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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 567848678   1 KEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP 40
Cdd:PTZ00141  44 KEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETP 83

elongation factor 1- alpha; Provisional

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 567848678   1 KEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP 40
Cdd:PTZ00141  44 KEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETP 83

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 567848678   1 KEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP 40
Cdd:COG5256   44 EEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETD 83

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]

                          10        20        30
                  ....*....|....*....|....*....|..
gi 567848678    9 GSFKYAWVLDKLKAERERGITIDIALWKFETP 40
Cdd:TIGR02034  47 GEIDLALLVDGLQAEREQGITIDVAYRYFSTD 78

elongation factor 1- alpha; Provisional

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 567848678   1 KEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP 40
Cdd:PTZ00141  44 KEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETP 83

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 567848678   1 KEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP 40
Cdd:COG5256   44 EEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETD 83

elongation factor 1-alpha; Provisional

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 567848678   1 KEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFET 39
Cdd:PLN00043  44 KEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFET 82

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

                         10        20        30
                 ....*....|....*....|....*....|....
gi 567848678   7 GKGSFKYAWVLDKLKAERERGITIDIALWKFETP 40
Cdd:COG2895   60 GTQEIDLALLTDGLQAEREQGITIDVAYRYFSTP 93

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.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 567848678   7 GKGSFKYAWVLDKLKAERERGITIDIALWKFETP 40
Cdd:cd04166   43 QGEKLDLALLVDGLQAEREQGITIDVAYRYFSTP 76

sulfate adenylyltransferase subunit 1; Provisional

                         10        20
                 ....*....|....*....|....*..
gi 567848678  13 YAWVLDKLKAERERGITIDIALWKFET 39
Cdd:PRK05124  78 LALLVDGLQAEREQGITIDVAYRYFST 104

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.

                         10
                 ....*....|....*
gi 567848678  16 VLDKLKAERERGITI 30
Cdd:cd01890   36 VLDSMDLERERGITI 50

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

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 567848678   4 AELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP 40
Cdd:COG0050   37 AKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETE 73

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

                         10
                 ....*....|....*
gi 567848678  16 VLDKLKAERERGITI 30
Cdd:COG0481   42 VLDSMDLERERGITI 56

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.

                         10        20
                 ....*....|....*....|....
gi 567848678  17 LDKLKAERERGITIDIALWKFETP 40
Cdd:cd01889   29 FDKNPQSQERGITLDLGFSSFEVD 52