#=GF ID AvrM_N
#=GF AC PF18247.2
#=GF DE Flax-rust effector AvrM N-terminal domain
#=GF AU Smart A;0000-0002-6965-5633
#=GF SE ECOD:EUF03970
#=GF GA 25.00 25.00;
#=GF TC 28.00 57.10;
#=GF NC 23.00 24.20;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 24101475
#=GF RT Structures of the flax-rust effector AvrM reveal insights into
#=GF RT the molecular basis of plant-cell entry and effector-triggered
#=GF RT immunity.
#=GF RA Ve T, Williams SJ, Catanzariti AM, Rafiqi M, Rahman M, Ellis JG,
#=GF RA Hardham AR, Jones DA, Anderson PA, Dodds PN, Kobe B;
#=GF RL Proc Natl Acad Sci U S A. 2013;110:17594-17599.
#=GF DR INTERPRO; IPR041353;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC This is the N-terminal domain found in AvrM present in
#=GF CC Melampsora lini. AvrM is a secreted effector protein that can
#=GF CC internalize into plant cells in the absence of pathogens, binds
#=GF CC to phosphoinositides and results in effector-triggered immunity.
#=GF CC This domain is related to the WY domain core in oomycete
#=GF CC effectors [1].
#=GF SQ 6
#=GS F4RW29_MELLP/135-192 AC F4RW29.1
#=GS F4R586_MELLP/207-271 AC F4R586.1
#=GS F4RW28_MELLP/131-193 AC F4RW28.1
#=GS F4S8Q3_MELLP/220-284 AC F4S8Q3.1
#=GS F4S6E1_MELLP/159-223 AC F4S6E1.1
#=GS F4RGY5_MELLP/230-294 AC F4RGY5.1
F4RW29_MELLP/135-192 qhvvtp-------------QKLEFLNPAQVRELSHDDLIKYVAERDAVAANEAKNLYQRAQEYTQAEQNAF
F4R586_MELLP/207-271 ......DEAFKNQNGMVLKGQMEDIKPVEVAKLSPDRLIRYAADRNDNVEGMARNLYKASEKYIKDEQRAF
F4RW28_MELLP/131-193 ......DPIFKSH--KLFDWNVKFLKPSQLKYLSTDETIRYVAERDTILSKEVMKLYKIGKEYERAEENAF
F4S8Q3_MELLP/220-284 ......PPIFAKGLGKAFRIDFKYLKPAEVQKLPPYELLRYISERDVNVRKNTRKLDDLARNYYSAQKDAF
F4S6E1_MELLP/159-223 ......EPVFERAHIKPYGETMEFLNRDHVEKLSNDALIRYMAEKDTQIQKMAIDFQEAAQAHKEAEAKAF
F4RGY5_MELLP/230-294 ......DEAFKNQNIMLFRGQMEDIKPVEVAKLSPDRLIRYAADRNEDVEGMARNLYKASEKYTQAEQKAF
#=GC seq_cons ......-.hFcpt.hhhactphEaLKPscVpKLSsDcLIRYsAERDsslpp.A+sLYctuccYppAEpcAF
//
