DMA_TREPA
ID DMA_TREPA Reviewed; 303 AA.
AC O33844;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=DNA adenine methylase;
DE EC=2.1.1.72;
DE AltName: Full=DNA adenine methyltransferase;
DE AltName: Full=Deoxyadenosyl-methyltransferase;
DE AltName: Full=M.TpaI;
GN Name=dam {ECO:0000303|PubMed:9345771}; OrderedLocusNames=TP_0810;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Nichols;
RX PubMed=9345771; DOI=10.1111/j.1574-6968.1997.tb12694.x;
RA Stamm L.V., Greene S.R., Barnes N.Y., Bergen H.L., Hardham J.M.;
RT "Identification and characterization of a Treponema pallidum subsp.
RT pallidum gene encoding a DNA adenine methyltransferase.";
RL FEMS Microbiol. Lett. 155:115-119(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
RN [3]
RP NOMENCLATURE, AND SUBTYPE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
CC -!- FUNCTION: An alpha subtype methylase that recognizes the double-
CC stranded sequence 5'-GATC-3' and methylates A-2 on both strands
CC (Probable) (PubMed:12654995). Directly involved in methyl-directed DNA
CC mismatch repair, DNA replication, and gene expression (By similarity).
CC {ECO:0000250|UniProtKB:P0AEE8, ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:9345771}.
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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF006263; AAB82782.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65779.1; -; Genomic_DNA.
DR PIR; H71277; H71277.
DR RefSeq; WP_010882255.1; NC_021490.2.
DR AlphaFoldDB; O33844; -.
DR SMR; O33844; -.
DR IntAct; O33844; 1.
DR STRING; 243276.TPANIC_0810; -.
DR EnsemblBacteria; AAC65779; AAC65779; TP_0810.
DR GeneID; 57879328; -.
DR KEGG; tpa:TP_0810; -.
DR eggNOG; COG0338; Bacteria.
DR HOGENOM; CLU_063430_0_0_12; -.
DR OMA; MNRHGFN; -.
DR OrthoDB; 1206955at2; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1020.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR012263; M_m6A_EcoRV.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR30481; PTHR30481; 2.
DR Pfam; PF02086; MethyltransfD12; 2.
DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00571; dam; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA replication; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..303
FT /note="DNA adenine methylase"
FT /id="PRO_0000087998"
FT BINDING 13
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 303 AA; 33919 MW; 62D2155EAE22DB90 CRC64;
MSRSDTARPF VKWAGGKRAL APTLFAHMPQ TFGSYFEPFV GGGALFWHLC ACTRVRLHDI
YLSDINWPLL CAYAAVRDRV EELIVRVGQH IACHTPTYYR LARRKFAVCE HPLEVAALFL
YLNRSCYNGL YRVNKAGQFN VPLGRAAPAS PFLNTTAPTP RSTQPAAQVG HLAIRIDEEN
LRSCARALAN TTLNCQHFSC IQPARGDFVY LDPPYLGTFS AYDKTGFDRA AHESLAAFCM
HLDARGVLFM LSNSDCPEVR AWYRPFRVQQ LNAPRCIARS AHARGKRCEV LITNYPCADT
ATP
