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Conserved domains on  [gi|1720377497|ref|XP_030103432|]
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serine protease-like protein 51 isoform X2 [Mus musculus]

Protein Classification

S1 family serine peptidase( domain architecture ID 12184331)

S1 family trypsin-like serine peptidase such as snake venom serine proteases and trypsin, which preferentially cleaves peptide bonds after arginine and lysine residues

CATH:  2.40.10.10
EC:  3.4.-.-
Gene Ontology:  GO:0008236|GO:0006508
MEROPS:  S1
SCOP:  3000114

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
3-210 6.02e-43

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: 145.90  E-value: 6.02e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497    3 GKHLCGGSIIHRWWVLTAAHCFPRTllelVAVNVTVVMG-IKTFSDTNLERKQVQKIIAHRDYKPPDLDSDLCLLLLATP 81
Cdd:smart00020  24 GRHFCGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGsHDLSSGEEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEP 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497   82 IQFNKDKMPICLPQRENSW---DRCWMSEWAYThgHGSAKGSNMHLKKLRVVQISWRTCAKR---VTQLSRNMLCAWKEV 155
Cdd:smart00020 100 VTLSDNVRPICLPSSNYNVpagTTCTVSGWGRT--SEGAGSLPDTLQEVNVPIVSNATCRRAysgGGAITDNMLCAGGLE 177
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720377497  156 GTNGKCQGDSGAPMVCANwetRRLFQVGVFSWGITSGSRGRPGIFVSVAQFIPWI 210
Cdd:smart00020 178 GGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
3-210 6.02e-43

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: 145.90  E-value: 6.02e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497    3 GKHLCGGSIIHRWWVLTAAHCFPRTllelVAVNVTVVMG-IKTFSDTNLERKQVQKIIAHRDYKPPDLDSDLCLLLLATP 81
Cdd:smart00020  24 GRHFCGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGsHDLSSGEEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEP 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497   82 IQFNKDKMPICLPQRENSW---DRCWMSEWAYThgHGSAKGSNMHLKKLRVVQISWRTCAKR---VTQLSRNMLCAWKEV 155
Cdd:smart00020 100 VTLSDNVRPICLPSSNYNVpagTTCTVSGWGRT--SEGAGSLPDTLQEVNVPIVSNATCRRAysgGGAITDNMLCAGGLE 177
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720377497  156 GTNGKCQGDSGAPMVCANwetRRLFQVGVFSWGITSGSRGRPGIFVSVAQFIPWI 210
Cdd:smart00020 178 GGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
3-210 6.91e-43

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: 145.50  E-value: 6.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497   3 GKHLCGGSIIHRWWVLTAAHCFPRTllelVAVNVTVVMGIKTFSDTNLERK--QVQKIIAHRDYKPPDLDSDLCLLLLAT 80
Cdd:cd00190    23 GRHFCGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQviKVKKVIVHPNYNPSTYDNDIALLKLKR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497  81 PIQFNKDKMPICLPQRENSW---DRCWMSEWAYTHGHGSakgSNMHLKKLRVVQISWRTCAKR---VTQLSRNMLCAWKE 154
Cdd:cd00190    99 PVTLSDNVRPICLPSSGYNLpagTTCTVSGWGRTSEGGP---LPDVLQEVNVPIVSNAECKRAysyGGTITDNMLCAGGL 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720377497 155 VGTNGKCQGDSGAPMVCANweTRRLFQVGVFSWGITSGSRGRPGIFVSVAQFIPWI 210
Cdd:cd00190   176 EGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
3-210 5.06e-38

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 132.57  E-value: 5.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497   3 GKHLCGGSIIHRWWVLTAAHCFPRtllelvAVNVTVVMGIKTF--SDTNLERKQVQKIIAHRDYKPPDLDSDLCLLLLAT 80
Cdd:pfam00089  23 GKHFCGGSLISENWVLTAAHCVSG------ASDVKVVLGAHNIvlREGGEQKFDVEKIIVHPNYNPDTLDNDIALLKLES 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497  81 PIQFNKDKMPICLPQRENS---WDRCWMSEWaythGHGSAKGSNMHLKKLRVVQISWRTCAKRV-TQLSRNMLCAwkevG 156
Cdd:pfam00089  97 PVTLGDTVRPICLPDASSDlpvGTTCTVSGW----GNTKTLGPSDTLQEVTVPVVSRETCRSAYgGTVTDTMICA----G 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720377497 157 TNGK--CQGDSGAPMVCANwetrrLFQVGVFSWGITSGSRGRPGIFVSVAQFIPWI 210
Cdd:pfam00089 169 AGGKdaCQGDSGGPLVCSD-----GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
5-210 6.22e-29

