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Conserved domains on  [gi|2168437777|gb|UHH90333|]
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granzyme B precursor [Acinonyx jubatus]

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

 Zoom to residue level

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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 ...
21-242 2.56e-92

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: 271.46  E-value: 2.56e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  21 IIGGHEAKPHSRPYMAHLWIQNREVCskCGGFLIQEKFVLTAAHCWGSS----INVTLGAHNIKKQEKTQQIIPVRRAIP 96
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHF--CGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  97 HPDYNPKNYSNDIMLLQLVKKAKLTAAVRPLGLPKGKDRVRPGQVCSVAGWGRVA-TGRYPDTLQEVELIVQEDQECKSR 175
Cdd:cd00190    79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168437777 176 FPNYYN-HKTQLCVGDPKEKKSSFQGDSGGPLLCN----NVAQGIVSYGLK--DRASPRAYTKVTSFLPWIKKT 242
Cdd:cd00190   159 YSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGcaRPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-242 2.56e-92

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: 271.46  E-value: 2.56e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  21 IIGGHEAKPHSRPYMAHLWIQNREVCskCGGFLIQEKFVLTAAHCWGSS----INVTLGAHNIKKQEKTQQIIPVRRAIP 96
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHF--CGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  97 HPDYNPKNYSNDIMLLQLVKKAKLTAAVRPLGLPKGKDRVRPGQVCSVAGWGRVA-TGRYPDTLQEVELIVQEDQECKSR 175
Cdd:cd00190    79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168437777 176 FPNYYN-HKTQLCVGDPKEKKSSFQGDSGGPLLCN----NVAQGIVSYGLK--DRASPRAYTKVTSFLPWIKKT 242
Cdd:cd00190   159 YSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGcaRPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 4.80e-88

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: 260.69  E-value: 4.80e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777   20 EIIGGHEAKPHSRPYMAHLWIQNREVCskCGGFLIQEKFVLTAAHCWG----SSINVTLGAHNIKKQEKtQQIIPVRRAI 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHF--CGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777   96 PHPDYNPKNYSNDIMLLQLVKKAKLTAAVRPLGLPKGKDRVRPGQVCSVAGWGRVA--TGRYPDTLQEVELIVQEDQECK 173
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSegAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168437777  174 SRFPNYYNH-KTQLCVGDPKEKKSSFQGDSGGPLLCNN---VAQGIVSYGLK--DRASPRAYTKVTSFLPWI 239
Cdd:smart00020 158 RAYSGGGAItDNMLCAGGLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGcaRPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 3.44e-78

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.41  E-value: 3.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  21 IIGGHEAKPHSRPYMAHLwiQNREVCSKCGGFLIQEKFVLTAAHCW--GSSINVTLGAHNIKKQEKTQQIIPVRRAIPHP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL--QLSSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  99 DYNPKNYSNDIMLLQLVKKAKLTAAVRPLGLPKGKDRVRPGQVCSVAGWGRVATGRYPDTLQEVELIVQEDQECKSRFPN 178
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168437777 179 YYNhKTQLCVGDpkEKKSSFQGDSGGPLLCNNV-AQGIVSYGLK--DRASPRAYTKVTSFLPWI 239
Cdd:pfam00089 159 TVT-DTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGcaSGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-246 4.39e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 180.23  E-value: 4.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  13 PSRAKAGEIIGGHEAKPHSRPYMAHLWIQNREVCSKCGGFLIQEKFVLTAAHC----WGSSINVTLGAHNIKKQEktQQI 88
Cdd:COG5640    23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSG--GTV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  89 IPVRRAIPHPDYNPKNYSNDIMLLQLVKKAKltaAVRPLGLPKGKDRVRPGQVCSVAGWGRVAT--GRYPDTLQEVELIV 166
Cdd:COG5640   101 VKVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgpGSQSGTLRKADVPV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777 167 QEDQECKSrfPNYYNHKTQLCVGDPKEKKSSFQGDSGGPLL----CNNVAQGIVSYGLKDRA--SPRAYTKVTSFLPWIK 240
Cdd:COG5640   178 VSDATCAA--YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAagYPGVYTRVSAYRDWIK 255

                  ....*.
gi 2168437777 241 KTMRGL 246
Cdd:COG5640   256 STAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-242 2.56e-92

