#=GF ID   Anophelin
#=GF AC   PF10731.13
#=GF DE   Thrombin inhibitor from mosquito
#=GF AU   Coggill P;0000-0001-5731-1588
#=GF SE   Rawlings N
#=GF GA   25.00 25.00;
#=GF TC   77.50 77.50;
#=GF NC   22.50 21.60;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 --cpu 4 -Z 75585367 HMM pfamseq
#=GF TP   Family
#=GF RN   [1]
#=GF RM   10460178
#=GF RT   Purification, cloning, and synthesis of a novel salivary
#=GF RT   anti-thrombin from the mosquito Anopheles albimanus. 
#=GF RA   Valenzuela JG, Francischetti IM, Ribeiro JM; 
#=GF RL   Biochemistry. 1999;38:11209-11215.
#=GF DR   INTERPRO; IPR018932;
#=GF DR   MEROPS; I77;
#=GF DR   SO; 0100021; polypeptide_conserved_region;
#=GF CC   Members of this family are all inhibitors of thrombin, the
#=GF CC   peptidase that is at the end of the blood coagulation cascade
#=GF CC   and which creates the clot by cleaving fibrinogen.  The
#=GF CC   interaction between thrombin and fibrinogen involves two
#=GF CC   different areas of contact - via the thrombin active site and
#=GF CC   via a second substrate-binding site known as an exosite.  The
#=GF CC   inhibitor acts by blocking the exosite, rather than by
#=GF CC   interacting with the active site.  The inhibitors are from
#=GF CC   mosquitoes that feed on human blood and which, by inhibiting
#=GF CC   thrombin, prevent the blood from clotting and keep it flowing.
#=GF SQ   2
#=GS Q7Q3R9_ANOGA/1-65  AC Q7Q3R9.3
#=GS Q8I6P7_ANOST/1-65  AC Q8I6P7.1
Q7Q3R9_ANOGA/1-65             MASKLFVLAFLCLALVVVVQSAPQYARGDVPTYDEEDFDEESLKPHSSSSSDDGEEEFDPSLLEE.
Q8I6P7_ANOST/1-65             MASKVIVIALLCIALAAFVQGAPQYTHGEEPEYDEDDGADEPVQPHSSSNHADTEDDFDLSLLD-k
#=GC seq_cons                 MASKlhVlAhLClALsshVQuAPQYs+G-.PpYDE-Dhs-EslpPHSSSspsDsE--FD.SLL-..
//