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Conserved domains on  [gi|1720418967|ref|XP_030111491|]
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trypsin X5 isoform X2 [Mus musculus]

Protein Classification

serine protease family protein( domain architecture ID 229414)

trypsin-like serine protease family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
36-243 2.14e-33

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: 120.84  E-value: 2.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967  36 NVPYMVYLQSSPEP--CVGTLIDPQWVLTAAHC---SLPT--KIRLGVYRPNIKNEKEQICNYSFTVVHPNFDAKLLKND 108
Cdd:cd00190    11 SFPWQVSLQYTGGRhfCGGSLISPRWVLTAAHCvysSAPSnyTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDND 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967 109 LMLIKLSYPATINMYVGTIAIA--MEPMAFNESCFIPTWTwNNYKNLSDPDILTWINEYSLSPSDCLDTLHQQKQETRiN 186
Cdd:cd00190    91 IALLKLKRPVTLSDNVRPICLPssGYNLPAGTTCTVSGWG-RTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGTITD-N 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720418967 187 IMCIGHSLNAMSATKEVSAAPAIC----SGRVHGILSWGKASVANGSKGFFTEIHPYARWI 243
Cdd:cd00190   169 MLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
36-243 2.14e-33

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: 120.84  E-value: 2.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967  36 NVPYMVYLQSSPEP--CVGTLIDPQWVLTAAHC---SLPT--KIRLGVYRPNIKNEKEQICNYSFTVVHPNFDAKLLKND 108
Cdd:cd00190    11 SFPWQVSLQYTGGRhfCGGSLISPRWVLTAAHCvysSAPSnyTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDND 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967 109 LMLIKLSYPATINMYVGTIAIA--MEPMAFNESCFIPTWTwNNYKNLSDPDILTWINEYSLSPSDCLDTLHQQKQETRiN 186
Cdd:cd00190    91 IALLKLKRPVTLSDNVRPICLPssGYNLPAGTTCTVSGWG-RTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGTITD-N 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720418967 187 IMCIGHSLNAMSATKEVSAAPAIC----SGRVHGILSWGKASVANGSKGFFTEIHPYARWI 243
Cdd:cd00190   169 MLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
36-243 1.90e-31

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: 115.47  E-value: 1.90e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967   36 NVPYMVYLQSSPEP--CVGTLIDPQWVLTAAHC---SLPT--KIRLGVYRPNiKNEKEQICNYSFTVVHPNFDAKLLKND 108
Cdd:smart00020  12 SFPWQVSLQYGGGRhfCGGSLISPRWVLTAAHCvrgSDPSniRVRLGSHDLS-SGEEGQVIKVSKVIIHPNYNPSTYDND 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967  109 LMLIKLSYPATINMYVGTIAIA--MEPMAFNESCFIPTWTWNNYKNLSDPDILTWINEYSLSPSDCLDTLHQQKQETRiN 186
Cdd:smart00020  91 IALLKLKEPVTLSDNVRPICLPssNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAITD-N 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720418967  187 IMCIGHSLNAMSATKEVSAAPAICSGR---VHGILSWGKaSVANGSK-GFFTEIHPYARWI 243
Cdd:smart00020 170 MLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGS-GCARPGKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
36-243 9.89e-31

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 113.31  E-value: 9.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967  36 NVPYMVYLQ--SSPEPCVGTLIDPQWVLTAAHC---SLPTKIRLGVYRPNIKNEKEQICNYSFTVVHPNFDAKLLKNDLM 110
Cdd:pfam00089  11 SFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCvsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967 111 LIKLSYPATINMYVGTIAIAME--PMAFNESCFIPTWTwnNYKNLSDPDILTWINEYSLSPSDCldtLHQQKQETRINIM 188
Cdd:pfam00089  91 LLKLESPVTLGDTVRPICLPDAssDLPVGTTCTVSGWG--NTKTLGPSDTLQEVTVPVVSRETC---RSAYGGTVTDTMI 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720418967 189 CIGhsLNAMSATKEVSAAPAICS-GRVHGILSWGKASVANGSKGFFTEIHPYARWI 243
Cdd:pfam00089 166 CAG--AGGKDACQGDSGGPLVCSdGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
38-249 4.91e-21

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 88.94  E-value: 4.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967  38 PYMVYLQSSPEP----CVGTLIDPQWVLTAAHC---SLPTKIRLGVYRPNIKNEKEQICNYSFTVVHPNFDAKLLKNDLM 110
Cdd:COG5640    43 PWMVALQSSNGPsgqfCGGTLIAPRWVLTAAHCvdgDGPSDLRVVIGSTDLSTSGGTVVKVARIVVHPDYDPATPGNDIA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967 111 LIKLSYPATINMYV-----------GTIAIAMepmafnescfipTW--TWNNYKnlSDPDILTWINEYSLSPSDClDTLH 177
Cdd:COG5640   123 LLKLATPVPGVAPAplatsadaaapGTPATVA------------GWgrTSEGPG--SQSGTLRKADVPVVSDATC-AAYG 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967 178 QQKQETRInimCIGhslnamsatkEVSAAPAICSG--------------RVHGILSWGKASVANGSKGFFTEIHPYARWI 243
Cdd:COG5640   188 GFDGGTML---CAG----------YPEGGKDACQGdsggplvvkdgggwVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254

