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Conserved domains on  [gi|568957569|ref|XP_006531431|]
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inactive serine protease 54 isoform X2 [Mus musculus]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-253 1.37e-34

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 127.39  E-value: 1.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569  42 EFPWVVSIQDKQYTHLAFGCILSEFWILSTASALQ--HRKEVIAVVGISNMDPRKTDHREYSVNTIIPHENFDNVSMGNN 119
Cdd:cd00190   11 SFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDND 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569 120 IALLKTESAMHFNDLVQAICfLGKKLHKPPALKNCWVAGWNPTSATGNHmtMSILRRISVKDI--EVCpLRRHQKTE--- 194
Cdd:cd00190   91 IALLKLKRPVTLSDNVRPIC-LPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVsnAEC-KRAYSYGGtit 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568957569 195 ----CASHTKEPNNVCLGEPGSPMMCQAKklDLWILRGLLAYgGDSC-----PGlfLYTSVADYSDWI 253
Cdd:cd00190  167 dnmlCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSW-GSGCarpnyPG--VYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-253 1.37e-34

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 127.39  E-value: 1.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569  42 EFPWVVSIQDKQYTHLAFGCILSEFWILSTASALQ--HRKEVIAVVGISNMDPRKTDHREYSVNTIIPHENFDNVSMGNN 119
Cdd:cd00190   11 SFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDND 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569 120 IALLKTESAMHFNDLVQAICfLGKKLHKPPALKNCWVAGWNPTSATGNHmtMSILRRISVKDI--EVCpLRRHQKTE--- 194
Cdd:cd00190   91 IALLKLKRPVTLSDNVRPIC-LPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVsnAEC-KRAYSYGGtit 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568957569 195 ----CASHTKEPNNVCLGEPGSPMMCQAKklDLWILRGLLAYgGDSC-----PGlfLYTSVADYSDWI 253
Cdd:cd00190  167 dnmlCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSW-GSGCarpnyPG--VYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
42-253 8.98e-33

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 122.40  E-value: 8.98e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569    42 EFPWVVSIQDKQYTHLAFGCILSEFWILSTASALQ--HRKEVIAVVGISNMDpRKTDHREYSVNTIIPHENFDNVSMGNN 119
Cdd:smart00020  12 SFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIHPNYNPSTYDND 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569   120 IALLKTESAMHFNDLVQAICfLGKKLHKPPALKNCWVAGWNPTSatGNHMTMS-ILRRISVKDI--EVCpLRRHQKTE-- 194
Cdd:smart00020  91 IALLKLKEPVTLSDNVRPIC-LPSSNYNVPAGTTCTVSGWGRTS--EGAGSLPdTLQEVNVPIVsnATC-RRAYSGGGai 166
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568957569   195 -----CASHTKEPNNVCLGEPGSPMMCQakkLDLWILRGLLAYgGDSC-----PGlfLYTSVADYSDWI 253
Cdd:smart00020 167 tdnmlCAGGLEGGKDACQGDSGGPLVCN---DGRWVLVGIVSW-GSGCarpgkPG--VYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
42-253 3.72e-22

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 93.66  E-value: 3.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569   42 EFPWVVSIQDKQYTHLAFGCILSEFWILSTASALQHRKEVIAVVGISNMDPRKTDHREYSVNTIIPHENFDNVSMGNNIA 121
Cdd:pfam00089  11 SFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569  122 LLKTESAMHFNDLVQAICfLGKKLHKPPALKNCWVAGWNPTSATGNHMTMSILrRISVKDIEVC----PLRRHQKTECAS 197
Cdd:pfam00089  91 LLKLESPVTLGDTVRPIC-LPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEV-TVPVVSRETCrsayGGTVTDTMICAG 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568957569  198 HTKEpnNVCLGEPGSPMMCQAKKLDlwilrGLLaYGGDSC-----PGlfLYTSVADYSDWI 253
Cdd:pfam00089 169 AGGK--DACQGDSGGPLVCSDGELI-----GIV-SWGYGCasgnyPG--VYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-253 1.37e-34

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 127.39  E-value: 1.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569  42 EFPWVVSIQDKQYTHLAFGCILSEFWILSTASALQ--HRKEVIAVVGISNMDPRKTDHREYSVNTIIPHENFDNVSMGNN 119
Cdd:cd00190   11 SFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDND 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569 120 IALLKTESAMHFNDLVQAICfLGKKLHKPPALKNCWVAGWNPTSATGNHmtMSILRRISVKDI--EVCpLRRHQKTE--- 194
Cdd:cd00190   91 IALLKLKRPVTLSDNVRPIC-LPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVsnAEC-KRAYSYGGtit 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568957569 195 ----CASHTKEPNNVCLGEPGSPMMCQAKklDLWILRGLLAYgGDSC-----PGlfLYTSVADYSDWI 253
Cdd:cd00190  167 dnmlCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSW-GSGCarpnyPG--VYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
42-253 8.98e-33

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 122.40  E-value: 8.98e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569    42 EFPWVVSIQDKQYTHLAFGCILSEFWILSTASALQ--HRKEVIAVVGISNMDpRKTDHREYSVNTIIPHENFDNVSMGNN 119
Cdd:smart00020  12 SFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIHPNYNPSTYDND 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569   120 IALLKTESAMHFNDLVQAICfLGKKLHKPPALKNCWVAGWNPTSatGNHMTMS-ILRRISVKDI--EVCpLRRHQKTE-- 194
Cdd:smart00020  91 IALLKLKEPVTLSDNVRPIC-LPSSNYNVPAGTTCTVSGWGRTS--EGAGSLPdTLQEVNVPIVsnATC-RRAYSGGGai 166
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568957569   195 -----CASHTKEPNNVCLGEPGSPMMCQakkLDLWILRGLLAYgGDSC-----PGlfLYTSVADYSDWI 253
Cdd:smart00020 167 tdnmlCAGGLEGGKDACQGDSGGPLVCN---DGRWVLVGIVSW-GSGCarpgkPG--VYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
42-253 3.72e-22

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 93.66  E-value: 3.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569   42 EFPWVVSIQDKQYTHLAFGCILSEFWILSTASALQHRKEVIAVVGISNMDPRKTDHREYSVNTIIPHENFDNVSMGNNIA 121
Cdd:pfam00089  11 SFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957569  122 LLKTESAMHFNDLVQAICfLGKKLHKPPALKNCWVAGWNPTSATGNHMTMSILrRISVKDIEVC----PLRRHQKTECAS 197
Cdd:pfam00089  91 LLKLESPVTLGDTVRPIC-LPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEV-TVPVVSRETCrsayGGTVTDTMICAG 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568957569  198 HTKEpnNVCLGEPGSPMMCQAKKLDlwilrGLLaYGGDSC-----PGlfLYTSVADYSDWI 253
Cdd:pfam00089 169 AGGK--DACQGDSGGPLVCSDGELI-----GIV-SWGYGCasgnyPG--VYTPVSSYLDWI 219
 
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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