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Conserved domains on  [gi|319738594|ref|NP_956439|]
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ovochymase-1 precursor [Danio rerio]

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.-
Gene Ontology:  GO:0008236|GO:0008233|GO:0006508|GO:0004252
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 ...
 57-281 1.74e-91

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: 280.32  E-value: 1.74e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  57 IIGGKEAWAHSWPWQVSLQYND-VPTCGGAILDQLWVITAGHCFKRYKkPSMWNAVVGLHNLdNANESSRESIQVQKIFS 135
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDL-SSNEGGGQVIKVKKVIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 136 HKNYNQKTNENDIALLKLQSPLVFSKFVRPIGV--FNNDLPPLVTCTVTGWGSVTENGPQASRLQEVNVTVYEPQKCNRF 213
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLpsSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 214 YR--GKVLKSMICAGANEGGMDACQGDSGGPLSCFDGERYKLAGVVSWGVGCGRAQKPGVYTTLYHYRQW 281
Cdd:cd00190  159 YSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 331-551 1.78e-49

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: 170.53  E-value: 1.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 331 SEACPNAWPWQASLQNDD-THYCSGVLVHPRWVLAPRHCLVKAGD---VVVLGAHDLN--FMSGQTVDVESV-------Q 397
Cdd:cd00190    5 SEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSAPsnyTVRLGSHDLSsnEGGGQVIKVKKVivhpnynP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 398 SLSHNgrnrtvsDLSMIYLTVPARIGPLIFPVCITDKDDELVNGDSssCVTTGWGpRKATLDLQPEILHMARVKPLSEDT 477
Cdd:cd00190   85 STYDN-------DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTT--CTVSGWG-RTSEGGPLPDVLQEVNVPIVSNAE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319738594 478 CRTGWGDGFNRQ-SHLCT--HAAASTSCLGDSGAPLVCAKNGIYHLVGLTTWGSkKC-QPQKPAVFTRVSAYHSWIQN 551
Cdd:cd00190  155 CKRAYSYGGTITdNMLCAggLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS-GCaRPNYPGVYTRVSSYLDWIQK 231
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 57-281 1.74e-91

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: 280.32  E-value: 1.74e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  57 IIGGKEAWAHSWPWQVSLQYND-VPTCGGAILDQLWVITAGHCFKRYKkPSMWNAVVGLHNLdNANESSRESIQVQKIFS 135
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDL-SSNEGGGQVIKVKKVIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 136 HKNYNQKTNENDIALLKLQSPLVFSKFVRPIGV--FNNDLPPLVTCTVTGWGSVTENGPQASRLQEVNVTVYEPQKCNRF 213
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLpsSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 214 YR--GKVLKSMICAGANEGGMDACQGDSGGPLSCFDGERYKLAGVVSWGVGCGRAQKPGVYTTLYHYRQW 281
Cdd:cd00190  159 YSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 56-281 3.54e-88

