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Database: UniProt
Entry: S3L278_TREMA
LinkDB: S3L278_TREMA
Original site: S3L278_TREMA 
ID   S3L278_TREMA            Unreviewed;       370 AA.
AC   S3L278;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=HMPREF9194_01209 {ECO:0000313|EMBL:EPF30884.1};
OS   Treponema maltophilum ATCC 51939.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=1125699 {ECO:0000313|EMBL:EPF30884.1, ECO:0000313|Proteomes:UP000014541};
RN   [1] {ECO:0000313|EMBL:EPF30884.1, ECO:0000313|Proteomes:UP000014541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51939 {ECO:0000313|EMBL:EPF30884.1,
RC   ECO:0000313|Proteomes:UP000014541};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Leonetti C., Blanton J.M.,
RA   Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Treponema maltophilum ATCC 51939.";
RL   Submitted (APR-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPF30884.1}.
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DR   EMBL; ATFF01000006; EPF30884.1; -; Genomic_DNA.
DR   RefSeq; WP_016525495.1; NZ_KE332518.1.
DR   AlphaFoldDB; S3L278; -.
DR   STRING; 1125699.HMPREF9194_01209; -.
DR   REBASE; 415758; M.Tma51939ORF1209P.
DR   PATRIC; fig|1125699.3.peg.1230; -.
DR   eggNOG; COG3392; Bacteria.
DR   HOGENOM; CLU_034356_0_0_12; -.
DR   OrthoDB; 9805629at2; -.
DR   Proteomes; UP000014541; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000014541}.
SQ   SEQUENCE   370 AA;  42108 MW;  F0FC33F0238FE4E4 CRC64;
     MQNENAEYLS DQLITYLGNK RRLLNFIGEA VDSVKKKLNK EKLRIFDVFS GSGIVSRYLK
     QSASYLAAND LELYSYLINT CYLSNSSERD MVQLRGFFCD LKEKLDECEF TGEWKRGVIS
     ELYAPEDDSN IKKGERVFYT KRNAAYIDTA RSFIDSYPER LRVFFIAPLL AAASVHANTG
     GVFKGFYKNR ETGIGEFGGK NRDALSRITG DIDLEFPVFS TYDCQVDIYR RDANELVLST
     AEVDLAYLDP PYNQHPYGSN YFMLNVIAEN KRPHNPSSVS GIPSDWNRSA YNTAKGAQKA
     LGELIENVRA KYVLLSFNSE GFTTKDELTC MMGSMGKLNV FESPYNAFRA SRNLKNRNAH
     VTEYLFLLEK
//
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