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Conserved domains on  [gi|694092663|ref|WP_032437327|]
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MULTISPECIES: GTP-binding protein, partial [Enterobacterales]

Protein Classification

elongation factor Tu( domain architecture ID 1000100)

elongation factor Tu promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis

Gene Ontology:  GO:0005525|GO:0003746|GO:0003924
PubMed:  31708880|17446867|8073502

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK00049 super family cl35051
elongation factor Tu; Reviewed
 1-85 4.90e-69

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 210.43  E-value: 4.90e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK00049   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80


                 ....*
gi 694092663  81 DCPGH 85
Cdd:PRK00049  81 DCPGH 85
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-85 4.90e-69

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 210.43  E-value: 4.90e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK00049   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80


                 ....*
gi 694092663  81 DCPGH 85
Cdd:PRK00049  81 DCPGH 85
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-85 1.22e-67

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: 206.92  E-value: 1.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:COG0050    1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80


                 ....*
gi 694092663  81 DCPGH 85
Cdd:COG0050   81 DCPGH 85
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-85 5.45e-59

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: 184.60  E-value: 5.45e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663    1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:TIGR00485   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80


                  ....*
gi 694092663   81 DCPGH 85
Cdd:TIGR00485  81 DCPGH 85
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 11-85 6.51e-54

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. 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.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 165.45  E-value: 6.51e-54
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694092663  11 PHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGH 85
Cdd:cd01884    1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGH 75
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 10-85 4.79e-35

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 117.24  E-value: 4.79e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694092663   10 KPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQ---IDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGH 85
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGH 79
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-85 4.90e-69

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 210.43  E-value: 4.90e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK00049   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80


                 ....*
gi 694092663  81 DCPGH 85
Cdd:PRK00049  81 DCPGH 85
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-85 1.22e-67

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: 206.92  E-value: 1.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:COG0050    1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80


                 ....*
gi 694092663  81 DCPGH 85
Cdd:COG0050   81 DCPGH 85
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-85 3.99e-67

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 205.46  E-value: 3.99e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK12735   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80


                 ....*
gi 694092663  81 DCPGH 85
Cdd:PRK12735  81 DCPGH 85
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-85 7.76e-62

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 191.70  E-value: 7.76e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK12736   1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80


                 ....*
gi 694092663  81 DCPGH 85
Cdd:PRK12736  81 DCPGH 85
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-85 5.45e-59

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: 184.60  E-value: 5.45e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663    1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:TIGR00485   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80


                  ....*
gi 694092663   81 DCPGH 85
Cdd:TIGR00485  81 DCPGH 85
tufA CHL00071
elongation factor Tu
 1-85 4.54e-58

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 182.46  E-value: 4.54e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:CHL00071   1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80


                 ....*
gi 694092663  81 DCPGH 85
Cdd:CHL00071  81 DCPGH 85
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 11-85 6.51e-54

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. 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.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 165.45  E-value: 6.51e-54
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694092663  11 PHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGH 85
Cdd:cd01884    1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGH 75
PLN03127 PLN03127
Elongation factor Tu; Provisional
 2-85 4.26e-50

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 162.69  E-value: 4.26e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   2 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVD 81
Cdd:PLN03127  51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130


                 ....
gi 694092663  82 CPGH 85
Cdd:PLN03127 131 CPGH 134
PLN03126 PLN03126
Elongation factor Tu; Provisional
 2-85 5.75e-45

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 150.15  E-value: 5.75e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   2 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVD 81
Cdd:PLN03126  71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150


                 ....
gi 694092663  82 CPGH 85
Cdd:PLN03126 151 CPGH 154
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 10-85 4.79e-35

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 117.24  E-value: 4.79e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694092663   10 KPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQ---IDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGH 85
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGH 79
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 14-85 7.33e-27

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 96.21  E-value: 7.33e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694092663  14 NVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGH 85
Cdd:cd00881    1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGH 72
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 8-85 8.77e-18

