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Conserved domains on  [gi|167871895|gb|EDS35278|]
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elongation factor tu [Culex quinquefasciatus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 121-207 6.08e-43

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: 140.06  E-value: 6.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 121 LKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDL-AGQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGKTV 199
Cdd:cd03706    6 FEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLpEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLREGGRTI 85


                 ....*...
gi 167871895 200 STGLVTKV 207
Cdd:cd03706   86 GTGVVTKL 93
 
Name Accession Description Interval E-value
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 121-207 6.08e-43

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: 140.06  E-value: 6.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 121 LKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDL-AGQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGKTV 199
Cdd:cd03706    6 FEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLpEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLREGGRTI 85


                 ....*...
gi 167871895 200 STGLVTKV 207
Cdd:cd03706   86 GTGVVTKL 93
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 119-207 1.47e-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: 82.70  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895  119 TTLKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRV-----------DLAGQEMLMPGDHGAVRLTLLRRMVMSCG 187
Cdd:pfam03143   6 TKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhkldpggVSENPEFVMPGDNVIVTVELIKPIALEKG 85

                          90       100
                  ....*....|....*....|
gi 167871895  188 QTFTIRENGKTVSTGLVTKV 207
Cdd:pfam03143  86 QRFAIREGGRTVAAGVVTEI 105
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 119-209 5.69e-19

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: 84.05  E-value: 5.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 119 TTLKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDLA-GQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGK 197
Cdd:COG0050  305 TKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVITLPeGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGR 384

                         90
                 ....*....|..
gi 167871895 198 TVSTGLVTKVLD 209
Cdd:COG0050  385 TVGAGVVTKIIE 396
PRK12736 PRK12736
elongation factor Tu; Reviewed
 119-209 4.74e-18

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 81.53  E-value: 4.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 119 TTLKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDL-AGQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGK 197
Cdd:PRK12736 303 TKFKAEVYILTKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELpEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGR 382

                         90
                 ....*....|..
gi 167871895 198 TVSTGLVTKVLD 209
Cdd:PRK12736 383 TVGAGTVTEILD 394
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 119-208 5.47e-16

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: 75.97  E-value: 5.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895  119 TTLKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDL-AGQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGK 197
Cdd:TIGR00485 303 TKFEAEVYVLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELpEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGR 382

                          90
                  ....*....|.
gi 167871895  198 TVSTGLVTKVL 208
Cdd:TIGR00485 383 TVGAGVVSKIL 393
 
Name Accession Description Interval E-value
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 121-207 6.08e-43

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: 140.06  E-value: 6.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 121 LKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDL-AGQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGKTV 199
Cdd:cd03706    6 FEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLpEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLREGGRTI 85


                 ....*...
gi 167871895 200 STGLVTKV 207
Cdd:cd03706   86 GTGVVTKL 93
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 122-204 9.56e-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: 87.95  E-value: 9.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 122 KGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDL-AGQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGKTVS 200
Cdd:cd03707    7 EAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELpEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIREGGRTVG 86


                 ....
gi 167871895 201 TGLV 204
Cdd:cd03707   87 AGVV 90
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 119-207 1.47e-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: 82.70  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895  119 TTLKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRV-----------DLAGQEMLMPGDHGAVRLTLLRRMVMSCG 187
Cdd:pfam03143   6 TKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhkldpggVSENPEFVMPGDNVIVTVELIKPIALEKG 85

                          90       100
                  ....*....|....*....|
gi 167871895  188 QTFTIRENGKTVSTGLVTKV 207
Cdd:pfam03143  86 QRFAIREGGRTVAAGVVTEI 105
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 119-209 5.69e-19

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: 84.05  E-value: 5.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 119 TTLKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDLA-GQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGK 197
Cdd:COG0050  305 TKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVITLPeGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGR 384

                         90
                 ....*....|..
gi 167871895 198 TVSTGLVTKVLD 209
Cdd:COG0050  385 TVGAGVVTKIIE 396
PRK12736 PRK12736
elongation factor Tu; Reviewed
 119-209 4.74e-18

