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Conserved domains on  [gi|6678293|ref|NP_033381|]
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inactive serine protease 39 isoform 1 precursor [Mus musculus]

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

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 ...
68-310 7.47e-74

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: 228.70  E-value: 7.47e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293   68 IYGGQIAKAERWPWQASLIFR-GRHICGAVLIDKTWLLSAAHCFQRSlTPSDYRILLGYNQLSNPSNYSRQMTVNKVILH 146
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293  147 EDYSKlSRLEKNIVLIQLHHPVIYSTHIFPACVPDGTTKVSPNNLCWISGWGMLSADKFLqaPFPLLDAEVSLIDEEECT 226
Cdd:cd00190  80 PNYNP-STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293  227 TFFQTPEVsiteydvIKDDVLCAGDLTNQKSSCRGDSGGPLVCFLNSFWYVVGLANWNGACLEPiHSPNIFTKVSYFSDW 306
Cdd:cd00190 157 RAYSYGGT-------ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARP-NYPGVYTRVSSYLDW 228

                ....
gi 6678293  307 IKQK 310
Cdd:cd00190 229 IQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
68-310 7.47e-74

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: 228.70  E-value: 7.47e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293   68 IYGGQIAKAERWPWQASLIFR-GRHICGAVLIDKTWLLSAAHCFQRSlTPSDYRILLGYNQLSNPSNYSRQMTVNKVILH 146
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293  147 EDYSKlSRLEKNIVLIQLHHPVIYSTHIFPACVPDGTTKVSPNNLCWISGWGMLSADKFLqaPFPLLDAEVSLIDEEECT 226
Cdd:cd00190  80 PNYNP-STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293  227 TFFQTPEVsiteydvIKDDVLCAGDLTNQKSSCRGDSGGPLVCFLNSFWYVVGLANWNGACLEPiHSPNIFTKVSYFSDW 306
Cdd:cd00190 157 RAYSYGGT-------ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARP-NYPGVYTRVSSYLDW 228

                ....
gi 6678293  307 IKQK 310
Cdd:cd00190 229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
67-307 8.78e-70

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: 218.32  E-value: 8.78e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293      67 KIYGGQIAKAERWPWQASLIFRG-RHICGAVLIDKTWLLSAAHCFQRSlTPSDYRILLGYNQLSNPsNYSRQMTVNKVIL 145
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSG-EEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293     146 HEDYSKlSRLEKNIVLIQLHHPVIYSTHIFPACVPDGTTKVSPNNLCWISGWGmLSADKFLQAPFPLLDAEVSLIDEEEC 225
Cdd:smart00020  79 HPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWG-RTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293     226 TTFFQTPEVsiteydvIKDDVLCAGDLTNQKSSCRGDSGGPLVCfLNSFWYVVGLANWNGACLEPiHSPNIFTKVSYFSD 305
Cdd:smart00020 157 RRAYSGGGA-------ITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARP-GKPGVYTRVSSYLD 227

                   ..
gi 6678293     306 WI 307
Cdd:smart00020 228 WI 229
Trypsin pfam00089
Trypsin;
68-307 2.34e-49

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 165.31  E-value: 2.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293     68 IYGGQIAKAERWPWQASLIFR-GRHICGAVLIDKTWLLSAAHCFQRSltpSDYRILLGYNQLSNPSNYSRQMTVNKVILH 146
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA---SDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293    147 EDYSKlSRLEKNIVLIQLHHPVIYSTHIFPACVPDGTTKVSPNNLCWISGWGmlsADKFLQAPFPLLDAEVSLIDEEECT 226
Cdd:pfam00089  78 PNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG---NTKTLGPSDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293    227 TFFQTPevsiteydvIKDDVLCAGdlTNQKSSCRGDSGGPLVCFLNsfwYVVGLANWNGAClEPIHSPNIFTKVSYFSDW 306
Cdd:pfam00089 154 SAYGGT---------VTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGC-ASGNYPGVYTPVSSYLDW 218

                  .
gi 6678293    307 I 307
Cdd:pfam00089 219 I 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
65-309 1.62e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 164.44  E-value: 1.62e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293   65 QGKIYGGQIAKAERWPWQASLIFRG---RHICGAVLIDKTWLLSAAHCFQRSlTPSDYRILLGYNQLSNPSNYSRqmTVN 141
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGGTVV--KVA 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293  142 KVILHEDYSKlSRLEKNIVLIQLHHPViysTHIFPACVPDGTTKVSPNNLCWISGWGMLSADkflQAPFP--LLDAEVSL 219
Cdd:COG5640 105 RIVVHPDYDP-ATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEG---PGSQSgtLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293  220 IDEEECTTFFqtpevsiteyDVIKDDVLCAGDLTNQKSSCRGDSGGPLVCFLNSFWYVVGLANW-NGAClePIHSPNIFT 298
Cdd:COG5640 178 VSDATCAAYG----------GFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWgGGPC--AAGYPGVYT 245
                       250
                ....*....|.
gi 6678293  299 KVSYFSDWIKQ 309
Cdd:COG5640 246 RVSAYRDWIKS 256
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
68-310 7.47e-74

