#=GF ID His_Me_b4a2
#=GF AC PF18275.5
#=GF DE His-Me finger endonuclease beta4-alpha2 domain
#=GF AU Smart A;0000-0002-6965-5633
#=GF SE ECOD:EUF03014
#=GF GA 25.00 25.00;
#=GF TC 114.30 114.30;
#=GF NC 24.40 19.70;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -E 1000 --cpu 4 -Z 75585367 HMM pfamseq
#=GF TP Domain
#=GF CL CL0263
#=GF RN [1]
#=GF RM 19380375
#=GF RT Crystal structure of the beta beta alpha-Me type II restriction
#=GF RT endonuclease Hpy99I with target DNA.
#=GF RA Sokolowska M, Czapinska H, Bochtler M;
#=GF RL Nucleic Acids Res. 2009;37:3799-3810.
#=GF DR INTERPRO; IPR041475;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC This domain is found in Hpy991 present in Helicobacter pylori.
#=GF CC Hpy991 is a beta-beta-alpha-Me restriction endonuclease that
#=GF CC recognizes the CGWCG target sequence and cleaves both DNA
#=GF CC strands with a stagger that leads to 5'-recessed ends in the
#=GF CC cleavage products. This domain is the first of two beta4-alpha2
#=GF CC repeats found after the N-terminal domain. The two repeats have
#=GF CC low overall sequence similarity but readily identified by a
#=GF CC structural comparison. Both repeats contain contains two CXXC
#=GF CC motifs that map to the first beta-hairpin and the first
#=GF CC alpha-helix. The four cysteine residues coordinate a
#=GF CC structurally bound Zn2+ ion tetrahedrally. The major groove is
#=GF CC in contact with the first repeat, with the beta-hairpin 2
#=GF CC inserting deeply into the groove [1].
#=GF SQ 3
#=GS V8C7I2_9HELI/55-106 AC V8C7I2.1
#=GS A0A4U7NDG2_9SPIR/56-107 AC A0A4U7NDG2.1
#=GS I7HE83_9HELI/56-107 AC I7HE83.1
V8C7I2_9HELI/55-106 DIYKTGKGYDKKICNICHILKDTDDFEINQTDAKGRKTTRPSCRECRKNIDG
A0A4U7NDG2_9SPIR/56-107 DIYKTGKGYKNKICNICHILKPTDEFEINQTDAKGIKTTRPSCRECRKTIDG
I7HE83_9HELI/56-107 DIYKTGKGFDCKICNICHILKDTGSFEINQTDAKGNKTTRPSCRECRKHIDG
#=GC seq_cons DIYKTGKGYDsKICNICHILKDTD-FEINQTDAKGpKTTRPSCRECRKsIDG
//
