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Conserved domains on  [gi|195109238|ref|XP_001999194|]
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serine protease grass [Drosophila mojavensis]

Protein Classification

CLIP and Tryp_SPc domain-containing protein( domain architecture ID 10572270)

CLIP and Tryp_SPc domain-containing protein

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 ...
118-370 8.19e-75

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: 231.40  E-value: 8.19e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 118 VANGYEVKLSSRPWMALLRYQSlgeSRFLCGGTIIANRYILTAAHCVYGLEDQLYEIRLGEHRISTERdcrqqgrkekca 197
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNE------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 198 PPVKDLGIEKFIIHDKYDSKRIINDIALLRLNESVLFDKHIKPICLPISNELkqqaesLPDY---FVTGWGTT-ENGSSS 273
Cdd:cd00190   66 GGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN------LPAGttcTVSGWGRTsEGGPLP 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 274 DVLLQAKVPMQSRSVCSQTYRREVPHT--QLCVGGGDL-QDSCKGDSGGPLqapapyLDEYKVRMVEFGIVSMGVtSCGQ 350
Cdd:cd00190  140 DVLQEVNVPIVSNAECKRAYSYGGTITdnMLCAGGLEGgKDACQGDSGGPL------VCNDNGRGVLVGIVSWGS-GCAR 212
                        250       260
                 ....*....|....*....|
gi 195109238 351 ISLPGLYTNVADYVQWITDV 370
Cdd:cd00190  213 PNYPGVYTRVSSYLDWIQKT 232
CLIP pfam12032
Regulatory CLIP domain of proteinases; CLIP is a regulatory domain which controls the ...
31-88 7.59e-11

Regulatory CLIP domain of proteinases; CLIP is a regulatory domain which controls the proteinase action of various proteins of the trypsin family, e.g. easter and pap2. The CLIP domain remains linked to the protease domain after cleavage of a conserved residue which retains the protein in zymogen form. It is named CLIP because it can be drawn in the shape of a paper clip. It has many disulphide bonds and highly conserved cysteine residues, and so it folds extensively.


:

Pssm-ID: 463440  Cd Length: 54  Bit Score: 57.03  E-value: 7.59e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 195109238   31 CDTPNGERGQCMPFSSCSDIEQRLLAaqqsgQRVSPEYASYLQKASCGEI-DGVRHFCC 88
Cdd:pfam12032   1 CTTPNGEPGRCVPIRECPSLLDLLRK-----RNLSPEERNFLRQSQCGEGsDGKPLVCC 54
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
118-370 8.19e-75

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: 231.40  E-value: 8.19e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 118 VANGYEVKLSSRPWMALLRYQSlgeSRFLCGGTIIANRYILTAAHCVYGLEDQLYEIRLGEHRISTERdcrqqgrkekca 197
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNE------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 198 PPVKDLGIEKFIIHDKYDSKRIINDIALLRLNESVLFDKHIKPICLPISNELkqqaesLPDY---FVTGWGTT-ENGSSS 273
Cdd:cd00190   66 GGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN------LPAGttcTVSGWGRTsEGGPLP 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 274 DVLLQAKVPMQSRSVCSQTYRREVPHT--QLCVGGGDL-QDSCKGDSGGPLqapapyLDEYKVRMVEFGIVSMGVtSCGQ 350
Cdd:cd00190  140 DVLQEVNVPIVSNAECKRAYSYGGTITdnMLCAGGLEGgKDACQGDSGGPL------VCNDNGRGVLVGIVSWGS-GCAR 212
                        250       260
                 ....*....|....*....|
gi 195109238 351 ISLPGLYTNVADYVQWITDV 370
Cdd:cd00190  213 PNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
117-367 2.06e-73

