ID K2FUV1_9BACT Unreviewed; 682 AA.
AC K2FUV1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ACD_7C00189G0003 {ECO:0000313|EMBL:EKE21559.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE21559.1};
RN [1] {ECO:0000313|EMBL:EKE21559.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKE21559.1}.
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DR EMBL; AMFJ01002428; EKE21559.1; -; Genomic_DNA.
DR AlphaFoldDB; K2FUV1; -.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR046819; MmeI_hel.
DR InterPro; IPR046816; MmeI_Mtase.
DR InterPro; IPR046817; MmeI_N.
DR InterPro; IPR046820; MmeI_TRD.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841:SF6; DNA METHYLTRANSFERASE A; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF20465; MmeI_hel; 1.
DR Pfam; PF20473; MmeI_Mtase; 1.
DR Pfam; PF20464; MmeI_N; 1.
DR Pfam; PF20466; MmeI_TRD; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EKE21559.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKE21559.1}.
FT DOMAIN 11..172
FT /note="MmeI-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20464"
FT DOMAIN 179..257
FT /note="MmeI-like helicase spacer"
FT /evidence="ECO:0000259|Pfam:PF20465"
FT DOMAIN 333..594
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
FT DOMAIN 617..677
FT /note="MmeI-like target recognition"
FT /evidence="ECO:0000259|Pfam:PF20466"
SQ SEQUENCE 682 AA; 78096 MW; 2252F43FDD321CE4 CRC64;
MPLSWNEIKS RAIEFSKEWE DEASEDAEAK SFWDGFFNVF GLTRRRLASF EFQVKKYGGN
QGFIDLFWPG MLIVEHKSRG RDLEKAHVQA MDYFPGLTEK ELPKYVLVSD FEKIKLYDLE
EGTEQEFLLK DLHKKAHLFG FIAGYKKQEY KEEDEVNIKA AELMGKLYDV MIETGYSGHE
LNVFLVRILF CLFADDANIF LHHQFRSYLE NRTSEDGSDT GMHIATLFQT MNTSPEKRQA
TLDEELSQFP YVNGGLFAEQ ITYPSFNSEM RKRLIEACAF DWSKISPAIF GSLFQSVMDK
DARRHLGAHY TSEKNILKLI KPLFLDDLYL ELESCGKNIK KLNELHEKIS KLKFLDPACG
CGNFLIIAYR ELRQLELELL KKRLGQVVLG FGVASYIRIK PEQFYGIEID EFPARIAQTA
MWLMDHQMNE IASQAFGQNI KDLPLTKGAE IFIGNALQKD WEEVISKNEL SYILGNPPFV
GSKMMSKIQR DDIIAVFGKV KGIGVLDYVS GWYVKAAKYI QGTQIKVAFV STNSITQGEQ
VGILWNELLS NYGIKINFAH KTFKWSNEAR GKAGVYCVII GFANFDVDKK YLYEYENVKG
ESHQIIAKNI NPYLVPADDV IIISRQNPIC DIPKMSFGNM PLDGGNLLLS DEEKNNLLLS
NLDVEKFVKP LMGHTQYMVL SK
//
