ID A8TX11_9PROT Unreviewed; 807 AA.
AC A8TX11;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=BAL199_18846 {ECO:0000313|EMBL:EDP62940.1};
OS alpha proteobacterium BAL199.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP62940.1, ECO:0000313|Proteomes:UP000003417};
RN [1] {ECO:0000313|EMBL:EDP62940.1, ECO:0000313|Proteomes:UP000003417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP62940.1,
RC ECO:0000313|Proteomes:UP000003417};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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:EDP62940.1}.
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DR EMBL; ABHC01000017; EDP62940.1; -; Genomic_DNA.
DR AlphaFoldDB; A8TX11; -.
DR STRING; 331869.BAL199_18846; -.
DR eggNOG; COG0286; Bacteria.
DR OrthoDB; 9806213at2; -.
DR Proteomes; UP000003417; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EDP62940.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003417};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 278..543
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 807 AA; 89202 MW; 20E3305768C7C04F CRC64;
MARVRVAEVR TEVLLTELLK AQGWDCRRPP NGEMLRQHEY KDHSHLRDVF LHRSKVRMIG
HGLPEAVVVD RQSMQPLIVI EAKASISDLD KALREATEIY GNACIDAGYS PLAVAIAGTS
EDDFAVRVHK WNGSAWKAVT YEGNPIGWIP NRVDVERLRV PSATPELRPS VPSPEVLANF
ADEINRLLRE SNVNDRSRPS VVGACMLALW QSKGALRKDP RNILGDINQA CEKAFWNAGK
AVLAKSLHVD EANDKLAVKA RRIISILERL NVSVLTAEHD YLGQLYETFF RYAGGNTIGQ
YFTPRHIASF GADLLGVSID DVVLDPTCGT GGFLIAAMER VAREHQISRS EMVKLVSTRL
IGFDDEPITA ALCVANMILR GDGSSSVHRG DAFTAPEYPI GTASVVLMNP PYPHKQTDTP
TEAFVERALE GLSQGSRLAA VIPLSLLVKS NKASWRKAIL KNNTLEAAIK LPDELFQPYA
QPYTVIVYLR KGIPHPKGKR AFFARIENDG FRIRKAVRVA CEGSELPKML AHFQAGTSEA
GVCGWSQVDE DASFGPGAYI PAKEMTGEES DDATQEVIRA RTSFVAYHAA DLVQLYTDNP
LDVRAMRKRP WQFQGVKLGT VAAYFDIYYG QKELHSKDGL LPGRSLVISS SKFDNGCYGL
FDFEHILKPP FVTVPGNGSI AYAHVQEWPC GVSDDCMLLL PKEGVSHSMM YVAAAAIRNE
RWRFSYGRKA TPDRIAEFPL PHTDELLARV DEYLARAARV EDRMIEDAED ALDSQTARMR
LADLGSGKAT AVSGAELETR LAAMMEN
//