NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1519315262|ref|NP_006135|]
View 

granzyme A precursor [Homo sapiens]

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

show extra options »

Show site features     Horizontal zoom: ×

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 ...
29-254 1.64e-86

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: 257.20  E-value: 1.64e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262  29 IIGGNEVTPHSRPYMVLLSLDRKT-ICAGALIAKDWVLTAAHCNLN---KRSQVILGAHSITREEPTKQIMLVKKEFPYP 104
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSsapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262 105 CYDPATREGDLKLLQLMEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASWSDTLREVNITIIDRKVCNDrnH 184
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR--A 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519315262 185 YNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE----GVFRGVTSFGLEnkCGDPRGPGVYILLSkKHLNWI 254
Cdd:cd00190   159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG--CARPNYPGVYTRVS-SYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
29-254 1.64e-86

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: 257.20  E-value: 1.64e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262  29 IIGGNEVTPHSRPYMVLLSLDRKT-ICAGALIAKDWVLTAAHCNLN---KRSQVILGAHSITREEPTKQIMLVKKEFPYP 104
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSsapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262 105 CYDPATREGDLKLLQLMEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASWSDTLREVNITIIDRKVCNDrnH 184
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR--A 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519315262 185 YNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE----GVFRGVTSFGLEnkCGDPRGPGVYILLSkKHLNWI 254
Cdd:cd00190   159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG--CARPNYPGVYTRVS-SYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-254 2.20e-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: 244.12  E-value: 2.20e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262   28 KIIGGNEVTPHSRPYMVLLSLDRKT-ICAGALIAKDWVLTAAHC---NLNKRSQVILGAHSITREEPtKQIMLVKKEFPY 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCvrgSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262  104 PCYDPATREGDLKLLQLMEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSA-SWSDTLREVNITIIDRKVCndR 182
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAgSLPDTLQEVNVPIVSNATC--R 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519315262  183 NHYNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE---GVFRGVTSFGleNKCGDPRGPGVYILLSkKHLNWI 254
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWG--SGCARPGKPGVYTRVS-SYLDWI 229
Trypsin pfam00089
Trypsin;
29-254 8.35e-67

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 206.52  E-value: 8.35e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262  29 IIGGNEVTPHSRPYMVLLSL-DRKTICAGALIAKDWVLTAAHCNLNKRS-QVILGAHSITREEPTKQIMLVKKEFPYPCY 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDvKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262 107 DPATREGDLKLLQLMEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASwSDTLREVNITIIDRKVCNDRnhyn 186
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSA---- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519315262 187 FNPVIGMNMVCAGSlrGGRDSCNGDSGSPLLCEGVF-RGVTSFGleNKCGDPRGPGVYILLSkKHLNWI 254
Cdd:pfam00089 156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGElIGIVSWG--YGCASGNYPGVYTPVS-SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
22-254 3.74e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 175.61  E-value: 3.74e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262  22 PEDVCEKIIGGNEVTPHSRPYMVLLSLD---RKTICAGALIAKDWVLTAAHC---NLNKRSQVILGAHSITREEPTKqiM 95
Cdd:COG5640    24 AADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCvdgDGPSDLRVVIGSTDLSTSGGTV--V 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262  96 LVKKEFPYPCYDPATREGDLKLLQLMEKAKINKYVTilhLPKKGDDVKPGTMCQVAGWGRT-HNSASWSDTLREVNITII 174
Cdd:COG5640   102 KVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262 175 DRKVCNDRNHYNFNpvigmNMVCAGSLRGGRDSCNGDSGSPLL--CEGVFR--GVTSFGlENKCGdPRGPGVYILLSkKH 250
Cdd:COG5640   179 SDATCAAYGGFDGG-----TMLCAGYPEGGKDACQGDSGGPLVvkDGGGWVlvGVVSWG-GGPCA-AGYPGVYTRVS-AY 250

                  ....
gi 1519315262 251 LNWI 254
Cdd:COG5640   251 RDWI 254
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
29-254 1.64e-86

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: 257.20  E-value: 1.64e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262  29 IIGGNEVTPHSRPYMVLLSLDRKT-ICAGALIAKDWVLTAAHCNLN---KRSQVILGAHSITREEPTKQIMLVKKEFPYP 104
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSsapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262 105 CYDPATREGDLKLLQLMEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASWSDTLREVNITIIDRKVCNDrnH 184
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR--A 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519315262 185 YNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE----GVFRGVTSFGLEnkCGDPRGPGVYILLSkKHLNWI 254
Cdd:cd00190   159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG--CARPNYPGVYTRVS-SYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-254 2.20e-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: 244.12  E-value: 2.20e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262   28 KIIGGNEVTPHSRPYMVLLSLDRKT-ICAGALIAKDWVLTAAHC---NLNKRSQVILGAHSITREEPtKQIMLVKKEFPY 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCvrgSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262  104 PCYDPATREGDLKLLQLMEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSA-SWSDTLREVNITIIDRKVCndR 182
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAgSLPDTLQEVNVPIVSNATC--R 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519315262  183 NHYNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE---GVFRGVTSFGleNKCGDPRGPGVYILLSkKHLNWI 254
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWG--SGCARPGKPGVYTRVS-SYLDWI 229
Trypsin pfam00089
Trypsin;
29-254 8.35e-67

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 206.52  E-value: 8.35e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262  29 IIGGNEVTPHSRPYMVLLSL-DRKTICAGALIAKDWVLTAAHCNLNKRS-QVILGAHSITREEPTKQIMLVKKEFPYPCY 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDvKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262 107 DPATREGDLKLLQLMEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASwSDTLREVNITIIDRKVCNDRnhyn 186
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSA---- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519315262 187 FNPVIGMNMVCAGSlrGGRDSCNGDSGSPLLCEGVF-RGVTSFGleNKCGDPRGPGVYILLSkKHLNWI 254
Cdd:pfam00089 156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGElIGIVSWG--YGCASGNYPGVYTPVS-SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
22-254 3.74e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 175.61  E-value: 3.74e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262  22 PEDVCEKIIGGNEVTPHSRPYMVLLSLD---RKTICAGALIAKDWVLTAAHC---NLNKRSQVILGAHSITREEPTKqiM 95
Cdd:COG5640    24 AADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCvdgDGPSDLRVVIGSTDLSTSGGTV--V 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262  96 LVKKEFPYPCYDPATREGDLKLLQLMEKAKINKYVTilhLPKKGDDVKPGTMCQVAGWGRT-HNSASWSDTLREVNITII 174
Cdd:COG5640   102 KVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315262 175 DRKVCNDRNHYNFNpvigmNMVCAGSLRGGRDSCNGDSGSPLL--CEGVFR--GVTSFGlENKCGdPRGPGVYILLSkKH 250
Cdd:COG5640   179 SDATCAAYGGFDGG-----TMLCAGYPEGGKDACQGDSGGPLVvkDGGGWVlvGVVSWG-GGPCA-AGYPGVYTRVS-AY 250

                  ....
gi 1519315262 251 LNWI 254
Cdd:COG5640   251 RDWI 254
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
45-70 7.03e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 39.66  E-value: 7.03e-04
                          10        20
                  ....*....|....*....|....*.
gi 1519315262  45 LLSLDRKTICAGALIAKDWVLTAAHC 70
Cdd:COG3591     5 LETDGGGGVCTGTLIGPNLVLTAGHC 30
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH