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Conserved domains on  [gi|2107782769|gb|UCC27167|]
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MAG: elongation factor Tu, partial [Gemmatimonadales bacterium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK00049 super family cl35051
elongation factor Tu; Reviewed
 1-45 6.20e-28

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 101.42  E-value: 6.20e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEIIE 45
Cdd:PRK00049  352 MVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-45 6.20e-28

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 101.42  E-value: 6.20e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEIIE 45
Cdd:PRK00049  352 MVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-45 2.31e-27

Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 99.84  E-value: 2.31e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEIIE 45
Cdd:COG0050   352 MVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 1-40 3.04e-23

Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.


Pssm-ID: 294006 [Multi-domain]  Cd Length: 90  Bit Score: 82.56  E-value: 3.04e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 2107782769  1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVV 40
Cdd:cd03707   51 MVMPGDNVKMTVELIHPIALEEGLRFAIREGGRTVGAGVV 90
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 1-43 1.80e-20

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 76.15  E-value: 1.80e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEI 43
Cdd:pfam03143  63 FVMPGDNVIVTVELIKPIALEKGQRFAIREGGRTVAAGVVTEI 105
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-45 5.53e-20

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 79.82  E-value: 5.53e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEIIE 45
Cdd:TIGR00485 350 MVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-45 6.20e-28

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 101.42  E-value: 6.20e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEIIE 45
Cdd:PRK00049  352 MVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-45 1.90e-27

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 99.91  E-value: 1.90e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEIIE 45
Cdd:PRK12735  352 MVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-45 2.31e-27

Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 99.84  E-value: 2.31e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEIIE 45
Cdd:COG0050   352 MVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-45 8.55e-24

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 90.39  E-value: 8.55e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEIIE 45
Cdd:PRK12736  350 MVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 1-40 3.04e-23

Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.


Pssm-ID: 294006 [Multi-domain]  Cd Length: 90  Bit Score: 82.56  E-value: 3.04e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 2107782769  1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVV 40
Cdd:cd03707   51 MVMPGDNVKMTVELIHPIALEEGLRFAIREGGRTVGAGVV 90
tufA CHL00071
elongation factor Tu
 1-45 3.02e-22

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 86.16  E-value: 3.02e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEIIE 45
Cdd:CHL00071  365 MVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGAGVVSKILK 409
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 1-43 1.80e-20

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 76.15  E-value: 1.80e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEI 43
Cdd:pfam03143  63 FVMPGDNVIVTVELIKPIALEKGQRFAIREGGRTVAAGVVTEI 105
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-45 5.53e-20

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 79.82  E-value: 5.53e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEIIE 45
Cdd:TIGR00485 350 MVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-45 4.33e-18

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 74.48  E-value: 4.33e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEIIE 45
Cdd:PLN03127  403 MVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-45 8.57e-17

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 71.18  E-value: 8.57e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEIIE 45
Cdd:PLN03126  434 MVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGAGVIQSIIE 478
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 1-43 8.27e-13

Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.


Pssm-ID: 294005 [Multi-domain]  Cd Length: 93  Bit Score: 56.47  E-value: 8.27e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 2107782769  1 MVMPGDNVQMEVELITPIAMDKELRFAIREGGRTVGAGVVTEI 43
Cdd:cd03706   51 MVMPGEDTSVKLTLLKPMVLEKGQRFTLREGGRTIGTGVVTKL 93
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 1-40 8.60e-08

Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).


Pssm-ID: 275447 [Multi-domain]  Cd Length: 102  Bit Score: 43.92  E-value: 8.60e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2107782769   1 MVMPGDNVQMEVELITPIAMDK------ELRFAIREGGRTVGAGVV 40
Cdd:cd01513    57 SLQPGENGTVEVELQKPVVLERgkefptLGRFALRDGGRTVGAGLI 102
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 11-43 1.28e-06

C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.


Pssm-ID: 294008 [Multi-domain]  Cd Length: 109  Bit Score: 40.99  E-value: 1.28e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2107782769  11 EVELITPIAMD-----KEL-RFAIREGGRTVGAGVVTEI 43
Cdd:cd04093    71 EIELERPIPLEtfkdnKELgRFVLRRGGETIAAGIVTEI 109
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 25-43 4.82e-04

Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 34.91  E-value: 4.82e-04
                          10
                  ....*....|....*....
gi 2107782769  25 RFAIREGGRTVGAGVVTEI 43
Cdd:COG5256   401 RFAIRDMGQTVAAGVVLDV 419
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 25-43 2.80e-03

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 32.59  E-value: 2.80e-03
                          10
                  ....*....|....*....
gi 2107782769  25 RFAIREGGRTVGAGVVTEI 43
Cdd:PRK12317  402 RFAIRDMGQTIAAGMVIDV 420
 
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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