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Conserved domains on  [gi|291084498|ref|NP_001166166|]
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elongation factor Ts, mitochondrial isoform 3 precursor [Homo sapiens]

Protein Classification

translation elongation factor Ts( domain architecture ID 1012257)

translation elongation factor Ts associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP

CATH:  3.30.479.20
Gene Ontology:  GO:0003746|GO:0006414
SCOP:  4001143

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tsf super family cl33821
Translation elongation factor EF-Ts [Translation, ribosomal structure and biogenesis]; ...
 48-142 1.76e-30

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


The actual alignment was detected with superfamily member COG0264:

Pssm-ID: 440034 [Multi-domain]  Cd Length: 290  Bit Score: 111.71  E-value: 1.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084498  48 ELLMKLRRKTGYSFVNCKKALETCGGDLKQAEIWLhkeaQKEGWSKAAKLQGRKTKEGLIGLLQEGNTTVLVEVNCETDF 127
Cdd:COG0264    6 ALVKELRERTGAGMMDCKKALTEADGDIEKAIEIL----RKKGLAKAAKKAGRVAAEGLVAVAVDGKKGAIVEVNCETDF 81

                         90
                 ....*....|....*
gi 291084498 128 VSRNLKFQLLVQQVA 142
Cdd:COG0264   82 VAKNEDFQAFANEVA 96
 
Name Accession Description Interval E-value
Tsf COG0264
Translation elongation factor EF-Ts [Translation, ribosomal structure and biogenesis]; ...
 48-142 1.76e-30

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


Pssm-ID: 440034 [Multi-domain]  Cd Length: 290  Bit Score: 111.71  E-value: 1.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084498  48 ELLMKLRRKTGYSFVNCKKALETCGGDLKQAEIWLhkeaQKEGWSKAAKLQGRKTKEGLIGLLQEGNTTVLVEVNCETDF 127
Cdd:COG0264    6 ALVKELRERTGAGMMDCKKALTEADGDIEKAIEIL----RKKGLAKAAKKAGRVAAEGLVAVAVDGKKGAIVEVNCETDF 81

                         90
                 ....*....|....*
gi 291084498 128 VSRNLKFQLLVQQVA 142
Cdd:COG0264   82 VAKNEDFQAFANEVA 96
tsf PRK12332
elongation factor Ts; Reviewed
 44-148 3.60e-27

elongation factor Ts; Reviewed


Pssm-ID: 183447 [Multi-domain]  Cd Length: 198  Bit Score: 100.74  E-value: 3.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084498  44 ASSKELLMKLRRKTGYSFVNCKKALETCGGDLKQAEIWLhkeaQKEGWSKAAKLQGRKTKEGLIGLLQEGNTT--VLVEV 121
Cdd:PRK12332   2 AITAKLVKELREKTGAGMMDCKKALEEANGDMEKAIEWL----REKGLAKAAKKAGRVAAEGLVGSYIHTGGRigVLVEL 77

                         90       100
                 ....*....|....*....|....*..
gi 291084498 122 NCETDFVSRNLKFQLLVQQVAlgtmMH 148
Cdd:PRK12332  78 NCETDFVARTEEFKELAKDIA----MQ 100
tsf TIGR00116
translation elongation factor Ts; Translational elongation factor Ts (EF-Ts) catalyzes the ...
 43-142 2.36e-23

translation elongation factor Ts; Translational elongation factor Ts (EF-Ts) catalyzes the exchange of GTP for the GDP of the EF-Tu.GDP complex as part of the cycle of translation elongation. This protein is found in Bacteria, mitochondria, and chloroplasts. [Protein synthesis, Translation factors]


Pssm-ID: 272914 [Multi-domain]  Cd Length: 291  Bit Score: 92.92  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084498   43 SASSKELLMKLRRKTGYSFVNCKKALETCGGDLKQAEIWLhkeaQKEGWSKAAKLQGRKTKEGLIGLLQEGNTTVLVEVN 122
Cdd:TIGR00116   2 MAITAQLVKELRERTGAGMMDCKKALVEANGDFEKAIKWL----REKGIAKAAKKADRVAAEGVIVLKSDNHKAVIVEVN 77

                          90       100
                  ....*....|....*....|
gi 291084498  123 CETDFVSRNLKFQLLVQQVA 142
Cdd:TIGR00116  78 SETDFVAKNEGFKEFANKLL 97
UBA_EF-Ts cd14275
UBA domain found in elongation factor Ts (EF-Ts) from bacteria, chloroplasts and mitochondria ...
 48-84 3.52e-14