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: 271.47  E-value: 3.54e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594    56 RIIGGKEAWAHSWPWQVSLQYND-VPTCGGAILDQLWVITAGHCFkRYKKPSMWNAVVGLHNLDNANESsrESIQVQKIF 134
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGEEG--QVIKVSKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594   135 SHKNYNQKTNENDIALLKLQSPLVFSKFVRPIGV--FNNDLPPLVTCTVTGWGSVTENGPQASR-LQEVNVTVYEPQKCN 211
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLpsSNYNVPAGTTCTVSGWGRTSEGAGSLPDtLQEVNVPIVSNATCR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319738594   212 RFYRG--KVLKSMICAGANEGGMDACQGDSGGPLSCfDGERYKLAGVVSWGVGCGRAQKPGVYTTLYHYRQW 281
Cdd:smart00020 158 RAYSGggAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
57-282 7.16e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 228.87  E-value: 7.16e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594   57 IIGGKEAWAHSWPWQVSLQY-NDVPTCGGAILDQLWVITAGHCFKRYKKpsmWNAVVGLHNLDNaNESSRESIQVQKIFS 135
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVL-REGGEQKFDVEKIIV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  136 HKNYNQKTNENDIALLKLQSPLVFSKFVRPIGV--FNNDLPPLVTCTVTGWGSVTENGPqASRLQEVNVTVYEPQKCNRF 213
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLpdASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSA 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319738594  214 YRGKVLKSMICAGAneGGMDACQGDSGGPLSCFDGErykLAGVVSWGVGCGRAQKPGVYTTLYHYRQWM 282
Cdd:pfam00089 156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 54-288 3.06e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 205.27  E-value: 3.06e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  54 ESRIIGGKEAWAHSWPWQVSLQYNDVP---TCGGAILDQLWVITAGHCFKRYKKPSMWnAVVGLHNLdnaNESSRESIQV 130
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSDLR-VVIGSTDL---STSGGTVVKV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 131 QKIFSHKNYNQKTNENDIALLKLQSPLVFSKFVrPIGVFNNDLPPLVTCTVTGWGSVTEN-GPQASRLQEVNVTVYEPQK 209
Cdd:COG5640  104 ARIVVHPDYDPATPGNDIALLKLATPVPGVAPA-PLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDAT 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319738594 210 CNRfYRGKVLKSMICAGANEGGMDACQGDSGGPLSCFDGERYKLAGVVSWGVGCGRAQKPGVYTTLYHYRQWMVSSMRG 288
Cdd:COG5640  183 CAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 331-551 1.78e-49

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: 170.53  E-value: 1.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 331 SEACPNAWPWQASLQNDD-THYCSGVLVHPRWVLAPRHCLVKAGD---VVVLGAHDLN--FMSGQTVDVESV-------Q 397
Cdd:cd00190    5 SEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSAPsnyTVRLGSHDLSsnEGGGQVIKVKKVivhpnynP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 398 SLSHNgrnrtvsDLSMIYLTVPARIGPLIFPVCITDKDDELVNGDSssCVTTGWGpRKATLDLQPEILHMARVKPLSEDT 477
Cdd:cd00190   85 STYDN-------DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTT--CTVSGWG-RTSEGGPLPDVLQEVNVPIVSNAE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319738594 478 CRTGWGDGFNRQ-SHLCT--HAAASTSCLGDSGAPLVCAKNGIYHLVGLTTWGSkKC-QPQKPAVFTRVSAYHSWIQN 551
Cdd:cd00190  155 CKRAYSYGGTITdNMLCAggLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS-GCaRPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 331-549 3.53e-48

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: 167.08  E-value: 3.53e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594   331 SEACPNAWPWQASLQNDD-THYCSGVLVHPRWVLAPRHCLVKAGD---VVVLGAHDLNF-MSGQTVDVESVqSLSHNGRN 405
Cdd:smart00020   6 SEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPsniRVRLGSHDLSSgEEGQVIKVSKV-IIHPNYNP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594   406 RTVS-DLSMIYLTVPARIGPLIFPVCITDKDDELVNGdsSSCVTTGWGPRKATLDLQPEILHMARVKPLSEDTCRTGWGD 484
Cdd:smart00020  85 STYDnDIALLKLKEPVTLSDNVRPICLPSSNYNVPAG--TTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSG 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594   485 GFN-RQSHLCthAAAST----SCLGDSGAPLVCaKNGIYHLVGLTTWGSKKCQPQKPAVFTRVSAYHSWI 549
Cdd:smart00020 163 GGAiTDNMLC--AGGLEggkdACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 331-556 1.82e-42

