ID   MTM1_MORSP              Reviewed;         418 AA.
AC   P11408;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   13-SEP-2023, entry version 110.
DE   RecName: Full=Type II methyltransferase M.MspI {ECO:0000303|PubMed:12654995};
DE            Short=M.MspI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase MspI;
DE   AltName: Full=Modification methylase MspI;
GN   Name=mspIM;
OS   Moraxella sp.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 49670;
RX   PubMed=2471145; DOI=10.1093/nar/17.8.3001;
RA   Lin P.M., Lee C.H., Roberts R.J.;
RT   "Cloning and characterization of the genes encoding the MspI restriction
RT   modification system.";
RL   Nucleic Acids Res. 17:3001-3011(1989).
RN   [2]
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'-CCGG-
CC       3', methylates C-1 on both strands, and protects the DNA from cleavage
CC       by the MspI endonuclease. {ECO:0000269|PubMed:2471145,
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: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; X14191; CAA32393.1; -; Genomic_DNA.
DR   PIR; S04188; CTKEMM.
DR   AlphaFoldDB; P11408; -.
DR   SMR; P11408; -.
DR   REBASE; 3447; M.MspI.
DR   PRO; PR:P11408; -.
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   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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; IPR031303; C5_meth_CS.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
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; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 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..418
FT                   /note="Type II methyltransferase M.MspI"
FT                   /id="PRO_0000087895"
FT   DOMAIN          105..404
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   418 AA;  47657 MW;  7F8922F9CCAD926E CRC64;
     MKPEILKLIR SKLDLTQKQA SEIIEVSDKT WQQWESGKTE MHPAYYSFLQ EKLKDKINFE
     ELSAQKTLQK KIFDKYNQNQ ITKNAEELAE ITHIEERKDA YSSDFKFIDL FSGIGGIRQS
     FEVNGGKCVF SSEIDPFAKF TYYTNFGVVP FGDITKVEAT TIPQHDILCA GFPCQPFSHI
     GKREGFEHPT QGTMFHEIVR IIETKKTPVL FLENVPGLIN HDDGNTLKVI IETLEDMGYK
     VHHTVLDASH FGIPQKRKRF YLVAFLNQNI HFEFPKPPMI SKDIGEVLES DVTGYSISEH
     LQKSYLFKKD DGKPSLIDKN TTGAVKTLVS TYHKIQRLTG TFVKDGETGI RLLTTNECKA
     IMGFPKDFVI PVSRTQMYRQ MGNSVVVPVV TKIAEQISLA LKTVNQQSPQ ENFELELV
//