ID A0A0R2FI34_9LACO Unreviewed; 345 AA.
AC A0A0R2FI34;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=IV38_GL001303 {ECO:0000313|EMBL:KRN28305.1}, IV40_GL001090
GN {ECO:0000313|EMBL:KRN31807.1};
OS Lactobacillus selangorensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=81857 {ECO:0000313|EMBL:KRN28305.1, ECO:0000313|Proteomes:UP000051751};
RN [1] {ECO:0000313|Proteomes:UP000051645, ECO:0000313|Proteomes:UP000051751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-66 {ECO:0000313|EMBL:KRN28305.1,
RC ECO:0000313|Proteomes:UP000051751}, and DSM 13344
RC {ECO:0000313|EMBL:KRN31807.1, ECO:0000313|Proteomes:UP000051645};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN28305.1}.
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DR EMBL; JQAT01000003; KRN28305.1; -; Genomic_DNA.
DR EMBL; JQAZ01000003; KRN31807.1; -; Genomic_DNA.
DR RefSeq; WP_057769272.1; NZ_JQAZ01000003.1.
DR AlphaFoldDB; A0A0R2FI34; -.
DR STRING; 81857.IV38_GL001303; -.
DR PATRIC; fig|81857.3.peg.1311; -.
DR OrthoDB; 9813673at2; -.
DR Proteomes; UP000051645; Unassembled WGS sequence.
DR Proteomes; UP000051751; Unassembled WGS sequence.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF07669; Eco57I; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:KRN28305.1};
KW Helicase {ECO:0000313|EMBL:KRN28305.1};
KW Hydrolase {ECO:0000313|EMBL:KRN28305.1};
KW Nucleotide-binding {ECO:0000313|EMBL:KRN28305.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051645}.
FT DOMAIN 6..102
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
SQ SEQUENCE 345 AA; 39349 MW; 764D44EB8EEE28E6 CRC64;
MSKEFKFDVV IGNPPYQEEV EGTSDKQIFP YFMDQAYKIG KKVELITPAK FLSNAGKTPK
KWNEKMLKDP HLKVLFFEQD SSKVFSNTDI KGGVCVTYRD VDSSFGAIGT FTPYAELNSI
LKKVKTSNFK SFSELIYAPE SYKLTQKLHD DFPDIGSRLS KGHKFDITTN IFDKLGDIFQ
NVKPSGSSEQ YVGLYGRQNN RRTLKWIKSK YVKGPDNLEN YKILVPKSNG SGALGEVLTT
PLIGEPLIGG TQTFITIGNF QDINCTKAAM KYIKSKFARA MLGTLKVTQD NKKRTWVNVP
LQDFTQHSDI DWSKSIHEID QQLYKKYRLN QEEISFIETK VKEMD
//
