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Conserved domains on  [gi|296176|emb|CAA48624|]
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granzyme-like protein II [Rattus norvegicus]

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

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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 ...
21-241 4.50e-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 [Multi-domain]  Cd Length: 232  Bit Score: 245.26  E-value: 4.50e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176    21 IIWGTESKPHSRPYMAFIKFYDSNsepHHCGGFLVAKDIVMTAAHC----NGRNIKVTLGAHNIKKQENT-QVISVVKAK 95
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGgQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176    96 PHENYDRDSHFNDIMLLKLERKAQLNGVVKTIALPRSQDWVKPGQVCTVAGWGRLANC-TSSNTLQEVNLEVQKGQKCQD 174
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGgPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296176   175 MSEDYN--DSIQLCVGNPSEGKATGKGDSGGPFVCD----GVAQGIVSYRL-CTGT-LPRVFTRISSFIPWIQKT 241
Cdd:cd00190 158 AYSYGGtiTDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSgCARPnYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-241 4.50e-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 [Multi-domain]  Cd Length: 232  Bit Score: 245.26  E-value: 4.50e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176    21 IIWGTESKPHSRPYMAFIKFYDSNsepHHCGGFLVAKDIVMTAAHC----NGRNIKVTLGAHNIKKQENT-QVISVVKAK 95
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGgQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176    96 PHENYDRDSHFNDIMLLKLERKAQLNGVVKTIALPRSQDWVKPGQVCTVAGWGRLANC-TSSNTLQEVNLEVQKGQKCQD 174
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGgPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296176   175 MSEDYN--DSIQLCVGNPSEGKATGKGDSGGPFVCD----GVAQGIVSYRL-CTGT-LPRVFTRISSFIPWIQKT 241
Cdd:cd00190 158 AYSYGGtiTDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSgCARPnYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-238 3.42e-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: 242.97  E-value: 3.42e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176       20 EIIWGTESKPHSRPYMAFIKFydsNSEPHHCGGFLVAKDIVMTAAHC----NGRNIKVTLGAHNIKKQENTQVISVVKAK 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176       96 PHENYDRDSHFNDIMLLKLERKAQLNGVVKTIALPRSQDWVKPGQVCTVAGWGRLANC--TSSNTLQEVNLEVQKGQKCQ 173
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGagSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296176      174 DMSEDYN--DSIQLCVGNPSEGKATGKGDSGGPFVCD---GVAQGIVSYRL-CT-GTLPRVFTRISSFIPWI 238
Cdd:smart00020 158 RAYSGGGaiTDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSgCArPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-238 3.82e-65

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 201.90  E-value: 3.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176      21 IIWGTESKPHSRPYMAFIKFydsNSEPHHCGGFLVAKDIVMTAAHC--NGRNIKVTLGAHNIKKQE-NTQVISVVKAKPH 97
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREgGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176      98 ENYDRDSHFNDIMLLKLERKAQLNGVVKTIALPRSQDWVKPGQVCTVAGWGRLANCTSSNTLQEVNLEVQKGQKCQDMSE 177
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296176     178 DYNDSIQLCVGnpSEGKATGKGDSGGPFVC-DGVAQGIVSY-RLCTGTL-PRVFTRISSFIPWI 238
Cdd:pfam00089 158 GTVTDTMICAG--AGGKDACQGDSGGPLVCsDGELIGIVSWgYGCASGNyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
3-245 1.14e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 181.39  E-value: 1.14e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176     3 LFLFFLVAILPVNTEGGEIIWGTESKPHSRPYMAFIkFYDSNSEPHHCGGFLVAKDIVMTAAHC----NGRNIKVTLGAH 78
Cdd:COG5640  13 AALALALAAAPAADAAPAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGST 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176    79 NIKKQEnTQVISVVKAKPHENYDRDSHFNDIMLLKLERKAQLngvVKTIALPRSQDWVKPGQVCTVAGWGRLANC--TSS 156
Cdd:COG5640  92 DLSTSG-GTVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGpgSQS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176   157 NTLQEVNLEVQKGQKCQDMSeDYNDSIQLCVGNPSEGKATGKGDSGGPFV--CDGVAQ--GIVSY--RLCTGTLPRVFTR 230
Cdd:COG5640 168 GTLRKADVPVVSDATCAAYG-GFDGGTMLCAGYPEGGKDACQGDSGGPLVvkDGGGWVlvGVVSWggGPCAAGYPGVYTR 246
                       250
                ....*....|....*
gi 296176   231 ISSFIPWIQKTMKVL 245
Cdd:COG5640 247 VSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-241 4.50e-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 [Multi-domain]  Cd Length: 232  Bit Score: 245.26  E-value: 4.50e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176    21 IIWGTESKPHSRPYMAFIKFYDSNsepHHCGGFLVAKDIVMTAAHC----NGRNIKVTLGAHNIKKQENT-QVISVVKAK 95
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGgQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176    96 PHENYDRDSHFNDIMLLKLERKAQLNGVVKTIALPRSQDWVKPGQVCTVAGWGRLANC-TSSNTLQEVNLEVQKGQKCQD 174
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGgPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296176   175 MSEDYN--DSIQLCVGNPSEGKATGKGDSGGPFVCD----GVAQGIVSYRL-CTGT-LPRVFTRISSFIPWIQKT 241
Cdd:cd00190 158 AYSYGGtiTDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSgCARPnYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-238 3.42e-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: 242.97  E-value: 3.42e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176       20 EIIWGTESKPHSRPYMAFIKFydsNSEPHHCGGFLVAKDIVMTAAHC----NGRNIKVTLGAHNIKKQENTQVISVVKAK 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176       96 PHENYDRDSHFNDIMLLKLERKAQLNGVVKTIALPRSQDWVKPGQVCTVAGWGRLANC--TSSNTLQEVNLEVQKGQKCQ 173
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGagSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296176      174 DMSEDYN--DSIQLCVGNPSEGKATGKGDSGGPFVCD---GVAQGIVSYRL-CT-GTLPRVFTRISSFIPWI 238
Cdd:smart00020 158 RAYSGGGaiTDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSgCArPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-238 3.82e-65

