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Conserved domains on  [gi|15718702|ref|NP_203126|]
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caspase-7 isoform beta [Homo sapiens]

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 ...
 60-148 3.01e-35

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 cd00032:

Pssm-ID: 444667  Cd Length: 243  Bit Score: 125.79  E-value: 3.01e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718702  60 YNMNFEKLGKCIIINNKNFDKvtGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFAC 139
Cdd:cd00032   2 YKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFVC 79


                ....*....
gi 15718702 140 ILLSHGEEN 148
Cdd:cd00032  80 VILSHGEEG 88
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 60-148 3.01e-35

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.


Pssm-ID: 237997  Cd Length: 243  Bit Score: 125.79  E-value: 3.01e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718702  60 YNMNFEKLGKCIIINNKNFDKvtGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFAC 139
Cdd:cd00032   2 YKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFVC 79


                ....*....
gi 15718702 140 ILLSHGEEN 148
Cdd:cd00032  80 VILSHGEEG 88
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 60-164 1.50e-34

Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as 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 homologues.


Pssm-ID: 214521  Cd Length: 241  Bit Score: 123.89  E-value: 1.50e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718702     60 YNMNFEKLGKCIIINNKNFDKvtgMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKK-ASEEDHTNAACFA 138
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEfAAMPEHSDSDSFV 77

                           90       100
                   ....*....|....*....|....*.
gi 15718702    139 CILLSHGEENMeSCSVTQAGVQRRDL 164
Cdd:smart00115  78 CVLLSHGEEGG-IYGTDGDPLPLDEI 102
Peptidase_C14 pfam00656
Caspase domain;
68-148 5.10e-23

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 93.16  E-value: 5.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718702    68 GKCIIINNKNFDKVTGmgVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKK-ASEEDHTNAACFACILL---S 143
Cdd:pfam00656   2 GLALIIGNNNYPGTKA--PLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDfAARADHSDGDSFVVVLLyysG 79


                  ....*
gi 15718702   144 HGEEN 148
Cdd:pfam00656  80 HGEQV 84
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 60-148 3.01e-35

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.


Pssm-ID: 237997  Cd Length: 243  Bit Score: 125.79  E-value: 3.01e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718702  60 YNMNFEKLGKCIIINNKNFDKvtGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFAC 139
Cdd:cd00032   2 YKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFVC 79


                ....*....
gi 15718702 140 ILLSHGEEN 148
Cdd:cd00032  80 VILSHGEEG 88
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 60-164 1.50e-34

Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as 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 homologues.


Pssm-ID: 214521  Cd Length: 241  Bit Score: 123.89  E-value: 1.50e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718702     60 YNMNFEKLGKCIIINNKNFDKvtgMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKK-ASEEDHTNAACFA 138
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEfAAMPEHSDSDSFV 77

                           90       100
                   ....*....|....*....|....*.
gi 15718702    139 CILLSHGEENMeSCSVTQAGVQRRDL 164
Cdd:smart00115  78 CVLLSHGEEGG-IYGTDGDPLPLDEI 102
Peptidase_C14 pfam00656
Caspase domain;
68-148 5.10e-23

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 93.16  E-value: 5.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718702    68 GKCIIINNKNFDKVTGmgVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKK-ASEEDHTNAACFACILL---S 143
Cdd:pfam00656   2 GLALIIGNNNYPGTKA--PLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDfAARADHSDGDSFVVVLLyysG 79


                  ....*
gi 15718702   144 HGEEN 148
Cdd:pfam00656  80 HGEQV 84
 
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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