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Conserved domains on  [gi|2765010|emb|CAA70820|]
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Protein Classification

serine protease (domain architecture ID 12184331)

trypsin-like serine protease such as snake venom serine proteases and trypsin, which preferentially cleaves peptide bonds after arginine and lysine residues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-254 4.41e-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: 215.23  E-value: 4.41e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010      31 RIIGGTEANISNFPWQVSVESAGD-HTCGGSLISPDWVLTFSLCLDGFSgvfehlLQFVSLRAGTS--TKGSGGVVLLAA 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSD------PSNIRVRLGSHdlSSGEEGQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010     108 EMYEHPLYIPLTVDYDVALIKVNGSFALGPNVQAVSLPEQGYDPPVGLPVTITGWGY-NVTDGSLSSVLQKVDVNIVDRA 186
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2765010     187 VCQATYV-IRNVTARMVCAGELLRG--SCDGDFG*PLVSGS---TQVGVLSWTlFPCELGL--DVYANVVSFRSWI 254
Cdd:smart00020 155 TCRRAYSgGGAITDNMLCAGGLEGGkdACQGDSGGPLVCNDgrwVLVGIVSWG-SGCARPGkpGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-254 4.41e-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: 215.23  E-value: 4.41e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010      31 RIIGGTEANISNFPWQVSVESAGD-HTCGGSLISPDWVLTFSLCLDGFSgvfehlLQFVSLRAGTS--TKGSGGVVLLAA 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSD------PSNIRVRLGSHdlSSGEEGQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010     108 EMYEHPLYIPLTVDYDVALIKVNGSFALGPNVQAVSLPEQGYDPPVGLPVTITGWGY-NVTDGSLSSVLQKVDVNIVDRA 186
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2765010     187 VCQATYV-IRNVTARMVCAGELLRG--SCDGDFG*PLVSGS---TQVGVLSWTlFPCELGL--DVYANVVSFRSWI 254
Cdd:smart00020 155 TCRRAYSgGGAITDNMLCAGGLEGGkdACQGDSGGPLVCNDgrwVLVGIVSWG-SGCARPGkpGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
32-257 5.71e-70

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: 214.83  E-value: 5.71e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010   32 IIGGTEANISNFPWQVSVE-SAGDHTCGGSLISPDWVLTFSLCLDGFSgvfehlLQFVSLRAGTSTKGS---GGVVLLAA 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSA------PSNYTVRLGSHDLSSnegGGQVIKVK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010  108 EMYEHPLYIPLTVDYDVALIKVNGSFALGPNVQAVSLPEQGYDPPVGLPVTITGWGYNVTDGSLSSVLQKVDVNIVDRAV 187
Cdd:cd00190  75 KVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAE 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2765010  188 CQATYVIRN-VTARMVCAGELLRG--SCDGDFG*PLVSGS----TQVGVLSWTLFpCELGL--DVYANVVSFRSWISEV 257
Cdd:cd00190 155 CKRAYSYGGtITDNMLCAGGLEGGkdACQGDSGGPLVCNDngrgVLVGIVSWGSG-CARPNypGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
32-254 3.51e-51

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 166.46  E-value: 3.51e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010     32 IIGGTEANISNFPWQVSVE-SAGDHTCGGSLISPDWVLTFSLCLDGFSGVFehllqfVSLRAGTSTKGSGGVVLLAAEM- 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVK------VVLGAHNIVLREGGEQKFDVEKi 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010    110 YEHPLYIPLTVDYDVALIKVNGSFALGPNVQAVSLPEQGYDPPVGLPVTITGWGYNVTDGsLSSVLQKVDVNIVDRAVCQ 189
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2765010    190 ATYVIRnVTARMVCAGELLRGSCDGDFG*PLVSGSTQV-GVLSWTlFPCELGL--DVYANVVSFRSWI 254
Cdd:pfam00089 154 SAYGGT-VTDTMICAGAGGKDACQGDSGGPLVCSDGELiGIVSWG-YGCASGNypGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
31-257 1.53e-22

