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Conserved domains on  [gi|4503149|ref|NP_001902|]
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cathepsin G 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 ...
21-241 3.71e-83

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: 248.35  E-value: 3.71e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149   21 IIGGRESRPHSRPYMAYLQIQSpaGQSRCGGFLVREDFVLTAAHCWGS----NINVTLGAHNIQRRENTQQHITARRAIR 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149   97 HPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMR-RGTDTLREVQLRVQRDRQCLRI 175
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGgPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503149  176 F--GSYDPRRQICVGDRRERKAAFKGDSGGPLLCN----NVAHGIVSYGKSSGVP--PEVFTRVSSFLPWIRTT 241
Cdd:cd00190 159 YsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-241 3.71e-83

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: 248.35  E-value: 3.71e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149   21 IIGGRESRPHSRPYMAYLQIQSpaGQSRCGGFLVREDFVLTAAHCWGS----NINVTLGAHNIQRRENTQQHITARRAIR 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149   97 HPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMR-RGTDTLREVQLRVQRDRQCLRI 175
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGgPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503149  176 F--GSYDPRRQICVGDRRERKAAFKGDSGGPLLCN----NVAHGIVSYGKSSGVP--PEVFTRVSSFLPWIRTT 241
Cdd:cd00190 159 YsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-238 7.25e-78

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: 234.88  E-value: 7.25e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149      20 EIIGGRESRPHSRPYMAYLQIQSpaGQSRCGGFLVREDFVLTAAHCWG----SNINVTLGAHNIQRRENtQQHITARRAI 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149      96 RHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGT--DTLREVQLRVQRDRQCL 173
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlpDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503149     174 RIFG--SYDPRRQICVGDRRERKAAFKGDSGGPLLCNN---VAHGIVSYGKSSGVP--PEVFTRVSSFLPWI 238
Cdd:smart00020 158 RAYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-238 3.98e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 212.30  E-value: 3.98e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149     21 IIGGRESRPHSRPYMAYLQIQSpaGQSRCGGFLVREDFVLTAAHCW--GSNINVTLGAHNIQRRENTQQHITARRAIRHP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSS--GKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149     99 QYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGS 178
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503149    179 YDPRRQICVGDRreRKAAFKGDSGGPLLCNNV-AHGIVSYGKSSGVP--PEVFTRVSSFLPWI 238
Cdd:pfam00089 159 TVTDTMICAGAG--GKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-244 7.53e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 174.45  E-value: 7.53e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149   13 PTGAEAGEIIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHC----WGSNINVTLGAHNiqRRENTQQH 88
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTD--LSTSGGTV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149   89 ITARRAIRHPQYNQRTIQNDIMLLQLSrrvRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGT--DTLREVQLRV 166
Cdd:COG5640 101 VKVARIVVHPDYDPATPGNDIALLKLA---TPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSqsGTLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149  167 QRDRQClRIFGSYDPRRQICVGDRRERKAAFKGDSGGPLL----CNNVAHGIVSYGKSSGVP--PEVFTRVSSFLPWIRT 240
Cdd:COG5640 178 VSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIKS 256

                ....
gi 4503149  241 TMRS 244
Cdd:COG5640 257 TAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-241 3.71e-83

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: 248.35  E-value: 3.71e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149   21 IIGGRESRPHSRPYMAYLQIQSpaGQSRCGGFLVREDFVLTAAHCWGS----NINVTLGAHNIQRRENTQQHITARRAIR 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149   97 HPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMR-RGTDTLREVQLRVQRDRQCLRI 175
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGgPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503149  176 F--GSYDPRRQICVGDRRERKAAFKGDSGGPLLCN----NVAHGIVSYGKSSGVP--PEVFTRVSSFLPWIRTT 241
Cdd:cd00190 159 YsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-238 7.25e-78

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: 234.88  E-value: 7.25e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149      20 EIIGGRESRPHSRPYMAYLQIQSpaGQSRCGGFLVREDFVLTAAHCWG----SNINVTLGAHNIQRRENtQQHITARRAI 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149      96 RHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGT--DTLREVQLRVQRDRQCL 173
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlpDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503149     174 RIFG--SYDPRRQICVGDRRERKAAFKGDSGGPLLCNN---VAHGIVSYGKSSGVP--PEVFTRVSSFLPWI 238
Cdd:smart00020 158 RAYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-238 3.98e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 212.30  E-value: 3.98e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149     21 IIGGRESRPHSRPYMAYLQIQSpaGQSRCGGFLVREDFVLTAAHCW--GSNINVTLGAHNIQRRENTQQHITARRAIRHP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSS--GKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149     99 QYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGS 178
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503149    179 YDPRRQICVGDRreRKAAFKGDSGGPLLCNNV-AHGIVSYGKSSGVP--PEVFTRVSSFLPWI 238
Cdd:pfam00089 159 TVTDTMICAGAG--GKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-244 7.53e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 174.45  E-value: 7.53e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149   13 PTGAEAGEIIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHC----WGSNINVTLGAHNiqRRENTQQH 88
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTD--LSTSGGTV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149   89 ITARRAIRHPQYNQRTIQNDIMLLQLSrrvRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGT--DTLREVQLRV 166
Cdd:COG5640 101 VKVARIVVHPDYDPATPGNDIALLKLA---TPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSqsGTLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149  167 QRDRQClRIFGSYDPRRQICVGDRRERKAAFKGDSGGPLL----CNNVAHGIVSYGKSSGVP--PEVFTRVSSFLPWIRT 240
Cdd:COG5640 178 VSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIKS 256

                ....
gi 4503149  241 TMRS 244
Cdd:COG5640 257 TAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
39-218 5.22e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.82  E-value: 5.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149   39 QIQSPAGQSRCGGFLVREDFVLTAAHC--------WGSNINVTLGahniqRRENTQQHITARRAIRHPQYNQRT-IQNDI 109
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPG-----YNGGPYGTATATRFRVPPGWVASGdAGYDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503149  110 MLLQLSrrvrRNRNVNPVALP-RAQEGLRPGTLCTVAGWGrvsmrrgtdtlREVQLRVQRDRQClRIFGSYDPRRQI-Cv 187
Cdd:COG3591  79 ALLRLD----EPLGDTTGWLGlAFNDAPLAGEPVTIIGYP-----------GDRPKDLSLDCSG-RVTGVQGNRLSYdC- 141
                       170       180       190
                ....*....|....*....|....*....|....*
gi 4503149  188 gdrrerkAAFKGDSGGPLLCNNVAH----GIVSYG 218
Cdd:COG3591 142 -------DTTGGSSGSPVLDDSDGGgrvvGVHSAG 169
 
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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