#=GF ID Dbr1_C
#=GF AC PF20890.1
#=GF DE Dbr1, C-terminal domain
#=GF AU Lazaro Pinto Beatriz;0000-0001-6837-2941
#=GF AU Bateman A;0000-0002-6982-4660
#=GF AU Chuguransky S;0000-0002-0520-0736
#=GF SE ECOD:6147.1.1
#=GF GA 27.00 27.00;
#=GF TC 27.80 196.80;
#=GF NC 26.40 21.30;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch --cpu 4 -Z 75585367 -E 1000 HMM pfamseq
#=GF TP Domain
#=GF RC Paper describing PDB structure 4pef
#=GF RN [1]
#=GF RM 25123664
#=GF RT Structural basis of lariat RNA recognition by the intron
#=GF RT debranching enzyme Dbr1.
#=GF RA Montemayor EJ, Katolik A, Clark NE, Taylor AB, Schuermann JP,
#=GF RA Combs DJ, Johnsson R, Holloway SP, Stevens SW, Damha MJ, Hart
#=GF RA PJ;
#=GF RL Nucleic Acids Res. 2014;42:10845-10855.
#=GF RC Paper describing PDB structure 5k77
#=GF RN [2]
#=GF RM 27930312
#=GF RT Metal dependence and branched RNA cocrystal structures of the
#=GF RT RNA lariat debranching enzyme Dbr1.
#=GF RA Clark NE, Katolik A, Roberts KM, Taylor AB, Holloway SP,
#=GF RA Schuermann JP, Montemayor EJ, Stevens SW, Fitzpatrick PF, Damha
#=GF RA MJ, Hart PJ;
#=GF RL Proc Natl Acad Sci U S A. 2016;113:14727-14732.
#=GF RC Paper describing PDB structure 5uki
#=GF RN [3]
#=GF RM 28504306
#=GF RT Crystal structure of the Entamoeba histolytica RNA lariat
#=GF RT debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+)
#=GF RT heterobinucleation.
#=GF RA Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR;
#=GF RL FEBS Lett. 2017;591:2003-2010.
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC Dbr1 is an eukaryotic intron debranching enzyme that hydrolyses
#=GF CC the linkages produced by the spliceosome in RNA for them to be
#=GF CC processed into essential cellular factors, such as snoRNA and
#=GF CC miRNA. This protein is organized into an N-terminal
#=GF CC metallophosphoesterase (MPE) domain (Pfam:PF00149) and a
#=GF CC C-terminal domain (CTD, this entry). This domain consists of
#=GF CC four alpha-helices and three connecting loops. It is located on
#=GF CC the posterior of the protein, opposite the active site and is
#=GF CC joined to the MPE domain by an extended linker region [1-3].
#=GF SQ 1
#=GS C4M1P9_ENTH1/268-353 AC C4M1P9.1
C4M1P9_ENTH1/268-353 DLEYDKDWVCNLIMTWPAFSNKAQFPDLSYSISELLSKRTKELDKKIIELWEKYIGLKIIYDSDTFDIQFTSRRFYIEKIYNELNI
#=GC seq_cons DLEYDKDWVCNLIMTWPAFSNKAQFPDLSYSISELLSKRTKELDKKIIELWEKYIGLKIIYDSDTFDIQFTSRRFYIEKIYNELNI
//
