The domain within your query sequence starts at position 64 and ends at position 221; the E-value for the SKI domain shown below is 5.8e-40.

PGSGKTTVGRILGDKLGCCVIDVDSDVLEKAWNMSASEKLQDVGNERFLEEEGKTVLNLS
ASGSVISLSGSNPMHDASMWHLKKNGIVVYLDVPLTDIISRLKSMRIDRIVGQNTGASLR
DSLKHVRLYYKKWYDARVFCESGASAEEVADKVLDVVK

SKI

SKI
PFAM accession number:PF01202
Interpro abstract (IPR031322):

Shikimate kinase (EC 2.7.1.71) catalyses the fifth step in the biosynthesis of aromatic amino acids from chorismate (the so-called shikimate pathway) [(PUBMED:7612934)]. The enzyme catalyses the following reaction:

ATP + shikimate = ADP + shikimate-3-phosphate

The protein is found in bacteria (gene aroK or aroL), plants and fungi (where it is part of a multifunctional enzyme that catalyses five consecutive steps in this pathway). In 1994, the 3D structure of shikimate kinase was predicted to be very close to that of adenylate kinase, suggesting a functional similarity as well as an evolutionary relationship [(PUBMED:7703851)]. This prediction has since been confirmed experimentally. The protein is reported to possess an alpha/beta fold, consisting of a central sheet of five parallel beta-strands flanked by alpha-helices. Such a topology is very similar to that of adenylate kinase [(PUBMED:9600856)].

The N terminus of threonine synthase-like 1 from metazoan shares protein sequence similarity with shikimate kinase and is included in this entry. However, their functions may be different.

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