ID F9ZFX8_9PROT Unreviewed; 549 AA.
AC F9ZFX8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=NAL212_2263 {ECO:0000313|EMBL:ADZ27086.1};
OS Nitrosomonas sp. AL212.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=153948 {ECO:0000313|EMBL:ADZ27086.1, ECO:0000313|Proteomes:UP000001629};
RN [1] {ECO:0000313|EMBL:ADZ27086.1, ECO:0000313|Proteomes:UP000001629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL212 {ECO:0000313|EMBL:ADZ27086.1,
RC ECO:0000313|Proteomes:UP000001629};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Suwa Y., Klotz M.G.,
RA Bollmann A., Stein L.Y., Laanbroek H.J., Arp D.J., Norton J.M., Woyke T.;
RT "Complete sequence of chromosome of Nitrosomonas sp. AL212.";
RL Submitted (FEB-2011) 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};
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DR EMBL; CP002552; ADZ27086.1; -; Genomic_DNA.
DR AlphaFoldDB; F9ZFX8; -.
DR STRING; 153948.NAL212_2263; -.
DR REBASE; 33877; M.Nsp212ORF2263P.
DR KEGG; nit:NAL212_2263; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_013049_4_1_4; -.
DR Proteomes; UP000001629; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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 Gene3D; 1.20.1260.30; -; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 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 Methyltransferase {ECO:0000313|EMBL:ADZ27086.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001629};
KW Transferase {ECO:0000313|EMBL:ADZ27086.1}.
FT DOMAIN 12..143
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 155..511
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 549 AA; 61353 MW; 8C1BB0F879D04607 CRC64;
MAKTKAIKTE PLEKQLWKAA CKLQKNIDAA EYKHVVLGLM FLKYISDAFE ELHDRLEKGE
GDLVGADPED KDEYRAENVF FVPAESRWPH LVAHARQPDI GTHVDAAMDA IEKENPSLKG
VLPKVYARQN LDPTSLGELI DLIGNIALGD AKARSQDVLG HVFEYFLGEF ALAEGKQGGQ
FYTPRSIVEL LVNMLEPYQG RVFDPCCGSG GMFVQSEKFV EEHQGRIDDI SIYGQESNQT
TWRLAKMNLA IRGIDSSQVK WNNEGSFLND AHKDLKADFI IANPPFNVSD WSGEQLRGDA
RWQYGTPPPG NANFAWLQHF IYHLSPTGIA GVVLAKGALT SKTSGEGDIR KRLITDGNLI
DCIVNLPAKL FLNTQIPAAL WFLNRNRAGM DIGGHAKTIV GANNHLPLQN PPQQNPPQYH
HPRTHEILFI DARNLGHLIN RRTKELSHDD IQQIANTYHA WRNPAVIPAQ TGIQPYEDIK
GFCASVPVER VAELDYVLTP GRYVGLPDEE DDFNFPERFA ALKAEFEAQL QEEVALNQAI
VESLARVKV
//
