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Conserved domains on  [gi|1958788069|ref|XP_038934496|]
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granzyme M isoform X2 [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 ...
26-253 6.44e-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: 245.65  E-value: 6.44e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  26 IIGGREAVPHSRPYMVSLQNTK-SHVCGGVLVHQKWVLTAAHCL-SEPLQQLKLVFGLHSLHDPQDPGLTFYIKQAIKHP 103
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069 104 GYNLK-YENDLALLKLDGRVKPSKNVKPLALPRKPRDkPAEGSRCSTAGWGITHQRGQLAKSLQELDLRLLDTRMCNNSR 182
Cdd:cd00190    81 NYNPStYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-LPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958788069 183 FWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVC---GKGKVDGILSFSSkNCTDIFKPTVATAVAPYSSWIRKV 253
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 ...
26-253 6.44e-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: 245.65  E-value: 6.44e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  26 IIGGREAVPHSRPYMVSLQNTK-SHVCGGVLVHQKWVLTAAHCL-SEPLQQLKLVFGLHSLHDPQDPGLTFYIKQAIKHP 103
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069 104 GYNLK-YENDLALLKLDGRVKPSKNVKPLALPRKPRDkPAEGSRCSTAGWGITHQRGQLAKSLQELDLRLLDTRMCNNSR 182
Cdd:cd00190    81 NYNPStYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-LPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958788069 183 FWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVC---GKGKVDGILSFSSkNCTDIFKPTVATAVAPYSSWIRKV 253
Cdd:cd00190   160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndnGRGVLVGIVSWGS-GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-250 1.92e-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: 234.11  E-value: 1.92e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069   26 IIGGREAVPHSRPYMVSLQNTK-SHVCGGVLVHQKWVLTAAHCL-SEPLQQLKLVFGLHSLHDPQDpGLTFYIKQAIKHP 103
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVrGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  104 GYNLK-YENDLALLKLDGRVKPSKNVKPLALPRKpRDKPAEGSRCSTAGWGITHQR-GQLAKSLQELDLRLLDTRMCNNS 181
Cdd:smart00020  81 NYNPStYDNDIALLKLKEPVTLSDNVRPICLPSS-NYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958788069  182 RFWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVCGKGK--VDGILSFSSkNCTDIFKPTVATAVAPYSSWI 250
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRwvLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
26-250 1.08e-76

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.95  E-value: 1.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  26 IIGGREAVPHSRPYMVSLQN-TKSHVCGGVLVHQKWVLTAAHCLSEPlQQLKLVFGLHSLHDPQDPGLTFYIKQAIKHPG 104
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGA-SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069 105 YNLK-YENDLALLKLDGRVKPSKNVKPLALPRKPRDKPAeGSRCSTAGWGITHQRGqLAKSLQELDLRLLDTRMCNNSrf 183
Cdd:pfam00089  80 YNPDtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPV-GTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSA-- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788069 184 WNGVLTDSMLClkAGAKGQAPCKGDSGGPLVCGKGKVDGILSFsSKNCTDIFKPTVATAVAPYSSWI 250
Cdd:pfam00089 156 YGGTVTDTMIC--AGAGGKDACQGDSGGPLVCSDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-258 7.15e-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: 7.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  23 EAQIIGGREAVPHSRPYMVSLQNTK---SHVCGGVLVHQKWVLTAAHCLSEP-LQQLKLVFGLHSLHDpqDPGLTFYIKQ 98
Cdd:COG5640    28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgPSDLRVVIGSTDLST--SGGTVVKVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  99 AIKHPGYNLK-YENDLALLKLDgrvKPSKNVKPLALPRkPRDKPAEGSRCSTAGWGIT-HQRGQLAKSLQELDLRLLDTR 176
Cdd:COG5640   106 IVVHPDYDPAtPGNDIALLKLA---TPVPGVAPAPLAT-SADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069 177 MCNNsrfWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVC---GKGKVDGILSFSSKNCtDIFKPTVATAVAPYSSWIRKV 253
Cdd:COG5640   182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVkdgGGWVLVGVVSWGGGPC-AAGYPGVYTRVSAYRDWIKST 257

