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Conserved domains on  [gi|17986193|ref|NP_524555|]
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jonah 99Ci [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

 Zoom to residue level

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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 ...
41-266 4.27e-61

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: 192.88  E-value: 4.27e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193  41 ITNGNLASEGQVPYIVgvSLNSNGNWWWCGGSIIGHTWVLTAAHCTAGADEASL--YYGAVNYNEP-AFRHTVSSENFIR 117
Cdd:cd00190   1 IVGGSEAKIGSFPWQV--SLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYtvRLGSHDLSSNeGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193 118 YPHYVG--LDHDLALIKTPHVDFYSL-VNKIELPSLDdrYNSYENNWVQAAGWGAIYDGSNVVEDLRVVDLKVISVAECQ 194
Cdd:cd00190  79 HPNYNPstYDNDIALLKLKRPVTLSDnVRPICLPSSG--YNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17986193 195 -AYYGTDTASENTICVETPD-GKATCQGDSGGPLVTKEGDK--LIGITSFVsaYGC-QVGGPAGFTRVTKYLEWIKE 266
Cdd:cd00190 157 rAYSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRgvLVGIVSWG--SGCaRPNYPGVYTRVSSYLDWIQK 231
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
41-266 4.27e-61

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: 192.88  E-value: 4.27e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193  41 ITNGNLASEGQVPYIVgvSLNSNGNWWWCGGSIIGHTWVLTAAHCTAGADEASL--YYGAVNYNEP-AFRHTVSSENFIR 117
Cdd:cd00190   1 IVGGSEAKIGSFPWQV--SLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYtvRLGSHDLSSNeGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193 118 YPHYVG--LDHDLALIKTPHVDFYSL-VNKIELPSLDdrYNSYENNWVQAAGWGAIYDGSNVVEDLRVVDLKVISVAECQ 194
Cdd:cd00190  79 HPNYNPstYDNDIALLKLKRPVTLSDnVRPICLPSSG--YNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17986193 195 -AYYGTDTASENTICVETPD-GKATCQGDSGGPLVTKEGDK--LIGITSFVsaYGC-QVGGPAGFTRVTKYLEWIKE 266
Cdd:cd00190 157 rAYSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRgvLVGIVSWG--SGCaRPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
40-264 8.36e-60

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: 189.43  E-value: 8.36e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193     40 RITNGNLASEGQVPYIVgvSLNSNGNWWWCGGSIIGHTWVLTAAHCTAGADEASL--YYGAVNYNEPAFRHTVSSENFIR 117
Cdd:smart00020   1 RIVGGSEANIGSFPWQV--SLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIrvRLGSHDLSSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193    118 YPHY--VGLDHDLALIK-TPHVDFYSLVNKIELPSldDRYNSYENNWVQAAGWGAIYDGSNVV-EDLRVVDLKVISVAEC 193
Cdd:smart00020  79 HPNYnpSTYDNDIALLKlKEPVTLSDNVRPICLPS--SNYNVPAGTTCTVSGWGRTSEGAGSLpDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17986193    194 Q-AYYGTDTASENTICVETPD-GKATCQGDSGGPLVTKEGD-KLIGITSFVsaYGC-QVGGPAGFTRVTKYLEWI 264
Cdd:smart00020 157 RrAYSGGGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDGRwVLVGIVSWG--SGCaRPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-269 2.47e-51

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 168.67  E-value: 2.47e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193   1 MRgLTLLSLAFLGVCSALTVPHSLVhprdleirhGGIEGRITNGNLASEGQVPYIVGVSLNSNGNWWWCGGSIIGHTWVL 80
Cdd:COG5640   1 MR-RRRLLAALAAAALALALAAAPA---------ADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193  81 TAAHCTAG--ADEASLYYGAVNYN-EPAFRHTVSSenFIRYPHYVG--LDHDLALIK--TPhvdfYSLVNKIELPSLDDr 153
Cdd:COG5640  71 TAAHCVDGdgPSDLRVVIGSTDLStSGGTVVKVAR--IVVHPDYDPatPGNDIALLKlaTP----VPGVAPAPLATSAD- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193 154 yNSYENNWVQAAGWGAIYDGSNVV-EDLRVVDLKVISVAECQAYYGTDTASEntICVETPDG-KATCQGDSGGPLVTKEG 231
Cdd:COG5640 144 -AAAPGTPATVAGWGRTSEGPGSQsGTLRKADVPVVSDATCAAYGGFDGGTM--LCAGYPEGgKDACQGDSGGPLVVKDG 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17986193 232 D--KLIGITSFVSAyGCQVGGPAGFTRVTKYLEWIKEETG 269
Cdd:COG5640 221 GgwVLVGVVSWGGG-PCAAGYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
41-264 1.63e-42

