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Conserved domains on  [gi|1039780316|ref|XP_017167876|]
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polyserase-2 isoform X5 [Mus musculus]

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 ...
 1-171 5.44e-62

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: 205.97  E-value: 5.44e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316   1 MRSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPLPLpwVLQEVEL 80
Cdd:cd00190    70 VIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNV 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316  81 RLLGEAACQCLYSRPGPFNltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTA 160
Cdd:cd00190   148 PIVSNAECKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTR 221

                         170
                  ....*....|.
gi 1039780316 161 VAPYESWIREH 171
Cdd:cd00190   222 VSSYLDWIQKT 232
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 396-578 6.57e-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: 95.04  E-value: 6.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 396 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSTTvpyIEVYLGRAGVSSLPQGHQVSRSVVSIrlpRHLGLRPP 474
Cdd:cd00190    12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 475 -----LALLELNSRVEPSPSALPICLHPGG--IPSGASCWVLGW-----KNPQDRVPVVAAVSILTPRLCHCLY--PGIL 540
Cdd:cd00190    86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYsyGGTI 165

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039780316 541 TPGTFCVLYSEGQEDRCEVTSAPPLLCQTeEGPWVLVG 578
Cdd:cd00190   166 TDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVG 202
Trypsin super family cl47494
Trypsin;
208-251 4.43e-03

Trypsin;


The actual alignment was detected with superfamily member pfam00089:

Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 38.96  E-value: 4.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1039780316 208 GKAPRPGTWPWEAQVTVPGSTP-CYGALVSDRWVLAPASCFLETR 251
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGAS 48
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 1-171 5.44e-62

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: 205.97  E-value: 5.44e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316   1 MRSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPLPLpwVLQEVEL 80
Cdd:cd00190    70 VIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNV 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316  81 RLLGEAACQCLYSRPGPFNltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTA 160
Cdd:cd00190   148 PIVSNAECKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTR 221

                         170
                  ....*....|.
gi 1039780316 161 VAPYESWIREH 171
Cdd:cd00190   222 VSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 1-168 1.23e-57

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: 194.05  E-value: 1.23e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316    1 MRSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPlPLPWVLQEVEL 80
Cdd:smart00020  70 VIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNV 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316   81 RLLGEAACQCLYSRPGPFNltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDgGRWFLAGITSFGFGCGRRNRPGVFTA 160
Cdd:smart00020 149 PIVSNATCRRAYSGGGAIT------DNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTR 221


                   ....*...
gi 1039780316  161 VAPYESWI 168
Cdd:smart00020 222 VSSYLDWI 229
Trypsin pfam00089
Trypsin;
2-168 2.51e-42

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 152.21  E-value: 2.51e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316   2 RSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPlplPWVLQEVELR 81
Cdd:pfam00089  69 FDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVP 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316  82 LLGEAACQCLYSRPgpfnltfqLLPGMLCAGYpaGRRDTCQGDSGGPLVCEDGgrwFLAGITSFGFGCGRRNRPGVFTAV 161
Cdd:pfam00089 146 VVSRETCRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPV 212


                  ....*..
gi 1039780316 162 APYESWI 168
Cdd:pfam00089 213 SSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 2-172 4.90e-38

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 141.71  E-value: 4.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316   2 RSVATILIPDNYSTVELGADLALLRLASPAklgPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPlPLPWVLQEVELR 81
Cdd:COG5640   101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVP 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316  82 LLGEAACQcLYSRPGPfnltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAV 161
Cdd:COG5640   177 VVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRV 247

                         170
                  ....*....|.
gi 1039780316 162 APYESWIREHV 172
Cdd:COG5640   248 SAYRDWIKSTA 258
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 396-578 6.57e-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: 95.04  E-value: 6.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 396 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSTTvpyIEVYLGRAGVSSLPQGHQVSRSVVSIrlpRHLGLRPP 474
Cdd:cd00190    12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 475 -----LALLELNSRVEPSPSALPICLHPGG--IPSGASCWVLGW-----KNPQDRVPVVAAVSILTPRLCHCLY--PGIL 540
Cdd:cd00190    86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYsyGGTI 165

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039780316 541 TPGTFCVLYSEGQEDRCEVTSAPPLLCQTeEGPWVLVG 578
Cdd:cd00190   166 TDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 396-578 4.69e-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: 89.27  E-value: 4.69e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316  396 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCilrLGSTTVPYIEVYLGRAGVSSlpQGHQVSRSVVSIRlpRHLGLRPP 474
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHC---VRGSDPSNIRVRLGSHDLSS--GEEGQVIKVSKVI--IHPNYNPS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316  475 -----LALLELNSRVEPSPSALPICLHPGG--IPSGASCWVLGW---KNPQDRVPVV---AAVSILTPRLCHCLYPG--I 539
Cdd:smart00020  86 tydndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtSEGAGSLPDTlqeVNVPIVSNATCRRAYSGggA 165

