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Conserved domains on  [gi|922581024|ref|NP_001300082|]
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DRBM domain-containing protein [Caenorhabditis elegans]

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: ...
 258-410 1.55e-62

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 pfam06162:

Pssm-ID: 444776  Cd Length: 166  Bit Score: 199.38  E-value: 1.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581024  258 MLTMCNNFPGFEAP--MRYMIENSHDVVTVFDG-------SPAVIVLDELVKADESSYLPFKMKKSYKKVDEIAAKMASE 328
Cdd:pfam06162   1 MLSMCNKYPFFPDDdsERVVIIKLYAIVTVFDEpvegkqpSSAVIVYEELAKSGSDKMLFLKMEESYDKVDQVVQEMAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581024  329 EIHFTIHLSSHSQKNVIQIFQSAYSDGYTEEDKKGKIPEGGRVKCAGTETGARSNVKCEEVAKEVNEYIDSNKDKFGDLK 408
Cdd:pfam06162  81 PSVVAIHLSSHSLKNTIQIVRTAFSNGYTQKDKKGNVPEGNKVKCDGDETVMKTTVDCEDVVKDVNEFMEEDRQKFGELE 160


                  ..
gi 922581024  409 VE 410
Cdd:pfam06162 161 IQ 162
Peptidase_C15 super family cl00237
Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: ...
 13-175 3.22e-62

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 pfam06162:

Pssm-ID: 444776  Cd Length: 166  Bit Score: 198.61  E-value: 3.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581024   13 MLSMCNKYPDFDDEERVRRVDDDFRDVITVFDAPFEGKSPSPAVIVFDELVDSdGSSKYLNFKMEQSYEKVDEIPEKIDA 92
Cdd:pfam06162   1 MLSMCNKYPFFPDDDSERVVIIKLYAIVTVFDEPVEGKQPSSAVIVYEELAKS-GSDKMLFLKMEESYDKVDQVVQEMAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581024   93 ERIRYAIHLGSHSQKNVLQIFQSAYSDGYTEEDKNGKVPVGGKVKCAETETGFRTKINCENVVTAVNEYMDSNREKFGEL 172
Cdd:pfam06162  80 IPSVVAIHLSSHSLKNTIQIVRTAFSNGYTQKDKKGNVPEGNKVKCDGDETVMKTTVDCEDVVKDVNEFMEEDRQKFGEL 159


                  ...
gi 922581024  173 RIE 175
Cdd:pfam06162 160 EIQ 162
 
Name Accession Description Interval E-value
PgaPase_1 pfam06162
Putative pyroglutamyl peptidase PgaPase_1; PgaPase_1 is a family of functionally diverse ...
 258-410 1.55e-62

Putative pyroglutamyl peptidase PgaPase_1; PgaPase_1 is a family of functionally diverse Caenorhabditis proteins. The family is homologous to the cysteine-peptidases, but lack of a strictly conserved Glu-Cys-His catalytic triad or pGlu binding site implies that it has other functions that could have resulted in a change in reaction-specificity or even of catalytic activity.


Pssm-ID: 310625  Cd Length: 166  Bit Score: 199.38  E-value: 1.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581024  258 MLTMCNNFPGFEAP--MRYMIENSHDVVTVFDG-------SPAVIVLDELVKADESSYLPFKMKKSYKKVDEIAAKMASE 328
Cdd:pfam06162   1 MLSMCNKYPFFPDDdsERVVIIKLYAIVTVFDEpvegkqpSSAVIVYEELAKSGSDKMLFLKMEESYDKVDQVVQEMAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581024  329 EIHFTIHLSSHSQKNVIQIFQSAYSDGYTEEDKKGKIPEGGRVKCAGTETGARSNVKCEEVAKEVNEYIDSNKDKFGDLK 408
Cdd:pfam06162  81 PSVVAIHLSSHSLKNTIQIVRTAFSNGYTQKDKKGNVPEGNKVKCDGDETVMKTTVDCEDVVKDVNEFMEEDRQKFGELE 160


                  ..
gi 922581024  409 VE 410
Cdd:pfam06162 161 IQ 162
PgaPase_1 pfam06162
Putative pyroglutamyl peptidase PgaPase_1; PgaPase_1 is a family of functionally diverse ...
 13-175 3.22e-62

Putative pyroglutamyl peptidase PgaPase_1; PgaPase_1 is a family of functionally diverse Caenorhabditis proteins. The family is homologous to the cysteine-peptidases, but lack of a strictly conserved Glu-Cys-His catalytic triad or pGlu binding site implies that it has other functions that could have resulted in a change in reaction-specificity or even of catalytic activity.


