NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720428173|ref|XP_030099582|]
View 

pyroglutamyl-peptidase 1 isoform X2 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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: ...
 1-122 3.96e-32

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: 111.98  E-value: 3.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428173   1 MATTVTLEKCGHNKGYKGLDNCR-FCPGSQCCVEDGPESIDSIIDMDAVCKRVTTLGLDVsvTISQDAGRYLCDFTYYTS 79
Cdd:cd00501    72 GRSTITIERVAINIDDARIPDNEgNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPA--RVSNDAGTYLCNHVYYGS 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720428173  80 LYQGRGRSAFVHVPPLGKPYNADQLGRALRA--IIEEMLGVLEQA 122
Cdd:cd00501   150 LHESATRGPFIRAGFIHVPYSPEQVADKGAPsmSLETILRALEAA 194
 
Name Accession Description Interval E-value
Peptidase_C15 cd00501
Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: ...
 1-122 3.96e-32

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: 111.98  E-value: 3.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428173   1 MATTVTLEKCGHNKGYKGLDNCR-FCPGSQCCVEDGPESIDSIIDMDAVCKRVTTLGLDVsvTISQDAGRYLCDFTYYTS 79
Cdd:cd00501    72 GRSTITIERVAINIDDARIPDNEgNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPA--RVSNDAGTYLCNHVYYGS 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720428173  80 LYQGRGRSAFVHVPPLGKPYNADQLGRALRA--IIEEMLGVLEQA 122
Cdd:cd00501   150 LHESATRGPFIRAGFIHVPYSPEQVADKGAPsmSLETILRALEAA 194
Pcp COG2039
Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational ...
 2-119 1.26e-13

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


Pssm-ID: 441642  Cd Length: 203  Bit Score: 64.44  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428173   2 ATTVTLEKCGHN-KGYKGLDNCRFCPGSQCCVEDGPESIDSIIDMDAVCKRVTTLGLDVSVtiSQDAGRYLCDFTYYTSL 80
Cdd:COG2039    73 RAAITIERVAINvDDARIPDNDGNQPIDEPIVADGPAAYFSTLPIKAIVAALRAAGIPASV--SNTAGTYVCNHVMYRLL 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720428173  81 Y----QGRG-RSAFVHVPPL--------GKPY-NADQLGRALRAIIEEMLGVL 119
Cdd:COG2039   151 HllatKGPPiRAGFIHVPYLpeqaaakpGTPSmSLEDIVRALEAAIEAALEAL 203
PRK13196 PRK13196
pyroglutamyl-peptidase I;
30-117 1.46e-04

pyroglutamyl-peptidase I;


Pssm-ID: 171895 [Multi-domain]  Cd Length: 211  Bit Score: 39.59  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428173  30 CCVEDGPESIDSIIDMDAVCKRVTTLGLDVSvtISQDAGRYLCDFTYYTSLYQ--GRGRSA----FVHV----------- 92
Cdd:PRK13196  105 CTEPDAPAAYLSTLPLRAILAAWHDAGIPGH--ISNTAGLYVCNFVLYHALHQlhLRGRAEvpcgFLHVpanaqvalava 182

                          90       100
                  ....*....|....*....|....*....
gi 1720428173  93 ---PPLgkPY-NADQLGRALRAIIEEMLG 117
Cdd:PRK13196  183 gdrPPL--PYlPQEEITRAVRVAAETMAG 209
 
Name Accession Description Interval E-value
Peptidase_C15 cd00501
Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: ...
 1-122 3.96e-32

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: 111.98  E-value: 3.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428173   1 MATTVTLEKCGHNKGYKGLDNCR-FCPGSQCCVEDGPESIDSIIDMDAVCKRVTTLGLDVsvTISQDAGRYLCDFTYYTS 79
Cdd:cd00501    72 GRSTITIERVAINIDDARIPDNEgNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPA--RVSNDAGTYLCNHVYYGS 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720428173  80 LYQGRGRSAFVHVPPLGKPYNADQLGRALRA--IIEEMLGVLEQA 122
Cdd:cd00501   150 LHESATRGPFIRAGFIHVPYSPEQVADKGAPsmSLETILRALEAA 194
Pcp COG2039
Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational ...
 2-119 1.26e-13

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


Pssm-ID: 441642  Cd Length: 203  Bit Score: 64.44  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428173   2 ATTVTLEKCGHN-KGYKGLDNCRFCPGSQCCVEDGPESIDSIIDMDAVCKRVTTLGLDVSVtiSQDAGRYLCDFTYYTSL 80
Cdd:COG2039    73 RAAITIERVAINvDDARIPDNDGNQPIDEPIVADGPAAYFSTLPIKAIVAALRAAGIPASV--SNTAGTYVCNHVMYRLL 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720428173  81 Y----QGRG-RSAFVHVPPL--------GKPY-NADQLGRALRAIIEEMLGVL 119
Cdd:COG2039   151 HllatKGPPiRAGFIHVPYLpeqaaakpGTPSmSLEDIVRALEAAIEAALEAL 203
PRK13196 PRK13196
pyroglutamyl-peptidase I;
30-117 1.46e-04

pyroglutamyl-peptidase I;


Pssm-ID: 171895 [Multi-domain]  Cd Length: 211  Bit Score: 39.59  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428173  30 CCVEDGPESIDSIIDMDAVCKRVTTLGLDVSvtISQDAGRYLCDFTYYTSLYQ--GRGRSA----FVHV----------- 92
Cdd:PRK13196  105 CTEPDAPAAYLSTLPLRAILAAWHDAGIPGH--ISNTAGLYVCNFVLYHALHQlhLRGRAEvpcgFLHVpanaqvalava 182

                          90       100
                  ....*....|....*....|....*....
gi 1720428173  93 ---PPLgkPY-NADQLGRALRAIIEEMLG 117
Cdd:PRK13196  183 gdrPPL--PYlPQEEITRAVRVAAETMAG 209
PRK13197 PRK13197
pyrrolidone-carboxylate peptidase; Provisional
 32-126 7.25e-04

pyrrolidone-carboxylate peptidase; Provisional


Pssm-ID: 237299  Cd Length: 215  Bit Score: 37.54  E-value: 7.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720428173  32 VEDGPESIDSIIDMDAVCKRVTTLGLDVSVtiSQDAGRYLCDFTYYTSLYQGRG-----RSAFVHVPPL-----GKPY-- 99
Cdd:PRK13197  105 VEDGPAAYFSTLPIKAMVKAIREAGIPASV--SNTAGTFVCNHVMYGLLHLLDKkypniRAGFIHIPYLpeqavNKPGtp 182

                          90       100
                  ....*....|....*....|....*....
gi 1720428173 100 --NADQLGRALRAIIEEMLgvleQAEGDI 126
Cdd:PRK13197  183 smSLEDIVRGLELAIEAIV----ENEDDI 207
PRK13194 PRK13194
pyrrolidone-carboxylate peptidase; Provisional
 32-104 8.89e-04

pyrrolidone-carboxylate peptidase; Provisional


Pssm-ID: 183887  Cd Length: 208  Bit Score: 37.56  E-value: 8.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720428173  32 VEDGPESIDSIIDMDAVCKRVTTLGldVSVTISQDAGRYLCDFTYYTSLY----QGRGRSA-FVHVpplgkPYNADQL 104
Cdd:PRK13194  104 VEGAPAAYFATLPTREIVEELKKNG--IPAVLSYSAGTYLCNYVMYLTLHhsatKGYPKMAgFIHV-----PYTPDQV 174
 
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