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 152.88  E-value: 1.82e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 331 SEACPNAWPWQASLQNDD---THYCSGVLVHPRWVLAPRHCLVK--AGDV-VVLGAHDLNFMSGQTVDVESVqsLSHNG- 403
Cdd:COG5640   35 TPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGdgPSDLrVVIGSTDLSTSGGTVVKVARI--VVHPDy 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 404 -RNRTVSDLSMIYLTVPArigPLIFPVCITDKDDELVNGDSSscVTTGWGPRKATLDLQPEILHMARVKPLSEDTCRTGw 482
Cdd:COG5640  113 dPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPA--TVAGWGRTSEGPGSQSGTLRKADVPVVSDATCAAY- 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 319738594 483 gDGFNRQSHLCT--HAAASTSCLGDSGAPLVCAKNGIYHLVGLTTWGSKKCQPQKPAVFTRVSAYHSWIQNYIKTA 556
Cdd:COG5640  187 -GGFDGGTMLCAgyPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
Trypsin pfam00089
Trypsin;
331-549 3.42e-41

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 147.97  E-value: 3.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  331 SEACPNAWPWQASLQN-DDTHYCSGVLVHPRWVLAPRHCLVKAGDV-VVLGAHDLNFMSG--QTVDVESVQSLSHNGRNR 406
Cdd:pfam00089   5 DEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVkVVLGAHNIVLREGgeQKFDVEKIIVHPNYNPDT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  407 TVSDLSMIYLTVPARIGPLIFPVCITDKDDELVNGDSssCVTTGWGpRKATLDLqPEILHMARVKPLSEDTCRTGWGDGF 486
Cdd:pfam00089  85 LDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTT--CTVSGWG-NTKTLGP-SDTLQEVTVPVVSRETCRSAYGGTV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 319738594  487 NrQSHLCTHAAASTSCLGDSGAPLVCAKNgiyHLVGLTTWGSKKCQPQKPAVFTRVSAYHSWI 549
Cdd:pfam00089 161 T-DTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 57-281 1.74e-91

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: 280.32  E-value: 1.74e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  57 IIGGKEAWAHSWPWQVSLQYND-VPTCGGAILDQLWVITAGHCFKRYKkPSMWNAVVGLHNLdNANESSRESIQVQKIFS 135
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDL-SSNEGGGQVIKVKKVIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 136 HKNYNQKTNENDIALLKLQSPLVFSKFVRPIGV--FNNDLPPLVTCTVTGWGSVTENGPQASRLQEVNVTVYEPQKCNRF 213
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLpsSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 214 YR--GKVLKSMICAGANEGGMDACQGDSGGPLSCFDGERYKLAGVVSWGVGCGRAQKPGVYTTLYHYRQW 281
Cdd:cd00190  159 YSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 56-281 3.54e-88

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: 271.47  E-value: 3.54e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594    56 RIIGGKEAWAHSWPWQVSLQYND-VPTCGGAILDQLWVITAGHCFkRYKKPSMWNAVVGLHNLDNANESsrESIQVQKIF 134
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGEEG--QVIKVSKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594   135 SHKNYNQKTNENDIALLKLQSPLVFSKFVRPIGV--FNNDLPPLVTCTVTGWGSVTENGPQASR-LQEVNVTVYEPQKCN 211
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLpsSNYNVPAGTTCTVSGWGRTSEGAGSLPDtLQEVNVPIVSNATCR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319738594   212 RFYRG--KVLKSMICAGANEGGMDACQGDSGGPLSCfDGERYKLAGVVSWGVGCGRAQKPGVYTTLYHYRQW 281
Cdd:smart00020 158 RAYSGggAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
57-282 7.16e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 228.87  E-value: 7.16e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594   57 IIGGKEAWAHSWPWQVSLQY-NDVPTCGGAILDQLWVITAGHCFKRYKKpsmWNAVVGLHNLDNaNESSRESIQVQKIFS 135
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVL-REGGEQKFDVEKIIV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  136 HKNYNQKTNENDIALLKLQSPLVFSKFVRPIGV--FNNDLPPLVTCTVTGWGSVTENGPqASRLQEVNVTVYEPQKCNRF 213
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLpdASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSA 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319738594  214 YRGKVLKSMICAGAneGGMDACQGDSGGPLSCFDGErykLAGVVSWGVGCGRAQKPGVYTTLYHYRQWM 282
Cdd:pfam00089 156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 54-288 3.06e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 205.27  E-value: 3.06e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  54 ESRIIGGKEAWAHSWPWQVSLQYNDVP---TCGGAILDQLWVITAGHCFKRYKKPSMWnAVVGLHNLdnaNESSRESIQV 130
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSDLR-VVIGSTDL---STSGGTVVKV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 131 QKIFSHKNYNQKTNENDIALLKLQSPLVFSKFVrPIGVFNNDLPPLVTCTVTGWGSVTEN-GPQASRLQEVNVTVYEPQK 209
Cdd:COG5640  104 ARIVVHPDYDPATPGNDIALLKLATPVPGVAPA-PLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDAT 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319738594 210 CNRfYRGKVLKSMICAGANEGGMDACQGDSGGPLSCFDGERYKLAGVVSWGVGCGRAQKPGVYTTLYHYRQWMVSSMRG 288
Cdd:COG5640  183 CAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 331-551 1.78e-49

