ID N1WNI7_9LEPT Unreviewed; 601 AA.
AC N1WNI7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=LEP1GSC060_3739 {ECO:0000313|EMBL:EMY78812.1};
OS Leptospira weilii serovar Ranarum str. ICFT.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1218598 {ECO:0000313|EMBL:EMY78812.1, ECO:0000313|Proteomes:UP000012313};
RN [1] {ECO:0000313|EMBL:EMY78812.1, ECO:0000313|Proteomes:UP000012313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICFT {ECO:0000313|EMBL:EMY78812.1,
RC ECO:0000313|Proteomes:UP000012313};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (MAR-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 -!- 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:EMY78812.1}.
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DR EMBL; AOHC02000017; EMY78812.1; -; Genomic_DNA.
DR AlphaFoldDB; N1WNI7; -.
DR STRING; 1218598.LEP1GSC060_3739; -.
DR Proteomes; UP000012313; 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:UniProtKB-EC.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR Pfam; PF12950; TaqI_C; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EMY78812.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 436..544
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 601 AA; 70952 MW; CCE4E8371BBCF06C CRC64;
MQYFLALLDL FIMSSQILIH NNQTRLKGEF KDFFDYFIGY QKKHQESLST VDRKRNGIFL
TDDLTIIDSL LDILDSYDDI KYYKILEPSC GKGIFLIRLL DRIYKLTNNK EIIYSAINDV
IYFNDIDPNM VRMTKNNISD FYFYTFEEEY RGKFNSFNTD FTVSNNGENN LFYCSNENND
SFESMYNFFD FVIGNPPYIT LYGRRDKKEN ELQRIKYLDA YNQFPDSLKN GKLNLMMLFI
EKSINLLKNG GKLSFILDIS FFETAFKYTR KYLLENTTIV SIDTNIKGFS VASGQMILKL
IKQQPDSTHT VQINESKFKN PIFVKQNDWY NEKDEFKFRW NSSEFDFIIL DKLTNKSSSD
RLGELFFNKN LRTCTMMLDM ENLFTENRSN HVDKMNLYPY YQGSKSLREK YGSFKFEKVF
SYNKKLQDEI NDRLKIELES KGIKNKKRIG LGEQVIYDNF KIYIRQSAKQ LIASIDLGKS
SANNSLYVFS FRDSTNTTLE KLYYICGILN SKIMTYFAQK TKIIRFSEGK QPQIKISDLS
TLPIPKSSQL EKEISLLVQK IYSEEENERN KYINSIDVLL SKYFNLTEDE IKHVENEVIA
F
//
