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Conserved domains on  [gi|667695992|gb|AIG86966|]
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translation elongation factor 1-alpha, partial [Fusarium sp. 2 JM-2014]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-95 8.88e-77

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PTZ00141:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 446  Bit Score: 232.33  E-value: 8.88e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:PTZ00141   7 HINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYY 86

                         90
                 ....*....|....*
gi 667695992  81 VTVIDAPGHRDFIKN 95
Cdd:PTZ00141  87 FTIIDAPGHRDFIKN 101
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-95 8.88e-77

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 232.33  E-value: 8.88e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:PTZ00141   7 HINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYY 86

                         90
                 ....*....|....*
gi 667695992  81 VTVIDAPGHRDFIKN 95
Cdd:PTZ00141  87 FTIIDAPGHRDFIKN 101
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 3-95 5.34e-70

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: 207.73  E-value: 5.34e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYYVT 82
Cdd:cd01883    1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80

                         90
                 ....*....|...
gi 667695992  83 VIDAPGHRDFIKN 95
Cdd:cd01883   81 IIDAPGHRDFVKN 93
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-95 1.96e-58

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 184.30  E-value: 1.96e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992    1 HLNVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:TIGR00483   7 HINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYE 86

                          90
                  ....*....|....*
gi 667695992   81 VTVIDAPGHRDFIKN 95
Cdd:TIGR00483  87 VTIVDCPGHRDFIKN 101
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-95 5.85e-58

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: 183.21  E-value: 5.85e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:COG5256    7 HLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYY 86

                         90
                 ....*....|....*
gi 667695992  81 VTVIDAPGHRDFIKN 95
Cdd:COG5256   87 FTIIDAPGHRDFVKN 101
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-95 1.42e-40

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: 131.88  E-value: 1.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992    1 HLNVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAaelgkgsfkyawVLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:pfam00009   3 HRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKDYL 70

                          90
                  ....*....|....*
gi 667695992   81 VTVIDAPGHRDFIKN 95
Cdd:pfam00009  71 INLIDTPGHVDFVKE 85
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-95 8.88e-77

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 232.33  E-value: 8.88e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:PTZ00141   7 HINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYY 86

                         90
                 ....*....|....*
gi 667695992  81 VTVIDAPGHRDFIKN 95
Cdd:PTZ00141  87 FTIIDAPGHRDFIKN 101
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 3-95 5.34e-70

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: 207.73  E-value: 5.34e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYYVT 82
Cdd:cd01883    1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80

                         90
                 ....*....|...
gi 667695992  83 VIDAPGHRDFIKN 95
Cdd:cd01883   81 IIDAPGHRDFVKN 93
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-95 1.96e-58

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 184.30  E-value: 1.96e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992    1 HLNVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:TIGR00483   7 HINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYE 86

                          90
                  ....*....|....*
gi 667695992   81 VTVIDAPGHRDFIKN 95
Cdd:TIGR00483  87 VTIVDCPGHRDFIKN 101
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-95 5.85e-58

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: 183.21  E-value: 5.85e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:COG5256    7 HLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYY 86

                         90
                 ....*....|....*
gi 667695992  81 VTVIDAPGHRDFIKN 95
Cdd:COG5256   87 FTIIDAPGHRDFVKN 101
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-95 4.87e-57

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 180.89  E-value: 4.87e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:PRK12317   6 HLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYY 85

                         90
                 ....*....|....*
gi 667695992  81 VTVIDAPGHRDFIKN 95
Cdd:PRK12317  86 FTIVDCPGHRDFVKN 100
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-95 9.29e-57

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 180.67  E-value: 9.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:PLN00043   7 HINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYY 86

                         90
                 ....*....|....*
gi 667695992  81 VTVIDAPGHRDFIKN 95
Cdd:PLN00043  87 CTVIDAPGHRDFIKN 101
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-95 1.42e-40

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: 131.88  E-value: 1.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992    1 HLNVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAaelgkgsfkyawVLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:pfam00009   3 HRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKDYL 70

