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Conserved domains on  [gi|110578663|ref|NP_940866|]
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serine protease 55 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 ...
68-298 1.07e-85

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: 258.36  E-value: 1.07e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663  68 ITGGMEAEVGEFPWQVSIQ-ARSEPFCGGSILNKWWILTAAHCLYSEElfPEELSVVLGTNDLTS--PSMEIKEVASIIL 144
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSneGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663 145 HKDFKRANMDNDIALLLLASPIKLDDLKVPICLPTQPG-PATWRECWVAGWGQTNAADKNSVKtdLMKAPMVIMDWEECS 223
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSEGGPLPDV--LQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110578663 224 KMFPK---LTKNMLCAGYKNESYDACKGDSGGPLVCtpEPGEKWYQVGIISWGKSCGEKNTPGIYTSLVNYNLWIEKV 298
Cdd:cd00190  157 RAYSYggtITDNMLCAGGLEGGKDACQGDSGGPLVC--NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
68-298 1.07e-85

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: 258.36  E-value: 1.07e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663  68 ITGGMEAEVGEFPWQVSIQ-ARSEPFCGGSILNKWWILTAAHCLYSEElfPEELSVVLGTNDLTS--PSMEIKEVASIIL 144
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSneGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663 145 HKDFKRANMDNDIALLLLASPIKLDDLKVPICLPTQPG-PATWRECWVAGWGQTNAADKNSVKtdLMKAPMVIMDWEECS 223
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSEGGPLPDV--LQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110578663 224 KMFPK---LTKNMLCAGYKNESYDACKGDSGGPLVCtpEPGEKWYQVGIISWGKSCGEKNTPGIYTSLVNYNLWIEKV 298
Cdd:cd00190  157 RAYSYggtITDNMLCAGGLEGGKDACQGDSGGPLVC--NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
67-295 5.76e-85

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: 256.45  E-value: 5.76e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663    67 RITGGMEAEVGEFPWQVSIQARS-EPFCGGSILNKWWILTAAHCLYSEElfPEELSVVLGTNDLTSP-SMEIKEVASIIL 144
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD--PSNIRVRLGSHDLSSGeEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663   145 HKDFKRANMDNDIALLLLASPIKLDDLKVPICLPTQPG-PATWRECWVAGWGQTNAADKNSVKTdLMKAPMVIMDWEECS 223
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGAGSLPDT-LQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110578663   224 KMFP---KLTKNMLCAGYKNESYDACKGDSGGPLVCTpepGEKWYQVGIISWGKSCGEKNTPGIYTSLVNYNLWI 295
Cdd:smart00020 158 RAYSgggAITDNMLCAGGLEGGKDACQGDSGGPLVCN---DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
66-299 2.03e-68

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 215.28  E-value: 2.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663  66 SRITGGMEAEVGEFPWQVSIQARSEP---FCGGSILNKWWILTAAHCLYSEElfPEELSVVLGTNDLTSPSMEIKEVASI 142
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDG--PSDLRVVIGSTDLSTSGGTVVKVARI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663 143 ILHKDFKRANMDNDIALLLLASPIkldDLKVPICLPTQP-GPATWRECWVAGWGQTNAaDKNSVKTDLMKAPMVIMDWEE 221
Cdd:COG5640  107 VVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSAdAAAPGTPATVAGWGRTSE-GPGSQSGTLRKADVPVVSDAT 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110578663 222 CSKMFPKLTKNMLCAGYKNESYDACKGDSGGPLVcTPEPGEkWYQVGIISWGKSCGEKNTPGIYTSLVNYNLWIEKVT 299
Cdd:COG5640  183 CAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGG-WVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
68-295 4.03e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 203.06  E-value: 4.03e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663   68 ITGGMEAEVGEFPWQVSIQARS-EPFCGGSILNKWWILTAAHCLYSeelfPEELSVVLGTNDLTS--PSMEIKEVASIIL 144
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVSG----ASDVKVVLGAHNIVLreGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663  145 HKDFKRANMDNDIALLLLASPIKLDDLKVPICLPTQ-PGPATWRECWVAGWGQTNAADKNSVktdLMKAPMVIMDWEECS 223
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGPSDT---LQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110578663  224 KMFP-KLTKNMLCAGYKNEsyDACKGDSGGPLVCtpepgEKWYQVGIISWGKSCGEKNTPGIYTSLVNYNLWI 295
Cdd:pfam00089 154 SAYGgTVTDTMICAGAGGK--DACQGDSGGPLVC-----SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
68-298 1.07e-85

