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Conserved domains on  [gi|1958648462|ref|XP_038942656|]
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polyserase-2 isoform X4 [Rattus norvegicus]

Protein Classification

Tryp_SPc domain-containing protein( domain architecture ID 10076278)

Tryp_SPc domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
59-271 1.08e-58

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: 196.34  E-value: 1.08e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  59 IVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPLEGAHMRSVATI 137
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 138 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVpwVLQEVELKLLGETA 217
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958648462 218 CQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQKDSGWSLLCREEGTWFLAG 271
Cdd:cd00190   155 CKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVG 202
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
346-541 6.50e-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: 97.73  E-value: 6.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 346 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYLGLAGVSSLPQGHQVSRSVVSIrlpRHSGLRPP 424
Cdd:cd00190    12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 425 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW-----KDPQNRVPVAAAVSILTPRLCHCLYQ--GAL 490
Cdd:cd00190    86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648462 491 TPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQTEGGpWVLVG 541
Cdd:cd00190   166 TDNMLCAGGLEGGKDAC--QG--DSG-G--------PLVCNDNGR-GVLVG 202
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
59-271 1.08e-58

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: 196.34  E-value: 1.08e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  59 IVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPLEGAHMRSVATI 137
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 138 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVpwVLQEVELKLLGETA 217
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958648462 218 CQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQKDSGWSLLCREEGTWFLAG 271
Cdd:cd00190   155 CKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
58-271 5.87e-55

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: 186.34  E-value: 5.87e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462   58 RIVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPlEGAHMRSVAT 136
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFcGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGSHDLSSG-EEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  137 ILVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQEVELKLLGET 216
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958648462  217 ACQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQKDSGWSLLCrEEGTWFLAG 271
Cdd:smart00020 155 TCRRAYSGGGAIT------DNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVG 202
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
50-271 2.68e-40

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 147.87  E-value: 2.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  50 CGRPEPSSRIVGGSDAHPGTWPWQVSLHHGGGHICGG---SLIAPSWVLSAAHCFVTNGtlepADEWSVLLGVHSQDGPl 126
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFcggTLIAPRWVLTAAHCVDGDG----PSDLRVVIGSTDLSTS- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 127 eGAHMRSVATILVPDNYSRVELGADLALLRLASPAklgPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQ 206
Cdd:COG5640    97 -GGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLR 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958648462 207 EVELKLLGETACQcLYSRPGPfnltlqllPGMLCAGYPEGRRDTCQKDSGWSLLCREEGTWFLAG 271
Cdd:COG5640   172 KADVPVVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVG 227
Trypsin pfam00089
Trypsin;
59-279 1.36e-38

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 141.81  E-value: 1.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  59 IVGGSDAHPGTWPWQVSLHHGGGHICGG-SLIAPSWVLSAAHCFVTngtlepADEWSVLLGVHSQDGPLEGAHMRSVATI 137
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGgSLISENWVLTAAHCVSG------ASDVKVVLGAHNIVLREGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 138 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlpvPWVLQEVELKLLGETA 217
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958648462 218 CQCLYSRPgpfnltlqLLPGMLCAGYpeGRRDTCQKDSGWSLLCREEgtwFLAGYRTLSNGC 279
Cdd:pfam00089 152 CRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGC 200
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
346-541 6.50e-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: 97.73  E-value: 6.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 346 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYLGLAGVSSLPQGHQVSRSVVSIrlpRHSGLRPP 424
Cdd:cd00190    12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 425 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW-----KDPQNRVPVAAAVSILTPRLCHCLYQ--GAL 490
Cdd:cd00190    86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648462 491 TPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQTEGGpWVLVG 541
Cdd:cd00190   166 TDNMLCAGGLEGGKDAC--QG--DSG-G--------PLVCNDNGR-GVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
346-541 1.52e-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: 90.81  E-value: 1.52e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  346 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCilrLGSSTVPYIDVYLGLAGVSSlpQGHQVSRSVVSIRlpRHSGLRPP 424
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHC---VRGSDPSNIRVRLGSHDLSS--GEEGQVIKVSKVI--IHPNYNPS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  425 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHCLYQG--A 489
Cdd:smart00020  86 tydndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtsegAGSLPDTLQEVNVPIVSNATCRRAYSGggA 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958648462  490 LTPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQteGGPWVLVG 541
Cdd:smart00020 166 ITDNMLCAGGLEGGKDAC--QG--DSG-G--------PLVCN--DGRWVLVG 202
Trypsin pfam00089
Trypsin;
346-507 4.88e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 77.48  E-value: 4.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 346 WPWLTEVHVTGDRV-CTGILVAPGWVLAATHCILRLGSstvpyIDVYLGlAGVSSLPQGHQVSRSVVSIRlpRHSGLRPP 424
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLG-AHNIVLREGGEQKFDVEKII--VHPNYNPD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 425 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGWKDPQNRVPVA----AAVSILTPRLCHCLYQGALTPG 493
Cdd:pfam00089  84 tldndIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDtlqeVTVPVVSRETCRSAYGGTVTDT 163
                         170
                  ....*....|....
gi 1958648462 494 TFCVFYTeeQEDRC 507
Cdd:pfam00089 164 MICAGAG--GKDAC 175
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
346-568 2.32e-11

