NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2026808258|gb|QTX15636|]
View 

granzyme M [Camelus bactrianus]

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

show extra options »

Show site features     Horizontal zoom: ×

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 ...
27-252 1.75e-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: 246.42  E-value: 1.75e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  27 IIGGREAAPNSHPYMVSLQ-KAGTHRCGGVLVHQKWVLTAAHCLTNR-IEQLRLVLGLHVLGDPSLT---YRIRKVVKHP 101
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSaPSNYTVRLGSHDLSSNEGGgqvIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258 102 EYkEAPSLQNDLALLKLDGKVKPSRTIRPLALPQRRQAVAAGARCSVAGWGLTHQGGQLAKALQELDVHVLDARMCNNSR 181
Cdd:cd00190    81 NY-NPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2026808258 182 FWNGDITPDMICLAANAKNQAPCKGDSGGPVVCR---RGQVAGIVSFSSNvCTDIFKPSVATAVAPYTPWIKKT 252
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 ...
27-252 1.75e-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: 246.42  E-value: 1.75e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  27 IIGGREAAPNSHPYMVSLQ-KAGTHRCGGVLVHQKWVLTAAHCLTNR-IEQLRLVLGLHVLGDPSLT---YRIRKVVKHP 101
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSaPSNYTVRLGSHDLSSNEGGgqvIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258 102 EYkEAPSLQNDLALLKLDGKVKPSRTIRPLALPQRRQAVAAGARCSVAGWGLTHQGGQLAKALQELDVHVLDARMCNNSR 181
Cdd:cd00190    81 NY-NPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2026808258 182 FWNGDITPDMICLAANAKNQAPCKGDSGGPVVCR---RGQVAGIVSFSSNvCTDIFKPSVATAVAPYTPWIKKT 252
Cdd:cd00190   160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngRGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-249 3.96e-81

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: 242.97  E-value: 3.96e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258   26 HIIGGREAAPNSHPYMVSLQ-KAGTHRCGGVLVHQKWVLTAAHCLTNR-IEQLRLVLGLHVL--GDPSLTYRIRKVVKHP 101
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSdPSNIRVRLGSHDLssGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  102 EYKEApSLQNDLALLKLDGKVKPSRTIRPLALPQRRQAVAAGARCSVAGWGLTHQG-GQLAKALQELDVHVLDARMCNNS 180
Cdd:smart00020  81 NYNPS-TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2026808258  181 RFWNGDITPDMICLAANAKNQAPCKGDSGGPVVC--RRGQVAGIVSFSSNvCTDIFKPSVATAVAPYTPWI 249
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCndGRWVLVGIVSWGSG-CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
27-249 5.47e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 219.62  E-value: 5.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  27 IIGGREAAPNSHPYMVSLQ-KAGTHRCGGVLVHQKWVLTAAHCLTNRiEQLRLVLGLH--VLGDPSLTYR-IRKVVKHPE 102
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGA-SDVKVVLGAHniVLREGGEQKFdVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258 103 YkEAPSLQNDLALLKLDGKVKPSRTIRPLALPQRRQAVAAGARCSVAGWGLTHQGGqLAKALQELDVHVLDARMCNNSrf 182
Cdd:pfam00089  80 Y-NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSA-- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2026808258 183 WNGDITPDMIClaANAKNQAPCKGDSGGPVVCRRGQVAGIVSFSSNvCTDIFKPSVATAVAPYTPWI 249
Cdd:pfam00089 156 YGGTVTDTMIC--AGAGGKDACQGDSGGPLVCSDGELIGIVSWGYG-CASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-254 1.98e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 189.09  E-value: 1.98e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  24 ETHIIGGREAAPNSHPYMVSLQKAG---THRCGGVLVHQKWVLTAAHCLTN-RIEQLRLVLGLHVL-GDPSLTYRIRKVV 98
Cdd:COG5640    28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGdGPSDLRVVIGSTDLsTSGGTVVKVARIV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  99 KHPEYkEAPSLQNDLALLKLDgkvKPSRTIRPLALPQRRQAVAAGARCSVAGWGLT-HQGGQLAKALQELDVHVLDARMC 177
Cdd:COG5640   108 VHPDY-DPATPGNDIALLKLA---TPVPGVAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDATC 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258 178 NNsrfWNGDITPDMICLAANAKNQAPCKGDSGGPVVCR---RGQVAGIVSFSSNVCtDIFKPSVATAVAPYTPWIKKTIR 254
Cdd:COG5640   184 AA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKdggGWVLVGVVSWGGGPC-AAGYPGVYTRVSAYRDWIKSTAG 259
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-252 1.75e-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: 246.42  E-value: 1.75e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  27 IIGGREAAPNSHPYMVSLQ-KAGTHRCGGVLVHQKWVLTAAHCLTNR-IEQLRLVLGLHVLGDPSLT---YRIRKVVKHP 101
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSaPSNYTVRLGSHDLSSNEGGgqvIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258 102 EYkEAPSLQNDLALLKLDGKVKPSRTIRPLALPQRRQAVAAGARCSVAGWGLTHQGGQLAKALQELDVHVLDARMCNNSR 181
Cdd:cd00190    81 NY-NPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2026808258 182 FWNGDITPDMICLAANAKNQAPCKGDSGGPVVCR---RGQVAGIVSFSSNvCTDIFKPSVATAVAPYTPWIKKT 252
Cdd:cd00190   160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngRGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-249 3.96e-81

