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Conserved domains on  [gi|122937420|ref|NP_001073961|]
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inactive serine protease 54 isoform 1 precursor [Homo sapiens]

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 ...
52-264 1.69e-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: 1.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420  52 EFPWVVSLQDSQYTHLAFGCILSEFWVLSIASAIQNR--KDIVVIVGISNMDPSKIAHTEYPVNTIIIHEDFDNNSMSNN 129
Cdd:cd00190   11 SFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDND 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420 130 IALLKTDTAMHFGNLVQSICfLGRMLHTPPVLQNCWVSGWNPTSATGNHmtMSVLRK--IFVKDLDMC-----PLYKLQK 202
Cdd:cd00190   91 IALLKLKRPVTLSDNVRPIC-LPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEvnVPIVSNAECkraysYGGTITD 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 122937420 203 TE-CGShTKEETKTACLGDPGSPMMCQLQqfDLWVLRGVLNFgGETC-----PGlfLYTKVEDYSKWI 264
Cdd:cd00190  168 NMlCAG-GLEGGKDACQGDSGGPLVCNDN--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 ...
52-264 1.69e-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: 1.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420  52 EFPWVVSLQDSQYTHLAFGCILSEFWVLSIASAIQNR--KDIVVIVGISNMDPSKIAHTEYPVNTIIIHEDFDNNSMSNN 129
Cdd:cd00190   11 SFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDND 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420 130 IALLKTDTAMHFGNLVQSICfLGRMLHTPPVLQNCWVSGWNPTSATGNHmtMSVLRK--IFVKDLDMC-----PLYKLQK 202
Cdd:cd00190   91 IALLKLKRPVTLSDNVRPIC-LPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEvnVPIVSNAECkraysYGGTITD 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 122937420 203 TE-CGShTKEETKTACLGDPGSPMMCQLQqfDLWVLRGVLNFgGETC-----PGlfLYTKVEDYSKWI 264
Cdd:cd00190  168 NMlCAG-GLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSW-GSGCarpnyPG--VYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
52-264 1.93e-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: 124.71  E-value: 1.93e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420    52 EFPWVVSLQDSQYTHLAFGCILSEFWVLSIASAIQNR--KDIVVIVGISNMDpSKIAHTEYPVNTIIIHEDFDNNSMSNN 129
Cdd:smart00020  12 SFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLS-SGEEGQVIKVSKVIIHPNYNPSTYDND 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420   130 IALLKTDTAMHFGNLVQSICfLGRMLHTPPVLQNCWVSGWNPTSATGNHMTmSVLRKIFVK--DLDMC-PLYKLQKTECG 206
Cdd:smart00020  91 IALLKLKEPVTLSDNVRPIC-LPSSNYNVPAGTTCTVSGWGRTSEGAGSLP-DTLQEVNVPivSNATCrRAYSGGGAITD 168
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122937420   207 SH----TKEETKTACLGDPGSPMMCQLqqfDLWVLRGVLNFgGETC-----PGlfLYTKVEDYSKWI 264
Cdd:smart00020 169 NMlcagGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSW-GSGCarpgkPG--VYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
52-264 6.33e-24

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 98.67  E-value: 6.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420   52 EFPWVVSLQDSQYTHLAFGCILSEFWVLSIASAIQNRKDIVVIVGISNMDPSKIAHTEYPVNTIIIHEDFDNNSMSNNIA 131
Cdd:pfam00089  11 SFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420  132 LLKTDTAMHFGNLVQSICfLGRMLHTPPVLQNCWVSGWNPTSATGnhmTMSVLRKIFVK--DLDMCP-LYKLQKTE---C 205
Cdd:pfam00089  91 LLKLESPVTLGDTVRPIC-LPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPvvSRETCRsAYGGTVTDtmiC 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122937420  206 gshTKEETKTACLGDPGSPMMCQLQQfdlwvLRGVLNFGGETCPGLF--LYTKVEDYSKWI 264
Cdd:pfam00089 167 ---AGAGGKDACQGDSGGPLVCSDGE-----LIGIVSWGYGCASGNYpgVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
52-264 1.69e-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: 1.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420  52 EFPWVVSLQDSQYTHLAFGCILSEFWVLSIASAIQNR--KDIVVIVGISNMDPSKIAHTEYPVNTIIIHEDFDNNSMSNN 129
Cdd:cd00190   11 SFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDND 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420 130 IALLKTDTAMHFGNLVQSICfLGRMLHTPPVLQNCWVSGWNPTSATGNHmtMSVLRK--IFVKDLDMC-----PLYKLQK 202
Cdd:cd00190   91 IALLKLKRPVTLSDNVRPIC-LPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEvnVPIVSNAECkraysYGGTITD 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 122937420 203 TE-CGShTKEETKTACLGDPGSPMMCQLQqfDLWVLRGVLNFgGETC-----PGlfLYTKVEDYSKWI 264
Cdd:cd00190  168 NMlCAG-GLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSW-GSGCarpnyPG--VYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
52-264 1.93e-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: 124.71  E-value: 1.93e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420    52 EFPWVVSLQDSQYTHLAFGCILSEFWVLSIASAIQNR--KDIVVIVGISNMDpSKIAHTEYPVNTIIIHEDFDNNSMSNN 129
Cdd:smart00020  12 SFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLS-SGEEGQVIKVSKVIIHPNYNPSTYDND 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420   130 IALLKTDTAMHFGNLVQSICfLGRMLHTPPVLQNCWVSGWNPTSATGNHMTmSVLRKIFVK--DLDMC-PLYKLQKTECG 206
Cdd:smart00020  91 IALLKLKEPVTLSDNVRPIC-LPSSNYNVPAGTTCTVSGWGRTSEGAGSLP-DTLQEVNVPivSNATCrRAYSGGGAITD 168
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122937420   207 SH----TKEETKTACLGDPGSPMMCQLqqfDLWVLRGVLNFgGETC-----PGlfLYTKVEDYSKWI 264
Cdd:smart00020 169 NMlcagGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSW-GSGCarpgkPG--VYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
52-264 6.33e-24

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 98.67  E-value: 6.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420   52 EFPWVVSLQDSQYTHLAFGCILSEFWVLSIASAIQNRKDIVVIVGISNMDPSKIAHTEYPVNTIIIHEDFDNNSMSNNIA 131
Cdd:pfam00089  11 SFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937420  132 LLKTDTAMHFGNLVQSICfLGRMLHTPPVLQNCWVSGWNPTSATGnhmTMSVLRKIFVK--DLDMCP-LYKLQKTE---C 205
Cdd:pfam00089  91 LLKLESPVTLGDTVRPIC-LPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPvvSRETCRsAYGGTVTDtmiC 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122937420  206 gshTKEETKTACLGDPGSPMMCQLQQfdlwvLRGVLNFGGETCPGLF--LYTKVEDYSKWI 264
Cdd:pfam00089 167 ---AGAGGKDACQGDSGGPLVCSDGE-----LIGIVSWGYGCASGNYpgVYTPVSSYLDWI 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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