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Conserved domains on  [gi|53157|emb|CAA48704|]
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serine protease 4, partial [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 ...
15-236 5.18e-94

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: 275.31  E-value: 5.18e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157     15 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVLTAAHC----SGREITVTLGAHDVSKTESTQQKIKVEKQI 90
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157     91 VHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDILREVKLRIMDKEACKN 170
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53157    171 YWHYDYNL---QVCVGSPRKKRSAYKGDSGGPLLC----AGVAHGIVSYGRGDAKP--PAVFTRISSYVPWINRV 236
Cdd:cd00190 158 AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
15-236 5.18e-94

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: 275.31  E-value: 5.18e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157     15 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVLTAAHC----SGREITVTLGAHDVSKTESTQQKIKVEKQI 90
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157     91 VHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDILREVKLRIMDKEACKN 170
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53157    171 YWHYDYNL---QVCVGSPRKKRSAYKGDSGGPLLC----AGVAHGIVSYGRGDAKP--PAVFTRISSYVPWINRV 236
Cdd:cd00190 158 AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
14-233 3.45e-87

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: 257.99  E-value: 3.45e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157        14 EIIGGVESRPHSRPYMAHLEItteRGFTATCGGFLITRQFVLTAAHC----SGREITVTLGAHDVSKTEStQQKIKVEKQ 89
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157        90 IVHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPT-SDILREVKLRIMDKEAC 168
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53157       169 KNYWHYDYNL---QVCVGSPRKKRSAYKGDSGGPLLC---AGVAHGIVSYGRGDAKP--PAVFTRISSYVPWI 233
Cdd:smart00020 157 RRAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
15-233 1.97e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 220.01  E-value: 1.97e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157       15 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVLTAAHC--SGREITVTLGAHDVSKTESTQQKIKVEKQIVH 92
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHF---CGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157       93 PKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPtSDILREVKLRIMDKEACKNYW 172
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53157      173 -HYDYNLQVCVGSprKKRSAYKGDSGGPLLCAGV-AHGIVSYGRGDAKP--PAVFTRISSYVPWI 233
Cdd:pfam00089 157 gGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
2-239 5.19e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 194.87  E-value: 5.19e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157      2 MALLLPSGAGAE---EIIGGVESRPHSRPYMAHLeITTERGFTATCGGFLITRQFVLTAAHC----SGREITVTLGAHDv 74
Cdd:COG5640  15 LALALAAAPAADaapAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTD- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157     75 sKTESTQQKIKVEKQIVHPKYNFYSNLHDIMLLKLqkkAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEP-TSD 153
Cdd:COG5640  93 -LSTSGGTVVKVARIVVHPDYDPATPGNDIALLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157    154 ILREVKLRIMDKEACKNYWHYDYNLQVCVGSPRKKRSAYKGDSGGPLL----CAGVAHGIVSYGRGDAKP--PAVFTRIS 227
Cdd:COG5640 169 TLRKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVS 248
                       250
                ....*....|..
gi 53157    228 SYVPWINRVIKG 239
Cdd:COG5640 249 AYRDWIKSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
15-236 5.18e-94

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: 275.31  E-value: 5.18e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157     15 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVLTAAHC----SGREITVTLGAHDVSKTESTQQKIKVEKQI 90
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157     91 VHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDILREVKLRIMDKEACKN 170
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53157    171 YWHYDYNL---QVCVGSPRKKRSAYKGDSGGPLLC----AGVAHGIVSYGRGDAKP--PAVFTRISSYVPWINRV 236
Cdd:cd00190 158 AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
14-233 3.45e-87

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: 257.99  E-value: 3.45e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157        14 EIIGGVESRPHSRPYMAHLEItteRGFTATCGGFLITRQFVLTAAHC----SGREITVTLGAHDVSKTEStQQKIKVEKQ 89
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157        90 IVHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPT-SDILREVKLRIMDKEAC 168
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53157       169 KNYWHYDYNL---QVCVGSPRKKRSAYKGDSGGPLLC---AGVAHGIVSYGRGDAKP--PAVFTRISSYVPWI 233
Cdd:smart00020 157 RRAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
15-233 1.97e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 220.01  E-value: 1.97e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157       15 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVLTAAHC--SGREITVTLGAHDVSKTESTQQKIKVEKQIVH 92
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHF---CGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157       93 PKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPtSDILREVKLRIMDKEACKNYW 172
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53157      173 -HYDYNLQVCVGSprKKRSAYKGDSGGPLLCAGV-AHGIVSYGRGDAKP--PAVFTRISSYVPWI 233
Cdd:pfam00089 157 gGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
2-239 5.19e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 194.87  E-value: 5.19e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157      2 MALLLPSGAGAE---EIIGGVESRPHSRPYMAHLeITTERGFTATCGGFLITRQFVLTAAHC----SGREITVTLGAHDv 74
Cdd:COG5640  15 LALALAAAPAADaapAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTD- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157     75 sKTESTQQKIKVEKQIVHPKYNFYSNLHDIMLLKLqkkAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEP-TSD 153
Cdd:COG5640  93 -LSTSGGTVVKVARIVVHPDYDPATPGNDIALLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157    154 ILREVKLRIMDKEACKNYWHYDYNLQVCVGSPRKKRSAYKGDSGGPLL----CAGVAHGIVSYGRGDAKP--PAVFTRIS 227
Cdd:COG5640 169 TLRKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVS 248
                       250
                ....*....|..
gi 53157    228 SYVPWINRVIKG 239
Cdd:COG5640 249 AYRDWIKSTAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
30-216 5.83e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.44  E-value: 5.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157     30 AHLEITTERGFtatCGGFLITRQFVLTAAHC-----SGR---EITVTLGAHDvskteSTQQKIKVEKQIVHPKYNFYSNL 101
Cdd:COG3591   3 GRLETDGGGGV---CTGTLIGPNLVLTAGHCvydgaGGGwatNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53157    102 -HDIMLLKLqkkaKETPSVNVIPLP-RPSDFIKPGKMCRAAGWGRTGVTEPTsdilREVKLRIMDKEAckNYWHYDynlq 179
Cdd:COG3591  75 gYDYALLRL----DEPLGDTTGWLGlAFNDAPLAGEPVTIIGYPGDRPKDLS----LDCSGRVTGVQG--NRLSYD---- 140
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 53157    180 vCVGSPrkkrsaykGDSGGPLL----CAGVAHGIVSYGRGD 216
Cdd:COG3591 141 -CDTTG--------GSSGSPVLddsdGGGRVVGVHSAGGAD 172
 
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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