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 75.73  E-value: 8.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   8 RTKPHVNVGTIGHVDHGKTTL-------TAAITTVL-------AKTYGGSARAFDQI-DNAPEEKARGITINTSHVEYDT 72
Cdd:PRK12317   2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIDEHIieelreeAKEKGKESFKFAWVmDRLKEERERGVTIDLAHKKFET 81

                         90
                 ....*....|...
gi 694092663  73 PTRHYAHVDCPGH 85
Cdd:PRK12317  82 DKYYFTIVDCPGH 94
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 8-85 8.82e-17

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: 73.04  E-value: 8.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   8 RTKPHVNVGTIGHVDHGKTTL-------TAAITTVLAKTYGGSARAFDQ--------IDNAPEEKARGITINTSHVEYDT 72
Cdd:COG5256    3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDEHIIEKYEEEAEKKGKesfkfawvMDRLKEERERGVTIDLAHKKFET 82

                         90
                 ....*....|...
gi 694092663  73 PTRHYAHVDCPGH 85
Cdd:COG5256   83 DKYYFTIIDAPGH 95
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 13-85 1.10e-13

selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 64.12  E-value: 1.10e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694092663   13 VNVGTIGHVDHGKTTLTAAITTVLAktyggsarafdqiDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGH 85
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGH 60
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 13-85 1.30e-13

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 62.38  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  13 VNVGTIGHVDHGKTTLTAAITTVLaktyggSARAFDQidnAPEEKARGITINT--SHVEYDTPTRHYAH----------- 79
Cdd:cd01889    1 VNVGLLGHVDSGKTSLAKALSEIA------STAAFDK---NPQSQERGITLDLgfSSFEVDKPKHLEDNenpqienyqit 71


                 ....*..
gi 694092663  80 -VDCPGH 85
Cdd:cd01889   72 lVDCPGH 78
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 14-85 1.43e-13

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 62.51  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  14 NVGTIGHVDHGKTTLTAAITTVL--------------AKTYGGSARAFDQI-DNAPEEKARGITINTSHVEYDTPTRHYA 78
Cdd:cd01883    1 NLVVIGHVDAGKSTLTGHLLYKLggvdkrtiekyekeAKEMGKESFKYAWVlDKLKEERERGVTIDVGLAKFETEKYRFT 80


                 ....*..
gi 694092663  79 HVDCPGH 85
Cdd:cd01883   81 IIDAPGH 87
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 15-85 3.10e-13

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 61.08  E-value: 3.10e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694092663  15 VGTIGHVDHGKTTLTAAITTVlaktyggsarafdQIDNAPEEKARGITINTSHVEYDTPT-RHYAHVDCPGH 85
Cdd:cd04171    2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGH 60
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 13-85 7.15e-13

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 61.85  E-value: 7.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  13 VNVGTIGHVDHGKTTLTAAITTVLAktyggsarafdqiDNAPEEKARGITINTShveydtptrhYAH-----------VD 81
Cdd:COG3276    1 MIIGTAGHIDHGKTTLVKALTGIDT-------------DRLKEEKKRGITIDLG----------FAYlplpdgrrlgfVD 57


                 ....
gi 694092663  82 CPGH 85
Cdd:COG3276   58 VPGH 61
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 13-85 1.05e-12

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 59.97  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  13 VNVGTIGHVDHGKTTLTAAITTVlaktyggsarafdQIDNAPEEKARGITI-------------------NTSHVEYDTP 73
Cdd:cd01888    1 INIGTIGHVAHGKTTLVKALSGV-------------WTVRHKEELKRNITIklgyanakiykcpncgcprPYDTPECECP 67

                         90       100
                 ....*....|....*....|
gi 694092663  74 T--------RHYAHVDCPGH 85
Cdd:cd01888   68 GcggetklvRHVSFVDCPGH 87
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 17-85 1.74e-11

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 58.14  E-value: 1.74e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  17 TIGHVDHGKTTLTAAITTVLAktyggsarafdqiDNAPEEKARGITINTSHVEYDTPT-RHYAHVDCPGH 85
Cdd:PRK10512   5 TAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGH 61
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 7-63 1.97e-11

