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Conserved domains on  [gi|114600290|ref|XP_001148261|]
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granzyme A [Pan troglodytes]

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

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 ...
29-254 2.11e-89

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: 264.52  E-value: 2.11e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290  29 IIGGNEVTPHSRPYMVLLSLDRKN-ICAGALIAKDWVLTAAHCNLN---KRSQVILGAHSITREEPTKQIMLVKKEFPYP 104
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSsapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290 105 CYDPDTREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASRSDTLREVNITIIDRKVCNDqnH 184
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR--A 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114600290 185 YNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE----GVFRGVTSFGLEnkCGDPRGPGVYTLLSkKHLNWI 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 2.11e-89

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: 264.52  E-value: 2.11e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290  29 IIGGNEVTPHSRPYMVLLSLDRKN-ICAGALIAKDWVLTAAHCNLN---KRSQVILGAHSITREEPTKQIMLVKKEFPYP 104
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSsapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290 105 CYDPDTREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASRSDTLREVNITIIDRKVCNDqnH 184
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR--A 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114600290 185 YNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE----GVFRGVTSFGLEnkCGDPRGPGVYTLLSkKHLNWI 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 5.39e-84

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: 250.67  E-value: 5.39e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290    28 KIIGGNEVTPHSRPYMV-LLSLDRKNICAGALIAKDWVLTAAHC---NLNKRSQVILGAHSITREEPtKQIMLVKKEFPY 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVsLQYGGGRHFCGGSLISPRWVLTAAHCvrgSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290   104 PCYDPDTREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSA-SRSDTLREVNITIIDRKVCNDq 182
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAgSLPDTLQEVNVPIVSNATCRR- 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114600290   183 nHYNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE---GVFRGVTSFGleNKCGDPRGPGVYTLLSkKHLNWI 254
Cdd:smart00020 159 -AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWG--SGCARPGKPGVYTRVS-SYLDWI 229
Trypsin pfam00089
Trypsin;
29-254 1.38e-68

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 211.15  E-value: 1.38e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290   29 IIGGNEVTPHSRPYMVLLSL-DRKNICAGALIAKDWVLTAAHCNLNKRS-QVILGAHSITREEPTKQIMLVKKEFPYPCY 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDvKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290  107 DPDTREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSaSRSDTLREVNITIIDRKVCNDQnhyn 186
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL-GPSDTLQEVTVPVVSRETCRSA---- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114600290  187 FNPVIGMNMVCAGSlrGGRDSCNGDSGSPLLCEGVF-RGVTSFGleNKCGDPRGPGVYTLLSkKHLNWI 254
Cdd:pfam00089 156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGElIGIVSWG--YGCASGNYPGVYTPVS-SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
22-254 6.94e-57

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 182.54  E-value: 6.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290  22 PEDVCEKIIGGNEVTPHSRPYMVLLSLD---RKNICAGALIAKDWVLTAAHC---NLNKRSQVILGAHSITREEPTKqiM 95
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCvdgDGPSDLRVVIGSTDLSTSGGTV--V 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290  96 LVKKEFPYPCYDPDTREGDLKLLQLTEKAKINKYVTilhLPKKGDDVKPGTMCQVAGWGRT-HNSASRSDTLREVNITII 174
Cdd:COG5640  102 KVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVV 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290 175 DRKVCNDQNHYNFNpvigmNMVCAGSLRGGRDSCNGDSGSPLL--CEGVFR--GVTSFGlENKCGdPRGPGVYTLLSkKH 250
Cdd:COG5640  179 SDATCAAYGGFDGG-----TMLCAGYPEGGKDACQGDSGGPLVvkDGGGWVlvGVVSWG-GGPCA-AGYPGVYTRVS-AY 250

                 ....
gi 114600290 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 2.11e-89

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: 264.52  E-value: 2.11e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290  29 IIGGNEVTPHSRPYMVLLSLDRKN-ICAGALIAKDWVLTAAHCNLN---KRSQVILGAHSITREEPTKQIMLVKKEFPYP 104
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSsapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290 105 CYDPDTREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASRSDTLREVNITIIDRKVCNDqnH 184
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR--A 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114600290 185 YNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE----GVFRGVTSFGLEnkCGDPRGPGVYTLLSkKHLNWI 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 5.39e-84

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: 250.67  E-value: 5.39e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290    28 KIIGGNEVTPHSRPYMV-LLSLDRKNICAGALIAKDWVLTAAHC---NLNKRSQVILGAHSITREEPtKQIMLVKKEFPY 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVsLQYGGGRHFCGGSLISPRWVLTAAHCvrgSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290   104 PCYDPDTREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSA-SRSDTLREVNITIIDRKVCNDq 182
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAgSLPDTLQEVNVPIVSNATCRR- 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114600290   183 nHYNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE---GVFRGVTSFGleNKCGDPRGPGVYTLLSkKHLNWI 254
Cdd:smart00020 159 -AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWG--SGCARPGKPGVYTRVS-SYLDWI 229
Trypsin pfam00089
Trypsin;
29-254 1.38e-68

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 211.15  E-value: 1.38e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290   29 IIGGNEVTPHSRPYMVLLSL-DRKNICAGALIAKDWVLTAAHCNLNKRS-QVILGAHSITREEPTKQIMLVKKEFPYPCY 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDvKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290  107 DPDTREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSaSRSDTLREVNITIIDRKVCNDQnhyn 186
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL-GPSDTLQEVTVPVVSRETCRSA---- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114600290  187 FNPVIGMNMVCAGSlrGGRDSCNGDSGSPLLCEGVF-RGVTSFGleNKCGDPRGPGVYTLLSkKHLNWI 254
Cdd:pfam00089 156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGElIGIVSWG--YGCASGNYPGVYTPVS-SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
22-254 6.94e-57

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 182.54  E-value: 6.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290  22 PEDVCEKIIGGNEVTPHSRPYMVLLSLD---RKNICAGALIAKDWVLTAAHC---NLNKRSQVILGAHSITREEPTKqiM 95
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCvdgDGPSDLRVVIGSTDLSTSGGTV--V 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290  96 LVKKEFPYPCYDPDTREGDLKLLQLTEKAKINKYVTilhLPKKGDDVKPGTMCQVAGWGRT-HNSASRSDTLREVNITII 174
Cdd:COG5640  102 KVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVV 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114600290 175 DRKVCNDQNHYNFNpvigmNMVCAGSLRGGRDSCNGDSGSPLL--CEGVFR--GVTSFGlENKCGdPRGPGVYTLLSkKH 250
Cdd:COG5640  179 SDATCAAYGGFDGG-----TMLCAGYPEGGKDACQGDSGGPLVvkDGGGWVlvGVVSWG-GGPCA-AGYPGVYTRVS-AY 250

                 ....
gi 114600290 251 LNWI 254
Cdd:COG5640  251 RDWI 254
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
45-70 3.73e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 40.43  E-value: 3.73e-04
                         10        20
                 ....*....|....*....|....*.
gi 114600290  45 LLSLDRKNICAGALIAKDWVLTAAHC 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.
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