                  ....*
gi 1958788069 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 6.44e-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: 245.65  E-value: 6.44e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  26 IIGGREAVPHSRPYMVSLQNTK-SHVCGGVLVHQKWVLTAAHCL-SEPLQQLKLVFGLHSLHDPQDPGLTFYIKQAIKHP 103
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069 104 GYNLK-YENDLALLKLDGRVKPSKNVKPLALPRKPRDkPAEGSRCSTAGWGITHQRGQLAKSLQELDLRLLDTRMCNNSR 182
Cdd:cd00190    81 NYNPStYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-LPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958788069 183 FWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVC---GKGKVDGILSFSSkNCTDIFKPTVATAVAPYSSWIRKV 253
Cdd:cd00190   160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndnGRGVLVGIVSWGS-GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-250 1.92e-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: 234.11  E-value: 1.92e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069   26 IIGGREAVPHSRPYMVSLQNTK-SHVCGGVLVHQKWVLTAAHCL-SEPLQQLKLVFGLHSLHDPQDpGLTFYIKQAIKHP 103
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVrGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  104 GYNLK-YENDLALLKLDGRVKPSKNVKPLALPRKpRDKPAEGSRCSTAGWGITHQR-GQLAKSLQELDLRLLDTRMCNNS 181
Cdd:smart00020  81 NYNPStYDNDIALLKLKEPVTLSDNVRPICLPSS-NYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958788069  182 RFWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVCGKGK--VDGILSFSSkNCTDIFKPTVATAVAPYSSWI 250
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRwvLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
26-250 1.08e-76

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.95  E-value: 1.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  26 IIGGREAVPHSRPYMVSLQN-TKSHVCGGVLVHQKWVLTAAHCLSEPlQQLKLVFGLHSLHDPQDPGLTFYIKQAIKHPG 104
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGA-SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069 105 YNLK-YENDLALLKLDGRVKPSKNVKPLALPRKPRDKPAeGSRCSTAGWGITHQRGqLAKSLQELDLRLLDTRMCNNSrf 183
Cdd:pfam00089  80 YNPDtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPV-GTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSA-- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788069 184 WNGVLTDSMLClkAGAKGQAPCKGDSGGPLVCGKGKVDGILSFsSKNCTDIFKPTVATAVAPYSSWI 250
Cdd:pfam00089 156 YGGTVTDTMIC--AGAGGKDACQGDSGGPLVCSDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-258 7.15e-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: 7.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  23 EAQIIGGREAVPHSRPYMVSLQNTK---SHVCGGVLVHQKWVLTAAHCLSEP-LQQLKLVFGLHSLHDpqDPGLTFYIKQ 98
Cdd:COG5640    28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgPSDLRVVIGSTDLST--SGGTVVKVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  99 AIKHPGYNLK-YENDLALLKLDgrvKPSKNVKPLALPRkPRDKPAEGSRCSTAGWGIT-HQRGQLAKSLQELDLRLLDTR 176
Cdd:COG5640   106 IVVHPDYDPAtPGNDIALLKLA---TPVPGVAPAPLAT-SADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069 177 MCNNsrfWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVC---GKGKVDGILSFSSKNCtDIFKPTVATAVAPYSSWIRKV 253
Cdd:COG5640   182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVkdgGGWVLVGVVSWGGGPC-AAGYPGVYTRVSAYRDWIKST 257

                  ....*
gi 1958788069 254 IGRWS 258
Cdd:COG5640   258 AGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
48-251 8.92e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 51.22  E-value: 8.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  48 SHVCGGVLVHQKWVLTAAHCLSEP-----LQQLKLVFGLHslhdpQDPGLTFYIKQAIKHPGY--NLKYENDLALLKLDG 120
Cdd:COG3591    11 GGVCTGTLIGPNLVLTAGHCVYDGagggwATNIVFVPGYN-----GGPYGTATATRFRVPPGWvaSGDAGYDYALLRLDE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069 121 RVKPSknVKPLALprKPRDKPAEGSRCSTAGWGITHqrgQLAKSLQELdlrlldtrmCNNSRFWNGVLtdSMLClkagak 200
Cdd:COG3591    86 PLGDT--TGWLGL--AFNDAPLAGEPVTIIGYPGDR---PKDLSLDCS---------GRVTGVQGNRL--SYDC------ 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958788069 201 gqAPCKGDSGGPL---VCGKGKVDGILSFSSKNCTDIFKPTVATAVAPYSSWIR 251
Cdd:COG3591   142 --DTTGGSSGSPVlddSDGGGRVVGVHSAGGADRANTGVRLTSAIVAALRAWAS 193
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
53-223 4.03e-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: 4.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069  53 GVLV-HQKWVLTAAHCLSEPlqqlklvfglhslHDPQDPGLTFYIKQAIKHPGYNLKY--ENDLALLKLDGrvkPSKNVK 129
Cdd:pfam13365   3 GFVVsSDGLVLTNAHVVDDA-------------EEAAVELVSVVLADGREYPATVVARdpDLDLALLRVSG---DGRGLP 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788069 130 PLALprKPRDKPAEGSRCSTAGwgitHQRGQLAKSLQEldlrlldTRMCNNSRFWNGVLTDSMLCLKAgakgqAPCKGDS 209
Cdd:pfam13365  67 PLPL--GDSEPLVGGERVYAVG----YPLGGEKLSLSE-------GIVSGVDEGRDGGDDGRVIQTDA-----ALSPGSS 128
                         170
                  ....*....|....
gi 1958788069 210 GGPLVCGKGKVDGI 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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