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Conserved domains on  [gi|57114332|ref|NP_001008864|]
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inactive serine protease 45 precursor [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 ...
57-289 5.00e-70

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: 217.53  E-value: 5.00e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332  57 ERHHWPWEVSLQIE-NEHVCGGALIDQSWVVSAAHCIQGN--KEYLVMLGSSTLQpSGSPWALKIPVGDIIMHPKYwGQN 133
Cdd:cd00190   8 KIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLS-SNEGGGQVIKVKKVIVHPNY-NPS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332 134 FIRSDIALLCLETPVTFNKYIQPICLPEHNFNLKVGMKCWVTGWGqakqHPSAKLTRSLELWEAEVSIVDNKNCDRVFHK 213
Cdd:cd00190  86 TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG----RTSEGGPLPDVLQEVNVPIVSNAECKRAYSY 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57114332 214 KtfypqviPLIRKNMICTTNHR--ENPCYGDPGGPLACEVHGRWILAGIFSWEKACTKAPNLSVYTRIDKYTGWIKEQ 289
Cdd:cd00190 162 G-------GTITDNMLCAGGLEggKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
57-289 5.00e-70

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: 217.53  E-value: 5.00e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332  57 ERHHWPWEVSLQIE-NEHVCGGALIDQSWVVSAAHCIQGN--KEYLVMLGSSTLQpSGSPWALKIPVGDIIMHPKYwGQN 133
Cdd:cd00190   8 KIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLS-SNEGGGQVIKVKKVIVHPNY-NPS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332 134 FIRSDIALLCLETPVTFNKYIQPICLPEHNFNLKVGMKCWVTGWGqakqHPSAKLTRSLELWEAEVSIVDNKNCDRVFHK 213
Cdd:cd00190  86 TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG----RTSEGGPLPDVLQEVNVPIVSNAECKRAYSY 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57114332 214 KtfypqviPLIRKNMICTTNHR--ENPCYGDPGGPLACEVHGRWILAGIFSWEKACTKAPNLSVYTRIDKYTGWIKEQ 289
Cdd:cd00190 162 G-------GTITDNMLCAGGLEggKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
57-286 2.77e-64

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: 202.91  E-value: 2.77e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332     57 ERHHWPWEVSLQIEN-EHVCGGALIDQSWVVSAAHCIQG--NKEYLVMLGSSTLQPSGSpwALKIPVGDIIMHPKYwGQN 133
Cdd:smart00020   9 NIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEE--GQVIKVSKVIIHPNY-NPS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332    134 FIRSDIALLCLETPVTFNKYIQPICLPEHNFNLKVGMKCWVTGWGQAKqhpSAKLTRSLELWEAEVSIVDNKNCDRVFHK 213
Cdd:smart00020  86 TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTS---EGAGSLPDTLQEVNVPIVSNATCRRAYSG 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57114332    214 ktfypqvIPLIRKNMICTTNHR--ENPCYGDPGGPLACEVhGRWILAGIFSWEKACTKAPNLSVYTRIDKYTGWI 286
Cdd:smart00020 163 -------GGAITDNMLCAGGLEggKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
57-286 2.98e-57

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 184.57  E-value: 2.98e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332    57 ERHHWPWEVSLQIE-NEHVCGGALIDQSWVVSAAHCIQGNKEYLVMLGSSTLQpSGSPWALKIPVGDIIMHPKYwGQNFI 135
Cdd:pfam00089   8 QPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIV-LREGGEQKFDVEKIIVHPNY-NPDTL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332   136 RSDIALLCLETPVTFNKYIQPICLPEHNFNLKVGMKCWVTGWGQakqhpSAKLTRSLELWEAEVSIVDNKNCDRVFHKKt 215
Cdd:pfam00089  86 DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGN-----TKTLGPSDTLQEVTVPVVSRETCRSAYGGT- 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57114332   216 fypqviplIRKNMICTTNHRENPCYGDPGGPLACEVHgrwILAGIFSWEKACTKAPNLSVYTRIDKYTGWI 286
Cdd:pfam00089 160 --------VTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
61-290 1.05e-47

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 161.36  E-value: 1.05e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332  61 WPWEVSLQIEN---EHVCGGALIDQSWVVSAAHCIQGN--KEYLVMLGSSTLQPSGSPwalKIPVGDIIMHPKYWGQNFi 135
Cdd:COG5640  42 YPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGT---VVKVARIVVHPDYDPATP- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332 136 RSDIALLCLETPVTFNKYIQpicLPEHNFNLKVGMKCWVTGWGQAKQHPSaklTRSLELWEAEVSIVDNKNCdrvfhkkT 215
Cdd:COG5640 118 GNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPG---SQSGTLRKADVPVVSDATC-------A 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57114332 216 FYPQVIPlirKNMICT--TNHRENPCYGDPGGPLACEVHGRWILAGIFSW-EKACtkAPNL-SVYTRIDKYTGWIKEQV 290
Cdd:COG5640 185 AYGGFDG---GTMLCAgyPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWgGGPC--AAGYpGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
57-289 5.00e-70

