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Conserved domains on  [gi|150421533|sp|Q27289|]
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RecName: Full=Chymotrypsin-1; AltName: Full=AnChym1; Flags: Precursor

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 ...
32-250 7.39e-81

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: 242.58  E-value: 7.39e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533    32 RVVGGEVAKNGSAPYQVSLQVPGWGHNCGGSLLNDRWVLTAAHCLVGHAPGDLMVLVGTNSLKEGGE--LLKVDKLLYHS 109
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEgqVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533   110 RYNLPRFHNDIGLVRLEQPVRFSELVQSVEYSEKA--VPANATVRLTGWGHTSANGPS-PTLLQSLNVVTLSNEDCNKKG 186
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150421533   187 GDPGYTDVGHLCTLTKT-GEGACNGDSGGPLVYEGK---LVGVVNFGVPCAL-GYPDGFARVSYYHDWV 250
Cdd:smart00020 161 SGGGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARpGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
32-250 7.39e-81

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: 242.58  E-value: 7.39e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533    32 RVVGGEVAKNGSAPYQVSLQVPGWGHNCGGSLLNDRWVLTAAHCLVGHAPGDLMVLVGTNSLKEGGE--LLKVDKLLYHS 109
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEgqVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533   110 RYNLPRFHNDIGLVRLEQPVRFSELVQSVEYSEKA--VPANATVRLTGWGHTSANGPS-PTLLQSLNVVTLSNEDCNKKG 186
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150421533   187 GDPGYTDVGHLCTLTKT-GEGACNGDSGGPLVYEGK---LVGVVNFGVPCAL-GYPDGFARVSYYHDWV 250
Cdd:smart00020 161 SGGGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARpGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
33-253 1.30e-80

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: 241.80  E-value: 1.30e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533  33 VVGGEVAKNGSAPYQVSLQVPGWGHNCGGSLLNDRWVLTAAHCLVGHAPGDLMVLVGT---NSLKEGGELLKVDKLLYHS 109
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGShdlSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533 110 RYNLPRFHNDIGLVRLEQPVRFSELVQSVE--YSEKAVPANATVRLTGWGHTSANGPSPTLLQSLNVVTLSNEDCNKKGG 187
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPIClpSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150421533 188 DPGYTDVGHLCTLTKT-GEGACNGDSGGPLVYE----GKLVGVVNFGVPCAL-GYPDGFARVSYYHDWVRTT 253
Cdd:cd00190  161 YGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
33-250 2.74e-62

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 194.97  E-value: 2.74e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533   33 VVGGEVAKNGSAPYQVSLQVPGWGHNCGGSLLNDRWVLTAAHCLVGhaPGDLMVLVGTNSLK--EGGE-LLKVDKLLYHS 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVlrEGGEqKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533  110 RYNLPRFHNDIGLVRLEQPVRFSELVQSVEYSEKA--VPANATVRLTGWGHTSANGPSPTlLQSLNVVTLSNEDCNKKGG 187
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150421533  188 dpGYTDVGHLCTLTkTGEGACNGDSGGPLVYE-GKLVGVVNFGVPCALG-YPDGFARVSYYHDWV 250
Cdd:pfam00089 158 --GTVTDTMICAGA-GGKDACQGDSGGPLVCSdGELIGIVSWGYGCASGnYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
32-254 3.51e-25

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 102.65  E-value: 3.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533  32 RVVGGEVAKNGSAPYQVSLQVPGW----GHNCGGSLLNDRWVLTAAHCLVGHAP--GD-LMVLVGTNSLKEgGELLKVDK 104
Cdd:COG5640   32 RIIGGSNANAGEYPSLVALVDRISdyvsGTFCGGSKLGGRYVLTAAHCADASSPisSDvNRVVVDLNDSSQ-AERGHVRT 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533 105 LLYHSRYNLPRFHNDIGLVRLEQ----PVRFSELVQSVEYSEKAVPA-----NATVRLTGWGHTSANGPSPTLLQSLNV- 174
Cdd:COG5640  111 IYVHEFYSPGNLGNDIAVLELARaaslPRVKITSFDASDTFLNSVTTvspmtNGTFGVTTPSDVPRSSPKGTILHEVAVl 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533 175 -VTLSN-----EDCNKKGGDPGYTDVghlcTLTKTGEGACNGDSGGPLVYEG----KLVGVVNFGV-PCA-LGYPDGFAR 242
Cdd:COG5640  191 fVPLSTcaqykGCANASDGATGLTGF----CAGRPPKDACQGDSGGPIFHKGeegrVQRGVVSWGDgGCGgTLIPGVYTN 266
                        250
                 ....*....|..
gi 150421533 243 VSYYHDWVRTTM 254
Cdd:COG5640  267 VSNYQDWIAAMT 278
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
32-250 7.39e-81