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039780316  540 LTPGTFCVLYSEGQEDRCEVTSAPPLLCQTEEgpWVLVG 578
Cdd:smart00020 166 ITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR--WVLVG 202
Trypsin pfam00089
Trypsin;
396-567 1.80e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 78.64  E-value: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 396 WPWLTEVHVTGDRV-CTGILVAPGWVLAATHCILRLGSttvpyIEVYLGRAGVSSlPQGHQVSRSVVSIRlpRHLGLRPP 474
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLGAHNIVL-REGGEQKFDVEKII--VHPNYNPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 475 -----LALLELNSRVEPSPSALPICL-HPGGIPS-GASCWVLGWKNP-QDRVPVV---AAVSILTPRLCHCLYPGILTPG 543
Cdd:pfam00089  84 tldndIALLKLESPVTLGDTVRPICLpDASSDLPvGTTCTVSGWGNTkTLGPSDTlqeVTVPVVSRETCRSAYGGTVTDT 163

                         170       180
                  ....*....|....*....|....
gi 1039780316 544 TFCVLYseGQEDRCEVTSAPPLLC 567
Cdd:pfam00089 164 MICAGA--GGKDACQGDSGGPLVC 185
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 396-605 4.16e-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: 4.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 396 WPWLTEVHVTGDR---VCTGILVAPGWVLAATHCILRLGSTTvpyIEVYLGRAGVSSlpQGHQVsRSVVSIRlpRHLGLR 472
Cdd:COG5640    42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGSTDLST--SGGTV-VKVARIV--VHPDYD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 473 PP-----LALLELNsrvEPSPSALPICLHPGG--IPSGASCWVLGW---KNPQDRVPVV---AAVSILTPRLCHcLYPGI 539
Cdd:COG5640   114 PAtpgndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtSEGPGSQSGTlrkADVPVVSDATCA-AYGGF 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039780316 540 LTPGTFCVLYSEGQEDRCEVTSAPPLLcQTEEGPWVLVGMAVRGNRE-------LFAAIGPEATWISQTVGEA 605
Cdd:COG5640   190 DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPcaagypgVYTRVSAYRDWIKSTAGGL 261
Trypsin pfam00089
Trypsin;
208-251 4.43e-03

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 38.96  E-value: 4.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1039780316 208 GKAPRPGTWPWEAQVTVPGSTP-CYGALVSDRWVLAPASCFLETR 251
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGAS 48
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 1-171 5.44e-62

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: 205.97  E-value: 5.44e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316   1 MRSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPLPLpwVLQEVEL 80
Cdd:cd00190    70 VIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNV 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316  81 RLLGEAACQCLYSRPGPFNltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTA 160
Cdd:cd00190   148 PIVSNAECKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTR 221

                         170
                  ....*....|.
gi 1039780316 161 VAPYESWIREH 171
Cdd:cd00190   222 VSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 1-168 1.23e-57

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: 194.05  E-value: 1.23e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316    1 MRSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPlPLPWVLQEVEL 80
Cdd:smart00020  70 VIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNV 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316   81 RLLGEAACQCLYSRPGPFNltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDgGRWFLAGITSFGFGCGRRNRPGVFTA 160
Cdd:smart00020 149 PIVSNATCRRAYSGGGAIT------DNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTR 221


                   ....*...
gi 1039780316  161 VAPYESWI 168
Cdd:smart00020 222 VSSYLDWI 229
Trypsin pfam00089
Trypsin;
2-168 2.51e-42

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 152.21  E-value: 2.51e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316   2 RSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPlplPWVLQEVELR 81
Cdd:pfam00089  69 FDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVP 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316  82 LLGEAACQCLYSRPgpfnltfqLLPGMLCAGYpaGRRDTCQGDSGGPLVCEDGgrwFLAGITSFGFGCGRRNRPGVFTAV 161
Cdd:pfam00089 146 VVSRETCRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPV 212


                  ....*..
gi 1039780316 162 APYESWI 168
Cdd:pfam00089 213 SSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 2-172 4.90e-38

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 141.71  E-value: 4.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316   2 RSVATILIPDNYSTVELGADLALLRLASPAklgPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPlPLPWVLQEVELR 81
Cdd:COG5640   101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVP 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316  82 LLGEAACQcLYSRPGPfnltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAV 161
Cdd:COG5640   177 VVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRV 247

