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Database: UniProt
Entry: E3VXA4_AQUSE
LinkDB: E3VXA4_AQUSE
Original site: E3VXA4_AQUSE 
ID   E3VXA4_AQUSE            Unreviewed;       552 AA.
AC   E3VXA4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   Name=aseIM {ECO:0000313|EMBL:ADO24185.1};
OS   Aquaspirillum serpens.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Aquaspirillum.
OX   NCBI_TaxID=190 {ECO:0000313|EMBL:ADO24185.1};
RN   [1] {ECO:0000313|EMBL:ADO24185.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NEB 448 {ECO:0000313|EMBL:ADO24185.1};
RA   Stewart F., Morgan R.D.;
RT   "AseI restriction-modification system genes.";
RL   Submitted (SEP-2010) 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; HQ327700; ADO24185.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3VXA4; -.
DR   REBASE; 3285; M.AseI.
DR   PRO; PR:E3VXA4; -.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025931; TaqI_C.
DR   PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   Pfam; PF12950; TaqI_C; 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:0000256|ARBA:ARBA00022603};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          105..280
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          406..519
FT                   /note="TaqI-like C-terminal specificity"
FT                   /evidence="ECO:0000259|Pfam:PF12950"
SQ   SEQUENCE   552 AA;  62978 MW;  A169844B74C7254C CRC64;
     MGMHEMRNME QQTFLDIENL EYFSIEESAK ILGVSSATIR NWVKTGYLEI ISKGKISRNS
     VENFDKKISG VEKLNQRANK SKKDNHNHEY LAAEFLRKID LGIEKIDSMG DLYESGLSDS
     YRNKEGIYYT PSYIVNDLLS LKNQLTGDET FCDPCCGSGN FLVRALEIGF KPENIFGFDT
     DHVAVEIAKR RILEKTGYKS NNIKCYDFLH LSVSEKAGSY DYIFTNPPWG KKIEQAEKKS
     ISKILKGGSS IDTCSLFYFC CIKSLNLGGT LGLLLPESFF NVATYEDARL SALMLQIQRL
     SHYGKPFKGI LTGAVGMVIS KKDSILDQNI DCVYKDKNFK RNVDSFRKNP KSIFNISCTD
     DEAKVIEHVY SIPYVTLRGR AQWGIGIVTG NNKKYVDNIL KDGLIPVYKG SDITKYGLKP
     ASTYIPKDFS LYQQVAPINL YEAPEKLIYK FISSNLCFFY DTESRFVINS ANILITEKEF
     PVSMKVICEL FNSDFMNWIF RKLFNTHKVL RGDLELLPIH DQFLSGKNFI ESEYLTSINV
     ERTNCGTFRI KK
//
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