MTN4_NEILA
ID MTN4_NEILA Reviewed; 423 AA.
AC P50182;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Type II methyltransferase M.NlaIV {ECO:0000303|Ref.2};
DE Short=M.NlaIV {ECO:0000303|PubMed:8190068};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase NlaIV;
DE AltName: Full=Modification methylase NlaIV;
GN Name=nlaIVM;
OS Neisseria lactamica.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=486;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23970 / DSM 4691 / CCUG 5853 / CIP 72.17 / NCTC 10617 / NCDC
RC A7515;
RX PubMed=8190068; DOI=10.1007/bf00283872;
RA Lau P.C.K., Forghani F., Labbe D., Bergeron H., Brousseau R., Holtke H.J.;
RT "The NlaIV restriction and modification genes of Neisseria lactamica are
RT flanked by leucine biosynthesis genes.";
RL Mol. Gen. Genet. 243:24-31(1994).
RN [2]
RP ERRATUM OF PUBMED:8190068.
RA Lau P.C.K., Forghani F., Labbe D., Bergeron H., Brousseau R., Holtke H.J.;
RL Mol. Gen. Genet. 244:167-167(1994).
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 that recognizes the double-stranded sequence 5'-
CC GGNNCC-3', methylates C-? on both strands, and protects the DNA from
CC cleavage by the NlaIV endonuclease. {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; U06074; AAA53237.1; -; Genomic_DNA.
DR PIR; S43886; S43886.
DR RefSeq; WP_003708503.1; NZ_QQKV01000001.1.
DR AlphaFoldDB; P50182; -.
DR SMR; P50182; -.
DR STRING; 486.B2G52_08325; -.
DR REBASE; 3469; M.NlaIV.
DR PRO; PR:P50182; -.
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.NlaIV"
FT /id="PRO_0000087901"
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; 47615 MW; 027E49558AEFDB19 CRC64;
MQQIKFIDLF SGMSGIRKGF EQACRKQSVA CKCVFTSEIK PAALEVLKQN YPDEVPYGDI
TKIETGDIPD FDILLAGFPC QAFSFAGKRL GFEDTRGTLF FDVARILKAK KPKGFILENV
EGLVTHDRKD PTQKIGRTLT VILETLEALG YYVSWKVLNA KDFGIPQNRK RIYLTGSLKS
KPDLSFETTP SPKLKNILES GLPTESSPFI KKLLKKFPPS ELYGKSVKDK RGGKNNIHSW
DIELKGAVTE EEKQLLNILL KERRKKKWAS EIGIDWMDGM PLTKAQISTF YKHPDLQNIL
DSLTDKGYLV LEHPKQKIGG QRIKDESLPK GYNIVSGKKS FEINKILDPN DVAPTLVAMD
MEHLFVVDNG GLRTLTGKEG LRLFGYPDDY SFDIPKKDKY DLLGNTVAVP VIKAVSERLL
HTL
