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Conserved domains on  [gi|699114741|ref|NP_001289414|]
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granzyme M isoform 2 precursor [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 ...
26-253 5.82e-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: 240.64  E-value: 5.82e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741  26 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCL-SEPLQNLKLVLGLHNLHDLQDPGLTFYIREAIKHP 103
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741 104 GYNHK-YENDLALLKLDRRVQPSKNVKPLALPRKpRSKPAEGTWCSTAGWGMTHQGGPRARALQELDLRVLDTQMCNNSR 182
Cdd:cd00190   81 NYNPStYDNDIALLKLKRPVTLSDNVRPICLPSS-GYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 699114741 183 FWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVC---GKGQVDGILSFSSKtCTDIFKPPVATAVAPYSSWIRKV 253
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 ...
26-253 5.82e-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: 240.64  E-value: 5.82e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741  26 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCL-SEPLQNLKLVLGLHNLHDLQDPGLTFYIREAIKHP 103
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741 104 GYNHK-YENDLALLKLDRRVQPSKNVKPLALPRKpRSKPAEGTWCSTAGWGMTHQGGPRARALQELDLRVLDTQMCNNSR 182
Cdd:cd00190   81 NYNPStYDNDIALLKLKRPVTLSDNVRPICLPSS-GYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 699114741 183 FWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVC---GKGQVDGILSFSSKtCTDIFKPPVATAVAPYSSWIRKV 253
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndnGRGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-250 5.85e-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: 227.56  E-value: 5.85e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741    26 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCL-SEPLQNLKLVLGLHNLhDLQDPGLTFYIREAIKHP 103
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVrGSDPSNIRVRLGSHDL-SSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741   104 GYNHK-YENDLALLKLDRRVQPSKNVKPLALPRKPRSkPAEGTWCSTAGWGMTHQG-GPRARALQELDLRVLDTQMCNNS 181
Cdd:smart00020  81 NYNPStYDNDIALLKLKEPVTLSDNVRPICLPSSNYN-VPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 699114741   182 RFWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVCGK--GQVDGILSFSSKtCTDIFKPPVATAVAPYSSWI 250
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDgrWVLVGIVSWGSG-CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
26-250 1.24e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 218.85  E-value: 1.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741   26 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCLSEPlQNLKLVLGLHNLHDLQDPGLTFYIREAIKHPG 104
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGA-SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741  105 YNHK-YENDLALLKLDRRVQPSKNVKPLALPRKPrSKPAEGTWCSTAGWGMTHQGGPrARALQELDLRVLDTQMCNNSrf 183
Cdd:pfam00089  80 YNPDtLDNDIALLKLESPVTLGDTVRPICLPDAS-SDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSA-- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 699114741  184 WNGVLIDSMLClkAGSKSQAPCKGDSGGPLVCGKGQVDGILSFsSKTCTDIFKPPVATAVAPYSSWI 250
Cdd:pfam00089 156 YGGTVTDTMIC--AGAGGKDACQGDSGGPLVCSDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-258 2.09e-57

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 184.08  E-value: 2.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741  23 ETQIIGGREAVPHSRPYMASLQKAK---SHVCGGVLVHRKWVLTAAHCLSEP-LQNLKLVLGLHNLHDlqDPGLTFYIRE 98
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgPSDLRVVIGSTDLST--SGGTVVKVAR 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741  99 AIKHPGYN-HKYENDLALLKLDRrvqPSKNVKPLALPRkPRSKPAEGTWCSTAGWGMT-HQGGPRARALQELDLRVLDTQ 176
Cdd:COG5640  106 IVVHPDYDpATPGNDIALLKLAT---PVPGVAPAPLAT-SADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741 177 MCNNsrfWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVC---GKGQVDGILSFSSKTCtDIFKPPVATAVAPYSSWIRKV 253
Cdd:COG5640  182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVkdgGGWVLVGVVSWGGGPC-AAGYPGVYTRVSAYRDWIKST 257

