ID   B3PQK5_RHIE6            Unreviewed;       830 AA.
AC   B3PQK5;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
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=RHECIAT_CH0000865 {ECO:0000313|EMBL:ACE89851.1};
OS   Rhizobium etli (strain CIAT 652).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916 {ECO:0000313|EMBL:ACE89851.1, ECO:0000313|Proteomes:UP000008817};
RN   [1] {ECO:0000313|EMBL:ACE89851.1, ECO:0000313|Proteomes:UP000008817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652 {ECO:0000313|EMBL:ACE89851.1,
RC   ECO:0000313|Proteomes:UP000008817};
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA   Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA   Palacios R., Davila G.;
RT   "Genome diversity and DNA divergence of Rhizobium etli.";
RL   Submitted (APR-2008) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001074; ACE89851.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3PQK5; -.
DR   REBASE; 18154; M.RetCI.
DR   KEGG; rec:RHECIAT_CH0000865; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_013049_6_0_5; -.
DR   Proteomes; UP000008817; 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   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; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004546; Restrct_endonuc_T1M.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   NCBIfam; TIGR00497; hsdM; 1.
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.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:ACE89851.1};
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:ACE89851.1}.
FT   DOMAIN          28..139
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          154..460
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          655..686
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   830 AA;  92633 MW;  BFF33EC94FC550D0 CRC64;
     MPRKIEGLLL RHPWNEDRMA IKKSDIYRSL WDSCDQLRGG MDASLYKDYI LTLLFVKYVS
     DRAAQADALI EVPKGCSFDD LRKLRGSKDI GEGIDKAIAG IAEANDLKNV IDRAFFNDAE
     KFGRGEKMVK TLTALINIFS REELNFSRNR ADGDDILGDA YEYLMRNFAT ESGKSKGQFY
     TPAEVSRVVA AVAGINRANS PRQTVYDPTC GSGSLLLKAA DAASVELTIY GQEFDITTRG
     LAKMNMIMHG REDAEIAQGD VIADPQFRAS ETAIQTFDFV VANPPFSTKA WSSGLTANNR
     FGRFDIGMPP EKNGDFAFLL HILASMKATG SGAVILPHGV LFRGNKEAEL REKILKRGYV
     KAIIGLPANL FYGTGIPATI IVLDKSGACD RRPVFMIDAS RGFIKDGNKN RLRERDIHKI
     IDVYARQVEI KGYSSLVSYD DITRSDFNLN IARYIDGADP EDLQDIEAHL KGGVPDRDID
     LLDDFWKVMP SVRSALFGPN PRPAYSDPLV EPEDVRATIR KHPEFSAFRD CVHTIHDGWA
     RANAPVLHGI RPGDNPKTLI HTIAEDMLRR FIDAPLIDQY EAYQRLMTYW STVMQDDVFI
     IAHDGWAAAK ELREARKEVD KDNKVKWLED ADLTMNKVRL VADVIKPGLI VARFFPEMQT
     ALEDAQAKAE ELAREIEELV EEHGSEGALL ADALTEAGKL TAASVKARIK AEEAEPEEVK
     LLKQAAKLID AETAAKRAVK EAEDALTQAT LKKYPRLKED EIRSLVVDDK WLTDIAKLIE
     AEIEARTEQL TARVRVLTER YGHTLPEIST RMVELEAKVS EHLIALGFSA
//