#=GF ID   Rap1_C_Sp
#=GF AC   PF21411.1
#=GF DE   S. pombe DNA-binding protein Rap1, C-terminal
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF AU   Chuguransky S;0000-0002-0520-0736
#=GF SE   ECOD:EF17442
#=GF GA   27.00 27.00;
#=GF TC   27.20 93.40;
#=GF NC   26.40 19.10;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 75585367 --cpu 4 -E 1000 HMM pfamseq
#=GF TP   Domain
#=GF RC   Paper describing PDB structure 2l3n
#=GF RN   [1]
#=GF RM   21217703
#=GF RT   A conserved motif within RAP1 has diversified roles in telomere
#=GF RT   protection and regulation in different organisms.
#=GF RA   Chen Y, Rai R, Zhou ZR, Kanoh J, Ribeyre C, Yang Y, Zheng H,
#=GF RA   Damay P, Wang F, Tsujii H, Hiraoka Y, Shore D, Hu HY, Chang S,
#=GF RA   Lei M;
#=GF RL   Nat Struct Mol Biol. 2011;18:213-221.
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   DNA-binding protein Rap1 is involved in protecting chromosome
#=GF CC   ends in fission yeast and its C-terminal domain (RCT)
#=GF CC   structurally resembles the first 3-helix bundle found in yeast
#=GF CC   and human RAP1 RCT. S. pombe RAP1 lacks direct DNA-binding
#=GF CC   activity and is localised to telomeres via Taz1 [1]. This entry
#=GF CC   represents the C-terminal domain of Rap1 from S. pombe.
#=GF SQ   2
#=GS S9XJW4_SCHCR/667-706  AC S9XJW4.1
#=GS RAP1_SCHPO/650-689    AC Q96TL7.1
S9XJW4_SCHCR/667-706             KVDEAIDMILRYTRSSEQQFLDALELAEGNISAAIAKLLL
RAP1_SCHPO/650-689               EVDEAIDNILRYTNSTEQQFLEAMESTGGRVRIAIAKLLS
#=GC seq_cons                    cVDEAID.ILRYTpSoEQQFL-AhE.stGplphAIAKLL.
//