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Conserved domains on  [gi|1958648456|ref|XP_038942643|]
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polyserase-2 isoform X2 [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 ...
 58-300 2.03e-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: 2.03e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  58 IVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPLEGAHMRSVATI 136
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 137 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVpwVLQEVELKLLGETA 216
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 217 CQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAVAHYESW 296
Cdd:cd00190   155 CKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                  ....
gi 1958648456 297 IREH 300
Cdd:cd00190   229 IQKT 232
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 606-801 8.22e-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: 8.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 606 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYLGLAGVSSLPQGHQVSRSVVSIrlpRHSGLRPP 684
Cdd:cd00190    12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 685 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW-----KDPQNRVPVAAAVSILTPRLCHCLYQ--GAL 750
Cdd:cd00190    86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648456 751 TPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQTEGGpWVLVG 801
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 ...
 337-531 3.74e-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: 3.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 337 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHdfETWRVLL--------PSRPEEKRVVRLVAHEN 407
Cdd:cd00190     4 GSEAKIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAP--SNYTVRLgshdlssnEGGGQVIKVKKVIVHPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 408 A-SRNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQL-EAQL--LNSWWCHCLYGr 483
Cdd:cd00190    82 YnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLqEVNVpiVSNAECKRAYS- 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958648456 484 qgesvPPPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCREEGTWFLAG 531
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 ...
 58-300 2.03e-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: 2.03e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  58 IVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPLEGAHMRSVATI 136
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 137 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVpwVLQEVELKLLGETA 216
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 217 CQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAVAHYESW 296
Cdd:cd00190   155 CKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                  ....
gi 1958648456 297 IREH 300
Cdd:cd00190   229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 57-297 6.28e-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: 6.28e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456   57 RIVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPlEGAHMRSVAT 135
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFcGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGSHDLSSG-EEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  136 ILVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQEVELKLLGET 215
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  216 ACQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDgGRWFLAGITSFGFGCGRRNRPGVFTAVAHYES 295
Cdd:smart00020 155 TCRRAYSGGGAIT------DNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227


                   ..
gi 1958648456  296 WI 297
Cdd:smart00020 228 WI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 49-301 3.90e-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: 3.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  49 CGRPEPSSRIVGGSDAHPGTWPWQVSLHHGGGHICGG---SLIAPSWVLSAAHCFVTNGtlepADEWSVLLGVHSQDGPl 125
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFcggTLIAPRWVLTAAHCVDGDG----PSDLRVVIGSTDLSTS- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 126 eGAHMRSVATILVPDNYSRVELGADLALLRLASPAklgPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQ 205
Cdd:COG5640    97 -GGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 206 EVELKLLGETACQcLYSRPGPfnltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPG 285
Cdd:COG5640   172 KADVPVVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242

                         250
                  ....*....|....*.
gi 1958648456 286 VFTAVAHYESWIREHV 301
Cdd:COG5640   243 VYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
58-297 8.67e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 199.98  E-value: 8.67e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  58 IVGGSDAHPGTWPWQVSLHHGGGHICGG-SLIAPSWVLSAAHCFVTngtlepADEWSVLLGVHSQDGPLEGAHMRSVATI 136
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGgSLISENWVLTAAHCVSG------ASDVKVVLGAHNIVLREGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 137 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlpvPWVLQEVELKLLGETA 216
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 217 CQCLYSRPgpfnltlqLLPGMLCAGYpeGRRDTCQGDSGGPLVCEDGgrwFLAGITSFGFGCGRRNRPGVFTAVAHYESW 296
Cdd:pfam00089 152 CRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218


                  .
gi 1958648456 297 I 297
Cdd:pfam00089 219 I 219
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 606-801 8.22e-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: 8.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 606 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYLGLAGVSSLPQGHQVSRSVVSIrlpRHSGLRPP 684
Cdd:cd00190    12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 685 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW-----KDPQNRVPVAAAVSILTPRLCHCLYQ--GAL 750
Cdd:cd00190    86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648456 751 TPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQTEGGpWVLVG 801
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 ...
 337-531 3.74e-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: 3.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 337 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHdfETWRVLL--------PSRPEEKRVVRLVAHEN 407
Cdd:cd00190     4 GSEAKIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAP--SNYTVRLgshdlssnEGGGQVIKVKKVIVHPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 408 A-SRNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQL-EAQL--LNSWWCHCLYGr 483
Cdd:cd00190    82 YnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLqEVNVpiVSNAECKRAYS- 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958648456 484 qgesvPPPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCREEGTWFLAG 531
Cdd:cd00190   161 -----YGGTITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 606-801 1.89e-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: 1.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  606 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCilrLGSSTVPYIDVYLGLAGVSSlpQGHQVSRSVVSIRlpRHSGLRPP 684
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHC---VRGSDPSNIRVRLGSHDLSS--GEEGQVIKVSKVI--IHPNYNPS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  685 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHCLYQG--A 749
Cdd:smart00020  86 tydndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtsegAGSLPDTLQEVNVPIVSNATCRRAYSGggA 165

