#=GF ID   efb-c
#=GF AC   PF12199.11
#=GF DE   Extracellular fibrinogen binding protein C terminal
#=GF AU   Mistry J;0000-0003-2479-5322
#=GF AU   Gavin OL;
#=GF SE   pdb_2gox
#=GF GA   27.00 27.00;
#=GF TC   33.20 129.80;
#=GF NC   23.00 20.70;
#=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   17351618
#=GF RT   A structural basis for complement inhibition by Staphylococcus
#=GF RT   aureus.
#=GF RA   Hammel M, Sfyroera G, Ricklin D, Magotti P, Lambris JD,
#=GF RA   Geisbrecht BV;
#=GF RL   Nat Immunol. 2007;8:430-437.
#=GF DR   INTERPRO; IPR021033;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   This domain family is found in bacteria, and is approximately 70
#=GF CC   amino acids in length. There is a conserved VLK sequence motif.
#=GF CC   It is the C terminal domain of bacterial extracellular
#=GF CC   fibrinogen binding protein. It contains a helical motif involved
#=GF CC   in complement regulation. This motif binds to complement and
#=GF CC   changes its conformation to a form which cannot activate
#=GF CC   downstream components of the complement cascade.
#=GF SQ   2
#=GS Q2FZB8_STAA8/101-165  AC Q2FZB8.1
#=GS Q2FZC2_STAA8/45-109   AC Q2FZC2.1
Q2FZB8_STAA8/101-165             TDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVK
Q2FZC2_STAA8/45-109              TNFKKQVNKKVVDAQKAVNFFKRTRTVATHRKAQRAVNLIHFQHSYEKKKLQRQIDLVLKYNTLK
#=GC seq_cons                    TshphphppKllpAQphVp.Fc+T+TVusHRKAQ+AVNLlpFpaphcKhhLQcpID.VLK.shlK
//