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Conserved domains on  [gi|117613|sp|P00769|]
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RecName: Full=Chymotrypsin-2; AltName: Full=Chymotrypsin II

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 ...
1-216 8.47e-82

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: 243.34  E-value: 8.47e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613     1 IVGGTDAPRGKYPYQVSLR--APKHFCGGS-ISKRYVLTAAHCLVGKSKHQVTVHAGSVLLNKEEA---VYNAEELIVNK 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQytGGRHFCGGSlISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGggqVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613    75 NYNSIRLINDIGLIRVSKDISYTQLVQPVKLPVSNTI-KAGDPVVLTGWGRIYVNGPIPNNLQQITLSIVNQQTCKFKHW 153
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNlPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117613   154 G---LTDSQICTFT-KLGEGACDGDSGGPLVAN----GVQIGIVSYGHPCAV-GSPNVFTRVYSFLDWIQKN 216
Cdd:cd00190 161 YggtITDNMLCAGGlEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-216 8.47e-82

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: 243.34  E-value: 8.47e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613     1 IVGGTDAPRGKYPYQVSLR--APKHFCGGS-ISKRYVLTAAHCLVGKSKHQVTVHAGSVLLNKEEA---VYNAEELIVNK 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQytGGRHFCGGSlISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGggqVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613    75 NYNSIRLINDIGLIRVSKDISYTQLVQPVKLPVSNTI-KAGDPVVLTGWGRIYVNGPIPNNLQQITLSIVNQQTCKFKHW 153
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNlPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117613   154 G---LTDSQICTFT-KLGEGACDGDSGGPLVAN----GVQIGIVSYGHPCAV-GSPNVFTRVYSFLDWIQKN 216
Cdd:cd00190 161 YggtITDNMLCAGGlEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-213 1.35e-78

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: 234.88  E-value: 1.35e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613        1 IVGGTDAPRGKYPYQVSLR--APKHFCGGS-ISKRYVLTAAHCLVGKSKHQVTVHAGSVLLNKEEA--VYNAEELIVNKN 75
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQygGGRHFCGGSlISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEgqVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613       76 YNSIRLINDIGLIRVSKDISYTQLVQPVKLPVSN-TIKAGDPVVLTGWGRI-YVNGPIPNNLQQITLSIVNQQTCKFKHW 153
Cdd:smart00020  82 YNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNyNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATCRRAYS 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117613      154 G---LTDSQICTFT-KLGEGACDGDSGGPLVAN---GVQIGIVSYGHPCA-VGSPNVFTRVYSFLDWI 213
Cdd:smart00020 162 GggaITDNMLCAGGlEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCArPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-213 7.13e-59

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 184.57  E-value: 7.13e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613       1 IVGGTDAPRGKYPYQVSL--RAPKHFCGGS-ISKRYVLTAAHCLvgKSKHQVTVHAGSVLLNKEEA---VYNAEELIVNK 74
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqlSSGKHFCGGSlISENWVLTAAHCV--SGASDVKVVLGAHNIVLREGgeqKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613      75 NYNSIRLINDIGLIRVSKDISYTQLVQPVKLP-VSNTIKAGDPVVLTGWGRIYVNGPiPNNLQQITLSIVNQQTCKfKHW 153
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPdASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCR-SAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117613     154 G--LTDSQICTFTKlGEGACDGDSGGPLVANGVQ-IGIVSYGHPCAVGS-PNVFTRVYSFLDWI 213
Cdd:pfam00089 157 GgtVTDTMICAGAG-GKDACQGDSGGPLVCSDGElIGIVSWGYGCASGNyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-218 1.19e-29

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 113.82  E-value: 1.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613     1 IVGGTDAPRGKYPYQVSL------RAPKHFCGGSISK-RYVLTAAHCLVGKSKHQVTVHAGSVLLNKEEAV--YNAEELI 71
Cdd:COG5640  33 IIGGSNANAGEYPSLVALvdrisdYVSGTFCGGSKLGgRYVLTAAHCADASSPISSDVNRVVVDLNDSSQAerGHVRTIY 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613    72 VNKNYNSIRLINDIGLIRVSkDISYTQLVQ--------PVKLPVSNTIKAGDPVVLTGwGRIYVNGPIPNN--LQQITLS 141
Cdd:COG5640 113 VHEFYSPGNLGNDIAVLELA-RAASLPRVKitsfdasdTFLNSVTTVSPMTNGTFGVT-TPSDVPRSSPKGtiLHEVAVL 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613   142 IVNQQTCKFK---------HWGLTDSQICTFTKlgeGACDGDSGGPLVANG----VQIGIVSYG-HPCA-VGSPNVFTRV 206
Cdd:COG5640 191 FVPLSTCAQYkgcanasdgATGLTGFCAGRPPK---DACQGDSGGPIFHKGeegrVQRGVVSWGdGGCGgTLIPGVYTNV 267
                       250
                ....*....|..
gi 117613   207 YSFLDWIQKNQL 218
Cdd:COG5640 268 SNYQDWIAAMTN 279
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-216 8.47e-82

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: 243.34  E-value: 8.47e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613     1 IVGGTDAPRGKYPYQVSLR--APKHFCGGS-ISKRYVLTAAHCLVGKSKHQVTVHAGSVLLNKEEA---VYNAEELIVNK 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQytGGRHFCGGSlISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGggqVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613    75 NYNSIRLINDIGLIRVSKDISYTQLVQPVKLPVSNTI-KAGDPVVLTGWGRIYVNGPIPNNLQQITLSIVNQQTCKFKHW 153
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNlPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117613   154 G---LTDSQICTFT-KLGEGACDGDSGGPLVAN----GVQIGIVSYGHPCAV-GSPNVFTRVYSFLDWIQKN 216
Cdd:cd00190 161 YggtITDNMLCAGGlEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-213 1.35e-78

