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Conserved domains on  [gi|1677538875|ref|NP_036599|]
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tryptase gamma preproprotein [Homo sapiens]

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 ...
38-268 2.07e-93

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: 276.85  E-value: 2.07e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875  38 IVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSGSlNSSDYQVHLGELEIT---LSPHFSTVRQIILH 113
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSsneGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875 114 SSPSGQPgTSGDIALVELSVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEPLPppYSLREVKVSVVDTETCR 193
Cdd:cd00190    80 PNYNPST-YDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP--DVLQEVNVPIVSNAECK 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677538875 194 RDYPGpgGSILQPDMLCARGPG---DACQDDSGGPLVCQVNGAWVQAGTVSWGEGCGRPNRPGVYTRVPAYVNWIRRH 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 2.07e-93

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: 276.85  E-value: 2.07e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875  38 IVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSGSlNSSDYQVHLGELEIT---LSPHFSTVRQIILH 113
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSsneGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875 114 SSPSGQPgTSGDIALVELSVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEPLPppYSLREVKVSVVDTETCR 193
Cdd:cd00190    80 PNYNPST-YDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP--DVLQEVNVPIVSNAECK 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677538875 194 RDYPGpgGSILQPDMLCARGPG---DACQDDSGGPLVCQVNGAWVQAGTVSWGEGCGRPNRPGVYTRVPAYVNWIRRH 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 1.04e-89

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: 267.62  E-value: 1.04e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875   37 RIVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSGSLNSSdYQVHLGELEITLSPHFST--VRQIILH 113
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSN-IRVRLGSHDLSSGEEGQVikVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875  114 ssPSGQPGTSG-DIALVELSVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEPlPPPYSLREVKVSVVDTETC 192
Cdd:smart00020  80 --PNYNPSTYDnDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538875  193 RRDYPGPGgsILQPDMLCARGPG---DACQDDSGGPLVCQvNGAWVQAGTVSWGEGCGRPNRPGVYTRVPAYVNWI 265
Cdd:smart00020 157 RRAYSGGG--AITDNMLCAGGLEggkDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
38-265 3.55e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 222.32  E-value: 3.55e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875  38 IVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSgslNSSDYQVHLGELEITL---SPHFSTVRQIILH 113
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLregGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875 114 SSpSGQPGTSGDIALVELSVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEplpPPYSLREVKVSVVDTETCR 193
Cdd:pfam00089  78 PN-YNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677538875 194 RDYPGPggsiLQPDMLCARGPG-DACQDDSGGPLVCqvNGAWVQaGTVSWGEGCGRPNRPGVYTRVPAYVNWI 265
Cdd:pfam00089 154 SAYGGT----VTDTMICAGAGGkDACQGDSGGPLVC--SDGELI-GIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
29-273 1.07e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.89  E-value: 1.07e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875  29 PQVSDAGGRIVGGHAAPAGAWPWQASLRLR---RVHVCGGSLLSPQWVLTAAHCFSGSlNSSDYQVHLGELEITLSPHF- 104
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGGTv 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875 105 STVRQIILHssPSGQPGTSG-DIALVELSVPVTLSSrilPVCLPEASDDFCPGIRCWVTGWGYTREGEPLPPPYsLREVK 183
Cdd:COG5640   101 VKVARIVVH--PDYDPATPGnDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGT-LRKAD 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875 184 VSVVDTETCRrdypgPGGSILQPDMLCA---RGPGDACQDDSGGPLVCQVNGAWVQAGTVSWGEGCGRPNRPGVYTRVPA 260
Cdd:COG5640   175 VPVVSDATCA-----AYGGFDGGTMLCAgypEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSA 249
                         250
                  ....*....|...
gi 1677538875 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 2.07e-93

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: 276.85  E-value: 2.07e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875  38 IVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSGSlNSSDYQVHLGELEIT---LSPHFSTVRQIILH 113
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSsneGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875 114 SSPSGQPgTSGDIALVELSVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEPLPppYSLREVKVSVVDTETCR 193
Cdd:cd00190    80 PNYNPST-YDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP--DVLQEVNVPIVSNAECK 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677538875 194 RDYPGpgGSILQPDMLCARGPG---DACQDDSGGPLVCQVNGAWVQAGTVSWGEGCGRPNRPGVYTRVPAYVNWIRRH 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 1.04e-89

