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   08-NOV-2023, entry version 89.
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; Pseudomonadota; 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 /
RC   NCDC 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   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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
//