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Conserved domains on  [gi|2738867|gb|AAB94559|]
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hemocyte protease-3 [Manduca sexta]

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 ...
31-250 1.30e-91

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: 269.92  E-value: 1.30e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867   31 IYGGHDISIEQAPFMASLRLNGTDHYCGASVIHERFILTAAHCIL--PDRKYTVQVGTTYAN---DGGQVYDVEKIMKHE 105
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSsneGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867  106 MYNYTTHDYDICLIKLKTNLTFSAKVNKIDLADRSVRLKQNIQVEVTGWGATSADGDISNNLQQVTIPIISTFSCCLKYL 185
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2738867  186 KvRHAITSRMFCAG--EQGKDSCQGDSGGPLTLN----NVQVGVTSFGSGCGK--LPGVYTKISAMLPWINDN 250
Cdd:cd00190 161 Y-GGTITDNMLCAGglEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpnYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-250 1.30e-91

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: 269.92  E-value: 1.30e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867   31 IYGGHDISIEQAPFMASLRLNGTDHYCGASVIHERFILTAAHCIL--PDRKYTVQVGTTYAN---DGGQVYDVEKIMKHE 105
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSsneGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867  106 MYNYTTHDYDICLIKLKTNLTFSAKVNKIDLADRSVRLKQNIQVEVTGWGATSADGDISNNLQQVTIPIISTFSCCLKYL 185
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2738867  186 KvRHAITSRMFCAG--EQGKDSCQGDSGGPLTLN----NVQVGVTSFGSGCGK--LPGVYTKISAMLPWINDN 250
Cdd:cd00190 161 Y-GGTITDNMLCAGglEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpnYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-247 1.49e-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: 266.85  E-value: 1.49e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867      31 IYGGHDISIEQAPFMASLRLNGTDHYCGASVIHERFILTAAHCIL--PDRKYTVQVGTTYANDGG--QVYDVEKIMKHEM 106
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsDPSNIRVRLGSHDLSSGEegQVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867     107 YNYTTHDYDICLIKLKTNLTFSAKVNKIDLADRSVRLKQNIQVEVTGWGATS-ADGDISNNLQQVTIPIISTFScCLKYL 185
Cdd:smart00020  82 YNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNAT-CRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2738867     186 KVRHAITSRMFCAG--EQGKDSCQGDSGGPLTLNN---VQVGVTSFGSGCGK--LPGVYTKISAMLPWI 247
Cdd:smart00020 161 SGGGAITDNMLCAGglEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGCARpgKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
7-254 1.98e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.51  E-value: 1.98e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867    7 LIVVFAGLITIALGLDAASVNNVG--IYGGHDISIEQAPFMASL-RLNGTD-HYCGASVIHERFILTAAHCILPDR--KY 80
Cdd:COG5640   5 RLLAALAAAALALALAAAPAADAApaIVGGTPATVGEYPWMVALqSSNGPSgQFCGGTLIAPRWVLTAAHCVDGDGpsDL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867   81 TVQVGTT-YANDGGQVYDVEKIMKHEMYNYTTHDYDICLIKLKTNLTFSAkvnKIDLADRSVRLKQNIQVEVTGWGATSA 159
Cdd:COG5640  85 RVVIGSTdLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867  160 D-GDISNNLQQVTIPIISTFSCclkyLKVRHAITSRMFCAG--EQGKDSCQGDSGGPLTLNN----VQVGVTSFGSG-C- 230
Cdd:COG5640 162 GpGSQSGTLRKADVPVVSDATC----AAYGGFDGGTMLCAGypEGGKDACQGDSGGPLVVKDgggwVLVGVVSWGGGpCa 237
                       250       260
                ....*....|....*....|....
gi 2738867  231 GKLPGVYTKISAMLPWINDNIKKN 254
Cdd:COG5640 238 AGYPGVYTRVSAYRDWIKSTAGGL 261
Trypsin pfam00089
Trypsin;
31-247 5.90e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 204.21  E-value: 5.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867     31 IYGGHDISIEQAPFMASLRLNGTDHYCGASVIHERFILTAAHCILPDRKYTVQVGTT---YANDGGQVYDVEKIMKHEMY 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHnivLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867    108 NYTTHDYDICLIKLKTNLTFSAKVNKIDLADRSVRLKQNIQVEVTGWGATSADGdISNNLQQVTIPIISTFSCCLKYlkv 187
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAY--- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2738867    188 RHAITSRMFCAGEQGKDSCQGDSGGPL-TLNNVQVGVTSFGSGC--GKLPGVYTKISAMLPWI 247
Cdd:pfam00089 157 GGTVTDTMICAGAGGKDACQGDSGGPLvCSDGELIGIVSWGYGCasGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-250 1.30e-91

