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Database: Pfam
Entry: Staphostatin_A
LinkDB: Staphostatin_A
Original site: Staphostatin_A 
#=GF ID   Staphostatin_A
#=GF AC   PF09022.13
#=GF DE   Staphostatin A
#=GF AU   Mistry J;0000-0003-2479-5322
#=GF AU   Sammut SJ;0000-0003-4472-904X
#=GF SE   pdb_1oh1
#=GF GA   24.10 24.10;
#=GF TC   25.50 27.30;
#=GF NC   20.30 19.50;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
#=GF TP   Domain
#=GF CL   CL0354
#=GF RN   [1]
#=GF RM   14621990
#=GF RT   A novel class of cysteine protease inhibitors: solution
#=GF RT   structure of staphostatin A from Staphylococcus aureus. 
#=GF RA   Dubin G, Krajewski M, Popowicz G, Stec-Niemczyk J, Bochtler M,
#=GF RA   Potempa J, Dubin A, Holak TA; 
#=GF RL   Biochemistry. 2003;42:13449-13456.
#=GF DR   INTERPRO; IPR015112;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   The staphostatin A polypeptide chain folds into a slightly
#=GF CC   deformed, eight-stranded beta-barrel, with strands beta-4
#=GF CC   through beta-8 forming an antiparallel sheet while the
#=GF CC   N-terminus forms a a psi-loop motif. Members of this family
#=GF CC   constitute a class of cysteine protease inhibitors distinct in
#=GF CC   the fold and the mechanism of action from any known inhibitors
#=GF CC   of these enzymes [1].
#=GF SQ   3
#=GS Q5HKF5_STAEQ/1-105  AC Q5HKF5.1
#=GS Q2G2R7_STAA8/1-105  AC Q2G2R7.1
#=GS W1W6I3_9STAP/1-105  AC W1W6I3.1
Q5HKF5_STAEQ/1-105             MHNYNNINIVSDDSKYQ..EICWFHTLEGIWHPVEVETSPLNITFNKEITPNYVCTLINEDSRKIILSNVDNPNIIIEMILINSKKLVFNAISKEGLGTSPKITFTK..
Q2G2R7_STAA8/1-105             MEQIELFSIDKFKCNSE..AKYYLNIIEGEWHPQDLNDSPLKFILSTSDDSDYICKYINTEHKQLTLYNKNNSSIVIEIFIPNDNKILLTIMNTEALGTSPRMTFIK..
W1W6I3_9STAP/1-105             MHNYNNINIVSDDSKYQ..EICWFHTLEGIWHPVEVETSPLNITFNKDITPNYVCTLINEDSRKIILSNVDNPNIIIEMILINSKKLVFNAISKEGLGTSPKITFTK..
#=GC seq_cons                  MHNYNNINIVSDDSKYQ..EICWFHTLEGIWHPVEVETSPLNITFNK-ITPNYVCTLINEDSRKIILSNVDNPNIIIEMILINSKKLVFNAISKEGLGTSPKITFTK..
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