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Conserved domains on  [gi|209572670|sp|Q5K4E3|]
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RecName: Full=Polyserase-2; AltName: Full=Polyserine protease 2; AltName: Full=Serine protease 36; Flags: Precursor

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 3.39e-81

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: 260.67  E-value: 3.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  47 IVGGSNAQPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFMTNgtlePAAEWSVLLGVHSQDGPLDGAHTRAVAAI 125
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 126 VVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPLPLpwVLQEVELRLLGEAT 205
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 206 CQCLYSQPGPfnltlqILPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEAW 285
Cdd:cd00190  155 CKRAYSYGGT------ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                 ....
gi 209572670 286 IREQ 289
Cdd:cd00190  229 IQKT 232
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 330-538 6.56e-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: 6.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 330 RPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFLDPNSSDspprdldaWRVLL--------PSRPRAERVARLVQH 400
Cdd:cd00190    8 KIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAPSN--------YTVRLgshdlssnEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 401 EN---ASWDNasDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGR-GEPALGPGALLEAEL--LGGWWCHC 474
Cdd:cd00190   80 PNynpSTYDN--DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRtSEGGPLPDVLQEVNVpiVSNAECKR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209572670 475 LYGRQGAavplpgDPPHALCpAYQEKEEVGSCWNDSRWSLLCQEEGTWFLAGIRDFPSGCLRPR 538
Cdd:cd00190  158 AYSYGGT------ITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPN 214
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 601-783 1.49e-22

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: 97.35  E-value: 1.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 601 WPWLAEVHVAGDR-VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGRAGASSLPQGHQVsRLVISIRlpQHLGLRPP 679
Cdd:cd00190   12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQV-IKVKKVI--VHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 680 -----LALLELSSRVEPSPSALPICLHPAG--IPPGASCWVLGW-----KEPQDRVPVAAAVSILTQRICDCLYQ--GIL 745
Cdd:cd00190   86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 209572670 746 PPGTLCVLYAEGQENRCEMTSAPPLLCQmTEGSWILVG 783
Cdd:cd00190  166 TDNMLCAGGLEGGKDACQGDSGGPLVCN-DNGRGVLVG 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 3.39e-81

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: 260.67  E-value: 3.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  47 IVGGSNAQPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFMTNgtlePAAEWSVLLGVHSQDGPLDGAHTRAVAAI 125
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 126 VVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPLPLpwVLQEVELRLLGEAT 205
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 206 CQCLYSQPGPfnltlqILPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEAW 285
Cdd:cd00190  155 CKRAYSYGGT------ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                 ....
gi 209572670 286 IREQ 289
Cdd:cd00190  229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 46-286 5.44e-77

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 249.52  E-value: 5.44e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670    46 RIVGGSNAQPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFMTNgtlePAAEWSVLLGVHSQDGPlDGAHTRAVAA 124
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFcGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGSHDLSSG-EEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   125 IVVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPlPLPWVLQEVELRLLGEA 204
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   205 TCQCLYSQPGPfnltlqILPGMLCAGYPEGRRDTCQGDSGGPLVCeEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEA 284
Cdd:smart00020 155 TCRRAYSGGGA------ITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227


                   ..
gi 209572670   285 WI 286
Cdd:smart00020 228 WI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 38-290 2.62e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 202.96  E-value: 2.62e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  38 CGRPEPSARIVGGSNAQPGTWPWQVSLHHGGGHICGG---SLIAPSWVLSAAHCFMTNGtlepAAEWSVLLGVHSQDGpl 114
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFcggTLIAPRWVLTAAHCVDGDG----PSDLRVVIGSTDLST-- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 115 DGAHTRAVAAIVVPANYSQVELGADLALLRLASPASLGPavwPVCLPRASHRFVHGTACWATGWGDVQEADPlPLPWVLQ 194
Cdd:COG5640   96 SGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 195 EVELRLLGEATCQcLYSQPGPfnltlqilPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPG 274
Cdd:COG5640  172 KADVPVVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242

