# STOCKHOLM 1.0
#=GF ID   DDAH_eukar
#=GF AC   PF19420.2
#=GF DE   N,N dimethylarginine dimethylhydrolase, eukaryotic
#=GF AU   Mian N;0000-0003-4284-4749
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF AU   Chuguransky S;0000-0002-0520-0736
#=GF SE   Pfam-B_5784 (release 5.2) and Pfam-B_1850 (release 5.5)
#=GF GA   23.00 23.00;
#=GF TC   23.00 23.00;
#=GF NC   22.90 22.90;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
#=GF TP   Family
#=GF CL   CL0197
#=GF RN   [1]
#=GF RM   11504612
#=GF RT   A novel superfamily of enzymes that catalyze the modification of
#=GF RT   guanidino groups. 
#=GF RA   Shirai H, Blundell TL, Mizuguchi K; 
#=GF RL   Trends Biochem Sci 2001;26:465-468.
#=GF RN   [2]
#=GF RM   14675764
#=GF RT   Prediction of the structure and function of AstA and AstB, the
#=GF RT   first two enzymes of the arginine succinyltransferase pathway of
#=GF RT   arginine catabolism. 
#=GF RA   Shirai H, Mizuguchi K; 
#=GF RL   FEBS Lett 2003;555:505-510.
#=GF DR   SCOP; 1jdw; fa;
#=GF DR   SO; 0100021; polypeptide_conserved_region;
#=GF CC   This family contains N(G),N(G)-dimethylarginine
#=GF CC   dimethylaminohydrolases (DDAH) from eukaryotes. It also includes
#=GF CC   arginine deiminases and DDAH from prokaryotes. These enzymes are
#=GF CC   involved in arginine metabolism and belong to the
#=GF CC   amidinotransferase (AT) superfamily as they share the alpha/beta
#=GF CC   propeller fold, which includes structurally important residues
#=GF CC   (buried hydrophobic residues, buried hydrophilic residues
#=GF CC   hydrogen-bonded with mainchain groups and the hallmark of three
#=GF CC   consecutive buried Gly residues near the C-terminus, conserved
#=GF CC   among its members [1,2].
#=GF SQ   12755
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