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Conserved domains on  [gi|23346543|ref|NP_694692|]
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granzyme N isoform 2 precursor [Mus musculus]

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 ...
21-244 9.34e-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: 244.49  E-value: 9.34e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543  21 VIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCIGSS----MTVTLGAHNLRAQEETQQIIPVNKAL 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQ---VSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543  97 PHPDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSiNTTEGSALLEEAELIIQENKECK 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTS-EGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23346543 177 KQFRHYSKITE--ICAGDPNKIEAPSKGDSGGPLVCNNK----AHGVLSYVKS--KKISSGVFTKVVHFLPWISTN 244
Cdd:cd00190 157 RAYSYGGTITDnmLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSGcaRPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-244 9.34e-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: 244.49  E-value: 9.34e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543  21 VIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCIGSS----MTVTLGAHNLRAQEETQQIIPVNKAL 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQ---VSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543  97 PHPDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSiNTTEGSALLEEAELIIQENKECK 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTS-EGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23346543 177 KQFRHYSKITE--ICAGDPNKIEAPSKGDSGGPLVCNNK----AHGVLSYVKS--KKISSGVFTKVVHFLPWISTN 244
Cdd:cd00190 157 RAYSYGGTITDnmLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSGcaRPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-241 2.46e-80

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: 240.66  E-value: 2.46e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543     20 EVIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCIG----SSMTVTLGAHNLRaQEETQQIIPVNKA 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQ---VSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLS-SGEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543     96 LPHPDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSINTTEGSALLEEAELIIQENKEC 175
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23346543    176 KKQFRHYSKITE--ICAGDPNKIEAPSKGDSGGPLVCNNK---AHGVLSYVKS--KKISSGVFTKVVHFLPWI 241
Cdd:smart00020 157 RRAYSGGGAITDnmLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGcaRPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-241 2.22e-67

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 207.29  E-value: 2.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543    21 VIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCI--GSSMTVTLGAHNLRAQEETQQIIPVNKALPH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQ---VSLQLSSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543    99 PDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSINTTegSALLEEAELIIQENKECKKQ 178
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP--SDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23346543   179 FRHYSKITEICAGDPNKieAPSKGDSGGPLVCNNK-AHGVLSYVKSKKISS--GVFTKVVHFLPWI 241
Cdd:pfam00089 156 YGGTVTDTMICAGAGGK--DACQGDSGGPLVCSDGeLIGIVSWGYGCASGNypGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-248 2.99e-50

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 165.21  E-value: 2.99e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543   1 MLPVLILLIFLL-----PVGDGAEEVIGGHEVKPHSRPYMALVVFlkVNG-IGSSCGGFLVQDYFVLTAAHCI----GSS 70
Cdd:COG5640   6 LLAALAAAALALalaaaPAADAAPAIVGGTPATVGEYPWMVALQS--SNGpSGQFCGGTLIAPRWVLTAAHCVdgdgPSD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543  71 MTVTLGAHNLRAQEEtqQIIPVNKALPHPDYNPLDHTNDIMLLKLESKAKGtrdVRPLKLPGPKDKVNPGDVCSVAGWGK 150
Cdd:COG5640  84 LRVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543 151 TSINTTEGSALLEEAELIIQENKECkKQFRHYSKITEICAGDPNKIEAPSKGDSGGPLV----CNNKAHGVLSYVKSK-- 224
Cdd:COG5640 159 TSEGPGSQSGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPca 237
                       250       260
                ....*....|....*....|....
gi 23346543 225 KISSGVFTKVVHFLPWISTNMKLL 248
Cdd:COG5640 238 AGYPGVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-244 9.34e-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: 244.49  E-value: 9.34e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543  21 VIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCIGSS----MTVTLGAHNLRAQEETQQIIPVNKAL 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQ---VSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543  97 PHPDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSiNTTEGSALLEEAELIIQENKECK 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTS-EGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23346543 177 KQFRHYSKITE--ICAGDPNKIEAPSKGDSGGPLVCNNK----AHGVLSYVKS--KKISSGVFTKVVHFLPWISTN 244
Cdd:cd00190 157 RAYSYGGTITDnmLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSGcaRPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-241 2.46e-80