                        250
                 ....*....|....*.
gi 209572670 275 VFTAVATYEAWIREQV 290
Cdd:COG5640  243 VYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
47-286 6.18e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 197.28  E-value: 6.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   47 IVGGSNAQPGTWPWQVSLHHGGGHICGG-SLIAPSWVLSAAHCFmtngtlEPAAEWSVLLGVHSQDGPLDGAHTRAVAAI 125
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGgSLISENWVLTAAHCV------SGASDVKVVLGAHNIVLREGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  126 VVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPlplPWVLQEVELRLLGEAT 205
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  206 CQCLYSQPgpfnltlqILPGMLCAGYpeGRRDTCQGDSGGPLVCEEGgrwFQAGITSFGFGCGRRNRPGVFTAVATYEAW 285
Cdd:pfam00089 152 CRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218


                  .
gi 209572670  286 I 286
Cdd:pfam00089 219 I 219
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 330-538 6.56e-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: 6.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 330 RPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFLDPNSSDspprdldaWRVLL--------PSRPRAERVARLVQH 400
Cdd:cd00190    8 KIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAPSN--------YTVRLgshdlssnEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 401 EN---ASWDNasDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGR-GEPALGPGALLEAEL--LGGWWCHC 474
Cdd:cd00190   80 PNynpSTYDN--DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRtSEGGPLPDVLQEVNVpiVSNAECKR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209572670 475 LYGRQGAavplpgDPPHALCpAYQEKEEVGSCWNDSRWSLLCQEEGTWFLAGIRDFPSGCLRPR 538
Cdd:cd00190  158 AYSYGGT------ITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPN 214
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 601-783 1.49e-22

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: 97.35  E-value: 1.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 601 WPWLAEVHVAGDR-VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGRAGASSLPQGHQVsRLVISIRlpQHLGLRPP 679
Cdd:cd00190   12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQV-IKVKKVI--VHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 680 -----LALLELSSRVEPSPSALPICLHPAG--IPPGASCWVLGW-----KEPQDRVPVAAAVSILTQRICDCLYQ--GIL 745
Cdd:cd00190   86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 209572670 746 PPGTLCVLYAEGQENRCEMTSAPPLLCQmTEGSWILVG 783
Cdd:cd00190  166 TDNMLCAGGLEGGKDACQGDSGGPLVCN-DNGRGVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 330-538 6.65e-21

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 92.36  E-value: 6.65e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   330 RPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFLDPNSSDSPPRdLDAWRVLLPSRPRAERVARLVQHEN---ASW 405
Cdd:smart00020   9 NIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRVR-LGSHDLSSGEEGQVIKVSKVIIHPNynpSTY 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   406 DNasDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGRGEPALGPGA--LLEAEL--LGGWWCHCLYGRQGA 481
Cdd:smart00020  88 DN--DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVpiVSNATCRRAYSGGGA 165

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 209572670   482 avplpgDPPHALCpAYQEKEEVGSCWNDSRWSLLCQeEGTWFLAGIRDFPSGCLRPR 538
Cdd:smart00020 166 ------ITDNMLC-AGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPG 214
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 601-783 1.68e-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: 1.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   601 WPWLAEVHVAGDR-VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGRAGASSlPQGHQVSRLVISIRLPQHLGLRPP 679
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGSDPSN---IRVRLGSHDLSS-GEEGQVIKVSKVIIHPNYNPSTYD 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   680 --LALLELSSRVEPSPSALPICLHPAG--IPPGASCWVLGW------KEPQDRVPVAAAVSILTQRICDCLYQG--ILPP 747
Cdd:smart00020  89 ndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtsegAGSLPDTLQEVNVPIVSNATCRRAYSGggAITD 168

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 209572670   748 GTLCVLYAEGQENRCEMTSAPPLLCQmtEGSWILVG 783
Cdd:smart00020 169 NMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVG 202
Trypsin pfam00089
Trypsin;
326-466 3.00e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 78.64  E-value: 3.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  326 GKAPRPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFldPNSSDSPPRDLDAWRVLLPSRPRAERVARLVQHENAS 404
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCV--SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209572670  405 WDNA-SDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGRGEPALGPGALLEAEL 466
Cdd:pfam00089  82 PDTLdNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTV 144
Trypsin pfam00089
Trypsin;
601-772 3.14e-15