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: 227.95  E-value: 2.06e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238   117 RVANGYEVKLSSRPWMALLRYQSlgeSRFLCGGTIIANRYILTAAHCVYGLEDQLYEIRLGEHRISTERDcrQQGRKekc 196
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG---GRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE--GQVIK--- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238   197 appvkdlgIEKFIIHDKYDSKRIINDIALLRLNESVLFDKHIKPICLPISNelkqqaESLPDY---FVTGWGTTEN--GS 271
Cdd:smart00020  73 --------VSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN------YNVPAGttcTVSGWGRTSEgaGS 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238   272 SSDVLLQAKVPMQSRSVCSQTYRRE--VPHTQLCVGGGDL-QDSCKGDSGGPLQApapyldeYKVRMVEFGIVSMGVtSC 348
Cdd:smart00020 139 LPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEGgKDACQGDSGGPLVC-------NDGRWVLVGIVSWGS-GC 210
                          250
                   ....*....|....*....
gi 195109238   349 GQISLPGLYTNVADYVQWI 367
Cdd:smart00020 211 ARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
120-367 1.18e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 192.27  E-value: 1.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238  120 NGYEVKLSSRPWMALLryqSLGESRFLCGGTIIANRYILTAAHCVYGLEDqlYEIRLGEHRISterdcRQQGRKEKcapp 199
Cdd:pfam00089   3 GGDEAQPGSFPWQVSL---QLSSGKHFCGGSLISENWVLTAAHCVSGASD--VKVVLGAHNIV-----LREGGEQK---- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238  200 vkdLGIEKFIIHDKYDSKRIINDIALLRLNESVLFDKHIKPICLP-ISNELKQQAESlpdyFVTGWGTTENGSSSDVLLQ 278
Cdd:pfam00089  69 ---FDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPdASSDLPVGTTC----TVSGWGNTKTLGPSDTLQE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238  279 AKVPMQSRSVCSQTYRREVPHTQLCVGGGDlQDSCKGDSGGPLQAPAPYLDeykvrmvefGIVSMGVtSCGQISLPGLYT 358
Cdd:pfam00089 142 VTVPVVSRETCRSAYGGTVTDTMICAGAGG-KDACQGDSGGPLVCSDGELI---------GIVSWGY-GCASGNYPGVYT 210

                  ....*....
gi 195109238  359 NVADYVQWI 367
Cdd:pfam00089 211 PVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
116-375 4.99e-55

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 181.77  E-value: 4.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 116 QRVANGYEVKLSSRPWMALLrYQSLGESRFLCGGTIIANRYILTAAHCVYGLEDQLYEIRLGEHRISTerdcrQQGRKek 195
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLST-----SGGTV-- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 196 cappvkdLGIEKFIIHDKYDSKRIINDIALLRLNESVlfdKHIKPICLPISNElkqQAESLPDYFVTGWGTTEN--GSSS 273
Cdd:COG5640  101 -------VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSAD---AAAPGTPATVAGWGRTSEgpGSQS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 274 DVLLQAKVPMQSRSVCsQTYRREVPHTQLCVGGGDL-QDSCKGDSGGPLQAPAPylDEYKVrmveFGIVSMGVTSCGqIS 352
Cdd:COG5640  168 GTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGgKDACQGDSGGPLVVKDG--GGWVL----VGVVSWGGGPCA-AG 239
                        250       260
                 ....*....|....*....|...
gi 195109238 353 LPGLYTNVADYVQWITDVMAKHG 375
Cdd:COG5640  240 YPGVYTRVSAYRDWIKSTAGGLG 262
CLIP pfam12032
Regulatory CLIP domain of proteinases; CLIP is a regulatory domain which controls the ...
31-88 7.59e-11

Regulatory CLIP domain of proteinases; CLIP is a regulatory domain which controls the proteinase action of various proteins of the trypsin family, e.g. easter and pap2. The CLIP domain remains linked to the protease domain after cleavage of a conserved residue which retains the protein in zymogen form. It is named CLIP because it can be drawn in the shape of a paper clip. It has many disulphide bonds and highly conserved cysteine residues, and so it folds extensively.


Pssm-ID: 463440  Cd Length: 54  Bit Score: 57.03  E-value: 7.59e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 195109238   31 CDTPNGERGQCMPFSSCSDIEQRLLAaqqsgQRVSPEYASYLQKASCGEI-DGVRHFCC 88
Cdd:pfam12032   1 CTTPNGEPGRCVPIRECPSLLDLLRK-----RNLSPEERNFLRQSQCGEGsDGKPLVCC 54
CLIP smart00680
Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, ...
31-89 3.83e-10

Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, Drosophila Easter and silkworm prophenoloxidase-activating enzyme.