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 201.90  E-value: 3.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176      21 IIWGTESKPHSRPYMAFIKFydsNSEPHHCGGFLVAKDIVMTAAHC--NGRNIKVTLGAHNIKKQE-NTQVISVVKAKPH 97
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREgGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176      98 ENYDRDSHFNDIMLLKLERKAQLNGVVKTIALPRSQDWVKPGQVCTVAGWGRLANCTSSNTLQEVNLEVQKGQKCQDMSE 177
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296176     178 DYNDSIQLCVGnpSEGKATGKGDSGGPFVC-DGVAQGIVSY-RLCTGTL-PRVFTRISSFIPWI 238
Cdd:pfam00089 158 GTVTDTMICAG--AGGKDACQGDSGGPLVCsDGELIGIVSWgYGCASGNyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
3-245 1.14e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 181.39  E-value: 1.14e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176     3 LFLFFLVAILPVNTEGGEIIWGTESKPHSRPYMAFIkFYDSNSEPHHCGGFLVAKDIVMTAAHC----NGRNIKVTLGAH 78
Cdd:COG5640  13 AALALALAAAPAADAAPAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGST 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176    79 NIKKQEnTQVISVVKAKPHENYDRDSHFNDIMLLKLERKAQLngvVKTIALPRSQDWVKPGQVCTVAGWGRLANC--TSS 156
Cdd:COG5640  92 DLSTSG-GTVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGpgSQS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176   157 NTLQEVNLEVQKGQKCQDMSeDYNDSIQLCVGNPSEGKATGKGDSGGPFV--CDGVAQ--GIVSY--RLCTGTLPRVFTR 230
Cdd:COG5640 168 GTLRKADVPVVSDATCAAYG-GFDGGTMLCAGYPEGGKDACQGDSGGPLVvkDGGGWVlvGVVSWggGPCAAGYPGVYTR 246
                       250
                ....*....|....*
gi 296176   231 ISSFIPWIQKTMKVL 245
Cdd:COG5640 247 VSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
42-149 3.40e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 46.21  E-value: 3.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296176    42 DSNSEPHHCGGFLVAKDIVMTAAHC-----NGR---NIKVTLGAHNikkqENTQVISVVKAKPHENYDRDSHFN-DIMLL 112
Cdd:COG3591   6 ETDGGGGVCTGTLIGPNLVLTAGHCvydgaGGGwatNIVFVPGYNG----GPYGTATATRFRVPPGWVASGDAGyDYALL 81
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 296176   113 KLERKaqLNGVVKTIALPRSQDWVkPGQVCTVAGWGR 149
Cdd:COG3591  82 RLDEP--LGDTTGWLGLAFNDAPL-AGEPVTIIGYPG 115
 
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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