#=GF ID Cortex-I_coil
#=GF AC PF09304.16
#=GF DE Cortexillin coiled-coil region
#=GF AU Mistry J;0000-0003-2479-5322
#=GF AU Sammut SJ;0000-0003-4472-904X
#=GF AU Bateman A;0000-0002-6982-4660
#=GF SE pdb_1d7m
#=GF GA 60.00 60.00;
#=GF TC 131.50 131.50;
#=GF NC 50.80 26.30;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 81514348 --cpu 4 -E 1000 HMM pfamseq
#=GF TP Coiled-coil
#=GF RN [1]
#=GF RM 10745004
#=GF RT The coiled-coil trigger site of the rod domain of cortexillin I
#=GF RT unveils a distinct network of interhelical and intrahelical salt
#=GF RT bridges.
#=GF RA Burkhard P, Kammerer RA, Steinmetz MO, Bourenkov GP, Aebi U;
#=GF RL Structure. 2000;8:223-230.
#=GF DR INTERPRO; IPR015383;
#=GF DR SO; 0001080; coiled_coil;
#=GF CC This entry represents the coiled-coil oligomerization domain
#=GF CC found in cortexillin I, an actin-bundling protein. The domain
#=GF CC forms a parallel two-stranded alpha-helical coiled coil
#=GF CC approximately 18 heptad repeats in length. The structure reveals
#=GF CC novel types of ionic coiled-coil interactions including distinct
#=GF CC interhelical salt bridge patterns. A key feature is the presence
#=GF CC of a 14-residue trigger site (residues 311-324) that is
#=GF CC essential for proper coiled-coil formation. This region contains
#=GF CC an elaborate network of interhelical and intrahelical salt
#=GF CC bridges that are crucial for dimer assembly and stability. The
#=GF CC domain shows several unusual features including charged residues
#=GF CC at core a and d heptad positions that participate in stabilizing
#=GF CC salt bridge networks [1].
#=GF SQ 12
#=GS A0A152A2Y5_TIELA/235-341 AC A0A152A2Y5.1
#=GS CTXA_DICDI/231-337 AC Q54HG2.1
#=GS CTXB_DICDI/233-339 AC Q550R2.1
#=GS CTXB_HETP5/235-341 AC Q9Y0T3.1
#=GS CTXA_HETP5/231-337 AC Q9Y0T4.1
#=GS F4QBP2_CACFS/234-340 AC F4QBP2.1
#=GS A0A151ZH67_TIELA/231-337 AC A0A151ZH67.1
#=GS F4PG89_CACFS/231-337 AC F4PG89.1
#=GS A0A8J4PPE7_9MYCE/236-342 AC A0A8J4PPE7.1
#=GS F0ZQ22_DICPU/216-322 AC F0ZQ22.1
#=GS F0Z9U7_DICPU/233-339 AC F0Z9U7.1
#=GS A0A8J4PRH1_9MYCE/232-338 AC A0A8J4PRH1.1
A0A152A2Y5_TIELA/235-341 KEEREALEASQNSLANKLASMEKSLEGEKLSQEELLKNKQQLESALNKIKNENEQRNHRISDLQSKIDDALRGLDDEKLAKLDLESRLAKTEKDKAILELKLAEILD.
CTXA_DICDI/231-337 KEEKARLESSKNEMANRLAGLENSLESEKVSREQLIKQKDQLNSLLASLESEGAEREKRLRELEAKLDETLKNLELEKLARMELEARLAKTEKDRAILELKLAEAID.
CTXB_DICDI/233-339 KEEREALEASQNSLNNKLASLEQSLEGEKHSQEELVKQKKDLEDALNKIREQNDNRNSRITDLQSKIDDALRGLDDEKLAKLDLESRLAKCEKDKAILELKLAEILD.
CTXB_HETP5/235-341 KEEREALEASQNSLANKLASLEQSLEGEKTSQDELARQKKELEESLRLIRQQNEQRNQRIADIQSKIDDALRGIDDEKMAKLDLESRLSKTEKDKAILELKLAETLD.
CTXA_HETP5/231-337 KEEKERLEASKSDLASKLAGLQNSLESEKLSREQLIKQKDELKSLLASLEGEAAEREKFLRELEAKLEEILKNLELERLARMELESRLSKMEKDKAILELKLAEAQD.
F4QBP2_CACFS/234-340 KEEREALEASQNSLQNTLSSLEGALQGEKLSQEELAKQKKDLENTLNELRAQNEARNKKISDIQARIDDALRGIDDERMAKLDLEARLSKTEKDKAILELKLQEMRD.
A0A151ZH67_TIELA/231-337 KEEKERLESSKNEIATRLAGLQNSLENEKVSREHLIKQQEEMKSLLASLEFEGAEREKRIKELEAKLDETLKNLELERLARLELEARLAKTEKDRAILELKLSDASD.
F4PG89_CACFS/231-337 KEEKERLEESKSAIASRLAGLQSSLENEKMSRELLIKQKEELKSLLASLEGEAASREHHLRELEAKLDEVLKNLELEKLARLELENRLAKTEKDKALLELALAEATD.
A0A8J4PPE7_9MYCE/236-342 KEEREALEAGQNALSNKLASLEQNLESEKHSHEELLKQKQELENSLNKIRSDNDHRNTLISDLQSRIDDALRGLDDEKLAKLDLESRLAKTEKDKAILELKLAEMLD.
F0ZQ22_DICPU/216-322 KEEKERLESSKNEIANRLAGLQNSLENEKVSREQLIKQKDELKSLLASLEFEGAEREKRLRELEAKLEDTLKNLELEKLARMELEARLAKTEKDRAILELKLAEAT-e
F0Z9U7_DICPU/233-339 KEEREALEASQNSLNNKLASLEQSLEGEKHSQEELLKQKQELENALNKIRSENENRNNRITDLQSRIDDALRGLDDEKLAKLDLESRLAKTEKDKAILELKLAEILD.
A0A8J4PRH1_9MYCE/232-338 KEEKERIEKDKNEIATRLAGLQNSLENEKITREQLIKQKDELKSLLASLEFEGAEREKRLRELEAKLEETLKNLELEKLARMEMEARLAKTEKDRAILELKLAEAT-e
#=GC seq_cons KEE+EtLEuSpNslAN+LAuLppSLEuEKhSpEpLlKQKcELcshLsplctEsspRp+Rlp-LpuKlD-sL+sL-.EKLA+L-LEuRLAKTEKDKAILELKLAEhhD.
//
