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Conserved domains on  [gi|386781478|ref|NP_001011560|]
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polyserase-2 precursor [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 ...
 47-289 2.46e-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: 269.15  E-value: 2.46e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  47 IVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPLEGAHMRSVATI 125
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 126 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVpwVLQEVELKLLGETA 205
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 206 CQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAVAHYESW 285
Cdd:cd00190  155 CKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                 ....
gi 386781478 286 IREH 289
Cdd:cd00190  229 IQKT 232
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 595-777 2.80e-24

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: 102.35  E-value: 2.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 595 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYLGLAGVSSLPQGHQVSRSVVSIrlpRHSGLRPP 673
Cdd:cd00190   12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 674 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW-----KDPQNRVPVAAAVSILTPRLCHCLYQ--GAL 739
Cdd:cd00190   86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 386781478 740 TPGTFCVFYTEEQEDRCEMTSAPPLLCQTEGGpWVLVG 777
Cdd:cd00190  166 TDNMLCAGGLEGGKDACQGDSGGPLVCNDNGR-GVLVG 202
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 326-520 4.54e-19

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: 86.95  E-value: 4.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 326 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHDF------ETWRVLLPSRPEEKRVVRLVAHENA- 397
Cdd:cd00190    4 GSEAKIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAPSNytvrlgSHDLSSNEGGGQVIKVKKVIVHPNYn 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 398 SRNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQL-EAQL--LNSWWCHCLYGrqg 474
Cdd:cd00190   84 PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLqEVNVpiVSNAECKRAYS--- 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 386781478 475 esvPPPGDPPHLLCpAYQEEEEAGACWVNSGWSLLCREEGTWFLAG 520
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 ...
 47-289 2.46e-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: 269.15  E-value: 2.46e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  47 IVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPLEGAHMRSVATI 125
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 126 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVpwVLQEVELKLLGETA 205
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 206 CQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAVAHYESW 285
Cdd:cd00190  155 CKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                 ....
gi 386781478 286 IREH 289
Cdd:cd00190  229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 46-286 9.42e-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: 256.84  E-value: 9.42e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478    46 RIVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPlEGAHMRSVAT 124
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFcGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGSHDLSSG-EEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   125 ILVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQEVELKLLGET 204
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   205 ACQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDgGRWFLAGITSFGFGCGRRNRPGVFTAVAHYES 284
Cdd:smart00020 155 TCRRAYSGGGAIT------DNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227


                   ..
gi 386781478   285 WI 286
Cdd:smart00020 228 WI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 38-290 5.68e-60

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 204.50  E-value: 5.68e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  38 CGRPEPSSRIVGGSDAHPGTWPWQVSLHHGGGHICGG---SLIAPSWVLSAAHCFVTNGtlepADEWSVLLGVHSQDGPl 114
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFcggTLIAPRWVLTAAHCVDGDG----PSDLRVVIGSTDLSTS- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 115 eGAHMRSVATILVPDNYSRVELGADLALLRLASPAklgPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQ 194
Cdd:COG5640   97 -GGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 195 EVELKLLGETACQcLYSRPGPfnltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPG 274
Cdd:COG5640  172 KADVPVVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242

                        250
                 ....*....|....*.
gi 386781478 275 VFTAVAHYESWIREHV 290
Cdd:COG5640  243 VYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
47-286 1.12e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 199.59  E-value: 1.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   47 IVGGSDAHPGTWPWQVSLHHGGGHICGG-SLIAPSWVLSAAHCFVTngtlepADEWSVLLGVHSQDGPLEGAHMRSVATI 125
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGgSLISENWVLTAAHCVSG------ASDVKVVLGAHNIVLREGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  126 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlpvPWVLQEVELKLLGETA 205
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  206 CQCLYSRPgpfnltlqLLPGMLCAGYpeGRRDTCQGDSGGPLVCEDGgrwFLAGITSFGFGCGRRNRPGVFTAVAHYESW 285
Cdd:pfam00089 152 CRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218


                  .
gi 386781478  286 I 286
Cdd:pfam00089 219 I 219
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 595-777 2.80e-24

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: 102.35  E-value: 2.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 595 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYLGLAGVSSLPQGHQVSRSVVSIrlpRHSGLRPP 673
Cdd:cd00190   12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 674 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW-----KDPQNRVPVAAAVSILTPRLCHCLYQ--GAL 739
Cdd:cd00190   86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 386781478 740 TPGTFCVFYTEEQEDRCEMTSAPPLLCQTEGGpWVLVG 777
Cdd:cd00190  166 TDNMLCAGGLEGGKDACQGDSGGPLVCNDNGR-GVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 595-777 6.54e-22