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958648456  750 LTPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQteGGPWVLVG 801
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 ...
 337-531 4.18e-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: 4.18e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  337 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHDFET-----WRVLLPSRPEEKRVVRLVAHENA-S 409
Cdd:smart00020   5 GSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRvrlgsHDLSSGEEGQVIKVSKVIIHPNYnP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  410 RNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGH-GEPAPRSSAQL-EAQL--LNSWWCHCLYGRQg 485
Cdd:smart00020  85 STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLqEVNVpiVSNATCRRAYSGG- 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958648456  486 esvppPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCrEEGTWFLAG 531
Cdd:smart00020 164 -----GAITDNMLC-AGGLEGGKDACQGDSGGPLVC-NDGRWVLVG 202
Trypsin pfam00089
Trypsin;
606-767 4.09e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 78.25  E-value: 4.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 606 WPWLTEVHVTGDRV-CTGILVAPGWVLAATHCILRLGSstvpyIDVYLGlAGVSSLPQGHQVSRSVVSIRlpRHSGLRPP 684
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLG-AHNIVLREGGEQKFDVEKII--VHPNYNPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 685 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGWKDPQNRVPVA----AAVSILTPRLCHCLYQGALTPG 753
Cdd:pfam00089  84 tldndIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDtlqeVTVPVVSRETCRSAYGGTVTDT 163

                         170
                  ....*....|....
gi 1958648456 754 TFCVFYTeeQEDRC 767
Cdd:pfam00089 164 MICAGAG--GKDAC 175
Trypsin pfam00089
Trypsin;
337-539 5.49e-14

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 72.09  E-value: 5.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 337 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSlHDFETW-----RVLLPSRPEEKRVVRLVAHENA-S 409
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA-SDVKVVlgahnIVLREGGEQKFDVEKIIVHPNYnP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 410 RNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQLEAQLLnswwchcLYGR-QGESV 488
Cdd:pfam00089  83 DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVP-------VVSReTCRSA 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648456 489 PPPGDPPHLLCpayQEEEEAGACWKDSGWSLLCREEgtwFLAGYRTLSNGC 539
Cdd:pfam00089 156 YGGTVTDTMIC---AGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGC 200
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 606-828 1.17e-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: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 606 WPWLTEVHVTGDR---VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYlglAGVSSLPQGHQVSRSVVSIRlpRHSGLR 682
Cdd:COG5640    42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVV---IGSTDLSTSGGTVVKVARIV--VHPDYD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 683 PP-----LALLELNsrvEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHcLYQGA 749
Cdd:COG5640   114 PAtpgndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtsegPGSQSGTLRKADVPVVSDATCA-AYGGF 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 750 LTPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLcQTEGGPWVLVGMAVRGSRE-------LFAAIGPEATWIS 822
Cdd:COG5640   190 DGGTMLCAGYPEGGKDAC--QG--DSG-G--------PLV-VKDGGGWVLVGVVSWGGGPcaagypgVYTRVSAYRDWIK 255


                  ....*.
gi 1958648456 823 QTVGEA 828
Cdd:COG5640   256 STAGGL 261
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 337-531 1.77e-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: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 337 GKATRPGTWPWEAQVMVPGSTP---CYGALVSDSWVLAPASCFLDSlhDFETWRV------LLPSRPEEKRVVRLVAHEN 407
Cdd:COG5640    34 GTPATVGEYPWMVALQSSNGPSgqfCGGTLIAPRWVLTAAHCVDGD--GPSDLRVvigstdLSTSGGTVVKVARIVVHPD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 408 -ASRNFASDLALLQLRTRVNLTAAPSavcLPHREHYFLPGSRCRLARWGHGEPAPRSSA----QLEAQLLNSWWChclyg 482
Cdd:COG5640   112 yDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSgtlrKADVPVVSDATC----- 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958648456 483 rqgeSVPPPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCREEGTWFLAG 531
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 ...
 58-300 2.03e-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: 2.03e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  58 IVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPLEGAHMRSVATI 136
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 137 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVpwVLQEVELKLLGETA 216
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 217 CQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAVAHYESW 296
Cdd:cd00190   155 CKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                  ....
gi 1958648456 297 IREH 300
Cdd:cd00190   229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 57-297 6.28e-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: 6.28e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456   57 RIVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPlEGAHMRSVAT 135
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFcGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGSHDLSSG-EEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  136 ILVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQEVELKLLGET 215
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  216 ACQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDgGRWFLAGITSFGFGCGRRNRPGVFTAVAHYES 295
Cdd:smart00020 155 TCRRAYSGGGAIT------DNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227