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 95.33  E-value: 1.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010   31 RIIGGTEANISNFPWQVS-VESAGDHT----CGGSLISPDWVLTFSLCLDGfSGVFEHLLQFVSLRAGTSTKGSGGVVLL 105
Cdd:COG5640  32 RIIGGSNANAGEYPSLVAlVDRISDYVsgtfCGGSKLGGRYVLTAAHCADA-SSPISSDVNRVVVDLNDSSQAERGHVRT 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010  106 AaemYEHPLYIPLTVDYDVALIKVNgsfalgpnvQAVSLPE---QGYDPPVGLPVTITGWGYnVTDGSL----------- 171
Cdd:COG5640 111 I---YVHEFYSPGNLGNDIAVLELA---------RAASLPRvkiTSFDASDTFLNSVTTVSP-MTNGTFgvttpsdvprs 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010  172 ---SSVLQKVDVNIVDRAVCQATYVIRN-----VTARMVCAGELLRGSCDGDFG*PLV----SGSTQVGVLSWTLFPC-- 237
Cdd:COG5640 178 spkGTILHEVAVLFVPLSTCAQYKGCANasdgaTGLTGFCAGRPPKDACQGDSGGPIFhkgeEGRVQRGVVSWGDGGCgg 257
                       250       260
                ....*....|....*....|
gi 2765010  238 ELGLDVYANVVSFRSWISEV 257
Cdd:COG5640 258 TLIPGVYTNVSNYQDWIAAM 277
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-254 4.41e-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: 215.23  E-value: 4.41e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010      31 RIIGGTEANISNFPWQVSVESAGD-HTCGGSLISPDWVLTFSLCLDGFSgvfehlLQFVSLRAGTS--TKGSGGVVLLAA 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSD------PSNIRVRLGSHdlSSGEEGQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010     108 EMYEHPLYIPLTVDYDVALIKVNGSFALGPNVQAVSLPEQGYDPPVGLPVTITGWGY-NVTDGSLSSVLQKVDVNIVDRA 186
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2765010     187 VCQATYV-IRNVTARMVCAGELLRG--SCDGDFG*PLVSGS---TQVGVLSWTlFPCELGL--DVYANVVSFRSWI 254
Cdd:smart00020 155 TCRRAYSgGGAITDNMLCAGGLEGGkdACQGDSGGPLVCNDgrwVLVGIVSWG-SGCARPGkpGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
32-257 5.71e-70

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: 214.83  E-value: 5.71e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010   32 IIGGTEANISNFPWQVSVE-SAGDHTCGGSLISPDWVLTFSLCLDGFSgvfehlLQFVSLRAGTSTKGS---GGVVLLAA 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSA------PSNYTVRLGSHDLSSnegGGQVIKVK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010  108 EMYEHPLYIPLTVDYDVALIKVNGSFALGPNVQAVSLPEQGYDPPVGLPVTITGWGYNVTDGSLSSVLQKVDVNIVDRAV 187
Cdd:cd00190  75 KVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAE 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2765010  188 CQATYVIRN-VTARMVCAGELLRG--SCDGDFG*PLVSGS----TQVGVLSWTLFpCELGL--DVYANVVSFRSWISEV 257
Cdd:cd00190 155 CKRAYSYGGtITDNMLCAGGLEGGkdACQGDSGGPLVCNDngrgVLVGIVSWGSG-CARPNypGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
32-254 3.51e-51

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 166.46  E-value: 3.51e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010     32 IIGGTEANISNFPWQVSVE-SAGDHTCGGSLISPDWVLTFSLCLDGFSGVFehllqfVSLRAGTSTKGSGGVVLLAAEM- 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVK------VVLGAHNIVLREGGEQKFDVEKi 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010    110 YEHPLYIPLTVDYDVALIKVNGSFALGPNVQAVSLPEQGYDPPVGLPVTITGWGYNVTDGsLSSVLQKVDVNIVDRAVCQ 189
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2765010    190 ATYVIRnVTARMVCAGELLRGSCDGDFG*PLVSGSTQV-GVLSWTlFPCELGL--DVYANVVSFRSWI 254
Cdd:pfam00089 154 SAYGGT-VTDTMICAGAGGKDACQGDSGGPLVCSDGELiGIVSWG-YGCASGNypGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
31-257 1.53e-22

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 95.33  E-value: 1.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010   31 RIIGGTEANISNFPWQVS-VESAGDHT----CGGSLISPDWVLTFSLCLDGfSGVFEHLLQFVSLRAGTSTKGSGGVVLL 105
Cdd:COG5640  32 RIIGGSNANAGEYPSLVAlVDRISDYVsgtfCGGSKLGGRYVLTAAHCADA-SSPISSDVNRVVVDLNDSSQAERGHVRT 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010  106 AaemYEHPLYIPLTVDYDVALIKVNgsfalgpnvQAVSLPE---QGYDPPVGLPVTITGWGYnVTDGSL----------- 171
Cdd:COG5640 111 I---YVHEFYSPGNLGNDIAVLELA---------RAASLPRvkiTSFDASDTFLNSVTTVSP-MTNGTFgvttpsdvprs 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2765010  172 ---SSVLQKVDVNIVDRAVCQATYVIRN-----VTARMVCAGELLRGSCDGDFG*PLV----SGSTQVGVLSWTLFPC-- 237
Cdd:COG5640 178 spkGTILHEVAVLFVPLSTCAQYKGCANasdgaTGLTGFCAGRPPKDACQGDSGGPIFhkgeEGRVQRGVVSWGDGGCgg 257
                       250       260
                ....*....|....*....|
gi 2765010  238 ELGLDVYANVVSFRSWISEV 257
Cdd:COG5640 258 TLIPGVYTNVSNYQDWIAAM 277
 
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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