#=GF ID   HiaBD2
#=GF AC   PF15403.10
#=GF DE   HiaBD2_N domain of Trimeric autotransporter adhesin (GIN)
#=GF AU   Coggill P;0000-0001-5731-1588
#=GF SE   Jackhmmer:Q48152
#=GF GA   25.00 25.00;
#=GF TC   26.00 38.80;
#=GF NC   23.80 17.70;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch --cpu 4 -E 1000 -Z 75585367 HMM pfamseq
#=GF TP   Motif
#=GF WK   Trimeric_autotransporter_adhesin
#=GF RN   [1]
#=GF RM   18948113
#=GF RT   Repetitive architecture of the Haemophilus influenzae Hia
#=GF RT   trimeric autotransporter.
#=GF RA   Meng G, St Geme JW 3rd, Waksman G;
#=GF RL   J Mol Biol. 2008;384:824-836.
#=GF RN   [2]
#=GF RM   20862217
#=GF RT   Structure of a Burkholderia pseudomallei trimeric
#=GF RT   autotransporter adhesin head.
#=GF RA   Edwards TE, Phan I, Abendroth J, Dieterich SH, Masoudi A, Guo W,
#=GF RA   Hewitt SN, Kelley A, Leibly D, Brittnacher MJ, Staker BL, Miller
#=GF RA   SI, Van Voorhis WC, Myler PJ, Stewart LJ;
#=GF RL   PLoS One. 2010; [Epub ahead of print]
#=GF DR   INTERPRO; IPR029275;
#=GF DR   SO; 0001067; polypeptide_motif;
#=GF CC   HiaBD2_N may represent the GIN domain of the Head region of TAAs
#=GF CC   - trimeric autotransporter adhesins. Not all TAAs carry this
#=GF CC   domain; however, in those that do, the GIN in combination with
#=GF CC   the Trp-ring domain is necessary for adhesion to fibronectin in
#=GF CC   the host cell.
#=GF SQ   1
#=GS F9N556_9FIRM/23-67  AC F9N556.1
F9N556_9FIRM/23-67             g-NVTSGLQKYGDTVD---GKEV----PGSTKANNGLVDLSTPTDGSKPKVSD
#=GC seq_cons                  G.NVTSGLQKYGDTVD...GKEV....PGSTKANNGLVDLSTPTDGSKPKVSD
//