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 75.56  E-value: 3.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  601 WPWLAEVHVAGDRV-CTGILLAPGWVLAATHCVLRPGSttvpyIEVYLGrAGASSLPQGHQVSRLVISIRLpqHLGLRPP 679
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLG-AHNIVLREGGEQKFDVEKIIV--HPNYNPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  680 -----LALLELSSRVEPSPSALPICL--HPAGIPPGASCWVLGW-KEPQDRVPVA---AAVSILTQRICDCLYQGILPPG 748
Cdd:pfam00089  84 tldndIALLKLESPVTLGDTVRPICLpdASSDLPVGTTCTVSGWgNTKTLGPSDTlqeVTVPVVSRETCRSAYGGTVTDT 163

                         170       180
                  ....*....|....*....|....
gi 209572670  749 TLCVLYaeGQENRCEMTSAPPLLC 772
Cdd:pfam00089 164 MICAGA--GGKDACQGDSGGPLVC 185
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 601-810 5.87e-12

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 66.98  E-value: 5.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 601 WPWLAEVHVAGDR---VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGRA-GASSLPQGHQVSRLVISirlPQHLGL 676
Cdd:COG5640   42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGSTdLSTSGGTVVKVARIVVH---PDYDPA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 677 RPP--LALLELSsrvEPSPSALPICLHPAG--IPPGASCWVLGW---KEPQDRVPVA---AAVSILTQRICDcLYQGILP 746
Cdd:COG5640  116 TPGndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtSEGPGSQSGTlrkADVPVVSDATCA-AYGGFDG 191

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209572670 747 PGTLCVLYAEGQENRCEMTSAPPLLcQMTEGSWILVGMA-------VQGSRELFAAIGPEEAWISQTVGEA 810
Cdd:COG5640  192 GTMLCAGYPEGGKDACQGDSGGPLV-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 3.39e-81

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: 260.67  E-value: 3.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  47 IVGGSNAQPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFMTNgtlePAAEWSVLLGVHSQDGPLDGAHTRAVAAI 125
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 126 VVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPLPLpwVLQEVELRLLGEAT 205
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 206 CQCLYSQPGPfnltlqILPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEAW 285
Cdd:cd00190  155 CKRAYSYGGT------ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228


                 ....
gi 209572670 286 IREQ 289
Cdd:cd00190  229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 46-286 5.44e-77

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 249.52  E-value: 5.44e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670    46 RIVGGSNAQPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFMTNgtlePAAEWSVLLGVHSQDGPlDGAHTRAVAA 124
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFcGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGSHDLSSG-EEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   125 IVVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPlPLPWVLQEVELRLLGEA 204
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   205 TCQCLYSQPGPfnltlqILPGMLCAGYPEGRRDTCQGDSGGPLVCeEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEA 284
Cdd:smart00020 155 TCRRAYSGGGA------ITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227


                   ..
gi 209572670   285 WI 286
Cdd:smart00020 228 WI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 38-290 2.62e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 202.96  E-value: 2.62e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  38 CGRPEPSARIVGGSNAQPGTWPWQVSLHHGGGHICGG---SLIAPSWVLSAAHCFMTNGtlepAAEWSVLLGVHSQDGpl 114
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFcggTLIAPRWVLTAAHCVDGDG----PSDLRVVIGSTDLST-- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 115 DGAHTRAVAAIVVPANYSQVELGADLALLRLASPASLGPavwPVCLPRASHRFVHGTACWATGWGDVQEADPlPLPWVLQ 194
Cdd:COG5640   96 SGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 195 EVELRLLGEATCQcLYSQPGPfnltlqilPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPG 274
Cdd:COG5640  172 KADVPVVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242

                        250
                 ....*....|....*.
gi 209572670 275 VFTAVATYEAWIREQV 290
Cdd:COG5640  243 VYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
47-286 6.18e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 197.28  E-value: 6.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   47 IVGGSNAQPGTWPWQVSLHHGGGHICGG-SLIAPSWVLSAAHCFmtngtlEPAAEWSVLLGVHSQDGPLDGAHTRAVAAI 125
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGgSLISENWVLTAAHCV------SGASDVKVVLGAHNIVLREGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  126 VVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPlplPWVLQEVELRLLGEAT 205
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  206 CQCLYSQPgpfnltlqILPGMLCAGYpeGRRDTCQGDSGGPLVCEEGgrwFQAGITSFGFGCGRRNRPGVFTAVATYEAW 285
Cdd:pfam00089 152 CRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218


