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Conserved domains on  [gi|385137135|ref|NP_001245220|]
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polyserase-2 isoform 3 precursor [Homo sapiens]

Protein Classification

Tryp_SPc domain-containing protein( domain architecture ID 10076278)

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 ...
 47-289 4.02e-82

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: 261.06  E-value: 4.02e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  47 IVGGSNAQPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFMTNgtlePAAEWSVLLGVHSQDGPLDGAHTRAVAAI 125
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 126 VVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPLPLpwVLQEVELRLLGEAT 205
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 206 CQCLYSQPGPfnltlqILPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEAW 285
Cdd:cd00190  155 CKRAYSYGGT------ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                 ....
gi 385137135 286 IREQ 289
Cdd:cd00190  229 IQKT 232
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 330-538 4.98e-23

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.


The actual alignment was detected with superfamily member cd00190:

Pssm-ID: 473915 [Multi-domain]  Cd Length: 232  Bit Score: 98.50  E-value: 4.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 330 RPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFLDPNSSDspprdldaWRVLL--------PSRPRAERVARLVQH 400
Cdd:cd00190    8 KIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAPSN--------YTVRLgshdlssnEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 401 EN---ASWDNasDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGR-GEPALGPGALLEAEL--LGGWWCHC 474
Cdd:cd00190   80 PNynpSTYDN--DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRtSEGGPLPDVLQEVNVpiVSNAECKR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385137135 475 LYGRQGAavplpgDPPHALCpAYQEKEEVGSCWNDSRWSLLCQEEGTWFLAGIRDFPSGCLRPR 538
Cdd:cd00190  158 AYSYGGT------ITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPN 214
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 601-650 4.99e-05

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.


The actual alignment was detected with superfamily member pfam09342:

Pssm-ID: 473915  Cd Length: 116  Bit Score: 43.31  E-value: 4.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 385137135  601 WPWLAEVHVAGDRVCTGILLAPGWVLAATHCvLRPGSTTVPYIEVYLGRA 650
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSC-LRDTNLRHQYISVVLGGA 49
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 47-289 4.02e-82

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: 261.06  E-value: 4.02e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  47 IVGGSNAQPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFMTNgtlePAAEWSVLLGVHSQDGPLDGAHTRAVAAI 125
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 126 VVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPLPLpwVLQEVELRLLGEAT 205
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 206 CQCLYSQPGPfnltlqILPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEAW 285
Cdd:cd00190  155 CKRAYSYGGT------ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                 ....
gi 385137135 286 IREQ 289
Cdd:cd00190  229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 46-286 7.18e-78

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: 249.90  E-value: 7.18e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135    46 RIVGGSNAQPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFMTNgtlePAAEWSVLLGVHSQDGPlDGAHTRAVAA 124
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFcGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGSHDLSSG-EEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135   125 IVVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPlPLPWVLQEVELRLLGEA 204
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135   205 TCQCLYSQPGPfnltlqILPGMLCAGYPEGRRDTCQGDSGGPLVCeEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEA 284
Cdd:smart00020 155 TCRRAYSGGGA------ITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227


                   ..
gi 385137135   285 WI 286
Cdd:smart00020 228 WI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 38-290 1.49e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 202.19  E-value: 1.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  38 CGRPEPSARIVGGSNAQPGTWPWQVSLHHGGGHICGG---SLIAPSWVLSAAHCFMTNGtlepAAEWSVLLGVHSQDGpl 114
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFcggTLIAPRWVLTAAHCVDGDG----PSDLRVVIGSTDLST-- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 115 DGAHTRAVAAIVVPANYSQVELGADLALLRLASPASLGPavwPVCLPRASHRFVHGTACWATGWGDVQEADPlPLPWVLQ 194
Cdd:COG5640   96 SGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 195 EVELRLLGEATCQcLYSQPGPfnltlqilPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPG 274
Cdd:COG5640  172 KADVPVVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242

                        250
                 ....*....|....*.
gi 385137135 275 VFTAVATYEAWIREQV 290
Cdd:COG5640  243 VYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
47-286 2.32e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 197.28  E-value: 2.32e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135   47 IVGGSNAQPGTWPWQVSLHHGGGHICGG-SLIAPSWVLSAAHCFmtngtlEPAAEWSVLLGVHSQDGPLDGAHTRAVAAI 125
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGgSLISENWVLTAAHCV------SGASDVKVVLGAHNIVLREGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  126 VVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPlplPWVLQEVELRLLGEAT 205
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  206 CQCLYSQPgpfnltlqILPGMLCAGYpeGRRDTCQGDSGGPLVCEEGgrwFQAGITSFGFGCGRRNRPGVFTAVATYEAW 285
Cdd:pfam00089 152 CRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218


                  .
gi 385137135  286 I 286
Cdd:pfam00089 219 I 219
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 330-538 4.98e-23

