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Conserved domains on  [gi|1617302096|dbj|GCY53923|]
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peptidase [Escherichia coli]

Protein Classification

serine protease( domain architecture ID 10007588)

serine protease-like (Spl) protein, having the catalytic triad His, Asp and Ser, has three main activity types: trypsin-, chymotrypsin-, and elastase-like, which cleave amide substrates following Arg or Lys, or following one of the hydrophobic amino acids, or following an Ala, respectively

CATH:  2.40.10.10
EC:  3.4.21.-
Gene Ontology:  GO:0006508|GO:0004252
SCOP:  3000114

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
57-272 2.37e-46

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


:

Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 153.68  E-value: 2.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096  57 AVGQLET-ASGNLCTATLIAPNLALTAGHCLLTPPKGKADKAVALRFVSNKGLWRYEiHDIEGRVDPtlgkrlkadgdGW 135
Cdd:COG3591     1 AVGRLETdGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTA-TATRFRVPP-----------GW 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096 136 IVPPAAApWDFGLIVLRNPPSGIT-PLPLFegdkaelTAALKAAGRKVTQAGYPEDHLDTLYSHQNCEVTGWaQTSVMSH 214
Cdd:COG3591    69 VASGDAG-YDYALLRLDEPLGDTTgWLGLA-------FNDAPLAGEPVTIIGYPGDRPKDLSLDCSGRVTGV-QGNRLSY 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1617302096 215 QCDTLPGDSGSPLMLHTDDGWQLIGVQSSAPAAKdrwraDNRAISVTgfRDKLDQLSQ 272
Cdd:COG3591   140 DCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR-----ANTGVRLT--SAIVAALRA 190
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
57-272 2.37e-46

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 153.68  E-value: 2.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096  57 AVGQLET-ASGNLCTATLIAPNLALTAGHCLLTPPKGKADKAVALRFVSNKGLWRYEiHDIEGRVDPtlgkrlkadgdGW 135
Cdd:COG3591     1 AVGRLETdGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTA-TATRFRVPP-----------GW 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096 136 IVPPAAApWDFGLIVLRNPPSGIT-PLPLFegdkaelTAALKAAGRKVTQAGYPEDHLDTLYSHQNCEVTGWaQTSVMSH 214
Cdd:COG3591    69 VASGDAG-YDYALLRLDEPLGDTTgWLGLA-------FNDAPLAGEPVTIIGYPGDRPKDLSLDCSGRVTGV-QGNRLSY 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1617302096 215 QCDTLPGDSGSPLMLHTDDGWQLIGVQSSAPAAKdrwraDNRAISVTgfRDKLDQLSQ 272
Cdd:COG3591   140 DCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR-----ANTGVRLT--SAIVAALRA 190
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
69-240 4.22e-07

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 48.19  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096  69 CTATLIAPN-LALTAGHCLLTPPkgkadkavalrfvsNKGLWRYEIHDIEGRVDPtlGKRLKADGDgwivppaaapWDFG 147
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVVDDAE--------------EAAVELVSVVLADGREYP--ATVVARDPD----------LDLA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096 148 LIVLRNPPSGITPLPLFEGDKAELTAALKAAGRkvtQAGYPEDHLDT-LYSHQNCEVTGWAQTSVMSHQCDTLPGDSGSP 226
Cdd:pfam13365  55 LLRVSGDGRGLPPLPLGDSEPLVGGERVYAVGY---PLGGEKLSLSEgIVSGVDEGRDGGDDGRVIQTDAALSPGSSGGP 131
                         170
                  ....*....|....
gi 1617302096 227 LMlhtDDGWQLIGV 240
Cdd:pfam13365 132 VF---DADGRVVGI 142
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
63-240 1.48e-05

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: 44.96  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096  63 TASGNLCTATLIAPNLALTAGHClltppkgkadkavalrfVSNKGLWRYEI----HDIEGRVDPtlGKRLKADGdgwIVP 138
Cdd:cd00190    21 TGGRHFCGGSLISPRWVLTAAHC-----------------VYSSAPSNYTVrlgsHDLSSNEGG--GQVIKVKK---VIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096 139 -----PAAAPWDFGLIVLRNPP---SGITPLPLfegdkaeltaalkaagrkvtqagyPEDHlDTLYSHQNCEVTGWAQTS 210
Cdd:cd00190    79 hpnynPSTYDNDIALLKLKRPVtlsDNVRPICL------------------------PSSG-YNLPAGTTCTVSGWGRTS 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096 211 ---------------VMSHQ-----------------C--------DTLPGDSGSPLMLHTDDGWQLIGV 240
Cdd:cd00190   134 eggplpdvlqevnvpIVSNAeckraysyggtitdnmlCaggleggkDACQGDSGGPLVCNDNGRGVLVGI 203
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
57-272 2.37e-46

