ID A0A2K8UDJ1_9GAMM Unreviewed; 521 AA.
AC A0A2K8UDJ1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=THSYN_22805 {ECO:0000313|EMBL:AUB83499.1};
OS Candidatus Thiodictyon syntrophicum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiodictyon.
OX NCBI_TaxID=1166950 {ECO:0000313|EMBL:AUB83499.1, ECO:0000313|Proteomes:UP000232638};
RN [1] {ECO:0000313|EMBL:AUB83499.1, ECO:0000313|Proteomes:UP000232638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cad16T {ECO:0000313|EMBL:AUB83499.1,
RC ECO:0000313|Proteomes:UP000232638};
RA Luedin S.M., Pothier J.F., Danza F., Storelli N., Wittwer M., Tonolla M.;
RT "Complete genome sequence of Candidatus 'Thiodictyon syntrophicum' sp. nov.
RT strain Cad16T, a photolithoautotroph purple sulfur bacterium isolated from
RT an alpine meromictic lake.";
RL Submitted (MAR-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}.
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DR EMBL; CP020370; AUB83499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8UDJ1; -.
DR REBASE; 226740; M.Tsy16TORF22805P.
DR KEGG; tsy:THSYN_22805; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000232638; 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 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; 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; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AUB83499.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000232638};
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:AUB83499.1}.
FT DOMAIN 169..462
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 521 AA; 58446 MW; AB2161863FD5E238 CRC64;
MSPKKSAAPQ TTAQQLAAII KSARNTMRKD KGLNGDLDRL PMLTWIMFLK FLDDMELMRE
TNAQLAGQPF RPDLAPPYRW RDWGADPTGM TGEDLIAFVN NDEAMRPNGS RGAGLFYYLR
GLRSAAGADR RDVIGTVFRG MQNRMADGYL LREVINQINR IHFTATQEMH TLSRLYETLL
REMRDAAGDS GEFYTPRPAV RFMVQVMDPR LGETVLDPAC GTGGFLVEAF SHMQAQCRCV
ADEKTLQTAS IRGGEAKSLP YLLAQMNLLL HGLDHPQIDP GNSLRIPLRD ITDQDRVDLI
LTNVPFGGEE DRGILGNFPK DRQTAETALL FLQLIMRRIK RPGAGKDRGG RAGVIVPNGT
LFGDGIAARI KEDLLKHYNL HTIVRLPEGV FAPYTDIPSN LIFFDRSGPT RDIWYYQVSL
PEGKRKFTKT KPMEDGDFAD CLAWWSDRAE GPNAWRVSSA DVLKYDSEGR LMSVNLDIKN
PHSLEALEHR EPEELVESIL AKENEVLQLL LQMKADLSAA L
//