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: 95.44  E-value: 6.54e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   595 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCilrLGSSTVPYIDVYLGLAGVSSlpQGHQVSRSVVSIRlpRHSGLRPP 673
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHC---VRGSDPSNIRVRLGSHDLSS--GEEGQVIKVSKVI--IHPNYNPS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   674 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHCLYQG--A 738
Cdd:smart00020  86 tydndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtsegAGSLPDTLQEVNVPIVSNATCRRAYSGggA 165

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 386781478   739 LTPGTFCVFYTEEQEDRCEMTSAPPLLCQteGGPWVLVG 777
Cdd:smart00020 166 ITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVG 202
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 326-520 4.54e-19

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: 86.95  E-value: 4.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 326 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHDF------ETWRVLLPSRPEEKRVVRLVAHENA- 397
Cdd:cd00190    4 GSEAKIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAPSNytvrlgSHDLSSNEGGGQVIKVKKVIVHPNYn 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 398 SRNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQL-EAQL--LNSWWCHCLYGrqg 474
Cdd:cd00190   84 PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLqEVNVpiVSNAECKRAYS--- 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 386781478 475 esvPPPGDPPHLLCpAYQEEEEAGACWVNSGWSLLCREEGTWFLAG 520
Cdd:cd00190  161 ---YGGTITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 326-520 4.50e-18

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: 84.27  E-value: 4.50e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   326 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHDFET-----WRVLLPSRPEEKRVVRLVAHENA-S 398
Cdd:smart00020   5 GSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRvrlgsHDLSSGEEGQVIKVSKVIIHPNYnP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   399 RNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGH-GEPAPRSSAQL-EAQL--LNSWWCHCLYGRQg 474
Cdd:smart00020  85 STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLqEVNVpiVSNATCRRAYSGG- 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 386781478   475 esvppPGDPPHLLCpAYQEEEEAGACWVNSGWSLLCrEEGTWFLAG 520
Cdd:smart00020 164 -----GAITDNMLC-AGGLEGGKDACQGDSGGPLVC-NDGRWVLVG 202
Trypsin pfam00089
Trypsin;
595-766 6.74e-17

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 80.56  E-value: 6.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  595 WPWLTEVHVTGDRV-CTGILVAPGWVLAATHCILRLGSstvpyIDVYLGlAGVSSLPQGHQVSRSVVSIRlpRHSGLRPP 673
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLG-AHNIVLREGGEQKFDVEKII--VHPNYNPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  674 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGWKDPQNRVPVA----AAVSILTPRLCHCLYQGALTPG 742
Cdd:pfam00089  84 tldndIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDtlqeVTVPVVSRETCRSAYGGTVTDT 163

                         170       180
                  ....*....|....*....|....
gi 386781478  743 TFCVFYTeeQEDRCEMTSAPPLLC 766
Cdd:pfam00089 164 MICAGAG--GKDACQGDSGGPLVC 185
Trypsin pfam00089
Trypsin;
326-528 2.35e-13

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 70.16  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  326 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSlHDFETW-----RVLLPSRPEEKRVVRLVAHENA-S 398
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA-SDVKVVlgahnIVLREGGEQKFDVEKIIVHPNYnP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  399 RNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQLEAQLLnswwchcLYGR-QGESV 477
Cdd:pfam00089  83 DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVP-------VVSReTCRSA 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386781478  478 PPPGDPPHLLCpayQEEEEAGACWVNSGWSLLCREEgtwFLAGYRTLSNGC 528
Cdd:pfam00089 156 YGGTVTDTMIC---AGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGC 200
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 595-804 4.05e-12

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 67.37  E-value: 4.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 595 WPWLTEVHVTGDR---VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYlglAGVSSLPQGHQVSRSVVSIRlpRHSGLR 671
Cdd:COG5640   42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVV---IGSTDLSTSGGTVVKVARIV--VHPDYD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 672 PP-----LALLELNsrvEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHcLYQGA 738
Cdd:COG5640  114 PAtpgndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtsegPGSQSGTLRKADVPVVSDATCA-AYGGF 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386781478 739 LTPGTFCVFYTEEQEDRCEMTSAPPLLcQTEGGPWVLVGMAVRGSRE-------LFAAIGPEATWISQTVGEA 804
Cdd:COG5640  190 DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPcaagypgVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 47-289 2.46e-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: 269.15  E-value: 2.46e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  47 IVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPLEGAHMRSVATI 125
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 126 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVpwVLQEVELKLLGETA 205
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 206 CQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAVAHYESW 285
Cdd:cd00190  155 CKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                 ....
gi 386781478 286 IREH 289
Cdd:cd00190  229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 46-286 9.42e-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: 256.84  E-value: 9.42e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478    46 RIVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPlEGAHMRSVAT 124
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFcGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGSHDLSSG-EEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   125 ILVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQEVELKLLGET 204
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   205 ACQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDgGRWFLAGITSFGFGCGRRNRPGVFTAVAHYES 284
Cdd:smart00020 155 TCRRAYSGGGAIT------DNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227