                          90
                  ....*....|....*
gi 667695992   81 VTVIDAPGHRDFIKN 95
Cdd:pfam00009  71 INLIDTPGHVDFVKE 85
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 3-95 2.07e-31

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: 108.54  E-value: 2.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFekeaaelgkgsfkyaWVLDKLKAERERGITIDIALWKFETPRYYVT 82
Cdd:cd00881    1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65

                         90
                 ....*....|...
gi 667695992  83 VIDAPGHRDFIKN 95
Cdd:cd00881   66 FIDTPGHEDFSKE 78
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 2-95 1.92e-21

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: 86.29  E-value: 1.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   2 LNVVVIGHVDSGKSTTTGHLIYQCGGI--DKrtIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP-R 78
Cdd:COG2895   18 LRFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPkR 95

                         90
                 ....*....|....*..
gi 667695992  79 YYVtVIDAPGHRDFIKN 95
Cdd:COG2895   96 KFI-IADTPGHEQYTRN 111
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 3-95 3.38e-21

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: 83.00  E-value: 3.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGI--DK-RTIEKFEKEAAELGKgsFKYAWVLDKLKAERERGITIDIALWKFETPRY 79
Cdd:cd04166    1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlAALERSKSSGTQGEK--LDLALLVDGLQAEREQGITIDVAYRYFSTPKR 78

                         90
                 ....*....|....*.
gi 667695992  80 YVTVIDAPGHRDFIKN 95
Cdd:cd04166   79 KFIIADTPGHEQYTRN 94
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-95 5.62e-16

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: 70.95  E-value: 5.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIyqcggidkrtiekfeKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP-RY 79
Cdd:COG0050   12 HVNIGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEkRH 76

                         90
                 ....*....|....*.
gi 667695992  80 YVTViDAPGHRDFIKN 95
Cdd:COG0050   77 YAHV-DCPGHADYVKN 91
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-95 1.48e-15

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 69.83  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIyqcggidkrtiekfeKEAAELGKGSFK-YAWVlDKLKAERERGITIDIALWKFETP-R 78
Cdd:PRK00049  12 HVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAEAKaYDQI-DKAPEEKARGITINTAHVEYETEkR 75

                         90
                 ....*....|....*..
gi 667695992  79 YYVTViDAPGHRDFIKN 95
Cdd:PRK00049  76 HYAHV-DCPGHADYVKN 91
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 8-95 3.09e-15

sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 213679 [Multi-domain]  Cd Length: 406  Bit Score: 68.94  E-value: 3.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992    8 GHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELGK--GSFKYAWVLDKLKAERERGITIDIALWKFETPRYYVTVID 85
Cdd:TIGR02034   7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86

                          90
                  ....*....|
gi 667695992   86 APGHRDFIKN 95
Cdd:TIGR02034  87 TPGHEQYTRN 96
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-95 5.16e-15

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 68.33  E-value: 5.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIyqcggidkrtiekfeKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP-RY 79
Cdd:PRK12735  12 HVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETAnRH 76

                         90
                 ....*....|....*.
gi 667695992  80 YVTViDAPGHRDFIKN 95
Cdd:PRK12735  77 YAHV-DCPGHADYVKN 91
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 8-95 5.92e-15

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 68.42  E-value: 5.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   8 GHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKEAAELG--KGSFKYAWVLDKLKAERERGITIDIALWKFETPRYYVTVID 85
Cdd:PRK05506  31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110

                         90
                 ....*....|
gi 667695992  86 APGHRDFIKN 95
Cdd:PRK05506 111 TPGHEQYTRN 120
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-95 1.41e-14

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 67.28  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLiyqcggidkrtiekfEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP-RY 79
Cdd:PRK12736  12 HVNIGTIGHVDHGKTTLTAAI---------------TKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEkRH 76

                         90
                 ....*....|....*.
gi 667695992  80 YVTViDAPGHRDFIKN 95
Cdd:PRK12736  77 YAHV-DCPGHADYVKN 91
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-95 1.94e-14

