MTN3_NEILA
ID MTN3_NEILA Reviewed; 334 AA.
AC P24582;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Type II methyltransferase M.NlaIII {ECO:0000303|PubMed:12654995};
DE Short=M.NlaIII {ECO:0000303|PubMed:2277628};
DE EC=2.1.1.72;
DE AltName: Full=Adenine-specific methyltransferase NlaIII;
DE AltName: Full=Modification methylase NlaIII;
GN Name=nlaIIIM;
OS Neisseria lactamica.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=486;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND 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'-CATG-
CC 3', methylates A-2 on both strands and protects the DNA from cleavage
CC by the NlaIII endonuclease. {ECO:0000269|PubMed:2277628,
CC ECO:0000303|PubMed:12654995}.
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}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-57 is the initiator.
CC {ECO:0000305|PubMed:2277628}.
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DR EMBL; X54485; CAA38356.1; -; Genomic_DNA.
DR PIR; S12036; XYNHAL.
DR RefSeq; WP_003709316.1; NZ_LR590477.1.
DR AlphaFoldDB; P24582; -.
DR PRIDE; P24582; -.
DR PRO; PR:P24582; -.
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 Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..334
FT /note="Type II methyltransferase M.NlaIII"
FT /id="PRO_0000087968"
SQ SEQUENCE 334 AA; 38382 MW; 8BCF1A1A35F02E89 CRC64;
MNYIGSKLKL SNWLETEISN VAGHSLSDKV FCDLFAGTGI VGRKFKTNVK QVIANDMEYY
SYVLNRNYIG NCQSILKAGE LLQRLEQLPP REGLIYQHYC LGSGSERQYF SDENGKKIDA
VRIQIEEWKN TRYIDEDTYY FLLATLLEGA DKVANTASVY GAFLKNLKKS ALKPLSLEPA
LFEIGSDGHQ VYQADANQLI KNISGDILYL DPPYNARQYG ANYHLLNSIA LYDDFTPKGK
TGLREYSRSK YCSKSDVVPV FEALIRDADF QYIFLSYNNE GLMSVGQVRE IFERFGKYDL
VQTEYRRFKA DKTENRNHKA NSTFEYLHIL EKTF