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Conserved domains on  [gi|1160852464|ref|WP_079697356|]
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MULTISPECIES: ABC-three component system protein [unclassified Paenibacillus]

Protein Classification

trypsin-like serine peptidase( domain architecture ID 1904017)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
eMpr super family cl42390
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
11-189 1.07e-04

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


The actual alignment was detected with superfamily member COG3591:

Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 43.13  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160852464  11 VRIQVGGTKpSLGSGCLFQPHsdeysYVLTAKHCLigkdFDNPNVLELSDISI---FRDSDFGGEklNVISYKIH----- 82
Cdd:COG3591     3 GRLETDGGG-GVCTGTLIGPN-----LVLTAGHCV----YDGAGGGWATNIVFvpgYNGGPYGTA--TATRFRVPpgwva 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160852464  83 -EDDSYDIACIIVKK----------VNDLPNLLMGEPhrnceIISYGYPyilndrnicgqlfEAKIMHIQRNEQKQFTAk 151
Cdd:COG3591    71 sGDAGYDYALLRLDEplgdttgwlgLAFNDAPLAGEP-----VTIIGYP-------------GDRPKDLSLDCSGRVTG- 131
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1160852464 152 VDVGFLTYENDALtniEGYSGSAVYIQENEGLLIVGVI 189
Cdd:COG3591   132 VQGNRLSYDCDTT---GGSSGSPVLDDSDGGGRVVGVH 166
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
11-189 1.07e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 43.13  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160852464  11 VRIQVGGTKpSLGSGCLFQPHsdeysYVLTAKHCLigkdFDNPNVLELSDISI---FRDSDFGGEklNVISYKIH----- 82
Cdd:COG3591     3 GRLETDGGG-GVCTGTLIGPN-----LVLTAGHCV----YDGAGGGWATNIVFvpgYNGGPYGTA--TATRFRVPpgwva 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160852464  83 -EDDSYDIACIIVKK----------VNDLPNLLMGEPhrnceIISYGYPyilndrnicgqlfEAKIMHIQRNEQKQFTAk 151
Cdd:COG3591    71 sGDAGYDYALLRLDEplgdttgwlgLAFNDAPLAGEP-----VTIIGYP-------------GDRPKDLSLDCSGRVTG- 131
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1160852464 152 VDVGFLTYENDALtniEGYSGSAVYIQENEGLLIVGVI 189
Cdd:COG3591   132 VQGNRLSYDCDTT---GGSSGSPVLDDSDGGGRVVGVH 166
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
11-189 1.07e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 43.13  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160852464  11 VRIQVGGTKpSLGSGCLFQPHsdeysYVLTAKHCLigkdFDNPNVLELSDISI---FRDSDFGGEklNVISYKIH----- 82
Cdd:COG3591     3 GRLETDGGG-GVCTGTLIGPN-----LVLTAGHCV----YDGAGGGWATNIVFvpgYNGGPYGTA--TATRFRVPpgwva 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160852464  83 -EDDSYDIACIIVKK----------VNDLPNLLMGEPhrnceIISYGYPyilndrnicgqlfEAKIMHIQRNEQKQFTAk 151
Cdd:COG3591    71 sGDAGYDYALLRLDEplgdttgwlgLAFNDAPLAGEP-----VTIIGYP-------------GDRPKDLSLDCSGRVTG- 131
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1160852464 152 VDVGFLTYENDALtniEGYSGSAVYIQENEGLLIVGVI 189
Cdd:COG3591   132 VQGNRLSYDCDTT---GGSSGSPVLDDSDGGGRVVGVH 166
 
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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