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Conserved domains on  [gi|6754102|ref|NP_034500|]
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granzyme A precursor [Mus musculus]

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 ...
28-252 9.54e-82

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: 244.89  E-value: 9.54e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102      28 RIIGGDTVVPHSRPYMALLKLSSNT-ICAGALIEKNWVLTAAHCNVGKRSKFI---LGAHSINKEPEQQILTVKKAFPYP 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGSDPSNIrvrLGSHDLSSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102     104 CYDEYTREGDLQLVRLKKKATVNRNVAILHLPKKGDDVKPGTRCRVAGWGR-FGNKSAPSETLREVNITVIDRKICNdeK 182
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLQEVNVPIVSNATCR--R 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6754102     183 HYNFHPVIGLNMICAGDLRGGKDSCNGDSGSPLLCD---GILRGITSFgGEKCGDRRWPGVYTFLSdKHLNWI 252
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSW-GSGCARPGKPGVYTRVS-SYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-252 9.54e-82

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: 244.89  E-value: 9.54e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102      28 RIIGGDTVVPHSRPYMALLKLSSNT-ICAGALIEKNWVLTAAHCNVGKRSKFI---LGAHSINKEPEQQILTVKKAFPYP 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGSDPSNIrvrLGSHDLSSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102     104 CYDEYTREGDLQLVRLKKKATVNRNVAILHLPKKGDDVKPGTRCRVAGWGR-FGNKSAPSETLREVNITVIDRKICNdeK 182
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLQEVNVPIVSNATCR--R 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6754102     183 HYNFHPVIGLNMICAGDLRGGKDSCNGDSGSPLLCD---GILRGITSFgGEKCGDRRWPGVYTFLSdKHLNWI 252
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSW-GSGCARPGKPGVYTRVS-SYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
29-255 5.77e-81

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: 242.95  E-value: 5.77e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102   29 IIGGDTVVPHSRPYMALLKLSSNT-ICAGALIEKNWVLTAAHCNVGKRSKFI---LGAHSINK-EPEQQILTVKKAFPYP 103
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSNYtvrLGSHDLSSnEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102  104 CYDEYTREGDLQLVRLKKKATVNRNVAILHLPKKGDDVKPGTRCRVAGWGRFGNKSAPSETLREVNITVIDRKICNdeKH 183
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK--RA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6754102  184 YNFHPVIGLNMICAGDLRGGKDSCNGDSGSPLLCD----GILRGITSFgGEKCGDRRWPGVYTFLSdKHLNWIKKI 255
Cdd:cd00190 159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSW-GSGCARPNYPGVYTRVS-SYLDWIQKT 232
Trypsin pfam00089
Trypsin;
29-252 4.52e-62

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 194.20  E-value: 4.52e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102     29 IIGGDTVVPHSRPYMALLKLSSNT-ICAGALIEKNWVLTAAHCNVGKRS-KFILGAHSINK-EPEQQILTVKKAFPYPCY 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKhFCGGSLISENWVLTAAHCVSGASDvKVVLGAHNIVLrEGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102    106 DEYTREGDLQLVRLKKKATVNRNVAILHLPKKGDDVKPGTRCRVAGWGRfGNKSAPSETLREVNITVIDRKICNdeKHYN 185
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGN-TKTLGPSDTLQEVTVPVVSRETCR--SAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6754102    186 fhPVIGLNMICAGDlrGGKDSCNGDSGSPLLC-DGILRGITSFgGEKCGDRRWPGVYTfLSDKHLNWI 252
Cdd:pfam00089 158 --GTVTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSW-GYGCASGNYPGVYT-PVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
21-258 2.22e-23

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 97.64  E-value: 2.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102   21 IPEGGCERIIGGDTVVPHSRPYM-ALLK----LSSNTICAGALIEKNWVLTAAHCNVGK---RSKFILGAHSINKEPEQQ 92
Cdd:COG5640  25 TADEVSSRIIGGSNANAGEYPSLvALVDrisdYVSGTFCGGSKLGGRYVLTAAHCADASspiSSDVNRVVVDLNDSSQAE 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102   93 ILTVKKAFPYPCYDEYTREGDLQLVRLKKKATVNRNVAILHLPKKG--DDVKPGTRCRVAGWGR----FGNKSAPSET-L 165
Cdd:COG5640 105 RGHVRTIYVHEFYSPGNLGNDIAVLELARAASLPRVKITSFDASDTflNSVTTVSPMTNGTFGVttpsDVPRSSPKGTiL 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102  166 REVNITVIDRKIC----NDEKHYNFHPviGLNMICAGdlRGGKDSCNGDSGSPLLCDG----ILRGITSFGGEKCGDRRW 237
Cdd:COG5640 185 HEVAVLFVPLSTCaqykGCANASDGAT--GLTGFCAG--RPPKDACQGDSGGPIFHKGeegrVQRGVVSWGDGGCGGTLI 260
                       250       260
                ....*....|....*....|.
gi 6754102  238 PGVYTFLSDkHLNWIKKIMKG 258
Cdd:COG5640 261 PGVYTNVSN-YQDWIAAMTNG 280
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-252 9.54e-82