                   ..
gi 1958648456  296 WI 297
Cdd:smart00020 228 WI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 49-301 3.90e-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: 3.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  49 CGRPEPSSRIVGGSDAHPGTWPWQVSLHHGGGHICGG---SLIAPSWVLSAAHCFVTNGtlepADEWSVLLGVHSQDGPl 125
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFcggTLIAPRWVLTAAHCVDGDG----PSDLRVVIGSTDLSTS- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 126 eGAHMRSVATILVPDNYSRVELGADLALLRLASPAklgPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQ 205
Cdd:COG5640    97 -GGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 206 EVELKLLGETACQcLYSRPGPfnltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPG 285
Cdd:COG5640   172 KADVPVVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242

                         250
                  ....*....|....*.
gi 1958648456 286 VFTAVAHYESWIREHV 301
Cdd:COG5640   243 VYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
58-297 8.67e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 199.98  E-value: 8.67e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  58 IVGGSDAHPGTWPWQVSLHHGGGHICGG-SLIAPSWVLSAAHCFVTngtlepADEWSVLLGVHSQDGPLEGAHMRSVATI 136
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGgSLISENWVLTAAHCVSG------ASDVKVVLGAHNIVLREGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 137 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlpvPWVLQEVELKLLGETA 216
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 217 CQCLYSRPgpfnltlqLLPGMLCAGYpeGRRDTCQGDSGGPLVCEDGgrwFLAGITSFGFGCGRRNRPGVFTAVAHYESW 296
Cdd:pfam00089 152 CRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218


                  .
gi 1958648456 297 I 297
Cdd:pfam00089 219 I 219
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 606-801 8.22e-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: 8.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 606 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYLGLAGVSSLPQGHQVSRSVVSIrlpRHSGLRPP 684
Cdd:cd00190    12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 685 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW-----KDPQNRVPVAAAVSILTPRLCHCLYQ--GAL 750
Cdd:cd00190    86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648456 751 TPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQTEGGpWVLVG 801
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 ...
 337-531 3.74e-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: 3.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 337 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHdfETWRVLL--------PSRPEEKRVVRLVAHEN 407
Cdd:cd00190     4 GSEAKIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAP--SNYTVRLgshdlssnEGGGQVIKVKKVIVHPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 408 A-SRNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQL-EAQL--LNSWWCHCLYGr 483
Cdd:cd00190    82 YnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLqEVNVpiVSNAECKRAYS- 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958648456 484 qgesvPPPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCREEGTWFLAG 531
Cdd:cd00190   161 -----YGGTITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 606-801 1.89e-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: 1.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  606 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCilrLGSSTVPYIDVYLGLAGVSSlpQGHQVSRSVVSIRlpRHSGLRPP 684
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHC---VRGSDPSNIRVRLGSHDLSS--GEEGQVIKVSKVI--IHPNYNPS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  685 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHCLYQG--A 749
Cdd:smart00020  86 tydndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtsegAGSLPDTLQEVNVPIVSNATCRRAYSGggA 165

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958648456  750 LTPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQteGGPWVLVG 801
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 ...
 337-531 4.18e-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: 4.18e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  337 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHDFET-----WRVLLPSRPEEKRVVRLVAHENA-S 409
Cdd:smart00020   5 GSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRvrlgsHDLSSGEEGQVIKVSKVIIHPNYnP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  410 RNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGH-GEPAPRSSAQL-EAQL--LNSWWCHCLYGRQg 485
Cdd:smart00020  85 STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLqEVNVpiVSNATCRRAYSGG- 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958648456  486 esvppPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCrEEGTWFLAG 531
Cdd:smart00020 164 -----GAITDNMLC-AGGLEGGKDACQGDSGGPLVC-NDGRWVLVG 202
Trypsin pfam00089
Trypsin;
606-767 4.09e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 78.25  E-value: 4.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 606 WPWLTEVHVTGDRV-CTGILVAPGWVLAATHCILRLGSstvpyIDVYLGlAGVSSLPQGHQVSRSVVSIRlpRHSGLRPP 684
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLG-AHNIVLREGGEQKFDVEKII--VHPNYNPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 685 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGWKDPQNRVPVA----AAVSILTPRLCHCLYQGALTPG 753
Cdd:pfam00089  84 tldndIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDtlqeVTVPVVSRETCRSAYGGTVTDT 163

