ID Q1Q861_PSYCK Unreviewed; 526 AA.
AC Q1Q861;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=Pcryo_2365 {ECO:0000313|EMBL:ABE76142.1};
OS Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS / K5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=335284 {ECO:0000313|EMBL:ABE76142.1, ECO:0000313|Proteomes:UP000002425};
RN [1] {ECO:0000313|Proteomes:UP000002425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5
RC {ECO:0000313|Proteomes:UP000002425};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL Submitted (MAR-2006) 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; CP000323; ABE76142.1; -; Genomic_DNA.
DR RefSeq; WP_011514670.1; NC_007969.1.
DR AlphaFoldDB; Q1Q861; -.
DR STRING; 335284.Pcryo_2365; -.
DR REBASE; 12287; M.PcrKORF2365P.
DR KEGG; pcr:Pcryo_2365; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_013049_4_1_6; -.
DR Proteomes; UP000002425; 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 CDD; cd02440; AdoMet_MTases; 1.
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; 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.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:ABE76142.1};
KW Transferase {ECO:0000313|EMBL:ABE76142.1}.
FT DOMAIN 8..142
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 152..486
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 526 AA; 58815 MW; 47C05A3867246D30 CRC64;
MDISIKQLES DLWNAADNLR ANSTLTAAEY KDPLLGLVFL RFVQNRHEDA KVKIQESLAI
NPRTGQKREV TKDDFVAAGS ILLPEKAKYD YLAALPESEN IAEAINNAMK LIEEEYPSLV
GILPKNYQVF DNKLLRDLVR VFNKDAVRKA KGDIFGRIYE FFLMKFSMQG AGAQEGGEFF
TPPSLVNLIV NFIQPDHGII HDPACGSGGM FVQTAHFIQG HMPNKSVNEA ITVYGTELKS
NNTKLAKMNL AVHGIEGAII ESNSFYTNPH DLNGKCDFVM ANPPFNVSGI DGKNKFLTED
ARLPFGAPLT KGGTIGNGNY LWIQYFHSYL NKTGRAGFVM ASSATDAGHA EKLIRQQLIE
TGDVECIVSI ANNFFYTRSL PCHVWFFNKE KKAENKDKIL MIDARNTYRK VSSTIQDFSE
DQLEGLTALI NAFRGDELGV SKDNEWFTEH FPDGTYTDVE GLCKVVDLDA LKEQDYSLTP
GRYVGVNIDI DMDFDYKGRM TEIRSELSSL NKEAAELMKK IQGVEL
//
