#=GF ID   RIF2_lid
#=GF AC   PF21450.4
#=GF DE   RIF2, AAA+ lid domain
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF AU   Chuguransky S;0000-0002-0520-0736
#=GF SE   ECOD:EF15929
#=GF GA   27.00 27.00;
#=GF TC   31.70 178.50;
#=GF NC   22.70 22.40;
#=GF BM   hmmbuild  HMM.ann SEED.ann
#=GF SM   hmmsearch --cpu 8 -E 1000 -Z 90746521 HMM pfamseq
#=GF TP   Domain
#=GF CL   CL0671
#=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; IPR049045;
#=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 alpha-helical AAA+ lid domain described in [1].
#=GF SQ   2
#=GS RIF2_YEAST/284-368    AC Q06208.1
#=GS J6EF69_SACK1/284-368  AC J6EF69.1
RIF2_YEAST/284-368               CAQEQEYLKKMIKFTFDSGSKLLQSYNSLVTCQLNNKESNLAIFFEFLKVFPHPFTYLFNAYTEIIVQSRTFDELLDKIRNRLTI
J6EF69_SACK1/284-368             SVQVQEHLKKMIKFPSDPGNELLRLYNTLIARQLDNKKSCLVEFLEFLKDFPHPFTYLFNAYTEILVQSKTFDGLLDRINNKFTM
#=GC seq_cons                    ssQ.QEaLKKMIKFs.DsGscLLp.YNoLlspQLsNKcSsLs.FhEFLKsFPHPFTYLFNAYTEIlVQS+TFDtLLD+IpN+hTh
//