SMART: Pfam domain TsaE

TsaE

PFAM accession number:	PF02367
Interpro abstract (IPR003442):	Members of this family have a conserved nucleotide-binding motif GXXGXGKT and a nucleotide-binding fold. Member protein YjeE of Haemophilus influenzae (HI0065) was shown to have ATPase activity [ (PUBMED:12112691) (PUBMED:17581233) ]. The protein has a nucleotide-binding fold with a four-stranded parallel beta-sheet flanked by antiparallel beta-strands on each side. The topology of the beta-sheet is unique among P-loop proteins and has features of different families of enzymes. ADP has been shown to bind to the P-loop in the presence of Mg2+. Recently YjeE has been renamed as TsaE [ (PUBMED:22378793) ]. It is responsible for tRNA threonylcarbamoyl adenosine modification together with proteins TsaB, TsaC, and TsaD, and probably forms a complex with them [ (PUBMED:22378793) (PUBMED:23072323) ].
GO process:	tRNA threonylcarbamoyladenosine modification (GO:0002949)

PFAM accession number:

PF02367

Interpro abstract (IPR003442):

Members of this family have a conserved nucleotide-binding motif GXXGXGKT and a nucleotide-binding fold. Member protein YjeE of Haemophilus influenzae (HI0065) was shown to have ATPase activity [ (PUBMED:12112691) (PUBMED:17581233) ]. The protein has a nucleotide-binding fold with a four-stranded parallel beta-sheet flanked by antiparallel beta-strands on each side. The topology of the beta-sheet is unique among P-loop proteins and has features of different families of enzymes. ADP has been shown to bind to the P-loop in the presence of Mg2+.

Recently YjeE has been renamed as TsaE [ (PUBMED:22378793) ]. It is responsible for tRNA threonylcarbamoyl adenosine modification together with proteins TsaB, TsaC, and TsaD, and probably forms a complex with them [ (PUBMED:22378793) (PUBMED:23072323) ].

GO process:

tRNA threonylcarbamoyladenosine modification (GO:0002949)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry TsaE