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: 269.92  E-value: 1.30e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867   31 IYGGHDISIEQAPFMASLRLNGTDHYCGASVIHERFILTAAHCIL--PDRKYTVQVGTTYAN---DGGQVYDVEKIMKHE 105
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSsneGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867  106 MYNYTTHDYDICLIKLKTNLTFSAKVNKIDLADRSVRLKQNIQVEVTGWGATSADGDISNNLQQVTIPIISTFSCCLKYL 185
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2738867  186 KvRHAITSRMFCAG--EQGKDSCQGDSGGPLTLN----NVQVGVTSFGSGCGK--LPGVYTKISAMLPWINDN 250
Cdd:cd00190 161 Y-GGTITDNMLCAGglEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpnYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-247 1.49e-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: 266.85  E-value: 1.49e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867      31 IYGGHDISIEQAPFMASLRLNGTDHYCGASVIHERFILTAAHCIL--PDRKYTVQVGTTYANDGG--QVYDVEKIMKHEM 106
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsDPSNIRVRLGSHDLSSGEegQVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867     107 YNYTTHDYDICLIKLKTNLTFSAKVNKIDLADRSVRLKQNIQVEVTGWGATS-ADGDISNNLQQVTIPIISTFScCLKYL 185
Cdd:smart00020  82 YNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNAT-CRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2738867     186 KVRHAITSRMFCAG--EQGKDSCQGDSGGPLTLNN---VQVGVTSFGSGCGK--LPGVYTKISAMLPWI 247
Cdd:smart00020 161 SGGGAITDNMLCAGglEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGCARpgKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
7-254 1.98e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.51  E-value: 1.98e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867    7 LIVVFAGLITIALGLDAASVNNVG--IYGGHDISIEQAPFMASL-RLNGTD-HYCGASVIHERFILTAAHCILPDR--KY 80
Cdd:COG5640   5 RLLAALAAAALALALAAAPAADAApaIVGGTPATVGEYPWMVALqSSNGPSgQFCGGTLIAPRWVLTAAHCVDGDGpsDL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867   81 TVQVGTT-YANDGGQVYDVEKIMKHEMYNYTTHDYDICLIKLKTNLTFSAkvnKIDLADRSVRLKQNIQVEVTGWGATSA 159
Cdd:COG5640  85 RVVIGSTdLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867  160 D-GDISNNLQQVTIPIISTFSCclkyLKVRHAITSRMFCAG--EQGKDSCQGDSGGPLTLNN----VQVGVTSFGSG-C- 230
Cdd:COG5640 162 GpGSQSGTLRKADVPVVSDATC----AAYGGFDGGTMLCAGypEGGKDACQGDSGGPLVVKDgggwVLVGVVSWGGGpCa 237
                       250       260
                ....*....|....*....|....
gi 2738867  231 GKLPGVYTKISAMLPWINDNIKKN 254
Cdd:COG5640 238 AGYPGVYTRVSAYRDWIKSTAGGL 261
Trypsin pfam00089
Trypsin;
31-247 5.90e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 204.21  E-value: 5.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867     31 IYGGHDISIEQAPFMASLRLNGTDHYCGASVIHERFILTAAHCILPDRKYTVQVGTT---YANDGGQVYDVEKIMKHEMY 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHnivLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867    108 NYTTHDYDICLIKLKTNLTFSAKVNKIDLADRSVRLKQNIQVEVTGWGATSADGdISNNLQQVTIPIISTFSCCLKYlkv 187
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAY--- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2738867    188 RHAITSRMFCAGEQGKDSCQGDSGGPL-TLNNVQVGVTSFGSGC--GKLPGVYTKISAMLPWI 247
Cdd:pfam00089 157 GGTVTDTMICAGAGGKDACQGDSGGPLvCSDGELIGIVSWGYGCasGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
48-237 7.77e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.44  E-value: 7.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867   48 LRLNGTDHYCGASVIHERFILTAAHCILPDRKYTVQVGTT----YANDGGQVYDVEKIMKHEMYNYTTH-DYDICLIKLK 122
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVfvpgYNGGPYGTATATRFRVPPGWVASGDaGYDYALLRLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738867  123 TNLTFSAKVNKIDLADRSVRlkqNIQVEVTGWGatsADGDISNNLQQvtipiistfSCclkylKVRHAITSRMF--Cage 200
Cdd:COG3591  85 EPLGDTTGWLGLAFNDAPLA---GEPVTIIGYP---GDRPKDLSLDC---------SG-----RVTGVQGNRLSydC--- 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 2738867  201 qgkDSCQGDSGGPL----TLNNVQVGVTSFGSGCGKLPGVY 237
Cdd:COG3591 142 ---DTTGGSSGSPVlddsDGGGRVVGVHSAGGADRANTGVR 179
 
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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