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: 267.62  E-value: 1.04e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875   37 RIVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSGSLNSSdYQVHLGELEITLSPHFST--VRQIILH 113
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSN-IRVRLGSHDLSSGEEGQVikVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875  114 ssPSGQPGTSG-DIALVELSVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEPlPPPYSLREVKVSVVDTETC 192
Cdd:smart00020  80 --PNYNPSTYDnDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538875  193 RRDYPGPGgsILQPDMLCARGPG---DACQDDSGGPLVCQvNGAWVQAGTVSWGEGCGRPNRPGVYTRVPAYVNWI 265
Cdd:smart00020 157 RRAYSGGG--AITDNMLCAGGLEggkDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
38-265 3.55e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 222.32  E-value: 3.55e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875  38 IVGGHAAPAGAWPWQASLRLRR-VHVCGGSLLSPQWVLTAAHCFSgslNSSDYQVHLGELEITL---SPHFSTVRQIILH 113
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLregGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875 114 SSpSGQPGTSGDIALVELSVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEplpPPYSLREVKVSVVDTETCR 193
Cdd:pfam00089  78 PN-YNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677538875 194 RDYPGPggsiLQPDMLCARGPG-DACQDDSGGPLVCqvNGAWVQaGTVSWGEGCGRPNRPGVYTRVPAYVNWI 265
Cdd:pfam00089 154 SAYGGT----VTDTMICAGAGGkDACQGDSGGPLVC--SDGELI-GIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
29-273 1.07e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.89  E-value: 1.07e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875  29 PQVSDAGGRIVGGHAAPAGAWPWQASLRLR---RVHVCGGSLLSPQWVLTAAHCFSGSlNSSDYQVHLGELEITLSPHF- 104
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGGTv 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875 105 STVRQIILHssPSGQPGTSG-DIALVELSVPVTLSSrilPVCLPEASDDFCPGIRCWVTGWGYTREGEPLPPPYsLREVK 183
Cdd:COG5640   101 VKVARIVVH--PDYDPATPGnDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGT-LRKAD 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875 184 VSVVDTETCRrdypgPGGSILQPDMLCA---RGPGDACQDDSGGPLVCQVNGAWVQAGTVSWGEGCGRPNRPGVYTRVPA 260
Cdd:COG5640   175 VPVVSDATCA-----AYGGFDGGTMLCAgypEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSA 249
                         250
                  ....*....|...
gi 1677538875 261 YVNWIRRHITASG 273
Cdd:COG5640   250 YRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
61-271 7.65e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 48.90  E-value: 7.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875  61 HVCGGSLLSPQWVLTAAHCFSGSLNSSDYQvhlgelEITLSPHF-------STVRQIILHSSPSGQPGTSGDIALVELSV 133
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGAGGGWAT------NIVFVPGYnggpygtATATRFRVPPGWVASGDAGYDYALLRLDE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875 134 PVTLSSRILPVclpEASDDFCPGIRCWVTGWGYTRegeplPPPYSLRevkvsvvdtETCRRDYPGPGGSILQPDMLcarg 213
Cdd:COG3591    86 PLGDTTGWLGL---AFNDAPLAGEPVTIIGYPGDR-----PKDLSLD---------CSGRVTGVQGNRLSYDCDTT---- 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1677538875 214 PGdacqdDSGGPLVCQVNGAWVQAGTVSWGeGCGRPNRpGVYTRvPAYVNWIRRHITA 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 3.16e-05

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: 42.53  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538875  49 WPWQASLRLRRVHVCGGSLLSPQWVLTAAHCFSG-SLNSSDYQVHLGELEITLS---PHFSTVRQIILHSSPSGQpgtsg 124
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtNLRHQYISVVLGGAKTLKSiegPYEQIVRVDCRHDIPESE----- 75
                          90       100
                  ....*....|....*....|....*..
gi 1677538875 125 dIALVELSVPVTLSSRILPVCLPEASD 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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