ID Q5LGD1_BACFN Unreviewed; 890 AA.
AC Q5LGD1; A0A380YVT5;
DT 21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 21-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
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=BF9343_1028 {ECO:0000313|EMBL:CAH06809.1};
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH06809.1, ECO:0000313|Proteomes:UP000006731};
RN [1] {ECO:0000313|EMBL:CAH06809.1, ECO:0000313|Proteomes:UP000006731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC Onslow {ECO:0000313|Proteomes:UP000006731};
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
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};
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DR EMBL; CR626927; CAH06809.1; -; Genomic_DNA.
DR RefSeq; WP_010992295.1; NZ_UFTH01000001.1.
DR REBASE; 312893; M.BfaSIV.
DR REBASE; 378130; M.Bfr9343II.
DR PaxDb; 272559-BF9343_1028; -.
DR KEGG; bfs:BF9343_1028; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_013049_6_0_10; -.
DR BioCyc; BFRA272559:G1GHZ-1122-MONOMER; -.
DR Proteomes; UP000006731; Chromosome.
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; 1.20.1260.30; -; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000006731};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..123
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 137..468
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 663..697
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 858..885
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 890 AA; 101470 MW; 98B6A87AE17C1B49 CRC64;
MAIKKTQLYS ILWESCNILR GSMDASQYKN YVLTMLFLKY ISDKVQSDSD IFFDLPEGCF
FNDIVALKGK PNIGEEIQKK LHVIARANPR LDHIINEADF DDSTKLGTGK AKVDTLTSLI
SVFQRDFLDF SKNRAGDDDL IGDAYEYLMK NFAAESGKKK GQFYTPAEVS RLMARLIGIH
KDNRPQISIY DPTCGSGSLL LRAAAEYTKH RDGVSIFGQE LDGATRGMAV MNMYLHGYDD
PELEVGDTIE KPFFKSTPNQ LETFNYVVAN PPFSQKGWIK GEIKINDTFG RWGNSDNLPP
IPPIGYEDYA FLLHIIKSIN SQGRGACILP NGVLFRGNEE EAVRRKIIEK RYIRGIISLP
TNLFFGTGIP ACIVIIDKAK TSTSKGIFMI DARSGFTKDG AKNRLREQDI RRVFDAWEAL
ENLEANGNLD DKEETIPHYA RFVPYTEITN ERNDCNLNVS RYITPVDTEI QQDLYAHLKL
NGGLPTKDVE EGFSYLWRHC PTLKNELFEP LEENYYKLRV GRNEIPNTII HNKEFSTLSG
FFSDAIEEWY KLVSQQMFAL APGCQPKKLI ADWSESLLEM LSEIDGLVDK YTIYDILLNY
WNSAMQDDCY LISRYGWTVE LSCDVLTTDK KSKEVKFVPK KNPTFRDYNC DLLPVHVVVN
HYFKEENEAV NEAEERVSQL KGEIEQMEEE YPEELNDTVT EIISKYIYAI CPKPLKGEKD
VLETYLAINE KGKIGKEKRE AIIAKNRNVF DRLSDMSVNA IKYRLKEVVN YAALPDDTIK
LYKQYIDLNR ELANAKTDVK QKISKLTKLV VAKYPTLQES EIKGMVVNDK WHTAIVGGAI
SAAFDVTVDI EQQVTALVDR YARRLSDIDA SVRELEEKVN AHLAKMGFEL
//