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Conserved domains on  [gi|4504235|ref|NP_002095|]
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granzyme K precursor [Homo sapiens]

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 ...
27-257 5.53e-92

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: 271.07  E-value: 5.53e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235   27 IIGGKEVSPHSRPFMASIQYG-GHHVCGGVLIDPQWVLTAAHCQYRFTKGQSpTVVLGAHSLSKNEASKQTLEIKKFIPF 105
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNY-TVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235  106 SRVTSDPQSNDIMLVKLQTAAKLNKHVKMLHI-RSKTSLRSGTKCKVTGWGATDPDSlRPSDTLREVTVTVLSRKLCNSq 184
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLpSSGYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKR- 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504235  185 sYYNGDPFITKDMVCAGDAKGQKDSCKGDSGGPLICK----GVFHAIVSGGHECGVATKPGIYTLLTkKYQTWIKSN 257
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 ...
27-257 5.53e-92

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: 271.07  E-value: 5.53e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235   27 IIGGKEVSPHSRPFMASIQYG-GHHVCGGVLIDPQWVLTAAHCQYRFTKGQSpTVVLGAHSLSKNEASKQTLEIKKFIPF 105
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNY-TVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235  106 SRVTSDPQSNDIMLVKLQTAAKLNKHVKMLHI-RSKTSLRSGTKCKVTGWGATDPDSlRPSDTLREVTVTVLSRKLCNSq 184
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLpSSGYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKR- 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504235  185 sYYNGDPFITKDMVCAGDAKGQKDSCKGDSGGPLICK----GVFHAIVSGGHECGVATKPGIYTLLTkKYQTWIKSN 257
Cdd:cd00190 158 -AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVS-SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-254 1.74e-88

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: 262.23  E-value: 1.74e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235      26 EIIGGKEVSPHSRPFMASIQY-GGHHVCGGVLIDPQWVLTAAHCQYRFTKgQSPTVVLGAHSLSKNEaSKQTLEIKKFIP 104
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSDP-SNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235     105 ---FSRVTSDpqsNDIMLVKLQTAAKLNKHVKMLHI-RSKTSLRSGTKCKVTGWGATDPDSLRPSDTLREVTVTVLSRKL 180
Cdd:smart00020  79 hpnYNPSTYD---NDIALLKLKEPVTLSDNVRPICLpSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504235     181 CNSqsYYNGDPFITKDMVCAGDAKGQKDSCKGDSGGPLICK---GVFHAIVSGGHECGVATKPGIYTLLTkKYQTWI 254
Cdd:smart00020 156 CRR--AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVS-SYLDWI 229
Trypsin pfam00089
Trypsin;
27-254 1.57e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 218.85  E-value: 1.57e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235     27 IIGGKEVSPHSRPFMASIQY-GGHHVCGGVLIDPQWVLTAAHCqyrFTKGQSPTVVLGAHSLSKNEASKQTLEIKKFIPF 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235    106 SRVTSDPQSNDIMLVKLQTAAKLNKHVKMLHIRSKTSLRS-GTKCKVTGWGATdpDSLRPSDTLREVTVTVLSRKLCNSQ 184
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPvGTTCTVSGWGNT--KTLGPSDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504235    185 syYNGDpfITKDMVCAGDakGQKDSCKGDSGGPLICKGVF-HAIVSGGHECGVATKPGIYTLLTkKYQTWI 254
Cdd:pfam00089 156 --YGGT--VTDTMICAGA--GGKDACQGDSGGPLVCSDGElIGIVSWGYGCASGNYPGVYTPVS-SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
27-256 5.98e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 192.94  E-value: 5.98e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235   27 IIGGKEVSPHSRPFMASIQYGG---HHVCGGVLIDPQWVLTAAHCQYRFTKGqSPTVVLGAHSLSKNEAskQTLEIKKFI 103
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVVIGSTDLSTSGG--TVVKVARIV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235  104 PFSRVTSDPQSNDIMLVKLQTAAKLNKHVKMLhiRSKTSLRSGTKCKVTGWGATDPDSLRPSDTLREVTVTVLSRKLCNS 183
Cdd:COG5640 108 VHPDYDPATPGNDIALLKLATPVPGVAPAPLA--TSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCAA 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504235  184 QSYYNGDpfitkDMVCAGDAKGQKDSCKGDSGGPLI----CKGVFHAIVSGGHECGVATKPGIYTLLTkKYQTWIKS 256
Cdd:COG5640 186 YGGFDGG-----TMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVS-AYRDWIKS 256
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-257 5.53e-92

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: 271.07  E-value: 5.53e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235   27 IIGGKEVSPHSRPFMASIQYG-GHHVCGGVLIDPQWVLTAAHCQYRFTKGQSpTVVLGAHSLSKNEASKQTLEIKKFIPF 105
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNY-TVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235  106 SRVTSDPQSNDIMLVKLQTAAKLNKHVKMLHI-RSKTSLRSGTKCKVTGWGATDPDSlRPSDTLREVTVTVLSRKLCNSq 184
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLpSSGYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKR- 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504235  185 sYYNGDPFITKDMVCAGDAKGQKDSCKGDSGGPLICK----GVFHAIVSGGHECGVATKPGIYTLLTkKYQTWIKSN 257
Cdd:cd00190 158 -AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVS-SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-254 1.74e-88