                         170
                  ....*....|....
gi 1958648456 754 TFCVFYTeeQEDRC 767
Cdd:pfam00089 164 MICAGAG--GKDAC 175
Trypsin pfam00089
Trypsin;
337-539 5.49e-14

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 72.09  E-value: 5.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 337 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSlHDFETW-----RVLLPSRPEEKRVVRLVAHENA-S 409
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA-SDVKVVlgahnIVLREGGEQKFDVEKIIVHPNYnP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 410 RNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQLEAQLLnswwchcLYGR-QGESV 488
Cdd:pfam00089  83 DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVP-------VVSReTCRSA 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648456 489 PPPGDPPHLLCpayQEEEEAGACWKDSGWSLLCREEgtwFLAGYRTLSNGC 539
Cdd:pfam00089 156 YGGTVTDTMIC---AGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGC 200
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 606-828 1.17e-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: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 606 WPWLTEVHVTGDR---VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYlglAGVSSLPQGHQVSRSVVSIRlpRHSGLR 682
Cdd:COG5640    42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVV---IGSTDLSTSGGTVVKVARIV--VHPDYD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 683 PP-----LALLELNsrvEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHcLYQGA 749
Cdd:COG5640   114 PAtpgndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtsegPGSQSGTLRKADVPVVSDATCA-AYGGF 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 750 LTPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLcQTEGGPWVLVGMAVRGSRE-------LFAAIGPEATWIS 822
Cdd:COG5640   190 DGGTMLCAGYPEGGKDAC--QG--DSG-G--------PLV-VKDGGGWVLVGVVSWGGGPcaagypgVYTRVSAYRDWIK 255


                  ....*.
gi 1958648456 823 QTVGEA 828
Cdd:COG5640   256 STAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 86-283 1.86e-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: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456  86 SLIAPSWVLSAAHCFVTNGTLEPADEWSVLLGvhSQDGPLEGAHMRSVATilVPDNYSRVELGADLALLRLASPakLGPS 165
Cdd:COG3591    17 TLIGPNLVLTAGHCVYDGAGGGWATNIVFVPG--YNGGPYGTATATRFRV--PPGWVASGDAGYDYALLRLDEP--LGDT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 166 VKPVCLpRASHLFAHGTACWATGWGDVQESDPlpvpwvlqevelkllgETACQCLYSRPGPFNLTLQllpgmlCagypeg 245
Cdd:COG3591    91 TGWLGL-AFNDAPLAGEPVTIIGYPGDRPKDL----------------SLDCSGRVTGVQGNRLSYD------C------ 141

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958648456 246 rrDTCQGDSGGPLVCEDGGRWFLAGITSFGfGCGRRNR 283
Cdd:COG3591   142 --DTTGGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT 176
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 337-531 1.77e-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: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 337 GKATRPGTWPWEAQVMVPGSTP---CYGALVSDSWVLAPASCFLDSlhDFETWRV------LLPSRPEEKRVVRLVAHEN 407
Cdd:COG5640    34 GTPATVGEYPWMVALQSSNGPSgqfCGGTLIAPRWVLTAAHCVDGD--GPSDLRVvigstdLSTSGGTVVKVARIVVHPD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 408 -ASRNFASDLALLQLRTRVNLTAAPSavcLPHREHYFLPGSRCRLARWGHGEPAPRSSA----QLEAQLLNSWWChclyg 482
Cdd:COG5640   112 yDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSgtlrKADVPVVSDATC----- 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958648456 483 rqgeSVPPPGDPPHLLCpAYQEEEEAGACWKDSGWSLLCREEGTWFLAG 531
Cdd:COG5640   184 ----AAYGGFDGGTMLC-AGYPEGGKDACQGDSGGPLVVKDGGGWVLVG 227
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 606-653 1.80e-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: 1.80e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958648456 606 WPWLTEVHVTGDRVCTGILVAPGWVLAATHCiLRLGSSTVPYIDVYLG 653
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSC-LRDTNLRHQYISVVLG 47
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 345-449 1.31e-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: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648456 345 WPWEAQVMVPGSTPCYGALVSDSWVLAPASCFLDSLHDFETWRVLLPS-------RPEEKRVVRLVAHENASRnfaSDLA 417
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGaktlksiEGPYEQIVRVDCRHDIPE---SEIS 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958648456 418 LLQLRTRVNLTAAPSAVCLPHREHYFLPGSRC 449
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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