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Conserved domains on  [gi|1958648454|ref|XP_038942639|]
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polyserase-2 isoform X1 [Rattus norvegicus]

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 ...
 59-301 2.02e-84

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: 269.53  E-value: 2.02e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  59 IVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPLEGAHMRSVATI 137
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 138 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVpwVLQEVELKLLGETA 217
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 218 CQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAVAHYESW 297
Cdd:cd00190   155 CKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                  ....
gi 1958648454 298 IREH 301
Cdd:cd00190   229 IQKT 232
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 607-802 8.23e-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: 98.12  E-value: 8.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 607 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYLGLAGVSSLPQGHQVSRSVVSIrlpRHSGLRPP 685
Cdd:cd00190    12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 686 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW-----KDPQNRVPVAAAVSILTPRLCHCLYQ--GAL 751
Cdd:cd00190    86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648454 752 TPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQTEGGpWVLVG 802
Cdd:cd00190   166 TDNMLCAGGLEGGKDAC--QG--DSG-G--------PLVCNDNGR-GVLVG 202
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 338-532 3.86e-21

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: 93.11  E-value: 3.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 338 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHdfETWRVLL--------PSRPEEKRVVRLVAHEN 408
Cdd:cd00190     4 GSEAKIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAP--SNYTVRLgshdlssnEGGGQVIKVKKVIVHPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 409 A-SRNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQL-EAQL--LNSWWCHCLYGr 484
Cdd:cd00190    82 YnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLqEVNVpiVSNAECKRAYS- 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958648454 485 qgesvPPPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCREEGTWFLAG 532
Cdd:cd00190   161 -----YGGTITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVG 202
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 59-301 2.02e-84

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: 269.53  E-value: 2.02e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  59 IVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPLEGAHMRSVATI 137
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 138 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVpwVLQEVELKLLGETA 217
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 218 CQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAVAHYESW 297
Cdd:cd00190   155 CKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                  ....
gi 1958648454 298 IREH 301
Cdd:cd00190   229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 58-298 6.18e-80

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: 257.61  E-value: 6.18e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454   58 RIVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPlEGAHMRSVAT 136
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFcGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGSHDLSSG-EEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  137 ILVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQEVELKLLGET 216
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  217 ACQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDgGRWFLAGITSFGFGCGRRNRPGVFTAVAHYES 296
Cdd:smart00020 155 TCRRAYSGGGAIT------DNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227


                   ..
gi 1958648454  297 WI 298
Cdd:smart00020 228 WI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 50-302 4.54e-60

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 205.27  E-value: 4.54e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  50 CGRPEPSSRIVGGSDAHPGTWPWQVSLHHGGGHICGG---SLIAPSWVLSAAHCFVTNGtlepADEWSVLLGVHSQDGPl 126
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFcggTLIAPRWVLTAAHCVDGDG----PSDLRVVIGSTDLSTS- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 127 eGAHMRSVATILVPDNYSRVELGADLALLRLASPAklgPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQ 206
Cdd:COG5640    97 -GGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 207 EVELKLLGETACQcLYSRPGPfnltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPG 286
Cdd:COG5640   172 KADVPVVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242

                         250
                  ....*....|....*.
gi 1958648454 287 VFTAVAHYESWIREHV 302
Cdd:COG5640   243 VYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
59-298 8.56e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 199.98  E-value: 8.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  59 IVGGSDAHPGTWPWQVSLHHGGGHICGG-SLIAPSWVLSAAHCFVTngtlepADEWSVLLGVHSQDGPLEGAHMRSVATI 137
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGgSLISENWVLTAAHCVSG------ASDVKVVLGAHNIVLREGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 138 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlpvPWVLQEVELKLLGETA 217
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 218 CQCLYSRPgpfnltlqLLPGMLCAGYpeGRRDTCQGDSGGPLVCEDGgrwFLAGITSFGFGCGRRNRPGVFTAVAHYESW 297
Cdd:pfam00089 152 CRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218