                  .
gi 209572670  286 I 286
Cdd:pfam00089 219 I 219
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 330-538 6.56e-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: 6.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 330 RPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFLDPNSSDspprdldaWRVLL--------PSRPRAERVARLVQH 400
Cdd:cd00190    8 KIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAPSN--------YTVRLgshdlssnEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 401 EN---ASWDNasDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGR-GEPALGPGALLEAEL--LGGWWCHC 474
Cdd:cd00190   80 PNynpSTYDN--DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRtSEGGPLPDVLQEVNVpiVSNAECKR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209572670 475 LYGRQGAavplpgDPPHALCpAYQEKEEVGSCWNDSRWSLLCQEEGTWFLAGIRDFPSGCLRPR 538
Cdd:cd00190  158 AYSYGGT------ITDNMLC-AGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPN 214
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 601-783 1.49e-22

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: 97.35  E-value: 1.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 601 WPWLAEVHVAGDR-VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGRAGASSLPQGHQVsRLVISIRlpQHLGLRPP 679
Cdd:cd00190   12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQV-IKVKKVI--VHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 680 -----LALLELSSRVEPSPSALPICLHPAG--IPPGASCWVLGW-----KEPQDRVPVAAAVSILTQRICDCLYQ--GIL 745
Cdd:cd00190   86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 209572670 746 PPGTLCVLYAEGQENRCEMTSAPPLLCQmTEGSWILVG 783
Cdd:cd00190  166 TDNMLCAGGLEGGKDACQGDSGGPLVCN-DNGRGVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 330-538 6.65e-21

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 92.36  E-value: 6.65e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   330 RPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFLDPNSSDSPPRdLDAWRVLLPSRPRAERVARLVQHEN---ASW 405
Cdd:smart00020   9 NIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRVR-LGSHDLSSGEEGQVIKVSKVIIHPNynpSTY 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   406 DNasDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGRGEPALGPGA--LLEAEL--LGGWWCHCLYGRQGA 481
Cdd:smart00020  88 DN--DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVpiVSNATCRRAYSGGGA 165

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 209572670   482 avplpgDPPHALCpAYQEKEEVGSCWNDSRWSLLCQeEGTWFLAGIRDFPSGCLRPR 538
Cdd:smart00020 166 ------ITDNMLC-AGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPG 214
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 601-783 1.68e-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: 1.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   601 WPWLAEVHVAGDR-VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGRAGASSlPQGHQVSRLVISIRLPQHLGLRPP 679
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGSDPSN---IRVRLGSHDLSS-GEEGQVIKVSKVIIHPNYNPSTYD 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670   680 --LALLELSSRVEPSPSALPICLHPAG--IPPGASCWVLGW------KEPQDRVPVAAAVSILTQRICDCLYQG--ILPP 747
Cdd:smart00020  89 ndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtsegAGSLPDTLQEVNVPIVSNATCRRAYSGggAITD 168

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 209572670   748 GTLCVLYAEGQENRCEMTSAPPLLCQmtEGSWILVG 783
Cdd:smart00020 169 NMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVG 202
Trypsin pfam00089
Trypsin;
326-466 3.00e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 78.64  E-value: 3.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  326 GKAPRPGAWPWEAQVMVPGSRP-CHGALVSESWVLAPASCFldPNSSDSPPRDLDAWRVLLPSRPRAERVARLVQHENAS 404
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCV--SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209572670  405 WDNA-SDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGRGEPALGPGALLEAEL 466
Cdd:pfam00089  82 PDTLdNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTV 144
Trypsin pfam00089
Trypsin;
601-772 3.14e-15