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: 64.91  E-value: 1.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIYQCggidkrtiekfekeaAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP-RY 79
Cdd:cd01884    2 HVNVGTIGHVDHGKTTLTAAITKVL---------------AKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETAnRH 66

                         90
                 ....*....|....*.
gi 667695992  80 YVTViDAPGHRDFIKN 95
Cdd:cd01884   67 YAHV-DCPGHADYIKN 81
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 3-92 5.79e-14

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: 63.32  E-value: 5.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDKRtiekfEKEAAelgkgsfkyawVLDKLKAERERGITID---IAL-WKFETPR 78
Cdd:cd01890    2 NFSIIAHIDHGKSTLADRLLELTGTVSER-----EMKEQ-----------VLDSMDLERERGITIKaqaVRLfYKAKDGE 65

                         90
                 ....*....|....*
gi 667695992  79 YYV-TVIDAPGHRDF 92
Cdd:cd01890   66 EYLlNLIDTPGHVDF 80
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-95 2.33e-13

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: 63.64  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992    1 HLNVVVIGHVDSGKSTTTGHLIyqcggidkrtiekfeKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP-RY 79
Cdd:TIGR00485  12 HVNVGTIGHVDHGKTTLTAAIT---------------TVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETEtRH 76

                          90
                  ....*....|....*.
gi 667695992   80 YVTViDAPGHRDFIKN 95
Cdd:TIGR00485  77 YAHV-DCPGHADYVKN 91
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 3-92 2.58e-13

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: 62.25  E-value: 2.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIekfekeaaelgkGSFKYawvLDKLKAERERGITID---IALwKFETPR- 78
Cdd:cd01885    2 NICIIAHVDHGKTTLSDSLLASAGIISEKLA------------GKARY---LDTREDEQERGITIKssaISL-YFEYEEe 65

                         90       100
                 ....*....|....*....|
gi 667695992  79 ------YYVTVIDAPGHRDF 92
Cdd:cd01885   66 kmdgndYLINLIDSPGHVDF 85
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-95 2.91e-13

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 63.48  E-value: 2.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIYQCGGIDKRTIEKFEKeaaelgkgsfkyawvLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:PLN03126  81 HVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYETENRH 145

                         90
                 ....*....|....*
gi 667695992  81 VTVIDAPGHRDFIKN 95
Cdd:PLN03126 146 YAHVDCPGHADYVKN 160
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-95 1.39e-12

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 61.38  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIyqcggidkrtiekfeKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYY 80
Cdd:PLN03127  61 HVNVGTIGHVDHGKTTLTAAIT---------------KVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRH 125

                         90
                 ....*....|....*
gi 667695992  81 VTVIDAPGHRDFIKN 95
Cdd:PLN03127 126 YAHVDCPGHADYVKN 140
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 3-93 2.98e-12

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: 60.44  E-value: 2.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDKrtIEKFEKEAAelgkgsfkyawVLDKLKAERERGITIDIAL----WKfetpR 78
Cdd:COG0480   11 NIGIVAHIDAGKTTLTERILFYTGAIHR--IGEVHDGNT-----------VMDWMPEEQERGITITSAAttceWK----G 73

                         90
                 ....*....|....*
gi 667695992  79 YYVTVIDAPGHRDFI 93
Cdd:COG0480   74 HKINIIDTPGHVDFT 88
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 8-95 3.19e-12

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 60.31  E-value: 3.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   8 GHVDSGKSTTTGHLIYqcggiDKRTIekFEKEAAELGKGSFK---------YAWVLDKLKAERERGITIDIALWKFETPR 78
Cdd:PRK05124  34 GSVDDGKSTLIGRLLH-----DTKQI--YEDQLASLHNDSKRhgtqgekldLALLVDGLQAEREQGITIDVAYRYFSTEK 106

                         90
                 ....*....|....*..
gi 667695992  79 YYVTVIDAPGHRDFIKN 95
Cdd:PRK05124 107 RKFIIADTPGHEQYTRN 123
PRK13351 PRK13351
elongation factor G-like protein;
3-92 5.97e-12