                         170
                  ....*....|.
gi 1039780316 162 APYESWIREHV 172
Cdd:COG5640   248 SAYRDWIKSTA 258
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 396-578 6.57e-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: 95.04  E-value: 6.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 396 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSTTvpyIEVYLGRAGVSSLPQGHQVSRSVVSIrlpRHLGLRPP 474
Cdd:cd00190    12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 475 -----LALLELNSRVEPSPSALPICLHPGG--IPSGASCWVLGW-----KNPQDRVPVVAAVSILTPRLCHCLY--PGIL 540
Cdd:cd00190    86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYsyGGTI 165

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039780316 541 TPGTFCVLYSEGQEDRCEVTSAPPLLCQTeEGPWVLVG 578
Cdd:cd00190   166 TDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVG 202
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 396-578 4.69e-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: 89.27  E-value: 4.69e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316  396 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCilrLGSTTVPYIEVYLGRAGVSSlpQGHQVSRSVVSIRlpRHLGLRPP 474
Cdd:smart00020  13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHC---VRGSDPSNIRVRLGSHDLSS--GEEGQVIKVSKVI--IHPNYNPS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316  475 -----LALLELNSRVEPSPSALPICLHPGG--IPSGASCWVLGW---KNPQDRVPVV---AAVSILTPRLCHCLYPG--I 539
Cdd:smart00020  86 tydndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtSEGAGSLPDTlqeVNVPIVSNATCRRAYSGggA 165

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039780316  540 LTPGTFCVLYSEGQEDRCEVTSAPPLLCQTEEgpWVLVG 578
Cdd:smart00020 166 ITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR--WVLVG 202
Trypsin pfam00089
Trypsin;
396-567 1.80e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 78.64  E-value: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 396 WPWLTEVHVTGDRV-CTGILVAPGWVLAATHCILRLGSttvpyIEVYLGRAGVSSlPQGHQVSRSVVSIRlpRHLGLRPP 474
Cdd:pfam00089  12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLGAHNIVL-REGGEQKFDVEKII--VHPNYNPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 475 -----LALLELNSRVEPSPSALPICL-HPGGIPS-GASCWVLGWKNP-QDRVPVV---AAVSILTPRLCHCLYPGILTPG 543
Cdd:pfam00089  84 tldndIALLKLESPVTLGDTVRPICLpDASSDLPvGTTCTVSGWGNTkTLGPSDTlqeVTVPVVSRETCRSAYGGTVTDT 163

                         170       180
                  ....*....|....*....|....
gi 1039780316 544 TFCVLYseGQEDRCEVTSAPPLLC 567
Cdd:pfam00089 164 MICAGA--GGKDACQGDSGGPLVC 185
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 396-605 4.16e-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: 4.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 396 WPWLTEVHVTGDR---VCTGILVAPGWVLAATHCILRLGSTTvpyIEVYLGRAGVSSlpQGHQVsRSVVSIRlpRHLGLR 472
Cdd:COG5640    42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGSTDLST--SGGTV-VKVARIV--VHPDYD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 473 PP-----LALLELNsrvEPSPSALPICLHPGG--IPSGASCWVLGW---KNPQDRVPVV---AAVSILTPRLCHcLYPGI 539
Cdd:COG5640   114 PAtpgndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtSEGPGSQSGTlrkADVPVVSDATCA-AYGGF 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039780316 540 LTPGTFCVLYSEGQEDRCEVTSAPPLLcQTEEGPWVLVGMAVRGNRE-------LFAAIGPEATWISQTVGEA 605
Cdd:COG5640   190 DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPcaagypgVYTRVSAYRDWIKSTAGGL 261
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 396-445 5.07e-06

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: 46.00  E-value: 5.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039780316 396 WPWLTEVHVTGDRVCTGILVAPGWVLAATHCiLRLGSTTVPYIEVYLGRA 445
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSC-LRDTNLRHQYISVVLGGA 49
Trypsin pfam00089
Trypsin;
208-251 4.43e-03

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 38.96  E-value: 4.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1039780316 208 GKAPRPGTWPWEAQVTVPGSTP-CYGALVSDRWVLAPASCFLETR 251
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGAS 48
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 406-517 4.88e-03

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 38.89  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780316 406 GDRVCTGILVAPGWVLAATHCILRLGSTTVPY-IEVYLGRAGvssLPQGHQVSRSVVSIRLPRHLGLRPP-LALLELNSR 483
Cdd:COG3591    10 GGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATnIVFVPGYNG---GPYGTATATRFRVPPGWVASGDAGYdYALLRLDEP 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039780316 484 VEPSPSALPIcLHPGGIPSGASCWVLGWknPQDR 517
Cdd:COG3591    87 LGDTTGWLGL-AFNDAPLAGEPVTIIGY--PGDR 117
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 119-154 6.49e-03

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 38.50  E-value: 6.49e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1039780316 119 DTCQGDSGGPLVCEDGGRWFLAGITSFGfGCGRRNR 154
Cdd:COG3591   142 DTTGGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT 176
 
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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