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Conserved domains on  [gi|1057656568|ref|WP_068933790|]
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MULTISPECIES: serine protease [Pseudomonas]

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

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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, ...
79-238 2.27e-11

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


:

Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 62.77  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057656568  79 VGPAYVLTAGHCVfysYGTARVRQAFTAEVTFNYfHDTP--EQRATYAVKTAHW--SSMAGTDLAVLELDTSLGVLVAga 154
Cdd:COG3591    19 IGPNLVLTAGHCV---YDGAGGGWATNIVFVPGY-NGGPygTATATRFRVPPGWvaSGDAGYDYALLRLDEPLGDTTG-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057656568 155 imPLKLASQRQT-SNREVINVGAPTGFLKK-GLRMSACVESTLNSFAEHpgvfpsalrnRCNGLrPGSSGSPMLDRNT-- 230
Cdd:COG3591    93 --WLGLAFNDAPlAGEPVTIIGYPGDRPKDlSLDCSGRVTGVQGNRLSY----------DCDTT-GGSSGSPVLDDSDgg 159

                  ....*...
gi 1057656568 231 NEITSIIS 238
Cdd:COG3591   160 GRVVGVHS 167
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
79-238 2.27e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 62.77  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057656568  79 VGPAYVLTAGHCVfysYGTARVRQAFTAEVTFNYfHDTP--EQRATYAVKTAHW--SSMAGTDLAVLELDTSLGVLVAga 154
Cdd:COG3591    19 IGPNLVLTAGHCV---YDGAGGGWATNIVFVPGY-NGGPygTATATRFRVPPGWvaSGDAGYDYALLRLDEPLGDTTG-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057656568 155 imPLKLASQRQT-SNREVINVGAPTGFLKK-GLRMSACVESTLNSFAEHpgvfpsalrnRCNGLrPGSSGSPMLDRNT-- 230
Cdd:COG3591    93 --WLGLAFNDAPlAGEPVTIIGYPGDRPKDlSLDCSGRVTGVQGNRLSY----------DCDTT-GGSSGSPVLDDSDgg 159

                  ....*...
gi 1057656568 231 NEITSIIS 238
Cdd:COG3591   160 GRVVGVHS 167
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
83-229 3.51e-04

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 40.87  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057656568  83 YVLTAGHCVfysygtarvrqAFTAEVTFNYFHDTPEQRATYAVKTAHWSsmAGTDLAVLELDTSLGVLVagaimPLKLAS 162
Cdd:pfam13365  11 LVLTNAHVV-----------DDAEEAAVELVSVVLADGREYPATVVARD--PDLDLALLRVSGDGRGLP-----PLPLGD 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057656568 163 QRQTSN-REVINVGAPTGflkkgLRMSACVESTLNSFAEHPGVFPSALRNRCNG-LRPGSSGSPMLDRN 229
Cdd:pfam13365  73 SEPLVGgERVYAVGYPLG-----GEKLSLSEGIVSGVDEGRDGGDDGRVIQTDAaLSPGSSGGPVFDAD 136
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
79-238 2.27e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 62.77  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057656568  79 VGPAYVLTAGHCVfysYGTARVRQAFTAEVTFNYfHDTP--EQRATYAVKTAHW--SSMAGTDLAVLELDTSLGVLVAga 154
Cdd:COG3591    19 IGPNLVLTAGHCV---YDGAGGGWATNIVFVPGY-NGGPygTATATRFRVPPGWvaSGDAGYDYALLRLDEPLGDTTG-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057656568 155 imPLKLASQRQT-SNREVINVGAPTGFLKK-GLRMSACVESTLNSFAEHpgvfpsalrnRCNGLrPGSSGSPMLDRNT-- 230
Cdd:COG3591    93 --WLGLAFNDAPlAGEPVTIIGYPGDRPKDlSLDCSGRVTGVQGNRLSY----------DCDTT-GGSSGSPVLDDSDgg 159

                  ....*...
gi 1057656568 231 NEITSIIS 238
Cdd:COG3591   160 GRVVGVHS 167
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
83-229 3.51e-04

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 40.87  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057656568  83 YVLTAGHCVfysygtarvrqAFTAEVTFNYFHDTPEQRATYAVKTAHWSsmAGTDLAVLELDTSLGVLVagaimPLKLAS 162
Cdd:pfam13365  11 LVLTNAHVV-----------DDAEEAAVELVSVVLADGREYPATVVARD--PDLDLALLRVSGDGRGLP-----PLPLGD 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057656568 163 QRQTSN-REVINVGAPTGflkkgLRMSACVESTLNSFAEHPGVFPSALRNRCNG-LRPGSSGSPMLDRN 229
Cdd:pfam13365  73 SEPLVGgERVYAVGYPLG-----GEKLSLSEGIVSGVDEGRDGGDDGRVIQTDAaLSPGSSGGPVFDAD 136
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
61-168 4.80e-04

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 41.94  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057656568  61 GQTCNAVLldtlnrqgkaVGPAYVLTAGHCVF-YSYGTARVRqaftaeVTFNYFHDTPEQRATYAVKTAH---WSSMAGT 136
Cdd:COG5640    56 GQFCGGTL----------IAPRWVLTAAHCVDgDGPSDLRVV------IGSTDLSTSGGTVVKVARIVVHpdyDPATPGN 119
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1057656568 137 DLAVLELDTSLgvlvaGAIMPLKLASQRQTSN 168
Cdd:COG5640   120 DIALLKLATPV-----PGVAPAPLATSADAAA 146
 
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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