UBA domain found in elongation factor Ts (EF-Ts) from bacteria, chloroplasts and mitochondria of eukaryotes; EF-Ts functions as a nucleotide exchange factor in the functional cycle of EF-Tu, another translation elongation factor that facilitates the binding of aminoacylated transfer RNAs (aminoacyl-tRNA) to the ribosomal A site as a ternary complex with guanosine triphosphate during the elongation cycle of protein biosynthesis, and then catalyzes the hydrolysis of GTP and release itself in GDP-bound form. EF-Ts forms complex with EF-Tu and catalyzes the nucleotide exchange reaction promoting the formation of EF-Tu in GTP-bound form from EF-Tu in GDP-bound form. EF-Ts from Thermus thermophiles is shorter than EF-Ts from Escherichia coli, but it has higher thermostability. The mitochondrial translational EF-Ts from chloroplasts and mitochondria display high similarity to the bacterial EF-Ts. The majority of family members contain one ubiquitin-associated (UBA) domain, but some family members from plants harbor two tandem UBA domains.


Pssm-ID: 270461 [Multi-domain]  Cd Length: 37  Bit Score: 62.80  E-value: 3.52e-14
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 291084498  48 ELLMKLRRKTGYSFVNCKKALETCGGDLKQAEIWLHK 84
Cdd:cd14275    1 ELIKELREKTGAGIMDCKKALEEANGDLEKAIEWLRK 37
EF_TS pfam00889
Elongation factor TS;
117-142 6.86e-09

Elongation factor TS;


Pssm-ID: 459984  Cd Length: 204  Bit Score: 52.53  E-value: 6.86e-09
                          10        20
                  ....*....|....*....|....*.
gi 291084498  117 VLVEVNCETDFVSRNLKFQLLVQQVA 142
Cdd:pfam00889   2 VIVEVNSETDFVAKNEDFQEFVNKIA 27
 
Name Accession Description Interval E-value
Tsf COG0264
Translation elongation factor EF-Ts [Translation, ribosomal structure and biogenesis]; ...
 48-142 1.76e-30

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


Pssm-ID: 440034 [Multi-domain]  Cd Length: 290  Bit Score: 111.71  E-value: 1.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084498  48 ELLMKLRRKTGYSFVNCKKALETCGGDLKQAEIWLhkeaQKEGWSKAAKLQGRKTKEGLIGLLQEGNTTVLVEVNCETDF 127
Cdd:COG0264    6 ALVKELRERTGAGMMDCKKALTEADGDIEKAIEIL----RKKGLAKAAKKAGRVAAEGLVAVAVDGKKGAIVEVNCETDF 81

                         90
                 ....*....|....*
gi 291084498 128 VSRNLKFQLLVQQVA 142
Cdd:COG0264   82 VAKNEDFQAFANEVA 96
tsf PRK12332
elongation factor Ts; Reviewed
 44-148 3.60e-27

elongation factor Ts; Reviewed


Pssm-ID: 183447 [Multi-domain]  Cd Length: 198  Bit Score: 100.74  E-value: 3.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084498  44 ASSKELLMKLRRKTGYSFVNCKKALETCGGDLKQAEIWLhkeaQKEGWSKAAKLQGRKTKEGLIGLLQEGNTT--VLVEV 121
Cdd:PRK12332   2 AITAKLVKELREKTGAGMMDCKKALEEANGDMEKAIEWL----REKGLAKAAKKAGRVAAEGLVGSYIHTGGRigVLVEL 77

                         90       100
                 ....*....|....*....|....*..
gi 291084498 122 NCETDFVSRNLKFQLLVQQVAlgtmMH 148
Cdd:PRK12332  78 NCETDFVARTEEFKELAKDIA----MQ 100
tsf TIGR00116
translation elongation factor Ts; Translational elongation factor Ts (EF-Ts) catalyzes the ...
 43-142 2.36e-23

translation elongation factor Ts; Translational elongation factor Ts (EF-Ts) catalyzes the exchange of GTP for the GDP of the EF-Tu.GDP complex as part of the cycle of translation elongation. This protein is found in Bacteria, mitochondria, and chloroplasts. [Protein synthesis, Translation factors]


Pssm-ID: 272914 [Multi-domain]  Cd Length: 291  Bit Score: 92.92  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084498   43 SASSKELLMKLRRKTGYSFVNCKKALETCGGDLKQAEIWLhkeaQKEGWSKAAKLQGRKTKEGLIGLLQEGNTTVLVEVN 122
Cdd:TIGR00116   2 MAITAQLVKELRERTGAGMMDCKKALVEANGDFEKAIKWL----REKGIAKAAKKADRVAAEGVIVLKSDNHKAVIVEVN 77