                 ....*
gi 699114741 254 IGRWS 258
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 ...
26-253 5.82e-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: 240.64  E-value: 5.82e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741  26 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCL-SEPLQNLKLVLGLHNLHDLQDPGLTFYIREAIKHP 103
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741 104 GYNHK-YENDLALLKLDRRVQPSKNVKPLALPRKpRSKPAEGTWCSTAGWGMTHQGGPRARALQELDLRVLDTQMCNNSR 182
Cdd:cd00190   81 NYNPStYDNDIALLKLKRPVTLSDNVRPICLPSS-GYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 699114741 183 FWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVC---GKGQVDGILSFSSKtCTDIFKPPVATAVAPYSSWIRKV 253
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndnGRGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-250 5.85e-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: 227.56  E-value: 5.85e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741    26 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCL-SEPLQNLKLVLGLHNLhDLQDPGLTFYIREAIKHP 103
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVrGSDPSNIRVRLGSHDL-SSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741   104 GYNHK-YENDLALLKLDRRVQPSKNVKPLALPRKPRSkPAEGTWCSTAGWGMTHQG-GPRARALQELDLRVLDTQMCNNS 181
Cdd:smart00020  81 NYNPStYDNDIALLKLKEPVTLSDNVRPICLPSSNYN-VPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 699114741   182 RFWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVCGK--GQVDGILSFSSKtCTDIFKPPVATAVAPYSSWI 250
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDgrWVLVGIVSWGSG-CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
26-250 1.24e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 218.85  E-value: 1.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741   26 IIGGREAVPHSRPYMASLQ-KAKSHVCGGVLVHRKWVLTAAHCLSEPlQNLKLVLGLHNLHDLQDPGLTFYIREAIKHPG 104
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGA-SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741  105 YNHK-YENDLALLKLDRRVQPSKNVKPLALPRKPrSKPAEGTWCSTAGWGMTHQGGPrARALQELDLRVLDTQMCNNSrf 183
Cdd:pfam00089  80 YNPDtLDNDIALLKLESPVTLGDTVRPICLPDAS-SDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSA-- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 699114741  184 WNGVLIDSMLClkAGSKSQAPCKGDSGGPLVCGKGQVDGILSFsSKTCTDIFKPPVATAVAPYSSWI 250
Cdd:pfam00089 156 YGGTVTDTMIC--AGAGGKDACQGDSGGPLVCSDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-258 2.09e-57

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 184.08  E-value: 2.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741  23 ETQIIGGREAVPHSRPYMASLQKAK---SHVCGGVLVHRKWVLTAAHCLSEP-LQNLKLVLGLHNLHDlqDPGLTFYIRE 98
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgPSDLRVVIGSTDLST--SGGTVVKVAR 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741  99 AIKHPGYN-HKYENDLALLKLDRrvqPSKNVKPLALPRkPRSKPAEGTWCSTAGWGMT-HQGGPRARALQELDLRVLDTQ 176
Cdd:COG5640  106 IVVHPDYDpATPGNDIALLKLAT---PVPGVAPAPLAT-SADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741 177 MCNNsrfWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVC---GKGQVDGILSFSSKTCtDIFKPPVATAVAPYSSWIRKV 253
Cdd:COG5640  182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVkdgGGWVLVGVVSWGGGPC-AAGYPGVYTRVSAYRDWIKST 257

                 ....*
gi 699114741 254 IGRWS 258
Cdd:COG5640  258 AGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
48-231 1.10e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 59.30  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741  48 SHVCGGVLVHRKWVLTAAHCLSEP-----LQNLKLVLGLHNlhdlqDPGLTFYIREAIKHPGY--NHKYENDLALLKLDR 120
Cdd:COG3591   11 GGVCTGTLIGPNLVLTAGHCVYDGagggwATNIVFVPGYNG-----GPYGTATATRFRVPPGWvaSGDAGYDYALLRLDE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741 121 RVQPSknVKPLALprKPRSKPAEGTWCSTAGWGmthQGGPRARALQElDLRVLDTQmcnnsrfwNGVLidSMLClkagsk 200
Cdd:COG3591   86 PLGDT--TGWLGL--AFNDAPLAGEPVTIIGYP---GDRPKDLSLDC-SGRVTGVQ--------GNRL--SYDC------ 141
                        170       180       190
                 ....*....|....*....|....*....|....
gi 699114741 201 sqAPCKGDSGGPL---VCGKGQVDGILSFSSKTC 231
Cdd:COG3591  142 --DTTGGSSGSPVlddSDGGGRVVGVHSAGGADR 173
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
53-223 1.01e-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: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741   53 GVLV-HRKWVLTAAHCLSEPlqnlklvlglhnlHDLQDPGLTFYIREAIKHPGYNHKY--ENDLALLKLDrrvQPSKNVK 129
Cdd:pfam13365   3 GFVVsSDGLVLTNAHVVDDA-------------EEAAVELVSVVLADGREYPATVVARdpDLDLALLRVS---GDGRGLP 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114741  130 PLALprKPRSKPAEGTWCSTAGWGmthQGGPRaralqeldLRVLDTQMCNNSRFWNGVLIDSMLCLKAgsksqAPCKGDS 209
Cdd:pfam13365  67 PLPL--GDSEPLVGGERVYAVGYP---LGGEK--------LSLSEGIVSGVDEGRDGGDDGRVIQTDA-----ALSPGSS 128
                         170
                  ....*....|....
gi 699114741  210 GGPLVCGKGQVDGI 223
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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