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: 98.50  E-value: 4.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 330 RPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFLDPNSSDspprdldaWRVLL--------PSRPRAERVARLVQH 400
Cdd:cd00190    8 KIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAPSN--------YTVRLgshdlssnEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 401 EN---ASWDNasDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGR-GEPALGPGALLEAEL--LGGWWCHC 474
Cdd:cd00190   80 PNynpSTYDN--DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRtSEGGPLPDVLQEVNVpiVSNAECKR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385137135 475 LYGRQGAavplpgDPPHALCpAYQEKEEVGSCWNDSRWSLLCQEEGTWFLAGIRDFPSGCLRPR 538
Cdd:cd00190  158 AYSYGGT------ITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPN 214
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 330-538 4.77e-21

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: 92.74  E-value: 4.77e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135   330 RPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFLDPNSSDSPPRdLDAWRVLLPSRPRAERVARLVQHEN---ASW 405
Cdd:smart00020   9 NIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRVR-LGSHDLSSGEEGQVIKVSKVIIHPNynpSTY 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135   406 DNasDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGRGEPALGPGA--LLEAEL--LGGWWCHCLYGRQGA 481
Cdd:smart00020  88 DN--DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVpiVSNATCRRAYSGGGA 165

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 385137135   482 avplpgDPPHALCpAYQEKEEVGSCWNDSRWSLLCQeEGTWFLAGIRDFPSGCLRPR 538
Cdd:smart00020 166 ------ITDNMLC-AGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPG 214
Trypsin pfam00089
Trypsin;
326-466 2.66e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 78.64  E-value: 2.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  326 GKAPRPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFldPNSSDSPPRDLDAWRVLLPSRPRAERVARLVQHENAS 404
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCV--SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 385137135  405 WDNA-SDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGRGEPALGPGALLEAEL 466
Cdd:pfam00089  82 PDTLdNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTV 144
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 601-650 4.99e-05

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: 43.31  E-value: 4.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 385137135  601 WPWLAEVHVAGDRVCTGILLAPGWVLAATHCvLRPGSTTVPYIEVYLGRA 650
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSC-LRDTNLRHQYISVVLGGA 49
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 601-661 1.19e-04

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: 44.19  E-value: 1.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 385137135 601 WPWLAEVHVAGDR-VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGRAGASSLPQGHQM 661
Cdd:cd00190   12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQV 70
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 601-649 1.60e-03

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 41.17  E-value: 1.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385137135 601 WPWLAEVHVAGDR---VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGR 649
Cdd:COG5640   42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGS 90
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 601-654 1.74e-03

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: 40.74  E-value: 1.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 385137135   601 WPWLAEVHVAGDR-VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGRAGASS 654
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGSDPSN---IRVRLGSHDLSS 64
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 47-289 4.02e-82

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: 261.06  E-value: 4.02e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  47 IVGGSNAQPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFMTNgtlePAAEWSVLLGVHSQDGPLDGAHTRAVAAI 125
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 126 VVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPLPLpwVLQEVELRLLGEAT 205
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 206 CQCLYSQPGPfnltlqILPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEAW 285
Cdd:cd00190  155 CKRAYSYGGT------ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                 ....
gi 385137135 286 IREQ 289
Cdd:cd00190  229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 46-286 7.18e-78

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: 249.90  E-value: 7.18e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135    46 RIVGGSNAQPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFMTNgtlePAAEWSVLLGVHSQDGPlDGAHTRAVAA 124
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFcGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGSHDLSSG-EEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135   125 IVVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPlPLPWVLQEVELRLLGEA 204
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135   205 TCQCLYSQPGPfnltlqILPGMLCAGYPEGRRDTCQGDSGGPLVCeEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEA 284
Cdd:smart00020 155 TCRRAYSGGGA------ITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227


                   ..
gi 385137135   285 WI 286
Cdd:smart00020 228 WI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 38-290 1.49e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 202.19  E-value: 1.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  38 CGRPEPSARIVGGSNAQPGTWPWQVSLHHGGGHICGG---SLIAPSWVLSAAHCFMTNGtlepAAEWSVLLGVHSQDGpl 114
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFcggTLIAPRWVLTAAHCVDGDG----PSDLRVVIGSTDLST-- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 115 DGAHTRAVAAIVVPANYSQVELGADLALLRLASPASLGPavwPVCLPRASHRFVHGTACWATGWGDVQEADPlPLPWVLQ 194
Cdd:COG5640   96 SGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 195 EVELRLLGEATCQcLYSQPGPfnltlqilPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPG 274
Cdd:COG5640  172 KADVPVVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242

                        250
                 ....*....|....*.
gi 385137135 275 VFTAVATYEAWIREQV 290
Cdd:COG5640  243 VYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
47-286 2.32e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 197.28  E-value: 2.32e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135   47 IVGGSNAQPGTWPWQVSLHHGGGHICGG-SLIAPSWVLSAAHCFmtngtlEPAAEWSVLLGVHSQDGPLDGAHTRAVAAI 125
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGgSLISENWVLTAAHCV------SGASDVKVVLGAHNIVLREGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  126 VVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPlplPWVLQEVELRLLGEAT 205
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  206 CQCLYSQPgpfnltlqILPGMLCAGYpeGRRDTCQGDSGGPLVCEEGgrwFQAGITSFGFGCGRRNRPGVFTAVATYEAW 285
Cdd:pfam00089 152 CRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218


