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        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 149054420 130 RNVTLCGHLHHGKTCFVDCLIEQTHPEI--RKRYDQDLCYTDILFTEQER 177
Cdd:cd04167    1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTpsVKLGWKPLRYTDTRKDEQER 50

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 149054420 130 RNVTLCGHLHHGKTCFVDCLIEQTHPEI--RKRYDQDLCYTDILFTEQER 177
Cdd:cd04167    1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTpsVKLGWKPLRYTDTRKDEQER 50

elongation factor EF-2; Reviewed

                         10        20        30
                 ....*....|....*....|....*....|
gi 149054420 121 DLMDNSELIRNVTLCGHLHHGKTCFVDCLI 150
Cdd:PRK07560  12 ELMKNPEQIRNIGIIAHIDHGKTTLSDNLL 41

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 149054420 130 RNVTLCGHLHHGKTCFVDCLIEQTHPEI--RKRYDQDLCYTDILFTEQER 177
Cdd:cd04167    1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTpsVKLGWKPLRYTDTRKDEQER 50

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 149054420  127 ELIRNVTLCGHLHHGKTCFVDCLIEQTHP--EIRKRYDQDLCYTDILFTEQER 177
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAisKRGEVKGEGEAGLDNLPEERER 53

elongation factor 2; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 149054420 122 LMDNSELIRNVTLCGHLHHGKTCFVDCLIEQTHPeIRKRYDQDLCYTDILFTEQER 177
Cdd:PTZ00416  12 IMDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGI-ISSKNAGDARFTDTRADEQER 66

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.

                         10        20
                 ....*....|....*....|....*.
gi 149054420 129 IRNVTLCGHLHHGKTCFVDCLIEQTH 154
Cdd:cd01891    2 IRNIAIIAHVDHGKTTLVDALLKQSG 27