ID Q2LV08_SYNAS Unreviewed; 515 AA.
AC Q2LV08;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=SYN_00494 {ECO:0000313|EMBL:ABC77915.1};
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC77915.1, ECO:0000313|Proteomes:UP000001933};
RN [1] {ECO:0000313|EMBL:ABC77915.1, ECO:0000313|Proteomes:UP000001933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB {ECO:0000313|EMBL:ABC77915.1,
RC ECO:0000313|Proteomes:UP000001933};
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC77915.1; -; Genomic_DNA.
DR RefSeq; WP_011417936.1; NC_007759.1.
DR AlphaFoldDB; Q2LV08; -.
DR STRING; 56780.SYN_00494; -.
DR REBASE; 11846; M.SacSBORF493P.
DR KEGG; sat:SYN_00494; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_013049_4_1_7; -.
DR InParanoid; Q2LV08; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000001933; 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; -; 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; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000001933}.
FT DOMAIN 12..135
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 154..474
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 515 AA; 58043 MW; E18F5D1A5B324CAA CRC64;
MANNNNKTEA FEKTLFKAAD KLRKNMDAAE YKHIVLGLIF LKYISDSFEA LYEKIKEGKG
DFEGADPEDP DEYRAENVFF VPQAARWSYL HSRAKLPSIG KDVDDAMEAI EKENQTLKGI
LPQVYARPNL DKAALGGLID LVGNIALGTE AAKAKDLLGR VYEYFLGEFA NAEGKKGGQF
YTPKSIVRLM VEMIEPFKGR VYDPCCGSGG MFIMSERFVE NHQGKVDDIS IFGQESNQTT
YRLCRMNLAI RGIDGSQVKW NTEGSFLNDV HKDLKSDFIL ANPPFNDSDW SGQLLQSDPR
WKYGVPQAAN ANFAWLQHMI YHLSPKGIMA CVLANGSLSS QTNNEGEIRK SLVENDLVDC
IVALPKQLFY NTGIPACLWF LSRKRAGNGD RKRSSEILFI DASEEGFMED RTHRAFSDDD
IAKIAGTYHE WRKQGGKYED VRGFCKSADI EEITKHNFVL MPGRYVGIKD EEDDGIPFED
KMAGYLSELS IQMAEEKRLD EEIKKQLGNI GLKLK
//
