ID S4YG11_SORCE Unreviewed; 506 AA.
AC S4YG11;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=SCE1572_49355 {ECO:0000313|EMBL:AGP41808.1};
OS Sorangium cellulosum So0157-2.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP41808.1, ECO:0000313|Proteomes:UP000014803};
RN [1] {ECO:0000313|EMBL:AGP41808.1, ECO:0000313|Proteomes:UP000014803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP41808.1,
RC ECO:0000313|Proteomes:UP000014803};
RX PubMed=23812535; DOI=10.1038/srep02101;
RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT milieu.";
RL Sci. Rep. 3:2101-2101(2013).
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; CP003969; AGP41808.1; -; Genomic_DNA.
DR RefSeq; WP_020741701.1; NC_021658.1.
DR AlphaFoldDB; S4YG11; -.
DR STRING; 1254432.SCE1572_49355; -.
DR REBASE; 66710; M.Sce1572ORF49355P.
DR KEGG; scu:SCE1572_49355; -.
DR PATRIC; fig|1254432.3.peg.11133; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_018284_2_0_7; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000014803; 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; 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 Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..114
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 126..417
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 506 AA; 56303 MW; A7F3CAEC9D28CA85 CRC64;
MSNPSAQIVQ KLWSYCNVLR DDGLSYGDYV EQLTFLLFLK MAHERTQPPW NHKPFIPAGH
DWPALLAKDG DALEVQYRKT LDHLGRQPGM LGLIFRKAQN KIQDPAKLRR LVADLIDREQ
WTTLDADVKG DAYEGLLEKN AQDTKGGAGQ YFTPRPLIQA IVEVMRPGPD DTICDPACGT
GGFLLAAHDH IVRTHPSLTR DQKKHLKLGA LRGVELVPGV TRLCAMNLLL HGIGPSAEEG
QPPVETRDSL AADPGSRYSM VLTNPPFGKK SSVMVLTEEG DEAREALTVT REDFWATTSN
KQLNFVQHVK TILAIHGRAA VVVPDNVLFE GGAGETIRRK LLHDCDVHTL LRLPTGIFYA
QGVKANVLFF DKKPASEKPW TKKLWIYDLR TNQHFTLKTN PLSRADLDDF VACYKPGELH
KRRATWSEKN PAGQWRAYEV AELTARDKCS LDVFWLKDES LEASENLPAP DVIAGEIVED
LRAALEQFEA VEADLRARAS GASAAP
//
