ID   MTA1_AZOBR              Reviewed;         140 AA.
AC   P58284;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Type II methyltransferase M.AbrI {ECO:0000303|PubMed:12654995};
DE            Short=M.AbrI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase AbrI;
DE   AltName: Full=Modification methylase AbrI;
DE   Flags: Fragment;
GN   Name=abrIM;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29711 / DSM 1844 / Sp35;
RA   Schwabe G., Helke A., Klingmueller W.;
RT   "AbrI restriction modification system from Azospirillium brasilense,
RT   molecular cloning and characterization of its genes.";
RL   Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: A methylase, recognizes the double-stranded sequence 5'-
CC       CTCGAG-3', methylates A-5 on both strands, and protects the DNA from
CC       cleavage by the AbrI endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305}.
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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; X62690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P58284; -.
DR   REBASE; 4924; M.AbrI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   InterPro; IPR025931; TaqI_C.
DR   Pfam; PF12950; TaqI_C; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           <1..140
FT                   /note="Type II methyltransferase M.AbrI"
FT                   /id="PRO_0000087942"
FT   NON_TER         1
SQ   SEQUENCE   140 AA;  15900 MW;  7B5BC7D96697E174 CRC64;
     YRTIDRIYPA LTREHKLLIP DIKGEAHIVY EEGRLYPHHN LYYITSEIWD LRALQAVLLS
     GIARLFVSVY STKMHGGFLR FQAQYLRRIR VPNWSQVPAA VRQELITAGA KPDLAACNRA
     VFALYAMTAE ERAALGGNGD