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Database: UniProt
Entry: A0A0C5W5W8_9GAMM
LinkDB: A0A0C5W5W8_9GAMM
Original site: A0A0C5W5W8_9GAMM 
ID   A0A0C5W5W8_9GAMM        Unreviewed;       481 AA.
AC   A0A0C5W5W8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=H744_2c0119 {ECO:0000313|EMBL:AJR06881.1};
OS   Photobacterium gaetbulicola Gung47.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR06881.1, ECO:0000313|Proteomes:UP000032303};
RN   [1] {ECO:0000313|EMBL:AJR06881.1, ECO:0000313|Proteomes:UP000032303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gung47 {ECO:0000313|EMBL:AJR06881.1,
RC   ECO:0000313|Proteomes:UP000032303};
RA   Kim Y.-O.;
RT   "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT   gaetbulicola Gung47.";
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};
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DR   EMBL; CP005974; AJR06881.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C5W5W8; -.
DR   STRING; 658445.H744_2c0119; -.
DR   REBASE; 106415; M.Pga47ORF119P.
DR   KEGG; pgb:H744_2c0119; -.
DR   PATRIC; fig|658445.3.peg.2017; -.
DR   HOGENOM; CLU_013049_4_2_6; -.
DR   Proteomes; UP000032303; Chromosome 2.
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; 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; 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.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AJR06881.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032303};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          65..371
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   481 AA;  54311 MW;  616B064A903AD518 CRC64;
     MFNFAGIRKS LNKATEAIEE HNSSLEGVLV TIDFNIKNKL SDAKLRDLLS HFSQHRLRNE
     DFERPDMLGT AYEYLIKMFA DSAGKKGGEF YTPSEVVQLL VALLEPHAGM RIYDPTTGSG
     GMLVQTRNYL KEHGENPANL SLFGQEMNLN TWAICKMNMF LHGVQSADIR KGDTLREPKH
     TQGGELMSFD RVIANPPFSL KKWGKDECDN DGFGRFPYGT PPKDAGDLAF VQHMIASTNA
     EGMVGVVMPH GVLFRGSSEK AIRQGILEDD LLEVVVGLPS GLFYGTGIPA CLLIINKNKP
     ADRRGKVLFI NAELEFEEGK NQNKLREQDI SKIVETFNNY VDVKRYAKVV KYSEIAENDF
     NLNIRRYADT SPPAEIFDVR AILHGGVPIR EVHNEYIEEE VLAGFDASLV FDKTDNDYYA
     FKPSIARKEQ IREVAGEAEA KVITQLEHWW DKYQVSLHEL DLQVLDAEQE MQGYLKELGY
     E
//
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