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 110.12  E-value: 6.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497   5 HLCGGSIIHRWWVLTAAHCfprtLLELVAVNVTVVMGIKTFSDTNLERKQVQKIIAHRDYKPPDLDSDLCLLLLATPIQF 84
Cdd:COG5640    57 QFCGGTLIAPRWVLTAAHC----VDGDGPSDLRVVIGSTDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPG 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497  85 NKdkmPICLPQRENSW---DRCWMSEWAYThGHGSAKGSNmHLKKLRVVQISWRTCAKRVTQLSRNMLCAWKEVGTNGKC 161
Cdd:COG5640   133 VA---PAPLATSADAAapgTPATVAGWGRT-SEGPGSQSG-TLRKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGKDAC 207
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720377497 162 QGDSGAPMVcaNWETRRLFQVGVFSWGITSGSRGRPGIFVSVAQFIPWI 210
Cdd:COG5640   208 QGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
3-210 6.02e-43

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: 145.90  E-value: 6.02e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497    3 GKHLCGGSIIHRWWVLTAAHCFPRTllelVAVNVTVVMG-IKTFSDTNLERKQVQKIIAHRDYKPPDLDSDLCLLLLATP 81
Cdd:smart00020  24 GRHFCGGSLISPRWVLTAAHCVRGS----DPSNIRVRLGsHDLSSGEEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEP 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497   82 IQFNKDKMPICLPQRENSW---DRCWMSEWAYThgHGSAKGSNMHLKKLRVVQISWRTCAKR---VTQLSRNMLCAWKEV 155
Cdd:smart00020 100 VTLSDNVRPICLPSSNYNVpagTTCTVSGWGRT--SEGAGSLPDTLQEVNVPIVSNATCRRAysgGGAITDNMLCAGGLE 177
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720377497  156 GTNGKCQGDSGAPMVCANwetRRLFQVGVFSWGITSGSRGRPGIFVSVAQFIPWI 210
Cdd:smart00020 178 GGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
3-210 6.91e-43

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: 145.50  E-value: 6.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497   3 GKHLCGGSIIHRWWVLTAAHCFPRTllelVAVNVTVVMGIKTFSDTNLERK--QVQKIIAHRDYKPPDLDSDLCLLLLAT 80
Cdd:cd00190    23 GRHFCGGSLISPRWVLTAAHCVYSS----APSNYTVRLGSHDLSSNEGGGQviKVKKVIVHPNYNPSTYDNDIALLKLKR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497  81 PIQFNKDKMPICLPQRENSW---DRCWMSEWAYTHGHGSakgSNMHLKKLRVVQISWRTCAKR---VTQLSRNMLCAWKE 154
Cdd:cd00190    99 PVTLSDNVRPICLPSSGYNLpagTTCTVSGWGRTSEGGP---LPDVLQEVNVPIVSNAECKRAysyGGTITDNMLCAGGL 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720377497 155 VGTNGKCQGDSGAPMVCANweTRRLFQVGVFSWGITSGSRGRPGIFVSVAQFIPWI 210
Cdd:cd00190   176 EGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
3-210 5.06e-38

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 132.57  E-value: 5.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497   3 GKHLCGGSIIHRWWVLTAAHCFPRtllelvAVNVTVVMGIKTF--SDTNLERKQVQKIIAHRDYKPPDLDSDLCLLLLAT 80
Cdd:pfam00089  23 GKHFCGGSLISENWVLTAAHCVSG------ASDVKVVLGAHNIvlREGGEQKFDVEKIIVHPNYNPDTLDNDIALLKLES 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497  81 PIQFNKDKMPICLPQRENS---WDRCWMSEWaythGHGSAKGSNMHLKKLRVVQISWRTCAKRV-TQLSRNMLCAwkevG 156
Cdd:pfam00089  97 PVTLGDTVRPICLPDASSDlpvGTTCTVSGW----GNTKTLGPSDTLQEVTVPVVSRETCRSAYgGTVTDTMICA----G 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720377497 157 TNGK--CQGDSGAPMVCANwetrrLFQVGVFSWGITSGSRGRPGIFVSVAQFIPWI 210
Cdd:pfam00089 169 AGGKdaCQGDSGGPLVCSD-----GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
5-210 6.22e-29

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 110.12  E-value: 6.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497   5 HLCGGSIIHRWWVLTAAHCfprtLLELVAVNVTVVMGIKTFSDTNLERKQVQKIIAHRDYKPPDLDSDLCLLLLATPIQF 84
Cdd:COG5640    57 QFCGGTLIAPRWVLTAAHC----VDGDGPSDLRVVIGSTDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPG 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377497  85 NKdkmPICLPQRENSW---DRCWMSEWAYThGHGSAKGSNmHLKKLRVVQISWRTCAKRVTQLSRNMLCAWKEVGTNGKC 161
Cdd:COG5640   133 VA---PAPLATSADAAapgTPATVAGWGRT-SEGPGSQSG-TLRKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGKDAC 207
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720377497 162 QGDSGAPMVcaNWETRRLFQVGVFSWGITSGSRGRPGIFVSVAQFIPWI 210
Cdd:COG5640   208 QGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254
 
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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