                          90       100
                  ....*....|....*....|
gi 291084498  123 CETDFVSRNLKFQLLVQQVA 142
Cdd:TIGR00116  78 SETDFVAKNEGFKEFANKLL 97
tsf CHL00098
elongation factor Ts
 46-143 1.05e-22

elongation factor Ts


Pssm-ID: 214362  Cd Length: 200  Bit Score: 89.35  E-value: 1.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084498  46 SKELLMKLRRKTGYSFVNCKKALETCGGDLKQAEiwlhKEAQKEGWSKAAKLQGRKTKEGLI-GLLQEGNTT-VLVEVNC 123
Cdd:CHL00098   1 SAELVKELRDKTGAGMMDCKKALQEANGDFEKAL----ESLRQKGLASANKKSTRITTEGLIeSYIHTGGKLgVLVEINC 76

                         90       100
                 ....*....|....*....|
gi 291084498 124 ETDFVSRNLKFQLLVQQVAL 143
Cdd:CHL00098  77 ETDFVARREEFQKLAKNIAM 96
UBA_EF-Ts cd14275
UBA domain found in elongation factor Ts (EF-Ts) from bacteria, chloroplasts and mitochondria ...
 48-84 3.52e-14

UBA domain found in elongation factor Ts (EF-Ts) from bacteria, chloroplasts and mitochondria of eukaryotes; EF-Ts functions as a nucleotide exchange factor in the functional cycle of EF-Tu, another translation elongation factor that facilitates the binding of aminoacylated transfer RNAs (aminoacyl-tRNA) to the ribosomal A site as a ternary complex with guanosine triphosphate during the elongation cycle of protein biosynthesis, and then catalyzes the hydrolysis of GTP and release itself in GDP-bound form. EF-Ts forms complex with EF-Tu and catalyzes the nucleotide exchange reaction promoting the formation of EF-Tu in GTP-bound form from EF-Tu in GDP-bound form. EF-Ts from Thermus thermophiles is shorter than EF-Ts from Escherichia coli, but it has higher thermostability. The mitochondrial translational EF-Ts from chloroplasts and mitochondria display high similarity to the bacterial EF-Ts. The majority of family members contain one ubiquitin-associated (UBA) domain, but some family members from plants harbor two tandem UBA domains.


Pssm-ID: 270461 [Multi-domain]  Cd Length: 37  Bit Score: 62.80  E-value: 3.52e-14
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 291084498  48 ELLMKLRRKTGYSFVNCKKALETCGGDLKQAEIWLHK 84
Cdd:cd14275    1 ELIKELREKTGAGIMDCKKALEEANGDLEKAIEWLRK 37
EF_TS pfam00889
Elongation factor TS;
117-142 6.86e-09

Elongation factor TS;


Pssm-ID: 459984  Cd Length: 204  Bit Score: 52.53  E-value: 6.86e-09
                          10        20
                  ....*....|....*....|....*.
gi 291084498  117 VLVEVNCETDFVSRNLKFQLLVQQVA 142
Cdd:pfam00889   2 VIVEVNSETDFVAKNEDFQEFVNKIA 27
UBA_like_SF cd00194
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains ...
 53-79 4.06e-05

UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. UBA domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only bind the UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains.


Pssm-ID: 270455  Cd Length: 28  Bit Score: 38.93  E-value: 4.06e-05
                         10        20
                 ....*....|....*....|....*..
gi 291084498  53 LRRKTGYSFVNCKKALETCGGDLKQAE 79
Cdd:cd00194    1 LVDITGASQEEAQQALEACGGNLNIAA 27
UBA_NAC_like_bac cd14360
UBA-like domain found in uncharacterized bacteria proteins similar to eukaryotic nascent ...
 48-84 7.47e-04

UBA-like domain found in uncharacterized bacteria proteins similar to eukaryotic nascent polypeptide-associated complex proteins (NAC); This subfamily contains a group of uncharacterized proteins found in bacteria. They all contain an N-terminal ubiquitin-associated (UBA) that shows high sequence similarity with that of eukaryotic nascent polypeptide-associated complex proteins (NAC) which is one of the cytosolic chaperones that contact the nascent polypeptide chains as they emerge from the ribosome and assist in post-translational processes.


Pssm-ID: 270543 [Multi-domain]  Cd Length: 38  Bit Score: 35.72  E-value: 7.47e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 291084498  48 ELLMKLRRKTGYSFVNCKKALETCGGDLKQAEIWLHK 84
Cdd:cd14360    2 EKVDILRERTNISYEEAKEALEKCNGDLLDALIYLER 38
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
 58-82 6.07e-03

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 33.18  E-value: 6.07e-03
                         10        20
                 ....*....|....*....|....*
gi 291084498  58 GYSFVNCKKALETCGGDLKQAEIWL 82
Cdd:cd14306    8 GFPEEDCIRALRACGGNVEEAANWL 32
 
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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