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Conserved domains on  [gi|1336053|gb|AAB01218|]
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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 ...
26-265 5.58e-88

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: 261.06  E-value: 5.58e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053   26 IVGGDEAEAHEFPYQISLQWNFNdgqtetMHFCGASVLNENFVLTAAHCKTaYSNTGFIEVVAAEHDVAVAEGSEQRRLV 105
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGG------RHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053  106 AEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTVFpdYPDKLRKVVLPLVD 183
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpAGTtCTVSGWGRTSEGGP--LPDVLQEVNVPIVS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053  184 YEQCDTLWGNDSALAKSNVCAGPIDGSKSACSADSGGPLVKQSGEEVIQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWIE 263
Cdd:cd00190 152 NAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWG-SGCARPNYPGVYTRVSSYLDWIQ 230

                ..
gi 1336053  264 QQ 265
Cdd:cd00190 231 KT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
26-265 5.58e-88

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: 261.06  E-value: 5.58e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053   26 IVGGDEAEAHEFPYQISLQWNFNdgqtetMHFCGASVLNENFVLTAAHCKTaYSNTGFIEVVAAEHDVAVAEGSEQRRLV 105
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGG------RHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053  106 AEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTVFpdYPDKLRKVVLPLVD 183
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpAGTtCTVSGWGRTSEGGP--LPDVLQEVNVPIVS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053  184 YEQCDTLWGNDSALAKSNVCAGPIDGSKSACSADSGGPLVKQSGEEVIQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWIE 263
Cdd:cd00190 152 NAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWG-SGCARPNYPGVYTRVSSYLDWIQ 230

                ..
gi 1336053  264 QQ 265
Cdd:cd00190 231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
25-262 7.07e-83

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: 247.98  E-value: 7.07e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053      25 KIVGGDEAEAHEFPYQISLQWNFNDgqtetmHFCGASVLNENFVLTAAHCKTaYSNTGFIEVVAAEHDVAVaEGSEQRRL 104
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR------HFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSS-GEEGQVIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053     105 VAEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTVfPDYPDKLRKVVLPLV 182
Cdd:smart00020  73 VSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTtCTVSGWGRTSEGA-GSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053     183 DYEQCDTLWGNDSALAKSNVCAGPIDGSKSACSADSGGPLVKQSGEEViQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWI 262
Cdd:smart00020 152 SNATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWV-LVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
26-262 5.49e-63

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 196.89  E-value: 5.49e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053     26 IVGGDEAEAHEFPYQISLQWnfndgqTETMHFCGASVLNENFVLTAAHCktaYSNTGFIEVVAAEHDVAVAEGSEQRRLV 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL------SSGKHFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053    106 AEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTvfpDYPDKLRKVVLPLVD 183
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpVGTtCTVSGWGNTKTL---GPSDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336053    184 YEQCDTLWGNDsaLAKSNVCAGPidGSKSACSADSGGPLVKQSGEeviQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWI 262
Cdd:pfam00089 149 RETCRSAYGGT--VTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-265 5.35e-35

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 129.61  E-value: 5.35e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053    1 MAFKLTVAFLLvaSLALASSRATHKIVGGDEAEAHEFPYQISLQWNFNDGQTETmhFCGASVLNENFVLTAAHC---KTA 77
Cdd:COG5640  10 FGLSLFLTLQP--SAAQTADEVSSRIIGGSNANAGEYPSLVALVDRISDYVSGT--FCGGSKLGGRYVLTAAHCadaSSP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053   78 YSNTGFIEVVAAEhDVAVAEGSEqrrlVAEFIVHEDYQGGVSPDDIAVIRVDKPfelnDKVKAVKLPKQLEQFDGDVTLS 157
Cdd:COG5640  86 ISSDVNRVVVDLN-DSSQAERGH----VRTIYVHEFYSPGNLGNDIAVLELARA----ASLPRVKITSFDASDTFLNSVT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053  158 GWGSVSTTVFP-----DYPD------KLRKVVLPLVDYEQCDTLWGN----DSALAKSNVCAGPIdgSKSACSADSGGPL 222
Cdd:COG5640 157 TVSPMTNGTFGvttpsDVPRsspkgtILHEVAVLFVPLSTCAQYKGCanasDGATGLTGFCAGRP--PKDACQGDSGGPI 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 1336053  223 VKQSGEEVIQVGVVSWGAVPCGSPRRPTVFAGVSHYVDWIEQQ 265
Cdd:COG5640 235 FHKGEEGRVQRGVVSWGDGGCGGTLIPGVYTNVSNYQDWIAAM 277
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
26-265 5.58e-88

