ID A0A069DKD8_9BACL Unreviewed; 514 AA.
AC A0A069DKD8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=TCA2_5383 {ECO:0000313|EMBL:GAK42890.1};
OS Paenibacillus sp. TCA20.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1499968 {ECO:0000313|EMBL:GAK42890.1, ECO:0000313|Proteomes:UP000028160};
RN [1] {ECO:0000313|EMBL:GAK42890.1, ECO:0000313|Proteomes:UP000028160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCA20 {ECO:0000313|EMBL:GAK42890.1,
RC ECO:0000313|Proteomes:UP000028160};
RA Fujinami S., Takeda-Yano K., Onodera T., Satoh K., Sano M., Takahashi Y.,
RA Narumi I., Ito M.;
RT "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain TCA20,
RT Isolated from a Hot Spring Containing a High Concentration of Calcium
RT Ions.";
RL Genome Announc. 2:e00866-14(2014).
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:GAK42890.1}.
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DR EMBL; BBIW01000016; GAK42890.1; -; Genomic_DNA.
DR RefSeq; WP_047913917.1; NZ_BBIW01000016.1.
DR AlphaFoldDB; A0A069DKD8; -.
DR SMR; A0A069DKD8; -.
DR REBASE; 94991; M.PspTCA20ORF5383P.
DR eggNOG; COG0286; Bacteria.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000028160; 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004546; Restrct_endonuc_T1M.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR NCBIfam; TIGR00497; hsdM; 1.
DR PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000028160};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 174..471
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 514 AA; 59059 MW; 8AF0E9F7A4FDB0E7 CRC64;
MISSQRLELY NHLWARLESM RGFLEESAIR DYFLGIICYG YLSHKIEDRV SNSLLYDKCS
FEEAWKNEEM RNSIREELVS TLGYVIEPQY LFSTMVSQIK KSLFNVGYFQ LGIECFNRSI
KGADSEHSLR YLFANMELSA SLLRNLVNSE SNFMTDVMVA IYDLLFASDN IDPEFVGEAY
EFLISRFAES SGKKGGEFYT PPEISALIAK IVTADKDELR SVYDPTCGSA SLLLQIAKEA
KVGHFYGQEK MSTIYNMARM NMLLHEVAFN RFDIRNDDAL EQPKHLDMRF EAVVANPPYS
AKWSAHFHFL DDERFRSYGV LAPQSKADFA FIQHMIHQLD YKGILVAILP LGILFRGGPE
GKIRSFFVEK YNYIDAIIGL PPNLMYGTSI PVCIVVMKKS RETDDKVMFI DASHEYANGR
NQNQLRNVDV NKIVDTYINK KQIEHYSYLA TLDELKDNDY NLNISRYIDK DIENDIIDIT
SAERQLKGID RKIAEIDAVI KSKLKELGIV SKNL
//
