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Conserved domains on  [gi|71984548|ref|NP_500999|]
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Peptidase S1 domain-containing protein [Caenorhabditis elegans]

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

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 ...
38-279 2.40e-58

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  Cd Length: 232  Bit Score: 187.10  E-value: 2.40e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548  38 IIGGNSIDDGA-NWMAKLVSygdNGQGILCGATVIDDFWLVTAAHCALQLQTRSF-VYV----REPKNNRERSFSVKEAY 111
Cdd:cd00190   1 IVGGSEAKIGSfPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYtVRLgshdLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548 112 IHSGYNNQTADNDIALLRISSDLsKLG--IKPVCLvHDDSKLLKQYKNGVVIGYGLTlgedssgEPKLINSQTLQSTSVP 189
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPV-TLSdnVRPICL-PSSGYNLPAGTTCTVSGWGRT-------SEGGPLPDVLQEVNVP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548 190 IISDDDCVKTWRFLSllsvKITGYQICAGAYL--HGTAPGDSGGPlLIHKSNGEYVQIGITSYGADGldgviDQGKFPGV 267
Cdd:cd00190 149 IVSNAECKRAYSYGG----TITDNMLCAGGLEggKDACQGDSGGP-LVCNDNGRGVLVGIVSWGSGC-----ARPNYPGV 218
                       250
                ....*....|..
gi 71984548 268 YTRISKYVPWIQ 279
Cdd:cd00190 219 YTRVSSYLDWIQ 230
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
38-279 2.40e-58

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  Cd Length: 232  Bit Score: 187.10  E-value: 2.40e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548  38 IIGGNSIDDGA-NWMAKLVSygdNGQGILCGATVIDDFWLVTAAHCALQLQTRSF-VYV----REPKNNRERSFSVKEAY 111
Cdd:cd00190   1 IVGGSEAKIGSfPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYtVRLgshdLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548 112 IHSGYNNQTADNDIALLRISSDLsKLG--IKPVCLvHDDSKLLKQYKNGVVIGYGLTlgedssgEPKLINSQTLQSTSVP 189
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPV-TLSdnVRPICL-PSSGYNLPAGTTCTVSGWGRT-------SEGGPLPDVLQEVNVP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548 190 IISDDDCVKTWRFLSllsvKITGYQICAGAYL--HGTAPGDSGGPlLIHKSNGEYVQIGITSYGADGldgviDQGKFPGV 267
Cdd:cd00190 149 IVSNAECKRAYSYGG----TITDNMLCAGGLEggKDACQGDSGGP-LVCNDNGRGVLVGIVSWGSGC-----ARPNYPGV 218
                       250
                ....*....|..
gi 71984548 268 YTRISKYVPWIQ 279
Cdd:cd00190 219 YTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
37-278 9.60e-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: 182.88  E-value: 9.60e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548     37 RIIGGNSIDDGA-NWMAKLVSygdNGQGILCGATVIDDFWLVTAAHCALQLQTRSF-VYVREPKNNRERS---FSVKEAY 111
Cdd:smart00020   1 RIVGGSEANIGSfPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIrVRLGSHDLSSGEEgqvIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548    112 IHSGYNNQTADNDIALLRISSDLsKLG--IKPVCLvHDDSKLLKQYKNGVVIGYGLTLGEDSSgepkliNSQTLQSTSVP 189
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPV-TLSdnVRPICL-PSSNYNVPAGTTCTVSGWGRTSEGAGS------LPDTLQEVNVP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548    190 IISDDDCVKTWRFlsllSVKITGYQICAGAYL--HGTAPGDSGGPLLIHksNGEYVQIGITSYGAdgldgVIDQGKFPGV 267
Cdd:smart00020 150 IVSNATCRRAYSG----GGAITDNMLCAGGLEggKDACQGDSGGPLVCN--DGRWVLVGIVSWGS-----GCARPGKPGV 218
                          250
                   ....*....|.
gi 71984548    268 YTRISKYVPWI 278
Cdd:smart00020 219 YTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
38-278 1.57e-43