                  .
gi 1958648454 298 I 298
Cdd:pfam00089 219 I 219
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 607-802 8.23e-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: 98.12  E-value: 8.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 607 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYLGLAGVSSLPQGHQVSRSVVSIrlpRHSGLRPP 685
Cdd:cd00190    12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 686 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW-----KDPQNRVPVAAAVSILTPRLCHCLYQ--GAL 751
Cdd:cd00190    86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648454 752 TPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQTEGGpWVLVG 802
Cdd:cd00190   166 TDNMLCAGGLEGGKDAC--QG--DSG-G--------PLVCNDNGR-GVLVG 202
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 338-532 3.86e-21

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: 93.11  E-value: 3.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 338 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHdfETWRVLL--------PSRPEEKRVVRLVAHEN 408
Cdd:cd00190     4 GSEAKIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAP--SNYTVRLgshdlssnEGGGQVIKVKKVIVHPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 409 A-SRNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQL-EAQL--LNSWWCHCLYGr 484
Cdd:cd00190    82 YnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLqEVNVpiVSNAECKRAYS- 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958648454 485 qgesvPPPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCREEGTWFLAG 532
Cdd:cd00190   161 -----YGGTITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 607-802 1.86e-20

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: 91.20  E-value: 1.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  607 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCilrLGSSTVPYIDVYLGLAGVSSlpQGHQVSRSVVSIRlpRHSGLRPP 685
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHC---VRGSDPSNIRVRLGSHDLSS--GEEGQVIKVSKVI--IHPNYNPS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  686 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHCLYQG--A 750
Cdd:smart00020  86 tydndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtsegAGSLPDTLQEVNVPIVSNATCRRAYSGggA 165

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958648454  751 LTPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQteGGPWVLVG 802
Cdd:smart00020 166 ITDNMLCAGGLEGGKDAC--QG--DSG-G--------PLVCN--DGRWVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 338-532 4.03e-20

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: 90.04  E-value: 4.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  338 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHDFET-----WRVLLPSRPEEKRVVRLVAHENA-S 410
Cdd:smart00020   5 GSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRvrlgsHDLSSGEEGQVIKVSKVIIHPNYnP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  411 RNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGH-GEPAPRSSAQL-EAQL--LNSWWCHCLYGRQg 486
Cdd:smart00020  85 STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLqEVNVpiVSNATCRRAYSGG- 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958648454  487 esvppPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCrEEGTWFLAG 532
Cdd:smart00020 164 -----GAITDNMLC-AGGLEGGKDACQGDSGGPLVC-NDGRWVLVG 202
Trypsin pfam00089
Trypsin;
607-768 4.02e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 78.25  E-value: 4.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 607 WPWLTEVHVTGDRV-CTGILVAPGWVLAATHCILRLGSstvpyIDVYLGlAGVSSLPQGHQVSRSVVSIRlpRHSGLRPP 685
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLG-AHNIVLREGGEQKFDVEKII--VHPNYNPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 686 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGWKDPQNRVPVA----AAVSILTPRLCHCLYQGALTPG 754
Cdd:pfam00089  84 tldndIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDtlqeVTVPVVSRETCRSAYGGTVTDT 163

                         170
                  ....*....|....
gi 1958648454 755 TFCVFYTeeQEDRC 768
Cdd:pfam00089 164 MICAGAG--GKDAC 175
Trypsin pfam00089
Trypsin;
338-540 5.44e-14

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 72.09  E-value: 5.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 338 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSlHDFETW-----RVLLPSRPEEKRVVRLVAHENA-S 410
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA-SDVKVVlgahnIVLREGGEQKFDVEKIIVHPNYnP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 411 RNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQLEAQLLnswwchcLYGR-QGESV 489
Cdd:pfam00089  83 DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVP-------VVSReTCRSA 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648454 490 PPPGDPPHLLCpayQEEEEAGACWKDSGWSLLCREEgtwFLAGYRTLSNGC 540
Cdd:pfam00089 156 YGGTVTDTMIC---AGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGC 200
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 607-829 1.27e-11

