ID W5WMF1_9PSEU Unreviewed; 623 AA.
AC W5WMF1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=KALB_8686 {ECO:0000313|EMBL:AHI02043.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHI02043.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHI02043.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHI02043.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
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 type-I restriction system S methylase
CC family. {ECO:0000256|ARBA:ARBA00010923}.
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; CP007155; AHI02043.1; -; Genomic_DNA.
DR AlphaFoldDB; W5WMF1; -.
DR SMR; W5WMF1; -.
DR STRING; 1449976.KALB_8686; -.
DR KEGG; kal:KALB_8686; -.
DR eggNOG; COG0286; Bacteria.
DR eggNOG; COG0732; Bacteria.
DR HOGENOM; CLU_020304_0_0_11; -.
DR Proteomes; UP000019225; Chromosome.
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 CDD; cd16961; RMtype1_S_TRD-CR_like; 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; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR000055; Restrct_endonuc_typeI_TRD.
DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF01420; Methylase_S; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF116734; DNA methylase specificity domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 104..381
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 425..599
FT /note="Type I restriction modification DNA specificity"
FT /evidence="ECO:0000259|Pfam:PF01420"
SQ SEQUENCE 623 AA; 69384 MW; 8DCE8172E25FE6D5 CRC64;
MHYLHLLCSL TFLHHCAPRK WSELTQQITE VKSPHVLLRH ARRLVDTELR ERGVLPPRVS
FNALPLRSVR DLAPVMDLCS RLGASSFRVL LDHIEEAANT SAHMASTPVE VVDLMTKLVL
SDLAGSRDVY DPYTRSGEFL TAATEVAKRD GMAPITVYAE AADSDNLALA AMNLAVQGGA
KPVFKLSAVP WEDGLAEHKF DRVLTNPPFN LHRTPEQERE DRDWQFGPPP KDNDNFAWVQ
HVVTSLKEGG RAAMIMPDNA GASQRQQYRQ IRENLVESGA VEGVIGLPPN LFRNTPISAS
IWLLRSPKRE RREISFIDLR ARGAVRRGKR KLSLSDVTDA VSAMLSRQRS TDFSTCVDIN
TVQRRDYSLN PADYLTKAEE VEHSYEPVAK AYGATTEMRR RADVTDSHVD ALSLESAAAF
QNLTPNNWHR STLSELCEIQ PGPSYSRLGT KDRSTEGTVP VVLPKHLQDG RIVTDDNEKA
TAELAETLSH FRLKPGDIVC TRTGTTGASA IVHRAQEGWL LTANLLRIHK LDTALLTPEY
LLHYLSTPHV VAWIKNRAKF TSIIDSINRA ALGELPIPLP PLDAQRQIVD TLEALDSQCQ
AHDEIVKATR ETRAKLTAYL LSS
//
