#=GF ID   HEPN-like_int
#=GF AC   PF18867.5
#=GF DE   HEPN-like integron domain
#=GF AU   Iyer LM;0000-0002-4844-2022
#=GF AU   Aravind L;0000-0003-0771-253X
#=GF AU   Burroughs AM;0000-0002-2229-8771
#=GF AU   El-Gebali S;0000-0003-1378-5495
#=GF AU   Anantharaman V;0000-0001-8395-0009
#=GF SE   Iyer LM
#=GF GA   25.00 25.00;
#=GF TC   346.90 346.90;
#=GF NC   22.90 22.60;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch --cpu 4 -E 1000 -Z 75585367 HMM pfamseq
#=GF TP   Domain
#=GF CL   CL0291
#=GF RN   [1]
#=GF RM   23768067
#=GF RT   Comprehensive analysis of the HEPN superfamily: identification
#=GF RT   of novel roles in  intra-genomic conflicts, defense,
#=GF RT   pathogenesis and RNA processing.
#=GF RA   Anantharaman V, Makarova KS, Burroughs AM, Koonin EV, Aravind L;
#=GF RL   Biol Direct. 2013;8:15.
#=GF DR   INTERPRO; IPR041323;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   This is a HEPN-like nuclease. Part of mobile integron element.
#=GF CC   The integron cassettes are known to be activated by stress
#=GF CC   conditions, thereby allowing swapping of genetic material that
#=GF CC   might be of adaptive value. Hence it is hypothesized that the
#=GF CC   HEPN domains present in some integron cassettes contribute to
#=GF CC   the stress response by functioning as RNases that induce
#=GF CC   dormancy by probably inhibiting translation and thus enabling
#=GF CC   survival of harsh conditions [1].
#=GF SQ   1
#=GS A0A286E4C0_9NEIS/11-161  AC A0A286E4C0.1
A0A286E4C0_9NEIS/11-161             DKNTLLKMYFYFQYTAIEIQSAVNLLYMLEQFIEGKPYKEMIANEMLVLAPSQGSLNAYVTLSRVAFHNLIINIFKLGELIEKKQGILTHLPEFNKSVNEFRKIFFTQDLRLYRNTYVAHHSDKNKDKSDNFLNYEELIQTFCKIIGVDLS
#=GC seq_cons                       DKNTLLKMYFYFQYTAIEIQSAVNLLYMLEQFIEGKPYKEMIANEMLVLAPSQGSLNAYVTLSRVAFHNLIINIFKLGELIEKKQGILTHLPEFNKSVNEFRKIFFTQDLRLYRNTYVAHHSDKNKDKSDNFLNYEELIQTFCKIIGVDLS
//