MTG1_HERAU
ID MTG1_HERAU Reviewed; 126 AA.
AC P25267;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Type II methyltransferase M.HgiGI {ECO:0000303|PubMed:12654995};
DE Short=M.HgiGI {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase HgiGI;
DE AltName: Full=Modification methylase HgiGI;
DE Flags: Fragment;
GN Name=hgiGIM {ECO:0000303|Ref.1};
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=HPA1;
RA Duesterhoeft A., Kroeger M.;
RL Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
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, recognizes the double-stranded sequence 5'-
CC GRCGYC-3', methylates C-? on both strands, and protects the DNA from
CC cleavage by the HgiEI endonuclease. {ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:7607523}.
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; X55143; CAA38947.1; -; Genomic_DNA.
DR PIR; S21955; S21955.
DR AlphaFoldDB; P25267; -.
DR SMR; P25267; -.
DR REBASE; 3420; M.HgiGI.
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; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00094; C5_MTASE_1; 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..>126
FT /note="Type II methyltransferase M.HgiGI"
FT /id="PRO_0000087891"
FT DOMAIN 1..126
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"
FT NON_TER 126
SQ SEQUENCE 126 AA; 13871 MW; FF3695B03BC02399 CRC64;
MKTIDLFAGC GGMSLGFMQA GFEIVAAVDN WRPAITTYQQ NFIHPIHELD LAEVDEAISL
IKTYSPELII GGPPCQDFSS AGKRDEGLGR ANLTLDFVKI VLAIQPAWVI MENVERARLS
KIHQQA