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 59.58  E-value: 5.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDKRtiekfekeaAELGKGSFkyawVLDKLKAERERGITIDIALWKFETPRYYVT 82
Cdd:PRK13351  10 NIGILAHIDAGKTTLTERILFYTGKIHKM---------GEVEDGTT----VTDWMPQEQERGITIESAATSCDWDNHRIN 76

                         90
                 ....*....|
gi 667695992  83 VIDAPGHRDF 92
Cdd:PRK13351  77 LIDTPGHIDF 86
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 3-92 1.03e-11

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: 58.66  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDKRTiEKFEKEAaelgkgsfkyawVLDKLKAERERGITIDIALWKFETPRYYVT 82
Cdd:cd01886    1 NIGIIAHIDAGKTTTTERILYYTGRIHKIG-EVHGGGA------------TMDWMEQERERGITIQSAATTCFWKDHRIN 67

                         90
                 ....*....|
gi 667695992  83 VIDAPGHRDF 92
Cdd:cd01886   68 IIDTPGHVDF 77
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 3-93 1.68e-11

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: 57.63  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDkrtiekfekeaaELG---KGSFKyawvLDKLKAERERGITIDIALWKFETPRY 79
Cdd:cd04168    1 NIGILAHVDAGKTTLTESLLYTSGAIR------------ELGsvdKGTTR----TDSMELERQRGITIFSAVASFQWEDT 64

                         90
                 ....*....|....
gi 667695992  80 YVTVIDAPGHRDFI 93
Cdd:cd04168   65 KVNIIDTPGHMDFI 78
tufA CHL00071
elongation factor Tu
 1-95 2.74e-11

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 57.66  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   1 HLNVVVIGHVDSGKSTTTGHLIYQCggidkrtiekfekeAAELGKGSFKYAWVlDKLKAERERGITIDIALWKFETP-RY 79
Cdd:CHL00071  12 HVNIGTIGHVDHGKTTLTAAITMTL--------------AAKGGAKAKKYDEI-DSAPEEKARGITINTAHVEYETEnRH 76

                         90
                 ....*....|....*.
gi 667695992  80 YVTViDAPGHRDFIKN 95
Cdd:CHL00071  77 YAHV-DCPGHADYVKN 91
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
7-93 1.19e-10

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 55.90  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   7 IGHVDSGKSTTTGHLIYQCGGIDKR-TIEkfEKEAaelgkgsfkyawVLDKLKAERERGITIDIALWKFETPRYYVTVID 85
Cdd:PRK12740   1 VGHSGAGKTTLTEAILFYTGAIHRIgEVE--DGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66


                 ....*...
gi 667695992  86 APGHRDFI 93
Cdd:PRK12740  67 TPGHVDFT 74
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 8-95 1.42e-10

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: 55.69  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   8 GHVDSGKSTttghLIYQCGGIDkrTiekfekeaaelgkgsfkyawvlDKLKAERERGITIDIALWKFETPRYY-VTVIDA 86
Cdd:COG3276    7 GHIDHGKTT----LVKALTGID--T----------------------DRLKEEKKRGITIDLGFAYLPLPDGRrLGFVDV 58


                 ....*....
gi 667695992  87 PGHRDFIKN 95
Cdd:COG3276   59 PGHEKFIKN 67
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 2-95 1.50e-10

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: 55.65  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992    2 LNVVVIGHVDSGKSTttghLIYQCGGIDKrtiekfekeaaelgkgsfkyawvlDKLKAERERGITIDIALWKFETPRYYV 81
Cdd:TIGR00475   1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52

                          90
                  ....*....|....
gi 667695992   82 TVIDAPGHRDFIKN 95
Cdd:TIGR00475  53 GFIDVPGHEKFISN 66
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 7-92 2.93e-10

Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 55.03  E-value: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   7 IGHVDSGKSTTTGHLIYQCGGIDKRTIEkfekeaaelgkgsfkyAWVLDKLKAERERGITIdialwKFETPR-------- 78
Cdd:COG0481   12 IAHIDHGKSTLADRLLELTGTLSEREMK----------------EQVLDSMDLERERGITI-----KAQAVRlnykakdg 70

