#=GF ID efb-c
#=GF AC PF12199.13
#=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 25.40 22.60;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 81514348 --cpu 4 -E 1000 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
//