ID   MTA1_CELCE              Reviewed;         521 AA.
AC   P31974;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Type II methyltransferase M.AluI {ECO:0000303|PubMed:12654995};
DE            Short=M.AluI {ECO:0000303|PubMed:8451189};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase AluI;
DE   AltName: Full=Modification methylase AluI;
GN   Name=aluIM {ECO:0000303|PubMed:8451189};
OS   Cellulosimicrobium cellulans (Arthrobacter luteus).
OC   Bacteria; Actinobacteria; Micrococcales; Promicromonosporaceae;
OC   Cellulosimicrobium.
OX   NCBI_TaxID=1710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DOMAIN.
RC   STRAIN=ATCC 21606 / DSM 20424 / 73-14;
RX   PubMed=8451189; DOI=10.1093/nar/21.4.905;
RA   Zhang B., Tao T., Wilson G.G., Blumenthal R.M.;
RT   "The M.AluI DNA-(cytosine C5)-methyltransferase has an unusually large,
RT   partially dispensable, variable region.";
RL   Nucleic Acids Res. 21:905-911(1993).
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'-AGCT-
CC       3', methylates C-3 on both strands, and protects the DNA from cleavage
CC       by the AluI endonuclease. {ECO:0000269|PubMed:8451189,
CC       ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC   -!- DOMAIN: Replacement of residues 191-272 by a single Ser residue still
CC       protects DNA against digestion by AluI. {ECO:0000269|PubMed:8451189}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
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DR   EMBL; Z11841; CAA77866.1; -; Genomic_DNA.
DR   PIR; S35614; S35614.
DR   AlphaFoldDB; P31974; -.
DR   SMR; P31974; -.
DR   PRO; PR:P31974; -.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..521
FT                   /note="Type II methyltransferase M.AluI"
FT                   /id="PRO_0000087858"
FT   DOMAIN          8..491
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   521 AA;  58648 MW;  ACBBB2C4E5326BFB CRC64;
     MSKANAKYSF VDLFAGIGGF HAALAATGGV CEYAVEIDRE AAAVYERNWN KPALGDITDD
     ANDEGVTLRG YDGPIDVLTG GFPCQPFSKS GAQHGMAETR GTLFWNIARI IEEREPTVLI
     LENVRNLVGP RHRHEWLTII ETLRFFGYEV SGAPAIFSPH LLPAWMGGTP QVRERVFITA
     TLVPERMRDE RIPRTETGEI DAEAIGPKPV ATMNDRFPIK KGGTELFHPG DRKSGWNLLT
     SGIIREGDPE PSNVDLRLTE TETLWIDAWD DLESTIRRAT GRPLEGFPYW ADSWTDFREL
     SRLVVIRGFQ APEREVVGDR KRYVARTDMP EGFVPASVTR PAIDETLPAW KQSHLRRNYD
     FFERHFAEVV AWAYRWGVYT DLFPASRRKL EWQAQDAPRL WDTVMHFRPS GIRAKRPTYL
     PALVAITQTS IVGPLERRLS PRETARLQGL PEWFDFGEQR AAATYKQMGN GVNVGVVRHI
     LREHVRRDRA LLKLTPAGQR IINAVLADEP DATVGALGAA E