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 144.51  E-value: 1.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193    41 ITNGNLASEGQVPYIVGVSLNSNGnwWWCGGSIIGHTWVLTAAHCTAGADEASLYYGA--VNYNEPAFRHtVSSENFIRY 118
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK--HFCGGSLISENWVLTAAHCVSGASDVKVVLGAhnIVLREGGEQK-FDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193   119 PHY--VGLDHDLALIKTPH-VDFYSLVNKIELPSLDDRYNsyENNWVQAAGWGAIYDGsNVVEDLRVVDLKVISVAECQA 195
Cdd:pfam00089  78 PNYnpDTLDNDIALLKLESpVTLGDTVRPICLPDASSDLP--VGTTCTVSGWGNTKTL-GPSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193   196 YYGTDTaSENTICVEtPDGKATCQGDSGGPLVTKEGdKLIGITSFVsaYGCQVGG-PAGFTRVTKYLEWI 264
Cdd:pfam00089 155 AYGGTV-TDTMICAG-AGGKDACQGDSGGPLVCSDG-ELIGIVSWG--YGCASGNyPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
41-266 4.27e-61

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: 192.88  E-value: 4.27e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193  41 ITNGNLASEGQVPYIVgvSLNSNGNWWWCGGSIIGHTWVLTAAHCTAGADEASL--YYGAVNYNEP-AFRHTVSSENFIR 117
Cdd:cd00190   1 IVGGSEAKIGSFPWQV--SLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYtvRLGSHDLSSNeGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193 118 YPHYVG--LDHDLALIKTPHVDFYSL-VNKIELPSLDdrYNSYENNWVQAAGWGAIYDGSNVVEDLRVVDLKVISVAECQ 194
Cdd:cd00190  79 HPNYNPstYDNDIALLKLKRPVTLSDnVRPICLPSSG--YNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17986193 195 -AYYGTDTASENTICVETPD-GKATCQGDSGGPLVTKEGDK--LIGITSFVsaYGC-QVGGPAGFTRVTKYLEWIKE 266
Cdd:cd00190 157 rAYSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRgvLVGIVSWG--SGCaRPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
40-264 8.36e-60

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: 189.43  E-value: 8.36e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193     40 RITNGNLASEGQVPYIVgvSLNSNGNWWWCGGSIIGHTWVLTAAHCTAGADEASL--YYGAVNYNEPAFRHTVSSENFIR 117
Cdd:smart00020   1 RIVGGSEANIGSFPWQV--SLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIrvRLGSHDLSSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193    118 YPHY--VGLDHDLALIK-TPHVDFYSLVNKIELPSldDRYNSYENNWVQAAGWGAIYDGSNVV-EDLRVVDLKVISVAEC 193
Cdd:smart00020  79 HPNYnpSTYDNDIALLKlKEPVTLSDNVRPICLPS--SNYNVPAGTTCTVSGWGRTSEGAGSLpDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17986193    194 Q-AYYGTDTASENTICVETPD-GKATCQGDSGGPLVTKEGD-KLIGITSFVsaYGC-QVGGPAGFTRVTKYLEWI 264
Cdd:smart00020 157 RrAYSGGGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDGRwVLVGIVSWG--SGCaRPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-269 2.47e-51

