NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16129556|ref|NP_416115|]
View 

putative serine protease YdgD [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

trypsin-like serine peptidase( domain architecture ID 10007588)

trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  7845208|7733651
SCOP:  3000114

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
57-272 1.28e-44

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


:

Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 149.44  E-value: 1.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556  57 AVGQLET-ASGNLCTATLIAPNLALTAGHCLLTPPKGKADKAVALRFVSNKGLWRYEiHDIEGRVDPtlgkrlkadgdGW 135
Cdd:COG3591   1 AVGRLETdGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTA-TATRFRVPP-----------GW 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556 136 IVPPAAApWDFGLIVLRNPPSGIT-PLPLFEGDKAALtaalkaaGRKVTQAGYPEDHLDTLYSHQNCEVTGWaQTSVMSH 214
Cdd:COG3591  69 VASGDAG-YDYALLRLDEPLGDTTgWLGLAFNDAPLA-------GEPVTIIGYPGDRPKDLSLDCSGRVTGV-QGNRLSY 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129556 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 1.28e-44

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 149.44  E-value: 1.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556  57 AVGQLET-ASGNLCTATLIAPNLALTAGHCLLTPPKGKADKAVALRFVSNKGLWRYEiHDIEGRVDPtlgkrlkadgdGW 135
Cdd:COG3591   1 AVGRLETdGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTA-TATRFRVPP-----------GW 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556 136 IVPPAAApWDFGLIVLRNPPSGIT-PLPLFEGDKAALtaalkaaGRKVTQAGYPEDHLDTLYSHQNCEVTGWaQTSVMSH 214
Cdd:COG3591  69 VASGDAG-YDYALLRLDEPLGDTTgWLGLAFNDAPLA-------GEPVTIIGYPGDRPKDLSLDCSGRVTGV-QGNRLSY 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129556 215 QCDTLPGDSGSPLMLHTDDGWQLIGVQSSAPAAKdrwraDNRAISVTgfRDKLDQLSQ 272
Cdd:COG3591 140 DCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR-----ANTGVRLT--SAIVAALRA 190
Trypsin pfam00089
Trypsin;
52-242 7.13e-06

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 45.90  E-value: 7.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556    52 QSPWDAVGQLETaSGNLCTATLIAPNLALTAGHCLltppkgkadkavalrfvsnKGLWRYEIHDIEGRVDPTLGKRLKAD 131
Cdd:pfam00089  11 SFPWQVSLQLSS-GKHFCGGSLISENWVLTAAHCV-------------------SGASDVKVVLGAHNIVLREGGEQKFD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556   132 GDGWIVPPAAAPW----DFGLIVLRNP---PSGITPLPLfegdkaALTAALKAAGRKVTQAGYPEDHLD----------- 193
Cdd:pfam00089  71 VEKIIVHPNYNPDtldnDIALLKLESPvtlGDTVRPICL------PDASSDLPVGTTCTVSGWGNTKTLgpsdtlqevtv 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16129556   194 TLYSHQNC-EVTGWAQTSVM----SHQCDTLPGDSGSPLMLHTDdgwQLIGVQS 242
Cdd:pfam00089 145 PVVSRETCrSAYGGTVTDTMicagAGGKDACQGDSGGPLVCSDG---ELIGIVS 195
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
63-240 3.22e-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: 44.19  E-value: 3.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556  63 TASGNLCTATLIAPNLALTAGHClltppkgkadkavalrfVSNKGLWRYEI----HDIEGRVDPtlGKRLKADGdgwIVP 138
Cdd:cd00190  21 TGGRHFCGGSLISPRWVLTAAHC-----------------VYSSAPSNYTVrlgsHDLSSNEGG--GQVIKVKK---VIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556 139 -----PAAAPWDFGLIVLRNPP---SGITPLPLfegdkaaltaalkaagrkvtqagyPEDHlDTLYSHQNCEVTGWAQTS 210
Cdd:cd00190  79 hpnynPSTYDNDIALLKLKRPVtlsDNVRPICL------------------------PSSG-YNLPAGTTCTVSGWGRTS 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556 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 1.28e-44

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 149.44  E-value: 1.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556  57 AVGQLET-ASGNLCTATLIAPNLALTAGHCLLTPPKGKADKAVALRFVSNKGLWRYEiHDIEGRVDPtlgkrlkadgdGW 135
Cdd:COG3591   1 AVGRLETdGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTA-TATRFRVPP-----------GW 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556 136 IVPPAAApWDFGLIVLRNPPSGIT-PLPLFEGDKAALtaalkaaGRKVTQAGYPEDHLDTLYSHQNCEVTGWaQTSVMSH 214
Cdd:COG3591  69 VASGDAG-YDYALLRLDEPLGDTTgWLGLAFNDAPLA-------GEPVTIIGYPGDRPKDLSLDCSGRVTGV-QGNRLSY 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129556 215 QCDTLPGDSGSPLMLHTDDGWQLIGVQSSAPAAKdrwraDNRAISVTgfRDKLDQLSQ 272
Cdd:COG3591 140 DCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR-----ANTGVRLT--SAIVAALRA 190
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
49-242 1.43e-13