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 57.94  E-value: 1.97e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 694092663   7 ERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgsarafdqidnapEEKARGITI 63
Cdd:PRK04000   4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGITI 47
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 14-85 2.38e-11

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 57.57  E-value: 2.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  14 NVGTIGHVDHGKTTLT-----AA--ITTVLAktygGSARAFDQIDnapEEKARGITINTSHV----EY----------DT 72
Cdd:PRK07560  22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA----GEQLALDFDE---EEQARGITIKAANVsmvhEYegkeylinliDT 94

                         90
                 ....*....|...
gi 694092663  73 PtrhyAHVDCPGH 85
Cdd:PRK07560  95 P----GHVDFGGD 103
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 1-85 5.80e-11

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


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 56.59  E-value: 5.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   1 MSKEKFERTKphvNVGTIGHVDHGKTTLTAAI------TTVLAKTYGGSArafdQIDNAPEEKARGITINTS--HVEYDT 72
Cdd:COG0480    1 MAEYPLEKIR---NIGIVAHIDAGKTTLTERIlfytgaIHRIGEVHDGNT----VMDWMPEEQERGITITSAatTCEWKG 73

                         90
                 ....*....|....*..
gi 694092663  73 ptrhyaH----VDCPGH 85
Cdd:COG0480   74 ------HkiniIDTPGH 84
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
 11-63 8.01e-11

translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.


Pssm-ID: 274720 [Multi-domain]  Cd Length: 406  Bit Score: 56.21  E-value: 8.01e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 694092663   11 PHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgsarafdqidnapEEKARGITI 63
Cdd:TIGR03680   3 PEVNIGMVGHVDHGKTTLTKALTGVWTDTHS-------------EELKRGISI 42
GCD11 COG5257
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ...
 8-63 8.20e-11

Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444075 [Multi-domain]  Cd Length: 408  Bit Score: 56.00  E-value: 8.20e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 694092663   8 RTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgsarafdqidnapEEKARGITI 63
Cdd:COG5257    1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGITI 43
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 14-85 1.57e-10

Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.


Pssm-ID: 206672 [Multi-domain]  Cd Length: 218  Bit Score: 54.54  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  14 NVGTIGHVDHGKTTLTAA-------ITTVLAktygGSARAfdqIDNAPEEKARGITINTSHV----EYDTPTRHYAH--- 79
Cdd:cd01885    2 NICIIAHVDHGKTTLSDSllasagiISEKLA----GKARY---LDTREDEQERGITIKSSAIslyfEYEEEKMDGNDyli 74


                 ....*...
gi 694092663  80 --VDCPGH 85
Cdd:cd01885   75 nlIDSPGH 82
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-85 1.92e-10

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 55.14  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   1 MSKEKfertkPHVNVGTIGHVDHGKTTLTAAITTVL---------------AKTYGGSARAFDQIDNAPEEKARGITINT 65
Cdd:PTZ00141   1 MGKEK-----THINLVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeaAEMGKGSFKYAWVLDKLKAERERGITIDI 75

                         90       100
                 ....*....|....*....|
gi 694092663  66 SHVEYDTPTRHYAHVDCPGH 85
Cdd:PTZ00141  76 ALWKFETPKYYFTIIDAPGH 95
PTZ00416 PTZ00416
elongation factor 2; Provisional
 14-85 4.52e-10

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 53.90  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  14 NVGTIGHVDHGKTTLTAAITT---VLAKTYGGSARAfdqIDNAPEEKARGITINTS----HVEYDTPTRHYAH------V 80
Cdd:PTZ00416  21 NMSVIAHVDHGKSTLTDSLVCkagIISSKNAGDARF---TDTRADEQERGITIKSTgislYYEHDLEDGDDKQpflinlI 97


                 ....*
gi 694092663  81 DCPGH 85
Cdd:PTZ00416  98 DSPGH 102
PRK13351 PRK13351
elongation factor G-like protein;
14-85 1.83e-09