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 81.53  E-value: 4.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 119 TTLKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDL-AGQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGK 197
Cdd:PRK12736 303 TKFKAEVYILTKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELpEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGR 382

                         90
                 ....*....|..
gi 167871895 198 TVSTGLVTKVLD 209
Cdd:PRK12736 383 TVGAGTVTEILD 394
PRK12735 PRK12735
elongation factor Tu; Reviewed
 119-209 1.35e-17

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 80.27  E-value: 1.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 119 TTLKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDL-AGQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGK 197
Cdd:PRK12735 305 TKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGTIELpEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGR 384

                         90
                 ....*....|..
gi 167871895 198 TVSTGLVTKVLD 209
Cdd:PRK12735 385 TVGAGVVAKIIE 396
PRK00049 PRK00049
elongation factor Tu; Reviewed
 119-209 1.03e-16

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 77.92  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 119 TTLKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDL-AGQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGK 197
Cdd:PRK00049 305 TKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELpEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGR 384

                         90
                 ....*....|..
gi 167871895 198 TVSTGLVTKVLD 209
Cdd:PRK00049 385 TVGAGVVTKIIE 396
PLN03127 PLN03127
Elongation factor Tu; Provisional
 125-209 1.11e-16

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 77.94  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 125 MYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDL-AGQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGKTVSTGL 203
Cdd:PLN03127 362 IYVLTKDEGGRHTPFFSNYRPQFYLRTADVTGKVELpEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGV 441


                 ....*.
gi 167871895 204 VTKVLD 209
Cdd:PLN03127 442 VSKVLS 447
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 119-208 5.47e-16

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: 75.97  E-value: 5.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895  119 TTLKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRVDL-AGQEMLMPGDHGAVRLTLLRRMVMSCGQTFTIRENGK 197
Cdd:TIGR00485 303 TKFEAEVYVLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELpEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGR 382

                          90
                  ....*....|.
gi 167871895  198 TVSTGLVTKVL 208
Cdd:TIGR00485 383 TVGAGVVSKIL 393
tufA CHL00071
elongation factor Tu
 116-209 6.86e-14

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 69.60  E-value: 6.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 116 TFRTTLKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRV------DLAGQEMLMPGDHGAVRLTLLRRMVMSCGQT 189
Cdd:CHL00071 310 TPHTKFEAQVYILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIesftadDGSKTEMVMPGDRIKMTVELIYPIAIEKGMR 389

                         90       100
                 ....*....|....*....|
gi 167871895 190 FTIRENGKTVSTGLVTKVLD 209
Cdd:CHL00071 390 FAIREGGRTVGAGVVSKILK 409
PLN03126 PLN03126
Elongation factor Tu; Provisional
 119-209 1.95e-10

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 59.63  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 119 TTLKGRMYLLAKNEGGRSKPLTSKYIQQLFSKTWNVPCRV----DLAGQE--MLMPGDHGAVRLTLLRRMVMSCGQTFTI 192
Cdd:PLN03126 382 TKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimNDKDEEskMVMPGDRVKMVVELIVPVACEQGMRFAI 461

                         90
                 ....*....|....*..
gi 167871895 193 RENGKTVSTGLVTKVLD 209
Cdd:PLN03126 462 REGGKTVGAGVIQSIIE 478
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 134-204 1.81e-05

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: 42.38  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167871895 134 GRSKPLTSKYIQQLFSKTWNVPCRVDL------------AGQEMLMPGDHGAVRLTLLRRMVMSCGQT------FTIREN 195
Cdd:cd01513   14 EHPKPIRPGYKPVMDVGTAHVPGRIAKllskedgktkekKPPDSLQPGENGTVEVELQKPVVLERGKEfptlgrFALRDG 93


                 ....*....
gi 167871895 196 GKTVSTGLV 204
Cdd:cd01513   94 GRTVGAGLI 102
 
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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