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Database: UniProt
Entry: A0A105TSR8_9FLAO
LinkDB: A0A105TSR8_9FLAO
Original site: A0A105TSR8_9FLAO 
ID   A0A105TSR8_9FLAO        Unreviewed;       520 AA.
AC   A0A105TSR8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=AP058_00035 {ECO:0000313|EMBL:KVV16419.1};
OS   Flavobacterium sp. TAB 87.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1729581 {ECO:0000313|EMBL:KVV16419.1, ECO:0000313|Proteomes:UP000059935};
RN   [1] {ECO:0000313|EMBL:KVV16419.1, ECO:0000313|Proteomes:UP000059935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAB87 {ECO:0000313|EMBL:KVV16419.1,
RC   ECO:0000313|Proteomes:UP000059935};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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:KVV16419.1}.
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DR   EMBL; LLWK01000015; KVV16419.1; -; Genomic_DNA.
DR   RefSeq; WP_066305368.1; NZ_LLWK01000015.1.
DR   AlphaFoldDB; A0A105TSR8; -.
DR   STRING; 1729581.AP058_00035; -.
DR   REBASE; 151244; M.Fsp87ORF35P.
DR   PATRIC; fig|1729581.3.peg.36; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000059935; 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:InterPro.
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; 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; PF12161; HsdM_N; 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:KVV16419.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059935};
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:KVV16419.1}.
FT   DOMAIN          9..167
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          178..482
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   520 AA;  58514 MW;  81E967972D81E0C7 CRC64;
     MAAEQKQKLE QQLWNIANTL RGKMDADDFR DYILGFIFYK YLSTKMDMYA NQILQPDGLT
     FSDIIGHADE ALLMQAVKEL AIDKLGFFLE PSELFSELAH RGNAGGKNNF ILGDLAKVLT
     HIEQSTMGSE SEEDFGNLFS DLDLTSHKLG KSESDKNELI VKVLTHLDEI DFDLENTDSD
     VLGDAYEYLI GQFASGAGKK AGEFYTPQQV SSVLAQLVTV GKDKLKSVYD PTCGSGSLLL
     RVAKEVKDVS EFYGQEMNPT TYNLCRMNMI MHDVHYKRFD IKNEDTLERP QHLDMRFEAI
     VANPPFSANW SASPLFMTDE RFSAYGKLAP SSKADFAFVQ HMVHQLDDNG TMAIVLPHGV
     LFRGGAEGHI RKYLIEDKNY LDAVIGLPAN IFYGTSIPTC ILVLKKIRQN SEDVLFIDAS
     QHFDKVKTQN VLLDEHIAKI ISTYSNRTEE EKYSKIATLD FIAAQDYNLN IPRYVDTFET
     EESIDINAIA NELQAVDQHI SETDKTIASF CAELNIVTPF
//
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