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 65.83  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 607 WPWLTEVHVTGDR---VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYlglAGVSSLPQGHQVSRSVVSIRlpRHSGLR 683
Cdd:COG5640    42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVV---IGSTDLSTSGGTVVKVARIV--VHPDYD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 684 PP-----LALLELNsrvEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHcLYQGA 750
Cdd:COG5640   114 PAtpgndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtsegPGSQSGTLRKADVPVVSDATCA-AYGGF 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 751 LTPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLcQTEGGPWVLVGMAVRGSRE-------LFAAIGPEATWIS 823
Cdd:COG5640   190 DGGTMLCAGYPEGGKDAC--QG--DSG-G--------PLV-VKDGGGWVLVGVVSWGGGPcaagypgVYTRVSAYRDWIK 255


                  ....*.
gi 1958648454 824 QTVGEA 829
Cdd:COG5640   256 STAGGL 261
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 338-532 1.80e-08

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 56.58  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 338 GKATRPGTWPWEAQVMVPGSTP---CYGALVSDSWVLAPASCFLDSlhDFETWRV------LLPSRPEEKRVVRLVAHEN 408
Cdd:COG5640    34 GTPATVGEYPWMVALQSSNGPSgqfCGGTLIAPRWVLTAAHCVDGD--GPSDLRVvigstdLSTSGGTVVKVARIVVHPD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 409 -ASRNFASDLALLQLRTRVNLTAAPSavcLPHREHYFLPGSRCRLARWGHGEPAPRSSA----QLEAQLLNSWWChclyg 483
Cdd:COG5640   112 yDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSgtlrKADVPVVSDATC----- 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958648454 484 rqgeSVPPPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCREEGTWFLAG 532
Cdd:COG5640   184 ----AAYGGFDGGTMLC-AGYPEGGKDACQGDSGGPLVVKDGGGWVLVG 227
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 59-301 2.02e-84

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: 269.53  E-value: 2.02e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  59 IVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPLEGAHMRSVATI 137
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 138 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVpwVLQEVELKLLGETA 217
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 218 CQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAVAHYESW 297
Cdd:cd00190   155 CKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                  ....
gi 1958648454 298 IREH 301
Cdd:cd00190   229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 58-298 6.18e-80

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: 257.61  E-value: 6.18e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454   58 RIVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPlEGAHMRSVAT 136
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFcGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGSHDLSSG-EEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  137 ILVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQEVELKLLGET 216
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  217 ACQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDgGRWFLAGITSFGFGCGRRNRPGVFTAVAHYES 296
Cdd:smart00020 155 TCRRAYSGGGAIT------DNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227


                   ..
gi 1958648454  297 WI 298
Cdd:smart00020 228 WI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 50-302 4.54e-60

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 205.27  E-value: 4.54e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  50 CGRPEPSSRIVGGSDAHPGTWPWQVSLHHGGGHICGG---SLIAPSWVLSAAHCFVTNGtlepADEWSVLLGVHSQDGPl 126
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFcggTLIAPRWVLTAAHCVDGDG----PSDLRVVIGSTDLSTS- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 127 eGAHMRSVATILVPDNYSRVELGADLALLRLASPAklgPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQ 206
Cdd:COG5640    97 -GGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 207 EVELKLLGETACQcLYSRPGPfnltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPG 286
Cdd:COG5640   172 KADVPVVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242

                         250
                  ....*....|....*.
gi 1958648454 287 VFTAVAHYESWIREHV 302
Cdd:COG5640   243 VYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
59-298 8.56e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 199.98  E-value: 8.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  59 IVGGSDAHPGTWPWQVSLHHGGGHICGG-SLIAPSWVLSAAHCFVTngtlepADEWSVLLGVHSQDGPLEGAHMRSVATI 137
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGgSLISENWVLTAAHCVSG------ASDVKVVLGAHNIVLREGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 138 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlpvPWVLQEVELKLLGETA 217
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 218 CQCLYSRPgpfnltlqLLPGMLCAGYpeGRRDTCQGDSGGPLVCEDGgrwFLAGITSFGFGCGRRNRPGVFTAVAHYESW 297
Cdd:pfam00089 152 CRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218