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: 242.97  E-value: 3.96e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258   26 HIIGGREAAPNSHPYMVSLQ-KAGTHRCGGVLVHQKWVLTAAHCLTNR-IEQLRLVLGLHVL--GDPSLTYRIRKVVKHP 101
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSdPSNIRVRLGSHDLssGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  102 EYKEApSLQNDLALLKLDGKVKPSRTIRPLALPQRRQAVAAGARCSVAGWGLTHQG-GQLAKALQELDVHVLDARMCNNS 180
Cdd:smart00020  81 NYNPS-TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2026808258  181 RFWNGDITPDMICLAANAKNQAPCKGDSGGPVVC--RRGQVAGIVSFSSNvCTDIFKPSVATAVAPYTPWI 249
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCndGRWVLVGIVSWGSG-CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
27-249 5.47e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 219.62  E-value: 5.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  27 IIGGREAAPNSHPYMVSLQ-KAGTHRCGGVLVHQKWVLTAAHCLTNRiEQLRLVLGLH--VLGDPSLTYR-IRKVVKHPE 102
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGA-SDVKVVLGAHniVLREGGEQKFdVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258 103 YkEAPSLQNDLALLKLDGKVKPSRTIRPLALPQRRQAVAAGARCSVAGWGLTHQGGqLAKALQELDVHVLDARMCNNSrf 182
Cdd:pfam00089  80 Y-NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSA-- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2026808258 183 WNGDITPDMIClaANAKNQAPCKGDSGGPVVCRRGQVAGIVSFSSNvCTDIFKPSVATAVAPYTPWI 249
Cdd:pfam00089 156 YGGTVTDTMIC--AGAGGKDACQGDSGGPLVCSDGELIGIVSWGYG-CASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-254 1.98e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 189.09  E-value: 1.98e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  24 ETHIIGGREAAPNSHPYMVSLQKAG---THRCGGVLVHQKWVLTAAHCLTN-RIEQLRLVLGLHVL-GDPSLTYRIRKVV 98
Cdd:COG5640    28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGdGPSDLRVVIGSTDLsTSGGTVVKVARIV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  99 KHPEYkEAPSLQNDLALLKLDgkvKPSRTIRPLALPQRRQAVAAGARCSVAGWGLT-HQGGQLAKALQELDVHVLDARMC 177
Cdd:COG5640   108 VHPDY-DPATPGNDIALLKLA---TPVPGVAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDATC 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258 178 NNsrfWNGDITPDMICLAANAKNQAPCKGDSGGPVVCR---RGQVAGIVSFSSNVCtDIFKPSVATAVAPYTPWIKKTIR 254
Cdd:COG5640   184 AA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKdggGWVLVGVVSWGGGPC-AAGYPGVYTRVSAYRDWIKSTAG 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
47-230 5.24e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 62.77  E-value: 5.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  47 AGTHRCGGVLVHQKWVLTAAHCLTNR-----IEQLRLVLGLHvlGDPSLTYRIRKVVKHPEYKEAPSLQNDLALLKLDGK 121
Cdd:COG3591     9 GGGGVCTGTLIGPNLVLTAGHCVYDGagggwATNIVFVPGYN--GGPYGTATATRFRVPPGWVASGDAGYDYALLRLDEP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258 122 VkpSRTIRPLALPQRRQAvAAGARCSVAGwgltHQGGQLAKALQELDVHVLDARmcNNSRFWNGDITPdmiclaanaknq 201
Cdd:COG3591    87 L--GDTTGWLGLAFNDAP-LAGEPVTIIG----YPGDRPKDLSLDCSGRVTGVQ--GNRLSYDCDTTG------------ 145
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2026808258 202 apckGDSGGPVVCR---RGQVAGIVSFSSNVC 230
Cdd:COG3591   146 ----GSSGSPVLDDsdgGGRVVGVHSAGGADR 173
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
54-222 3.86e-10

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 56.66  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  54 GVLV-HQKWVLTAAHCLTnriEQLRLVLGLHVLGDPSLTYRIRKVVkhpeykeAPSLQNDLALLKLDGkvkPSRTIRPLA 132
Cdd:pfam13365   3 GFVVsSDGLVLTNAHVVD---DAEEAAVELVSVVLADGREYPATVV-------ARDPDLDLALLRVSG---DGRGLPPLP 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258 133 LpQRRQAVAAGARCSVAGwgltHQGGQLAKALQEldvhvldARMCNNSRFWNGDITPDMICLAAnaknqAPCKGDSGGPV 212
Cdd:pfam13365  70 L-GDSEPLVGGERVYAVG----YPLGGEKLSLSE-------GIVSGVDEGRDGGDDGRVIQTDA-----ALSPGSSGGPV 132
                         170
                  ....*....|
gi 2026808258 213 VCRRGQVAGI 222
Cdd:pfam13365 133 FDADGRVVGI 142
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
39-150 7.70e-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: 35.60  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026808258  39 PYMVSLQKAGTHRCGGVLVHQKWVLTAAHCLTN---RIEQLRLVLG-----LHVLGDPSLTYRIRKvvkhpeYKEAPslQ 110
Cdd:pfam09342   2 PWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtnlRHQYISVVLGgaktlKSIEGPYEQIVRVDC------RHDIP--E 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2026808258 111 NDLALLKLDGKVKPSRTIRPLALPQRRQAVAAGARCSVAG 150
Cdd:pfam09342  74 SEISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH