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Conserved domains on  [gi|494948602|ref|WP_007674630|]
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C13 family peptidase [Caulobacter sp. AP07]

Protein Classification

caspase family protein( domain architecture ID 1724)

caspase family protein similar to caspases which are cysteine class enzymes that drive the terminal stages of apoptosis as well as other cellular remodeling and inflammatory events

CATH:  3.40.50.1460
EC:  3.4.22.-
Gene Ontology:  GO:0008234
MEROPS:  C14
PubMed:  9357314
SCOP:  4003593

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CASc super family cl00042
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 112-237 4.62e-11

Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent aspartate-directed proteases that mediate programmed cell death (apoptosis). Caspases are synthesized as inactive zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologs.


The actual alignment was detected with superfamily member pfam01650:

Pssm-ID: 444667  Cd Length: 257  Bit Score: 61.15  E-value: 4.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494948602  112 YVSSHGAPEGVQVDDG-LLPPHLLAAMIDDACPAR---PSIVVVSACFSGVFVRPLQKDDRM-ILTAARSDRTSFG--CS 184
Cdd:pfam01650 113 YFTDHGAPGVLGFPELdYLYAKDLAEALKKMHARGkykKLVFYVEACESGSMFEGLPKDINVyATTAANADESSYGcyCP 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494948602  185 EDDKYPYFDDCFLSSAPTAHDFAALGRA--VQACVARRERDTGAEP-----ASEPQLWIG 237
Cdd:pfam01650 193 DPEDGTYLGDLFSVNWMEDSDDHDLSKEtlEQQFELVKNRTTGSHVmqygdKSLPQLPLS 252
 
Name Accession Description Interval E-value
Peptidase_C13 pfam01650
Peptidase C13 family; Members of this family are asparaginyl peptidases. The blood fluke ...
 112-237 4.62e-11

Peptidase C13 family; Members of this family are asparaginyl peptidases. The blood fluke parasite Schistosoma mansoni has at least five Clan CA cysteine peptidases in its digestive tract including cathepsins B (2 isoforms), C, F and L. All have been recombinantly expressed as active enzymes, albeit in various stages of activation. In addition, a Clan CD peptidase, termed asparaginyl endopeptidase or 'legumain' has been identified. This has formerly been characterized as a 'haemoglobinase', but this term is probably incorrect. Two cDNAs have been described for Schistosoma mansoni legumain; one encodes an active enzyme whereas the active site cysteine residue encoded by the second cDNA is substituted by an asparagine residue. Both forms have been recombinantly expressed.


Pssm-ID: 396290  Cd Length: 257  Bit Score: 61.15  E-value: 4.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494948602  112 YVSSHGAPEGVQVDDG-LLPPHLLAAMIDDACPAR---PSIVVVSACFSGVFVRPLQKDDRM-ILTAARSDRTSFG--CS 184
Cdd:pfam01650 113 YFTDHGAPGVLGFPELdYLYAKDLAEALKKMHARGkykKLVFYVEACESGSMFEGLPKDINVyATTAANADESSYGcyCP 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494948602  185 EDDKYPYFDDCFLSSAPTAHDFAALGRA--VQACVARRERDTGAEP-----ASEPQLWIG 237
Cdd:pfam01650 193 DPEDGTYLGDLFSVNWMEDSDDHDLSKEtlEQQFELVKNRTTGSHVmqygdKSLPQLPLS 252
COG4249 COG4249
Uncharacterized conserved protein, contains caspase domain [General function prediction only];
51-181 1.55e-04

Uncharacterized conserved protein, contains caspase domain [General function prediction only];


Pssm-ID: 443391  Cd Length: 238  Bit Score: 41.85  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494948602  51 DNARRDVSL---ALADLGFspgavrqysvrprryPAVKPGkTDLRR--IHAGLRELAVKNPAG--CLFYVSSHgapeGVQ 123
Cdd:COG4249   27 PNAVNDAEAlaeALREAGF---------------DEVILL-TDATRaeIRRALRDFFAKAQPGdvALFYFAGH----GIQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494948602 124 VDDGL-LPPH----------------LLAAMidDACPARPSIVVVSACFSGVFVRPLQKDD----------------RMI 170
Cdd:COG4249   87 DDGENyLLPVdaspddlestaislseLLDAL--AESPAKKVLVILDACRSGPFARGGRRSAgpsssrglaelaagrgTLV 164

                        170
                 ....*....|.
gi 494948602 171 LTAARSDRTSF 181
Cdd:COG4249  165 LTASAPGQVAL 175
 
Name Accession Description Interval E-value
Peptidase_C13 pfam01650
Peptidase C13 family; Members of this family are asparaginyl peptidases. The blood fluke ...
 112-237 4.62e-11

Peptidase C13 family; Members of this family are asparaginyl peptidases. The blood fluke parasite Schistosoma mansoni has at least five Clan CA cysteine peptidases in its digestive tract including cathepsins B (2 isoforms), C, F and L. All have been recombinantly expressed as active enzymes, albeit in various stages of activation. In addition, a Clan CD peptidase, termed asparaginyl endopeptidase or 'legumain' has been identified. This has formerly been characterized as a 'haemoglobinase', but this term is probably incorrect. Two cDNAs have been described for Schistosoma mansoni legumain; one encodes an active enzyme whereas the active site cysteine residue encoded by the second cDNA is substituted by an asparagine residue. Both forms have been recombinantly expressed.


Pssm-ID: 396290  Cd Length: 257  Bit Score: 61.15  E-value: 4.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494948602  112 YVSSHGAPEGVQVDDG-LLPPHLLAAMIDDACPAR---PSIVVVSACFSGVFVRPLQKDDRM-ILTAARSDRTSFG--CS 184
Cdd:pfam01650 113 YFTDHGAPGVLGFPELdYLYAKDLAEALKKMHARGkykKLVFYVEACESGSMFEGLPKDINVyATTAANADESSYGcyCP 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494948602  185 EDDKYPYFDDCFLSSAPTAHDFAALGRA--VQACVARRERDTGAEP-----ASEPQLWIG 237
Cdd:pfam01650 193 DPEDGTYLGDLFSVNWMEDSDDHDLSKEtlEQQFELVKNRTTGSHVmqygdKSLPQLPLS 252
COG4249 COG4249
Uncharacterized conserved protein, contains caspase domain [General function prediction only];
51-181 1.55e-04

Uncharacterized conserved protein, contains caspase domain [General function prediction only];


Pssm-ID: 443391  Cd Length: 238  Bit Score: 41.85  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494948602  51 DNARRDVSL---ALADLGFspgavrqysvrprryPAVKPGkTDLRR--IHAGLRELAVKNPAG--CLFYVSSHgapeGVQ 123
Cdd:COG4249   27 PNAVNDAEAlaeALREAGF---------------DEVILL-TDATRaeIRRALRDFFAKAQPGdvALFYFAGH----GIQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494948602 124 VDDGL-LPPH----------------LLAAMidDACPARPSIVVVSACFSGVFVRPLQKDD----------------RMI 170
Cdd:COG4249   87 DDGENyLLPVdaspddlestaislseLLDAL--AESPAKKVLVILDACRSGPFARGGRRSAgpsssrglaelaagrgTLV 164

                        170
                 ....*....|.
gi 494948602 171 LTAARSDRTSF 181
Cdd:COG4249  165 LTASAPGQVAL 175
 
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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