ID   MTHT_METTF              Reviewed;         330 AA.
AC   P29567;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Type II methyltransferase M.MthTI {ECO:0000303|PubMed:12654995};
DE            Short=M.MthTI {ECO:0000303|PubMed:1512204};
DE            EC=2.1.1.37 {ECO:0000269|PubMed:1512204};
DE   AltName: Full=Cytosine-specific methyltransferase MthTI;
DE   AltName: Full=Modification methylase MthTI;
GN   Name=mthTIM;
OS   Methanothermobacter thermautotrophicus (Methanobacterium thermoformicicum).
OG   Plasmid pFV1.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=145262;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DSM 3848 / THF;
RX   PubMed=1512204; DOI=10.1128/jb.174.17.5719-5726.1992;
RA   Noelling J., de Vos W.M.;
RT   "Characterization of the archaeal, plasmid-encoded type II restriction-
RT   modification system MthTI from Methanobacterium thermoformicicum THF:
RT   homology to the bacterial NgoPII system from Neisseria gonorrhoeae.";
RL   J. Bacteriol. 174:5719-5726(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 3848 / THF;
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.
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       GGCC-3', methylates C-3 on both strands, and protects the DNA from
CC       cleavage by the MthTI endonuclease. {ECO:0000269|PubMed:1512204,
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:0000269|PubMed:1512204};
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; M97222; AAA73370.1; -; Genomic_DNA.
DR   EMBL; X68366; CAA48436.1; -; Genomic_DNA.
DR   PIR; B42941; B42941.
DR   RefSeq; NP_039765.1; NC_001336.1.
DR   AlphaFoldDB; P29567; -.
DR   SMR; P29567; -.
DR   REBASE; 3448; M.MthTI.
DR   PRO; PR:P29567; -.
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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Plasmid; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..330
FT                   /note="Type II methyltransferase M.MthTI"
FT                   /id="PRO_0000087894"
FT   DOMAIN          3..328
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   REGION          192..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   330 AA;  37360 MW;  EFC15E57D86385A5 CRC64;
     MNMDIASFFS GAGGLDLGFT KAGFNIVFAN DNWKGCWKTF EKNHGIKINK KPIEWLKPSE
     IPDVVGFIGG PPCQSWSLAG SMCGADDPRG KTFYAYVDLV KEKDPLFFLA ENVPGIVSRT
     HLPEFKRLVN SFIDIGYNVE YKVLNAKDYG VPQDRKRVFI VGYREDLNLK FEFPKPLNKK
     VTLRDAIGDL PEPKPALEKN RSNGENLEVP NHEYMTGTFS SRYMSRNRVR SWDEVSFTIQ
     AGGRHAPCHP QANKMIKVGP DKFIFDPESP KPYRRLSVRE CARIQGFPDD FIFYYKNVAD
     GYTMVGNAVP VKLAEELAKK IKKDLEGVLN
//