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Conserved domains on  [gi|6678700|ref|NP_032530|]
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granzyme M isoform 1 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

 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 3.98e-80

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: 241.03  E-value: 3.98e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700   27 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCL-SEPLQNLKLVLGLHNLHDLQDPGLTFYIREAIKHP 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700  105 GYNHK-YENDLALLKLDRRVQPSKNVKPLALPRKpRSKPAEGTWCSTAGWGMTHQGGPRARALQELDLRVLDTQMCNNSR 183
Cdd:cd00190  81 NYNPStYDNDIALLKLKRPVTLSDNVRPICLPSS-GYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678700  184 FWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVC---GKGQVDGILSFSSKtCTDIFKPPVATAVAPYSSWIRKV 254
Cdd:cd00190 160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndnGRGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 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 3.98e-80

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: 241.03  E-value: 3.98e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700   27 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCL-SEPLQNLKLVLGLHNLHDLQDPGLTFYIREAIKHP 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700  105 GYNHK-YENDLALLKLDRRVQPSKNVKPLALPRKpRSKPAEGTWCSTAGWGMTHQGGPRARALQELDLRVLDTQMCNNSR 183
Cdd:cd00190  81 NYNPStYDNDIALLKLKRPVTLSDNVRPICLPSS-GYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678700  184 FWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVC---GKGQVDGILSFSSKtCTDIFKPPVATAVAPYSSWIRKV 254
Cdd:cd00190 160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndnGRGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-251 3.63e-75

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: 228.33  E-value: 3.63e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700      27 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCL-SEPLQNLKLVLGLHNLhDLQDPGLTFYIREAIKHP 104
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVrGSDPSNIRVRLGSHDL-SSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700     105 GYNHK-YENDLALLKLDRRVQPSKNVKPLALPRKPRSkPAEGTWCSTAGWGMTHQG-GPRARALQELDLRVLDTQMCNNS 182
Cdd:smart00020  81 NYNPStYDNDIALLKLKEPVTLSDNVRPICLPSSNYN-VPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678700     183 RFWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVCGK--GQVDGILSFSSKtCTDIFKPPVATAVAPYSSWI 251
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDgrWVLVGIVSWGSG-CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
27-251 9.53e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 219.24  E-value: 9.53e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700     27 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCLSEPlQNLKLVLGLHNLHDLQDPGLTFYIREAIKHPG 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGA-SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700    106 YNHK-YENDLALLKLDRRVQPSKNVKPLALPRKPrSKPAEGTWCSTAGWGMTHQGGPrARALQELDLRVLDTQMCNNSrf 184
Cdd:pfam00089  80 YNPDtLDNDIALLKLESPVTLGDTVRPICLPDAS-SDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSA-- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678700    185 WNGVLIDSMLClkAGSKSQAPCKGDSGGPLVCGKGQVDGILSFsSKTCTDIFKPPVATAVAPYSSWI 251
Cdd:pfam00089 156 YGGTVTDTMIC--AGAGGKDACQGDSGGPLVCSDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-259 1.18e-57

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 184.85  E-value: 1.18e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700   24 ETQIIGGREAVPHSRPYMASLQKAK---SHVCGGVLVHRKWVLTAAHCLSEP-LQNLKLVLGLHNLHDlqDPGLTFYIRE 99
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgPSDLRVVIGSTDLST--SGGTVVKVAR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700  100 AIKHPGYN-HKYENDLALLKLDRrvqPSKNVKPLALPRkPRSKPAEGTWCSTAGWGMT-HQGGPRARALQELDLRVLDTQ 177
Cdd:COG5640 106 IVVHPDYDpATPGNDIALLKLAT---PVPGVAPAPLAT-SADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDA 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700  178 MCNNsrfWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVC---GKGQVDGILSFSSKTCtDIFKPPVATAVAPYSSWIRKV 254
Cdd:COG5640 182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVkdgGGWVLVGVVSWGGGPC-AAGYPGVYTRVSAYRDWIKST 257

                ....*
gi 6678700  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 3.98e-80

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: 241.03  E-value: 3.98e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700   27 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCL-SEPLQNLKLVLGLHNLHDLQDPGLTFYIREAIKHP 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700  105 GYNHK-YENDLALLKLDRRVQPSKNVKPLALPRKpRSKPAEGTWCSTAGWGMTHQGGPRARALQELDLRVLDTQMCNNSR 183
Cdd:cd00190  81 NYNPStYDNDIALLKLKRPVTLSDNVRPICLPSS-GYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678700  184 FWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVC---GKGQVDGILSFSSKtCTDIFKPPVATAVAPYSSWIRKV 254
Cdd:cd00190 160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndnGRGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-251 3.63e-75

