ID A0A1G8LFN1_9FLAO Unreviewed; 522 AA.
AC A0A1G8LFN1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05421846_10986 {ECO:0000313|EMBL:SDI54435.1};
OS Chryseobacterium taeanense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=311334 {ECO:0000313|EMBL:SDI54435.1, ECO:0000313|Proteomes:UP000198869};
RN [1] {ECO:0000313|Proteomes:UP000198869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17071 {ECO:0000313|Proteomes:UP000198869};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNDW01000009; SDI54435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8LFN1; -.
DR STRING; 311334.SAMN05421846_10986; -.
DR OrthoDB; 32195at2; -.
DR Proteomes; UP000198869; Unassembled WGS sequence.
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:SDI54435.1};
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:SDI54435.1}.
FT DOMAIN 150..245
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
SQ SEQUENCE 522 AA; 60232 MW; F5DA5F41376CDC82 CRC64;
MSLQFPLPTN DEDPSVYADR LGNYYSDLVT TTHKKENGQY FTSINLANFI ADFNKIHKKK
IKILDPGCGI GILSTVLIQK LAFKENIKNI ELIAFENDPD ILTLTEANYE YLRNWLSERN
ISFSYYLCKN DFILHNSSVL EGEKVFSPEF DIVISNPPYF KLSKDDTRKK IAKSVIYGQS
NIYTIFMAIS ARLLKSNGQL IFIIPRSFCS GSYFRLFREK FLEYVNLNAI HVFDSRDKAF
KKDNVLQENI ILSASRNEKL DDYNVLLSSS MDLSDISKSF SKSYLISNLI DFKSEQKIIH
IPLTDKDDEI IKLFKSWNGS LKKYELEVST GPIVDFRNKE LIRFAEGSDT VPLIWLHNIY
PMQILWPNYK IKGKPKGQYV VDNEFTQKCL VSKGNLILIR RFSSKDDLKR IIAAPITKDF
FNNFGKIGIE NHLNYVYSKT NTLSITQTYG IAAILNSKIL DLYFRTFNGN INVSATELKN
LPLPAFEIIE RIGLKILKCI QNGREYNIDI IVNENFEIPI YK
//