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: 234.88  E-value: 1.35e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613        1 IVGGTDAPRGKYPYQVSLR--APKHFCGGS-ISKRYVLTAAHCLVGKSKHQVTVHAGSVLLNKEEA--VYNAEELIVNKN 75
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQygGGRHFCGGSlISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEgqVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613       76 YNSIRLINDIGLIRVSKDISYTQLVQPVKLPVSN-TIKAGDPVVLTGWGRI-YVNGPIPNNLQQITLSIVNQQTCKFKHW 153
Cdd:smart00020  82 YNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNyNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATCRRAYS 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117613      154 G---LTDSQICTFT-KLGEGACDGDSGGPLVAN---GVQIGIVSYGHPCA-VGSPNVFTRVYSFLDWI 213
Cdd:smart00020 162 GggaITDNMLCAGGlEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCArPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-213 7.13e-59

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 184.57  E-value: 7.13e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613       1 IVGGTDAPRGKYPYQVSL--RAPKHFCGGS-ISKRYVLTAAHCLvgKSKHQVTVHAGSVLLNKEEA---VYNAEELIVNK 74
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqlSSGKHFCGGSlISENWVLTAAHCV--SGASDVKVVLGAHNIVLREGgeqKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613      75 NYNSIRLINDIGLIRVSKDISYTQLVQPVKLP-VSNTIKAGDPVVLTGWGRIYVNGPiPNNLQQITLSIVNQQTCKfKHW 153
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPdASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCR-SAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117613     154 G--LTDSQICTFTKlGEGACDGDSGGPLVANGVQ-IGIVSYGHPCAVGS-PNVFTRVYSFLDWI 213
Cdd:pfam00089 157 GgtVTDTMICAGAG-GKDACQGDSGGPLVCSDGElIGIVSWGYGCASGNyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-218 1.19e-29

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 113.82  E-value: 1.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613     1 IVGGTDAPRGKYPYQVSL------RAPKHFCGGSISK-RYVLTAAHCLVGKSKHQVTVHAGSVLLNKEEAV--YNAEELI 71
Cdd:COG5640  33 IIGGSNANAGEYPSLVALvdrisdYVSGTFCGGSKLGgRYVLTAAHCADASSPISSDVNRVVVDLNDSSQAerGHVRTIY 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613    72 VNKNYNSIRLINDIGLIRVSkDISYTQLVQ--------PVKLPVSNTIKAGDPVVLTGwGRIYVNGPIPNN--LQQITLS 141
Cdd:COG5640 113 VHEFYSPGNLGNDIAVLELA-RAASLPRVKitsfdasdTFLNSVTTVSPMTNGTFGVT-TPSDVPRSSPKGtiLHEVAVL 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613   142 IVNQQTCKFK---------HWGLTDSQICTFTKlgeGACDGDSGGPLVANG----VQIGIVSYG-HPCA-VGSPNVFTRV 206
Cdd:COG5640 191 FVPLSTCAQYkgcanasdgATGLTGFCAGRPPK---DACQGDSGGPIFHKGeegrVQRGVVSWGdGGCGgTLIPGVYTNV 267
                       250
                ....*....|..
gi 117613   207 YSFLDWIQKNQL 218
Cdd:COG5640 268 SNYQDWIAAMTN 279
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
5-216 1.38e-05

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


Pssm-ID: 226119  Cd Length: 251  Bit Score: 44.68  E-value: 1.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613     5 TDAPRGKYPYQVSLRAPK-HFCGGS--ISKRYVLTAAHCLVG--KSKHQVTVHAGSVllNKEEAVYNAEELIVNKNYNSI 79
Cdd:COG3591  44 TDTTQFPYSAVVQFEAATgRLCTAAtlIGPNTVLTAGHCIYSpdYGEDDIAAAPPGV--NSDGGPFYGITKIEIRVYPGE 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613    80 RL-----INDIGLIRVSKDISYTQLVQPVKLPVSNTIKAGDPVVLTGWgriyvNGPIPNNLQQITLS--IVNQQTCKFKH 152
Cdd:COG3591 122 LYkedgaSYDVGEAALESGINIGDVVNYLKRNTASEAKANDRITVIGY-----PGDKPNIGTMWESTgkVNSIKGNKLFY 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117613   153 WglTDSQIctftklgegacdGDSGGP-LVANGVQIGIVsYGHPCAVGSPNVFTRVYS---FLDWIQKN 216
Cdd:COG3591 197 D--ADTLP------------GSSGSPvLISKDEVIGVH-YNGPGANGGSLANNAVRLtpeILNFIQQN 249
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
30-188 2.63e-04

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 404275 [Multi-domain]  Cd Length: 142  Bit Score: 39.72  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613      30 SKRYVLTAAHCLvgKSKHQVTVHAGSVLLnKEEAVYNAEELIVNKNYnsirlinDIGLIRVSKDISytqLVQPVKLPVSN 109
Cdd:pfam13365   8 PDGLVLTNAHVV--DDAEEAAVEFVSVVL-ADGREYPATVVARDPDL-------DLALLRVDGDGR---GLPPLPLGDSE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117613     110 TIKAGDPVVLTGWgriyvngPIPNNLQQITLSIVNQQTCKFKHWGLTDSQICTfTKLGEGAcdgdSGGPLV-ANGVQIGI 188
Cdd:pfam13365  75 PLVGGERVYAVGY-------PLGGEKLSLSEGIVSGVDEGRDGGDDGRFIQTD-AALSPGS----SGGPVFdADGRVVGI 142
 
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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