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Conserved domains on  [gi|24667782|ref|NP_649270.1|]
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seminase [Drosophila melanogaster]

Protein Classification

serine protease (domain architecture ID 12184331)

trypsin-like serine protease such as snake venom serine proteases and trypsin, which preferentially cleaves peptide bonds after arginine and lysine residues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
43-263 9.14e-61

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: 195.20  E-value: 9.14e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782     43 RVIGGRVttnAKLGG--YLVAMRYFNN-FICGGTLIHELIVLTAAHCFEDRAEKeAWSVDGGISRLS--EKGIRRQVKRF 117
Cdd:smart00020   1 RIVGGSE---ANIGSfpWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSDPS-NIRVRLGSHDLSsgEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782    118 IKSAQFKMVTMNMDVAVVLLNRPM-VGKNIGTLSLCSTALTP--GQTMDVSGWGMTNPDDEGPGHMLRTVSVPVIEKRIC 194
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVtLSDNVRPICLPSSNYNVpaGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667782    195 REAYRESVSISDSMFCASVL-GKKDACTYDSGGPLVYEK---QVCGIVSFGIGCASRRYPGVYTDVHYVKPFI 263
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLeGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
43-263 9.14e-61

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: 195.20  E-value: 9.14e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782     43 RVIGGRVttnAKLGG--YLVAMRYFNN-FICGGTLIHELIVLTAAHCFEDRAEKeAWSVDGGISRLS--EKGIRRQVKRF 117
Cdd:smart00020   1 RIVGGSE---ANIGSfpWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSDPS-NIRVRLGSHDLSsgEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782    118 IKSAQFKMVTMNMDVAVVLLNRPM-VGKNIGTLSLCSTALTP--GQTMDVSGWGMTNPDDEGPGHMLRTVSVPVIEKRIC 194
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVtLSDNVRPICLPSSNYNVpaGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667782    195 REAYRESVSISDSMFCASVL-GKKDACTYDSGGPLVYEK---QVCGIVSFGIGCASRRYPGVYTDVHYVKPFI 263
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLeGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
44-265 3.03e-59

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  Cd Length: 232  Bit Score: 191.34  E-value: 3.03e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782  44 VIGGRvttNAKLGG--YLVAMRYFNN-FICGGTLIHELIVLTAAHCFEDRAeKEAWSVDGGISRLSE---KGIRRQVKRF 117
Cdd:cd00190   1 IVGGS---EAKIGSfpWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSnegGGQVIKVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782 118 IKSAQFKMVTMNMDVAVVLLNRPMV-GKNIGTLSL--CSTALTPGQTMDVSGWGMTNPDDEGPGHmLRTVSVPVIEKRIC 194
Cdd:cd00190  77 IVHPNYNPSTYDNDIALLKLKRPVTlSDNVRPICLpsSGYNLPAGTTCTVSGWGRTSEGGPLPDV-LQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667782 195 REAYRESVSISDSMFCASVL-GKKDACTYDSGGPLVYEK----QVCGIVSFGIGCASRRYPGVYTDVHYVKPFIVK 265
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGLeGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Trypsin pfam00089
Trypsin;
44-263 4.22e-49

Trypsin;


Pssm-ID: 306573  Cd Length: 220  Bit Score: 164.92  E-value: 4.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782    44 VIGGRvTTNAKLGGYLVAMRYFNNF-ICGGTLIHELIVLTAAHCFEDRAEKEAWSVDGGISRLSEKGIRRQVKRFIKSAQ 122
Cdd:pfam00089   1 IVGGD-EAQPGSFPWQVSLQLSSGKhFCGGSLISENWVLTAAHCVSNAKDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782   123 FKMVTMNMDVAVVLLNRPM-VGKNIGTLSL--CSTALTPGQTMDVSGWGmtNPDDEGPGHMLRTVSVPVIEKRICREAYr 199
Cdd:pfam00089  80 YNPDTLDNDIALLKLESPVtLGDTVRPICLpdASSDLPVGTTCTVSGWG--NTKTLGPPDTLQEVTVPVVSRETCRSAY- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24667782   200 eSVSISDSMFCASVLGKKDACTYDSGGPLVYEKQ-VCGIVSFGIGCASRRYPGVYTDVHYVKPFI 263
Cdd:pfam00089 157 -GGTVTDNMICAGAPGGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 220
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
43-273 5.82e-17

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


Pssm-ID: 227927  Cd Length: 413  Bit Score: 79.92  E-value: 5.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782  43 RVIGGrvtTNAKLGGY--LVAM-----RYFNNFICGGTLIHELIVLTAAHCFEDRAEKEAWSVDG--GISRLSEkGIRRQ 113
Cdd:COG5640  32 RIIGG---SNANAGEYpsLVALvdrisDYVSGTFCGGSKLGGRYVLTAAHCADASSPISSDVNRVvvDLNDSSQ-AERGH 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782 114 VKRFIKSAQFKMVTMNMDVAVVLLNRPMVGKNIGTLS--------LCSTALTPgqtMDVSGWGMTNP-DDEG---PGHML 181
Cdd:COG5640 108 VRTIYVHEFYSPGNLGNDIAVLELARAASLPRVKITSfdasdtflNSVTTVSP---MTNGTFGVTTPsDVPRsspKGTIL 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782 182 RTVSVPVIEKRICrEAYRESVSISDSM-----FCASVLGkKDACTYDSGGPLVYE-----KQVcGIVSFGIG-CASRRYP 250
Cdd:COG5640 185 HEVAVLFVPLSTC-AQYKGCANASDGAtgltgFCAGRPP-KDACQGDSGGPIFHKgeegrVQR-GVVSWGDGgCGGTLIP 261
                       250       260
                ....*....|....*....|...
gi 24667782 251 GVYTDVHYVKPFIVKGIKALLSR 273
Cdd:COG5640 262 GVYTNVSNYQDWIAAMTNGLSYL 284
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
43-263 9.14e-61

