ID   MTBA$BACAM     STANDARD;      PRT;   265 AA.
AC   P18051;
DT   01-NOV-1990  (REL. 16, CREATED)
DT   01-NOV-1990  (REL. 16, LAST SEQUENCE UPDATE)
DT   01-NOV-1990  (REL. 16, LAST ANNOTATION UPDATE)
DE   MODIFICATION METHYLASE BAMH I (EC 2.1.1.-) (N-4 CYTOSINE-SPECIFIC
DE   METHYLTRANSFERASE BAMH I).
OS   BACILLUS AMYLOLIQUEFACIENS.
OC   PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE.
RN   [1] (STRAIN H, SEQUENCE FROM N.A.)
RA   CONNAUGHTON J.F., KALOSS W.D., VANEK P.G., NARDONE G.A.,
RA   CHIRIKJIAN J.G.;
RL   NUCLEIC ACIDS RES. 18:4002-4002(1990).
CC   -!- FUNCTION: THIS METHYLASE RECOGNIZES THE DOUBLE-STRANDED SEQUENCE
CC       GGATCC, CAUSES SPECIFIC METHYLATION ON C-5 ON BOTH STRANDS, AND
CC       PROTECTS THE DNA FROM CLEAVAGE BY THE BAMH I ENDONUCLEASE.
CC   -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE + DNA CYTOSINE =
CC       S-ADENOSYL-L-HOMOCYSTEINE + DNA 4-METHYLCYTOSINE.
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DR   EMBL; X53032; BABHIPM.
DR   REBASE; BAMHI; RELEASE 9102.
DR   PROSITE; PS00093; N4_MTASE.
KW   TRANSFERASE; METHYLTRANSFERASE; RESTRICTION SYSTEM.
SQ   SEQUENCE   265 AA;  30981 MW;  354972 CN;
     MKENIGDCTI DLTVTSPPYD DLRNYNGYSF NFEETAQELY RVTKEGGVVV WVVGDKTHKG
     SETGSSFRQA LYFKELGFNL HDTMIYEKDS ISFPDKNRYY QIFEYMFIFS KGKPKTINLL
     ADRKNKWYNG KKHIKGHYRK MDGEKVRHHK QNLLKEFGVR FNIWRIPNGH QKSTLDKIAF
     QHPAIFPEKL AEDHILSWSN EGDIVFDPFM GSGTTAKMAA LNNRKYIGTE ISKEYCDIAN
     ERLKNYIILH KRMEGKGYRL PQVHS
//