                  ....*.
gi 1720418967 244 LKMIRS 249
Cdd:COG5640   255 KSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
36-243 2.14e-33

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: 120.84  E-value: 2.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967  36 NVPYMVYLQSSPEP--CVGTLIDPQWVLTAAHC---SLPT--KIRLGVYRPNIKNEKEQICNYSFTVVHPNFDAKLLKND 108
Cdd:cd00190    11 SFPWQVSLQYTGGRhfCGGSLISPRWVLTAAHCvysSAPSnyTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDND 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967 109 LMLIKLSYPATINMYVGTIAIA--MEPMAFNESCFIPTWTwNNYKNLSDPDILTWINEYSLSPSDCLDTLHQQKQETRiN 186
Cdd:cd00190    91 IALLKLKRPVTLSDNVRPICLPssGYNLPAGTTCTVSGWG-RTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGTITD-N 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720418967 187 IMCIGHSLNAMSATKEVSAAPAIC----SGRVHGILSWGKASVANGSKGFFTEIHPYARWI 243
Cdd:cd00190   169 MLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
36-243 1.90e-31

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: 115.47  E-value: 1.90e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967   36 NVPYMVYLQSSPEP--CVGTLIDPQWVLTAAHC---SLPT--KIRLGVYRPNiKNEKEQICNYSFTVVHPNFDAKLLKND 108
Cdd:smart00020  12 SFPWQVSLQYGGGRhfCGGSLISPRWVLTAAHCvrgSDPSniRVRLGSHDLS-SGEEGQVIKVSKVIIHPNYNPSTYDND 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967  109 LMLIKLSYPATINMYVGTIAIA--MEPMAFNESCFIPTWTWNNYKNLSDPDILTWINEYSLSPSDCLDTLHQQKQETRiN 186
Cdd:smart00020  91 IALLKLKEPVTLSDNVRPICLPssNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAITD-N 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720418967  187 IMCIGHSLNAMSATKEVSAAPAICSGR---VHGILSWGKaSVANGSK-GFFTEIHPYARWI 243
Cdd:smart00020 170 MLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGS-GCARPGKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
36-243 9.89e-31

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 113.31  E-value: 9.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967  36 NVPYMVYLQ--SSPEPCVGTLIDPQWVLTAAHC---SLPTKIRLGVYRPNIKNEKEQICNYSFTVVHPNFDAKLLKNDLM 110
Cdd:pfam00089  11 SFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCvsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967 111 LIKLSYPATINMYVGTIAIAME--PMAFNESCFIPTWTwnNYKNLSDPDILTWINEYSLSPSDCldtLHQQKQETRINIM 188
Cdd:pfam00089  91 LLKLESPVTLGDTVRPICLPDAssDLPVGTTCTVSGWG--NTKTLGPSDTLQEVTVPVVSRETC---RSAYGGTVTDTMI 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720418967 189 CIGhsLNAMSATKEVSAAPAICS-GRVHGILSWGKASVANGSKGFFTEIHPYARWI 243
Cdd:pfam00089 166 CAG--AGGKDACQGDSGGPLVCSdGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
38-249 4.91e-21

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 88.94  E-value: 4.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967  38 PYMVYLQSSPEP----CVGTLIDPQWVLTAAHC---SLPTKIRLGVYRPNIKNEKEQICNYSFTVVHPNFDAKLLKNDLM 110
Cdd:COG5640    43 PWMVALQSSNGPsgqfCGGTLIAPRWVLTAAHCvdgDGPSDLRVVIGSTDLSTSGGTVVKVARIVVHPDYDPATPGNDIA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967 111 LIKLSYPATINMYV-----------GTIAIAMepmafnescfipTW--TWNNYKnlSDPDILTWINEYSLSPSDClDTLH 177
Cdd:COG5640   123 LLKLATPVPGVAPAplatsadaaapGTPATVA------------GWgrTSEGPG--SQSGTLRKADVPVVSDATC-AAYG 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967 178 QQKQETRInimCIGhslnamsatkEVSAAPAICSG--------------RVHGILSWGKASVANGSKGFFTEIHPYARWI 243
Cdd:COG5640   188 GFDGGTML---CAG----------YPEGGKDACQGdsggplvvkdgggwVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254

                  ....*.
gi 1720418967 244 LKMIRS 249
Cdd:COG5640   255 KSTAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
41-130 1.75e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 44.28  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720418967  41 VYLQSSPEPCVGTLIDPQWVLTAAHC-------SLPTKIRlgvYRPNIKNEKEQICNYSFTVVHPNFDAK-LLKNDLMLI 112
Cdd:COG3591     5 LETDGGGGVCTGTLIGPNLVLTAGHCvydgaggGWATNIV---FVPGYNGGPYGTATATRFRVPPGWVASgDAGYDYALL 81
                          90
                  ....*....|....*...
gi 1720418967 113 KLSYPatINMYVGTIAIA 130
Cdd:COG3591    82 RLDEP--LGDTTGWLGLA 97
 
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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