ID A0A031LNR7_9GAMM Unreviewed; 773 AA.
AC A0A031LNR7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=CL42_10645 {ECO:0000313|EMBL:EZQ04774.1};
OS Acinetobacter sp. Ver3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=466088 {ECO:0000313|EMBL:EZQ04774.1, ECO:0000313|Proteomes:UP000023816};
RN [1] {ECO:0000313|EMBL:EZQ04774.1, ECO:0000313|Proteomes:UP000023816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ver3 {ECO:0000313|EMBL:EZQ04774.1,
RC ECO:0000313|Proteomes:UP000023816};
RA Kurth D.G., Ordonez O.F., Albarracin V.H., Revale S., Farias M.E.;
RT "Polyextremophylic features in the genome of Acinetobacter sp. Ver3
RT isolated from a high altitude andean lake.";
RL Submitted (MAR-2014) 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};
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:EZQ04774.1}.
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DR EMBL; JFYL01000037; EZQ04774.1; -; Genomic_DNA.
DR RefSeq; WP_035267956.1; NZ_JFYL01000037.1.
DR AlphaFoldDB; A0A031LNR7; -.
DR REBASE; 120390; M.AspVer3ORF10645P.
DR eggNOG; COG0286; Bacteria.
DR Proteomes; UP000023816; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
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; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 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 Endonuclease {ECO:0000313|EMBL:EZQ04774.1};
KW Hydrolase {ECO:0000313|EMBL:EZQ04774.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:EZQ04774.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..143
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 155..458
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 773 AA; 87321 MW; 6CCD155C792FE52E CRC64;
MINNNFSQVA AFIWSVADLL RGDFKQSQYG RVILPFTLLR RLECVLEASK ANVLAANEKV
KQMPLPEEAK EKMLLKATNG LSFCNTSELD LGSLGQKDIR ANLMNYIQHF SKDAREIFEH
FKFDEFVGLL DDANLLYKVV QKFAATDLSY SAVSNHEMGL VFEELIRRFA ESSNETAGEH
FTPRDIVRLT TGIVFGKDDD ALNKEGIIRT VYDPTAGTGG FLSSGTEYVR EHNPDAVIRV
YGQELNPESY AICKADMLIK GQDVKNIKLG NTLSNDQLAH DKFDYMLSNP PFGVDWKKIE
DDIKSEHEQK GFKGRFGAGL PRVSDGSLLF LMHLMSKMRE PNAENQQGSR IGIILNGSPL
FTGSAGSGES EIRRYILEAD LLEAIIALPT DMFYNTGIAT YVWVLSNKKD AERKGKVQLI
DGSNLYSKMR KSLGSKRNEM SEEDIALITR TYGNFEVMDA RELDKPAEVK SNRGRQSASP
KTETAKTFSS KIFNSYEFGY RRVTIERPLR LSAQVNDERI ATLRFAPKPF NAVMQKLYDD
YGNTWTADSY GQLAEYEAEI RALIKAEFSE LKEKDIKTVL EPKLWLEQRT LLNKAQALQA
KIGTAQFDDF NAFDDVFKQA LKDTNIKLET KEKKQFIDAI TWKNADAEPV INKVVKGAEN
PLYGQFSYKG KVVEFVQDGD LRDAENIALN PNVSTTDLIE SYFKREVGPH VPDAWINADK
RDAQDGEIGI VGYEIPFNRH FYVYEPPRDL SEIDADLDAV SREIMALLQE VHS
//
