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Conserved domains on  [gi|442618310|ref|NP_001097728|]
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uncharacterized protein Dmel_CG34409 [Drosophila melanogaster]

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 ...
252-501 4.06e-57

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: 189.79  E-value: 4.06e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 252 GGDQASAGQFPWLTRIAYRNRSssrisFRCSGSLISSNHIVTAAHCVVNlvSDLELSHVRLGSQD------GATPFAIEQ 325
Cdd:cd00190    3 GGSEAKIGSFPWQVSLQYTGGR-----HFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHDlssnegGGQVIKVKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 326 VIVHPNYDQPKYANDIALLRINS---TNGTFTPICLPfNGPITLGNrliGQIGVAAGWsiGSTENNSSmdpsnSTAGVRF 402
Cdd:cd00190   76 VIVHPNYNPSTYDNDIALLKLKRpvtLSDNVRPICLP-SSGYNLPA---GTTCTVSGW--GRTSEGGP-----LPDVLQE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 403 IRLPIVNTTSCAIAYaslsenfQQPIVITPNHLCAQGMPMN-DVCRGDSGGPFmddgtsgVFGTSGRYTIIGIVAFGPTl 481
Cdd:cd00190  145 VNVPIVSNAECKRAY-------SYGGTITDNMLCAGGLEGGkDACQGDSGGPL-------VCNDNGRGVLVGIVSWGSG- 209
                        250       260
                 ....*....|....*....|
gi 442618310 482 CGVTTIPGVYTLVSSFSDWI 501
Cdd:cd00190  210 CARPNYPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
252-501 4.06e-57

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: 189.79  E-value: 4.06e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 252 GGDQASAGQFPWLTRIAYRNRSssrisFRCSGSLISSNHIVTAAHCVVNlvSDLELSHVRLGSQD------GATPFAIEQ 325
Cdd:cd00190    3 GGSEAKIGSFPWQVSLQYTGGR-----HFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHDlssnegGGQVIKVKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 326 VIVHPNYDQPKYANDIALLRINS---TNGTFTPICLPfNGPITLGNrliGQIGVAAGWsiGSTENNSSmdpsnSTAGVRF 402
Cdd:cd00190   76 VIVHPNYNPSTYDNDIALLKLKRpvtLSDNVRPICLP-SSGYNLPA---GTTCTVSGW--GRTSEGGP-----LPDVLQE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 403 IRLPIVNTTSCAIAYaslsenfQQPIVITPNHLCAQGMPMN-DVCRGDSGGPFmddgtsgVFGTSGRYTIIGIVAFGPTl 481
Cdd:cd00190  145 VNVPIVSNAECKRAY-------SYGGTITDNMLCAGGLEGGkDACQGDSGGPL-------VCNDNGRGVLVGIVSWGSG- 209
                        250       260
                 ....*....|....*....|
gi 442618310 482 CGVTTIPGVYTLVSSFSDWI 501
Cdd:cd00190  210 CARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
249-501 2.32e-54

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: 182.49  E-value: 2.32e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310   249 RLLGGDQASAGQFPWLTRIAYRNRSssrisFRCSGSLISSNHIVTAAHCVVNlvSDLELSHVRLGSQD-----GATPFAI 323
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR-----HFCGGSLISPRWVLTAAHCVRG--SDPSNIRVRLGSHDlssgeEGQVIKV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310   324 EQVIVHPNYDQPKYANDIALLRINST---NGTFTPICLpfngPITLGNRLIGQIGVAAGWsiGSTENNSSMDPSNstagV 400
Cdd:smart00020  74 SKVIIHPNYNPSTYDNDIALLKLKEPvtlSDNVRPICL----PSSNYNVPAGTTCTVSGW--GRTSEGAGSLPDT----L 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310   401 RFIRLPIVNTTSCAIAYaslsenfQQPIVITPNHLCAQGMPMN-DVCRGDSGGPFMDDGtsgvfgtsGRYTIIGIVAFGP 479
Cdd:smart00020 144 QEVNVPIVSNATCRRAY-------SGGGAITDNMLCAGGLEGGkDACQGDSGGPLVCND--------GRWVLVGIVSWGS 208
                          250       260
                   ....*....|....*....|..
gi 442618310   480 TlCGVTTIPGVYTLVSSFSDWI 501
Cdd:smart00020 209 G-CARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
246-501 1.06e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 168.67  E-value: 1.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 246 VESRLLGGDQASAGQFPWLTRIAYRNrssSRISFRCSGSLISSNHIVTAAHCVVNL-VSDLelsHVRLGSQD----GATP 320
Cdd:COG5640   27 AAPAIVGGTPATVGEYPWMVALQSSN---GPSGQFCGGTLIAPRWVLTAAHCVDGDgPSDL---RVVIGSTDlstsGGTV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 321 FAIEQVIVHPNYDQPKYANDIALLRINSTNGTFTPICLPfngpiTLGNRL-IGQIGVAAGWsiGSTENNSSmdpsnSTAG 399
Cdd:COG5640  101 VKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLA-----TSADAAaPGTPATVAGW--GRTSEGPG-----SQSG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 400 V-RFIRLPIVNTTSCAiAYASlsenfqqpiVITPNHLCAQGM-PMNDVCRGDSGGPFmddgtsgVFGTSGRYTIIGIVAF 477
Cdd:COG5640  169 TlRKADVPVVSDATCA-AYGG---------FDGGTMLCAGYPeGGKDACQGDSGGPL-------VVKDGGGWVLVGVVSW 231
                        250       260
                 ....*....|....*....|....
gi 442618310 478 GPTLCGVTTiPGVYTLVSSFSDWI 501
Cdd:COG5640  232 GGGPCAAGY-PGVYTRVSAYRDWI 254
Trypsin pfam00089
Trypsin;
252-501 8.24e-43

