ID A0A328UY31_9CYAN Unreviewed; 281 AA. AC A0A328UY31; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 13-NOV-2019, entry version 5. DE RecName: Full=Site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|RuleBase:RU361257}; DE EC=2.1.1.72 {ECO:0000256|RuleBase:RU361257}; GN ORFNames=B9S53_06445 {ECO:0000313|EMBL:RAQ45878.1}, B9S53_21645 GN {ECO:0000313|EMBL:RAQ39456.1}; OS Arthrospira sp. O9.13F. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Microcoleaceae; Arthrospira; unclassified Arthrospira. OX NCBI_TaxID=1982223 {ECO:0000313|EMBL:RAQ39456.1}; RN [1] {ECO:0000313|EMBL:RAQ39456.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O9.13F {ECO:0000313|EMBL:RAQ39456.1}; RA Waleron M., Misztak A.E., Waleron K.F., Bazhenova O., Furmaniak M.A., RA Baurain D.; RT "Comparative genome analysis of the Arthrospira genus RT (Cyanobacteria)."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an CC N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, CC Rhea:RHEA-COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; CC EC=2.1.1.72; Evidence={ECO:0000256|RuleBase:RU361257}; CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC {ECO:0000256|RuleBase:RU361257}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:RAQ39456.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PKGD01000587; RAQ39456.1; -; Genomic_DNA. DR EMBL; PKGD01000099; RAQ45878.1; -; Genomic_DNA. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.1020.10; -; 1. DR InterPro; IPR023095; Ade_MeTrfase_dom_2. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR012263; M_m6A_EcoRV. DR InterPro; IPR012327; MeTrfase_D12. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR30481; PTHR30481; 1. DR Pfam; PF02086; MethyltransfD12; 1. DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1. DR PRINTS; PR00505; D12N6MTFRASE. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00571; dam; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Methyltransferase {ECO:0000256|RuleBase:RU361257, KW ECO:0000313|EMBL:RAQ39456.1}; KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU361257}; KW Transferase {ECO:0000256|RuleBase:RU361257, KW ECO:0000313|EMBL:RAQ39456.1}. FT BINDING 23 23 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR000398-1}. FT BINDING 27 27 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000256|PIRSR:PIRSR000398- FT 1}. FT BINDING 68 68 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR000398-1}. FT BINDING 193 193 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR000398-1}. SQ SEQUENCE 281 AA; 32397 MW; C1EBCDD3F4D5D561 CRC64; MSPTDHPTVT SQPQTTPKPF LKWAGGKTRL IPQYTTYFPD NYQTYYEPFL GGGAIFFYLQ PNRAILSDIN SELINAYQCV RDDTQSLISK LEQHQQNHNQ GYYYQMRSQK FENPLDQAAR LIYLNKTCFN GLYRENRQGQ FNVPMGKYKN PKICPKELLI TASKTLQSAT LQVQSFEAIV NEANSADDFV YFDPPYHPLS PTSNFTSYSH HKFGVDEQEK LAEIFKTLHN RGVKVMLSNS DTELIRDLYK DFNIHPIQAG RAINSNHQNR GKITELLITS Y //