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: 170.53  E-value: 1.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 331 SEACPNAWPWQASLQNDD-THYCSGVLVHPRWVLAPRHCLVKAGD---VVVLGAHDLN--FMSGQTVDVESV-------Q 397
Cdd:cd00190    5 SEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSAPsnyTVRLGSHDLSsnEGGGQVIKVKKVivhpnynP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 398 SLSHNgrnrtvsDLSMIYLTVPARIGPLIFPVCITDKDDELVNGDSssCVTTGWGpRKATLDLQPEILHMARVKPLSEDT 477
Cdd:cd00190   85 STYDN-------DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTT--CTVSGWG-RTSEGGPLPDVLQEVNVPIVSNAE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319738594 478 CRTGWGDGFNRQ-SHLCT--HAAASTSCLGDSGAPLVCAKNGIYHLVGLTTWGSkKC-QPQKPAVFTRVSAYHSWIQN 551
Cdd:cd00190  155 CKRAYSYGGTITdNMLCAggLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS-GCaRPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 331-549 3.53e-48

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: 167.08  E-value: 3.53e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594   331 SEACPNAWPWQASLQNDD-THYCSGVLVHPRWVLAPRHCLVKAGD---VVVLGAHDLNF-MSGQTVDVESVqSLSHNGRN 405
Cdd:smart00020   6 SEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPsniRVRLGSHDLSSgEEGQVIKVSKV-IIHPNYNP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594   406 RTVS-DLSMIYLTVPARIGPLIFPVCITDKDDELVNGdsSSCVTTGWGPRKATLDLQPEILHMARVKPLSEDTCRTGWGD 484
Cdd:smart00020  85 STYDnDIALLKLKEPVTLSDNVRPICLPSSNYNVPAG--TTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSG 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594   485 GFN-RQSHLCthAAAST----SCLGDSGAPLVCaKNGIYHLVGLTTWGSKKCQPQKPAVFTRVSAYHSWI 549
Cdd:smart00020 163 GGAiTDNMLC--AGGLEggkdACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 331-556 1.82e-42

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 152.88  E-value: 1.82e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 331 SEACPNAWPWQASLQNDD---THYCSGVLVHPRWVLAPRHCLVK--AGDV-VVLGAHDLNFMSGQTVDVESVqsLSHNG- 403
Cdd:COG5640   35 TPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGdgPSDLrVVIGSTDLSTSGGTVVKVARI--VVHPDy 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 404 -RNRTVSDLSMIYLTVPArigPLIFPVCITDKDDELVNGDSSscVTTGWGPRKATLDLQPEILHMARVKPLSEDTCRTGw 482
Cdd:COG5640  113 dPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPA--TVAGWGRTSEGPGSQSGTLRKADVPVVSDATCAAY- 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 319738594 483 gDGFNRQSHLCT--HAAASTSCLGDSGAPLVCAKNGIYHLVGLTTWGSKKCQPQKPAVFTRVSAYHSWIQNYIKTA 556
Cdd:COG5640  187 -GGFDGGTMLCAgyPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
Trypsin pfam00089
Trypsin;
331-549 3.42e-41

