ID   MTD2_HERAU              Reviewed;         354 AA.
AC   P25265;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Type II methylase M.HgiDII {ECO:0000303|PubMed:12654995};
DE            Short=M.HgiDII {ECO:0000303|PubMed:7607523};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase HgiDII;
DE   AltName: Full=Modification methylase HgiDII;
GN   Name=hgiDIIM {ECO:0000303|PubMed:1937045};
OS   Herpetosiphon aurantiacus (Herpetosiphon giganteus).
OC   Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC   Herpetosiphon.
OX   NCBI_TaxID=65;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=HPA2;
RX   PubMed=1937045; DOI=10.1016/0378-1119(91)90569-w;
RA   Duesterhoeft A., Kroeger M.;
RT   "Cloning, sequence and characterization of m5C-methyltransferase-encoding
RT   gene, hgiDIIM (GTCGAC), from Herpetosiphon giganteus strain Hpa2.";
RL   Gene 106:87-92(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       GTCGAC-3', methylates C-? on both strands and protects the DNA from
CC       cleavage by the HgiDII endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:1937045}.
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; X55141; CAA38941.1; -; Genomic_DNA.
DR   PIR; S21949; JT0594.
DR   AlphaFoldDB; P25265; -.
DR   SMR; P25265; -.
DR   REBASE; 101149; M.Rga602ORF33P.
DR   REBASE; 3418; M.HgiDII.
DR   PRO; PR:P25265; -.
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   Gene3D; 3.40.50.150; -; 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   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 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..354
FT                   /note="Type II methylase M.HgiDII"
FT                   /id="PRO_0000087889"
FT   DOMAIN          3..344
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   354 AA;  39853 MW;  BDA017785D5ADC75 CRC64;
     MVGAVIDLFC GVGGLTHGLI LEGFGVLAGI DNDPSCKYAY EQNNRTRFIE KSISEVDGRE
     LNALYPNNQH KILVGCAPCQ DFSQYTKKSR TGTKWQLLTE FSRLIREIEP DIISMENVPE
     VRTFNRGEVF NNFIQSLEQL GYHVSHSVVH CPDYGIPQQR DRLVLFAAKQ GVIKIIPPTH
     TPENYRTVRD VIGSLATNYS GGHWEGDSMH AASRLEDINL RRIQHSVPGG TWADWPEELI
     AECHKKESGE SYGSVYGRME WDKVAPTITT QCNGYGNGRF GHPEQDRAIS LREAALLQTF
     PRSYQFAPEG QLKFKTVSRQ IGNAVPVALG RVIAKSIKRF LEGLHERQRV RIII