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Conserved domains on  [gi|61680579]
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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

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 ...
36-271 5.03e-97

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  Cd Length: 232  Bit Score: 284.55  E-value: 5.03e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579  36 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHSPPRdSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 113
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrhFCGGSLISPRWVLTAAHCVYSSAPS-NYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579 114 TLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSgYSSSLREALVPLVADH 193
Cdd:cd00190  80 PNYNP-STYDNDIALLKLKRP----VTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61680579 194 KCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWIND 271
Cdd:cd00190 154 ECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
36-271 5.03e-97

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  Cd Length: 232  Bit Score: 284.55  E-value: 5.03e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579  36 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHSPPRdSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 113
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrhFCGGSLISPRWVLTAAHCVYSSAPS-NYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579 114 TLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSgYSSSLREALVPLVADH 193
Cdd:cd00190  80 PNYNP-STYDNDIALLKLKRP----VTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61680579 194 KCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWIND 271
Cdd:cd00190 154 ECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
35-269 1.01e-92

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: 273.40  E-value: 1.01e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579     35 RIIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFsHSPPRDSVSVVLGQHFFNRTTDvTQTFGIEKYIP 112
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrhFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579    113 YTLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPLVAD 192
Cdd:smart00020  79 HPNYNP-STYDNDIALLKLKEP----VTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61680579    193 HKCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACeKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 269
Cdd:smart00020 154 ATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin.
36-269 8.37e-78

Trypsin.


Pssm-ID: 365866  Cd Length: 219  Bit Score: 235.41  E-value: 8.37e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579    36 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHsppRDSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 113
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkhFCGGSLISENWVLTAAHCVSG---ASDVQVVLGEHNIVLREGGEQKFDVAKVIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579   114 TLYSVFNPsDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENvsGYSSSLREALVPLVADH 193
Cdd:pfam00089  78 PNYNPDTL-DNDIALLKLESP----VTLGDTVRPICLPDAGADLPVGTTCTVSGWGNTKTL--GPPDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61680579   194 KCSSpeVYGADISPNMLCAGYfdCKSDACQGDSGGPLACEKNgvaYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 269
Cdd:pfam00089 151 TCRS--AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
34-271 5.68e-24

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 99.95  E-value: 5.68e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579  34 PRIIGGSSSLPGSHPWLAA--IYIGD----SFCAGSLVHTCWVVSAAHCFSHSPP--RDSVSVVLG---QHFFNRTtDVT 102
Cdd:COG5640  31 SRIIGGSNANAGEYPSLVAlvDRISDyvsgTFCGGSKLGGRYVLTAAHCADASSPisSDVNRVVVDlndSSQAERG-HVR 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579 103 QTFGIEKYIPYTLysvfnpsDHDLVLIRLKKKGDRCATRSQFVQPiclPEPG-STFPAGHKCQIAGWGHL----DENVSG 177
Cdd:COG5640 110 TIYVHEFYSPGNL-------GNDIAVLELARAASLPRVKITSFDA---SDTFlNSVTTVSPMTNGTFGVTtpsdVPRSSP 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579 178 YSSSLREALVPLVADHKCS--SPEVYGADISPNM--LCAGYFdcKSDACQGDSGGPLACE-KNGVAYLyGIISWGDG-CG 251
Cdd:COG5640 180 KGTILHEVAVLFVPLSTCAqyKGCANASDGATGLtgFCAGRP--PKDACQGDSGGPIFHKgEEGRVQR-GVVSWGDGgCG 256
                       250       260
                ....*....|....*....|
gi 61680579 252 RLHKPGVYTRVANYVDWIND 271
Cdd:COG5640 257 GTLIPGVYTNVSNYQDWIAA 276
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
36-271 5.03e-97

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  Cd Length: 232  Bit Score: 284.55  E-value: 5.03e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579  36 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHSPPRdSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 113
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrhFCGGSLISPRWVLTAAHCVYSSAPS-NYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579 114 TLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSgYSSSLREALVPLVADH 193
Cdd:cd00190  80 PNYNP-STYDNDIALLKLKRP----VTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61680579 194 KCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWIND 271
Cdd:cd00190 154 ECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
35-269 1.01e-92

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: 273.40  E-value: 1.01e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579     35 RIIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFsHSPPRDSVSVVLGQHFFNRTTDvTQTFGIEKYIP 112
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrhFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579    113 YTLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPLVAD 192
Cdd:smart00020  79 HPNYNP-STYDNDIALLKLKEP----VTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61680579    193 HKCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACeKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 269
Cdd:smart00020 154 ATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin.
36-269 8.37e-78

Trypsin.


Pssm-ID: 365866  Cd Length: 219  Bit Score: 235.41  E-value: 8.37e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579    36 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHsppRDSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 113
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkhFCGGSLISENWVLTAAHCVSG---ASDVQVVLGEHNIVLREGGEQKFDVAKVIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579   114 TLYSVFNPsDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENvsGYSSSLREALVPLVADH 193
Cdd:pfam00089  78 PNYNPDTL-DNDIALLKLESP----VTLGDTVRPICLPDAGADLPVGTTCTVSGWGNTKTL--GPPDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61680579   194 KCSSpeVYGADISPNMLCAGYfdCKSDACQGDSGGPLACEKNgvaYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 269
Cdd:pfam00089 151 TCRS--AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
34-271 5.68e-24

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 99.95  E-value: 5.68e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579  34 PRIIGGSSSLPGSHPWLAA--IYIGD----SFCAGSLVHTCWVVSAAHCFSHSPP--RDSVSVVLG---QHFFNRTtDVT 102
Cdd:COG5640  31 SRIIGGSNANAGEYPSLVAlvDRISDyvsgTFCGGSKLGGRYVLTAAHCADASSPisSDVNRVVVDlndSSQAERG-HVR 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579 103 QTFGIEKYIPYTLysvfnpsDHDLVLIRLKKKGDRCATRSQFVQPiclPEPG-STFPAGHKCQIAGWGHL----DENVSG 177
Cdd:COG5640 110 TIYVHEFYSPGNL-------GNDIAVLELARAASLPRVKITSFDA---SDTFlNSVTTVSPMTNGTFGVTtpsdVPRSSP 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61680579 178 YSSSLREALVPLVADHKCS--SPEVYGADISPNM--LCAGYFdcKSDACQGDSGGPLACE-KNGVAYLyGIISWGDG-CG 251
Cdd:COG5640 180 KGTILHEVAVLFVPLSTCAqyKGCANASDGATGLtgFCAGRP--PKDACQGDSGGPIFHKgEEGRVQR-GVVSWGDGgCG 256
                       250       260
                ....*....|....*....|
gi 61680579 252 RLHKPGVYTRVANYVDWIND 271
Cdd:COG5640 257 GTLIPGVYTNVSNYQDWIAA 276
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
48-93 7.56e-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: 35.60  E-value: 7.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 61680579    48 PWLAAIYI-GDSFCAGSLVHTCWVVSAAHCFSHSPPRDS-VSVVLGQH 93
Cdd:pfam09342   2 PWIAKVYLdGNMICSGVLIDASWVIVSGSCLRDTNLRHQyISVVLGGA 49
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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