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Conserved domains on  [gi|1958681802|ref|XP_038949848|]
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serine protease 55 isoform X2 [Rattus norvegicus]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

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 ...
1-164 1.34e-57

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: 182.09  E-value: 1.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802   1 MELQVTNIIRHKDFKRHSMDNDIALLLLANPLTFNEQTVPICMPLQPT-PPSWQECWVAGWGTTnsADKESMNMDLMKVP 79
Cdd:cd00190    69 QVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRT--SEGGPLPDVLQEVN 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802  80 MRITDWKECLQLF---PSLTTNMLCASYGNESFDACQGDSGGPLVCNqeSDGRWYQVGIISWGKSCGQKGSPGIYTVLAN 156
Cdd:cd00190   147 VPIVSNAECKRAYsygGTITDNMLCAGGLEGGKDACQGDSGGPLVCN--DNGRGVLVGIVSWGSGCARPNYPGVYTRVSS 224

                  ....*...
gi 1958681802 157 YILWIEKI 164
Cdd:cd00190   225 YLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-164 1.34e-57

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: 182.09  E-value: 1.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802   1 MELQVTNIIRHKDFKRHSMDNDIALLLLANPLTFNEQTVPICMPLQPT-PPSWQECWVAGWGTTnsADKESMNMDLMKVP 79
Cdd:cd00190    69 QVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRT--SEGGPLPDVLQEVN 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802  80 MRITDWKECLQLF---PSLTTNMLCASYGNESFDACQGDSGGPLVCNqeSDGRWYQVGIISWGKSCGQKGSPGIYTVLAN 156
Cdd:cd00190   147 VPIVSNAECKRAYsygGTITDNMLCAGGLEGGKDACQGDSGGPLVCN--DNGRGVLVGIVSWGSGCARPNYPGVYTRVSS 224

                  ....*...
gi 1958681802 157 YILWIEKI 164
Cdd:cd00190   225 YLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
2-161 1.12e-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: 177.10  E-value: 1.12e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802    2 ELQVTNIIRHKDFKRHSMDNDIALLLLANPLTFNEQTVPICMPLQP-TPPSWQECWVAGWGTTnSADKESMNMDLMKVPM 80
Cdd:smart00020  70 VIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNyNVPAGTTCTVSGWGRT-SEGAGSLPDTLQEVNV 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802   81 RITDWKECLQLFP---SLTTNMLCASYGNESFDACQGDSGGPLVCNqesDGRWYQVGIISWGKSCGQKGSPGIYTVLANY 157
Cdd:smart00020 149 PIVSNATCRRAYSgggAITDNMLCAGGLEGGKDACQGDSGGPLVCN---DGRWVLVGIVSWGSGCARPGKPGVYTRVSSY 225

                   ....
gi 1958681802  158 ILWI 161
Cdd:smart00020 226 LDWI 229
Trypsin pfam00089
Trypsin;
3-161 7.27e-41

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 138.73  E-value: 7.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802   3 LQVTNIIRHKDFKRHSMDNDIALLLLANPLTFNEQTVPICMP-LQPTPPSWQECWVAGWGTTNSADKESMnmdLMKVPMR 81
Cdd:pfam00089  69 FDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPdASSDLPVGTTCTVSGWGNTKTLGPSDT---LQEVTVP 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802  82 ITDWKECLQLFP-SLTTNMLCASYGNEsfDACQGDSGGPLVCNQEsdgrwYQVGIISWGKSCGQKGSPGIYTVLANYILW 160
Cdd:pfam00089 146 VVSRETCRSAYGgTVTDTMICAGAGGK--DACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218

                  .
gi 1958681802 161 I 161
Cdd:pfam00089 219 I 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
5-165 3.67e-40

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 138.24  E-value: 3.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802   5 VTNIIRHKDFKRHSMDNDIALLLLANPLTFNeQTVPIcMPLQPTPPSWQECWVAGWGTTNSADKESMNmDLMKVPMRITD 84
Cdd:COG5640   103 VARIVVHPDYDPATPGNDIALLKLATPVPGV-APAPL-ATSADAAAPGTPATVAGWGRTSEGPGSQSG-TLRKADVPVVS 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802  85 WKECLQLFPSLTTNMLCASYGNESFDACQGDSGGPLVcnQESDGRWYQVGIISWGKSCGQKGSPGIYTVLANYILWIEKI 164
Cdd:COG5640   180 DATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257