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: 195.20  E-value: 9.14e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782     43 RVIGGRVttnAKLGG--YLVAMRYFNN-FICGGTLIHELIVLTAAHCFEDRAEKeAWSVDGGISRLS--EKGIRRQVKRF 117
Cdd:smart00020   1 RIVGGSE---ANIGSfpWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSDPS-NIRVRLGSHDLSsgEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782    118 IKSAQFKMVTMNMDVAVVLLNRPM-VGKNIGTLSLCSTALTP--GQTMDVSGWGMTNPDDEGPGHMLRTVSVPVIEKRIC 194
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVtLSDNVRPICLPSSNYNVpaGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24667782    195 REAYRESVSISDSMFCASVL-GKKDACTYDSGGPLVYEK---QVCGIVSFGIGCASRRYPGVYTDVHYVKPFI 263
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLeGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
44-265 3.03e-59

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  Cd Length: 232  Bit Score: 191.34  E-value: 3.03e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782  44 VIGGRvttNAKLGG--YLVAMRYFNN-FICGGTLIHELIVLTAAHCFEDRAeKEAWSVDGGISRLSE---KGIRRQVKRF 117
Cdd:cd00190   1 IVGGS---EAKIGSfpWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSnegGGQVIKVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782 118 IKSAQFKMVTMNMDVAVVLLNRPMV-GKNIGTLSL--CSTALTPGQTMDVSGWGMTNPDDEGPGHmLRTVSVPVIEKRIC 194
Cdd:cd00190  77 IVHPNYNPSTYDNDIALLKLKRPVTlSDNVRPICLpsSGYNLPAGTTCTVSGWGRTSEGGPLPDV-LQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667782 195 REAYRESVSISDSMFCASVL-GKKDACTYDSGGPLVYEK----QVCGIVSFGIGCASRRYPGVYTDVHYVKPFIVK 265
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGLeGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Trypsin pfam00089
Trypsin;
44-263 4.22e-49

Trypsin;


Pssm-ID: 306573  Cd Length: 220  Bit Score: 164.92  E-value: 4.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782    44 VIGGRvTTNAKLGGYLVAMRYFNNF-ICGGTLIHELIVLTAAHCFEDRAEKEAWSVDGGISRLSEKGIRRQVKRFIKSAQ 122
Cdd:pfam00089   1 IVGGD-EAQPGSFPWQVSLQLSSGKhFCGGSLISENWVLTAAHCVSNAKDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782   123 FKMVTMNMDVAVVLLNRPM-VGKNIGTLSL--CSTALTPGQTMDVSGWGmtNPDDEGPGHMLRTVSVPVIEKRICREAYr 199
Cdd:pfam00089  80 YNPDTLDNDIALLKLESPVtLGDTVRPICLpdASSDLPVGTTCTVSGWG--NTKTLGPPDTLQEVTVPVVSRETCRSAY- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24667782   200 eSVSISDSMFCASVLGKKDACTYDSGGPLVYEKQ-VCGIVSFGIGCASRRYPGVYTDVHYVKPFI 263
Cdd:pfam00089 157 -GGTVTDNMICAGAPGGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 220
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
43-273 5.82e-17

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


Pssm-ID: 227927  Cd Length: 413  Bit Score: 79.92  E-value: 5.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782  43 RVIGGrvtTNAKLGGY--LVAM-----RYFNNFICGGTLIHELIVLTAAHCFEDRAEKEAWSVDG--GISRLSEkGIRRQ 113
Cdd:COG5640  32 RIIGG---SNANAGEYpsLVALvdrisDYVSGTFCGGSKLGGRYVLTAAHCADASSPISSDVNRVvvDLNDSSQ-AERGH 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782 114 VKRFIKSAQFKMVTMNMDVAVVLLNRPMVGKNIGTLS--------LCSTALTPgqtMDVSGWGMTNP-DDEG---PGHML 181
Cdd:COG5640 108 VRTIYVHEFYSPGNLGNDIAVLELARAASLPRVKITSfdasdtflNSVTTVSP---MTNGTFGVTTPsDVPRsspKGTIL 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667782 182 RTVSVPVIEKRICrEAYRESVSISDSM-----FCASVLGkKDACTYDSGGPLVYE-----KQVcGIVSFGIG-CASRRYP 250
Cdd:COG5640 185 HEVAVLFVPLSTC-AQYKGCANASDGAtgltgFCAGRPP-KDACQGDSGGPIFHKgeegrVQR-GVVSWGDGgCGGTLIP 261
                       250       260
                ....*....|....*....|...
gi 24667782 251 GVYTDVHYVKPFIVKGIKALLSR 273
Cdd:COG5640 262 GVYTNVSNYQDWIAAMTNGLSYL 284
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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