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 148.74  E-value: 1.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548    38 IIGGNSIDDGA-NWMAKLVSygdNGQGILCGATVIDDFWLVTAAHC---ALQLQTRSFVYVREPKNNRERSFSVKEAYIH 113
Cdd:pfam00089   1 IVGGDEAQPGSfPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCvsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548   114 SGYNNQTADNDIALLRISSDLSK-LGIKPVCLVHDDSKLlkqyKNG---VVIGYGLTlgeDSSGEPklinsQTLQSTSVP 189
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLgDTVRPICLPDASSDL----PVGttcTVSGWGNT---KTLGPS-----DTLQEVTVP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548   190 IISDDDCVKTWRflsllsVKITGYQICAGAYLHGTAPGDSGGPLLihkSNGEYVqIGITSYGadgldGVIDQGKFPGVYT 269
Cdd:pfam00089 146 VVSRETCRSAYG------GTVTDTMICAGAGGKDACQGDSGGPLV---CSDGEL-IGIVSWG-----YGCASGNYPGVYT 210

                  ....*....
gi 71984548   270 RISKYVPWI 278
Cdd:pfam00089 211 PVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
35-278 2.62e-24

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 101.88  E-value: 2.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548  35 SFRIIGGNSIDDGaNW--MAKLVSY-GDNGQGILCGATVIDDFWLVTAAHCALQLQTRSFVYVR-----EPKNNRERSfS 106
Cdd:COG5640  30 SSRIIGGSNANAG-EYpsLVALVDRiSDYVSGTFCGGSKLGGRYVLTAAHCADASSPISSDVNRvvvdlNDSSQAERG-H 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548 107 VKEAYIHSGYNNQTADNDIALLRISSDLSKLGIKPVCLVHDDSKLLKQYKNG--VVIGYGLTLgeDSSGEPKLINSQTLQ 184
Cdd:COG5640 108 VRTIYVHEFYSPGNLGNDIAVLELARAASLPRVKITSFDASDTFLNSVTTVSpmTNGTFGVTT--PSDVPRSSPKGTILH 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548 185 STSVPIISDDDC--VKTWRFLSLLSVKITGyqICAGAYLHGTAPGDSGGPlLIHKSNGEYVQIGITSYGadglDGVIDQG 262
Cdd:COG5640 186 EVAVLFVPLSTCaqYKGCANASDGATGLTG--FCAGRPPKDACQGDSGGP-IFHKGEEGRVQRGVVSWG----DGGCGGT 258
                       250
                ....*....|....*.
gi 71984548 263 KFPGVYTRISKYVPWI 278
Cdd:COG5640 259 LIPGVYTNVSNYQDWI 274
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
38-279 2.40e-58