                         90
                 ....*....|....*.
gi 667695992  79 --YYVTVIDAPGHRDF 92
Cdd:COG0481   71 etYQLNLIDTPGHVDF 86
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 3-92 1.22e-09

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: 52.21  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGidkrtiekfEKEAAELGKGsfkyawVLDKLKAERERGITIdiaLWK---FETPRY 79
Cdd:cd01891    4 NIAIIAHVDHGKTTLVDALLKQSGT---------FRENEEVGER------VMDSNDLERERGITI---LAKntaITYKDT 65

                         90
                 ....*....|...
gi 667695992  80 YVTVIDAPGHRDF 92
Cdd:cd01891   66 KINIIDTPGHADF 78
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 3-92 1.24e-09

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 53.33  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDKRTiekfekeAAElgkgsfkyAWVLDKLKAERERGITIDIA----LWKFETPR 78
Cdd:PRK07560  22 NIGIIAHIDHGKTTLSDNLLAGAGMISEEL-------AGE--------QLALDFDEEEQARGITIKAAnvsmVHEYEGKE 86

                         90
                 ....*....|....
gi 667695992  79 YYVTVIDAPGHRDF 92
Cdd:PRK07560  87 YLINLIDTPGHVDF 100
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 6-92 2.24e-09

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: 52.21  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   6 VIGHVDSGKSTTTGHLIYQCGGIdkrtiekfeKEAAEL-GKGSFKYAwVLDKLKAERERGITIDIALWKFETPRYYVTVI 84
Cdd:cd04169    7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76


                 ....*...
gi 667695992  85 DAPGHRDF 92
Cdd:cd04169   77 DTPGHEDF 84
PRK10218 PRK10218
translational GTPase TypA;
3-92 2.55e-09

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 52.40  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDKRTiEKFEKeaaelgkgsfkyawVLDKLKAERERGITIDIALWKFETPRYYVT 82
Cdd:PRK10218   7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA-ETQER--------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71

                         90
                 ....*....|
gi 667695992  83 VIDAPGHRDF 92
Cdd:PRK10218  72 IVDTPGHADF 81
PTZ00416 PTZ00416
elongation factor 2; Provisional
 3-92 3.48e-09

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 51.97  E-value: 3.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDkrtiekfEKEAAElgkgsfkyAWVLDKLKAERERGITID---IALWkFETP-- 77
Cdd:PTZ00416  21 NMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNAGD--------ARFTDTRADEQERGITIKstgISLY-YEHDle 84

                         90       100
                 ....*....|....*....|.
gi 667695992  78 ------RYYVTVIDAPGHRDF 92
Cdd:PTZ00416  85 dgddkqPFLINLIDSPGHVDF 105
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 8-95 4.55e-09

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: 50.30  E-value: 4.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   8 GHVDSGKSTttghLIYQCGGIDKrtiekfekeaaelgkgsfkyawvlDKLKAERERGITIDIALWKFETPRYYVT-VIDA 86
Cdd:cd04171    6 GHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLGFAYLDLPDGKRLgFIDV 57


                 ....*....
gi 667695992  87 PGHRDFIKN 95
Cdd:cd04171   58 PGHEKFVKN 66
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 3-94 1.49e-08

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: 49.29  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTtghliyqcggidkrtiekfekeAAELGKGSFKYAwvLDKLKAERERGITIDIALWKFETP----- 77
Cdd:cd01889    2 NVGLLGHVDSGKTSL----------------------AKALSEIASTAA--FDKNPQSQERGITLDLGFSSFEVDkpkhl 57

                         90       100
                 ....*....|....*....|....*.
gi 667695992  78 ---------RYYVTVIDAPGHRDFIK 94
Cdd:cd01889   58 ednenpqieNYQITLVDCPGHASLIR 83
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 3-92 2.09e-08

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 49.72  E-value: 2.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIdkrtiekfEKEAAelgkGSFKYAwvlDKLKAERERGITI------------DIA 70
Cdd:PLN00116  21 NMSVIAHVDHGKSTLTDSLVAAAGII--------AQEVA----GDVRMT---DTRADEAERGITIkstgislyyemtDES 85