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: 271.46  E-value: 2.56e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  21 IIGGHEAKPHSRPYMAHLWIQNREVCskCGGFLIQEKFVLTAAHCWGSS----INVTLGAHNIKKQEKTQQIIPVRRAIP 96
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHF--CGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  97 HPDYNPKNYSNDIMLLQLVKKAKLTAAVRPLGLPKGKDRVRPGQVCSVAGWGRVA-TGRYPDTLQEVELIVQEDQECKSR 175
Cdd:cd00190    79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168437777 176 FPNYYN-HKTQLCVGDPKEKKSSFQGDSGGPLLCN----NVAQGIVSYGLK--DRASPRAYTKVTSFLPWIKKT 242
Cdd:cd00190   159 YSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGcaRPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 4.80e-88

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: 260.69  E-value: 4.80e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777   20 EIIGGHEAKPHSRPYMAHLWIQNREVCskCGGFLIQEKFVLTAAHCWG----SSINVTLGAHNIKKQEKtQQIIPVRRAI 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHF--CGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777   96 PHPDYNPKNYSNDIMLLQLVKKAKLTAAVRPLGLPKGKDRVRPGQVCSVAGWGRVA--TGRYPDTLQEVELIVQEDQECK 173
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSegAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168437777  174 SRFPNYYNH-KTQLCVGDPKEKKSSFQGDSGGPLLCNN---VAQGIVSYGLK--DRASPRAYTKVTSFLPWI 239
Cdd:smart00020 158 RAYSGGGAItDNMLCAGGLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGcaRPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 3.44e-78

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.41  E-value: 3.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  21 IIGGHEAKPHSRPYMAHLwiQNREVCSKCGGFLIQEKFVLTAAHCW--GSSINVTLGAHNIKKQEKTQQIIPVRRAIPHP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL--QLSSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  99 DYNPKNYSNDIMLLQLVKKAKLTAAVRPLGLPKGKDRVRPGQVCSVAGWGRVATGRYPDTLQEVELIVQEDQECKSRFPN 178
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168437777 179 YYNhKTQLCVGDpkEKKSSFQGDSGGPLLCNNV-AQGIVSYGLK--DRASPRAYTKVTSFLPWI 239
Cdd:pfam00089 159 TVT-DTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGcaSGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-246 4.39e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 180.23  E-value: 4.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  13 PSRAKAGEIIGGHEAKPHSRPYMAHLWIQNREVCSKCGGFLIQEKFVLTAAHC----WGSSINVTLGAHNIKKQEktQQI 88
Cdd:COG5640    23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSG--GTV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  89 IPVRRAIPHPDYNPKNYSNDIMLLQLVKKAKltaAVRPLGLPKGKDRVRPGQVCSVAGWGRVAT--GRYPDTLQEVELIV 166
Cdd:COG5640   101 VKVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgpGSQSGTLRKADVPV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777 167 QEDQECKSrfPNYYNHKTQLCVGDPKEKKSSFQGDSGGPLL----CNNVAQGIVSYGLKDRA--SPRAYTKVTSFLPWIK 240
Cdd:COG5640   178 VSDATCAA--YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAagYPGVYTRVSAYRDWIK 255

                  ....*.
gi 2168437777 241 KTMRGL 246
Cdd:COG5640   256 STAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
42-224 4.22e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 51.99  E-value: 4.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777  42 NREVCSkcgGFLIQEKFVLTAAHC--------WGSSINVTLGAHNikkqeKTQQIIPVRRAIPHPDY-NPKNYSNDIMLL 112
Cdd:COG3591    10 GGGVCT---GTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWvASGDAGYDYALL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168437777 113 QLvkKAKLTAAVRPLGLPKGkDRVRPGQVCSVAGwgrvatgrYPDTLQEVeLIVQEDQECKSRFPNYYNHKTQLCvgdpk 192
Cdd:COG3591    82 RL--DEPLGDTTGWLGLAFN-DAPLAGEPVTIIG--------YPGDRPKD-LSLDCSGRVTGVQGNRLSYDCDTT----- 144
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2168437777 193 ekkssfQGDSGGPLL----CNNVAQGIVSYGLKDRA 224
Cdd:COG3591   145 ------GGSSGSPVLddsdGGGRVVGVHSAGGADRA 174
 
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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