                  .
gi 1958681802 165 T 165
Cdd:COG5640   258 A 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-164 1.34e-57

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: 182.09  E-value: 1.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802   1 MELQVTNIIRHKDFKRHSMDNDIALLLLANPLTFNEQTVPICMPLQPT-PPSWQECWVAGWGTTnsADKESMNMDLMKVP 79
Cdd:cd00190    69 QVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRT--SEGGPLPDVLQEVN 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802  80 MRITDWKECLQLF---PSLTTNMLCASYGNESFDACQGDSGGPLVCNqeSDGRWYQVGIISWGKSCGQKGSPGIYTVLAN 156
Cdd:cd00190   147 VPIVSNAECKRAYsygGTITDNMLCAGGLEGGKDACQGDSGGPLVCN--DNGRGVLVGIVSWGSGCARPNYPGVYTRVSS 224

                  ....*...
gi 1958681802 157 YILWIEKI 164
Cdd:cd00190   225 YLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
2-161 1.12e-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: 177.10  E-value: 1.12e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802    2 ELQVTNIIRHKDFKRHSMDNDIALLLLANPLTFNEQTVPICMPLQP-TPPSWQECWVAGWGTTnSADKESMNMDLMKVPM 80
Cdd:smart00020  70 VIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNyNVPAGTTCTVSGWGRT-SEGAGSLPDTLQEVNV 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802   81 RITDWKECLQLFP---SLTTNMLCASYGNESFDACQGDSGGPLVCNqesDGRWYQVGIISWGKSCGQKGSPGIYTVLANY 157
Cdd:smart00020 149 PIVSNATCRRAYSgggAITDNMLCAGGLEGGKDACQGDSGGPLVCN---DGRWVLVGIVSWGSGCARPGKPGVYTRVSSY 225

                   ....
gi 1958681802  158 ILWI 161
Cdd:smart00020 226 LDWI 229
Trypsin pfam00089
Trypsin;
3-161 7.27e-41

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 138.73  E-value: 7.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802   3 LQVTNIIRHKDFKRHSMDNDIALLLLANPLTFNEQTVPICMP-LQPTPPSWQECWVAGWGTTNSADKESMnmdLMKVPMR 81
Cdd:pfam00089  69 FDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPdASSDLPVGTTCTVSGWGNTKTLGPSDT---LQEVTVP 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802  82 ITDWKECLQLFP-SLTTNMLCASYGNEsfDACQGDSGGPLVCNQEsdgrwYQVGIISWGKSCGQKGSPGIYTVLANYILW 160
Cdd:pfam00089 146 VVSRETCRSAYGgTVTDTMICAGAGGK--DACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218

                  .
gi 1958681802 161 I 161
Cdd:pfam00089 219 I 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
5-165 3.67e-40

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 138.24  E-value: 3.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802   5 VTNIIRHKDFKRHSMDNDIALLLLANPLTFNeQTVPIcMPLQPTPPSWQECWVAGWGTTNSADKESMNmDLMKVPMRITD 84
Cdd:COG5640   103 VARIVVHPDYDPATPGNDIALLKLATPVPGV-APAPL-ATSADAAAPGTPATVAGWGRTSEGPGSQSG-TLRKADVPVVS 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802  85 WKECLQLFPSLTTNMLCASYGNESFDACQGDSGGPLVcnQESDGRWYQVGIISWGKSCGQKGSPGIYTVLANYILWIEKI 164
Cdd:COG5640   180 DATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257

                  .
gi 1958681802 165 T 165
Cdd:COG5640   258 A 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
4-162 2.95e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 43.13  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802   4 QVTNIIRHKDFKRHSMDN-DIALLLLANPLTfnEQTVPICMPLQPTPPSWQECWVAGWGTtNSADKESMNMDLmkvpmRI 82
Cdd:COG3591    58 TATRFRVPPGWVASGDAGyDYALLRLDEPLG--DTTGWLGLAFNDAPLAGEPVTIIGYPG-DRPKDLSLDCSG-----RV 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681802  83 TDWkeclqlfpslTTNMLcaSYGNesfDACQGDSGGPLVcnQESDGRWYQVGIISWG-KSCGQKGSPGIYTVLANYILWI 161
Cdd:COG3591   130 TGV----------QGNRL--SYDC---DTTGGSSGSPVL--DDSDGGGRVVGVHSAGgADRANTGVRLTSAIVAALRAWA 192

                  .
gi 1958681802 162 E 162
Cdd:COG3591   193 S 193
 
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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