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: 262.23  E-value: 1.74e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235      26 EIIGGKEVSPHSRPFMASIQY-GGHHVCGGVLIDPQWVLTAAHCQYRFTKgQSPTVVLGAHSLSKNEaSKQTLEIKKFIP 104
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSDP-SNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235     105 ---FSRVTSDpqsNDIMLVKLQTAAKLNKHVKMLHI-RSKTSLRSGTKCKVTGWGATDPDSLRPSDTLREVTVTVLSRKL 180
Cdd:smart00020  79 hpnYNPSTYD---NDIALLKLKEPVTLSDNVRPICLpSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504235     181 CNSqsYYNGDPFITKDMVCAGDAKGQKDSCKGDSGGPLICK---GVFHAIVSGGHECGVATKPGIYTLLTkKYQTWI 254
Cdd:smart00020 156 CRR--AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVS-SYLDWI 229
Trypsin pfam00089
Trypsin;
27-254 1.57e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 218.85  E-value: 1.57e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235     27 IIGGKEVSPHSRPFMASIQY-GGHHVCGGVLIDPQWVLTAAHCqyrFTKGQSPTVVLGAHSLSKNEASKQTLEIKKFIPF 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235    106 SRVTSDPQSNDIMLVKLQTAAKLNKHVKMLHIRSKTSLRS-GTKCKVTGWGATdpDSLRPSDTLREVTVTVLSRKLCNSQ 184
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPvGTTCTVSGWGNT--KTLGPSDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504235    185 syYNGDpfITKDMVCAGDakGQKDSCKGDSGGPLICKGVF-HAIVSGGHECGVATKPGIYTLLTkKYQTWI 254
Cdd:pfam00089 156 --YGGT--VTDTMICAGA--GGKDACQGDSGGPLVCSDGElIGIVSWGYGCASGNYPGVYTPVS-SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
27-256 5.98e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 192.94  E-value: 5.98e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235   27 IIGGKEVSPHSRPFMASIQYGG---HHVCGGVLIDPQWVLTAAHCQYRFTKGqSPTVVLGAHSLSKNEAskQTLEIKKFI 103
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVVIGSTDLSTSGG--TVVKVARIV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235  104 PFSRVTSDPQSNDIMLVKLQTAAKLNKHVKMLhiRSKTSLRSGTKCKVTGWGATDPDSLRPSDTLREVTVTVLSRKLCNS 183
Cdd:COG5640 108 VHPDYDPATPGNDIALLKLATPVPGVAPAPLA--TSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCAA 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504235  184 QSYYNGDpfitkDMVCAGDAKGQKDSCKGDSGGPLI----CKGVFHAIVSGGHECGVATKPGIYTLLTkKYQTWIKS 256
Cdd:COG5640 186 YGGFDGG-----TMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVS-AYRDWIKS 256
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
46-246 1.90e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 55.84  E-value: 1.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235   46 YGGHHVCGGVLIDPQWVLTAAHCQYRFTKGQSPT---VVLGAHSLSKNEASKQTLeikkFIPFSRVTSDPQSNDIMLVKL 122
Cdd:COG3591   8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATnivFVPGYNGGPYGTATATRF----RVPPGWVASGDAGYDYALLRL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235  123 QTAakLNKHVKMLHIRSKTSLRSGTKCKVTGWGATDPD--SLRPSDTLREVTVTVLsrklcnsqsYYNGdpfitkdmvca 200
Cdd:COG3591  84 DEP--LGDTTGWLGLAFNDAPLAGEPVTIIGYPGDRPKdlSLDCSGRVTGVQGNRL---------SYDC----------- 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 4504235  201 gdakgqkDSCKGDSGGPLICK--------GVFHAIVSGGHECGVATKPGIYTLL 246
Cdd:COG3591 142 -------DTTGGSSGSPVLDDsdgggrvvGVHSAGGADRANTGVRLTSAIVAAL 188
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
39-153 3.54e-03

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 36.37  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504235     39 PFMASIQYGGHHVCGGVLIDPQWVLTAAHCQYRFT-KGQSPTVVLGAHSlSKNEASKQTLEIKKFIPFSRVtsdPQSNdI 117
Cdd:pfam09342   2 PWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNlRHQYISVVLGGAK-TLKSIEGPYEQIVRVDCRHDI---PESE-I 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 4504235    118 MLVKLQTAAKLNKHVK-MLHIRSKTSLRSGTKCKVTG 153
Cdd:pfam09342  77 SLLHLASPASFSNHVLpTFVPETRNENEKDNECLAVG 113
 
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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