ID D5EDF8_AMICL Unreviewed; 493 AA.
AC D5EDF8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=Amico_0449 {ECO:0000313|EMBL:ADE56590.1};
OS Aminobacterium colombiense (strain DSM 12261 / ALA-1).
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Aminobacterium.
OX NCBI_TaxID=572547 {ECO:0000313|EMBL:ADE56590.1, ECO:0000313|Proteomes:UP000002366};
RN [1] {ECO:0000313|EMBL:ADE56590.1, ECO:0000313|Proteomes:UP000002366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12261 / ALA-1 {ECO:0000313|Proteomes:UP000002366};
RX PubMed=21304712;
RA Chertkov O., Sikorski J., Brambilla E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Aminobacterium colombiense type strain (ALA-
RT 1).";
RL Stand. Genomic Sci. 2:280-289(2010).
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; CP001997; ADE56590.1; -; Genomic_DNA.
DR RefSeq; WP_013047856.1; NC_014011.1.
DR AlphaFoldDB; D5EDF8; -.
DR STRING; 572547.Amico_0449; -.
DR REBASE; 25203; M.Aco12261I.
DR KEGG; aco:Amico_0449; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_013049_4_1_0; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000002366; 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 Methyltransferase {ECO:0000313|EMBL:ADE56590.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002366};
KW Transferase {ECO:0000313|EMBL:ADE56590.1}.
FT DOMAIN 8..134
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 145..453
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 493 AA; 56552 MW; A4E5BA65AD0A0B96 CRC64;
MSVNLEFEDK LWEMADKLRG NIQPSDYKDV VLGLIFLKYI SDSFEEKYNE LVAEEEGFEE
DRDAYVAENI FYVPPSARWD FIKKNAKQST IGQIIDDAMI TIERENRNLK GVLPKNYARP
ELDKAKLGEL VDLFSFNLGN KEAKAQDILG RVYEYFLGKF GSSEGEFYTP PSIVKLLVGM
IEPYKGRVYD PCCGSGGMFV QSSRFVEEHQ GRKDDIHIFG QEYTATTWRL CKMNLAIRGI
DGNLGARDAD TFGNDLHKNI RADYILANPP FNVSDYTLIP DDARWKYGIP PEKNANYAWI
EHIISKLSPT GVAGFVLANG SMSTTTKAEA EIRKNIIEAG LVDCIVTMPP NLFYNVTIPV
CLWFISKKRE NKQDKILFID ARKMGTMVTR KHREFSDGEI AKIYDTYHNW RDNKKEYKDI
QGFCKSADIE EVREHEYILT PGRYVGIEEV EDDGEPFEEK MTRLTGELAE MFAKSHKLEE
EIKQRLGAIG YEF
//
