
pyroglutamyl-peptidase I; Alternate names include pyroglutamate aminopeptidase, ...
 36-111 3.89e-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: 41.75  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306267214  36 PGSPDVLESGVCMKAVCKRVAVEGVDVIFSRDAGRYVCDYTYYLSLHH--GKGC---AALIHVPPL------SRGLPASL 104
Cdd:TIGR00504 103 PDGPAAYFATLPVRAMVLAMKKAGIPADVSYTAGTFVCNHLMYGLLHHlaQKGLpvrAGFIHVPYLpsqvalKHGVPSMS 182


                  ....*..
gi 2306267214 105 LGRALRG 111
Cdd:TIGR00504 183 LDTAVAG 189
 
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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