ID C5S289_9PAST Unreviewed; 561 AA.
AC C5S289;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
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_09941 {ECO:0000313|EMBL:EER47016.1};
OS Actinobacillus minor NM305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=637911 {ECO:0000313|EMBL:EER47016.1, ECO:0000313|Proteomes:UP000005532};
RN [1] {ECO:0000313|EMBL:EER47016.1, ECO:0000313|Proteomes:UP000005532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM305 {ECO:0000313|EMBL:EER47016.1,
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:EER47016.1}.
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; ACQL01000097; EER47016.1; -; Genomic_DNA.
DR RefSeq; WP_005824196.1; NZ_ACQL01000097.1.
DR AlphaFoldDB; C5S289; -.
DR REBASE; 29451; M.Ami305ORF9941P.
DR eggNOG; COG0286; Bacteria.
DR Proteomes; UP000005532; 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: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; 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:EER47016.1};
KW Transferase {ECO:0000313|EMBL:EER47016.1}.
FT DOMAIN 31..188
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 210..522
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 561 AA; 63449 MW; 3EB27A951306400C CRC64;
MHSTAQHSTA HLAENLATQQ ADQQAFLNKL DADLWKAADK LRQQLDAANY KHIVLGLIFL
KYVSDSFSAQ QDIIKQRYTD PTSDFYLDPT AYSESELADI LNAELEERDN YAQDNVFWVP
QQARWDEIKV VVGANIGDKI WGEKTFKGIA NLIDDAFDAI EQDNPKLKNV IQRISPYKVD
ESILLGLIDL FSNTNFIRPT LDGKPISLAA KDILGHVYEY FLGQFALAEG KKGGQYFTPK
SIVTLIIEML EPYKGRIYDP AMGSGGFFVQ TERFIREHQG NVSEVSIFGQ EFNPTTWKLA
AMNMAIRGIE FDFGKGNADT FSNPQHRDKK MDFVMANPPF NMKDWWHPSL AQDLRWQYGI
PPESNANFAW LQHMIYHLSP NGRMALLLAN GSMSSNTNNE GEIRKNILKA DLVEAMIALP
SQLFTNTQIP ACIWILNKDK ARKGEVLFID ARQLGYMKDR VLRDFTADDI AKVADTYHSW
QQSADYQNIP AFCYTASLDE IAQNDFVLTP GRYVGAAEQE DDGVPFAEKM QELTALLQQQ
FKQSAELEAK IKANLGGLGY E
//