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: 258.36  E-value: 1.07e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663  68 ITGGMEAEVGEFPWQVSIQ-ARSEPFCGGSILNKWWILTAAHCLYSEElfPEELSVVLGTNDLTS--PSMEIKEVASIIL 144
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSneGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663 145 HKDFKRANMDNDIALLLLASPIKLDDLKVPICLPTQPG-PATWRECWVAGWGQTNAADKNSVKtdLMKAPMVIMDWEECS 223
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSEGGPLPDV--LQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110578663 224 KMFPK---LTKNMLCAGYKNESYDACKGDSGGPLVCtpEPGEKWYQVGIISWGKSCGEKNTPGIYTSLVNYNLWIEKV 298
Cdd:cd00190  157 RAYSYggtITDNMLCAGGLEGGKDACQGDSGGPLVC--NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
67-295 5.76e-85

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: 256.45  E-value: 5.76e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663    67 RITGGMEAEVGEFPWQVSIQARS-EPFCGGSILNKWWILTAAHCLYSEElfPEELSVVLGTNDLTSP-SMEIKEVASIIL 144
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD--PSNIRVRLGSHDLSSGeEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663   145 HKDFKRANMDNDIALLLLASPIKLDDLKVPICLPTQPG-PATWRECWVAGWGQTNAADKNSVKTdLMKAPMVIMDWEECS 223
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGAGSLPDT-LQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110578663   224 KMFP---KLTKNMLCAGYKNESYDACKGDSGGPLVCTpepGEKWYQVGIISWGKSCGEKNTPGIYTSLVNYNLWI 295
Cdd:smart00020 158 RAYSgggAITDNMLCAGGLEGGKDACQGDSGGPLVCN---DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
66-299 2.03e-68

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 215.28  E-value: 2.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663  66 SRITGGMEAEVGEFPWQVSIQARSEP---FCGGSILNKWWILTAAHCLYSEElfPEELSVVLGTNDLTSPSMEIKEVASI 142
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDG--PSDLRVVIGSTDLSTSGGTVVKVARI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663 143 ILHKDFKRANMDNDIALLLLASPIkldDLKVPICLPTQP-GPATWRECWVAGWGQTNAaDKNSVKTDLMKAPMVIMDWEE 221
Cdd:COG5640  107 VVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSAdAAAPGTPATVAGWGRTSE-GPGSQSGTLRKADVPVVSDAT 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110578663 222 CSKMFPKLTKNMLCAGYKNESYDACKGDSGGPLVcTPEPGEkWYQVGIISWGKSCGEKNTPGIYTSLVNYNLWIEKVT 299
Cdd:COG5640  183 CAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGG-WVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
68-295 4.03e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 203.06  E-value: 4.03e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663   68 ITGGMEAEVGEFPWQVSIQARS-EPFCGGSILNKWWILTAAHCLYSeelfPEELSVVLGTNDLTS--PSMEIKEVASIIL 144
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVSG----ASDVKVVLGAHNIVLreGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663  145 HKDFKRANMDNDIALLLLASPIKLDDLKVPICLPTQ-PGPATWRECWVAGWGQTNAADKNSVktdLMKAPMVIMDWEECS 223
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGPSDT---LQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110578663  224 KMFP-KLTKNMLCAGYKNEsyDACKGDSGGPLVCtpepgEKWYQVGIISWGKSCGEKNTPGIYTSLVNYNLWI 295
Cdd:pfam00089 154 SAYGgTVTDTMICAGAGGK--DACQGDSGGPLVC-----SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
88-273 1.33e-07

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 51.22  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663  88 RSEPFCGGSILNKWWILTAAHCLYSEEL--FPEELSVVLGTNDLTSPSMeikEVASIILHKDFKR-ANMDNDIALLLLAS 164
Cdd:COG3591    9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGggWATNIVFVPGYNGGPYGTA---TATRFRVPPGWVAsGDAGYDYALLRLDE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663 165 PIklDDLKVPICLPTQPGPATWRECWVAGWGQTnaadknsvktdlmkAPMVIMDWEECSKMfpKLTKNMLcaGYKNesyD 244
Cdd:COG3591   86 PL--GDTTGWLGLAFNDAPLAGEPVTIIGYPGD--------------RPKDLSLDCSGRVT--GVQGNRL--SYDC---D 142
                        170       180
                 ....*....|....*....|....*....
gi 110578663 245 ACKGDSGGPlVCTPEPGEkWYQVGIISWG 273
Cdd:COG3591  143 TTGGSSGSP-VLDDSDGG-GRVVGVHSAG 169
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
80-178 2.31e-03

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 37.53  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110578663   80 PWQVSIQARSEPFCGGSILNKWWILTAAHCLYSEELFPEELSVVLGTN----DLTSPSMEIKEVASiilHKDFKRANmdn 155
Cdd:pfam09342   2 PWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGAktlkSIEGPYEQIVRVDC---RHDIPESE--- 75
                          90       100
                  ....*....|....*....|...
gi 110578663  156 dIALLLLASPIKLDDLKVPICLP 178
Cdd:pfam09342  76 -ISLLHLASPASFSNHVLPTFVP 97
 
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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