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Conserved domains on  [gi|24582982|ref|NP_523518|]
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trypsin 29F, isoform C [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 ...
42-264 3.15e-99

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: 289.56  E-value: 3.15e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982  42 IVGGQVANIKDIPYQVSLQRS--YHFCGGSLIAQGWVLTAAHCTEGSAILLSKVRIGSSRTSV---GGQLVGIKRVHRHP 116
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTggRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982 117 KFDAYTIDFDFSLLELEEYSAKNVTQAFVGLPEQDADIADGTPVLVSGWGNTQSAQETSAVLRSVTVPKVSQTQCTEAYG 196
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582982 197 NFGSITDRMLCAGLPEGGKDACQGDSGGPLAAD----GVLWGVVSWGYGCARPNYPGVYSRVSAVRDWISSV 264
Cdd:cd00190 161 YGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-264 3.15e-99

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: 289.56  E-value: 3.15e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982  42 IVGGQVANIKDIPYQVSLQRS--YHFCGGSLIAQGWVLTAAHCTEGSAILLSKVRIGSSRTSV---GGQLVGIKRVHRHP 116
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTggRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982 117 KFDAYTIDFDFSLLELEEYSAKNVTQAFVGLPEQDADIADGTPVLVSGWGNTQSAQETSAVLRSVTVPKVSQTQCTEAYG 196
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582982 197 NFGSITDRMLCAGLPEGGKDACQGDSGGPLAAD----GVLWGVVSWGYGCARPNYPGVYSRVSAVRDWISSV 264
Cdd:cd00190 161 YGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
41-261 1.06e-97

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: 285.73  E-value: 1.06e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982     41 RIVGGQVANIKDIPYQVSLQRS--YHFCGGSLIAQGWVLTAAHCTEGSAILLSKVRIGSSRTSVGG--QLVGIKRVHRHP 116
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGggRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEegQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982    117 KFDAYTIDFDFSLLELEEYSAKNVTQAFVGLPEQDADIADGTPVLVSGWGNTQSAQET-SAVLRSVTVPKVSQTQCTEAY 195
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582982    196 GNFGSITDRMLCAGLPEGGKDACQGDSGGPLAAD---GVLWGVVSWGYGCARPNYPGVYSRVSAVRDWI 261
Cdd:smart00020 161 SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
17-266 8.90e-76

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 231.08  E-value: 8.90e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982  17 LFIGGILLVNLSLG-ATVRRPRLDGRIVGGQVANIKDIPYQVSLQRS----YHFCGGSLIAQGWVLTAAHCTEGSAILLS 91
Cdd:COG5640   5 RLLAALAAAALALAlAAAPAADAAPAIVGGTPATVGEYPWMVALQSSngpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982  92 KVRIGS-SRTSVGGQLVGIKRVHRHPKFDAYTIDFDFSLLELEEySAKNVtqAFVGLPEQDADIADGTPVLVSGWGNTQS 170
Cdd:COG5640  85 RVVIGStDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLAT-PVPGV--APAPLATSADAAAPGTPATVAGWGRTSE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982 171 AQ-ETSAVLRSVTVPKVSQTQCTeAYGNFgsITDRMLCAGLPEGGKDACQGDSGGPL----AADGVLWGVVSWGYGCARP 245
Cdd:COG5640 162 GPgSQSGTLRKADVPVVSDATCA-AYGGF--DGGTMLCAGYPEGGKDACQGDSGGPLvvkdGGGWVLVGVVSWGGGPCAA 238
                       250       260
                ....*....|....*....|.
gi 24582982 246 NYPGVYSRVSAVRDWISSVSG 266
Cdd:COG5640 239 GYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
42-261 3.06e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 215.38  E-value: 3.06e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982    42 IVGGQVANIKDIPYQVSLQRS--YHFCGGSLIAQGWVLTAAHCTEGSAILlsKVRIGSSRTSV---GGQLVGIKRVHRHP 116
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsgKHFCGGSLISENWVLTAAHCVSGASDV--KVVLGAHNIVLregGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982   117 KFDAYTIDFDFSLLELEEYSAKNVTQAFVGLPEQDADIADGTPVLVSGWGNTqSAQETSAVLRSVTVPKVSQTQCTEAYG 196
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNT-KTLGPSDTLQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582982   197 nfGSITDRMLCAGlpEGGKDACQGDSGGPL-AADGVLWGVVSWGYGCARPNYPGVYSRVSAVRDWI 261
Cdd:pfam00089 158 --GTVTDTMICAG--AGGKDACQGDSGGPLvCSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-264 3.15e-99