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 68.91  E-value: 1.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556  49 DTTQSPWDAVGQLETASG---NLCTATLIAPNLALTAGHCLltPPKGKADKAVALrfvsnkglwryeihdieGRVDPTLG 125
Cdd:COG5640  36 PATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCV--DGDGPSDLRVVI-----------------GSTDLSTS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556 126 KRLKADGDGWIVPPAAAPW----DFGLIVLRNPPSGITPLPLfegdkaALTAALKAAGRKVTQAGY------PEDHLDTL 195
Cdd:COG5640  97 GGTVVKVARIVVHPDYDPAtpgnDIALLKLATPVPGVAPAPL------ATSADAAAPGTPATVAGWgrtsegPGSQSGTL 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556 196 Y-------SHQNCEVTGWAQTSVM------SHQCDTLPGDSGSPLMLHTDDGWQLIGVQS 242
Cdd:COG5640 171 RkadvpvvSDATCAAYGGFDGGTMlcagypEGGKDACQGDSGGPLVVKDGGGWVLVGVVS 230
Trypsin pfam00089
Trypsin;
52-242 7.13e-06

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 45.90  E-value: 7.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556    52 QSPWDAVGQLETaSGNLCTATLIAPNLALTAGHCLltppkgkadkavalrfvsnKGLWRYEIHDIEGRVDPTLGKRLKAD 131
Cdd:pfam00089  11 SFPWQVSLQLSS-GKHFCGGSLISENWVLTAAHCV-------------------SGASDVKVVLGAHNIVLREGGEQKFD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556   132 GDGWIVPPAAAPW----DFGLIVLRNP---PSGITPLPLfegdkaALTAALKAAGRKVTQAGYPEDHLD----------- 193
Cdd:pfam00089  71 VEKIIVHPNYNPDtldnDIALLKLESPvtlGDTVRPICL------PDASSDLPVGTTCTVSGWGNTKTLgpsdtlqevtv 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16129556   194 TLYSHQNC-EVTGWAQTSVM----SHQCDTLPGDSGSPLMLHTDdgwQLIGVQS 242
Cdd:pfam00089 145 PVVSRETCrSAYGGTVTDTMicagAGGKDACQGDSGGPLVCSDG---ELIGIVS 195
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
63-240 3.22e-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: 44.19  E-value: 3.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556  63 TASGNLCTATLIAPNLALTAGHClltppkgkadkavalrfVSNKGLWRYEI----HDIEGRVDPtlGKRLKADGdgwIVP 138
Cdd:cd00190  21 TGGRHFCGGSLISPRWVLTAAHC-----------------VYSSAPSNYTVrlgsHDLSSNEGG--GQVIKVKK---VIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556 139 -----PAAAPWDFGLIVLRNPP---SGITPLPLfegdkaaltaalkaagrkvtqagyPEDHlDTLYSHQNCEVTGWAQTS 210
Cdd:cd00190  79 hpnynPSTYDNDIALLKLKRPVtlsDNVRPICL------------------------PSSG-YNLPAGTTCTVSGWGRTS 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556 211 ---------------VMSHQ-----------------C--------DTLPGDSGSPLMLHTDDGWQLIGV 240
Cdd:cd00190 134 eggplpdvlqevnvpIVSNAeckraysyggtitdnmlCaggleggkDACQGDSGGPLVCNDNGRGVLVGI 203
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
69-240 4.69e-05

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 42.41  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556    69 CTATLIAPN-LALTAGHCLLTPPkgkadkavalrfvsNKGLWRYEIHDIEGRVDPtlGKRLKADGDgwivppaaapWDFG 147
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVVDDAE--------------EAAVELVSVVLADGREYP--ATVVARDPD----------LDLA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129556   148 LIVLRNPPSGITPLPLFEGDKAALtaalkaaGRKVTQAGYP----EDHLDT-LYSHQNCEVTGWAQTSVMSHQCDTLPGD 222
Cdd:pfam13365  55 LLRVSGDGRGLPPLPLGDSEPLVG-------GERVYAVGYPlggeKLSLSEgIVSGVDEGRDGGDDGRVIQTDAALSPGS 127
                         170
                  ....*....|....*...
gi 16129556   223 SGSPLMlhtDDGWQLIGV 240
Cdd:pfam13365 128 SGGPVF---DADGRVVGI 142
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH