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Conserved domains on  [gi|158262012|ref|NP_476531|]
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granzyme M precursor [Rattus norvegicus]

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

 Zoom to residue level

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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 ...
27-254 8.30e-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: 245.26  E-value: 8.30e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012  27 IIGGREAVPHSRPYMVSLQNTK-SHVCGGVLVHQKWVLTAAHCL-SEPLQQLKLVFGLHSLHDPQDPGLTFYIKQAIKHP 104
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012 105 GYNLK-YENDLALLKLDGRVKPSKNVKPLALPRKPRDkPAEGSRCSTAGWGITHQRGQLAKSLQELDLRLLDTRMCNNSR 183
Cdd:cd00190   81 NYNPStYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-LPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262012 184 FWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVC---GKGKVDGILSFSSkNCTDIFKPTVATAVAPYSSWIRKV 254
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndnGRGVLVGIVSWGS-GCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-254 8.30e-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: 245.26  E-value: 8.30e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012  27 IIGGREAVPHSRPYMVSLQNTK-SHVCGGVLVHQKWVLTAAHCL-SEPLQQLKLVFGLHSLHDPQDPGLTFYIKQAIKHP 104
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012 105 GYNLK-YENDLALLKLDGRVKPSKNVKPLALPRKPRDkPAEGSRCSTAGWGITHQRGQLAKSLQELDLRLLDTRMCNNSR 183
Cdd:cd00190   81 NYNPStYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-LPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262012 184 FWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVC---GKGKVDGILSFSSkNCTDIFKPTVATAVAPYSSWIRKV 254
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndnGRGVLVGIVSWGS-GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-251 2.61e-77

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: 233.72  E-value: 2.61e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012    27 IIGGREAVPHSRPYMVSLQNTK-SHVCGGVLVHQKWVLTAAHCL-SEPLQQLKLVFGLHSLHDPQDpGLTFYIKQAIKHP 104
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVrGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012   105 GYNLK-YENDLALLKLDGRVKPSKNVKPLALPRKpRDKPAEGSRCSTAGWGITHQR-GQLAKSLQELDLRLLDTRMCNNS 182
Cdd:smart00020  81 NYNPStYDNDIALLKLKEPVTLSDNVRPICLPSS-NYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262012   183 RFWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVCGKGK--VDGILSFSSkNCTDIFKPTVATAVAPYSSWI 251
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRwvLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
27-251 1.45e-76

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.56  E-value: 1.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012   27 IIGGREAVPHSRPYMVSLQN-TKSHVCGGVLVHQKWVLTAAHCLSEPlQQLKLVFGLHSLHDPQDPGLTFYIKQAIKHPG 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGA-SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012  106 YNLK-YENDLALLKLDGRVKPSKNVKPLALPRKPRDKPAeGSRCSTAGWGITHQRGqLAKSLQELDLRLLDTRMCNNSrf 184
Cdd:pfam00089  80 YNPDtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPV-GTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSA-- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262012  185 WNGVLTDSMLClkAGAKGQAPCKGDSGGPLVCGKGKVDGILSFsSKNCTDIFKPTVATAVAPYSSWI 251
Cdd:pfam00089 156 YGGTVTDTMIC--AGAGGKDACQGDSGGPLVCSDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-259 1.02e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 187.55  E-value: 1.02e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012  24 EAQIIGGREAVPHSRPYMVSLQNTK---SHVCGGVLVHQKWVLTAAHCLSEP-LQQLKLVFGLHSLHDpqDPGLTFYIKQ 99
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgPSDLRVVIGSTDLST--SGGTVVKVAR 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012 100 AIKHPGYNLK-YENDLALLKLDgrvKPSKNVKPLALPRkPRDKPAEGSRCSTAGWGIT-HQRGQLAKSLQELDLRLLDTR 177
Cdd:COG5640  106 IVVHPDYDPAtPGNDIALLKLA---TPVPGVAPAPLAT-SADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012 178 MCNNsrfWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVC---GKGKVDGILSFSSKNCtDIFKPTVATAVAPYSSWIRKV 254
Cdd:COG5640  182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVkdgGGWVLVGVVSWGGGPC-AAGYPGVYTRVSAYRDWIKST 257

                 ....*
gi 158262012 255 IGRWS 259
Cdd:COG5640  258 AGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-254 8.30e-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: 245.26  E-value: 8.30e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012  27 IIGGREAVPHSRPYMVSLQNTK-SHVCGGVLVHQKWVLTAAHCL-SEPLQQLKLVFGLHSLHDPQDPGLTFYIKQAIKHP 104
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012 105 GYNLK-YENDLALLKLDGRVKPSKNVKPLALPRKPRDkPAEGSRCSTAGWGITHQRGQLAKSLQELDLRLLDTRMCNNSR 183
Cdd:cd00190   81 NYNPStYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-LPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262012 184 FWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVC---GKGKVDGILSFSSkNCTDIFKPTVATAVAPYSSWIRKV 254
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndnGRGVLVGIVSWGS-GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-251 2.61e-77

