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Conserved domains on  [gi|568987694|ref|XP_006519083|]
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granzyme N isoform X1 [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 ...
5-228 6.04e-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: 244.11  E-value: 6.04e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694   5 VIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCIGSS----MTVTLGAHNLRAQEETQQIIPVNKAL 80
Cdd:cd00190    1 IVGGSEAKIGSFPWQ---VSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694  81 PHPDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSiNTTEGSALLEEAELIIQENKECK 160
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTS-EGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987694 161 KQFRHYSKITE--ICAGDPNKIEAPSKGDSGGPLVCNNK----AHGVLSYVKS--KKISSGVFTKVVHFLPWISTN 228
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 ...
5-228 6.04e-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: 244.11  E-value: 6.04e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694   5 VIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCIGSS----MTVTLGAHNLRAQEETQQIIPVNKAL 80
Cdd:cd00190    1 IVGGSEAKIGSFPWQ---VSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694  81 PHPDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSiNTTEGSALLEEAELIIQENKECK 160
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTS-EGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987694 161 KQFRHYSKITE--ICAGDPNKIEAPSKGDSGGPLVCNNK----AHGVLSYVKS--KKISSGVFTKVVHFLPWISTN 228
Cdd:cd00190  157 RAYSYGGTITDnmLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSGcaRPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
4-225 1.40e-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: 1.40e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694     4 EVIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCIG----SSMTVTLGAHNLRaQEETQQIIPVNKA 79
Cdd:smart00020   1 RIVGGSEANIGSFPWQ---VSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLS-SGEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694    80 LPHPDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSINTTEGSALLEEAELIIQENKEC 159
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987694   160 KKQFRHYSKITE--ICAGDPNKIEAPSKGDSGGPLVCNNK---AHGVLSYVKS--KKISSGVFTKVVHFLPWI 225
Cdd:smart00020 157 RRAYSGGGAITDnmLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGcaRPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
5-225 1.19e-67

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 207.68  E-value: 1.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694    5 VIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCI--GSSMTVTLGAHNLRAQEETQQIIPVNKALPH 82
Cdd:pfam00089   1 IVGGDEAQPGSFPWQ---VSLQLSSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694   83 PDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSINTTegSALLEEAELIIQENKECKKQ 162
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP--SDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987694  163 FRHYSKITEICAGDPNKieAPSKGDSGGPLVCNNK-AHGVLSYVKSKKISS--GVFTKVVHFLPWI 225
Cdd:pfam00089 156 YGGTVTDTMICAGAGGK--DACQGDSGGPLVCSDGeLIGIVSWGYGCASGNypGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-232 2.60e-49

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 162.13  E-value: 2.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694   1 MEQEVIGGHEVKPHSRPYMALVVFlkVNG-IGSSCGGFLVQDYFVLTAAHCI----GSSMTVTLGAHNLRAQEEtqQIIP 75
Cdd:COG5640   27 AAPAIVGGTPATVGEYPWMVALQS--SNGpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLSTSGG--TVVK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694  76 VNKALPHPDYNPLDHTNDIMLLKLESKAKGtrdVRPLKLPGPKDKVNPGDVCSVAGWGKTSINTTEGSALLEEAELIIQE 155
Cdd:COG5640  103 VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694 156 NKECkKQFRHYSKITEICAGDPNKIEAPSKGDSGGPLV----CNNKAHGVLSYVKSK--KISSGVFTKVVHFLPWISTNM 229
Cdd:COG5640  180 DATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPcaAGYPGVYTRVSAYRDWIKSTA 258

