#=GF ID   AvrRps4_C
#=GF AC   PF21611.1
#=GF DE   Avirulence protein, C-terminal domain
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF AU   Lazaro Pinto Beatriz;0000-0001-6837-2941
#=GF SE   ECOD:EF19550
#=GF GA   27.00 27.00;
#=GF TC   29.10 147.00;
#=GF NC   23.50 22.40;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 75585367 --cpu 4 -E 1000 HMM pfamseq
#=GF TP   Domain
#=GF RC   Paper describing PDB structure 4b6x
#=GF RN   [1]
#=GF RM   22988101
#=GF RT   Distinct regions of the Pseudomonas syringae coiled-coil
#=GF RT   effector AvrRps4 are required for activation of immunity.
#=GF RA   Sohn KH, Hughes RK, Piquerez SJ, Jones JD, Banfield MJ;
#=GF RL   Proc Natl Acad Sci U S A. 2012;109:16371-16376.
#=GF RC   Paper describing PDB structure 7p8k
#=GF RN   [2]
#=GF RM   34880132
#=GF RT   Perception of structurally distinct effectors by the integrated
#=GF RT   WRKY domain of a  plant immune receptor.
#=GF RA   Mukhi N, Brown H, Gorenkin D, Ding P, Bentham AR, Stevenson CEM,
#=GF RA   Jones JDG, Banfield MJ;
#=GF RL   Proc Natl Acad Sci U S A. 2021; [Epub ahead of print]
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   This domain is found in the C-terminal region of Avirulence
#=GF CC   protein from Pseudomonas syringae (AvrRps4) and in similar
#=GF CC   sequences from plant pathogenic bacteria. AvrRps4 is a type III
#=GF CC   secretion system effector protein that triggers immunity in
#=GF CC   resistant accessions of Arabidopsis. This domain folds into an
#=GF CC   antiparallel alpha-helical coiled coil structure [1,2].
#=GF SQ   1
#=GS A1TL15_ACIAC/160-222  AC A1TL15.1
A1TL15_ACIAC/160-222             QLREAIQDKQLMIQTLTQELAQAEEEGNPAEIAQNQRLLAQARQDLAGYMRQAAVYGEESRRI
#=GC seq_cons                    QLREAIQDKQLMIQTLTQELAQAEEEGNPAEIAQNQRLLAQARQDLAGYMRQAAVYGEESRRI
//