#=GF ID   Bd3614_N
#=GF AC   PF14442.9
#=GF DE   Bd3614-like deaminase N-terminal
#=GF PI   Bd3614-N;
#=GF AU   Iyer LM;0000-0002-4844-2022
#=GF AU   Zhang D;0000-0001-8535-7620
#=GF AU   Aravind L;0000-0003-0771-253X
#=GF SE   Manual
#=GF GA   25.00 25.00;
#=GF TC   26.10 28.00;
#=GF NC   23.90 22.40;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
#=GF TP   Family
#=GF RN   [1]
#=GF RM   21890906
#=GF RT   Evolution of the deaminase fold and multiple origins of
#=GF RT   eukaryotic editing and mutagenic nucleic acid deaminases from
#=GF RT   bacterial toxin systems.
#=GF RA   Iyer LM, Zhang D, Rogozin IB, Aravind L;
#=GF RL   Nucleic Acids Res. 2011; [Epub ahead of print]
#=GF DR   INTERPRO; IPR025854;
#=GF DR   SO; 0100021; polypeptide_conserved_region;
#=GF CC   This is a globular domain that occurs N-terminal to the
#=GF CC   Bd3614-like deaminases, which are predicted to be involved in
#=GF CC   RNA editing [1].
#=GF SQ   3
#=GS C1MW10_MICPC/74-165  AC C1MW10.1
#=GS C1EBX0_MICCC/89-180  AC C1EBX0.1
#=GS A4S9Y1_OSTLU/2-46    AC A4S9Y1.1
C1MW10_MICPC/74-165             ..SSSARRRDVAFLVARSDADADADDVVWYATAPADAPAWDSPIARLVLGAREAGGRARANAWCRRRIVST.RAMSALDRAIVKVAAQRATYLDL..
C1EBX0_MICCC/89-180             ..TSSVEDDDVAFLVAPSSGDADAPSVVWFATSRKTSPPWDSALVRLVLGAREAGGRANGNRWARARMLTT.RALSDLDRAVVKVAAQRATAFDL..
A4S9Y1_OSTLU/2-46               rg--------------------------------------------------ESDGRNYGDAWMRRRVFTTaKALTTFERALVKVCATKATTV--rv
#=GC seq_cons                   ..oSSscccDVAFLVA.SsuDADAssVVWaATu.tsuPsWDSslsRLVLGAREAGGRApGNAWsRRRllTT.RALSsLDRAlVKVAAQRATslDL..
//