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 52.26  E-value: 1.83e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694092663  14 NVGTIGHVDHGKTTLTAAITtvlakTYGGSARAFDQIDNA-------PEEKARGITINTSHVEYDTPTRHYAHVDCPGH 85
Cdd:PRK13351  10 NIGILAHIDAGKTTLTERIL-----FYTGKIHKMGEVEDGttvtdwmPQEQERGITIESAATSCDWDNHRINLIDTPGH 83
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 13-85 5.99e-09

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 50.77  E-value: 5.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  13 VNVGTIGHVDHGKTTLTAAITTVLAKTYggsarafdqidnaPEEKARGITIN-----------------------TSHVE 69
Cdd:PTZ00327  35 INIGTIGHVAHGKSTVVKALSGVKTVRF-------------KREKVRNITIKlgyanakiykcpkcprptcyqsyGSSKP 101

                         90       100
                 ....*....|....*....|....*.
gi 694092663  70 YDTP----------TRHYAHVDCPGH 85
Cdd:PTZ00327 102 DNPPcpgcghkmtlKRHVSFVDCPGH 127
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
18-85 7.59e-09

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 50.51  E-value: 7.59e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694092663  18 IGHVDHGKTTLTAAI------TTVLAKTYGGSARAfdqiDNAPEEKARGITINTS--HVEYDTpTRHYAhVDCPGH 85
Cdd:PRK12740   1 VGHSGAGKTTLTEAIlfytgaIHRIGEVEDGTTTM----DFMPEERERGISITSAatTCEWKG-HKINL-IDTPGH 70
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 14-84 1.51e-08

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 49.51  E-value: 1.51e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694092663  14 NVGTIGHVDHGKTTLTAAI------TTVLAKTYGGSARAfdqiDNAPEEKARGITINTS--HVEYDTpTRHYAhVDCPG 84
Cdd:cd04170    1 NIALVGHSGSGKTTLAEALlyatgaIDRLGRVEDGNTVS----DYDPEEKKRKMSIETSvaPLEWNG-HKINL-IDTPG 73
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
 14-85 1.65e-08

GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]


Pssm-ID: 273597 [Multi-domain]  Cd Length: 594  Bit Score: 49.61  E-value: 1.65e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694092663   14 NVGTIGHVDHGKTTLTAAI---TTVLAKTYGGSARAFDQIDnapEEKARGITI---NTShVEYDtPTRhYAHVDCPGH 85
Cdd:TIGR01394   3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEAVAERVMDSND---LERERGITIlakNTA-IRYN-GTK-INIVDTPGH 74
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 17-85 1.98e-08

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 48.72  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  17 TIGHVDHGKTTL-------TAAI------TTVLAKTYGGSARAFDQ---IDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:cd04166    4 TCGSVDDGKSTLigrllydSKSIfedqlaALERSKSSGTQGEKLDLallVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83


                 ....*
gi 694092663  81 DCPGH 85
Cdd:cd04166   84 DTPGH 88
GTPBP1 COG5258
GTPase [General function prediction only];
4-62 2.50e-08

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 49.16  E-value: 2.50e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 694092663   4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFdqIDNAPEEKARGIT 62
Cdd:COG5258  114 EGKEKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLS 170
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 14-73 3.28e-08

Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 48.48  E-value: 3.28e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694092663  14 NVGTIGHVDHGKTTLTAAIttvL--AKTYGGSARAFDQI-DNAPEEKARGITI---NTShVEY--------DTP 73
Cdd:COG1217    8 NIAIIAHVDHGKTTLVDAL---LkqSGTFRENQEVAERVmDSNDLERERGITIlakNTA-VRYkgvkinivDTP 77
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 14-85 3.92e-08

Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.