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: 233.72  E-value: 2.61e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012    27 IIGGREAVPHSRPYMVSLQNTK-SHVCGGVLVHQKWVLTAAHCL-SEPLQQLKLVFGLHSLHDPQDpGLTFYIKQAIKHP 104
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVrGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012   105 GYNLK-YENDLALLKLDGRVKPSKNVKPLALPRKpRDKPAEGSRCSTAGWGITHQR-GQLAKSLQELDLRLLDTRMCNNS 182
Cdd:smart00020  81 NYNPStYDNDIALLKLKEPVTLSDNVRPICLPSS-NYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262012   183 RFWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVCGKGK--VDGILSFSSkNCTDIFKPTVATAVAPYSSWI 251
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRwvLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
27-251 1.45e-76

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.56  E-value: 1.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012   27 IIGGREAVPHSRPYMVSLQN-TKSHVCGGVLVHQKWVLTAAHCLSEPlQQLKLVFGLHSLHDPQDPGLTFYIKQAIKHPG 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGA-SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012  106 YNLK-YENDLALLKLDGRVKPSKNVKPLALPRKPRDKPAeGSRCSTAGWGITHQRGqLAKSLQELDLRLLDTRMCNNSrf 184
Cdd:pfam00089  80 YNPDtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPV-GTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSA-- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262012  185 WNGVLTDSMLClkAGAKGQAPCKGDSGGPLVCGKGKVDGILSFsSKNCTDIFKPTVATAVAPYSSWI 251
Cdd:pfam00089 156 YGGTVTDTMIC--AGAGGKDACQGDSGGPLVCSDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-259 1.02e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 187.55  E-value: 1.02e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012  24 EAQIIGGREAVPHSRPYMVSLQNTK---SHVCGGVLVHQKWVLTAAHCLSEP-LQQLKLVFGLHSLHDpqDPGLTFYIKQ 99
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgPSDLRVVIGSTDLST--SGGTVVKVAR 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012 100 AIKHPGYNLK-YENDLALLKLDgrvKPSKNVKPLALPRkPRDKPAEGSRCSTAGWGIT-HQRGQLAKSLQELDLRLLDTR 177
Cdd:COG5640  106 IVVHPDYDPAtPGNDIALLKLA---TPVPGVAPAPLAT-SADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012 178 MCNNsrfWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVC---GKGKVDGILSFSSKNCtDIFKPTVATAVAPYSSWIRKV 254
Cdd:COG5640  182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVkdgGGWVLVGVVSWGGGPC-AAGYPGVYTRVSAYRDWIKST 257

                 ....*
gi 158262012 255 IGRWS 259
Cdd:COG5640  258 AGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
49-252 1.00e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 50.83  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012  49 SHVCGGVLVHQKWVLTAAHCLSEP-----LQQLKLVFGLHslhdpQDPGLTFYIKQAIKHPGY--NLKYENDLALLKLDG 121
Cdd:COG3591   11 GGVCTGTLIGPNLVLTAGHCVYDGagggwATNIVFVPGYN-----GGPYGTATATRFRVPPGWvaSGDAGYDYALLRLDE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012 122 RVKPSknVKPLALprKPRDKPAEGSRCSTAGWGITHqrgQLAKSLQELdlrlldtrmCNNSRFWNGVLtdSMLClkagak 201
Cdd:COG3591   86 PLGDT--TGWLGL--AFNDAPLAGEPVTIIGYPGDR---PKDLSLDCS---------GRVTGVQGNRL--SYDC------ 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 158262012 202 gqAPCKGDSGGPL---VCGKGKVDGILSFSSKNCTDIFKPTVATAVAPYSSWIR 252
Cdd:COG3591  142 --DTTGGSSGSPVlddSDGGGRVVGVHSAGGADRANTGVRLTSAIVAALRAWAS 193
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
54-224 4.05e-06

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 45.49  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012   54 GVLV-HQKWVLTAAHCLSEPlqqlklvfglhslHDPQDPGLTFYIKQAIKHPGYNLKY--ENDLALLKLDGrvkPSKNVK 130
Cdd:pfam13365   3 GFVVsSDGLVLTNAHVVDDA-------------EEAAVELVSVVLADGREYPATVVARdpDLDLALLRVSG---DGRGLP 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262012  131 PLALprKPRDKPAEGSRCSTAGwgitHQRGQLAKSLQEldlrlldTRMCNNSRFWNGVLTDSMLCLKAgakgqAPCKGDS 210
Cdd:pfam13365  67 PLPL--GDSEPLVGGERVYAVG----YPLGGEKLSLSE-------GIVSGVDEGRDGGDDGRVIQTDA-----ALSPGSS 128
                         170
                  ....*....|....
gi 158262012  211 GGPLVCGKGKVDGI 224
Cdd:pfam13365 129 GGPVFDADGRVVGI 142
 
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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