                  .
gi 1958648454 298 I 298
Cdd:pfam00089 219 I 219
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 607-802 8.23e-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: 98.12  E-value: 8.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 607 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYLGLAGVSSLPQGHQVSRSVVSIrlpRHSGLRPP 685
Cdd:cd00190    12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 686 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW-----KDPQNRVPVAAAVSILTPRLCHCLYQ--GAL 751
Cdd:cd00190    86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648454 752 TPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQTEGGpWVLVG 802
Cdd:cd00190   166 TDNMLCAGGLEGGKDAC--QG--DSG-G--------PLVCNDNGR-GVLVG 202
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 338-532 3.86e-21

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: 93.11  E-value: 3.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 338 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHdfETWRVLL--------PSRPEEKRVVRLVAHEN 408
Cdd:cd00190     4 GSEAKIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAP--SNYTVRLgshdlssnEGGGQVIKVKKVIVHPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 409 A-SRNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQL-EAQL--LNSWWCHCLYGr 484
Cdd:cd00190    82 YnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLqEVNVpiVSNAECKRAYS- 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958648454 485 qgesvPPPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCREEGTWFLAG 532
Cdd:cd00190   161 -----YGGTITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 607-802 1.86e-20

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: 91.20  E-value: 1.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  607 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCilrLGSSTVPYIDVYLGLAGVSSlpQGHQVSRSVVSIRlpRHSGLRPP 685
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHC---VRGSDPSNIRVRLGSHDLSS--GEEGQVIKVSKVI--IHPNYNPS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  686 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHCLYQG--A 750
Cdd:smart00020  86 tydndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtsegAGSLPDTLQEVNVPIVSNATCRRAYSGggA 165

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958648454  751 LTPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQteGGPWVLVG 802
Cdd:smart00020 166 ITDNMLCAGGLEGGKDAC--QG--DSG-G--------PLVCN--DGRWVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 338-532 4.03e-20

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: 90.04  E-value: 4.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  338 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHDFET-----WRVLLPSRPEEKRVVRLVAHENA-S 410
Cdd:smart00020   5 GSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRvrlgsHDLSSGEEGQVIKVSKVIIHPNYnP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  411 RNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGH-GEPAPRSSAQL-EAQL--LNSWWCHCLYGRQg 486
Cdd:smart00020  85 STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLqEVNVpiVSNATCRRAYSGG- 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958648454  487 esvppPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCrEEGTWFLAG 532
Cdd:smart00020 164 -----GAITDNMLC-AGGLEGGKDACQGDSGGPLVC-NDGRWVLVG 202
Trypsin pfam00089
Trypsin;
607-768 4.02e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 78.25  E-value: 4.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 607 WPWLTEVHVTGDRV-CTGILVAPGWVLAATHCILRLGSstvpyIDVYLGlAGVSSLPQGHQVSRSVVSIRlpRHSGLRPP 685
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLG-AHNIVLREGGEQKFDVEKII--VHPNYNPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 686 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGWKDPQNRVPVA----AAVSILTPRLCHCLYQGALTPG 754
Cdd:pfam00089  84 tldndIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDtlqeVTVPVVSRETCRSAYGGTVTDT 163

                         170
                  ....*....|....
gi 1958648454 755 TFCVFYTeeQEDRC 768
Cdd:pfam00089 164 MICAGAG--GKDAC 175
Trypsin pfam00089
Trypsin;
338-540 5.44e-14

