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Database: UniProt
Entry: E0TGZ7_PARBH
LinkDB: E0TGZ7_PARBH
Original site: E0TGZ7_PARBH 
ID   E0TGZ7_PARBH            Unreviewed;       504 AA.
AC   E0TGZ7;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   OrderedLocusNames=PB2503_05832 {ECO:0000313|EMBL:ADM09237.1};
OS   Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC 12087).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC   Parvularculaceae; Parvularcula.
OX   NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM09237.1, ECO:0000313|Proteomes:UP000001302};
RN   [1] {ECO:0000313|Proteomes:UP000001302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC   {ECO:0000313|Proteomes:UP000001302};
RA   Kang D.-M., Oh H.-M., Cho J.-C.;
RT   "Genome sequence of Parvularcula bermudensis HTCC2503.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADM09237.1, ECO:0000313|Proteomes:UP000001302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC   {ECO:0000313|Proteomes:UP000001302};
RX   PubMed=21037002; DOI=10.1128/JB.01205-10;
RA   Oh H.M., Kang I., Vergin K.L., Kang D., Rhee K.H., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2503T of Parvularcula bermudensis,
RT   the type species of the order "Parvularculales" in the class
RT   Alphaproteobacteria.";
RL   J. Bacteriol. 193:305-306(2011).
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; CP002156; ADM09237.1; -; Genomic_DNA.
DR   RefSeq; WP_013300211.1; NC_014414.1.
DR   AlphaFoldDB; E0TGZ7; -.
DR   STRING; 314260.PB2503_05832; -.
DR   REBASE; 27630; M.PbeHORF5832P.
DR   KEGG; pbr:PB2503_05832; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_013049_4_2_5; -.
DR   OrthoDB; 9806213at2; -.
DR   Proteomes; UP000001302; Chromosome.
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; IPR022749; D12N6_MeTrfase_N.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001302};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..144
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          159..468
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          465..499
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   504 AA;  57433 MW;  D3167C67F09D12CF CRC64;
     MNAQVKQDEI NKAVWEACDT FRGTVDAGVY KDYVLTMLFL KYLSDVWNDH YEEYKKEYGD
     EPELINEMMK NERFVLPESA NFYALYKRRH EAGNGERIDK ALHAIEEANI AKLRDVFQDI
     SFNSNKLGEE AHKNELLKEL LEDFAKDKLN LRPSRIGKLD IIGNAYEFLI KQFAADSGRK
     AGEFYTPPEV SELMAELVAP KEGDEICDPT CGSGSLLMKC GKRVQIENKG SKKYALYGQE
     AIGSTWALAK MNMFLHGEDN HRIEWGDTIR NPKLLDGEDS LKHFDVVVAN PPFSLEKWGH
     GTAEGDKFSR FRRGIPPKTK GDYAFILHMV ETMKPKSGRM AVVAPHGVLF RGSTEGKIRQ
     KLVEENLLDA VIGLPEKLFY GTGIPATILI LRKKKSDRNV LFIDASREFI SGKNQNQLSN
     NHIAKIVETY QARKSVDKYA YFATPEEMAE NDYNLNIPRY VDTFEEEEEI DLMAVRAERE
     KLKAELTDLE AQMDGYLKEL GYGS
//
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