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: 289.56  E-value: 3.15e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982  42 IVGGQVANIKDIPYQVSLQRS--YHFCGGSLIAQGWVLTAAHCTEGSAILLSKVRIGSSRTSV---GGQLVGIKRVHRHP 116
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTggRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982 117 KFDAYTIDFDFSLLELEEYSAKNVTQAFVGLPEQDADIADGTPVLVSGWGNTQSAQETSAVLRSVTVPKVSQTQCTEAYG 196
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582982 197 NFGSITDRMLCAGLPEGGKDACQGDSGGPLAAD----GVLWGVVSWGYGCARPNYPGVYSRVSAVRDWISSV 264
Cdd:cd00190 161 YGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
41-261 1.06e-97

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: 285.73  E-value: 1.06e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982     41 RIVGGQVANIKDIPYQVSLQRS--YHFCGGSLIAQGWVLTAAHCTEGSAILLSKVRIGSSRTSVGG--QLVGIKRVHRHP 116
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGggRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEegQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982    117 KFDAYTIDFDFSLLELEEYSAKNVTQAFVGLPEQDADIADGTPVLVSGWGNTQSAQET-SAVLRSVTVPKVSQTQCTEAY 195
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582982    196 GNFGSITDRMLCAGLPEGGKDACQGDSGGPLAAD---GVLWGVVSWGYGCARPNYPGVYSRVSAVRDWI 261
Cdd:smart00020 161 SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
17-266 8.90e-76

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 231.08  E-value: 8.90e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982  17 LFIGGILLVNLSLG-ATVRRPRLDGRIVGGQVANIKDIPYQVSLQRS----YHFCGGSLIAQGWVLTAAHCTEGSAILLS 91
Cdd:COG5640   5 RLLAALAAAALALAlAAAPAADAAPAIVGGTPATVGEYPWMVALQSSngpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982  92 KVRIGS-SRTSVGGQLVGIKRVHRHPKFDAYTIDFDFSLLELEEySAKNVtqAFVGLPEQDADIADGTPVLVSGWGNTQS 170
Cdd:COG5640  85 RVVIGStDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLAT-PVPGV--APAPLATSADAAAPGTPATVAGWGRTSE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982 171 AQ-ETSAVLRSVTVPKVSQTQCTeAYGNFgsITDRMLCAGLPEGGKDACQGDSGGPL----AADGVLWGVVSWGYGCARP 245
Cdd:COG5640 162 GPgSQSGTLRKADVPVVSDATCA-AYGGF--DGGTMLCAGYPEGGKDACQGDSGGPLvvkdGGGWVLVGVVSWGGGPCAA 238
                       250       260
                ....*....|....*....|.
gi 24582982 246 NYPGVYSRVSAVRDWISSVSG 266
Cdd:COG5640 239 GYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
42-261 3.06e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 215.38  E-value: 3.06e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982    42 IVGGQVANIKDIPYQVSLQRS--YHFCGGSLIAQGWVLTAAHCTEGSAILlsKVRIGSSRTSV---GGQLVGIKRVHRHP 116
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsgKHFCGGSLISENWVLTAAHCVSGASDV--KVVLGAHNIVLregGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982   117 KFDAYTIDFDFSLLELEEYSAKNVTQAFVGLPEQDADIADGTPVLVSGWGNTqSAQETSAVLRSVTVPKVSQTQCTEAYG 196
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNT-KTLGPSDTLQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582982   197 nfGSITDRMLCAGlpEGGKDACQGDSGGPL-AADGVLWGVVSWGYGCARPNYPGVYSRVSAVRDWI 261
Cdd:pfam00089 158 --GTVTDTMICAG--AGGKDACQGDSGGPLvCSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
56-263 3.27e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 52.37  E-value: 3.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982  56 QVSLQRSYHFCGGSLIAQGWVLTAAHC--TEGSAILLSKVRIGSSRTSVGGQLVGIKRVHRHPKFDAYT-IDFDFSLLEL 132
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCvyDGAGGGWATNIVFVPGYNGGPYGTATATRFRVPPGWVASGdAGYDYALLRL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582982 133 EEysakNVTQAFVGLP-EQDADIADGTPVLVSGWGNTQsaqetsavlrsvtvPKVSQTQCTeayGNFGSITDRMLCAGLp 211
Cdd:COG3591  84 DE----PLGDTTGWLGlAFNDAPLAGEPVTIIGYPGDR--------------PKDLSLDCS---GRVTGVQGNRLSYDC- 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24582982 212 eggkDACQGDSGGP-LAADGVLW---GVVSWGYGcARPNYpGVY---SRVSAVRDWISS 263
Cdd:COG3591 142 ----DTTGGSSGSPvLDDSDGGGrvvGVHSAGGA-DRANT-GVRltsAIVAALRAWASA 194
 
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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