ID   MTNX_NEILA              Reviewed;         313 AA.
AC   P24581;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Type II methyltransferase M.NlaX {ECO:0000303|PubMed:12654995};
DE            Short=M.NlaX {ECO:0000303|PubMed:2277628};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase NlaX;
GN   Name=nlaXM;
OS   Neisseria lactamica.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND POSSIBLE FUNCTION.
RC   STRAIN=ATCC 23970 / DSM 4691 / CCUG 5853 / CIP 72.17 / NCTC 10617 / NCDC
RC   A7515;
RX   PubMed=2277628; DOI=10.1007/bf00259456;
RA   Labbe D., Hoeltke H.J., Lau P.C.K.;
RT   "Cloning and characterization of two tandemly arranged DNA
RT   methyltransferase genes of Neisseria lactamica: an adenine-specific
RT   M.NlaIII and a cytosine-type methylase.";
RL   Mol. Gen. Genet. 224:101-110(1990).
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       CCNGG-3' and methylates C-2 on both strands. May be the equivalent of
CC       dcm in this bacteria, or it may protect the DNA from cleavage by the
CC       putative NlaXP endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:2277628}.
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   -!- 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; X54485; CAA38357.1; -; Genomic_DNA.
DR   PIR; S12037; XYNHCL.
DR   AlphaFoldDB; P24581; -.
DR   SMR; P24581; -.
DR   STRING; 486.B2G52_01545; -.
DR   REBASE; 2158; M.NlaX.
DR   PRO; PR:P24581; -.
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; IPR031303; C5_meth_CS.
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; PS00095; C5_MTASE_2; 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..313
FT                   /note="Type II methyltransferase M.NlaX"
FT                   /id="PRO_0000087911"
FT   DOMAIN          2..308
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   313 AA;  34843 MW;  E75150C89ABEA611 CRC64;
     MFKIIDLFAG IGGIRLGFEQ AFDDVRCVFS SEIDKYAVQT YQANHGGETV CGDITQTDVA
     DIPDHDILSA GFPCQPFSQA GLKKGFADTR GTLFFDIERI LLAKKPQAFL LENVKQLKGH
     DKGRTLQVIL AHLQQAGYKV YTEVLKARDF GIPQNRERIY LVGFLNHDVD FRFPQPIGQA
     TAVGDILEAY PDEKYTISDK LWQGYQRRKA ENRAAGKGFG YGLFNAESAY TNTISARYYK
     DGSEILIEQP GKNPRKITPP EAARLQGFPD SFQIPVSDAQ AYRQFGNSVC VPVIRAIAEQ
     MKAALSAVSD RKV