ID D5U6B7_BRAM5 Unreviewed; 1076 AA.
AC D5U6B7;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=Bmur_2547 {ECO:0000313|EMBL:ADG72616.1};
OS Brachyspira murdochii (strain ATCC 51284 / DSM 12563 / 56-150) (Serpulina
OS murdochii).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=526224 {ECO:0000313|EMBL:ADG72616.1, ECO:0000313|Proteomes:UP000001915};
RN [1] {ECO:0000313|EMBL:ADG72616.1, ECO:0000313|Proteomes:UP000001915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51284 / DSM 12563 / 56-150
RC {ECO:0000313|Proteomes:UP000001915};
RX PubMed=21304710; DOI=10.4056/sigs.831993;
RA Pati A., Sikorski J., Gronow S., Munk C., Lapidus A., Copeland A.,
RA Glavina Del Tio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Brachyspira murdochii type strain (56-150).";
RL Stand. Genomic Sci. 2:260-269(2010).
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, Rhea:RHEA-
CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC Evidence={ECO:0000256|ARBA:ARBA00001279};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; CP001959; ADG72616.1; -; Genomic_DNA.
DR RefSeq; WP_013114953.1; NC_014150.1.
DR AlphaFoldDB; D5U6B7; -.
DR STRING; 526224.Bmur_2547; -.
DR REBASE; 26084; BmuSORF2547P.
DR KEGG; brm:Bmur_2547; -.
DR eggNOG; COG0827; Bacteria.
DR eggNOG; COG1002; Bacteria.
DR HOGENOM; CLU_002539_1_1_12; -.
DR OrthoDB; 305098at2; -.
DR Proteomes; UP000001915; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF12950; TaqI_C; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:ADG72616.1};
KW Hydrolase {ECO:0000313|EMBL:ADG72616.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:ADG72616.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 654..764
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT DOMAIN 862..1021
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 1076 AA; 125299 MW; 0D9EEAF8C2808E25 CRC64;
MKKNNSVKNI NTQNNNFKFD EPYNKQKWAE HFGENFKEEY GSVAGEEEII EKNKDFLNKI
IWIGDLNINE NEVIGVFEVY IKNTRLASRV KISRICSRIL MSGSYGKGIF FILYEDNKNN
YRVSYVKHDK MGIKGENGLI IMKDDYSNPK RYTFLLGEGI KVHTPASRIT SDIFGSVESI
ENAFSVEGVN KEFYKGVKEY FEKIHNDIIK YFDKDENKAK EFALRFLGRV LFCWFLREKE
LIPNEILNSG VFENLKYKKN YYSDVLEDLF FNVLNMDMEK RKFSKERVIY NYEKAIPFLN
GGLFSKKEDD EAVKSIDDEI IKGLFEFFEM YNFTVDESAP FDVEISIDPE MLGRIFENLL
AEINPETKES ARKETGSFYT PREIVDYMVM EAIKLYLYKK MPDMEKNKID RIFDVDESVK
YTDEERKGIL KNIHDMIILD PACGSGAFPL GILQRVFNVI DKLDPNHEYY KNYVIDKLPS
GAKAEFKKLY DAKKFSYAYK LDILQSMIHG VDIQPIAIEV SKLRAFLSLV VDEKKEKKEH
NLGIRTLPNL EFQFLCTNAL IGVDFNIKKG TFEYSVLEGI KTMMKNISEM FYVASSLEEK
ERVKIKFEEF REFVKNSAFI DESIKAKILS WCPFDNKSAE FFSPLVQFGI DRDFDIVIGN
PPYIQLQGMA KGLKEMYQNA GYESFKSTGD IYQLFYEKCL GLLSDDGVAS LITSNKWMRA
GYGASTREYF YKNADVFRII DLGAGRFESA TVDVNIIFYS KTKEKHTRGE RSFEGVTYSG
SLKEIASAEF DAVVSEAGRE WVIMSGLERS IFNKISRHKA LKDWDIKINY GIKTGYNEAF
IIDEETKDRL IKEDKKSAEL IKPLLRGRDI KRYSYDFNNL YLICTFPALK LNIDKYKAIK
KYLESFGKRL EQSGEKGCRK KTNNKWFETQ DTISYYKDFE NNKIIYPNMT KYLPFIYDEN
NFYVNQKCFF IIDNKNNKNN LKYLTGILNS KVSHFWIRWN CPELQGGTRE LSAIFFANIP
IPEADSKTKN NITKLVDQII ILKKQDKDTT ALEKQIDEIV YSLYGLSDEE VKVVEG
//