Pssm-ID: 206678 [Multi-domain]  Cd Length: 194  Bit Score: 47.97  E-value: 3.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  14 NVGTIGHVDHGKTTLTAAITtvlakTYGGSARAFDQI-----DNAPEEKARGITI---NTShVEYDTPTRHYahVDCPGH 85
Cdd:cd01891    4 NIAIIAHVDHGKTTLVDALL-----KQSGTFRENEEVgervmDSNDLERERGITIlakNTA-ITYKDTKINI--IDTPGH 75
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-85 3.16e-07

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 45.85  E-value: 3.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   1 MSKEKFERTKPHVNVG-----TIGHVDHGKTTL-------TAAITT----VLAKTyggSA-RAFDQIDNAP------EEK 57
Cdd:COG2895    1 MSTDIEAYLAQHENKDllrfiTCGSVDDGKSTLigrllydTKSIFEdqlaALERD---SKkRGTQEIDLALltdglqAER 77

                         90       100
                 ....*....|....*....|....*...
gi 694092663  58 ARGITINTSHVEYDTPTRHYAHVDCPGH 85
Cdd:COG2895   78 EQGITIDVAYRYFSTPKRKFIIADTPGH 105
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 14-85 3.40e-07

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 45.22  E-value: 3.40e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694092663  14 NVGTIGHVDHGKTTLTAAIttvLAKTYGGSARAF-DQI-DNAPEEKARGITINTSHV----EYDTPTRHYAH-VDCPGH 85
Cdd:cd01890    2 NFSIIAHIDHGKSTLADRL---LELTGTVSEREMkEQVlDSMDLERERGITIKAQAVrlfyKAKDGEEYLLNlIDTPGH 77
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 14-85 7.90e-07

Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.


Pssm-ID: 206731 [Multi-domain]  Cd Length: 237  Bit Score: 44.53  E-value: 7.90e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694092663  14 NVGTIGHVDHGKTTLTAAI---TTVLAKTygGSARAFD-QIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGH 85
Cdd:cd04168    1 NIGILAHVDAGKTTLTESLlytSGAIREL--GSVDKGTtRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGH 74
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 14-63 1.83e-06

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 43.94  E-value: 1.83e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 694092663  14 NVGTIGHVDHGKTTLT---AAITTVLAKTYGGSARAfdqIDNAPEEKARGITI 63
Cdd:PLN00116  21 NMSVIAHVDHGKSTLTdslVAAAGIIAQEVAGDVRM---TDTRADEAERGITI 70
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-85 4.37e-06

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 42.77  E-value: 4.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663   1 MSKEKFertkpHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQ---------------IDNAPEEKARGITINT 65
Cdd:PLN00043   1 MGKEKV-----HINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKeaaemnkrsfkyawvLDKLKAERERGITIDI 75

                         90       100
                 ....*....|....*....|
gi 694092663  66 SHVEYDTPTRHYAHVDCPGH 85
Cdd:PLN00043  76 ALWKFETTKYYCTVIDAPGH 95
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 14-85 6.31e-06

Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.


Pssm-ID: 206673 [Multi-domain]  Cd Length: 270  Bit Score: 42.09  E-value: 6.31e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694092663  14 NVGTIGHVDHGKTTLTAAI------TTVLAKTYGGSArafdQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGH 85
Cdd:cd01886    1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEVHGGGA----TMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGH 74
PRK10218 PRK10218
translational GTPase TypA;
14-85 8.01e-06

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 42.00  E-value: 8.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694092663  14 NVGTIGHVDHGKTTLtaaITTVLAKTYGGSARAFDQ---IDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGH 85
Cdd:PRK10218   7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSRAETQervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGH 78
infB CHL00189
translation initiation factor 2; Provisional
 15-85 8.37e-05

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 39.05  E-value: 8.37e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694092663  15 VGTIGHVDHGKTTLTAAITtvlaKTyggsarafdqidNAPEEKARGITINTS----HVEYDTPTRHYAHVDCPGH 85
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIR----KT------------QIAQKEAGGITQKIGayevEFEYKDENQKIVFLDTPGH 305
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 19-85 1.39e-04

