GenomeNet

Database: UniProt
Entry: A0A0Q9CF93_9CELL
LinkDB: A0A0Q9CF93_9CELL
Original site: A0A0Q9CF93_9CELL 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system