#=GF ID PA_Ig-like
#=GF AC PF20835.1
#=GF DE Anthrax protective antigen, immunoglobulin-like 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:5099.1.1
#=GF GA 27.00 27.00;
#=GF TC 27.50 28.50;
#=GF NC 26.50 23.90;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 75585367 -E 1000 --cpu 4 HMM pfamseq
#=GF TP Domain
#=GF WK Immunoglobulin_domain
#=GF RC Paper describing PDB structure 1acc
#=GF RN [1]
#=GF RM 9039918
#=GF RT Crystal structure of the anthrax toxin protective antigen.
#=GF RA Petosa C, Collier RJ, Klimpel KR, Leppla SH, Liddington RC;
#=GF RL Nature. 1997;385:833-838.
#=GF RC Paper describing PDB structure 1t6b
#=GF RN [2]
#=GF RM 15243628
#=GF RT Crystal structure of a complex between anthrax toxin and its
#=GF RT host cell receptor.
#=GF RA Santelli E, Bankston LA, Leppla SH, Liddington RC;
#=GF RL Nature. 2004;430:905-908.
#=GF RC Paper describing PDB structure 1tzn
#=GF RN [3]
#=GF RM 15326297
#=GF RT Structure of heptameric protective antigen bound to an anthrax
#=GF RT toxin receptor: a role for receptor in pH-dependent pore
#=GF RT formation.
#=GF RA Lacy DB, Wigelsworth DJ, Melnyk RA, Harrison SC, Collier RJ;
#=GF RL Proc Natl Acad Sci U S A. 2004;101:13147-13151.
#=GF RC Paper describing PDB structure 3etb
#=GF RN [4]
#=GF RM 19361425
#=GF RT Crystal structure of the engineered neutralizing antibody M18
#=GF RT complexed to domain 4 of the anthrax protective antigen.
#=GF RA Leysath CE, Monzingo AF, Maynard JA, Barnett J, Georgiou G,
#=GF RA Iverson BL, Robertus JD;
#=GF RL J Mol Biol. 2009;387:680-693.
#=GF RC Paper describing PDB structure 3hvd
#=GF RN [5]
#=GF RM 19627991
#=GF RT The protective antigen component of anthrax toxin forms
#=GF RT functional octameric complexes.
#=GF RA Kintzer AF, Thoren KL, Sterling HJ, Dong KC, Feld GK, Tang II,
#=GF RA Zhang TT, Williams ER, Berger JM, Krantz BA;
#=GF RL J Mol Biol. 2009;392:614-629.
#=GF RN [6]
#=GF RM 19722284
#=GF RT Domain 4 of the anthrax protective antigen maintains structure
#=GF RT and binding to the host receptor CMG2 at low pH.
#=GF RA Williams AS, Lovell S, Anbanandam A, El-Chami R, Bann JG;
#=GF RL Protein Sci. 2009;18:2277-2286.
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC Anthrax protective antigen (PA) is one of the three proteins
#=GF CC forming the anthrax toxin. It is involved in the first step of
#=GF CC toxin entry into host cells, enabling lethal factor (LF) and
#=GF CC oedema factor (EF) to cross to the cytosol. PA undergoes
#=GF CC cleavage by Furin to generate PA20 and PA63. The latter, which
#=GF CC adopts a ring-shaped heptameric assembly, shows four distinct
#=GF CC domains. The fourth domain, a carboxy- terminal receptor-binding
#=GF CC domain, shows an initial hairpin and helix, followed by a
#=GF CC beta-sandwich with an immunoglobulin-like fold (this entry)
#=GF CC [1-5].
#=GF SQ 3
#=GS A0A022QB08_ERYGU/10-112 AC A0A022QB08.1
#=GS Y6163_BACAN/28-174 AC P13422.3
#=GS PAG_BACAN/623-763 AC P13423.2
A0A022QB08_ERYGU/10-112 vfdkdgdgcinieelgivmrsldqnpse----------------------------------------------------------------------------KELRDMIN--EVDSDGNGTIDFDEF---LNLMT--AKEKMQVYNELKEAFKVFDKDQNGYISANELRQTMIN-------lgekltveev
Y6163_BACAN/28-174 ............................DPYHYDNNGNIVGVDDSYLKNAYKQILNWSSDGVSLNLDEDVNQALSGYMLQIKKPSNHLTNSPVTITLAGKDSGVGELYRVLS------DGTGFLDFNKFDENWRSLV-DPGDDVYVYAVTKEDFNAVTRDENGNIA-NKLKNTLVLSGKIKEI..........
PAG_BACAN/623-763 ............................KRFHYDRNNIAVGADESVVKEAHREVINSSTEGLLLNIDKDIRKILSGYIVEIEDTE-------------GLKEVINDRYDMLNISSLRQDGKTFIDFKKYNDKLPLYISNPNYKVNVYAVTKEN-TIINPSENGDTSTNGIKKILIFSKKGYEI..........
#=GC seq_cons ............................c.aHYDpNs.hVGsD-ShlKpAa+pllN.So-Gl.LNlDcDlpphLSGYhlpIccsp.............GhcpslsELYDMLN..plcpDGsGFIDFcKFs-pLsLhl.sPs-KVpVYAVTKEsFslls+DENGsISsNcLKpTLIhStKhhEI..........
//
