ID K1SFQ9_9ZZZZ Unreviewed; 397 AA.
AC K1SFQ9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
DE Flags: Fragment;
GN ORFNames=LEA_13319 {ECO:0000313|EMBL:EKC59512.1};
OS human gut metagenome.
OC unclassified sequences; metagenomes; organismal metagenomes.
OX NCBI_TaxID=408170 {ECO:0000313|EMBL:EKC59512.1};
RN [1] {ECO:0000313|EMBL:EKC59512.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22891823; DOI=10.1111/j.1462-2920.2012.02845.x;
RA Ferrer M., Ruiz A., Lanza F., Haange S.B., Oberbach A., Till H.,
RA Bargiela R., Campoy C., Segura M.T., Richter M., von Bergen M., Seifert J.,
RA Suarez A.;
RT "Microbiota from the distal guts of lean and obese adolescents exhibit
RT partial functional redundancy besides clear differences in community
RT structure.";
RL Environ. Microbiol. 15:211-226(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 -!- 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:EKC59512.1}.
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DR EMBL; AJWY01009041; EKC59512.1; -; Genomic_DNA.
DR AlphaFoldDB; K1SFQ9; -.
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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 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 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EKC59512.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 235..396
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT NON_TER 397
FT /evidence="ECO:0000313|EMBL:EKC59512.1"
SQ SEQUENCE 397 AA; 45166 MW; AE7EA4E9C1191B7B CRC64;
MNEHISLWVK QTGVLPVNLL HCQNAGVLKY AMLDGDINNF CLDYSENQDM DADAYKQQAW
SSNMRNYIRV AGDDVMLYRV GNVSPERISK SLVLNNMEKF YQYISPKQDV PNIEGIVPFV
MKEFRGIRNW LREENSAESS MTALLYMLAF IKDNGNIGND SLVSLGLPAN TLDIVGKLTT
MEEHLQHLRE GMNGFLPNIS LLLRHAAGQL FEEANYIAKF NPQLSLFTNY DIKYAYDPQK
LGAFYTPTYL ARSIVEKVIK ESHIEDKEEI SILDPACGSG EFLVEALRQL KTIGFTGKVK
VYGWDVSSIA INIANFVLHF EKEEWNNSLE LHIEEHDSIV CNWPNVDIVF MNPPYSSWEQ
LNDEQRESVK ELMPKGKPNL SGVFYLKAVN ALKESGV
//
