ID A0A0Q5JRB3_9MICO Unreviewed; 624 AA.
AC A0A0Q5JRB3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=ASF76_00300 {ECO:0000313|EMBL:KQR25783.1};
OS Microbacterium sp. Leaf151.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736276 {ECO:0000313|EMBL:KQR25783.1, ECO:0000313|Proteomes:UP000051582};
RN [1] {ECO:0000313|EMBL:KQR25783.1, ECO:0000313|Proteomes:UP000051582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf151 {ECO:0000313|EMBL:KQR25783.1,
RC ECO:0000313|Proteomes:UP000051582};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR25783.1, ECO:0000313|Proteomes:UP000051582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf151 {ECO:0000313|EMBL:KQR25783.1,
RC ECO:0000313|Proteomes:UP000051582};
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:KQR25783.1}.
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DR EMBL; LMOR01000001; KQR25783.1; -; Genomic_DNA.
DR RefSeq; WP_055951305.1; NZ_LMOR01000001.1.
DR AlphaFoldDB; A0A0Q5JRB3; -.
DR STRING; 1736276.ASF76_00300; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000051582; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Endonuclease {ECO:0000313|EMBL:KQR25783.1};
KW Hydrolase {ECO:0000313|EMBL:KQR25783.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:KQR25783.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 297..525
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 624 AA; 69370 MW; B56C534410B8157A CRC64;
MANERITEDL VEARLRSLGY YDDEDSIVVE KQQSAVEAIR KALSRASKSG KGRAAGYPEF
IITSPSTPDM VVLVECKADV RHHQSDARDL PKDYAVDGVL HYARHLSPNY TVISIAVSGT
PQTNAWSFFV TPKGSNLEHD LVSPTGAPVT TMIGLGDLIA AASFDPRVQR QRERDLLSFA
MEMHVFMRDE AELEEKEKPL AVAGSLIALK DQVFARTYDE YPAVDLPEYW IQSIKKVIRA
ARLPVDKLDN MTQPFTGIQV HPELRKPTKG YPKGLLNEIV TMLAEKVMPF ITVYHDFDVV
GAFYGEFLKY TGGDGKGLGI VLTPRHVTEL FGLIANVGKD DKVLDICAGT GGFLISSMVQ
MIRTATTEAE VADIKKNRLI GVEQNPSMYA LGASNMILRG DGKANLYQGS CFDTAIARGI
KAHRANVGMV NPPYAKTKED LHELRFVEQM LDSLEKGGTG IAIVPISCAT APSTHKRNLL
KKHTLEAVMS MPPEVFHPVG VITCIMVFSA GVPHAATDRK SWFGYWREDS FVKVKNLGRV
DKHHTWTQVR DRWVEAFRNR EVVPGESVMR KVTAEDEWVA EAYMETDYSA LDLADFERVL
LDYAMFSLSS TIDDGDDVET ELEE
//
