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Conserved domains on  [gi|8570164|gb|AAF76458|]
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gamma II-tryptase [Homo sapiens]

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

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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 ...
38-268 4.95e-94

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: 278.39  E-value: 4.95e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164   38 IVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSGSlNSSDYQVHLGELEIT---LSPHFSTVRQIILH 113
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSsneGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164  114 SSPSGQPgTSGDMALVELTVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEPLPppYSLREVKVSVVDTETCR 193
Cdd:cd00190  80 PNYNPST-YDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP--DVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8570164  194 RDYPGpgGSIIQPDMLCARGPG---DACQDDSGGPLVCQVNGAWVQAGIVSWGEGCGRPNRPGVYTRVPAYVNWIRRH 268
Cdd:cd00190 157 RAYSY--GGTITDNMLCAGGLEggkDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
38-268 4.95e-94

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: 278.39  E-value: 4.95e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164   38 IVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSGSlNSSDYQVHLGELEIT---LSPHFSTVRQIILH 113
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSsneGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164  114 SSPSGQPgTSGDMALVELTVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEPLPppYSLREVKVSVVDTETCR 193
Cdd:cd00190  80 PNYNPST-YDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP--DVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8570164  194 RDYPGpgGSIIQPDMLCARGPG---DACQDDSGGPLVCQVNGAWVQAGIVSWGEGCGRPNRPGVYTRVPAYVNWIRRH 268
Cdd:cd00190 157 RAYSY--GGTITDNMLCAGGLEggkDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
37-265 1.87e-90

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: 269.16  E-value: 1.87e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164      37 RIVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSGSLNSSdYQVHLGELEITLSPHFST--VRQIILH 113
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSN-IRVRLGSHDLSSGEEGQVikVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164     114 ssPSGQPGTSG-DMALVELTVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEPlPPPYSLREVKVSVVDTETC 192
Cdd:smart00020  80 --PNYNPSTYDnDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8570164     193 RRDYPGPGgsIIQPDMLCARGPG---DACQDDSGGPLVCQvNGAWVQAGIVSWGEGCGRPNRPGVYTRVPAYVNWI 265
Cdd:smart00020 157 RRAYSGGG--AITDNMLCAGGLEggkDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
38-265 4.76e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 224.63  E-value: 4.76e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164     38 IVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSgslNSSDYQVHLGELEITL---SPHFSTVRQIILH 113
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLregGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164    114 SSpSGQPGTSGDMALVELTVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEplpPPYSLREVKVSVVDTETCR 193
Cdd:pfam00089  78 PN-YNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8570164    194 RDYPGPggsiIQPDMLCARGPG-DACQDDSGGPLVCqvNGAWVQaGIVSWGEGCGRPNRPGVYTRVPAYVNWI 265
Cdd:pfam00089 154 SAYGGT----VTDTMICAGAGGkDACQGDSGGPLVC--SDGELI-GIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
29-273 1.43e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.51  E-value: 1.43e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164   29 PQVSDAGGRIVGGHAAPAGAWPWQASLRLR---RVHVCGGSLLSPQWVLTAAHCFSGSlNSSDYQVHLGELEITLSPHF- 104
Cdd:COG5640  22 APAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGGTv 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164  105 STVRQIILHssPSGQPGTSG-DMALVELTVPVTLSSrilPVCLPEASDDFCPGIRCWVTGWGYTREGEPLPPPYsLREVK 183
Cdd:COG5640 101 VKVARIVVH--PDYDPATPGnDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGT-LRKAD 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164  184 VSVVDTETCRrdypgPGGSIIQPDMLCA---RGPGDACQDDSGGPLVCQVNGAWVQAGIVSWGEGCGRPNRPGVYTRVPA 260
Cdd:COG5640 175 VPVVSDATCA-----AYGGFDGGTMLCAgypEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSA 249
                       250
                ....*....|...
gi 8570164  261 YVNWIRRHITASG 273
Cdd:COG5640 250 YRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
38-268 4.95e-94

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: 278.39  E-value: 4.95e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164   38 IVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSGSlNSSDYQVHLGELEIT---LSPHFSTVRQIILH 113
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSsneGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164  114 SSPSGQPgTSGDMALVELTVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEPLPppYSLREVKVSVVDTETCR 193
Cdd:cd00190  80 PNYNPST-YDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP--DVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8570164  194 RDYPGpgGSIIQPDMLCARGPG---DACQDDSGGPLVCQVNGAWVQAGIVSWGEGCGRPNRPGVYTRVPAYVNWIRRH 268
Cdd:cd00190 157 RAYSY--GGTITDNMLCAGGLEggkDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
37-265 1.87e-90

