#=GF ID   ID
#=GF AC   PF18543.5
#=GF DE   Intracellular delivery domain
#=GF AU   El-Gebali S;0000-0003-1378-5495
#=GF SE   ECOD:EUF06372
#=GF GA   31.40 31.40;
#=GF TC   32.20 33.90;
#=GF NC   30.60 18.30;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 75585367 --cpu 4 -E 1000 HMM pfamseq
#=GF TP   Domain
#=GF CL   CL0021
#=GF RN   [1]
#=GF RM   21213248
#=GF RT   Fic domain-catalyzed adenylylation: insight provided by the
#=GF RT   structural analysis of the type IV secretion system effector
#=GF RT   BepA.
#=GF RA   Palanivelu DV, Goepfert A, Meury M, Guye P, Dehio C, Schirmer T;
#=GF RL   Protein Sci. 2011;20:492-499.
#=GF DR   INTERPRO; IPR040548;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   This is a C-terminal domain found in BepA proteins from
#=GF CC   Bartonella henselae. It is a type IV secretion system (T4SS)
#=GF CC   effector protein. BepA from Bartonella henselae is composed of
#=GF CC   an N-terminal Fic domain and a C-terminal Bartonella
#=GF CC   intracellular delivery (ID) domain, the latter being responsible
#=GF CC   for T4SS-mediated translocation into host cells. The ID domain
#=GF CC   of BepA mediates inhibition of apoptosis and exhibits an OB
#=GF CC   (oligonucleotide/oligosaccharide binding)-fold [1].
#=GF SQ   14
#=GS A0A1S6XHJ4_9HYPH/329-387  AC A0A1S6XHJ4.1
#=GS A0A1S6XJJ5_9HYPH/256-309  AC A0A1S6XJJ5.1
#=GS A0A1S6XFY0_9HYPH/218-270  AC A0A1S6XFY0.1
#=GS A0A1S6XGV0_9HYPH/236-288  AC A0A1S6XGV0.1
#=GS A0A1S6XGX4_9HYPH/244-296  AC A0A1S6XGX4.1
#=GS A0A1S6XIN6_9HYPH/252-304  AC A0A1S6XIN6.1
#=GS A0A1S6XHG7_9HYPH/1-32     AC A0A1S6XHG7.1
#=GS A0A1S6XGW8_9HYPH/253-305  AC A0A1S6XGW8.1
#=GS A0A1S6XG85_9HYPH/272-324  AC A0A1S6XG85.1
#=GS A0A1S6XGZ0_9HYPH/268-320  AC A0A1S6XGZ0.1
#=GS A0A1S6XFZ8_9HYPH/365-417  AC A0A1S6XFZ8.1
#=GS A0A1S6XH13_9HYPH/244-296  AC A0A1S6XH13.1
#=GS A0A1S6XI27_9HYPH/249-302  AC A0A1S6XI27.1
#=GS A0A1S6XHK1_9HYPH/389-441  AC A0A1S6XHK1.1
A0A1S6XHJ4_9HYPH/329-387             ..l-APNKDEIYTGIYESDSPDSILLKIDRN.YiekplyMVFKKDYLSPEQLKALKVGDEFSF..
A0A1S6XJJ5_9HYPH/256-309             ...VAADKGFTYTGTYKGDSPDSIILKTGDNiY......SIFSKDNCTPEQLKVLKIGDDC--il
A0A1S6XFY0_9HYPH/218-270             ...VMPNEGETYTGIYKGCSLDSIMLMVKGS.Y......VLCQKDYLSPATVKALRLDDKFTF..
A0A1S6XGV0_9HYPH/236-288             ...IISRKGITYEGLYKKSGLDAVMIETKDF.C......VICHKDYLTPEQLKALKPGSELTV..
A0A1S6XGX4_9HYPH/244-296             ...VIPREGISYTGIYRGASVDSIIVETADS.C......VICHKDYLTPEQIKALKPGNELSF..
A0A1S6XIN6_9HYPH/252-304             ttp---IPGKSYTGVFENRKLDTIVIRTADS.L......VVCNRHVIPRDKLRNAKIGDKITF..
A0A1S6XHG7_9HYPH/1-32                ...---------------------MIKTTDF.C......VICYKDYFTPEQLRSLKFGDKITF..
A0A1S6XGW8_9HYPH/253-305             ...IMPQNDIIYTGRYKESSPDSIIIVTKDS.Y......VVYCKDYLAPEELKALKVGESVTF..
A0A1S6XG85_9HYPH/272-324             ...VMPNEGETYTGIYKGCSLDSIMLMVKGS.Y......VLCQKDYLSPATVKALRLDDKFTF..
A0A1S6XGZ0_9HYPH/268-320             ...VAPNEGDTYTGTYEADSPNSIMIKTTDF.C......VICYKDYFTPEQLRALKFGDKITF..
A0A1S6XFZ8_9HYPH/365-417             ...ILPTEGSTYTGIYKDCSPDSIRLMVKDN.Y......FICKKDYFAPETLKTLLPGQKLIF..
A0A1S6XH13_9HYPH/244-296             ...IMPREGISYTGIYRGASVDSIIVETADS.C......VICHKDYLTPEQIKALKPGNELSF..
A0A1S6XI27_9HYPH/249-302             ..m-APKEDVVYTGRCKDFSLDCVVIEIQQGiC......IVCNKDHLTPEQLRTLKLNDELTF..
A0A1S6XHK1_9HYPH/389-441             ...IIPRDNIVYTGTYKGSTGNAIMIDTKDS.C......VVCPKDRLTPKQLKELKIGGEFTF..
#=GC seq_cons                        ...lhPpcG.oYTGhY+ssS.DSIhlcTpDs.h......VlCpKDYLoPEQLKuLKhG-clTF..
//