MTB1_NEIGO
ID MTB1_NEIGO Reviewed; 317 AA.
AC Q59603;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Type II methyltransferase M.NgoBI {ECO:0000303|PubMed:12654995};
DE Short=M.NgoBI {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase NgoBI;
DE Short=M.NgoI {ECO:0000303|PubMed:9628358};
DE AltName: Full=Modification methylase NgoBI;
GN Name=ngoBIM;
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=9628358;
RA Stein D.C., Gunn J.S., Piekarowicz A.;
RT "Sequence similarities between the genes encoding the S.NgoI and HaeII
RT restriction/modification systems.";
RL Biol. Chem. 379:575-578(1998).
RN [2]
RP 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 [3]
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 RGCGCY-3', methylates C-5 on both strands, and protects the DNA from
CC cleavage by the NgoBI endonuclease. {ECO:0000269|PubMed:9628358,
CC ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:7607490}.
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; U42459; AAB03206.2; -; Genomic_DNA.
DR AlphaFoldDB; Q59603; -.
DR SMR; Q59603; -.
DR REBASE; 3607; M.NgoBI.
DR PRO; PR:Q59603; -.
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..317
FT /note="Type II methyltransferase M.NgoBI"
FT /id="PRO_0000087896"
FT DOMAIN 2..302
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
SQ SEQUENCE 317 AA; 35949 MW; F0549A5259D1A414 CRC64;
MYKTIDLFSG IGGIRLGFEK YGCTNVFSSE WDKYARQVYE ANFGEKPFGD INGIDPSDIP
DHDILLAGFP CQPFSIAGKG LGFEDTRGTL FFNIAEILKT KQPKAFLLEN VKRLTTHDSG
RTFRIVLETL KQLGYTVYFK VLNTLDFGLP QKRERIYIVG FSDNIPFYFP EPINQYRPLG
ELLENDRDVE PSYFLSDTLK QKRLAALKKA PPTPSIWHEN IGGNVSALPY SCALRAGGSY
NYLVVNGVRR LTGREMLRLQ GFPDDFEINI PYSQVRKVAG NSVSVPVIEA TRKICSLLFP
ARSNKKGNWI YWRQDDA