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 37.84  E-value: 1.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694092663  19 GHVDHGKTTLTAAITtvlaKTyggsarafdqidNAPEEKARGIT--INTSHVEYDTPTRHYAHVDCPGH 85
Cdd:cd01887    7 GHVDHGKTTLLDKIR----KT------------NVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGH 59
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 17-85 1.49e-04

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 38.07  E-value: 1.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694092663  17 TI-GHVDHGKTTLTAAI--TTVLAKtyggsarafdqidnapEekARGIT--INTSHVEydTPTRHYAHVDCPGH 85
Cdd:COG0532    8 TVmGHVDHGKTSLLDAIrkTNVAAG----------------E--AGGITqhIGAYQVE--TNGGKITFLDTPGH 61
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 18-85 1.56e-04

Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.


Pssm-ID: 206732 [Multi-domain]  Cd Length: 268  Bit Score: 37.96  E-value: 1.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694092663  18 IGHVDHGKTTLT-------AAIT---TVLAKTYGGSARAfdqiDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGH 85
Cdd:cd04169    8 ISHPDAGKTTLTeklllfgGAIQeagAVKARKSRKHATS----DWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGH 81
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
 9-85 3.24e-04

translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]


Pssm-ID: 273102 [Multi-domain]  Cd Length: 587  Bit Score: 37.44  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663    9 TKPHVnVGTIGHVDHGKTTLTAAI--TTVLAKTYGgsarafdqidnapeekarGIT--INTSHVEYDTpTRHYAHVDCPG 84
Cdd:TIGR00487  85 ERPPV-VTIMGHVDHGKTSLLDSIrkTKVAQGEAG------------------GITqhIGAYHVENED-GKMITFLDTPG 144


                  .
gi 694092663   85 H 85
Cdd:TIGR00487 145 H 145
PRK04004 PRK04004
translation initiation factor IF-2; Validated
 19-42 8.48e-04

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 36.31  E-value: 8.48e-04
                         10        20
                 ....*....|....*....|....*.
gi 694092663  19 GHVDHGKTTLTAAI--TTVLAKTYGG 42
Cdd:PRK04004  13 GHVDHGKTTLLDKIrgTAVAAKEAGG 38
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 14-85 1.37e-03

Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 35.32  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  14 NVGTIGHVDHGKTTLtaaITTVLAKTY--GGSARAFDQI----DNAPEEKARGITINTSHVEYDTP-TRHYAHV----DC 82
Cdd:cd04167    2 NVCIAGHLHHGKTSL---LDMLIEQTHkrTPSVKLGWKPlrytDTRKDEQERGISIKSNPISLVLEdSKGKSYLiniiDT 78


                 ...
gi 694092663  83 PGH 85
Cdd:cd04167   79 PGH 81
aIF-2 TIGR00491
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ...
 15-42 1.42e-03

translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]


Pssm-ID: 273104 [Multi-domain]  Cd Length: 591  Bit Score: 35.56  E-value: 1.42e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 694092663   15 VGTIGHVDHGKTTLTAAI--TTVLAKTYGG 42
Cdd:TIGR00491   7 VVVLGHVDHGKTTLLDKIrgTAVVKKEAGG 36
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 17-85 2.33e-03

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 34.90  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694092663  17 TIGHVDHGKTTLT---------------AAITTVlAKTYGGSARAFD---QIDNAPEEKARGITINTSHVEYDTPTRHYA 78
Cdd:PRK05506  29 TCGSVDDGKSTLIgrllydskmifedqlAALERD-SKKVGTQGDEIDlalLVDGLAAEREQGITIDVAYRYFATPKRKFI 107


                 ....*..
gi 694092663  79 HVDCPGH 85
Cdd:PRK05506 108 VADTPGH 114
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 13-85 8.16e-03

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 33.11  E-value: 8.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694092663   13 VNVGTIGHVDHGKTTLtaaiTTVLAKTYGgsarafdqidnAPEEKARGIT--INTSHVEYDTPTRHYAHVDCPGH 85
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTL----LNSLLGNKG-----------SITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQ 61
 
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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