ID C5RYW2_9PAST Unreviewed; 581 AA.
AC C5RYW2;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=AM305_04453 {ECO:0000313|EMBL:EER48149.1};
OS Actinobacillus minor NM305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=637911 {ECO:0000313|EMBL:EER48149.1, ECO:0000313|Proteomes:UP000005532};
RN [1] {ECO:0000313|EMBL:EER48149.1, ECO:0000313|Proteomes:UP000005532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM305 {ECO:0000313|EMBL:EER48149.1,
RC ECO:0000313|Proteomes:UP000005532};
RX PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030;
RA Arya G., Niven D.F.;
RT "Production of haemolysins by strains of the Actinobacillus
RT minor/"porcitonsillarum" complex.";
RL Vet. Microbiol. 141:332-341(2010).
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:EER48149.1}.
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DR EMBL; ACQL01000023; EER48149.1; -; Genomic_DNA.
DR RefSeq; WP_005822119.1; NZ_ACQL01000023.1.
DR AlphaFoldDB; C5RYW2; -.
DR REBASE; 29435; M1.Ami305ORF4453P.
DR eggNOG; COG0286; Bacteria.
DR eggNOG; COG0732; Bacteria.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000005532; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
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; 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; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF116734; DNA methylase specificity domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EER48149.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 166..379
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 581 AA; 66472 MW; D4B9147EE4AA2816 CRC64;
MIKLNKSKLM DLYKDMRGTF SIEDLNEIAL KAMALVILNV TSLLKTKEDI LKAIENAERE
YPQAFTDGSR NVLSHLTEDT IFDLIYDLSE NQQKGLFTPE NKFEWVQYIF NLMNGTKYGY
FAFDDSIYDF CNKLYSNVNH DEIYIPFENS FYHTLMFSQE QSVASEGVKT TPIPAILNII
LGGIQYKQSD AITNPAYIKD GKLRLFSKGF LAEPWGMKVN INDQDNQRFS VKSNNLQNYL
IQHLFQQVND FAIVIMPING LHSSVQSEEL MRQWLLEQGY LKAVISLPSG LSISTMTNSA
LLIFDFSTKY ETVNFISLKD SEFVEKRNRE TKLTQLDKLI DIIDSNLAHK SSKKVDVKSI
LNNSYILNPE RYVLDNSTQD ALNILQEYET KKLGDLVDIY RPIPVSKLKS DGSEMFFEIQ
GGDIPEFGYI DTASKENYID NELMNILSPH LLQENDIIIT VRGSSGKVGI VSKELLNKYQ
GKVIIGQANL ILRVKDPQNV NAIALLMQLR SELSQSRLQV LSSGAVLSGL SVKDLKEFLV
ANFSLEKQKK LEENFQKQEI IKQQIIQQKQ QMQFLANDFW N
//
