ID A0A0Q9CF93_9CELL Unreviewed; 957 AA.
AC A0A0Q9CF93;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=ASE27_04800 {ECO:0000313|EMBL:KRD40266.1};
OS Oerskovia sp. Root918.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Oerskovia.
OX NCBI_TaxID=1736607 {ECO:0000313|EMBL:KRD40266.1, ECO:0000313|Proteomes:UP000051694};
RN [1] {ECO:0000313|EMBL:KRD40266.1, ECO:0000313|Proteomes:UP000051694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root918 {ECO:0000313|EMBL:KRD40266.1,
RC ECO:0000313|Proteomes:UP000051694};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD40266.1, ECO:0000313|Proteomes:UP000051694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root918 {ECO:0000313|EMBL:KRD40266.1,
RC ECO:0000313|Proteomes:UP000051694};
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:KRD40266.1}.
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DR EMBL; LMJG01000011; KRD40266.1; -; Genomic_DNA.
DR RefSeq; WP_056648406.1; NZ_LMJG01000011.1.
DR AlphaFoldDB; A0A0Q9CF93; -.
DR Proteomes; UP000051694; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.90.220.20; DNA methylase specificity domains; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF12161; HsdM_N; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000051694};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..137
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 144..475
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 957 AA; 106140 MW; BE954CF6DA84CCD7 CRC64;
MITGELKSKI DRVWDAFWLA GISNPIEVIE QITHLLFVRR LDELQTLKEN RANRTGQPIQ
DPIFPAGNSP TGVPFEALRW KSFKNESPEN AYAVVDNHVF PFLRTLGSDG STYSSHMEGA
RLTIPTPGLL AKVIDMLNDV PMNRRDTNGD LYEYMLGKLS ASGQNGQFRT PRHLIDLMVR
MTAPTPKDSI CDPACGTAGF LMAASEYVRD EFGDDLHDPA TRDHFHESMF HGYDFDRTML
RIGSMNMLMH GVEKPDIRYR DSLSQAAGGD EGKYSLILAN PPFAGSLDYE AVSRDLLKVV
KTKKTELLFL ARILKLLQPG GRAAVVVPDG VLFGSSTAHR ALRRILVENH KLDAVVKLPA
GAFKPYAGVS TAILFFTRTD SGGTDDVWFY DIQADGWSLD DKRQPLLDAG QLGAAPDEAF
VVANHAKNNL PDVLDRWHQR DASEKSRPRT AQSFCVPKAE IVGNDYDFSL NRYRFQGASS
RLKLGHHVVS PLPKNGVDGF LVVNHRSIRL SGLEIDPLAA ERAVGRVTPL REGDIICRTI
GEPRFMAIGP ILDSQPLAAD KSLHVIRPEK VAPDVLLAIL RSEYVSQRIE ARRYSGPGMP
RITYENLLQV ELPQLPSSNF EGFDGLPLER LRGKAERLVA TLEARAGQAF SALEGDAALL
EYMDTVTDAS AAGRAIDQLS TALSIAQLTF PHPIARQLRA YSIARTSGDP RAESEAVLHL
FEACLITLGA TLGGCLASLS GTLNGNWRNN LRKRALSFGD WHRLASASAS DLLARGVSLS
GLADAAKQGS ELDSLLKDFI SWRNHRSHGS GPRTRSDFLV DNGERRLKID YLIKSLRPMT
RLQWRVVDDL DWDPNDQVFR TRIRDLRGDH PDFSVAETTR TSPVARGQVM VSDGSREWSL
DGVLRYAPCR ECGNDEFFYP DSRSEDGLLY RSLGRGHVVT SDFSELPTYL RAIVDRD
//