ID   MTE1_HERAU              Reviewed;         437 AA.
AC   P25266;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Type II methylase M.HgiEI {ECO:0000303|PubMed:12654995};
DE            Short=M.HgiEI {ECO:0000303|PubMed:7607523};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase HgiEI;
DE   AltName: Full=Modification methylase HgiEI;
GN   Name=hgiEIM {ECO:0000303|PubMed:7607523};
OS   Herpetosiphon aurantiacus (Herpetosiphon giganteus).
OC   Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC   Herpetosiphon.
OX   NCBI_TaxID=65;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HPG24;
RA   Erdmann D., Kroeger M.;
RL   Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   DISCUSSION OF SEQUENCE, AND FUNCTION.
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       GGWCC-3', methylates C-? on both strands, and protects the DNA from
CC       cleavage by the HgiEI endonuclease (PubMed:12654995). This system is
CC       more active than isoschizomeric RM.HgiBI (PubMed:7607523).
CC       {ECO:0000269|PubMed:7607523, 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; X55142; CAA38944.1; -; Genomic_DNA.
DR   AlphaFoldDB; P25266; -.
DR   SMR; P25266; -.
DR   REBASE; 3419; M.HgiEI.
DR   PRO; PR:P25266; -.
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..437
FT                   /note="Type II methylase M.HgiEI"
FT                   /id="PRO_0000087890"
FT   DOMAIN          4..431
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   437 AA;  49817 MW;  AC27AF38B5BC973F CRC64;
     MQQFRFIDLF AGIGGFRLGL EAVGGVCVAS AEIDQQAIKV YWQNWPTDGV DHNLGDITQI
     QQLPAHDVLV GGVPCQPWSI AGKNQAFDDP RGQLWADVIR LVQINQPKAF IFENVKGLVD
     PRNRLCLEII LDSFKDLGYS VFYKLLNSFD FGVAQNRDRV FIVGIQQKLD LNGFSFPEYA
     ESDQRLYHIL DNLEAPETKL ESIPIQRNLF GERIEVGYNK LTPRGAFNDF FILNDIRNGP
     TSIHSWEIYP TTEREKHICM IIMRNRRNSR YGNCDGNPMS YSDIAELVVD LAENELQILV
     KKRILRQYPD GKYEFFNRRL SGGIDGTYRI FMPNARFFGT LTARGMHDEI AEINVSGANA
     AEYKYNFIQQ VLIPKRYRPI TVSEAARLQG FPSTFKFHSN QSANFRLIGN SVAPPVIVAL
     GKRLQCVKLF EQELCEV