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Database: UniProt
Entry: F4LMV9_TREBD
LinkDB: F4LMV9_TREBD
Original site: F4LMV9_TREBD 
ID   F4LMV9_TREBD            Unreviewed;       509 AA.
AC   F4LMV9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
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=Trebr_2442 {ECO:0000313|EMBL:AEE17849.1};
OS   Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE17849.1, ECO:0000313|Proteomes:UP000006546};
RN   [1] {ECO:0000313|Proteomes:UP000006546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC   {ECO:0000313|Proteomes:UP000006546};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA   Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA   Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Treponema brennaborense DSM 12168.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002696; AEE17849.1; -; Genomic_DNA.
DR   RefSeq; WP_013759550.1; NC_015500.1.
DR   AlphaFoldDB; F4LMV9; -.
DR   STRING; 906968.Trebr_2442; -.
DR   REBASE; 35680; M.Tbr12168ORF2442P.
DR   KEGG; tbe:Trebr_2442; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_018284_4_0_12; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000006546; 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   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.20.1260.30; -; 1.
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; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI 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.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AEE17849.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006546};
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:AEE17849.1}.
FT   DOMAIN          20..146
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          157..471
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          481..508
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   509 AA;  58007 MW;  E947ED9BBFB1A7ED CRC64;
     MNGDALVKST TKIMFGDAGV SGTAQYMSQL IWILFLKVFD AKEEEWELKK GYVPVIPEGF
     RFRDWADLRK EDGSKDLANR LTGDKLIQFV NNTLFPFLQG KPVSVNDKEH LFTSDDPKAL
     IVREFMGESQ NYMKDGVKLR QLVNEIADID FDDAGIKHDF NDFYETLLKG LQNGGKATGE
     FYTPRAITKF ICDHVDPKIG ERVADFACGT GGFLAEAISH LMAQAKSPKD ITTIQNSIYG
     IEWKQLPYML ATTNMLLHDI DNPDIVHGDG LALNVLNLQP KDKYNCILMN PPFGGEFNKS
     DLQNFPDDLA SSESADLFVA RIIYCLEKDG RCGLVLPDGL LFNSDNSKVN LKKKLMTECN
     LHTIIRLPSS VFAPYTSINT NLLFFDKTGK TEEIWFYRMD MPEGVKHFNK TNPIKREDMK
     CVDEWWNNRV EIADEKESET STQTFKAKKY TFAEIEERGF DLDLCGYPEE EDVVLTPEET
     IKNYKERRES LEAKLDEKLA LIMNLLEVK
//
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