ID   MTHZ_METTF              Reviewed;         355 AA.
AC   P29568;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   RecName: Full=Type II methyltransferase M.MthZI {ECO:0000303|PubMed:12654995};
DE            Short=M.MthZI {ECO:0000303|PubMed:1408820};
DE            EC=2.1.1.113 {ECO:0000269|PubMed:1408820};
DE   AltName: Full=Modification methylase MthZI;
DE   AltName: Full=N-4 cytosine-specific methyltransferase MthZI;
GN   Name=mthZIM {ECO:0000303|PubMed:1408820};
OS   Methanothermobacter thermautotrophicus (Methanobacterium thermoformicicum).
OG   Plasmid pFZ1.
OC   Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC   Methanobacteria; Methanobacteriales; Methanobacteriaceae;
OC   Methanothermobacter.
OX   NCBI_TaxID=145262;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DSM 3720 / Z-245;
RX   PubMed=1408820; DOI=10.1093/nar/20.19.5047;
RA   Noelling J., de Vos W.M.;
RT   "Identification of the CTAG-recognizing restriction-modification systems
RT   MthZI and MthFI from Methanobacterium thermoformicicum and characterization
RT   of the plasmid-encoded mthZIM gene.";
RL   Nucleic Acids Res. 20:5047-5052(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 3720 / Z-245;
RX   PubMed=1336177; DOI=10.1093/nar/20.24.6501;
RA   Noelling J., van Eeden F.J.M., Eggen R.I.L., de Vos W.M.;
RT   "Modular organization of related Archaeal plasmids encoding different
RT   restriction-modification systems in Methanobacterium thermoformicicum.";
RL   Nucleic Acids Res. 20:6501-6507(1992).
RN   [3]
RP   NOMENCLATURE, AND SUBTYPE.
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 beta subtype methylase that recognizes the double-stranded
CC       sequence 5'-CTAG-3', methylates C-1 on both strands, and protects the
CC       DNA from cleavage by the MthZI endonuclease.
CC       {ECO:0000269|PubMed:1408820, ECO:0000303|PubMed:1336177}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC         methyl-2'-deoxycytidine in DNA + S-adenosyl-L-homocysteine + H(+);
CC         Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC         Evidence={ECO:0000269|PubMed:1408820};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X67212; CAA47651.1; -; Genomic_DNA.
DR   EMBL; X68367; CAA48447.1; -; Genomic_DNA.
DR   PIR; S30315; S30315.
DR   RefSeq; WP_010889862.1; NC_001337.1.
DR   AlphaFoldDB; P29568; -.
DR   SMR; P29568; -.
DR   REBASE; 3540; M.MthZI.
DR   GeneID; 24855017; -.
DR   BRENDA; 2.1.1.113; 3256.
DR   PRO; PR:P29568; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:TreeGrafter.
DR   GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; EXP:UniProtKB.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   PANTHER; PTHR13370:SF3; TRNA (GUANINE(10)-N2)-METHYLTRANSFERASE HOMOLOG; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Plasmid; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..355
FT                   /note="Type II methyltransferase M.MthZI"
FT                   /id="PRO_0000087928"
SQ   SEQUENCE   355 AA;  42477 MW;  0FC26598445CA704 CRC64;
     MKTTHRIYFK NSADMNELKD KSINLVVTSP PYPMVEIWDR LFSELNPKIE ETLIDEEDGL
     RSYNLMHEEL EKVWHEVDRV TAPGGVVIIN IGDATRKIGK KFQLYPNHVR TIDFFFDRGY
     QVLPFIIWRK QSNKPTKFMG SGMLPPNAYV THEHEYILIF RKEGPRQFKT EEERKLRRES
     AYFWEERNQW FSDVWTDLTG VSQRLNHKNL RKRAAAYPFE LAYRLINMYS IMGDWVLDPF
     LGTGTTMIAA ACAGRNSIGY ELDHNFKDLI ESRINETLKL SNEIVMRRIN DHIEFIREKN
     GKYYSENYKF KVTTRQEQDI RLYYPRTYKK IKNNEFEFFY QEVNPKKERQ SKLNI
//