SMART: Pfam domain DS

The domain within your query sequence starts at position 59 and ends at position 142; the E-value for the DS domain shown below is 1.1e-23.

YHALLDAYRTTGFQATNFGRAVQQVNAMIEKKLEPLAVDEDHHADLTQSRRPLTGCTIFL
GYTSNLISSGIRETIRYLVQHNMD

DS

PFAM accession number:	PF01916
Interpro abstract (IPR002773):	Eukaryotic initiation factor 5A (eIF-5A), now considered to be an elongation factor (see IPR001884 ), contains an unusual amino acid, hypusine [N epsilon-(4-aminobutyl-2-hydroxy)lysine]. The first step in the post-translational formation of hypusine is catalysed by the enzyme deoxyhypusine synthase (DS, EC 2.5.1.46 ). The enzyme catalyses the following reaction: Spermidine + [eIF-5A]-lysine = 1,3-diaminopropane + [eIF-5A]-deoxyhypusine The modified version of eIF-5A, and DS, are required for eukaryotic cell proliferation [ (PUBMED:9493264) ]. The structure is known for this enzyme [ (PUBMED:9493264) ] in complex with its NAD ⁺ cofactor.
GO process:	peptidyl-lysine modification to peptidyl-hypusine (GO:0008612)

PFAM accession number:

PF01916

Interpro abstract (IPR002773):

Eukaryotic initiation factor 5A (eIF-5A), now considered to be an elongation factor (see IPR001884 ), contains an unusual amino acid, hypusine [N epsilon-(4-aminobutyl-2-hydroxy)lysine]. The first step in the post-translational formation of hypusine is catalysed by the enzyme deoxyhypusine synthase (DS, EC 2.5.1.46 ). The enzyme catalyses the following reaction:

Spermidine + [eIF-5A]-lysine = 1,3-diaminopropane + [eIF-5A]-deoxyhypusine

The modified version of eIF-5A, and DS, are required for eukaryotic cell proliferation [ (PUBMED:9493264) ]. The structure is known for this enzyme [ (PUBMED:9493264) ] in complex with its NAD ⁺ cofactor.

GO process:

peptidyl-lysine modification to peptidyl-hypusine (GO:0008612)

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