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: 261.06  E-value: 5.58e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053   26 IVGGDEAEAHEFPYQISLQWNFNdgqtetMHFCGASVLNENFVLTAAHCKTaYSNTGFIEVVAAEHDVAVAEGSEQRRLV 105
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGG------RHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053  106 AEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTVFpdYPDKLRKVVLPLVD 183
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpAGTtCTVSGWGRTSEGGP--LPDVLQEVNVPIVS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053  184 YEQCDTLWGNDSALAKSNVCAGPIDGSKSACSADSGGPLVKQSGEEVIQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWIE 263
Cdd:cd00190 152 NAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWG-SGCARPNYPGVYTRVSSYLDWIQ 230

                ..
gi 1336053  264 QQ 265
Cdd:cd00190 231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
25-262 7.07e-83

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: 247.98  E-value: 7.07e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053      25 KIVGGDEAEAHEFPYQISLQWNFNDgqtetmHFCGASVLNENFVLTAAHCKTaYSNTGFIEVVAAEHDVAVaEGSEQRRL 104
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR------HFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSS-GEEGQVIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053     105 VAEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTVfPDYPDKLRKVVLPLV 182
Cdd:smart00020  73 VSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTtCTVSGWGRTSEGA-GSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053     183 DYEQCDTLWGNDSALAKSNVCAGPIDGSKSACSADSGGPLVKQSGEEViQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWI 262
Cdd:smart00020 152 SNATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWV-LVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
26-262 5.49e-63

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 196.89  E-value: 5.49e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053     26 IVGGDEAEAHEFPYQISLQWnfndgqTETMHFCGASVLNENFVLTAAHCktaYSNTGFIEVVAAEHDVAVAEGSEQRRLV 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL------SSGKHFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053    106 AEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTvfpDYPDKLRKVVLPLVD 183
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpVGTtCTVSGWGNTKTL---GPSDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336053    184 YEQCDTLWGNDsaLAKSNVCAGPidGSKSACSADSGGPLVKQSGEeviQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWI 262
Cdd:pfam00089 149 RETCRSAYGGT--VTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-265 5.35e-35

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 129.61  E-value: 5.35e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053    1 MAFKLTVAFLLvaSLALASSRATHKIVGGDEAEAHEFPYQISLQWNFNDGQTETmhFCGASVLNENFVLTAAHC---KTA 77
Cdd:COG5640  10 FGLSLFLTLQP--SAAQTADEVSSRIIGGSNANAGEYPSLVALVDRISDYVSGT--FCGGSKLGGRYVLTAAHCadaSSP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053   78 YSNTGFIEVVAAEhDVAVAEGSEqrrlVAEFIVHEDYQGGVSPDDIAVIRVDKPfelnDKVKAVKLPKQLEQFDGDVTLS 157
Cdd:COG5640  86 ISSDVNRVVVDLN-DSSQAERGH----VRTIYVHEFYSPGNLGNDIAVLELARA----ASLPRVKITSFDASDTFLNSVT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336053  158 GWGSVSTTVFP-----DYPD------KLRKVVLPLVDYEQCDTLWGN----DSALAKSNVCAGPIdgSKSACSADSGGPL 222
Cdd:COG5640 157 TVSPMTNGTFGvttpsDVPRsspkgtILHEVAVLFVPLSTCAQYKGCanasDGATGLTGFCAGRP--PKDACQGDSGGPI 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 1336053  223 VKQSGEEVIQVGVVSWGAVPCGSPRRPTVFAGVSHYVDWIEQQ 265
Cdd:COG5640 235 FHKGEEGRVQRGVVSWGDGGCGGTLIPGVYTNVSNYQDWIAAM 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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