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 75.56  E-value: 3.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  601 WPWLAEVHVAGDRV-CTGILLAPGWVLAATHCVLRPGSttvpyIEVYLGrAGASSLPQGHQVSRLVISIRLpqHLGLRPP 679
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLG-AHNIVLREGGEQKFDVEKIIV--HPNYNPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  680 -----LALLELSSRVEPSPSALPICL--HPAGIPPGASCWVLGW-KEPQDRVPVA---AAVSILTQRICDCLYQGILPPG 748
Cdd:pfam00089  84 tldndIALLKLESPVTLGDTVRPICLpdASSDLPVGTTCTVSGWgNTKTLGPSDTlqeVTVPVVSRETCRSAYGGTVTDT 163

                         170       180
                  ....*....|....*....|....
gi 209572670  749 TLCVLYaeGQENRCEMTSAPPLLC 772
Cdd:pfam00089 164 MICAGA--GGKDACQGDSGGPLVC 185
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 601-810 5.87e-12

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 66.98  E-value: 5.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 601 WPWLAEVHVAGDR---VCTGILLAPGWVLAATHCVLRPGSTTvpyIEVYLGRA-GASSLPQGHQVSRLVISirlPQHLGL 676
Cdd:COG5640   42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGSTdLSTSGGTVVKVARIVVH---PDYDPA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 677 RPP--LALLELSsrvEPSPSALPICLHPAG--IPPGASCWVLGW---KEPQDRVPVA---AAVSILTQRICDcLYQGILP 746
Cdd:COG5640  116 TPGndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtSEGPGSQSGTlrkADVPVVSDATCA-AYGGFDG 191

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209572670 747 PGTLCVLYAEGQENRCEMTSAPPLLcQMTEGSWILVGMA-------VQGSRELFAAIGPEEAWISQTVGEA 810
Cdd:COG5640  192 GTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVswgggpcAAGYPGVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 75-272 3.88e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 57.38  E-value: 3.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  75 SLIAPSWVLSAAHCFMTNGTLEPAAEWSVLLGvhSQDGPldGAHTRAVAAIVVPANYSQVELGADLALLRLASPasLGPA 154
Cdd:COG3591   17 TLIGPNLVLTAGHCVYDGAGGGWATNIVFVPG--YNGGP--YGTATATRFRVPPGWVASGDAGYDYALLRLDEP--LGDT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 155 VWPVCLpRASHRFVHGTACWATGWgdvqeadPLPLPWVLQevelrllgeATCQCLYSQPGPFNLTLQIlpgmlcagypeg 234
Cdd:COG3591   91 TGWLGL-AFNDAPLAGEPVTIIGY-------PGDRPKDLS---------LDCSGRVTGVQGNRLSYDC------------ 141

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 209572670 235 rrDTCQGDSGGPLVCEEGGRWFQAGITSFGfGCGRRNR 272
Cdd:COG3591  142 --DTTGGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT 176
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 334-444 5.68e-05

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


Pssm-ID: 286432  Cd Length: 116  Bit Score: 43.31  E-value: 5.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670  334 WPWEAQVMVPGSRPCHGALVSESWVLAPASCFLDPNSSDS-PPRDLDAWRVLLPSRPRAERVARLVQHENASwdnASDLA 412
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQyISVVLGGAKTLKSIEGPYEQIVRVDCRHDIP---ESEIS 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 209572670  413 LLQLRTPVNLSAASRPVCLPHPEHYFLPGSRC 444
Cdd:pfam09342  78 LLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 601-650 6.32e-05

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


Pssm-ID: 286432  Cd Length: 116  Bit Score: 43.31  E-value: 6.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 209572670  601 WPWLAEVHVAGDRVCTGILLAPGWVLAATHCvLRPGSTTVPYIEVYLGRA 650
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSC-LRDTNLRHQYISVVLGGA 49
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 610-722 2.85e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 42.74  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209572670 610 AGDRVCTGILLAPGWVLAATHCVLRPGSTTVPY-IEVYLGRAGASslPQGHQVSRLVISIRLPQHLGLRPPLALLELSSR 688
Cdd:COG3591    9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATnIVFVPGYNGGP--YGTATATRFRVPPGWVASGDAGYDYALLRLDEP 86

                         90       100       110
                 ....*....|....*....|....*....|....
gi 209572670 689 VEPSPSALPIcLHPAGIPPGASCWVLGWkePQDR 722
Cdd:COG3591   87 LGDTTGWLGL-AFNDAPLAGEPVTIIGY--PGDR 117
 
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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