#=GF ID   STIV_turret_2nd
#=GF AC   PF21876.1
#=GF DE   C381 turret protein 2nd galactose-binding domain-like
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF SE   ECOD:EF20029
#=GF GA   27.00 27.00;
#=GF TC   36.80 231.60;
#=GF NC   26.40 23.60;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch --cpu 4 -E 1000 -Z 81514348 HMM pfamseq
#=GF TP   Domain
#=GF CL   CL0202
#=GF RC   Paper describing PDB structure 3j31
#=GF RN   [1]
#=GF RM   23520050
#=GF RT   Atomic structure of the 75 MDa extremophile Sulfolobus turreted
#=GF RT   icosahedral virus determined by CryoEM and X-ray
#=GF RT   crystallography.
#=GF RA   Veesler D, Ng TS, Sendamarai AK, Eilers BJ, Lawrence CM, Lok SM,
#=GF RA   Young MJ, Johnson JE, Fu CY;
#=GF RL   Proc Natl Acad Sci U S A. 2013;110:5504-5509.
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   This entry represents the Sulfolobus turreted icosahedral virus
#=GF CC   (STIV) turret protein second jelly roll domain. The C381 turret
#=GF CC   protein is a component of the STIV virion vertex complex, which
#=GF CC   orchestrates virion assembly by coordinating interactions of the
#=GF CC   membrane and various protein components involved. The turret
#=GF CC   protein is apposed on the penton base C-terminal jelly-roll ring
#=GF CC   and forms a pentamer consisting of three consecutive layers of
#=GF CC   jelly-rolls, with each jelly-roll exhibiting different
#=GF CC   orientations. The interior of the C381 pentamer harbors two
#=GF CC   rather large cavities, which exhibit an overall positive
#=GF CC   electrostatic potential, suggesting that the turrets may act as
#=GF CC   STIV receptor-binding proteins carrying out recognition and
#=GF CC   attachment to the host receptors. The turret protein shares
#=GF CC   similarity with many carbohydrate-binding modules as well as
#=GF CC   domains involved in protein-protein interactions.
#=GF SQ   1
#=GS Q6Q0L3_9VIRU/154-259  AC Q6Q0L3.1
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND H; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND M; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND K; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND O; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND I; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND D; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND Q; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND L; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND E; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND R; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND T; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 3J31 P; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND B; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND P; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND S; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND G; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND F; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND N; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND C; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND A; 154-259;
#=GS Q6Q0L3_9VIRU/154-259  DR PDB; 4IND J; 154-259;
Q6Q0L3_9VIRU/154-259             RINIPKIIHTSGNGYISFRLRKGTYAIKMPYSYNNTTSTTFTNFQFGTISTSVATIPLVISSIPANGSGSGTFLVYLKITGDYEDVKFSVTYGGGLGVPFTFGLEV
#=GR Q6Q0L3_9VIRU/154-259  SS    -EEEEEEEEESS-EEEEEE--SEEEEEEEEEEEE--SS-EEEEEEEEEEE----EEEEEEEEE-TT-EEEEEEEEEEEE-SS--EEEEEE-S-TTSS--EEEEEEE
#=GC SS_cons                     -EEEEEEEEESS-EEEEEE--SEEEEEEEEEEEE--SS-EEEEEEEEEEE----EEEEEEEEE-TT-EEEEEEEEEEEE-SS--EEEEEE-S-TTSS--EEEEEEE
#=GC seq_cons                    RINIPKIIHTSGNGYISFRLRKGTYAIKMPYSYNNTTSTTFTNFQFGTISTSVATIPLVISSIPANGSGSGTFLVYLKITGDYEDVKFSVTYGGGLGVPFTFGLEV
//