ID DMA_BPT2 STANDARD; PRT; 259 AA. AC P12427; DT 01-OCT-1989 (REL. 12, CREATED) DT 01-OCT-1989 (REL. 12, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE DNA ADENINE METHYLASE (EC 2.1.1.72) (DEOXYADENOSYL-METHYLTRANSFERASE). GN DAM. OS BACTERIOPHAGE T2. OC VIRIDAE; DS-DNA NONENVELOPED VIRUSES; MYOVIRIDAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 89033901. RA MINER Z., HATTMAN S.; RL J. BACTERIOL. 170:5177-5184(1988). RN [2] RP MUTAGENESIS. RX MEDLINE; 90045940. RA MINER Z., SCHLAGMAN S.L., HATTMAN S.; RL NUCLEIC ACIDS RES. 17:8149-8157(1989). CC -!- FUNCTION: THIS METHYLASE RECOGNIZES THE DOUBLE-STRANDED SEQUENCE CC GATC, CAUSES SPECIFIC METHYLATION ON A-2 ON BOTH STRANDS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE + DNA ADENINE = CC S-ADENOSYL-L-HOMOCYSTEINE + DNA 6-METHYLAMINOPURINE. 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; M22342; G215793; -. DR PIR; A30195; XYBPT2. DR PIR; S09361; S09361. DR PROSITE; PS00092; N6_MTASE. KW TRANSFERASE; METHYLTRANSFERASE; DNA REPLICATION. SQ SEQUENCE 259 AA; 30439 MW; BE50FE8B CRC32; MLGAIAYTGN KQSLLPELKP HFPKYDRFVD LFCGGLSVSL NVNGPVLAND IQEPIIEMYK RLINVSWDDV LKVIKQYKLS KTSKEEFLKL REDYNKTRDP LLLYVLHFHG FSNMIRINDK GNFTTPFGKR TINKNSEKRF NHFKQNCDKI IFSSLHFKDV KILDGDFVYV DPPYLITVAD YNKFWSEEEE KDLLNLLDSL NDRGIKFGLS NVLEHHGKEN TLLKEWSKKY NVKHLNKKYV FNIYHSKEKN GTDEVYIFN //