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: 242.58  E-value: 7.39e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533    32 RVVGGEVAKNGSAPYQVSLQVPGWGHNCGGSLLNDRWVLTAAHCLVGHAPGDLMVLVGTNSLKEGGE--LLKVDKLLYHS 109
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEgqVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533   110 RYNLPRFHNDIGLVRLEQPVRFSELVQSVEYSEKA--VPANATVRLTGWGHTSANGPS-PTLLQSLNVVTLSNEDCNKKG 186
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150421533   187 GDPGYTDVGHLCTLTKT-GEGACNGDSGGPLVYEGK---LVGVVNFGVPCAL-GYPDGFARVSYYHDWV 250
Cdd:smart00020 161 SGGGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARpGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
33-253 1.30e-80

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: 241.80  E-value: 1.30e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533  33 VVGGEVAKNGSAPYQVSLQVPGWGHNCGGSLLNDRWVLTAAHCLVGHAPGDLMVLVGT---NSLKEGGELLKVDKLLYHS 109
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGShdlSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533 110 RYNLPRFHNDIGLVRLEQPVRFSELVQSVE--YSEKAVPANATVRLTGWGHTSANGPSPTLLQSLNVVTLSNEDCNKKGG 187
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPIClpSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150421533 188 DPGYTDVGHLCTLTKT-GEGACNGDSGGPLVYE----GKLVGVVNFGVPCAL-GYPDGFARVSYYHDWVRTT 253
Cdd:cd00190  161 YGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
33-250 2.74e-62

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 194.97  E-value: 2.74e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533   33 VVGGEVAKNGSAPYQVSLQVPGWGHNCGGSLLNDRWVLTAAHCLVGhaPGDLMVLVGTNSLK--EGGE-LLKVDKLLYHS 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVlrEGGEqKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533  110 RYNLPRFHNDIGLVRLEQPVRFSELVQSVEYSEKA--VPANATVRLTGWGHTSANGPSPTlLQSLNVVTLSNEDCNKKGG 187
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150421533  188 dpGYTDVGHLCTLTkTGEGACNGDSGGPLVYE-GKLVGVVNFGVPCALG-YPDGFARVSYYHDWV 250
Cdd:pfam00089 158 --GTVTDTMICAGA-GGKDACQGDSGGPLVCSdGELIGIVSWGYGCASGnYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
32-254 3.51e-25

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 102.65  E-value: 3.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533  32 RVVGGEVAKNGSAPYQVSLQVPGW----GHNCGGSLLNDRWVLTAAHCLVGHAP--GD-LMVLVGTNSLKEgGELLKVDK 104
Cdd:COG5640   32 RIIGGSNANAGEYPSLVALVDRISdyvsGTFCGGSKLGGRYVLTAAHCADASSPisSDvNRVVVDLNDSSQ-AERGHVRT 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533 105 LLYHSRYNLPRFHNDIGLVRLEQ----PVRFSELVQSVEYSEKAVPA-----NATVRLTGWGHTSANGPSPTLLQSLNV- 174
Cdd:COG5640  111 IYVHEFYSPGNLGNDIAVLELARaaslPRVKITSFDASDTFLNSVTTvspmtNGTFGVTTPSDVPRSSPKGTILHEVAVl 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421533 175 -VTLSN-----EDCNKKGGDPGYTDVghlcTLTKTGEGACNGDSGGPLVYEG----KLVGVVNFGV-PCA-LGYPDGFAR 242
Cdd:COG5640  191 fVPLSTcaqykGCANASDGATGLTGF----CAGRPPKDACQGDSGGPIFHKGeegrVQRGVVSWGDgGCGgTLIPGVYTN 266
                        250
                 ....*....|..
gi 150421533 243 VSYYHDWVRTTM 254
Cdd:COG5640  267 VSNYQDWIAAMT 278
 
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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