Pssm-ID: 197829  Cd Length: 52  Bit Score: 54.82  E-value: 3.83e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 195109238    31 CDTPNGERGQCMPFSSCSDIEQRLlaaqqsgQRVSPEYASYLQKASCGEIDGVRHFCCP 89
Cdd:smart00680   1 CRTPDGERGTCVPISDCPSLLSLL-------KKDPPEDLNFLRKSQCGFGNREPLVCCP 52
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
118-370 8.19e-75

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: 231.40  E-value: 8.19e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 118 VANGYEVKLSSRPWMALLRYQSlgeSRFLCGGTIIANRYILTAAHCVYGLEDQLYEIRLGEHRISTERdcrqqgrkekca 197
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNE------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 198 PPVKDLGIEKFIIHDKYDSKRIINDIALLRLNESVLFDKHIKPICLPISNELkqqaesLPDY---FVTGWGTT-ENGSSS 273
Cdd:cd00190   66 GGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN------LPAGttcTVSGWGRTsEGGPLP 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 274 DVLLQAKVPMQSRSVCSQTYRREVPHT--QLCVGGGDL-QDSCKGDSGGPLqapapyLDEYKVRMVEFGIVSMGVtSCGQ 350
Cdd:cd00190  140 DVLQEVNVPIVSNAECKRAYSYGGTITdnMLCAGGLEGgKDACQGDSGGPL------VCNDNGRGVLVGIVSWGS-GCAR 212
                        250       260
                 ....*....|....*....|
gi 195109238 351 ISLPGLYTNVADYVQWITDV 370
Cdd:cd00190  213 PNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
117-367 2.06e-73

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: 227.95  E-value: 2.06e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238   117 RVANGYEVKLSSRPWMALLRYQSlgeSRFLCGGTIIANRYILTAAHCVYGLEDQLYEIRLGEHRISTERDcrQQGRKekc 196
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG---GRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE--GQVIK--- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238   197 appvkdlgIEKFIIHDKYDSKRIINDIALLRLNESVLFDKHIKPICLPISNelkqqaESLPDY---FVTGWGTTEN--GS 271
Cdd:smart00020  73 --------VSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN------YNVPAGttcTVSGWGRTSEgaGS 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238   272 SSDVLLQAKVPMQSRSVCSQTYRRE--VPHTQLCVGGGDL-QDSCKGDSGGPLQApapyldeYKVRMVEFGIVSMGVtSC 348
Cdd:smart00020 139 LPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEGgKDACQGDSGGPLVC-------NDGRWVLVGIVSWGS-GC 210
                          250
                   ....*....|....*....
gi 195109238   349 GQISLPGLYTNVADYVQWI 367
Cdd:smart00020 211 ARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
120-367 1.18e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 192.27  E-value: 1.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238  120 NGYEVKLSSRPWMALLryqSLGESRFLCGGTIIANRYILTAAHCVYGLEDqlYEIRLGEHRISterdcRQQGRKEKcapp 199
Cdd:pfam00089   3 GGDEAQPGSFPWQVSL---QLSSGKHFCGGSLISENWVLTAAHCVSGASD--VKVVLGAHNIV-----LREGGEQK---- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238  200 vkdLGIEKFIIHDKYDSKRIINDIALLRLNESVLFDKHIKPICLP-ISNELKQQAESlpdyFVTGWGTTENGSSSDVLLQ 278
Cdd:pfam00089  69 ---FDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPdASSDLPVGTTC----TVSGWGNTKTLGPSDTLQE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238  279 AKVPMQSRSVCSQTYRREVPHTQLCVGGGDlQDSCKGDSGGPLQAPAPYLDeykvrmvefGIVSMGVtSCGQISLPGLYT 358
Cdd:pfam00089 142 VTVPVVSRETCRSAYGGTVTDTMICAGAGG-KDACQGDSGGPLVCSDGELI---------GIVSWGY-GCASGNYPGVYT 210

                  ....*....
gi 195109238  359 NVADYVQWI 367
Cdd:pfam00089 211 PVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
116-375 4.99e-55

