ID A0A0Q5N6V3_9MICO Unreviewed; 654 AA.
AC A0A0Q5N6V3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=ASF89_06530 {ECO:0000313|EMBL:KQR65028.1};
OS Frigoribacterium sp. Leaf172.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736285 {ECO:0000313|EMBL:KQR65028.1, ECO:0000313|Proteomes:UP000051720};
RN [1] {ECO:0000313|EMBL:KQR65028.1, ECO:0000313|Proteomes:UP000051720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf172 {ECO:0000313|EMBL:KQR65028.1,
RC ECO:0000313|Proteomes:UP000051720};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR65028.1, ECO:0000313|Proteomes:UP000051720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf172 {ECO:0000313|EMBL:KQR65028.1,
RC ECO:0000313|Proteomes:UP000051720};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQR65028.1}.
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DR EMBL; LMPB01000002; KQR65028.1; -; Genomic_DNA.
DR RefSeq; WP_055814702.1; NZ_LMPB01000002.1.
DR AlphaFoldDB; A0A0Q5N6V3; -.
DR STRING; 1736285.ASF89_06530; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000051720; Unassembled WGS sequence.
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 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; IPR029464; HSDR_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 1.
DR Pfam; PF13588; HSDR_N_2; 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:0000313|EMBL:KQR65028.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051720};
KW Transferase {ECO:0000313|EMBL:KQR65028.1}.
FT DOMAIN 33..155
FT /note="Type I restriction enzyme R protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13588"
FT DOMAIN 289..563
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 654 AA; 73288 MW; D2C4E4006556E64B CRC64;
MALIQDDNVS KSFIVPPGKI LDFIDGSIRS DTPEEYVRQE ILKSLVREYK YRKQNIAVEW
PLKIGSKRVR ADIAIFPDGI DFDHRSQSNV SLIIECKKSG TSPNSKTDGI EQLVSYMSAC
SNAHIGMWTN GTDLAAYRMV TKDGLRIPDE IPDIPHFGDV SESDRPEFNQ LRPAASDSLL
FAFRRAHDYI SGNQGMQKPE AFWELLKLIF CKIHDERESA RPEFYASPLE RTTAAGLIRI
NKRIGTLFSA VKATYPQIFK AAEEIELQPN ILAYIVTQLQ MFSLLSSDVD VKGKAYEEVV
GSNLRGDRGE FFTPRNVCRM MVEMIDPDER DLILDPACGT GGFLISAMNY VVEGVKSEVR
HSGRSDTSRD DAIQSRVQRF LRTNLIGLDF NPNLVRATKM NMVMNNDGSG GLFQANSLAP
AATWTEGLRD RELIGNVDVI ITNPPFGSKI PIDDPTILSQ YELGHAWTYV DRDDLWVRKD
ETTTRPPEIL FIERCVKFLK PGSGVAAMVL PDGILGSPGL GFVRQWLLEN TIILASIDLH
PDTFQPGTSV QTSVLIVRRK SPEQLSIEAA AGLQSDYDIF MAICDHIGHD KRGNTVYVRD
EDGYEVVAEV EEAVTANVMG PDIPEMHRAQ ERVPDDNTLM IAKAFREWMS LKEE
//