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 64.67  E-value: 2.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 346 WPWLTEVHVTGDR---VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYlglAGVSSLPQGHQVSRSVVSIRlpRHSGLR 422
Cdd:COG5640    42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVV---IGSTDLSTSGGTVVKVARIV--VHPDYD 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 423 PP-----LALLELNsrvEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHcLYQGA 489
Cdd:COG5640   114 PAtpgndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtsegPGSQSGTLRKADVPVVSDATCA-AYGGF 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 490 LTPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLcQTEGGPWVLVGMAVRGSRE-------LFAAIGPEATWIS 562
Cdd:COG5640   190 DGGTMLCAGYPEGGKDAC--QG--DSG-G--------PLV-VKDGGGWVLVGVVSWGGGPcaagypgVYTRVSAYRDWIK 255

                  ....*.
gi 1958648462 563 QTVGEA 568
Cdd:COG5640   256 STAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
59-271 1.08e-58

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: 196.34  E-value: 1.08e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  59 IVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPLEGAHMRSVATI 137
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFcGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQVIKVKKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 138 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVpwVLQEVELKLLGETA 217
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958648462 218 CQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQKDSGWSLLCREEGTWFLAG 271
Cdd:cd00190   155 CKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
58-271 5.87e-55

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: 186.34  E-value: 5.87e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462   58 RIVGGSDAHPGTWPWQVSLHHGGGHIC-GGSLIAPSWVLSAAHCFVTNgtlePADEWSVLLGVHSQDGPlEGAHMRSVAT 136
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFcGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGSHDLSSG-EEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  137 ILVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQEVELKLLGET 216
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958648462  217 ACQCLYSRPGPFNltlqllPGMLCAGYPEGRRDTCQKDSGWSLLCrEEGTWFLAG 271
Cdd:smart00020 155 TCRRAYSGGGAIT------DNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVG 202
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
50-271 2.68e-40

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 147.87  E-value: 2.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  50 CGRPEPSSRIVGGSDAHPGTWPWQVSLHHGGGHICGG---SLIAPSWVLSAAHCFVTNGtlepADEWSVLLGVHSQDGPl 126
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFcggTLIAPRWVLTAAHCVDGDG----PSDLRVVIGSTDLSTS- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 127 eGAHMRSVATILVPDNYSRVELGADLALLRLASPAklgPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlPVPWVLQ 206
Cdd:COG5640    97 -GGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLR 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958648462 207 EVELKLLGETACQcLYSRPGPfnltlqllPGMLCAGYPEGRRDTCQKDSGWSLLCREEGTWFLAG 271
Cdd:COG5640   172 KADVPVVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVG 227
Trypsin pfam00089
Trypsin;
59-279 1.36e-38