                         90       100
                 ....*....|....*....|....*.
gi 667695992  71 LWKFETPR----YYVTVIDAPGHRDF 92
Cdd:PLN00116  86 LKDFKGERdgneYLINLIDSPGHVDF 111
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 3-92 3.62e-08

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 48.86  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDKRtiekfeKEAAELgkgsfkyawVLDKLKAERERGITI---DIAL-WKfetpR 78
Cdd:COG1217    8 NIAIIAHVDHGKTTLVDALLKQSGTFREN------QEVAER---------VMDSNDLERERGITIlakNTAVrYK----G 68

                         90
                 ....*....|....
gi 667695992  79 YYVTVIDAPGHRDF 92
Cdd:COG1217   69 VKINIVDTPGHADF 82
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 3-93 6.34e-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: 47.97  E-value: 6.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQCGGIDKR-TIEkfekeaaelgKGSFkyawVLDKLKAERERGITIDIALWKFETPRYYV 81
Cdd:cd04170    1 NIALVGHSGSGKTTLAEALLYATGAIDRLgRVE----------DGNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKI 66

                         90
                 ....*....|..
gi 667695992  82 TVIDAPGHRDFI 93
Cdd:cd04170   67 NLIDTPGYADFV 78
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 3-93 4.95e-07

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: 45.34  E-value: 4.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIYQcggIDKRTIEKfekeaaELGKGSFKYawvLDKLKAERERGITI-----DIALWKFETP 77
Cdd:cd04167    2 NVCIAGHLHHGKTSLLDMLIEQ---THKRTPSV------KLGWKPLRY---TDTRKDEQERGISIksnpiSLVLEDSKGK 69

                         90
                 ....*....|....*.
gi 667695992  78 RYYVTVIDAPGHRDFI 93
Cdd:cd04167   70 SYLINIIDTPGHVNFM 85
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 8-95 5.70e-05

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 40.03  E-value: 5.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   8 GHVDSGKSTttghLIYQCGGIDKrtiekfekeaaelgkgsfkyawvlDKLKAERERGITIDI--ALWKFETPRYyVTVID 85
Cdd:PRK10512   7 GHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGRV-LGFID 57

                         90
                 ....*....|
gi 667695992  86 APGHRDFIKN 95
Cdd:PRK10512  58 VPGHEKFLSN 67
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 3-89 6.24e-04

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 36.75  E-value: 6.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   3 NVVVIGHVDSGKSTttghLIYQCGGIdkrtiekfekeaaelgkgsfkyaWVlDKLKAERERGITI-----DIALWK---F 74
Cdd:PRK04000  11 NIGMVGHVDHGKTT----LVQALTGV-----------------------WT-DRHSEELKRGITIrlgyaDATIRKcpdC 62

                         90       100       110
                 ....*....|....*....|....*....|...
gi 667695992  75 ETPRYYVT------------------VIDAPGH 89
Cdd:PRK04000  63 EEPEAYTTepkcpncgsetellrrvsFVDAPGH 95
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 3-29 1.29e-03

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 35.73  E-value: 1.29e-03
                         10        20
                 ....*....|....*....|....*..
gi 667695992   3 NVVVIGHVDSGKSTTTGHLIyqCGGID 29
Cdd:cd04165    1 RVAVVGNVDAGKSTLLGVLT--QGELD 25
prfC PRK00741
peptide chain release factor 3; Provisional
 6-92 1.36e-03

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 35.88  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667695992   6 VIGHVDSGKSTTTGHLIYQCGGIdkrtiekfeKEAAEL-GKGSFKYA---WvldkLKAERERGITIDIALWKFETPRYYV 81
Cdd:PRK00741  15 IISHPDAGKTTLTEKLLLFGGAI---------QEAGTVkGRKSGRHAtsdW----MEMEKQRGISVTSSVMQFPYRDCLI 81

                         90
                 ....*....|.
gi 667695992  82 TVIDAPGHRDF 92
Cdd:PRK00741  82 NLLDTPGHEDF 92
 
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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