MTN1_LENAE
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 03-AUG-2022, entry version 81.
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; Actinobacteria; Pseudonocardiales; 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 / JCM
RC 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 REBASE; 3452; M.NaeI.
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; 3.40.50.150; -; 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..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
