ID A0A0Q4FK00_9SPHN Unreviewed; 379 AA.
AC A0A0Q4FK00;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362026};
GN ORFNames=ASE75_04305 {ECO:0000313|EMBL:KQM65493.1};
OS Sphingomonas sp. Leaf17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735683 {ECO:0000313|EMBL:KQM65493.1, ECO:0000313|Proteomes:UP000051777};
RN [1] {ECO:0000313|EMBL:KQM65493.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM65493.1,
RC ECO:0000313|Proteomes:UP000051777};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM65493.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM65493.1,
RC ECO:0000313|Proteomes:UP000051777};
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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594, ECO:0000256|RuleBase:RU362026}.
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:KQM65493.1}.
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DR EMBL; LMKL01000004; KQM65493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q4FK00; -.
DR STRING; 1735683.ASE75_04305; -.
DR OrthoDB; 9800801at2; -.
DR Proteomes; UP000051777; 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR040843; RAMA.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR Pfam; PF18755; RAMA; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KQM65493.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051777};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 46..267
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
FT DOMAIN 276..376
FT /note="RAMA"
FT /evidence="ECO:0000259|Pfam:PF18755"
SQ SEQUENCE 379 AA; 42096 MW; 2E29191622157546 CRC64;
MVMVDTMTRK RAKPVAPVVD RATLPLDRIL QGDCIAQMKS LPAGSVDMIF ADPPYNLQLA
GELFRPDGTH VDAVTDDWDK FDTFAAYDRF TRAWLKEARR ILKDDGSIWV IGSYHNIFRV
GAAVQDLGYW ILNDIVWRKA NPMPNFRGTR FTNAHETLIW ASKAEGAKYT FNYRSMKTLN
DELQMRSDWE FPICGGAERL KKDGTKVHPT QKPEALLYRV LLACTKPGDV VLDPFFGTGT
TGAVAKRLGR HWIGIEREDD YIAAAKERIA AALPLDESAL ATMMSPRQQP KVAFGVLVEN
GYLTPGAVLC DGKRRFRAVV RADGSLLSDC GATGSIHKLG STVQGAPACN GWTFWHYEAA
DGLKPVDALR QTYLLATQP
//