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Database: UniProt
Entry: A0A0Q5N6V3_9MICO
LinkDB: A0A0Q5N6V3_9MICO
Original site: A0A0Q5N6V3_9MICO 
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
//
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