#=GF ID Lambda_ea8_5
#=GF AC PF20735.1
#=GF DE Bacteriophage lambda ea8.5-related domain
#=GF AU Bateman A;0000-0002-6982-4660
#=GF AU Lazaro Pinto Beatriz;0000-0001-6837-2941
#=GF SE ECOD:101.1.19
#=GF GA 27.00 27.00;
#=GF TC 27.60 65.10;
#=GF NC 24.80 26.80;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 75585367 -E 1000 --cpu 4 HMM pfamseq
#=GF TP Domain
#=GF RC Paper describing PDB structure 2m7a
#=GF RN [1]
#=GF RM 23672713
#=GF RT The solution structures of two prophage homologues of the
#=GF RT bacteriophage lambda Ea8.5 protein reveal a newly discovered
#=GF RT hybrid homeodomain/zinc-finger fold.
#=GF RA Kwan JJ, Smirnova E, Khazai S, Evanics F, Maxwell KL, Donaldson
#=GF RA LW;
#=GF RL Biochemistry. 2013;52:3612-3614.
#=GF RN [2]
#=GF RM 26798427
#=GF RT The Role of the Exo-Xis Region in Oxidative Stress-Mediated
#=GF RT Induction of Shiga Toxin-Converting Prophages.
#=GF RA Licznerska K, Dydecka A, Bloch S, Topka G, Nejman-Falenczyk B,
#=GF RA Wegrzyn A, Wegrzyn G;
#=GF RL Oxid Med Cell Longev. 2016;2016:8453135.
#=GF RN [3]
#=GF RM 32548406
#=GF RT Ea22 Proteins from Lambda and Shiga Toxin-Producing
#=GF RT Bacteriophages Balance Structural Diversity with Functional
#=GF RT Similarity.
#=GF RA Tong J, Nejman-Falenczyk B, Bloch S, Wegrzyn A, Wegrzyn G,
#=GF RA Donaldson LW;
#=GF RL ACS Omega. 2020;5:12236-12244.
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC This domain is found in Protein ea8.5 from Bacteriophage lambda
#=GF CC and similar protein sequences mostly from tailed bacteriophages
#=GF CC and bacterial prophages. It ranges from around 45 to 90 residues
#=GF CC in length and is associated with nucleic acid binding function,
#=GF CC playing an essential role in the inhibition of the initiation of
#=GF CC DNA synthesis in the phage host. NMR analysis shows it adopts an
#=GF CC homeodomain/zinc-finger fold, which suggests a regulatory role
#=GF CC [1, 2, 3].
#=GF SQ 11
#=GS K7P8A4_9CAUD/8-93 AC K7P8A4.1
#=GS A0A0K2FIU9_9CAUD/8-93 AC A0A0K2FIU9.1
#=GS A0A417Y9F9_9BACI/8-93 AC A0A417Y9F9.1
#=GS EA85_LAMBD/8-93 AC P03755.1
#=GS A0A3N9TA48_9VIBR/8-82 AC A0A3N9TA48.1
#=GS A0A3E2N3I0_9CLOT/8-70 AC A0A3E2N3I0.1
#=GS A0A346FJ45_9CAUD/8-93 AC A0A346FJ45.1
#=GS A0A1X7MFP7_9GAMM/1-44 AC A0A1X7MFP7.1
#=GS A0A0Q4J7S0_9SPHN/2-86 AC A0A0Q4J7S0.1
#=GS A0A1S1V716_9FIRM/8-93 AC A0A1S1V716.1
#=GS Q88G17_PSEPK/10-92 AC Q88G17.1
K7P8A4_9CAUD/8-93 SEQKDWALS..MLCRSGVLSPCRHHEGVYVDEGIDIESAYKYSMKVYKSNEDKSPF.CNVREMTDTVQNYYHEYG..GNDTCPLCtkHIDD
A0A0K2FIU9_9CAUD/8-93 SEQKDWALS..MLCRSGVLSPCRHHEGVYVDEGIDIESAYKYSMKVYKSNEDKSPF.CNVREMTDTVQNYYHEYG..GNDTCPLCtkHIDD
A0A417Y9F9_9BACI/8-93 SEQKDWALS..MLCRSGVLSPCRHHEGVYVDEGIDIESAYKYSMKVYKSNEDKSPF.CNVREMTDTVQNYYHEYG..GNDTCPLCtkHIDD
EA85_LAMBD/8-93 SEQKDWALS..MLCRSGVLSPCRHHEGVYVDEGIDIESAYKYSMKVYKSNEDKSPF.CNVREMTDTVQNYYHEYG..GNDTCPLCtkHIDD
A0A3N9TA48_9VIBR/8-82 SEQKDWALS..MLCRSGVLSPCRHHEGVYVDEGIDIESAYKYSMKVYKSNEDKSPF.CNVREMTDTVQNYYHEYG..GND-----..----
A0A3E2N3I0_9CLOT/8-70 SEQKDWALS..MLCRSCVLSPCRHHEGVYVDEGIDIESAYKYSMKVYKSNEDKSPF.CNVREMTDT---------..--------..----
A0A346FJ45_9CAUD/8-93 SEQKDWALS..MLCRSGVLSPCRHHEGVYVDEGIDIESAYKYSMKVYKSNEDKSPF.CNVREMTDTVQNYYHEYG..GNDTCPLCtkHIDD
A0A1X7MFP7_9GAMM/1-44 ---------..---------------------------------KVYKSNEDKSPF.CNVREMTDTVQNYYHEYG..GNDTCPLCtkHIDD
A0A0Q4J7S0_9SPHN/2-86 DDMRRAAED..VLIEAGALTKCDVHGDVYDCDSDRLASAYPIANSKISSGQIVLPSgWTRKDFTDVVKSVYEDNS..NIDYCPSC..DKND
A0A1S1V716_9FIRM/8-93 SEQKDWALS..MLCRSGVLSPCRHHEGVYVDEGIDIESAYKYSMKVYKSNEDKSPF.CNVREMTDTVQNYYHEYG..GNDTCPLCtkHIDD
Q88G17_PSEPK/10-92 EEDAKYSEAvyIAIEAGTLAECEVHEGTYFSDSGDISEAEELAREKFEKGEVS---.-NFDDVEELVKKVVAVCEelGAEECFSC..-DFD
#=GC seq_cons SEQKDWALS..MLCRSGVLSPCRHHEGVYVDEGIDIESAYKYSMKVYKSNEDKSPF.CNVREMTDTVQNYYHEYG..GNDTCPLCTKHIDD
//
