MTM4_NEIGO
ID MTM4_NEIGO Reviewed; 312 AA.
AC P31033;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Type II methyltransferase M.NgoMIV {ECO:0000303|PubMed:12654995};
DE Short=M.NgoMIV {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase NgoMIV;
DE AltName: Full=DNA methylase M.NgoMI {ECO:0000303|PubMed:1321116};
DE Short=M.NgoMI {ECO:0000303|PubMed:1321116};
DE AltName: Full=Modification methylase NgoMIV;
GN Name=ngoMIVM;
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=MS11;
RX PubMed=1321116; DOI=10.1128/jb.174.15.4899-4906.1992;
RA Stein D.C., Chien R., Seifert H.S.;
RT "Construction of a Neisseria gonorrhoeae MS11 derivative deficient in NgoMI
RT restriction and modification.";
RL J. Bacteriol. 174:4899-4906(1992).
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 GCCGGC-3', methylates C-2 on both strands, and protects the DNA from
CC cleavage by the NgoMIV endonuclease. {ECO:0000269|PubMed:1321116,
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 -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
CC -!- CAUTION: Was originally known as M.NgoMI. {ECO:0000305|PubMed:1321116}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M86915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A42709; A42709.
DR AlphaFoldDB; P31033; -.
DR SMR; P31033; -.
DR REBASE; 165908; M.Nse506ORF6588P.
DR PRO; PR:P31033; -.
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; -; 2.
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..312
FT /note="Type II methyltransferase M.NgoMIV"
FT /id="PRO_0000087899"
FT DOMAIN 3..311
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 312 AA; 35226 MW; 319E20242B873452 CRC64;
MQFTSLEICA GAGGQALGLE RAGFSHVALI EIEPSACQTL RLNRPDWNVI EGDVRLFQGE
GYDGIDLLAG GVPCPPFSKA GKQLGKDDER DLFPEAIRLA KETDPKAIML ENVRGLLDPK
FENYRNHITE QFAKLGYLGQ WKLLYAADYG VSQLRPRVLF VALKNEYTNF FKWPEPNSEQ
PKTVGELLFD LMSENNWQGA HNWRLKAAQI APTLVAVQKN TAVLTWDLHD PNAHGRSWVW
MVQVCGIVRR LKTFTGMPRL TVRMTARIQG FPDDWQFFGK KTPMYRQIGN AFPPPVAEAV
GRQIIKALKK EN