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Conserved domains on  [gi|6680143|ref|NP_032222|]
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granzyme K precursor [Mus musculus]

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

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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 ...
26-256 1.39e-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: 269.92  E-value: 1.39e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143   26 IIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHC-YSWFPRGHspTVVLGAHSLSKNEPMKQTFEIKKFIP 103
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCvYSSAPSNY--TVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143  104 FSRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKNY-LRDGTKCQVTGWGTTKPDLlTASDTLREVTVTIISRKRCNS 182
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6680143  183 qsYYNHKPVITKDMICAGDARGQKDSCKGDSGGPLICK----GIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWIKSK 256
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 ...
26-256 1.39e-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: 269.92  E-value: 1.39e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143   26 IIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHC-YSWFPRGHspTVVLGAHSLSKNEPMKQTFEIKKFIP 103
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCvYSSAPSNY--TVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143  104 FSRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKNY-LRDGTKCQVTGWGTTKPDLlTASDTLREVTVTIISRKRCNS 182
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6680143  183 qsYYNHKPVITKDMICAGDARGQKDSCKGDSGGPLICK----GIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWIKSK 256
Cdd:cd00190 158 --AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVS-SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
25-253 6.63e-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: 268.01  E-value: 6.63e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143      25 EIIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHCYsWFPRGHSPTVVLGAHSLSKNEPmKQTFEIKKFIP 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143     104 FSRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKNY-LRDGTKCQVTGWGTTKPDLLTASDTLREVTVTIISRKRCNS 182
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6680143     183 QSYYNHkpVITKDMICAGDARGQKDSCKGDSGGPLICK---GIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWI 253
Cdd:smart00020 159 AYSGGG--AITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVS-SYLDWI 229
Trypsin pfam00089
Trypsin;
26-253 2.20e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.49  E-value: 2.20e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143     26 IIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHCYSwfpRGHSPTVVLGAHSLSKNEPMKQTFEIKKFIPF 104
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143    105 SRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKN-YLRDGTKCQVTGWGTTKPDllTASDTLREVTVTIISRKRCNSQ 183
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASsDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680143    184 syynHKPVITKDMICAGDarGQKDSCKGDSGGPLIC-KGIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWI 253
Cdd:pfam00089 156 ----YGGTVTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNYPGVYTPVS-SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-258 7.08e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 187.93  E-value: 7.08e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143   24 TEIIGGREVQPHSRPFMASIQYRS---KHICGGVLIHPQWVLTAAHCYSwfprGHSP---TVVLGAHSLSKNEPmkQTFE 97
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD----GDGPsdlRVVIGSTDLSTSGG--TVVK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143   98 IKKFIPFSRLQSGSASHDIMLIKLRTAAELNKNVQLlhLGSKNYLRDGTKCQVTGWGTTKPDLLTASDTLREVTVTIISR 177
Cdd:COG5640 103 VARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPL--ATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSD 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143  178 KRCNSQSYYnhkpvITKDMICAGDARGQKDSCKGDSGGPLI----CKGIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWI 253
Cdd:COG5640 181 ATCAAYGGF-----DGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVS-AYRDWI 254

                ....*
gi 6680143  254 KSKLA 258
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 ...
26-256 1.39e-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: 269.92  E-value: 1.39e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143   26 IIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHC-YSWFPRGHspTVVLGAHSLSKNEPMKQTFEIKKFIP 103
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCvYSSAPSNY--TVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143  104 FSRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKNY-LRDGTKCQVTGWGTTKPDLlTASDTLREVTVTIISRKRCNS 182
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6680143  183 qsYYNHKPVITKDMICAGDARGQKDSCKGDSGGPLICK----GIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWIKSK 256
Cdd:cd00190 158 --AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVS-SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
25-253 6.63e-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: 268.01  E-value: 6.63e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143      25 EIIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHCYsWFPRGHSPTVVLGAHSLSKNEPmKQTFEIKKFIP 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143     104 FSRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKNY-LRDGTKCQVTGWGTTKPDLLTASDTLREVTVTIISRKRCNS 182
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6680143     183 QSYYNHkpVITKDMICAGDARGQKDSCKGDSGGPLICK---GIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWI 253
Cdd:smart00020 159 AYSGGG--AITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVS-SYLDWI 229
Trypsin pfam00089
Trypsin;
26-253 2.20e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.49  E-value: 2.20e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143     26 IIGGREVQPHSRPFMASIQYRS-KHICGGVLIHPQWVLTAAHCYSwfpRGHSPTVVLGAHSLSKNEPMKQTFEIKKFIPF 104
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143    105 SRLQSGSASHDIMLIKLRTAAELNKNVQLLHLGSKN-YLRDGTKCQVTGWGTTKPDllTASDTLREVTVTIISRKRCNSQ 183
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASsDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680143    184 syynHKPVITKDMICAGDarGQKDSCKGDSGGPLIC-KGIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWI 253
Cdd:pfam00089 156 ----YGGTVTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNYPGVYTPVS-SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-258 7.08e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 187.93  E-value: 7.08e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143   24 TEIIGGREVQPHSRPFMASIQYRS---KHICGGVLIHPQWVLTAAHCYSwfprGHSP---TVVLGAHSLSKNEPmkQTFE 97
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD----GDGPsdlRVVIGSTDLSTSGG--TVVK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143   98 IKKFIPFSRLQSGSASHDIMLIKLRTAAELNKNVQLlhLGSKNYLRDGTKCQVTGWGTTKPDLLTASDTLREVTVTIISR 177
Cdd:COG5640 103 VARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPL--ATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSD 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143  178 KRCNSQSYYnhkpvITKDMICAGDARGQKDSCKGDSGGPLI----CKGIFHALVSQGYKCGIAKKPGIYTLLTkKYQTWI 253
Cdd:COG5640 181 ATCAAYGGF-----DGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVS-AYRDWI 254

                ....*
gi 6680143  254 KSKLA 258
Cdd:COG5640 255 KSTAG 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
45-218 2.98e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 49.67  E-value: 2.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143   45 YRSKHICGGVLIHPQWVLTAAHCYSWFPRGHSPT---VVLGAHslskNEPMKQTFEIKKFIPFSRLQSGSASHDIMLIKL 121
Cdd:COG3591   8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATnivFVPGYN----GGPYGTATATRFRVPPGWVASGDAGYDYALLRL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680143  122 RTAaeLNKNVQLLHLGSKNYLRDGTKCQVTGWGTTKPDLLT--ASDTLREVTVTIIsrkrcnsqsYYNhkpvitkdmiCa 199
Cdd:COG3591  84 DEP--LGDTTGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLSldCSGRVTGVQGNRL---------SYD----------C- 141
                       170
                ....*....|....*....
gi 6680143  200 gdargqkDSCKGDSGGPLI 218
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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