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Database: UniProt
Entry: Q30T65_SULDN
LinkDB: Q30T65_SULDN
Original site: Q30T65_SULDN 
ID   Q30T65_SULDN            Unreviewed;       669 AA.
AC   Q30T65;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=Suden_0537 {ECO:0000313|EMBL:ABB43816.1};
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=326298 {ECO:0000313|EMBL:ABB43816.1, ECO:0000313|Proteomes:UP000002714};
RN   [1] {ECO:0000313|EMBL:ABB43816.1, ECO:0000313|Proteomes:UP000002714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251 {ECO:0000313|Proteomes:UP000002714};
RX   PubMed=18065616; DOI=10.1128/AEM.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(2008).
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; CP000153; ABB43816.1; -; Genomic_DNA.
DR   RefSeq; WP_011372170.1; NC_007575.1.
DR   AlphaFoldDB; Q30T65; -.
DR   STRING; 326298.Suden_0537; -.
DR   REBASE; 11531; SdeAORF537P.
DR   KEGG; tdn:Suden_0537; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_015410_1_0_7; -.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000002714; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF02384; N6_Mtase; 2.
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:ABB43816.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002714};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          335..482
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          487..601
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   669 AA;  75335 MW;  5719B3AF1D9BF2A8 CRC64;
     MALYKLEDHV NDWVKAKLEA LNLKNQKDYH TESAIPDYLK EALQGRAKTE KKTNFGKPDF
     SITKYKQAPI VIENKLGLKK LIEETKDGVK FDEKSISNYA VNGALYYATG MIASGKYHEV
     IAIGIAGDGD DAIELKVYYV YGSGENSFKL LENVSTLDFL ENQKTFDVFY KDAILTEDEK
     HEILIKSQAE LQKYSKSLNK LMHNHNITAP QRVLYVSGML LSMQNVVDTK GTKIQDGLVP
     QDLKGVQTES KRDAIQIVNQ IKEFLTARNI PIEKQNLMLS SFYEISKDVQ RDELEILDKE
     VSKLIDGKAS INKQIFTFIY HNIFLSIDAM AGHLDIMGEM YSEFLKYALG DGKEIGIVLT
     PPYITKMMTT ILGVNQNSKV MDLATGSAGF LISSMEMMID DAEANYGKET TAAKKKIDII
     KKEQLLGVEL NAEMFTLAAT NMILRGDGSS NIHKGNTFNT PEQLYTSFKA NKLLLNPPFS
     YDENGMPFIA FGLDKMEKGG LGAIIIQDSA GSGKATKSNQ AMLKKHTLKA SIKMPTDLFQ
     PMAGVQTSIY VLEAHKPHDF EQTVKFIDFR NDGYKRTSRA LQEIDEPTKR YADIVKIYKA
     GKNAKVEAPW NLNEVYIEDF ITPSGSDWNF DQHKTIDSKP TLEYFKKTVS DYLSWEVSNI
     LKQRGDKGK
//
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