ID   MTC1_HERAU              Reviewed;         420 AA.
AC   P25263;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   02-SEP-2026, entry version 96.
DE   RecName: Full=Type II methyltransferase M.HgiCI {ECO:0000303|PubMed:12654995};
DE            Short=M.HgiCI {ECO:0000303|PubMed:1662609};
DE            EC=2.1.1.37 {ECO:0000269|PubMed:1662609};
DE   AltName: Full=Cytosine-specific methyltransferase HgiCI;
DE   AltName: Full=Modification methylase HgiCI;
GN   Name=hgiCIM;
OS   Herpetosiphon aurantiacus (Herpetosiphon giganteus).
OC   Bacteria; Bacillati; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC   Herpetosiphonaceae; Herpetosiphon.
OX   NCBI_TaxID=65;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=HPG9;
RX   PubMed=1662609; DOI=10.1111/j.1432-1033.1991.tb16497.x;
RA   Erdmann D., Duesterhoeft A., Kroeger M.;
RT   "Cloning and molecular characterization of the HgiCI
RT   restriction/modification system from Herpetosiphon giganteus Hpg9 reveals
RT   high similarity to BanI.";
RL   Eur. J. Biochem. 202:1247-1256(1991).
RN   [2]
RP   SEQUENCE REVISION.
RA   Kroeger M.;
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
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       GGYRCC-3', methylates C-5 on both strands, and protects the DNA from
CC       cleavage by the HgiCI endonuclease. {ECO:0000269|PubMed:1662609,
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 + S-adenosyl-L-homocysteine + H(+);
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         ECO:0000269|PubMed:1662609};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X55138; CAA38933.1; -; Genomic_DNA.
DR   PIR; S19707; S19707.
DR   AlphaFoldDB; P25263; -.
DR   REBASE; 3415; M.HgiCI.
DR   PRO; PR:P25263; -.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; EXP:UniProtKB.
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; IPR050750; C5-MTase.
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; 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; 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   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..420
FT                   /note="Type II methyltransferase M.HgiCI"
FT                   /id="PRO_0000087886"
FT   DOMAIN          2..417
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   420 AA;  47641 MW;  EDB427C9D66CD971 CRC64;
     MLKFIDLFAG IGGMRLGFEQ AMHELGIETA CVLSSEIDKH AQTTYAMNFH EQSQGDITQI
     QDFPSFDFLL AGFPCQPFSY AGKQKGFGDT RGTLFFEIER ILKAYRPKGF LLENVRGLTT
     HDKGRTFKTI LQKLHELNYG VYLILNSSNF QVPQNRLRVY IVGLDQSQPE LTITSHIGAT
     DSHKFKQLSN QASLFDTNKI MLVRDILEDH PLDKYNCSTD FVNKLLAFIG HPIKLNGKRL
     IDYRNGNSIH SWELGIKGEC TSDEIQFMNA LIANRRKKHF GAHQDGKKLT IEQIKTFFEH
     DDLDSIMQSL ITKGYLQEVN GRFNPVAGNM SFEVFKFLDP DSVSITLVSS DAHKIGVVHQ
     NRIRRITPRE CARLQGFPDS FQFHPKDSLA YRQFGNSVSV PVVKAVILDL FKSADLASCF
//