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: 217.53  E-value: 5.00e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332  57 ERHHWPWEVSLQIE-NEHVCGGALIDQSWVVSAAHCIQGN--KEYLVMLGSSTLQpSGSPWALKIPVGDIIMHPKYwGQN 133
Cdd:cd00190   8 KIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLS-SNEGGGQVIKVKKVIVHPNY-NPS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332 134 FIRSDIALLCLETPVTFNKYIQPICLPEHNFNLKVGMKCWVTGWGqakqHPSAKLTRSLELWEAEVSIVDNKNCDRVFHK 213
Cdd:cd00190  86 TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG----RTSEGGPLPDVLQEVNVPIVSNAECKRAYSY 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57114332 214 KtfypqviPLIRKNMICTTNHR--ENPCYGDPGGPLACEVHGRWILAGIFSWEKACTKAPNLSVYTRIDKYTGWIKEQ 289
Cdd:cd00190 162 G-------GTITDNMLCAGGLEggKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
57-286 2.77e-64

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: 202.91  E-value: 2.77e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332     57 ERHHWPWEVSLQIEN-EHVCGGALIDQSWVVSAAHCIQG--NKEYLVMLGSSTLQPSGSpwALKIPVGDIIMHPKYwGQN 133
Cdd:smart00020   9 NIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEE--GQVIKVSKVIIHPNY-NPS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332    134 FIRSDIALLCLETPVTFNKYIQPICLPEHNFNLKVGMKCWVTGWGQAKqhpSAKLTRSLELWEAEVSIVDNKNCDRVFHK 213
Cdd:smart00020  86 TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTS---EGAGSLPDTLQEVNVPIVSNATCRRAYSG 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57114332    214 ktfypqvIPLIRKNMICTTNHR--ENPCYGDPGGPLACEVhGRWILAGIFSWEKACTKAPNLSVYTRIDKYTGWI 286
Cdd:smart00020 163 -------GGAITDNMLCAGGLEggKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
57-286 2.98e-57

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 184.57  E-value: 2.98e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332    57 ERHHWPWEVSLQIE-NEHVCGGALIDQSWVVSAAHCIQGNKEYLVMLGSSTLQpSGSPWALKIPVGDIIMHPKYwGQNFI 135
Cdd:pfam00089   8 QPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIV-LREGGEQKFDVEKIIVHPNY-NPDTL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332   136 RSDIALLCLETPVTFNKYIQPICLPEHNFNLKVGMKCWVTGWGQakqhpSAKLTRSLELWEAEVSIVDNKNCDRVFHKKt 215
Cdd:pfam00089  86 DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGN-----TKTLGPSDTLQEVTVPVVSRETCRSAYGGT- 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57114332   216 fypqviplIRKNMICTTNHRENPCYGDPGGPLACEVHgrwILAGIFSWEKACTKAPNLSVYTRIDKYTGWI 286
Cdd:pfam00089 160 --------VTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
61-290 1.05e-47

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 161.36  E-value: 1.05e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332  61 WPWEVSLQIEN---EHVCGGALIDQSWVVSAAHCIQGN--KEYLVMLGSSTLQPSGSPwalKIPVGDIIMHPKYWGQNFi 135
Cdd:COG5640  42 YPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGT---VVKVARIVVHPDYDPATP- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332 136 RSDIALLCLETPVTFNKYIQpicLPEHNFNLKVGMKCWVTGWGQAKQHPSaklTRSLELWEAEVSIVDNKNCdrvfhkkT 215
Cdd:COG5640 118 GNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPG---SQSGTLRKADVPVVSDATC-------A 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57114332 216 FYPQVIPlirKNMICT--TNHRENPCYGDPGGPLACEVHGRWILAGIFSW-EKACtkAPNL-SVYTRIDKYTGWIKEQV 290
Cdd:COG5640 185 AYGGFDG---GTMLCAgyPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWgGGPC--AAGYpGVYTRVSAYRDWIKSTA 258
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
61-176 8.76e-07

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: 47.16  E-value: 8.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57114332    61 WPWEVSLQIENEHVCGGALIDQSWVVSAAHCIQG---NKEYL-VMLGSS-TLQPSGSPWALKIPVGDIimhpkywgQNFI 135
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtnlRHQYIsVVLGGAkTLKSIEGPYEQIVRVDCR--------HDIP 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 57114332   136 RSDIALLCLETPVTFNKYIQPICLPEHNFNLKVGMKCWVTG 176
Cdd:pfam09342  73 ESEISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
 
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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