MTC1_HERAU
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 03-AUG-2022, entry version 86.
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; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC 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 + 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 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}.
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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; 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 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
