ID R4Z719_9ACTN Unreviewed; 601 AA.
AC R4Z719;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BN381_80341 {ECO:0000313|EMBL:CCM65811.1};
OS Candidatus Microthrix parvicella RN1.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Microthrixaceae; Microthrix.
OX NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM65811.1, ECO:0000313|Proteomes:UP000018291};
RN [1] {ECO:0000313|EMBL:CCM65811.1, ECO:0000313|Proteomes:UP000018291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN1 {ECO:0000313|EMBL:CCM65811.1,
RC ECO:0000313|Proteomes:UP000018291};
RX PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT based on genomic and metagenomic analyses.";
RL ISME J. 7:1161-1172(2013).
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:CCM65811.1}.
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DR EMBL; CANL01000078; CCM65811.1; -; Genomic_DNA.
DR AlphaFoldDB; R4Z719; -.
DR STRING; 1229780.BN381_80341; -.
DR eggNOG; COG0827; Bacteria.
DR HOGENOM; CLU_453932_0_0_11; -.
DR Proteomes; UP000018291; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006306; P:DNA methylation; IEA:InterPro.
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; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000018291};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 48..278
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 601 AA; 61679 MW; 719025C2F3ACB584 CRC64;
MSPLSAVATL AVHGRAPSEL PSWCDVTDHL AGGAAAALDP PPGAAICDLL GPLYELMLAD
AVRRSAGVHF TSPALASGLV ALAASIRVGE RFRTGEVVLD PACGAGAFLV ATARYLWAEA
GTDGRSTSAG GILSRLVGAD LDPDVLVVAR AALARWALDE ADAPGHDEAV GRARASGLSS
DEPTLVCCDA LTQPDVLARA IGGAPVGWVV GNPPFLAQLR AGTRHDARRR SSLTERFGAE
VGAYTDTAAL FLLAATELVA DTGVVCLIQP RSVLAARDAA GVRQTVTKRM PLAAAWVGDG
GFGAAVEVWA PVLGGFAAAP VGEVPVRGGS TVEMELGMVP VGALSSESWG ALVAAAEGLP
AVRRTSGTPL GRLGEVVRFS AGFRDEYYAM LELAQEATLT EREGRPEVPA GFAALVSSGL
IDPGVCRWGG KSMRFGKRRW ESPVVDLGAL AADDAPTTAW AKRQLVPKVL VASQTRVIEA
APDGQGRAIG LTPVIAGVPK GITLGHLLAV LCSPLSTLSL VSAMAGSGMG RAGVRVSTRA
LGDLDLPVHQ GPWDEAAGLL AGRCDLGDGI ESATLTWVHE LMVAASGVDD PDGVLSWFRE
R
//