                 ...
gi 568987694 230 KLL 232
Cdd:COG5640  259 GGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
5-228 6.04e-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: 244.11  E-value: 6.04e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694   5 VIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCIGSS----MTVTLGAHNLRAQEETQQIIPVNKAL 80
Cdd:cd00190    1 IVGGSEAKIGSFPWQ---VSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694  81 PHPDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSiNTTEGSALLEEAELIIQENKECK 160
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTS-EGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987694 161 KQFRHYSKITE--ICAGDPNKIEAPSKGDSGGPLVCNNK----AHGVLSYVKS--KKISSGVFTKVVHFLPWISTN 228
Cdd:cd00190  157 RAYSYGGTITDnmLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSGcaRPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
4-225 1.40e-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: 1.40e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694     4 EVIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCIG----SSMTVTLGAHNLRaQEETQQIIPVNKA 79
Cdd:smart00020   1 RIVGGSEANIGSFPWQ---VSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLS-SGEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694    80 LPHPDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSINTTEGSALLEEAELIIQENKEC 159
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987694   160 KKQFRHYSKITE--ICAGDPNKIEAPSKGDSGGPLVCNNK---AHGVLSYVKS--KKISSGVFTKVVHFLPWI 225
Cdd:smart00020 157 RRAYSGGGAITDnmLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGcaRPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
5-225 1.19e-67

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 207.68  E-value: 1.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694    5 VIGGHEVKPHSRPYMalvVFLKVNGIGSSCGGFLVQDYFVLTAAHCI--GSSMTVTLGAHNLRAQEETQQIIPVNKALPH 82
Cdd:pfam00089   1 IVGGDEAQPGSFPWQ---VSLQLSSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694   83 PDYNPLDHTNDIMLLKLESKAKGTRDVRPLKLPGPKDKVNPGDVCSVAGWGKTSINTTegSALLEEAELIIQENKECKKQ 162
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP--SDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987694  163 FRHYSKITEICAGDPNKieAPSKGDSGGPLVCNNK-AHGVLSYVKSKKISS--GVFTKVVHFLPWI 225
Cdd:pfam00089 156 YGGTVTDTMICAGAGGK--DACQGDSGGPLVCSDGeLIGIVSWGYGCASGNypGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-232 2.60e-49

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 162.13  E-value: 2.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694   1 MEQEVIGGHEVKPHSRPYMALVVFlkVNG-IGSSCGGFLVQDYFVLTAAHCI----GSSMTVTLGAHNLRAQEEtqQIIP 75
Cdd:COG5640   27 AAPAIVGGTPATVGEYPWMVALQS--SNGpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLSTSGG--TVVK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694  76 VNKALPHPDYNPLDHTNDIMLLKLESKAKGtrdVRPLKLPGPKDKVNPGDVCSVAGWGKTSINTTEGSALLEEAELIIQE 155
Cdd:COG5640  103 VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694 156 NKECkKQFRHYSKITEICAGDPNKIEAPSKGDSGGPLV----CNNKAHGVLSYVKSK--KISSGVFTKVVHFLPWISTNM 229
Cdd:COG5640  180 DATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPcaAGYPGVYTRVSAYRDWIKSTA 258

                 ...
gi 568987694 230 KLL 232
Cdd:COG5640  259 GGL 261
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
36-193 4.57e-06

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 45.10  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694   36 GFLV-QDYFVLTAAHCIGSSMTVTLGAHNLRAQEETQQIIPVNKAlphpdynplDHTNDIMLLKLEskaKGTRDVRPLKL 114
Cdd:pfam13365   3 GFVVsSDGLVLTNAHVVDDAEEAAVELVSVVLADGREYPATVVAR---------DPDLDLALLRVS---GDGRGLPPLPL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694  115 pGPKDKVNPGDVCSVAG--WGKTSINTTEGsalleeaelIIQENKECKKQFRHYSKITEICagdpnkieAPSKGDSGGPL 192
Cdd:pfam13365  71 -GDSEPLVGGERVYAVGypLGGEKLSLSEG---------IVSGVDEGRDGGDDGRVIQTDA--------ALSPGSSGGPV 132

                  .
gi 568987694  193 V 193
Cdd:pfam13365 133 F 133
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
22-143 1.34e-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: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987694  22 VVFLKVNGIGSSCGGFLVQDYFVLTAAHCIGS--------SMTVTLGAHNLRAQEETqqiipVNKALPHPDY-NPLDHTN 92
Cdd:COG3591    2 VGRLETDGGGGVCTGTLIGPNLVLTAGHCVYDgagggwatNIVFVPGYNGGPYGTAT-----ATRFRVPPGWvASGDAGY 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987694  93 DIMLLKLESKAKGTR---DVRPLKLPGPKDKVN----PGD---------VCSVAGWGKTSI----NTTEGS 143
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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