ID U7V555_9FUSO Unreviewed; 513 AA.
AC U7V555;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=HMPREF0202_02627 {ECO:0000313|EMBL:ERT66279.1};
OS Cetobacterium somerae ATCC BAA-474.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Cetobacterium.
OX NCBI_TaxID=1319815 {ECO:0000313|EMBL:ERT66279.1, ECO:0000313|Proteomes:UP000017081};
RN [1] {ECO:0000313|EMBL:ERT66279.1, ECO:0000313|Proteomes:UP000017081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-474 {ECO:0000313|EMBL:ERT66279.1,
RC ECO:0000313|Proteomes:UP000017081};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERT66279.1}.
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DR EMBL; AXZF01000144; ERT66279.1; -; Genomic_DNA.
DR AlphaFoldDB; U7V555; -.
DR STRING; 1319815.HMPREF0202_02627; -.
DR PATRIC; fig|1319815.3.peg.2514; -.
DR eggNOG; COG0827; Bacteria.
DR HOGENOM; CLU_025115_1_0_0; -.
DR Proteomes; UP000017081; 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; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR Pfam; PF12950; TaqI_C; 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:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000017081};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..143
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT DOMAIN 315..457
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 513 AA; 61199 MW; 3ED30FBAB4960F2A CRC64;
MEYNYKIYTP EKYASSMSKV ALNKYLENNL KENILNIKVI DISCGSGNLL LAILEELLKI
SKEIFGEYKY SENWITGFDV DLNALKLLEK RAEALFFKYG VFGKLNLKEC DSLYEKIEEK
YDIVIGNPPY LGEKNHKEIF HTIKETDFGK KYYKPKMDYF YFFIDKGIDI LKDSGILVYL
TTNYWLKADS AEGIREKMKF EGSFFRLENY SYSIFKDAIG QHNIIFYWQK NRENLEISVN
DDGIEYSIEQ ENIFTEEHSK IALIPPFWKE NIKKIREKSN VVLGDLVNIN QGIVSGADKV
FVFDEYKEEF KKYLKPFYKN RDIGKYEISK KPPFWIMYLN GKSKLDDVVT NYLLDYKSKL
SMRREVINNR INWWELQWAR DEDIFLKPKI IVRQRCKTNN FAYTEKEFYG SADIYYLTAK
TEEVNLYYIL GYLNSKIFFS WFNYIGKKKG KNLEFYSTPL KESPLYYPTI QDEIRYIENL
VKKQLENYSE NIQDEIDNYF SKVMNIKKMS EEN
//
