ID F7NEZ3_9FIRM Unreviewed; 582 AA.
AC F7NEZ3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=ALO_03051 {ECO:0000313|EMBL:EGO65554.1};
OS Acetonema longum DSM 6540.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Acetonema.
OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO65554.1, ECO:0000313|Proteomes:UP000003240};
RN [1] {ECO:0000313|EMBL:EGO65554.1, ECO:0000313|Proteomes:UP000003240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO65554.1,
RC ECO:0000313|Proteomes:UP000003240};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGO65554.1}.
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DR EMBL; AFGF01000017; EGO65554.1; -; Genomic_DNA.
DR RefSeq; WP_004092701.1; NZ_AFGF01000017.1.
DR AlphaFoldDB; F7NEZ3; -.
DR STRING; 1009370.ALO_03051; -.
DR REBASE; 39484; Alo6540ORF3051P.
DR eggNOG; COG0827; Bacteria.
DR eggNOG; COG1002; Bacteria.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000003240; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.220.10; Adenine-n6-DNA-methyltransferase Taqi, Chain A, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR023135; N6_DNA_MeTrfase_TaqI_C.
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; PF02384; N6_Mtase; 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 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EGO65554.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003240};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGO65554.1}.
FT DOMAIN 18..310
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 390..521
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 582 AA; 66065 MW; 90AC1453D8196925 CRC64;
MTGKRTEPDN PGLPITGEQY EKSMAREVRK ALGLYYTPGY IIDYILQRTV SEIDVRDDPF
VSILDPACGS GSFLLAAYDI LRAKFVAALP ELQKKYGSLT YEWQQGNCQI TLSGGEYWQE
EHIHYHILTH CLFGADIDRA AVRLAAEHLS LRDAACEVWP RHLIACDSLM HWEARSQPAG
ETESAAAGFW QRTFDYIVGN PPYIPITQMT QEQKQYYRAR YQTATGRMNA FALFLERCIA
KTGKKAGFIV PGRLLLNTQY GSIRRLVLEN TWIEEIFETD AAVFPEAVVD TVILILNRNK
RWAPGDKTLI RRMTRAGCSE QPVEQNRFLA TDHAYIQTHT STAEMGLLQT IRSRSALLGD
IAQVRDGIIQ GRVGNELFLG EKPTHDGYAK PVLFGQDIHC YQLTPGRQYI WYHSEKLTAL
ERQRTAGREI GLRLREPGIF ERPKILSRQT ADRIIACMDE TGHYYMNTLH SAYVTDPEFN
PWYVLAVLNS QLSRFYYTRY TGEAGQAYAQ VKIANLKGLP IPRADRESQA GIAHLARQLQ
NPSTPHDHAG RQVLFTEIDA RLFQLLRLTP EEVSLAKGTG ER
//