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 72.09  E-value: 5.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 338 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSlHDFETW-----RVLLPSRPEEKRVVRLVAHENA-S 410
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA-SDVKVVlgahnIVLREGGEQKFDVEKIIVHPNYnP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 411 RNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQLEAQLLnswwchcLYGR-QGESV 489
Cdd:pfam00089  83 DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVP-------VVSReTCRSA 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648454 490 PPPGDPPHLLCpayQEEEEAGACWKDSGWSLLCREEgtwFLAGYRTLSNGC 540
Cdd:pfam00089 156 YGGTVTDTMIC---AGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGC 200
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 607-829 1.27e-11

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 65.83  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 607 WPWLTEVHVTGDR---VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYlglAGVSSLPQGHQVSRSVVSIRlpRHSGLR 683
Cdd:COG5640    42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVV---IGSTDLSTSGGTVVKVARIV--VHPDYD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 684 PP-----LALLELNsrvEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHcLYQGA 750
Cdd:COG5640   114 PAtpgndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtsegPGSQSGTLRKADVPVVSDATCA-AYGGF 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 751 LTPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLcQTEGGPWVLVGMAVRGSRE-------LFAAIGPEATWIS 823
Cdd:COG5640   190 DGGTMLCAGYPEGGKDAC--QG--DSG-G--------PLV-VKDGGGWVLVGVVSWGGGPcaagypgVYTRVSAYRDWIK 255


                  ....*.
gi 1958648454 824 QTVGEA 829
Cdd:COG5640   256 STAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 87-284 1.96e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 58.15  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454  87 SLIAPSWVLSAAHCFVTNGTLEPADEWSVLLGvhSQDGPLEGAHMRSVATilVPDNYSRVELGADLALLRLASPakLGPS 166
Cdd:COG3591    17 TLIGPNLVLTAGHCVYDGAGGGWATNIVFVPG--YNGGPYGTATATRFRV--PPGWVASGDAGYDYALLRLDEP--LGDT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 167 VKPVCLpRASHLFAHGTACWATGWGDVQESDPlpvpwvlqevelkllgETACQCLYSRPGPFNLTLQllpgmlCagypeg 246
Cdd:COG3591    91 TGWLGL-AFNDAPLAGEPVTIIGYPGDRPKDL----------------SLDCSGRVTGVQGNRLSYD------C------ 141

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958648454 247 rrDTCQGDSGGPLVCEDGGRWFLAGITSFGfGCGRRNR 284
Cdd:COG3591   142 --DTTGGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT 176
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 338-532 1.80e-08

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 56.58  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 338 GKATRPGTWPWEAQVMVPGSTP---CYGALVSDSWVLAPASCFLDSlhDFETWRV------LLPSRPEEKRVVRLVAHEN 408
Cdd:COG5640    34 GTPATVGEYPWMVALQSSNGPSgqfCGGTLIAPRWVLTAAHCVDGD--GPSDLRVvigstdLSTSGGTVVKVARIVVHPD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 409 -ASRNFASDLALLQLRTRVNLTAAPSavcLPHREHYFLPGSRCRLARWGHGEPAPRSSA----QLEAQLLNSWWChclyg 483
Cdd:COG5640   112 yDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSgtlrKADVPVVSDATC----- 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958648454 484 rqgeSVPPPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCREEGTWFLAG 532
Cdd:COG5640   184 ----AAYGGFDGGTMLC-AGYPEGGKDACQGDSGGPLVVKDGGGWVLVG 227
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 607-654 1.82e-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: 44.85  E-value: 1.82e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958648454 607 WPWLTEVHVTGDRVCTGILVAPGWVLAATHCiLRLGSSTVPYIDVYLG 654
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSC-LRDTNLRHQYISVVLG 47
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 346-450 1.30e-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: 39.45  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648454 346 WPWEAQVMVPGSTPCYGALVSDSWVLAPASCFLDSLHDFETWRVLLPS-------RPEEKRVVRLVAHENASRnfaSDLA 418
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGaktlksiEGPYEQIVRVDCRHDIPE---SEIS 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958648454 419 LLQLRTRVNLTAAPSAVCLPHREHYFLPGSRC 450
Cdd:pfam09342  78 LLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
 
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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