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 147.97  E-value: 3.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  331 SEACPNAWPWQASLQN-DDTHYCSGVLVHPRWVLAPRHCLVKAGDV-VVLGAHDLNFMSG--QTVDVESVQSLSHNGRNR 406
Cdd:pfam00089   5 DEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVkVVLGAHNIVLREGgeQKFDVEKIIVHPNYNPDT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  407 TVSDLSMIYLTVPARIGPLIFPVCITDKDDELVNGDSssCVTTGWGpRKATLDLqPEILHMARVKPLSEDTCRTGWGDGF 486
Cdd:pfam00089  85 LDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTT--CTVSGWG-NTKTLGP-SDTLQEVTVPVVSRETCRSAYGGTV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 319738594  487 NrQSHLCTHAAASTSCLGDSGAPLVCAKNgiyHLVGLTTWGSKKCQPQKPAVFTRVSAYHSWI 549
Cdd:pfam00089 161 T-DTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 91-262 1.72e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 51.60  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  91 WVITAGHCFKRYKK---PSMWNAVVGLHNLDNANESSREsiqvqkIFSHKNYNQKTNEN-DIALLKLQSPLVFSkfVRPI 166
Cdd:COG3591   23 LVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGTATATR------FRVPPGWVASGDAGyDYALLRLDEPLGDT--TGWL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 167 GVFNNDLPPLVTC-TVTGWGSvteNGPQASRLQEVNVTVYEPQkcNRFYrgkvlksMICaganeggmDACQGDSGGPLSC 245
Cdd:COG3591   95 GLAFNDAPLAGEPvTIIGYPG---DRPKDLSLDCSGRVTGVQG--NRLS-------YDC--------DTTGGSSGSPVLD 154

                        170
                 ....*....|....*..
gi 319738594 246 FDGERYKLAGVVSWGVG 262
Cdd:COG3591  155 DSDGGGRVVGVHSAGGA 171
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 346-531 4.46e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 41.59  E-value: 4.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 346 NDDTHYCSGVLVHPRWVLAPRHCLVKAGD-------VVVLGAHDLNFMSGQTVDVESVQSLSHNGRNRTvsDLSMIYLT- 417
Cdd:COG3591    8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwatniVFVPGYNGGPYGTATATRFRVPPGWVASGDAGY--DYALLRLDe 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594 418 -VPARIGPLIFpvcitDKDDELVNGDSsscVT-TGWGprkatlDLQPEILHMarvkplsEDTCRTGWGDGfNRQSHLCTh 495
Cdd:COG3591   86 pLGDTTGWLGL-----AFNDAPLAGEP---VTiIGYP------GDRPKDLSL-------DCSGRVTGVQG-NRLSYDCD- 142

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 319738594 496 aaastSCLGDSGAPLVCAKNGIYHLVGLTTWGSKKC 531
Cdd:COG3591  143 -----TTGGSSGSPVLDDSDGGGRVVGVHSAGGADR 173
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 68-165 6.29e-04

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 39.84  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594   68 WPWQVSLQYNDVPTCGGAILDQLWVITAGHCFKRYKKPSMWNAVV-GLHNLDNANESSREsiQVQKIFSHKNynqkTNEN 146
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVlGGAKTLKSIEGPYE--QIVRVDCRHD----IPES 74

                          90
                  ....*....|....*....
gi 319738594  147 DIALLKLQSPLVFSKFVRP 165
Cdd:pfam09342  75 EISLLHLASPASFSNHVLP 93
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 338-450 4.51e-03

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 37.14  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738594  338 WPWQASLQNDDTHYCSGVLVHPRWVLAPRHCLVKAG------DVVVLGAHDLNFMSG---QTVDVESVQSLSHngrnrtv 408
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNlrhqyiSVVLGGAKTLKSIEGpyeQIVRVDCRHDIPE------- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 319738594  409 SDLSMIYLTVPARIGPLIFPVCITDKDDElvNGDSSSCVTTG 450
Cdd:pfam09342  74 SEISLLHLASPASFSNHVLPTFVPETRNE--NEKDNECLAVG 113
 
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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