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 151.44  E-value: 8.24e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310  252 GGDQASAGQFPWLTRIAYRNRSssrisFRCSGSLISSNHIVTAAHCVVNLVSDlelsHVRLG------SQDGATPFAIEQ 325
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSGK-----HFCGGSLISENWVLTAAHCVSGASDV----KVVLGahnivlREGGEQKFDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310  326 VIVHPNYDQPKYANDIALLRINST---NGTFTPICLPFNGPItlgnRLIGQIGVAAGWsiGSTENNSSMDPsnstagVRF 402
Cdd:pfam00089  74 IIVHPNYNPDTLDNDIALLKLESPvtlGDTVRPICLPDASSD----LPVGTTCTVSGW--GNTKTLGPSDT------LQE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310  403 IRLPIVNTTSCAIAYaslsenfqqPIVITPNHLCAqGMPMNDVCRGDSGGPFMDDGTsgvfgtsgryTIIGIVAFGPTlC 482
Cdd:pfam00089 142 VTVPVVSRETCRSAY---------GGTVTDTMICA-GAGGKDACQGDSGGPLVCSDG----------ELIGIVSWGYG-C 200
                         250
                  ....*....|....*....
gi 442618310  483 GVTTIPGVYTLVSSFSDWI 501
Cdd:pfam00089 201 ASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
252-501 4.06e-57

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: 189.79  E-value: 4.06e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 252 GGDQASAGQFPWLTRIAYRNRSssrisFRCSGSLISSNHIVTAAHCVVNlvSDLELSHVRLGSQD------GATPFAIEQ 325
Cdd:cd00190    3 GGSEAKIGSFPWQVSLQYTGGR-----HFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHDlssnegGGQVIKVKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 326 VIVHPNYDQPKYANDIALLRINS---TNGTFTPICLPfNGPITLGNrliGQIGVAAGWsiGSTENNSSmdpsnSTAGVRF 402
Cdd:cd00190   76 VIVHPNYNPSTYDNDIALLKLKRpvtLSDNVRPICLP-SSGYNLPA---GTTCTVSGW--GRTSEGGP-----LPDVLQE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 403 IRLPIVNTTSCAIAYaslsenfQQPIVITPNHLCAQGMPMN-DVCRGDSGGPFmddgtsgVFGTSGRYTIIGIVAFGPTl 481
Cdd:cd00190  145 VNVPIVSNAECKRAY-------SYGGTITDNMLCAGGLEGGkDACQGDSGGPL-------VCNDNGRGVLVGIVSWGSG- 209
                        250       260
                 ....*....|....*....|
gi 442618310 482 CGVTTIPGVYTLVSSFSDWI 501
Cdd:cd00190  210 CARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
249-501 2.32e-54