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  Cd Length: 232  Bit Score: 187.10  E-value: 2.40e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548  38 IIGGNSIDDGA-NWMAKLVSygdNGQGILCGATVIDDFWLVTAAHCALQLQTRSF-VYV----REPKNNRERSFSVKEAY 111
Cdd:cd00190   1 IVGGSEAKIGSfPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYtVRLgshdLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548 112 IHSGYNNQTADNDIALLRISSDLsKLG--IKPVCLvHDDSKLLKQYKNGVVIGYGLTlgedssgEPKLINSQTLQSTSVP 189
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPV-TLSdnVRPICL-PSSGYNLPAGTTCTVSGWGRT-------SEGGPLPDVLQEVNVP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548 190 IISDDDCVKTWRFLSllsvKITGYQICAGAYL--HGTAPGDSGGPlLIHKSNGEYVQIGITSYGADGldgviDQGKFPGV 267
Cdd:cd00190 149 IVSNAECKRAYSYGG----TITDNMLCAGGLEggKDACQGDSGGP-LVCNDNGRGVLVGIVSWGSGC-----ARPNYPGV 218
                       250
                ....*....|..
gi 71984548 268 YTRISKYVPWIQ 279
Cdd:cd00190 219 YTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
37-278 9.60e-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: 182.88  E-value: 9.60e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548     37 RIIGGNSIDDGA-NWMAKLVSygdNGQGILCGATVIDDFWLVTAAHCALQLQTRSF-VYVREPKNNRERS---FSVKEAY 111
Cdd:smart00020   1 RIVGGSEANIGSfPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIrVRLGSHDLSSGEEgqvIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548    112 IHSGYNNQTADNDIALLRISSDLsKLG--IKPVCLvHDDSKLLKQYKNGVVIGYGLTLGEDSSgepkliNSQTLQSTSVP 189
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPV-TLSdnVRPICL-PSSNYNVPAGTTCTVSGWGRTSEGAGS------LPDTLQEVNVP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548    190 IISDDDCVKTWRFlsllSVKITGYQICAGAYL--HGTAPGDSGGPLLIHksNGEYVQIGITSYGAdgldgVIDQGKFPGV 267
Cdd:smart00020 150 IVSNATCRRAYSG----GGAITDNMLCAGGLEggKDACQGDSGGPLVCN--DGRWVLVGIVSWGS-----GCARPGKPGV 218
                          250
                   ....*....|.
gi 71984548    268 YTRISKYVPWI 278
Cdd:smart00020 219 YTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
38-278 1.57e-43

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 148.74  E-value: 1.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548    38 IIGGNSIDDGA-NWMAKLVSygdNGQGILCGATVIDDFWLVTAAHC---ALQLQTRSFVYVREPKNNRERSFSVKEAYIH 113
Cdd:pfam00089   1 IVGGDEAQPGSfPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCvsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548   114 SGYNNQTADNDIALLRISSDLSK-LGIKPVCLVHDDSKLlkqyKNG---VVIGYGLTlgeDSSGEPklinsQTLQSTSVP 189
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLgDTVRPICLPDASSDL----PVGttcTVSGWGNT---KTLGPS-----DTLQEVTVP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548   190 IISDDDCVKTWRflsllsVKITGYQICAGAYLHGTAPGDSGGPLLihkSNGEYVqIGITSYGadgldGVIDQGKFPGVYT 269
Cdd:pfam00089 146 VVSRETCRSAYG------GTVTDTMICAGAGGKDACQGDSGGPLV---CSDGEL-IGIVSWG-----YGCASGNYPGVYT 210

                  ....*....
gi 71984548   270 RISKYVPWI 278
Cdd:pfam00089 211 PVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
35-278 2.62e-24

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 101.88  E-value: 2.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548  35 SFRIIGGNSIDDGaNW--MAKLVSY-GDNGQGILCGATVIDDFWLVTAAHCALQLQTRSFVYVR-----EPKNNRERSfS 106
Cdd:COG5640  30 SSRIIGGSNANAG-EYpsLVALVDRiSDYVSGTFCGGSKLGGRYVLTAAHCADASSPISSDVNRvvvdlNDSSQAERG-H 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548 107 VKEAYIHSGYNNQTADNDIALLRISSDLSKLGIKPVCLVHDDSKLLKQYKNG--VVIGYGLTLgeDSSGEPKLINSQTLQ 184
Cdd:COG5640 108 VRTIYVHEFYSPGNLGNDIAVLELARAASLPRVKITSFDASDTFLNSVTTVSpmTNGTFGVTT--PSDVPRSSPKGTILH 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984548 185 STSVPIISDDDC--VKTWRFLSLLSVKITGyqICAGAYLHGTAPGDSGGPlLIHKSNGEYVQIGITSYGadglDGVIDQG 262
Cdd:COG5640 186 EVAVLFVPLSTCaqYKGCANASDGATGLTG--FCAGRPPKDACQGDSGGP-IFHKGEEGRVQRGVVSWG----DGGCGGT 258
                       250
                ....*....|....*.
gi 71984548 263 KFPGVYTRISKYVPWI 278
Cdd:COG5640 259 LIPGVYTNVSNYQDWI 274
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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