                   ..
gi 386781478   285 WI 286
Cdd:smart00020 228 WI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 38-290 5.68e-60

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 204.50  E-value: 5.68e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  38 CGRPEPSSRIVGGSDAHPGTWPWQVSLHHGGGHICGG---SLIAPSWVLSAAHCFVTNGtlepADEWSVLLGVHSQDGPl 114
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFcggTLIAPRWVLTAAHCVDGDG----PSDLRVVIGSTDLSTS- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 115 eGAHMRSVATILVPDNYSRVELGADLALLRLASPAklgPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQ 194
Cdd:COG5640   97 -GGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 195 EVELKLLGETACQcLYSRPGPfnltlqllPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPG 274
Cdd:COG5640  172 KADVPVVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242

                        250
                 ....*....|....*.
gi 386781478 275 VFTAVAHYESWIREHV 290
Cdd:COG5640  243 VYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
47-286 1.12e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 199.59  E-value: 1.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   47 IVGGSDAHPGTWPWQVSLHHGGGHICGG-SLIAPSWVLSAAHCFVTngtlepADEWSVLLGVHSQDGPLEGAHMRSVATI 125
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGgSLISENWVLTAAHCVSG------ASDVKVVLGAHNIVLREGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  126 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlpvPWVLQEVELKLLGETA 205
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  206 CQCLYSRPgpfnltlqLLPGMLCAGYpeGRRDTCQGDSGGPLVCEDGgrwFLAGITSFGFGCGRRNRPGVFTAVAHYESW 285
Cdd:pfam00089 152 CRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218


                  .
gi 386781478  286 I 286
Cdd:pfam00089 219 I 219
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 595-777 2.80e-24

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: 102.35  E-value: 2.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 595 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYLGLAGVSSLPQGHQVSRSVVSIrlpRHSGLRPP 673
Cdd:cd00190   12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 674 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW-----KDPQNRVPVAAAVSILTPRLCHCLYQ--GAL 739
Cdd:cd00190   86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 386781478 740 TPGTFCVFYTEEQEDRCEMTSAPPLLCQTEGGpWVLVG 777
Cdd:cd00190  166 TDNMLCAGGLEGGKDACQGDSGGPLVCNDNGR-GVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 595-777 6.54e-22

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: 95.44  E-value: 6.54e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   595 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCilrLGSSTVPYIDVYLGLAGVSSlpQGHQVSRSVVSIRlpRHSGLRPP 673
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHC---VRGSDPSNIRVRLGSHDLSS--GEEGQVIKVSKVI--IHPNYNPS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   674 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHCLYQG--A 738
Cdd:smart00020  86 tydndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtsegAGSLPDTLQEVNVPIVSNATCRRAYSGggA 165

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 386781478   739 LTPGTFCVFYTEEQEDRCEMTSAPPLLCQteGGPWVLVG 777
Cdd:smart00020 166 ITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVG 202
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 326-520 4.54e-19

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: 86.95  E-value: 4.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 326 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHDF------ETWRVLLPSRPEEKRVVRLVAHENA- 397
Cdd:cd00190    4 GSEAKIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAPSNytvrlgSHDLSSNEGGGQVIKVKKVIVHPNYn 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 398 SRNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQL-EAQL--LNSWWCHCLYGrqg 474
Cdd:cd00190   84 PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLqEVNVpiVSNAECKRAYS--- 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 386781478 475 esvPPPGDPPHLLCpAYQEEEEAGACWVNSGWSLLCREEGTWFLAG 520
Cdd:cd00190  161 ---YGGTITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 326-520 4.50e-18