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: 182.49  E-value: 2.32e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310   249 RLLGGDQASAGQFPWLTRIAYRNRSssrisFRCSGSLISSNHIVTAAHCVVNlvSDLELSHVRLGSQD-----GATPFAI 323
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR-----HFCGGSLISPRWVLTAAHCVRG--SDPSNIRVRLGSHDlssgeEGQVIKV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310   324 EQVIVHPNYDQPKYANDIALLRINST---NGTFTPICLpfngPITLGNRLIGQIGVAAGWsiGSTENNSSMDPSNstagV 400
Cdd:smart00020  74 SKVIIHPNYNPSTYDNDIALLKLKEPvtlSDNVRPICL----PSSNYNVPAGTTCTVSGW--GRTSEGAGSLPDT----L 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310   401 RFIRLPIVNTTSCAIAYaslsenfQQPIVITPNHLCAQGMPMN-DVCRGDSGGPFMDDGtsgvfgtsGRYTIIGIVAFGP 479
Cdd:smart00020 144 QEVNVPIVSNATCRRAY-------SGGGAITDNMLCAGGLEGGkDACQGDSGGPLVCND--------GRWVLVGIVSWGS 208
                          250       260
                   ....*....|....*....|..
gi 442618310   480 TlCGVTTIPGVYTLVSSFSDWI 501
Cdd:smart00020 209 G-CARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
246-501 1.06e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 168.67  E-value: 1.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 246 VESRLLGGDQASAGQFPWLTRIAYRNrssSRISFRCSGSLISSNHIVTAAHCVVNL-VSDLelsHVRLGSQD----GATP 320
Cdd:COG5640   27 AAPAIVGGTPATVGEYPWMVALQSSN---GPSGQFCGGTLIAPRWVLTAAHCVDGDgPSDL---RVVIGSTDlstsGGTV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 321 FAIEQVIVHPNYDQPKYANDIALLRINSTNGTFTPICLPfngpiTLGNRL-IGQIGVAAGWsiGSTENNSSmdpsnSTAG 399
Cdd:COG5640  101 VKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLA-----TSADAAaPGTPATVAGW--GRTSEGPG-----SQSG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 400 V-RFIRLPIVNTTSCAiAYASlsenfqqpiVITPNHLCAQGM-PMNDVCRGDSGGPFmddgtsgVFGTSGRYTIIGIVAF 477
Cdd:COG5640  169 TlRKADVPVVSDATCA-AYGG---------FDGGTMLCAGYPeGGKDACQGDSGGPL-------VVKDGGGWVLVGVVSW 231
                        250       260
                 ....*....|....*....|....
gi 442618310 478 GPTLCGVTTiPGVYTLVSSFSDWI 501
Cdd:COG5640  232 GGGPCAAGY-PGVYTRVSAYRDWI 254
Trypsin pfam00089
Trypsin;
252-501 8.24e-43

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 151.44  E-value: 8.24e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310  252 GGDQASAGQFPWLTRIAYRNRSssrisFRCSGSLISSNHIVTAAHCVVNLVSDlelsHVRLG------SQDGATPFAIEQ 325
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSGK-----HFCGGSLISENWVLTAAHCVSGASDV----KVVLGahnivlREGGEQKFDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310  326 VIVHPNYDQPKYANDIALLRINST---NGTFTPICLPFNGPItlgnRLIGQIGVAAGWsiGSTENNSSMDPsnstagVRF 402
Cdd:pfam00089  74 IIVHPNYNPDTLDNDIALLKLESPvtlGDTVRPICLPDASSD----LPVGTTCTVSGW--GNTKTLGPSDT------LQE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310  403 IRLPIVNTTSCAIAYaslsenfqqPIVITPNHLCAqGMPMNDVCRGDSGGPFMDDGTsgvfgtsgryTIIGIVAFGPTlC 482
Cdd:pfam00089 142 VTVPVVSRETCRSAY---------GGTVTDTMICA-GAGGKDACQGDSGGPLVCSDG----------ELIGIVSWGYG-C 200
                         250
                  ....*....|....*....
gi 442618310  483 GVTTIPGVYTLVSSFSDWI 501
Cdd:pfam00089 201 ASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
278-503 6.18e-13

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 67.39  E-value: 6.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 278 SFRCSGSLISSNHIVTAAHCVVNLVSDLELS--HVRLGSQDG-ATPFAIEQVIVHPNYDQ-PKYANDIALLRIN-STNGT 352
Cdd:COG3591   11 GGVCTGTLIGPNLVLTAGHCVYDGAGGGWATniVFVPGYNGGpYGTATATRFRVPPGWVAsGDAGYDYALLRLDePLGDT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310 353 FTPICLPFNGPITLGNRlIGQIGVAAGWSigsteNNSSMDpsnstagvrfirlpivntTSCAIayASLSENFQQpivitp 432
Cdd:COG3591   91 TGWLGLAFNDAPLAGEP-VTIIGYPGDRP-----KDLSLD------------------CSGRV--TGVQGNRLS------ 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442618310 433 nHLCaqgmpmnDVCRGDSGGPFMDDgtsgvfgTSGRYTIIGIVAFGPTLCGVTTIPGVYTLVSSFSDWILR 503
Cdd:COG3591  139 -YDC-------DTTGGSSGSPVLDD-------SDGGGRVVGVHSAGGADRANTGVRLTSAIVAALRAWASA 194
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
281-386 1.35e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 39.33  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618310  281 CSGSLISSN-HIVTAAHcVVNLVSDLELSHVRLGSQDGaTPFAIEQVIVHPNYdqpkyanDIALLRINSTNGTFtpiclp 359
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAH-VVDDAEEAAVELVSVVLADG-REYPATVVARDPDL-------DLALLRVSGDGRGL------ 65
                          90       100       110
                  ....*....|....*....|....*....|
gi 442618310  360 fnGPITLGNRLIGQIG---VAAGWSIGSTE 386
Cdd:pfam13365  66 --PPLPLGDSEPLVGGervYAVGYPLGGEK 93
 
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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