ID   MTD1_HERAU              Reviewed;         309 AA.
AC   P24600;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   RecName: Full=Type II methyltransferase M.HgiDI {ECO:0000303|PubMed:12654995};
DE            Short=M.HgiDI {ECO:0000303|PubMed:2020544};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase HgiDI;
DE   AltName: Full=Modification methylase HgiDI;
GN   Name=hgiDIM {ECO:0000303|PubMed:2020544};
OS   Herpetosiphon aurantiacus (Herpetosiphon giganteus).
OC   Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC   Herpetosiphonaceae; Herpetosiphon.
OX   NCBI_TaxID=65;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=HPA2;
RX   PubMed=2020544; DOI=10.1093/nar/19.5.1049;
RA   Duesterhoeft A., Erdmann D., Kroeger M.;
RT   "Stepwise cloning and molecular characterization of the HgiDI restriction-
RT   modification system from Herpetosiphon giganteus Hpa2.";
RL   Nucleic Acids Res. 19:1049-1056(1991).
RN   [2]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=7607523; DOI=10.1016/0378-1119(94)00779-r;
RA   Kroeger M., Blum E., Deppe E., Duesterhoeft A., Erdmann D., Kilz S.,
RA   Meyer-Rogge S., Moestl D.;
RT   "Organization and gene expression within restriction-modification systems
RT   of Herpetosiphon giganteus.";
RL   Gene 157:43-47(1995).
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       GRCGYC-3', methylates C-? on both strands, and protects the DNA from
CC       cleavage by the HgiDI endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000303|PubMed:7607523, ECO:0000305|PubMed:2020544}.
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; X55140; CAA38938.1; -; Genomic_DNA.
DR   PIR; S14029; S14029.
DR   AlphaFoldDB; P24600; -.
DR   SMR; P24600; -.
DR   REBASE; 3417; M.HgiDI.
DR   PRO; PR:P24600; -.
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; 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; 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..309
FT                   /note="Type II methyltransferase M.HgiDI"
FT                   /id="PRO_0000087888"
FT   DOMAIN          1..297
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   309 AA;  34439 MW;  74F29BFBF13E142F CRC64;
     MKTIDLFAGC GGMSLGFMQA GFEIVAAVDN WRPAINTYQQ NFTHPIHELD LAQIDAAVSL
     IKTHSPELII GGPPCQDFSS AGKRDEGLGR ANLTLDFAKI VLAIQPAWVI MENVERARLS
     KIHQQACSML GDEGYSLAQV VLDASLCGVP QLRKRTFVIG HRHGSIADLA NVLQQRLAKQ
     SLTVRDYFGE SLDTDYYYRH PRTYERRAIF SVNEPSPTIR GVNRPIPATY RMHPKDAGDV
     SLARPLTTKE RSLIQTFPLD FKFVGTKSEQ EQMIGNAVPV NLAFFLATSL QAYLNQPRMQ
     QLSLLPSFF
//