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: 228.33  E-value: 3.63e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700      27 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCL-SEPLQNLKLVLGLHNLhDLQDPGLTFYIREAIKHP 104
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVrGSDPSNIRVRLGSHDL-SSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700     105 GYNHK-YENDLALLKLDRRVQPSKNVKPLALPRKPRSkPAEGTWCSTAGWGMTHQG-GPRARALQELDLRVLDTQMCNNS 182
Cdd:smart00020  81 NYNPStYDNDIALLKLKEPVTLSDNVRPICLPSSNYN-VPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678700     183 RFWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVCGK--GQVDGILSFSSKtCTDIFKPPVATAVAPYSSWI 251
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDgrWVLVGIVSWGSG-CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
27-251 9.53e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 219.24  E-value: 9.53e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700     27 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCLSEPlQNLKLVLGLHNLHDLQDPGLTFYIREAIKHPG 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGA-SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700    106 YNHK-YENDLALLKLDRRVQPSKNVKPLALPRKPrSKPAEGTWCSTAGWGMTHQGGPrARALQELDLRVLDTQMCNNSrf 184
Cdd:pfam00089  80 YNPDtLDNDIALLKLESPVTLGDTVRPICLPDAS-SDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSA-- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678700    185 WNGVLIDSMLClkAGSKSQAPCKGDSGGPLVCGKGQVDGILSFsSKTCTDIFKPPVATAVAPYSSWI 251
Cdd:pfam00089 156 YGGTVTDTMIC--AGAGGKDACQGDSGGPLVCSDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-259 1.18e-57

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 184.85  E-value: 1.18e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700   24 ETQIIGGREAVPHSRPYMASLQKAK---SHVCGGVLVHRKWVLTAAHCLSEP-LQNLKLVLGLHNLHDlqDPGLTFYIRE 99
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgPSDLRVVIGSTDLST--SGGTVVKVAR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700  100 AIKHPGYN-HKYENDLALLKLDRrvqPSKNVKPLALPRkPRSKPAEGTWCSTAGWGMT-HQGGPRARALQELDLRVLDTQ 177
Cdd:COG5640 106 IVVHPDYDpATPGNDIALLKLAT---PVPGVAPAPLAT-SADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDA 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700  178 MCNNsrfWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVC---GKGQVDGILSFSSKTCtDIFKPPVATAVAPYSSWIRKV 254
Cdd:COG5640 182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVkdgGGWVLVGVVSWGGGPC-AAGYPGVYTRVSAYRDWIKST 257

                ....*
gi 6678700  255 IGRWS 259
Cdd:COG5640 258 AGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
49-232 9.03e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 59.69  E-value: 9.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700   49 SHVCGGVLVHRKWVLTAAHCLSEP-----LQNLKLVLGLHNlhdlqDPGLTFYIREAIKHPGY--NHKYENDLALLKLDR 121
Cdd:COG3591  11 GGVCTGTLIGPNLVLTAGHCVYDGagggwATNIVFVPGYNG-----GPYGTATATRFRVPPGWvaSGDAGYDYALLRLDE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700  122 RVQPSknVKPLALprKPRSKPAEGTWCSTAGWGmthQGGPRARALQElDLRVLDTQmcnnsrfwNGVLidSMLClkagsk 201
Cdd:COG3591  86 PLGDT--TGWLGL--AFNDAPLAGEPVTIIGYP---GDRPKDLSLDC-SGRVTGVQ--------GNRL--SYDC------ 141
                       170       180       190
                ....*....|....*....|....*....|....
gi 6678700  202 sqAPCKGDSGGPL---VCGKGQVDGILSFSSKTC 232
Cdd:COG3591 142 --DTTGGSSGSPVlddSDGGGRVVGVHSAGGADR 173
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
54-224 1.02e-05

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 44.33  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700     54 GVLV-HRKWVLTAAHCLSEPlqnlklvlglhnlHDLQDPGLTFYIREAIKHPGYNHKY--ENDLALLKLDrrvQPSKNVK 130
Cdd:pfam13365   3 GFVVsSDGLVLTNAHVVDDA-------------EEAAVELVSVVLADGREYPATVVARdpDLDLALLRVS---GDGRGLP 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678700    131 PLALprKPRSKPAEGTWCSTAGWGmthQGGPRaralqeldLRVLDTQMCNNSRFWNGVLIDSMLCLKAgsksqAPCKGDS 210
Cdd:pfam13365  67 PLPL--GDSEPLVGGERVYAVGYP---LGGEK--------LSLSEGIVSGVDEGRDGGDDGRVIQTDA-----ALSPGSS 128
                         170
                  ....*....|....
gi 6678700    211 GGPLVCGKGQVDGI 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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