MTB5_NEIGO
ID MTB5_NEIGO Reviewed; 423 AA.
AC Q59605;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Type II methyltransferase M.NgoBV {ECO:0000303|PubMed:12654995};
DE Short=M.NgoBV {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase NgoV;
DE Short=M.NgoV {ECO:0000303|PubMed:7607490};
DE AltName: Full=Modification methylase NgoBV;
GN Name=ngoBVM; Synonyms=dcmE {ECO:0000303|PubMed:7607490};
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=WR302;
RX PubMed=7607490; DOI=10.1016/0378-1119(94)00649-d;
RA Stein D.C., Gunn J.S., Radlinska M., Piekarowicz A.;
RT "Restriction and modification systems of Neisseria gonorrhoeae.";
RL Gene 157:19-22(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, recognizes the double-stranded sequence 5'-
CC GGNNCC-3', methylates C-5 on both strands, and protects the DNA from
CC cleavage by the NgoBV endonuclease. {ECO:0000269|PubMed:7607490,
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}.
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DR EMBL; U43735; AAA86268.1; -; Genomic_DNA.
DR AlphaFoldDB; Q59605; -.
DR SMR; Q59605; -.
DR REBASE; 3608; M.NgoBV.
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; 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; 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..423
FT /note="Type II methyltransferase M.NgoBV"
FT /id="PRO_0000087897"
FT DOMAIN 4..423
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
SQ SEQUENCE 423 AA; 47571 MW; DFB0377B3E21480E CRC64;
MQQIKFIDLF SGMSGIRKGF EQACRKQSVA CECVFTSEIK PAALEVLKQN YPDEVPYGDI
TKIETGDIPD FDILLAGFPC QAFSFAGKRL GFEDTRGTLF FDVARILKAK KPKGFILENV
EGLVTHDRKD STQKIGRTLT VILETLEALG YYVSWKVLNA KEFGIPQNRK RIYLTGSLKS
KPDLSFETSP SPKLKNILES GLPTESSPFI KKLLKKFPPS ELYGKSVKDK RGGKNNIHSW
DIELKGAVTE EEKQLLNILL KERRKKNGLQ KIGIDWMDGM PLTKAQISTF YKHPDLQNIL
DSLTDKGYLV LEHPKQKIGG QRIKDESLPK GYNIVSGKKS FEINKILDPN DVAPTLFAMD
MEHLFVVDNG GLRTLTGKEG LRLFGYPDDY PFDIPKKDRC DLLGNTVAVP VIKAVSERLL
HTL
