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Conserved domains on  [gi|1278113281|gb|PIW90259|]
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MAG: hypothetical protein COZ92_01225 [Candidatus Nealsonbacteria bacterium CG_4_8_14_3_um_filter_40_11]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Translation_Factor_II_like super family cl02787
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 35-88 6.03e-03

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


The actual alignment was detected with superfamily member cd01342:

Pssm-ID: 445922 [Multi-domain]  Cd Length: 80  Bit Score: 32.62  E-value: 6.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1278113281 35 LKVGDTIRIVGgkTDFTQAVESMEVEHQKVEVAKKGESVGLKV--GQKVREGYKIY 88
Cdd:cd01342   27 LKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGIlgVKDILTGDTLT 80
 
Name Accession Description Interval E-value
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 35-88 6.03e-03

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 32.62  E-value: 6.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1278113281 35 LKVGDTIRIVGgkTDFTQAVESMEVEHQKVEVAKKGESVGLKV--GQKVREGYKIY 88
Cdd:cd01342   27 LKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGIlgVKDILTGDTLT 80
 
Name Accession Description Interval E-value
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 35-88 6.03e-03

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 32.62  E-value: 6.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1278113281 35 LKVGDTIRIVGgkTDFTQAVESMEVEHQKVEVAKKGESVGLKV--GQKVREGYKIY 88
Cdd:cd01342   27 LKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGIlgVKDILTGDTLT 80
 
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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