ID A0A1U7MPQ0_9MICO Unreviewed; 1061 AA.
AC A0A1U7MPQ0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, 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=BJF81_04740 {ECO:0000313|EMBL:OLT20581.1};
OS Ornithinimicrobium sp. CNJ-824.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Ornithinimicrobium.
OX NCBI_TaxID=1904966 {ECO:0000313|EMBL:OLT20581.1, ECO:0000313|Proteomes:UP000185694};
RN [1] {ECO:0000313|EMBL:OLT20581.1, ECO:0000313|Proteomes:UP000185694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNJ-824 {ECO:0000313|EMBL:OLT20581.1,
RC ECO:0000313|Proteomes:UP000185694};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT20581.1}.
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DR EMBL; MKKA01000044; OLT20581.1; -; Genomic_DNA.
DR RefSeq; WP_075958590.1; NZ_MKKA01000044.1.
DR AlphaFoldDB; A0A1U7MPQ0; -.
DR STRING; 1904966.BJF81_04740; -.
DR Proteomes; UP000185694; 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 PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000185694};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1027..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 118521 MW; 7DE2C1315B7CEC7F CRC64;
MATAPTTVLN SDQRRFLDTQ TQRARAAAQR AAEDALRALA VAEPSRPGYL NDEQNKLRLA
LRDKARQLGD DTSRTGVPLT NLIHDVAYEQ WHRLLFARFL EVNDLLRHPQ YRDIPLSMED
CGDLASDLGE PDAWAVAGRF ASEILPGVFR LTDPAVQVRF AAEHRNALER LLLEIPSEVF
TTEDALGWVY QFWQTAEKKR VNDSGVKIGG ADLSPVTQLF TENYMVRFLL ENSLGAWWVA
RHPDSSLRDG WEYLRVNEDG TPAAGTFSEW PDRASDVTMM DPCCGSGHFL VAMFGMLWRM
RAEEDSLTPA EAQDAVLRDN LHGLELDPRC TQLATFNVAL EAWKQGGFRE LPAPQIACSG
VPVRAARQDW ESLAGDDDDL RRAMRGLHSL FQNAEGLGSL IDPRRAENGD GLFGRDLTVG
VSAERVRGLL ATALREENRD TTVLGHAAND VMHAADLLGR NYTLVATNPP YLGTQRMDEA
AAQFIADRFP RSSSELATAM LERYLPEGAG TIAAVMPMNW LFLKSFNSLR IYLLDQAGWN
AVAPLGKGAF QTITGQVVQP ALVLLSTRRP REMLFVDARQ ATSVEAKAEA LRAAKIELPA
FDQVRQNPGS ILDASAFGKS LLSNYATSWQ GLVTMDTSQY VLRFWETSGD PAVWERYVTA
PSKTGASTGR QYFLRWESGR GRLQSSNAHN FNPPSVLGKR GVLVGQSSLR VTLYNGEMFN
DASAPVIPIN PDDLGAVWQY LQSSEYVQAV RRLNSKVVVN PGYLIRVPFD RERWRQVAED
AGAVIANATG DPTQWSFHGK VVGSDHPLQV AVARLLGYGW PDQIEDDLDS LVDRDGVAAL
VALPGEPDLS TRLREVLSVA YGEEWSGATE RRLVADAGGK NGRLEDWLRD SFFVQHVKVF
DNRPFLWHIW DGRKDGFSAI VNFHKLNRRT LEKLTFTSLG AWIDRQKHEA RAERAGADAR
LAAAEALQHR LKLILEGAPP YDIYVRWKRM AEQPIGWEPD RDDGVRLNIR PFVTADLLRS
KVNVHWRRDR GKNPDGSERH NDLHPTLEER RAARREAEAA E
//