#=GF ID   DUF1923
#=GF AC   PF09083.14
#=GF DE   Domain of unknown function (DUF1923)
#=GF AU   Sammut SJ;0000-0003-4472-904X
#=GF SE   pdb_1gjw
#=GF GA   25.00 25.00;
#=GF TC   25.70 156.10;
#=GF NC   23.80 20.90;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 -Z 75585367 --cpu 4 HMM pfamseq
#=GF TP   Domain
#=GF WK   Domain_of_unknown_function
#=GF CL   CL0369
#=GF RN   [1]
#=GF RM   11545590
#=GF RT   The crystal structure of Thermotoga maritima maltosyltransferase
#=GF RT   and its implications for the molecular basis of the novel
#=GF RT   transfer specificity. 
#=GF RA   Roujeinikova A, Raasch C, Burke J, Baker PJ, Liebl W, Rice DW; 
#=GF RL   J Mol Biol. 2001;312:119-131.
#=GF DR   INTERPRO; IPR015167;
#=GF DR   SCOP; 1gjw; fa;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   Members of this family are found in maltosyltransferases, and
#=GF CC   adopt a secondary structure consisting of eight antiparallel
#=GF CC   beta-strands, which form an open-sided 'jelly roll' Greek key
#=GF CC   beta-barrel. Their exact function is, as yet, unknown [1].
#=GF SQ   1
#=GS Q9S5X2_THEMA/575-638  AC Q9S5X2.1
Q9S5X2_THEMA/575-638             GKFENLTTKDLVMYSYEKNGQKIVIAANVGKEPKEITGGRVWNGKWSDEEKVVLKPLEFALVVQ
#=GC seq_cons                    GKFENLTTKDLVMYSYEKNGQKIVIAANVGKEPKEITGGRVWNGKWSDEEKVVLKPLEFALVVQ
//