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Conserved domains on  [gi|133778024|gb|AAI17982|]
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Gzmk protein, partial [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 ...
25-255 1.88e-91

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: 269.53  E-value: 1.88e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024  25 IIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHC-YSWFPRGHspTVVLGAHSLSKNEPMKQTFEIKKFIP 102
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCvYSSAPSNY--TVRLGSHDLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024 103 FSRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKNY-LRDGTKCQVTGWGTTKPDLlTASDTLREVTVTIISRKRCNS 181
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133778024 182 qsYYNHKPVITKDMICAGDARGQKDSCKGDSGGPLICK----GIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWIKSK 255
Cdd:cd00190  158 --AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVS-SYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-255 1.88e-91

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: 269.53  E-value: 1.88e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024  25 IIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHC-YSWFPRGHspTVVLGAHSLSKNEPMKQTFEIKKFIP 102
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCvYSSAPSNY--TVRLGSHDLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024 103 FSRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKNY-LRDGTKCQVTGWGTTKPDLlTASDTLREVTVTIISRKRCNS 181
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133778024 182 qsYYNHKPVITKDMICAGDARGQKDSCKGDSGGPLICK----GIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWIKSK 255
Cdd:cd00190  158 --AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVS-SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-252 9.57e-91

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: 267.62  E-value: 9.57e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024    24 EIIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHCYsWFPRGHSPTVVLGAHSLSKNEPmKQTFEIKKFIP 102
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024   103 FSRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKNY-LRDGTKCQVTGWGTTKPDLLTASDTLREVTVTIISRKRCNS 181
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 133778024   182 QSYYNHkpVITKDMICAGDARGQKDSCKGDSGGPLICK---GIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWI 252
Cdd:smart00020 159 AYSGGG--AITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVS-SYLDWI 229
Trypsin pfam00089
Trypsin;
25-252 3.66e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.10  E-value: 3.66e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024   25 IIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHCYSwfpRGHSPTVVLGAHSLSKNEPMKQTFEIKKFIPF 103
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024  104 SRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKN-YLRDGTKCQVTGWGTTKPDllTASDTLREVTVTIISRKRCNSQ 182
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASsDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133778024  183 syynHKPVITKDMICAGDarGQKDSCKGDSGGPLIC-KGIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWI 252
Cdd:pfam00089 156 ----YGGTVTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNYPGVYTPVS-SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-257 8.69e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 187.55  E-value: 8.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024  23 TEIIGGREVQPHSRPFMASIQYRS---KHICGGVLIHPQWVLTAAHCYSwfprGHSP---TVVLGAHSLSKNEPmkQTFE 96
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD----GDGPsdlRVVIGSTDLSTSGG--TVVK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024  97 IKKFIPFSRLQSGSASHDIMLIKLRTAAELNKNVQLlhLGSKNYLRDGTKCQVTGWGTTKPDLLTASDTLREVTVTIISR 176
Cdd:COG5640  103 VARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPL--ATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSD 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024 177 KRCNSQSYYnhkpvITKDMICAGDARGQKDSCKGDSGGPLI----CKGIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWI 252
Cdd:COG5640  181 ATCAAYGGF-----DGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVS-AYRDWI 254

                 ....*
gi 133778024 253 KSKLA 257
Cdd:COG5640  255 KSTAG 259
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-255 1.88e-91

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: 269.53  E-value: 1.88e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024  25 IIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHC-YSWFPRGHspTVVLGAHSLSKNEPMKQTFEIKKFIP 102
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCvYSSAPSNY--TVRLGSHDLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024 103 FSRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKNY-LRDGTKCQVTGWGTTKPDLlTASDTLREVTVTIISRKRCNS 181
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133778024 182 qsYYNHKPVITKDMICAGDARGQKDSCKGDSGGPLICK----GIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWIKSK 255
Cdd:cd00190  158 --AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVS-SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-252 9.57e-91

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: 267.62  E-value: 9.57e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024    24 EIIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHCYsWFPRGHSPTVVLGAHSLSKNEPmKQTFEIKKFIP 102
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024   103 FSRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKNY-LRDGTKCQVTGWGTTKPDLLTASDTLREVTVTIISRKRCNS 181
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 133778024   182 QSYYNHkpVITKDMICAGDARGQKDSCKGDSGGPLICK---GIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWI 252
Cdd:smart00020 159 AYSGGG--AITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVS-SYLDWI 229
Trypsin pfam00089
Trypsin;
25-252 3.66e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.10  E-value: 3.66e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024   25 IIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHCYSwfpRGHSPTVVLGAHSLSKNEPMKQTFEIKKFIPF 103
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024  104 SRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKN-YLRDGTKCQVTGWGTTKPDllTASDTLREVTVTIISRKRCNSQ 182
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASsDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133778024  183 syynHKPVITKDMICAGDarGQKDSCKGDSGGPLIC-KGIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWI 252
Cdd:pfam00089 156 ----YGGTVTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNYPGVYTPVS-SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-257 8.69e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 187.55  E-value: 8.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024  23 TEIIGGREVQPHSRPFMASIQYRS---KHICGGVLIHPQWVLTAAHCYSwfprGHSP---TVVLGAHSLSKNEPmkQTFE 96
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD----GDGPsdlRVVIGSTDLSTSGG--TVVK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024  97 IKKFIPFSRLQSGSASHDIMLIKLRTAAELNKNVQLlhLGSKNYLRDGTKCQVTGWGTTKPDLLTASDTLREVTVTIISR 176
Cdd:COG5640  103 VARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPL--ATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSD 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024 177 KRCNSQSYYnhkpvITKDMICAGDARGQKDSCKGDSGGPLI----CKGIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWI 252
Cdd:COG5640  181 ATCAAYGGF-----DGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVS-AYRDWI 254

                 ....*
gi 133778024 253 KSKLA 257
Cdd:COG5640  255 KSTAG 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
44-217 3.52e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 49.29  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024  44 YRSKHICGGVLIHPQWVLTAAHCYSWFPRGHSPT---VVLGAHslskNEPMKQTFEIKKFIPFSRLQSGSASHDIMLIKL 120
Cdd:COG3591    8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATnivFVPGYN----GGPYGTATATRFRVPPGWVASGDAGYDYALLRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778024 121 RTAaeLNKNVQLLHLGSKNYLRDGTKCQVTGWGTTKPDLLT--ASDTLREVTVTIIsrkrcnsqsYYNhkpvitkdmiCa 198
Cdd:COG3591   84 DEP--LGDTTGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLSldCSGRVTGVQGNRL---------SYD----------C- 141
                        170
                 ....*....|....*....
gi 133778024 199 gdargqkDSCKGDSGGPLI 217
Cdd:COG3591  142 -------DTTGGSSGSPVL 153
 
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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