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 181.77  E-value: 4.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 116 QRVANGYEVKLSSRPWMALLrYQSLGESRFLCGGTIIANRYILTAAHCVYGLEDQLYEIRLGEHRISTerdcrQQGRKek 195
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLST-----SGGTV-- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 196 cappvkdLGIEKFIIHDKYDSKRIINDIALLRLNESVlfdKHIKPICLPISNElkqQAESLPDYFVTGWGTTEN--GSSS 273
Cdd:COG5640  101 -------VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSAD---AAAPGTPATVAGWGRTSEgpGSQS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 274 DVLLQAKVPMQSRSVCsQTYRREVPHTQLCVGGGDL-QDSCKGDSGGPLQAPAPylDEYKVrmveFGIVSMGVTSCGqIS 352
Cdd:COG5640  168 GTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGgKDACQGDSGGPLVVKDG--GGWVL----VGVVSWGGGPCA-AG 239
                        250       260
                 ....*....|....*....|...
gi 195109238 353 LPGLYTNVADYVQWITDVMAKHG 375
Cdd:COG5640  240 YPGVYTRVSAYRDWIKSTAGGLG 262
CLIP pfam12032
Regulatory CLIP domain of proteinases; CLIP is a regulatory domain which controls the ...
31-88 7.59e-11

Regulatory CLIP domain of proteinases; CLIP is a regulatory domain which controls the proteinase action of various proteins of the trypsin family, e.g. easter and pap2. The CLIP domain remains linked to the protease domain after cleavage of a conserved residue which retains the protein in zymogen form. It is named CLIP because it can be drawn in the shape of a paper clip. It has many disulphide bonds and highly conserved cysteine residues, and so it folds extensively.


Pssm-ID: 463440  Cd Length: 54  Bit Score: 57.03  E-value: 7.59e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 195109238   31 CDTPNGERGQCMPFSSCSDIEQRLLAaqqsgQRVSPEYASYLQKASCGEI-DGVRHFCC 88
Cdd:pfam12032   1 CTTPNGEPGRCVPIRECPSLLDLLRK-----RNLSPEERNFLRQSQCGEGsDGKPLVCC 54
CLIP smart00680
Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, ...
31-89 3.83e-10

Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, Drosophila Easter and silkworm prophenoloxidase-activating enzyme.


Pssm-ID: 197829  Cd Length: 52  Bit Score: 54.82  E-value: 3.83e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 195109238    31 CDTPNGERGQCMPFSSCSDIEQRLlaaqqsgQRVSPEYASYLQKASCGEIDGVRHFCCP 89
Cdd:smart00680   1 CRTPDGERGTCVPISDCPSLLSLL-------KKDPPEDLNFLRKSQCGFGNREPLVCCP 52
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
141-367 5.64e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 49.67  E-value: 5.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 141 GESRFLCGGTIIANRYILTAAHCVYGLEDQLYEIRLgehRISTERDCRQQGRkekcappvkdLGIEKFIIHDKYDSKRII 220
Cdd:COG3591    8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNI---VFVPGYNGGPYGT----------ATATRFRVPPGWVASGDA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195109238 221 N-DIALLRLNEsvlfdkhikpiclPISN-----ELKQQAESLPD--YFVTGWGTTEngsssdvllqakvPMQSRSVCSQT 292
Cdd:COG3591   75 GyDYALLRLDE-------------PLGDttgwlGLAFNDAPLAGepVTIIGYPGDR-------------PKDLSLDCSGR 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195109238 293 YRRevphtqlcVGGGDLQ---DSCKGDSGGPLqapapYLDEYKVRMVeFGIVSMGVTSCGQISLPGLYTNVADYVQWI 367
Cdd:COG3591  129 VTG--------VQGNRLSydcDTTGGSSGSPV-----LDDSDGGGRV-VGVHSAGGADRANTGVRLTSAIVAALRAWA 192
DUF316 pfam03761
Nematode trypsin-6-like family; This is a family of trypsin-6-like proteins found in nematodes ...
110-165 3.62e-03

Nematode trypsin-6-like family; This is a family of trypsin-6-like proteins found in nematodes that are part of the chymotrypsin family S1, ie a serine peptidase. The C. elegans sequence UniProt:O01566 is trypsin-6: all the active site residues are present (His90, Asp168, Ser267).


Pssm-ID: 367641  Cd Length: 281  Bit Score: 38.95  E-value: 3.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 195109238  110 CGN---ILNQRVANGYEVKLSSRPWMALLRYQSLGESRFLCGGTIIANRYILTAAHCVY 165
Cdd:pfam03761  31 CGNktlPLPSQNINGIYLEKSEYPWLVKAAFQNGNQKNYKPPATFISTRHILTSSRLFL 89
 
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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