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: 228.70  E-value: 7.47e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293   68 IYGGQIAKAERWPWQASLIFR-GRHICGAVLIDKTWLLSAAHCFQRSlTPSDYRILLGYNQLSNPSNYSRQMTVNKVILH 146
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293  147 EDYSKlSRLEKNIVLIQLHHPVIYSTHIFPACVPDGTTKVSPNNLCWISGWGMLSADKFLqaPFPLLDAEVSLIDEEECT 226
Cdd:cd00190  80 PNYNP-STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293  227 TFFQTPEVsiteydvIKDDVLCAGDLTNQKSSCRGDSGGPLVCFLNSFWYVVGLANWNGACLEPiHSPNIFTKVSYFSDW 306
Cdd:cd00190 157 RAYSYGGT-------ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARP-NYPGVYTRVSSYLDW 228

                ....
gi 6678293  307 IKQK 310
Cdd:cd00190 229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
67-307 8.78e-70

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: 218.32  E-value: 8.78e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293      67 KIYGGQIAKAERWPWQASLIFRG-RHICGAVLIDKTWLLSAAHCFQRSlTPSDYRILLGYNQLSNPsNYSRQMTVNKVIL 145
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSG-EEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293     146 HEDYSKlSRLEKNIVLIQLHHPVIYSTHIFPACVPDGTTKVSPNNLCWISGWGmLSADKFLQAPFPLLDAEVSLIDEEEC 225
Cdd:smart00020  79 HPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWG-RTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293     226 TTFFQTPEVsiteydvIKDDVLCAGDLTNQKSSCRGDSGGPLVCfLNSFWYVVGLANWNGACLEPiHSPNIFTKVSYFSD 305
Cdd:smart00020 157 RRAYSGGGA-------ITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARP-GKPGVYTRVSSYLD 227

                   ..
gi 6678293     306 WI 307
Cdd:smart00020 228 WI 229
Trypsin pfam00089
Trypsin;
68-307 2.34e-49

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 165.31  E-value: 2.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293     68 IYGGQIAKAERWPWQASLIFR-GRHICGAVLIDKTWLLSAAHCFQRSltpSDYRILLGYNQLSNPSNYSRQMTVNKVILH 146
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA---SDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293    147 EDYSKlSRLEKNIVLIQLHHPVIYSTHIFPACVPDGTTKVSPNNLCWISGWGmlsADKFLQAPFPLLDAEVSLIDEEECT 226
Cdd:pfam00089  78 PNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG---NTKTLGPSDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293    227 TFFQTPevsiteydvIKDDVLCAGdlTNQKSSCRGDSGGPLVCFLNsfwYVVGLANWNGAClEPIHSPNIFTKVSYFSDW 306
Cdd:pfam00089 154 SAYGGT---------VTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGC-ASGNYPGVYTPVSSYLDW 218

                  .
gi 6678293    307 I 307
Cdd:pfam00089 219 I 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
65-309 1.62e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 164.44  E-value: 1.62e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293   65 QGKIYGGQIAKAERWPWQASLIFRG---RHICGAVLIDKTWLLSAAHCFQRSlTPSDYRILLGYNQLSNPSNYSRqmTVN 141
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGGTVV--KVA 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293  142 KVILHEDYSKlSRLEKNIVLIQLHHPViysTHIFPACVPDGTTKVSPNNLCWISGWGMLSADkflQAPFP--LLDAEVSL 219
Cdd:COG5640 105 RIVVHPDYDP-ATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEG---PGSQSgtLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293  220 IDEEECTTFFqtpevsiteyDVIKDDVLCAGDLTNQKSSCRGDSGGPLVCFLNSFWYVVGLANW-NGAClePIHSPNIFT 298
Cdd:COG5640 178 VSDATCAAYG----------GFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWgGGPC--AAGYPGVYT 245
                       250
                ....*....|.
gi 6678293  299 KVSYFSDWIKQ 309
Cdd:COG5640 246 RVSAYRDWIKS 256
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
79-192 1.30e-08

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: 52.55  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678293     79 WPWQASLIFRGRHICGAVLIDKTWLLSAAHCFQR-SLTPSDYRILLGYNQ--LSNPSNYSRqmtVNKVILHEDYSKlsrl 155
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtNLRHQYISVVLGGAKtlKSIEGPYEQ---IVRVDCRHDIPE---- 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 6678293    156 eKNIVLIQLHHPVIYSTHIFPACVPDGTTKVSPNNLC 192
Cdd:pfam09342  74 -SEISLLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
 
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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