# STOCKHOLM 1.0
#=GF ID pAdhesive_17
#=GF AC PF20609.1
#=GF DE Putative adhesive domain (group 17)
#=GF AU Bateman A;0000-0002-6982-4660
#=GF GA 27.0 27.0
#=GF NC 24.7 23.9
#=GF TC 39.2 38.8
#=GF SE Monzon V
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 19856273
#=GF RT Surface protein EF3314 contributes to virulence properties of
#=GF RT Enterococcus faecalis.
#=GF RA Creti R, Fabretti F, Koch S, Huebner J, Garsin DA, Baldassarri
#=GF RA L, Montanaro L, Arciola CR;
#=GF RL Int J Artif Organs. 2009;32:611-620.
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC The structure model of this domain folds into 10 beta strands 
#=GF CC arranged in two beta sheets as well as 4-5 elongated alpha
#=GF CC helices.  The beta sheets distantly resemble the Collagen_bind
#=GF CC (Pfam:PF05737)  domain. It is annotated N-terminal to repeating
#=GF CC stalk domains in  bacterial surface proteins. This domain can be
#=GF CC found on a  E. faecalis protein encoded by the EF3314 gene,
#=GF CC which was  proposed to contribute to the interaction of E.
#=GF CC faecalis  with the host and to the bacterial virulence [1].
#=GF SQ 2
A0A5R8QDZ6.1/34-322 SATDIILWSDTTLSSDKPVISETGTHDINFTLSAFTKDELRLLVQS-KTASFKIPEELVGKIEANGDAQIEIT--...YELAKALFEELGInnlvstidNGVDKLAAFLAE-----SELFGYNVNFDDIYAALDLKTIWDNISVLSLNAPVTVSEDGAYLSVTFEDNAFDKIAEVLRDIINNIGTALDTFEIT-NPGVMGGIISSIAMSMWdvvVDAYDLLAAPILHSLVDGADLIASIGDFRTKFTTKVILPTTLTAEYdffkTYAPHGLTVEVDGTFTTPALIPIELWTDRHDTTTITF
A0A5R8QIW4.1/67-240 -------------------------------------------FTGTKTISIPIPAELLPAAALIGDAKLEITYElaqVLLQNL-GINNLI........RTVDNAASKIMEFLNES-ELLGFNVNFDEVYAALDVQNFWESMPTALINSPITLSTDGVNVNVTFEETAFANIMVLVEAALANISNAIHAVQLTGQ-GVVGTFIARTVMDLW...-VVVEDVYDLFAQTVSDI----------------------------....-------------------------------------
//