                  .
gi 385137135  286 I 286
Cdd:pfam00089 219 I 219
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 330-538 4.98e-23

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: 98.50  E-value: 4.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 330 RPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFLDPNSSDspprdldaWRVLL--------PSRPRAERVARLVQH 400
Cdd:cd00190    8 KIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAPSN--------YTVRLgshdlssnEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 401 EN---ASWDNasDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGR-GEPALGPGALLEAEL--LGGWWCHC 474
Cdd:cd00190   80 PNynpSTYDN--DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRtSEGGPLPDVLQEVNVpiVSNAECKR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385137135 475 LYGRQGAavplpgDPPHALCpAYQEKEEVGSCWNDSRWSLLCQEEGTWFLAGIRDFPSGCLRPR 538
Cdd:cd00190  158 AYSYGGT------ITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPN 214
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 330-538 4.77e-21

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: 92.74  E-value: 4.77e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135   330 RPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFLDPNSSDSPPRdLDAWRVLLPSRPRAERVARLVQHEN---ASW 405
Cdd:smart00020   9 NIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRVR-LGSHDLSSGEEGQVIKVSKVIIHPNynpSTY 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135   406 DNasDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGRGEPALGPGA--LLEAEL--LGGWWCHCLYGRQGA 481
Cdd:smart00020  88 DN--DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVpiVSNATCRRAYSGGGA 165

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 385137135   482 avplpgDPPHALCpAYQEKEEVGSCWNDSRWSLLCQeEGTWFLAGIRDFPSGCLRPR 538
Cdd:smart00020 166 ------ITDNMLC-AGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPG 214
Trypsin pfam00089
Trypsin;
326-466 2.66e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 78.64  E-value: 2.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  326 GKAPRPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFldPNSSDSPPRDLDAWRVLLPSRPRAERVARLVQHENAS 404
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCV--SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 385137135  405 WDNA-SDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGRGEPALGPGALLEAEL 466
Cdd:pfam00089  82 PDTLdNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTV 144
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 75-272 5.40e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.61  E-value: 5.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  75 SLIAPSWVLSAAHCFMTNGTLEPAAEWSVLLGvhSQDGPldGAHTRAVAAIVVPANYSQVELGADLALLRLASPasLGPA 154
Cdd:COG3591   17 TLIGPNLVLTAGHCVYDGAGGGWATNIVFVPG--YNGGP--YGTATATRFRVPPGWVASGDAGYDYALLRLDEP--LGDT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135 155 VWPVCLpRASHRFVHGTACWATGWgdvqeadPLPLPWVLQevelrllgeATCQCLYSQPGPFNLTLQIlpgmlcagypeg 234
Cdd:COG3591   91 TGWLGL-AFNDAPLAGEPVTIIGY-------PGDRPKDLS---------LDCSGRVTGVQGNRLSYDC------------ 141

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 385137135 235 rrDTCQGDSGGPLVCEEGGRWFQAGITSFGfGCGRRNR 272
Cdd:COG3591  142 --DTTGGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT 176
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 334-444 4.49e-05

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: 43.31  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385137135  334 WPWEAQVMVPGSRPCHGALVSESWVLAPASCFLDPNSSDS-PPRDLDAWRVLLPSRPRAERVARLVQHENASwdnASDLA 412
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQyISVVLGGAKTLKSIEGPYEQIVRVDCRHDIP---ESEIS 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 385137135  413 LLQLRTPVNLSAASRPVCLPHPEHYFLPGSRC 444
Cdd:pfam09342  78 LLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 601-650 4.99e-05

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: 43.31  E-value: 4.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 385137135  601 WPWLAEVHVAGDRVCTGILLAPGWVLAATHCvLRPGSTTVPYIEVYLGRA 650
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSC-LRDTNLRHQYISVVLGGA 49
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 601-661 1.19e-04

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: 44.19  E-value: 1.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 385137135 601 WPWLAEVHVAGDR-VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGRAGASSLPQGHQM 661
Cdd:cd00190   12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQV 70
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 601-649 1.60e-03

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 41.17  E-value: 1.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385137135 601 WPWLAEVHVAGDR---VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGR 649
Cdd:COG5640   42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGS 90
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 601-654 1.74e-03

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: 40.74  E-value: 1.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 385137135   601 WPWLAEVHVAGDR-VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGRAGASS 654
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGSDPSN---IRVRLGSHDLSS 64
Trypsin pfam00089
Trypsin;
601-660 2.11e-03

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 40.12  E-value: 2.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385137135  601 WPWLAEVHVAGDRV-CTGILLAPGWVLAATHCVLRPGSttvpyIEVYLGRAGASSLPQGHQ 660
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLGAHNIVLREGGEQ 67
 
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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