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: 240.66  E-value: 2.46e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543     20 EVIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCIG----SSMTVTLGAHNLRaQEETQQIIPVNKA 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQ---VSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLS-SGEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543     96 LPHPDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSINTTEGSALLEEAELIIQENKEC 175
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23346543    176 KKQFRHYSKITE--ICAGDPNKIEAPSKGDSGGPLVCNNK---AHGVLSYVKS--KKISSGVFTKVVHFLPWI 241
Cdd:smart00020 157 RRAYSGGGAITDnmLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGcaRPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-241 2.22e-67

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 207.29  E-value: 2.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543    21 VIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCI--GSSMTVTLGAHNLRAQEETQQIIPVNKALPH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQ---VSLQLSSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543    99 PDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSINTTegSALLEEAELIIQENKECKKQ 178
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP--SDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23346543   179 FRHYSKITEICAGDPNKieAPSKGDSGGPLVCNNK-AHGVLSYVKSKKISS--GVFTKVVHFLPWI 241
Cdd:pfam00089 156 YGGTVTDTMICAGAGGK--DACQGDSGGPLVCSDGeLIGIVSWGYGCASGNypGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-248 2.99e-50

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 165.21  E-value: 2.99e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543   1 MLPVLILLIFLL-----PVGDGAEEVIGGHEVKPHSRPYMALVVFlkVNG-IGSSCGGFLVQDYFVLTAAHCI----GSS 70
Cdd:COG5640   6 LLAALAAAALALalaaaPAADAAPAIVGGTPATVGEYPWMVALQS--SNGpSGQFCGGTLIAPRWVLTAAHCVdgdgPSD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543  71 MTVTLGAHNLRAQEEtqQIIPVNKALPHPDYNPLDHTNDIMLLKLESKAKGtrdVRPLKLPGPKDKVNPGDVCSVAGWGK 150
Cdd:COG5640  84 LRVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543 151 TSINTTEGSALLEEAELIIQENKECkKQFRHYSKITEICAGDPNKIEAPSKGDSGGPLV----CNNKAHGVLSYVKSK-- 224
Cdd:COG5640 159 TSEGPGSQSGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPca 237
                       250       260
                ....*....|....*....|....
gi 23346543 225 KISSGVFTKVVHFLPWISTNMKLL 248
Cdd:COG5640 238 AGYPGVYTRVSAYRDWIKSTAGGL 261
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
52-209 1.23e-05

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 43.95  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543    52 GFLV-QDYFVLTAAHCIGSSMTVTLGAHNLRAQEETQQIIPVNKAlphpdynplDHTNDIMLLKLEskaKGTRDVRPLKL 130
Cdd:pfam13365   3 GFVVsSDGLVLTNAHVVDDAEEAAVELVSVVLADGREYPATVVAR---------DPDLDLALLRVS---GDGRGLPPLPL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543   131 pGPKDKVNPGDVCSVAG--WGKTSINTTEGsalleeaelIIQENKECKKQFRHYSKITEICagdpnkieAPSKGDSGGPL 208
Cdd:pfam13365  71 -GDSEPLVGGERVYAVGypLGGEKLSLSEG---------IVSGVDEGRDGGDDGRVIQTDA--------ALSPGSSGGPV 132

                  .
gi 23346543   209 V 209
Cdd:pfam13365 133 F 133
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
38-159 1.52e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 41.59  E-value: 1.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346543  38 VVFLKVNGIGSSCGGFLVQDYFVLTAAHCIGS--------SMTVTLGAHNLRAQEETqqiipVNKALPHPDY-NPLDHTN 108
Cdd:COG3591   2 VGRLETDGGGGVCTGTLIGPNLVLTAGHCVYDgagggwatNIVFVPGYNGGPYGTAT-----ATRFRVPPGWvASGDAGY 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23346543 109 DIMLLKLESKAKGTR---DVRPLKLPGPKDKVN----PGD---------VCSVAGWGKTSI----NTTEGS 159
Cdd:COG3591  77 DYALLRLDEPLGDTTgwlGLAFNDAPLAGEPVTiigyPGDrpkdlsldcSGRVTGVQGNRLsydcDTTGGS 147
 
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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