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: 244.89  E-value: 9.54e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102      28 RIIGGDTVVPHSRPYMALLKLSSNT-ICAGALIEKNWVLTAAHCNVGKRSKFI---LGAHSINKEPEQQILTVKKAFPYP 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGSDPSNIrvrLGSHDLSSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102     104 CYDEYTREGDLQLVRLKKKATVNRNVAILHLPKKGDDVKPGTRCRVAGWGR-FGNKSAPSETLREVNITVIDRKICNdeK 182
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLQEVNVPIVSNATCR--R 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6754102     183 HYNFHPVIGLNMICAGDLRGGKDSCNGDSGSPLLCD---GILRGITSFgGEKCGDRRWPGVYTFLSdKHLNWI 252
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSW-GSGCARPGKPGVYTRVS-SYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
29-255 5.77e-81

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: 242.95  E-value: 5.77e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102   29 IIGGDTVVPHSRPYMALLKLSSNT-ICAGALIEKNWVLTAAHCNVGKRSKFI---LGAHSINK-EPEQQILTVKKAFPYP 103
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSNYtvrLGSHDLSSnEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102  104 CYDEYTREGDLQLVRLKKKATVNRNVAILHLPKKGDDVKPGTRCRVAGWGRFGNKSAPSETLREVNITVIDRKICNdeKH 183
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK--RA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6754102  184 YNFHPVIGLNMICAGDLRGGKDSCNGDSGSPLLCD----GILRGITSFgGEKCGDRRWPGVYTFLSdKHLNWIKKI 255
Cdd:cd00190 159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSW-GSGCARPNYPGVYTRVS-SYLDWIQKT 232
Trypsin pfam00089
Trypsin;
29-252 4.52e-62

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 194.20  E-value: 4.52e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102     29 IIGGDTVVPHSRPYMALLKLSSNT-ICAGALIEKNWVLTAAHCNVGKRS-KFILGAHSINK-EPEQQILTVKKAFPYPCY 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKhFCGGSLISENWVLTAAHCVSGASDvKVVLGAHNIVLrEGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102    106 DEYTREGDLQLVRLKKKATVNRNVAILHLPKKGDDVKPGTRCRVAGWGRfGNKSAPSETLREVNITVIDRKICNdeKHYN 185
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGN-TKTLGPSDTLQEVTVPVVSRETCR--SAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6754102    186 fhPVIGLNMICAGDlrGGKDSCNGDSGSPLLC-DGILRGITSFgGEKCGDRRWPGVYTfLSDKHLNWI 252
Cdd:pfam00089 158 --GTVTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSW-GYGCASGNYPGVYT-PVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
21-258 2.22e-23

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 97.64  E-value: 2.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102   21 IPEGGCERIIGGDTVVPHSRPYM-ALLK----LSSNTICAGALIEKNWVLTAAHCNVGK---RSKFILGAHSINKEPEQQ 92
Cdd:COG5640  25 TADEVSSRIIGGSNANAGEYPSLvALVDrisdYVSGTFCGGSKLGGRYVLTAAHCADASspiSSDVNRVVVDLNDSSQAE 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102   93 ILTVKKAFPYPCYDEYTREGDLQLVRLKKKATVNRNVAILHLPKKG--DDVKPGTRCRVAGWGR----FGNKSAPSET-L 165
Cdd:COG5640 105 RGHVRTIYVHEFYSPGNLGNDIAVLELARAASLPRVKITSFDASDTflNSVTTVSPMTNGTFGVttpsDVPRSSPKGTiL 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102  166 REVNITVIDRKIC----NDEKHYNFHPviGLNMICAGdlRGGKDSCNGDSGSPLLCDG----ILRGITSFGGEKCGDRRW 237
Cdd:COG5640 185 HEVAVLFVPLSTCaqykGCANASDGAT--GLTGFCAG--RPPKDACQGDSGGPIFHKGeegrVQRGVVSWGDGGCGGTLI 260
                       250       260
                ....*....|....*....|.
gi 6754102  238 PGVYTFLSDkHLNWIKKIMKG 258
Cdd:COG5640 261 PGVYTNVSN-YQDWIAAMTNG 280
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
41-151 1.10e-03

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 37.91  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754102     41 PYMALLKLSSNTICAGALIEKNWVLTAAHC--NVGKRSKFI---LGAHSINKE---PEQQILTVKkafpypCYdEYTREG 112
Cdd:pfam09342   2 PWIAKVYLDGNMICSGVLIDASWVIVSGSClrDTNLRHQYIsvvLGGAKTLKSiegPYEQIVRVD------CR-HDIPES 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 6754102    113 DLQLVRLKKKATVNRNVAILHLPKKGDDVKPGTRCRVAG 151
Cdd:pfam09342  75 EISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
 
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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