ID S7WTK4_ACIJU Unreviewed; 761 AA.
AC S7WTK4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=L292_2463 {ECO:0000313|EMBL:EPR86516.1};
OS Acinetobacter junii CIP 107470 = MTCC 11364.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217666 {ECO:0000313|EMBL:EPR86516.1, ECO:0000313|Proteomes:UP000018420};
RN [1] {ECO:0000313|EMBL:EPR86516.1, ECO:0000313|Proteomes:UP000018420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTCC 11364 {ECO:0000313|EMBL:EPR86516.1,
RC ECO:0000313|Proteomes:UP000018420};
RA Khatri I., Singh N.K., Subramanian S., Mayilraj S.;
RT "Genome assembly of Acinetobacter junii MTCC 11364.";
RL Submitted (MAY-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:EPR86516.1}.
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DR EMBL; ASYZ01000053; EPR86516.1; -; Genomic_DNA.
DR RefSeq; WP_004914908.1; NZ_KB849610.1.
DR AlphaFoldDB; S7WTK4; -.
DR PATRIC; fig|1330047.3.peg.1067; -.
DR Proteomes; UP000018420; 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:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
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 PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 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:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EPR86516.1};
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:EPR86516.1}.
FT DOMAIN 9..143
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 154..465
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 761 AA; 85672 MW; 55A8A21C38BB9274 CRC64;
MTNNNFSQIA SFIWSVADLL RGDFKQSQYG RIILPFTLLR RLECVLEQSK AAVLAEHEKV
SKLNLPEEAQ EKLLLRATNG LAFFNTSPMD LSKMGQSDIK ANLSTYVQSF SKDAREIFEY
FNFIEFAGLL DDANLLYKVV QKFATTDLSP KNVSNHDMGL VFEELIRRFA ESSNETAGEH
FTPRDIVRLT TALVFMEDDD VLTKDGIIRT IYDPTAGTGG FLSSGMEYLH ELNPNAVMRA
FGQELNPESY AICKADMLIK GQDVSRIKLG NTLSNDQLTV DQFDYMLSNP PFGVDWKKIE
QDIKDEHEHK GFNGRFGAGL PRVSDGSLLF LMHLISKMRD ASSSESGSRI GIILNGSPLF
TGSAGSGESE IRRYILEADL LEAIIALPND MFYNTGIATY IWVLSNKKAA ERKGKVQLIN
ASNLSTKMRK SLGSKRNYLT ETEIATITQN YGDFVAVDTL AQDGETEQQK PFASKIFDSH
EFGYRRMTIE RPLRLSAQIT DSAIAALRFA PKPFNAVMQS IDAQLGTAFG TAWTAETYGQ
LQDVALEVRA LIKAEFPELK EKDIKEVLDS KIWLFQKALM EKAQALQNVI GTEQFDDFNQ
FDEVLKKALK QTDIKLDAKE KKQLLDAITW KNPEAEPVIS KVLKHAENPL YGQFSYQGKV
VEFVQDGDLR DAENIALNPK VSTTELIEDY FKREVQPHVA DAWINADKRD EKDSEIGIVG
YEIPFNRHFY VYQPPRNLAD IDADLDAVSA EIMQLLQEVH S
//