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 168.67  E-value: 2.47e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193   1 MRgLTLLSLAFLGVCSALTVPHSLVhprdleirhGGIEGRITNGNLASEGQVPYIVGVSLNSNGNWWWCGGSIIGHTWVL 80
Cdd:COG5640   1 MR-RRRLLAALAAAALALALAAAPA---------ADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193  81 TAAHCTAG--ADEASLYYGAVNYN-EPAFRHTVSSenFIRYPHYVG--LDHDLALIK--TPhvdfYSLVNKIELPSLDDr 153
Cdd:COG5640  71 TAAHCVDGdgPSDLRVVIGSTDLStSGGTVVKVAR--IVVHPDYDPatPGNDIALLKlaTP----VPGVAPAPLATSAD- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193 154 yNSYENNWVQAAGWGAIYDGSNVV-EDLRVVDLKVISVAECQAYYGTDTASEntICVETPDG-KATCQGDSGGPLVTKEG 231
Cdd:COG5640 144 -AAAPGTPATVAGWGRTSEGPGSQsGTLRKADVPVVSDATCAAYGGFDGGTM--LCAGYPEGgKDACQGDSGGPLVVKDG 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17986193 232 D--KLIGITSFVSAyGCQVGGPAGFTRVTKYLEWIKEETG 269
Cdd:COG5640 221 GgwVLVGVVSWGGG-PCAAGYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
41-264 1.63e-42

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 144.51  E-value: 1.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193    41 ITNGNLASEGQVPYIVGVSLNSNGnwWWCGGSIIGHTWVLTAAHCTAGADEASLYYGA--VNYNEPAFRHtVSSENFIRY 118
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK--HFCGGSLISENWVLTAAHCVSGASDVKVVLGAhnIVLREGGEQK-FDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193   119 PHY--VGLDHDLALIKTPH-VDFYSLVNKIELPSLDDRYNsyENNWVQAAGWGAIYDGsNVVEDLRVVDLKVISVAECQA 195
Cdd:pfam00089  78 PNYnpDTLDNDIALLKLESpVTLGDTVRPICLPDASSDLP--VGTTCTVSGWGNTKTL-GPSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193   196 YYGTDTaSENTICVEtPDGKATCQGDSGGPLVTKEGdKLIGITSFVsaYGCQVGG-PAGFTRVTKYLEWI 264
Cdd:pfam00089 155 AYGGTV-TDTMICAG-AGGKDACQGDSGGPLVCSDG-ELIGIVSWG--YGCASGNyPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
60-240 1.10e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.05  E-value: 1.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193  60 LNSNGNWWWCGGSIIGHTWVLTAAHCTAGADEASLYYGAV---NYNEPAFRHTVSSENFI--RYPHYVGLDHDLALIKTP 134
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVfvpGYNGGPYGTATATRFRVppGWVASGDAGYDYALLRLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193 135 HvdfySLVNKIELPSLDDRYNSYENNWVQAAGWGAIYDGSNVVEDlrvvDLKVISVAECQAYYGTDtasenticvetpdg 214
Cdd:COG3591  85 E----PLGDTTGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLSLDC----SGRVTGVQGNRLSYDCD-------------- 142
                       170       180
                ....*....|....*....|....*...
gi 17986193 215 kaTCQGDSGGPLVTKEGD--KLIGITSF 240
Cdd:COG3591 143 --TTGGSSGSPVLDDSDGggRVVGVHSA 168
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
71-237 1.72e-04

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 40.87  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193    71 GSIIGHT-WVLTAAHCTAGADEASLYYGAVnynepafrHTVSSENFIRYPHYVGLDHDLALIKTPHVDfyslvNKIELPS 149
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVELVSV--------VLADGREYPATVVARDPDLDLALLRVSGDG-----RGLPPLP 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17986193   150 LDDRYNSYENNWVQAAGWGAIYDGSNVVEDlRVVDL-KVISVAECQAYYGTDTASENticvetpdgkatcqGDSGGPLVT 228
Cdd:pfam13365  70 LGDSEPLVGGERVYAVGYPLGGEKLSLSEG-IVSGVdEGRDGGDDGRVIQTDAALSP--------------GSSGGPVFD 134

                  ....*....
gi 17986193   229 KEGdKLIGI 237
Cdd:pfam13365 135 ADG-RVVGI 142
 
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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