#=GF ID TAA-Trp-ring
#=GF AC PF15401.12
#=GF DE Tryptophan-ring motif of head of Trimeric autotransporter adhesin
#=GF AU Coggill P;0000-0001-5731-1588
#=GF SE Jackhmmer:Q48152
#=GF GA 25.80 17.30;
#=GF TC 26.60 17.50;
#=GF NC 25.40 17.00;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -E 1000 --cpu 8 -Z 90746521 HMM pfamseq
#=GF TP Domain
#=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 18397894
#=GF RT Domain annotation of trimeric autotransporter adhesins--daTAA.
#=GF RA Szczesny P, Lupas A;
#=GF RL Bioinformatics. 2008;24:1251-1256.
#=GF RN [3]
#=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 RN [4]
#=GF RM 21557062
#=GF RT Structure and biology of trimeric autotransporter adhesins.
#=GF RA Lyskowski A, Leo JC, Goldman A;
#=GF RL Adv Exp Med Biol. 2011;715:143-158.
#=GF DR INTERPRO; IPR028230;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC TAA-head_Trp-ring is the tryptophan-ring motif of some
#=GF CC Gram-negative Enterobacteriaceae. The Trp-ring folds into a
#=GF CC beta-meander type on the top of the head domain of its trimeric
#=GF CC autotransporter adhesin proteins. In conjunction with the GIN
#=GF CC domain it is thought to be the region of the head that adheres
#=GF CC to fibronectin.
#=GF SQ 11
#=GS F9N557_9FIRM/445-516 AC F9N557.1
#=GS NHHA_NEIMB/259-317 AC Q7DDJ2.1
#=GS A0A369ZTP5_9PAST/1276-1343 AC A0A369ZTP5.1
#=GS A0A378VLY9_NEILA/1555-1621 AC A0A378VLY9.1
#=GS A0A378VLY9_NEILA/2667-2746 AC A0A378VLY9.1
#=GS A0A378VLY9_NEILA/834-897 AC A0A378VLY9.1
#=GS A0A378VLY9_NEILA/454-504 AC A0A378VLY9.1
#=GS A0A378VKH7_NEILA/2966-3026 AC A0A378VKH7.1
#=GS A0A1V3J3Y5_9PAST/1631-1700 AC A0A1V3J3Y5.1
#=GS A0A378VKH7_NEILA/2071-2130 AC A0A378VKH7.1
#=GS A0A1V3J3Y5_9PAST/1899-1962 AC A0A1V3J3Y5.1
F9N557_9FIRM/445-516 ...........k-VTITNANGTKTD..AVKIGDN--YYKVDK----DGKPigfekgpdgkpagtpL---KVDPKTDKVT....NAGAGFVTGNTVANAI.....................
NHHA_NEIMB/259-317 ............VNVESKDNGKKTE..-VKIGAKTSVIKEKDGKLVTGKD...............------KGENGSST....DEGEGLVTAKEVIDAV.....................
A0A369ZTP5_9PAST/1276-1343 .....gdltaiv-------NGESTP..VTKVGDK--YYKTSDIDPKTGKPv............ddK---VSAVTPDKGTtpiaNAGDGYVTGNKVATAI.....................
A0A378VLY9_NEILA/1555-1621 ............VTVDSEDNGKTTK..-VKIGAKTSVIKEHNGKLLTGKQl.............kEANTGTATNTAEDA....DEGKGLVTAEAVINAV.....................
A0A378VLY9_NEILA/2667-2746 gevvksneftap-------DG--TS..LVKVDDK--YYSKDDIDTATGQPktgttek.yqtqngkIVSTNG-NTETTLT....NKGSGYVTGNQVADAI.....................
A0A378VLY9_NEILA/834-897 ............VVLKAKDNGKTTE..-VKFTPKTSVIKEKDGKLVTGQD...............-GKDNAKPDATNDN....DTGTGLVTAKAVIDAV.....................
A0A378VLY9_NEILA/454-504 ............VTVESKDNGKRTE..-VKIGVKTSVIAEKDGKLDTGT-...............-------------G....DEGKGLVTAKTVIDAV.....................
A0A378VKH7_NEILA/2966-3026 ...........k-VEITKNDGSKVH..AVIIDGK--YYERDE----NGKP..............kTDTEIPAADIKAAD....NGGSGFVTGNTVANAI.....................
A0A1V3J3Y5_9PAST/1631-1700 ......egtygd-------DN--KP..VVIVDGK--VYNKADIDPTTGKPfagkd.....pikdpT-DPTKDLRPDQVV....NNGKNFVTGNKVAQAI.....................
A0A378VKH7_NEILA/2071-2130 ............VTVVAKEGGKGAVvtITAKNDAGSITTA-GGKVVVG--...............-----TNGKASTDS....DAGNKVAKTGDVANAI.....................
A0A1V3J3Y5_9PAST/1899-1962 .....eagkmds---------QGNP..VVQVDGK--YYKPDDIDPNTGKPkdgav.....ptpddK-------------....----------------vversvvmkpttttvadgnia
#=GC seq_cons .............s..sptsGppTp..hVKlssK..hhcccDhc.sTGKs....................stspsspss....stGpGhVTuppVhsAl.....................
//