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 141.81  E-value: 1.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  59 IVGGSDAHPGTWPWQVSLHHGGGHICGG-SLIAPSWVLSAAHCFVTngtlepADEWSVLLGVHSQDGPLEGAHMRSVATI 137
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGgSLISENWVLTAAHCVSG------ASDVKVVLGAHNIVLREGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 138 LVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPlpvPWVLQEVELKLLGETA 217
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958648462 218 CQCLYSRPgpfnltlqLLPGMLCAGYpeGRRDTCQKDSGWSLLCREEgtwFLAGYRTLSNGC 279
Cdd:pfam00089 152 CRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGC 200
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
346-541 6.50e-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: 97.73  E-value: 6.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 346 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYLGLAGVSSLPQGHQVSRSVVSIrlpRHSGLRPP 424
Cdd:cd00190    12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 425 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW-----KDPQNRVPVAAAVSILTPRLCHCLYQ--GAL 490
Cdd:cd00190    86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYSygGTI 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958648462 491 TPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQTEGGpWVLVG 541
Cdd:cd00190   166 TDNMLCAGGLEGGKDAC--QG--DSG-G--------PLVCNDNGR-GVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
346-541 1.52e-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: 90.81  E-value: 1.52e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  346 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCilrLGSSTVPYIDVYLGLAGVSSlpQGHQVSRSVVSIRlpRHSGLRPP 424
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHC---VRGSDPSNIRVRLGSHDLSS--GEEGQVIKVSKVI--IHPNYNPS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  425 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHCLYQG--A 489
Cdd:smart00020  86 tydndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtsegAGSLPDTLQEVNVPIVSNATCRRAYSGggA 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958648462  490 LTPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLCQteGGPWVLVG 541
Cdd:smart00020 166 ITDNMLCAGGLEGGKDAC--QG--DSG-G--------PLVCN--DGRWVLVG 202
Trypsin pfam00089
Trypsin;
346-507 4.88e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 77.48  E-value: 4.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 346 WPWLTEVHVTGDRV-CTGILVAPGWVLAATHCILRLGSstvpyIDVYLGlAGVSSLPQGHQVSRSVVSIRlpRHSGLRPP 424
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLG-AHNIVLREGGEQKFDVEKII--VHPNYNPD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 425 -----LALLELNSRVEPSPSALPICLHPEG--VPPGASCWVLGWKDPQNRVPVA----AAVSILTPRLCHCLYQGALTPG 493
Cdd:pfam00089  84 tldndIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDtlqeVTVPVVSRETCRSAYGGTVTDT 163
                         170
                  ....*....|....
gi 1958648462 494 TFCVFYTeeQEDRC 507
Cdd:pfam00089 164 MICAGAG--GKDAC 175
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
346-568 2.32e-11

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 64.67  E-value: 2.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 346 WPWLTEVHVTGDR---VCTGILVAPGWVLAATHCILRLGSSTvpyIDVYlglAGVSSLPQGHQVSRSVVSIRlpRHSGLR 422
Cdd:COG5640    42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVV---IGSTDLSTSGGTVVKVARIV--VHPDYD 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 423 PP-----LALLELNsrvEPSPSALPICLHPEG--VPPGASCWVLGW------KDPQNRVPVAAAVSILTPRLCHcLYQGA 489
Cdd:COG5640   114 PAtpgndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtsegPGSQSGTLRKADVPVVSDATCA-AYGGF 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462 490 LTPGTFCVFYTEEQEDRCevQGprDLGpGrrkmtsapPLLcQTEGGPWVLVGMAVRGSRE-------LFAAIGPEATWIS 562
Cdd:COG5640   190 DGGTMLCAGYPEGGKDAC--QG--DSG-G--------PLV-VKDGGGWVLVGVVSWGGGPcaagypgVYTRVSAYRDWIK 255

                  ....*.
gi 1958648462 563 QTVGEA 568
Cdd:COG5640   256 STAGGL 261
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
346-393 1.39e-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: 1.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958648462 346 WPWLTEVHVTGDRVCTGILVAPGWVLAATHCiLRLGSSTVPYIDVYLG 393
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSC-LRDTNLRHQYISVVLG 47
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
87-170 1.90e-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: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648462  87 SLIAPSWVLSAAHCFVTNGTLEPADEWSVLLGvhSQDGPLEGAHMRSVATilVPDNYSRVELGADLALLRLASPakLGPS 166
Cdd:COG3591    17 TLIGPNLVLTAGHCVYDGAGGGWATNIVFVPG--YNGGPYGTATATRFRV--PPGWVASGDAGYDYALLRLDEP--LGDT 90

                  ....
gi 1958648462 167 VKPV 170
Cdd:COG3591    91 TGWL 94
 
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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