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Database: UniProt
Entry: C7NCK7_LEPBD
LinkDB: C7NCK7_LEPBD
Original site: C7NCK7_LEPBD 
ID   C7NCK7_LEPBD            Unreviewed;       691 AA.
AC   C7NCK7;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
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=Lebu_1991 {ECO:0000313|EMBL:ACV39853.1};
OS   Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
OS   10249 / C-1013-b).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=523794 {ECO:0000313|EMBL:ACV39853.1, ECO:0000313|Proteomes:UP000001910};
RN   [1] {ECO:0000313|EMBL:ACV39853.1, ECO:0000313|Proteomes:UP000001910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b
RC   {ECO:0000313|Proteomes:UP000001910};
RX   PubMed=21304648; DOI=10.4056/sigs.1854;
RA   Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA   Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA   Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT   b).";
RL   Stand. Genomic Sci. 1:126-132(2009).
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; CP001685; ACV39853.1; -; Genomic_DNA.
DR   RefSeq; WP_015770191.1; NC_013192.1.
DR   AlphaFoldDB; C7NCK7; -.
DR   STRING; 523794.Lebu_1991; -.
DR   REBASE; 21855; M.LbuDORF1991P.
DR   KEGG; lba:Lebu_1991; -.
DR   eggNOG; COG0827; Bacteria.
DR   HOGENOM; CLU_025185_0_0_0; -.
DR   OrthoDB; 9815272at2; -.
DR   Proteomes; UP000001910; Chromosome.
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   CDD; cd02440; AdoMet_MTases; 1.
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   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR   Pfam; PF07669; Eco57I; 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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:ACV39853.1};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACV39853.1}.
FT   DOMAIN          333..440
FT                   /note="Type II methyltransferase M.TaqI-like"
FT                   /evidence="ECO:0000259|Pfam:PF07669"
SQ   SEQUENCE   691 AA;  82482 MW;  5518517FBE7CDE3F CRC64;
     MNKKIVILQE ILDYQEKIFN FIKREEFFLE TSLNEEKLLK LISGLAIISS IYEKFTTKLI
     TIYCDIFMKT EKEKDGIIQN NKSIGNLSKM IKELKLEVDE MYRLLKLNND FEKNDILKKD
     SNLLTYGDLI VHMNKIYQKR NKYVHGAFEI NENIDKEKFE KYVLDTLDKE SAILLVLKNA
     FISKIPYYLI EKEELTKNYK KYEELYNNFF ENIDNEIIKE KSQFFTPIAI SQKLVDDLKH
     LNKKFEKENI KILDPSCGFG ILTINLLEKI VEISSDSNKR INKIEVDMID IDEKCIENCK
     IIMKEFLEKN NLNDLVEVNY IIGNYLNYEI KRKYDFIVQN PPFKKIKKEE KVKYDGEITK
     YINGQANLYH LFIIKSLKLL DEKGILFTIS PKNFLSGKYT ENLRKFLFNN YSLTRLHLFD
     ERKKIFKNII QEICITQIEK RKHKNIKISY NGSKPFELDR EILFLKRKNN ILLSPRNREE
     SNFIKSINEI FVKNNVFSFH PGKVVQFRVD KKNLSSEKFN KEKKQVPLLV PKHLKNERIE
     YEDLDKKKNK SISIFYNEET QNLFLKNKRY IILNKNSGKE EKKLIKPVLY DGIFDIEYIA
     LDNNLAYIEF FDNNVSDFIF YGVFCVLNSK QFDNYYRMIN GSHTLNSYEF QNLLFPKKEI
     LEKIGLEYLN TKKENSIEMC SEIFEKYIKN K
//
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