Pssm-ID: 310625  Cd Length: 166  Bit Score: 198.61  E-value: 3.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581024   13 MLSMCNKYPDFDDEERVRRVDDDFRDVITVFDAPFEGKSPSPAVIVFDELVDSdGSSKYLNFKMEQSYEKVDEIPEKIDA 92
Cdd:pfam06162   1 MLSMCNKYPFFPDDDSERVVIIKLYAIVTVFDEPVEGKQPSSAVIVYEELAKS-GSDKMLFLKMEESYDKVDQVVQEMAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581024   93 ERIRYAIHLGSHSQKNVLQIFQSAYSDGYTEEDKNGKVPVGGKVKCAETETGFRTKINCENVVTAVNEYMDSNREKFGEL 172
Cdd:pfam06162  80 IPSVVAIHLSSHSLKNTIQIVRTAFSNGYTQKDKKGNVPEGNKVKCDGDETVMKTTVDCEDVVKDVNEFMEEDRQKFGEL 159


                  ...
gi 922581024  173 RIE 175
Cdd:pfam06162 160 EIQ 162
 
Name Accession Description Interval E-value
PgaPase_1 pfam06162
Putative pyroglutamyl peptidase PgaPase_1; PgaPase_1 is a family of functionally diverse ...
 258-410 1.55e-62

Putative pyroglutamyl peptidase PgaPase_1; PgaPase_1 is a family of functionally diverse Caenorhabditis proteins. The family is homologous to the cysteine-peptidases, but lack of a strictly conserved Glu-Cys-His catalytic triad or pGlu binding site implies that it has other functions that could have resulted in a change in reaction-specificity or even of catalytic activity.


Pssm-ID: 310625  Cd Length: 166  Bit Score: 199.38  E-value: 1.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581024  258 MLTMCNNFPGFEAP--MRYMIENSHDVVTVFDG-------SPAVIVLDELVKADESSYLPFKMKKSYKKVDEIAAKMASE 328
Cdd:pfam06162   1 MLSMCNKYPFFPDDdsERVVIIKLYAIVTVFDEpvegkqpSSAVIVYEELAKSGSDKMLFLKMEESYDKVDQVVQEMAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581024  329 EIHFTIHLSSHSQKNVIQIFQSAYSDGYTEEDKKGKIPEGGRVKCAGTETGARSNVKCEEVAKEVNEYIDSNKDKFGDLK 408
Cdd:pfam06162  81 PSVVAIHLSSHSLKNTIQIVRTAFSNGYTQKDKKGNVPEGNKVKCDGDETVMKTTVDCEDVVKDVNEFMEEDRQKFGELE 160


                  ..
gi 922581024  409 VE 410
Cdd:pfam06162 161 IQ 162
PgaPase_1 pfam06162
Putative pyroglutamyl peptidase PgaPase_1; PgaPase_1 is a family of functionally diverse ...
 13-175 3.22e-62

Putative pyroglutamyl peptidase PgaPase_1; PgaPase_1 is a family of functionally diverse Caenorhabditis proteins. The family is homologous to the cysteine-peptidases, but lack of a strictly conserved Glu-Cys-His catalytic triad or pGlu binding site implies that it has other functions that could have resulted in a change in reaction-specificity or even of catalytic activity.


Pssm-ID: 310625  Cd Length: 166  Bit Score: 198.61  E-value: 3.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581024   13 MLSMCNKYPDFDDEERVRRVDDDFRDVITVFDAPFEGKSPSPAVIVFDELVDSdGSSKYLNFKMEQSYEKVDEIPEKIDA 92
Cdd:pfam06162   1 MLSMCNKYPFFPDDDSERVVIIKLYAIVTVFDEPVEGKQPSSAVIVYEELAKS-GSDKMLFLKMEESYDKVDQVVQEMAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581024   93 ERIRYAIHLGSHSQKNVLQIFQSAYSDGYTEEDKNGKVPVGGKVKCAETETGFRTKINCENVVTAVNEYMDSNREKFGEL 172
Cdd:pfam06162  80 IPSVVAIHLSSHSLKNTIQIVRTAFSNGYTQKDKKGNVPEGNKVKCDGDETVMKTTVDCEDVVKDVNEFMEEDRQKFGEL 159


                  ...
gi 922581024  173 RIE 175
Cdd:pfam06162 160 EIQ 162
 
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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