#=GF ID   RIF2_ASCE
#=GF AC   PF21449.4
#=GF DE   RIF2, ASCE domain
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF AU   Chuguransky S;0000-0002-0520-0736
#=GF SE   ECOD:EF14987
#=GF GA   27.60 27.60;
#=GF TC   28.20 171.80;
#=GF NC   25.40 22.30;
#=GF BM   hmmbuild  HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 --cpu 8 -Z 90746521 HMM pfamseq
#=GF TP   Domain
#=GF CL   CL0023
#=GF RC   Paper describing PDB structure 4bj1
#=GF RN   [1]
#=GF RM   23746845
#=GF RT   Rif1 and Rif2 shape telomere function and architecture through
#=GF RT   multivalent Rap1 interactions.
#=GF RA   Shi T, Bunker RD, Mattarocci S, Ribeyre C, Faty M, Gut H, Scrima
#=GF RA   A, Rass U, Rubin SM, Shore D, Thoma NH;
#=GF RL   Cell. 2013;153:1340-1353.
#=GF DR   INTERPRO; IPR049044;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   RIF2 is involved in transcriptional silencing and telomere
#=GF CC   length regulation [1]. It belongs to the ATPase family
#=GF CC   associated with diverse cellular activities. This domain
#=GF CC   represents the ASCE (NTPase) domain described in [1].
#=GF SQ   2
#=GS J6EF69_SACK1/185-277  AC J6EF69.1
#=GS RIF2_YEAST/185-277    AC Q06208.1
J6EF69_SACK1/185-277             .DDTFDLMMMIIREISQNSSLNHIICFRFEQLDESSSSNVIVPSKLTEFKRILLSLQRIKNIAFKFLVYSNNTNISSLLFTTFKNELKRELTIF
RIF2_YEAST/185-277               n-HTSDLMMMVMRKINNDESIDHIVYFKFEQLDKLSTSTIIEPSKLTEFINVLSVLEKSNNIAFKVLIYSNNVSISSLLSTSLKKKLNTKYTVF
#=GC seq_cons                    ..cT.DLMMMlhRcIspspSlsHIlhF+FEQLDc.SoSslI.PSKLTEFhplL.sLp+.pNIAFKhLlYSNNssISSLL.TohKpcLppchTlF
//