ID   MTN1_LENAE              Reviewed;         413 AA.
AC   P50188;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Type II methyltransferase M.NaeI {ECO:0000303|PubMed:12654995};
DE            Short=M.NaeI {ECO:0000303|PubMed:7698663};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase NaeI;
DE   AltName: Full=Modification methylase NaeI;
GN   Name=naeIM {ECO:0000303|PubMed:7698663};
OS   Lentzea aerocolonigenes (Lechevalieria aerocolonigenes) (Saccharothrix
OS   aerocolonigenes).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=68170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 23870 / DSM 40034 / BCRC 13661 / CBS 609.68 / CIP 107109 /
RC   JCM 4614 / KCTC 9379 / NBRC 13195 / NCIMB 12944 / NRRL B-3298 / 701;
RX   PubMed=7698663; DOI=10.1016/0378-1119(94)00806-4;
RA   Taron C.H., van Cott E.M., Wilson G.G., Moran L.S., Slatko B.E.,
RA   Hornstra L.J., Benner J.S., Kucera R.B., Guthrie E.P.;
RT   "Cloning and expression of the NaeI restriction endonuclease-encoding gene
RT   and sequence analysis of the NaeI restriction-modification system.";
RL   Gene 155:19-25(1995).
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 that recognizes the double-stranded sequence 5'-
CC       GCCGGC-3', methylates C-? on both strands, and protects the DNA from
CC       cleavage by the NaeI endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:7698663}.
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; U09581; AAC43325.1; -; Genomic_DNA.
DR   RefSeq; WP_030468108.1; NZ_JOFI01000013.1.
DR   AlphaFoldDB; P50188; -.
DR   SMR; P50188; -.
DR   STRING; 68170.GCA_000974445_06524; -.
DR   REBASE; 3452; M.NaeI.
DR   OrthoDB; 9813719at2; -.
DR   PRO; PR:P50188; -.
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; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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..413
FT                   /note="Type II methyltransferase M.NaeI"
FT                   /id="PRO_0000087903"
FT   DOMAIN          4..317
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   413 AA;  45180 MW;  649CF1C2B97EFD28 CRC64;
     MQSLEVVEIC AGAGGQALGL EKAGFSHRLA VELDVNAAAT LRKNLKSDVV ITGDVADPSV
     LNPMEHLGVS LLAGGVPCPP FSIAGKQLGA DDMRDLFAWA VELCDVMKPR ALMLENVRGL
     SMPRFAGYRQ HVLDRLNDMG YVAEWRLLHA SDFGVPQLRP RFVLVALQNK FAPYFTWPEP
     TGAAPTVGET LKDLMAADGW EGAEEWAAQA NDIAPTIVGG SKKHGGADLG PTRAKRAWAE
     LGVDAMGVAD APPQPGDKFK VGPKLTCEMV ARIQGWRDGE WIFEGRKTSR YRQIGNAFPP
     PVAEAIGKRI RAALNMEGEG RDRAVDSDHN PLYRALKESG DFMTHRQLER AVGRPIEAYE
     LERTISDLGR DFEVETKDGA SAMAYKLGPF KAFTGQEGHL RHEMFVRHRT KIS
//