ID   Q939Z3_ACILW            Unreviewed;      1262 AA.
AC   Q939Z3;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, 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   Name=AloIRMS {ECO:0000313|EMBL:CAC85954.1};
OS   Acinetobacter lwoffii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=28090 {ECO:0000313|EMBL:CAC85954.1};
RN   [1] {ECO:0000313|EMBL:CAC85954.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ks4-8 {ECO:0000313|EMBL:CAC85954.1};
RA   Cesnaviciene E., Petrusyte M., Kazlauskiene R., Maneliene Z., Timinskas A.,
RA   Lubys A., Janulaitis A.;
RT   "Characterization of AloI, a Restriction - Modification system of a new
RT   type.";
RL   Submitted (JUN-2001) 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   -!- SIMILARITY: Belongs to the type-I restriction system S methylase
CC       family. {ECO:0000256|ARBA:ARBA00010923}.
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DR   EMBL; AJ312389; CAC85954.1; -; mRNA.
DR   AlphaFoldDB; Q939Z3; -.
DR   SMR; Q939Z3; -.
DR   REBASE; 2812; AloI.
DR   GO; GO:0003677; F:DNA binding; 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   CDD; cd17267; RMtype1_S_EcoAO83I-TRD1-CR1_like; 1.
DR   CDD; cd17524; RMtype1_S_EcoUTORF5051P-TRD2-CR2_like; 1.
DR   Gene3D; 3.90.220.20; DNA methylase specificity domains; 2.
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; IPR000055; Restrct_endonuc_typeI_TRD.
DR   InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR30408:SF12; TYPE I RESTRICTION ENZYME MJAVIII SPECIFICITY SUBUNIT; 1.
DR   PANTHER; PTHR30408; TYPE-1 RESTRICTION ENZYME ECOKI SPECIFICITY PROTEIN; 1.
DR   Pfam; PF01420; Methylase_S; 2.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF116734; DNA methylase specificity domain; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          401..654
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          901..1042
FT                   /note="Type I restriction modification DNA specificity"
FT                   /evidence="ECO:0000259|Pfam:PF01420"
FT   DOMAIN          1123..1231
FT                   /note="Type I restriction modification DNA specificity"
FT                   /evidence="ECO:0000259|Pfam:PF01420"
SQ   SEQUENCE   1262 AA;  142945 MW;  F6AEF47636F7101C CRC64;
     MINQENLVAL LNHLGFAKNK SVYSKSIGTT SLSVDIDKKE ILYPEVDGFT VNERQICNFH
     ANENFVVFEC VHRLLEKGYN PEHIELEPKW KLGHGSSGGR ADILIRDNFG KPLLLIECKN
     SGSEFNKSWS KTLQDGDQLF SYAQQISEIR FLCLYASDFY DSELVYQSNI IAHRDNEAYL
     VANPQFKNFK SATDVKERFS VWRDTYKLDF TTKGIFENNI QPYQIGKDKY SIADLHAIAA
     SDQQKKYHQF ATILRQHNVS GRENAFDKLV NLFLCKLVDE IENPNDLKFY WKGVAYDSHF
     DLMDRLQQLY QSGMDKFLGE DITYINQNDV TNALRFIRQK PDATHRAVWN LFVKQKFFTN
     NDFSFLDVHN ERLFYQNAEV LLKVLQMWQD IRLTSATGHN QFLGDMFEGF LDQGVKQSEG
     QFFTPMPICR FILMSLPLES LVRDNPTPPM AVDYACGAGH FLTELALQFQ PLLEQHKPLA
     APAEYHKSMV GIEKEYRLSK VAKVSAFMYG HQGIQVCYGD GLVNSHEAFP DIRDGHFDLL
     VANPPYSVRG FLETLPEEDR KAYSLTNTIN DTETANSIET FFIERAKQLL KSGGVAAIIL
     PASILSNGGS AYIRAREILL QYFDIVAIAE FGSGTFGKTG TNTVSLFLRR KRTQPDTAEH
     YRERIEEWFK SCTTSKRKQV LYKDGHLIEK YCAHINVPLA DYQSFLRGEA EGSWMSHEHF
     QSYHDKFDTS TELANLRKQR KFKALSEYEQ TAEIAKRYLG YVHSIERDKL YHFCLASDQT
     NPVLIIRSPS GTKEMKQFLG YEWSSAKGDE GIKLIEDTSG KHVTKLYDGP NHANPTLFNR
     ANPTKLNSYI AANFEGTLGK ISPEVKDLTN VVQLVDMLDL KRSTFDKQLS LVAKKSVHIA
     SKWPQVKVGS ICSFEYGKPL PEENRVSGPY PVMGSNGRVG YHSEYLIKGP AIIIGRKGSA
     GQVVWEEEDC YPIDTTFYAK TLTSDIDKYF LFHVLKELDL GHLQGGVGVP GLNRNEAHEL
     PMPLPPIKVQ EQMVVDFKKI DADVASAAAL VSDSLSRINS EVDSLYSSGV GRISIEEIST
     NVQYGLNEKM NETGIGYKTF RMNEVIDGRM VDNGKMKRAN ISAKEFSKYQ LNKGDLLFIR
     SNGSLEHIGR FGLFDLDGEY CYASYLVRIV ADTSKIRPYY LAIIMNSAAL RKEVVSLAVK
     SGGTNNINAT KMKSIKVPVP SLDEQAKFIA KIELLQKQVA DAQATIDSAA ARKSTVMKKY
     LL
//