MTG1_AVIVO
ID MTG1_AVIVO Reviewed; 357 AA.
AC P25282;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Type II methyltransferase M1.HgaI {ECO:0000303|PubMed:12654995};
DE Short=M1.HgaI {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.37 {ECO:0000269|PubMed:1856224};
DE AltName: Full=Cytosine-specific methyltransferase HgaIA;
DE AltName: Full=M.HgaI-1 {ECO:0000303|PubMed:1856224};
DE AltName: Full=Modification methylase HgaIA;
DE Short=M.HgaIA;
GN Name=hgaIAM;
OS Avibacterium volantium (Pasteurella volantium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Avibacterium.
OX NCBI_TaxID=762;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 14385 / DSM 22841 / CCUG 3713 / NCTC 3438 / Lovell 6;
RX PubMed=1856224; DOI=10.1016/s0021-9258(18)92795-x;
RA Sugisaki H., Yamamoto K., Takanami M.;
RT "The HgaI restriction-modification system contains two cytosine methylase
RT genes responsible for modification of different DNA strands.";
RL J. Biol. Chem. 266:13952-13957(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14385 / DSM 22841 / CCUG 3713 / NCTC 3438 / Lovell 6;
RA Sugisaki H.;
RT "Nucleotide sequence of the gene of HgaI restriction endonuclease.";
RL Bull. Inst. Chem. Res., Kyoto Univ. 71:338-342(1993).
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 DNA with the sequence 5'-GCGTC-
CC 3', methylates C-2, and protects the DNA from cleavage by the HgaI
CC endonuclease. {ECO:0000269|PubMed:1856224,
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:1856224};
CC -!- MISCELLANEOUS: The HgaI modification system consists of two cytosine
CC methylase genes responsible for modification of different strands in
CC the target DNA. {ECO:0000269|PubMed:1856224}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA04206.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA14377.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D90363; BAA14377.1; ALT_INIT; Genomic_DNA.
DR EMBL; D17388; BAA04206.1; ALT_INIT; Genomic_DNA.
DR PIR; B39467; B39467.
DR AlphaFoldDB; P25282; -.
DR SMR; P25282; -.
DR PRO; PR:P25282; -.
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 SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00675; dcm; 1.
DR PROSITE; PS00094; C5_MTASE_1; 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..357
FT /note="Type II methyltransferase M1.HgaI"
FT /id="PRO_0000087879"
FT DOMAIN 5..357
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
SQ SEQUENCE 357 AA; 40863 MW; 9F3E10D620AF3154 CRC64;
MKKNIMGLSL FSSAGIGEYF LSRVGIDIIV ANELIKKRAD LYQKIYPNHK MVIGDIRDQR
IFNKVLNIAL TNQVDFLIAS PPCQGMSVAG KNRDVSNMAN DNRNYLIMYV IAMIKKLKPA
YILIENVPFL LKLELYIDNK LTPIKNILED EFGSEYHIHF DILDAADYGT PQRRKRAIIR
LNKKGTIWNL PLKQNIVSVE QAIGNLPSIE SGKHSGLKWH YGRGHTEQQI EWMKHTPTGK
SAFENLVHYP RKANGEKVKG YHSSYRRIRW DEPAPTITIR NDAISSQRNV HPGRPLLDGT
YSDARVLSVL ELMRLTGLPD NWEIPDDTPE ILIRQIIGEC IPPLLIENIT REIFNEN