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: 269.16  E-value: 1.87e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164      37 RIVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSGSLNSSdYQVHLGELEITLSPHFST--VRQIILH 113
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSN-IRVRLGSHDLSSGEEGQVikVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164     114 ssPSGQPGTSG-DMALVELTVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEPlPPPYSLREVKVSVVDTETC 192
Cdd:smart00020  80 --PNYNPSTYDnDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8570164     193 RRDYPGPGgsIIQPDMLCARGPG---DACQDDSGGPLVCQvNGAWVQAGIVSWGEGCGRPNRPGVYTRVPAYVNWI 265
Cdd:smart00020 157 RRAYSGGG--AITDNMLCAGGLEggkDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
38-265 4.76e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 224.63  E-value: 4.76e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164     38 IVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSgslNSSDYQVHLGELEITL---SPHFSTVRQIILH 113
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLregGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164    114 SSpSGQPGTSGDMALVELTVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEplpPPYSLREVKVSVVDTETCR 193
Cdd:pfam00089  78 PN-YNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8570164    194 RDYPGPggsiIQPDMLCARGPG-DACQDDSGGPLVCqvNGAWVQaGIVSWGEGCGRPNRPGVYTRVPAYVNWI 265
Cdd:pfam00089 154 SAYGGT----VTDTMICAGAGGkDACQGDSGGPLVC--SDGELI-GIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
29-273 1.43e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.51  E-value: 1.43e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164   29 PQVSDAGGRIVGGHAAPAGAWPWQASLRLR---RVHVCGGSLLSPQWVLTAAHCFSGSlNSSDYQVHLGELEITLSPHF- 104
Cdd:COG5640  22 APAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGGTv 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164  105 STVRQIILHssPSGQPGTSG-DMALVELTVPVTLSSrilPVCLPEASDDFCPGIRCWVTGWGYTREGEPLPPPYsLREVK 183
Cdd:COG5640 101 VKVARIVVH--PDYDPATPGnDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGT-LRKAD 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164  184 VSVVDTETCRrdypgPGGSIIQPDMLCA---RGPGDACQDDSGGPLVCQVNGAWVQAGIVSWGEGCGRPNRPGVYTRVPA 260
Cdd:COG5640 175 VPVVSDATCA-----AYGGFDGGTMLCAgypEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSA 249
                       250
                ....*....|...
gi 8570164  261 YVNWIRRHITASG 273
Cdd:COG5640 250 YRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
61-271 1.52e-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: 1.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164   61 HVCGGSLLSPQWVLTAAHCFSGSLNSSDYQvhlgelEITLSPHF-------STVRQIILHSSPSGQPGTSGDMALVELTV 133
Cdd:COG3591  12 GVCTGTLIGPNLVLTAGHCVYDGAGGGWAT------NIVFVPGYnggpygtATATRFRVPPGWVASGDAGYDYALLRLDE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164  134 PVTLSSRILPVclpEASDDFCPGIRCWVTGWGYTRegeplPPPYSLRevkvsvvdtETCRRDYPGPGGSIIQPDMLcarg 213
Cdd:COG3591  86 PLGDTTGWLGL---AFNDAPLAGEPVTIIGYPGDR-----PKDLSLD---------CSGRVTGVQGNRLSYDCDTT---- 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 8570164  214 PGdacqdDSGGPLVCQVNGAWVQAGIVSWGeGCGRPNRpGVYTRvPAYVNWIRRHITA 271
Cdd:COG3591 145 GG-----SSGSPVLDDSDGGGRVVGVHSAG-GADRANT-GVRLT-SAIVAALRAWASA 194
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
49-151 1.10e-04

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: 40.99  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8570164     49 WPWQASLRLRRVHVCGGSLLSPQWVLTAAHCFSG-SLNSSDYQVHLGELEITLS---PHFSTVRQIILHSSPSGQpgtsg 124
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtNLRHQYISVVLGGAKTLKSiegPYEQIVRVDCRHDIPESE----- 75
                          90       100
                  ....*....|....*....|....*..
gi 8570164    125 dMALVELTVPVTLSSRILPVCLPEASD 151
Cdd:pfam09342  76 -ISLLHLASPASFSNHVLPTFVPETRN 101
 
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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