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: 84.27  E-value: 4.50e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   326 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSLHDFET-----WRVLLPSRPEEKRVVRLVAHENA-S 398
Cdd:smart00020   5 GSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRvrlgsHDLSSGEEGQVIKVSKVIIHPNYnP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478   399 RNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGH-GEPAPRSSAQL-EAQL--LNSWWCHCLYGRQg 474
Cdd:smart00020  85 STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLqEVNVpiVSNATCRRAYSGG- 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 386781478   475 esvppPGDPPHLLCpAYQEEEEAGACWVNSGWSLLCrEEGTWFLAG 520
Cdd:smart00020 164 -----GAITDNMLC-AGGLEGGKDACQGDSGGPLVC-NDGRWVLVG 202
Trypsin pfam00089
Trypsin;
595-766 6.74e-17

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 80.56  E-value: 6.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  595 WPWLTEVHVTGDRV-CTGILVAPGWVLAATHCILRLGSstvpyIDVYLGlAGVSSLPQGHQVSRSVVSIRlpRHSGLRPP 673
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLG-AHNIVLREGGEQKFDVEKII--VHPNYNPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  674 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGWKDPQNRVPVA----AAVSILTPRLCHCLYQGALTPG 742
Cdd:pfam00089  84 tldndIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDtlqeVTVPVVSRETCRSAYGGTVTDT 163

                         170       180
                  ....*....|....*....|....
gi 386781478  743 TFCVFYTeeQEDRCEMTSAPPLLC 766
Cdd:pfam00089 164 MICAGAG--GKDACQGDSGGPLVC 185
Trypsin pfam00089
Trypsin;
326-528 2.35e-13

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 70.16  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  326 GKATRPGTWPWEAQVMVPGSTP-CYGALVSDSWVLAPASCFLDSlHDFETW-----RVLLPSRPEEKRVVRLVAHENA-S 398
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA-SDVKVVlgahnIVLREGGEQKFDVEKIIVHPNYnP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  399 RNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQLEAQLLnswwchcLYGR-QGESV 477
Cdd:pfam00089  83 DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVP-------VVSReTCRSA 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386781478  478 PPPGDPPHLLCpayQEEEEAGACWVNSGWSLLCREEgtwFLAGYRTLSNGC 528
Cdd:pfam00089 156 YGGTVTDTMIC---AGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGC 200
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 595-804 4.05e-12

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 67.37  E-value: 4.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 595 WPWLTEVHVTGDR---VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYlglAGVSSLPQGHQVSRSVVSIRlpRHSGLR 671
Cdd:COG5640   42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVV---IGSTDLSTSGGTVVKVARIV--VHPDYD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 672 PP-----LALLELNsrvEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHcLYQGA 738
Cdd:COG5640  114 PAtpgndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtsegPGSQSGTLRKADVPVVSDATCA-AYGGF 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386781478 739 LTPGTFCVFYTEEQEDRCEMTSAPPLLcQTEGGPWVLVGMAVRGSRE-------LFAAIGPEATWISQTVGEA 804
Cdd:COG5640  190 DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPcaagypgVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 75-272 2.29e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 57.76  E-value: 2.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  75 SLIAPSWVLSAAHCFVTNGTLEPADEWSVLLGvhSQDGPLEGAHMRSVATilVPDNYSRVELGADLALLRLASPakLGPS 154
Cdd:COG3591   17 TLIGPNLVLTAGHCVYDGAGGGWATNIVFVPG--YNGGPYGTATATRFRV--PPGWVASGDAGYDYALLRLDEP--LGDT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478 155 VKPVCLpRASHLFAHGTACWATGWGDVQESDPlpvpwvlqevelkllgETACQCLYSRPGPFNLTLQllpgmlCagypeg 234
Cdd:COG3591   91 TGWLGL-AFNDAPLAGEPVTIIGYPGDRPKDL----------------SLDCSGRVTGVQGNRLSYD------C------ 141

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 386781478 235 rrDTCQGDSGGPLVCEDGGRWFLAGITSFGfGCGRRNR 272
Cdd:COG3591  142 --DTTGGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT 176
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 595-642 1.91e-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: 44.46  E-value: 1.91e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 386781478  595 WPWLTEVHVTGDRVCTGILVAPGWVLAATHCiLRLGSSTVPYIDVYLG 642
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSC-LRDTNLRHQYISVVLG 47
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 334-438 1.40e-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: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781478  334 WPWEAQVMVPGSTPCYGALVSDSWVLAPASCFLDSLHDFETWRVLLPS-------RPEEKRVVRLVAHENASRnfaSDLA 406
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGaktlksiEGPYEQIVRVDCRHDIPE---SEIS 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 386781478  407 LLQLRTRVNLTAAPSAVCLPHREHYFLPGSRC 438
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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