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 153.68  E-value: 2.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096  57 AVGQLET-ASGNLCTATLIAPNLALTAGHCLLTPPKGKADKAVALRFVSNKGLWRYEiHDIEGRVDPtlgkrlkadgdGW 135
Cdd:COG3591     1 AVGRLETdGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTA-TATRFRVPP-----------GW 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096 136 IVPPAAApWDFGLIVLRNPPSGIT-PLPLFegdkaelTAALKAAGRKVTQAGYPEDHLDTLYSHQNCEVTGWaQTSVMSH 214
Cdd:COG3591    69 VASGDAG-YDYALLRLDEPLGDTTgWLGLA-------FNDAPLAGEPVTIIGYPGDRPKDLSLDCSGRVTGV-QGNRLSY 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1617302096 215 QCDTLPGDSGSPLMLHTDDGWQLIGVQSSAPAAKdrwraDNRAISVTgfRDKLDQLSQ 272
Cdd:COG3591   140 DCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR-----ANTGVRLT--SAIVAALRA 190
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
49-242 1.70e-14

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 71.22  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096  49 DTTQSPWDAVGQLETASG---NLCTATLIAPNLALTAGHCLltPPKGKADKAVALrfvsnkglwryeihdieGRVDPTLG 125
Cdd:COG5640    36 PATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCV--DGDGPSDLRVVI-----------------GSTDLSTS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096 126 KRLKADGDGWIVPPAAAPW----DFGLIVLRNPPSGITPLPLFEGDKAEltaalkAAGRKVTQAGY------PEDHLDTL 195
Cdd:COG5640    97 GGTVVKVARIVVHPDYDPAtpgnDIALLKLATPVPGVAPAPLATSADAA------APGTPATVAGWgrtsegPGSQSGTL 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096 196 Y-------SHQNCEVTGWAQTSVM------SHQCDTLPGDSGSPLMLHTDDGWQLIGVQS 242
Cdd:COG5640   171 RkadvpvvSDATCAAYGGFDGGTMlcagypEGGKDACQGDSGGPLVVKDGGGWVLVGVVS 230
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
69-240 4.22e-07

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 48.19  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096  69 CTATLIAPN-LALTAGHCLLTPPkgkadkavalrfvsNKGLWRYEIHDIEGRVDPtlGKRLKADGDgwivppaaapWDFG 147
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVVDDAE--------------EAAVELVSVVLADGREYP--ATVVARDPD----------LDLA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096 148 LIVLRNPPSGITPLPLFEGDKAELTAALKAAGRkvtQAGYPEDHLDT-LYSHQNCEVTGWAQTSVMSHQCDTLPGDSGSP 226
Cdd:pfam13365  55 LLRVSGDGRGLPPLPLGDSEPLVGGERVYAVGY---PLGGEKLSLSEgIVSGVDEGRDGGDDGRVIQTDAALSPGSSGGP 131
                         170
                  ....*....|....
gi 1617302096 227 LMlhtDDGWQLIGV 240
Cdd:pfam13365 132 VF---DADGRVVGI 142
Trypsin pfam00089
Trypsin;
52-242 1.10e-06

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 48.21  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096  52 QSPWDAVGQLETaSGNLCTATLIAPNLALTAGHCLltppkgkadkavalrfvsnKGLWRYEIHDIEGRVDPTLGKRLKAD 131
Cdd:pfam00089  11 SFPWQVSLQLSS-GKHFCGGSLISENWVLTAAHCV-------------------SGASDVKVVLGAHNIVLREGGEQKFD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096 132 GDGWIVPPAAAPW----DFGLIVLRNP---PSGITPLPLFEgdkaelTAALKAAGRKVTQAGYPEDHLD----------- 193
Cdd:pfam00089  71 VEKIIVHPNYNPDtldnDIALLKLESPvtlGDTVRPICLPD------ASSDLPVGTTCTVSGWGNTKTLgpsdtlqevtv 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1617302096 194 TLYSHQNC-EVTGWAQTSVM----SHQCDTLPGDSGSPLMLHtdDGwQLIGVQS 242
Cdd:pfam00089 145 PVVSRETCrSAYGGTVTDTMicagAGGKDACQGDSGGPLVCS--DG-ELIGIVS 195
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
63-240 1.48e-05

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: 44.96  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096  63 TASGNLCTATLIAPNLALTAGHClltppkgkadkavalrfVSNKGLWRYEI----HDIEGRVDPtlGKRLKADGdgwIVP 138
Cdd:cd00190    21 TGGRHFCGGSLISPRWVLTAAHC-----------------VYSSAPSNYTVrlgsHDLSSNEGG--GQVIKVKK---VIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096 139 -----PAAAPWDFGLIVLRNPP---SGITPLPLfegdkaeltaalkaagrkvtqagyPEDHlDTLYSHQNCEVTGWAQTS 210
Cdd:cd00190    79 hpnynPSTYDNDIALLKLKRPVtlsDNVRPICL------------------------PSSG-YNLPAGTTCTVSGWGRTS 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1617302096 211 ---------------VMSHQ-----------------C--------DTLPGDSGSPLMLHTDDGWQLIGV 240
Cdd:cd00190   134 eggplpdvlqevnvpIVSNAeckraysyggtitdnmlCaggleggkDACQGDSGGPLVCNDNGRGVLVGI 203
 
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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