#=GF ID   MA-Mit
#=GF AC   PF09245.14
#=GF DE   Mycoplasma arthritidis-derived mitogen
#=GF AU   Sammut SJ;0000-0003-4472-904X
#=GF SE   pdb_1r5i
#=GF GA   31.00 31.00;
#=GF TC   414.60 414.40;
#=GF NC   30.70 30.50;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 75585367 -E 1000 --cpu 4 HMM pfamseq
#=GF TP   Domain
#=GF RN   [1]
#=GF RM   14962388
#=GF RT   Crystal structure of Mycoplasma arthritidis mitogen complexed
#=GF RT   with HLA-DR1 reveals a novel superantigen fold and a dimerized
#=GF RT   superantigen-MHC complex. 
#=GF RA   Zhao Y, Li Z, Drozd SJ, Guo Y, Mourad W, Li H; 
#=GF RL   Structure. 2004;12:277-288.
#=GF DR   INTERPRO; IPR015326;
#=GF DR   SCOP; 1r5i; fa;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   Mycoplasma arthritidis-derived mitogen (MA-Mit) adopts a
#=GF CC   completely alpha-helical structure consisting of ten alpha
#=GF CC   helices. It is a superantigen that can activate large fractions
#=GF CC   of T cells bearing particular TCR V-beta elements. Two MA-Mit
#=GF CC   molecules form an asymmetric dimer and cross-link two MHC
#=GF CC   antigens to form a dimerised MA-Mit-MHC complex [1].
#=GF SQ   2
#=GS B3PN83_META1/25-238  AC B3PN83.1
#=GS B3PLU9_META1/25-237  AC B3PLU9.1
B3PN83_META1/25-238             SMKLRVPNPKRPNLPSLKAVKNEVVTLNELDKIIRLTNENDKTKEVIAQFRSKLNEFYQHAFNILEEYEGIEKHDDIFKMMFLKLKVVLDIQRKEPNNVEQIKRNINILDDIMKSADNELSYFVSQDLKFQALWDKAVLLSKTMKAEFKTSRPSTVDPYGPVNSVEKFFGADEDVKTIKWFKSLLIRAANYLIHYYDAPEVFQPKTDFEKAIFE
B3PLU9_META1/25-237             SMKLRVENPKKAQKHFVQNLNNVVFTNKELEDIYNLSNK-EETKEVLKLFKLKVNQFYRHAFGIVNDYNGLLEYKEIFNMMFLKLSVVFDTQRKEANNVEQIKRNIAILDEIMAKADNDLSYFISQNKNFQELWDKAVKLTKEMKIKLKGQKLDLRDGEVAINKVRELFGSDKNVKELWWFRSLLVKGVYLIKRYYEGDIELKTTSDFAKAVFE
#=GC seq_cons                   SMKLRV.NPK+sph..lpslpN.VhT.pEL-cIhpLoNc.-cTKEVlt.F+.KlNpFYpHAFsIlp-YpGl.cac-IFpMMFLKLpVVhDhQRKEsNNVEQIKRNIsILD-IMtpADN-LSYFlSQshpFQtLWDKAVhLoKpMKhchKsp+.shhDs.sslNpVcchFGuDcsVKplhWF+SLLl+us.hlh+YY-us..hpspoDFtKAlFE
//