ID   MTG2_AVIVO              Reviewed;         358 AA.
AC   P25283;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-MAY-2023, entry version 84.
DE   RecName: Full=Type II methlytransferase M2.HgaI {ECO:0000303|PubMed:12654995};
DE            Short=M2.HgaI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37 {ECO:0000269|PubMed:1856224};
DE   AltName: Full=Cytosine-specific methyltransferase HgaIB;
DE   AltName: Full=M.HgaI-2 {ECO:0000303|PubMed:1856224};
DE   AltName: Full=Modification methylase HgaIB;
DE            Short=M.HgaIB;
GN   Name=hgaIBM;
OS   Avibacterium volantium (Pasteurella volantium).
OC   Bacteria; Pseudomonadota; 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   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'-GACGC-
CC       3', methylates C-3, 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}.
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DR   EMBL; D90363; BAA14378.1; -; Genomic_DNA.
DR   EMBL; D17388; BAA04207.1; -; Genomic_DNA.
DR   PIR; A39467; A39467.
DR   AlphaFoldDB; P25283; -.
DR   SMR; P25283; -.
DR   PRO; PR:P25283; -.
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; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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..358
FT                   /note="Type II methlytransferase M2.HgaI"
FT                   /id="PRO_0000087880"
FT   DOMAIN          3..358
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   358 AA;  40690 MW;  0373563207685A91 CRC64;
     MKINAMSLFS SAGIGELDLH KGNLNFVVAN ELLKKRADTY QFFYPETKMF QGDISDEKLK
     REILLSAQQN NVKFLLATPP CQGLSSVGKN KHQDHFIKDN RNFLIFEVFE FIDVLNLDFI
     LIENVPRFIE MYFPYNGQLL LLEEILKIKY ASKYQIDIVI LNAKDYGICQ SRPRAIIKMY
     KYGITWKLPT IQAEISLQRA IGHLPPLEPG EVSSIKWHSA PNVKPSIIEA IRHTKPGTSA
     ISNPIFYPKK DNGERIKGFH NTYKRMEWDK PAPARTTYSG SISSHNNIHP GRLQLDGTYS
     DPRVLSLLET FIVSSIDENI EFPPGSSETY IRTIIGEAIP PKLLSAICFP DGENINVK
//