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Database: UniProt
Entry: A0A1Y4J0U2_9FIRM
LinkDB: A0A1Y4J0U2_9FIRM
Original site: A0A1Y4J0U2_9FIRM 
ID   A0A1Y4J0U2_9FIRM        Unreviewed;       492 AA.
AC   A0A1Y4J0U2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=B5F28_11395 {ECO:0000313|EMBL:OUP23421.1};
OS   Gemmiger sp. An194.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Gemmiger.
OX   NCBI_TaxID=1965582 {ECO:0000313|EMBL:OUP23421.1, ECO:0000313|Proteomes:UP000196090};
RN   [1] {ECO:0000313|Proteomes:UP000196090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An194 {ECO:0000313|Proteomes:UP000196090};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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:OUP23421.1}.
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DR   EMBL; NFKA01000019; OUP23421.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4J0U2; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000196090; 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; 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   InterPro; IPR038333; T1MK-like_N_sf.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI 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   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:OUP23421.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196090};
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:OUP23421.1}.
FT   DOMAIN          4..133
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          145..449
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   492 AA;  56289 MW;  4061CA1FACA2B96B CRC64;
     MSNLTGFVKR LRDIMRNDAG INGDAQRIEQ IAWMLFLKVY DAKEQDWEWD DEAYRSIIPE
     ECRWQNWAHD DKSGTALTGD RLLDFVNNKL FPTLKSLPVS ASTPIKKAIV QTTFADANNY
     MKDGVLLRQV INVIDDLDFS DYEESHAFGE IYETILKELQ SAGSAGEFYT PRAVTDFMAQ
     VIRPKIGETM ADFACGTGGF IISWLKELQK QIKSTADAEK YSNSIYGIEK KQFPYMLCVT
     NLLLHGLDVP QVYHANTLLH DVLDYTEDDK VDVVLMNPPY GGNEKADVKN HFPGDLASSE
     TADLFMSVIM YRLKKNGRAA VILPDGFLFG TDNAKVNIKK KLMREFNLHT IIRLPGSVFS
     PYTSITTNIL FFDNTHSTEE TWFYRLDMPE GYKHFSKTKP MKMEHFQPVL DWWNDRQELA
     EDGFDKAKKY TAQQLTEELG YNLDQCGYPH EEEEILAPMD LIQRYEEQRA SLNAEIDRVL
     AEITSLLGGN AE
//
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