MTH2_HAEAE
ID MTH2_HAEAE Reviewed; 318 AA.
AC O30868;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Type II methyltransferase M.HaeII {ECO:0000303|PubMed:12654995};
DE Short=M.HaeII {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase HaeII;
DE AltName: Full=Modification methylase HaeII;
GN Name=haeIIM; Synonyms=dcmA {ECO:0000303|PubMed:9628358};
OS Haemophilus aegyptius.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=197575;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11116 / CCUG 25716 / NCTC 8502 / 180-a;
RX PubMed=9628358;
RA Stein D.C., Gunn J.S., Piekarowicz A.;
RT "Sequence similarities between the genes encoding the S.NgoI and HaeII
RT restriction/modification systems.";
RL Biol. Chem. 379:575-578(1998).
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, recognizes the double-stranded sequence 5'-
CC RGCGCY-3', methylates C-? on both strands, and protects the DNA from
CC cleavage by the HaeII endonuclease. {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 -!- 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; AF019752; AAB70829.1; -; Genomic_DNA.
DR AlphaFoldDB; O30868; -.
DR SMR; O30868; -.
DR REBASE; 3409; M.HaeII.
DR PRO; PR:O30868; -.
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 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..318
FT /note="Type II methyltransferase M.HaeII"
FT /id="PRO_0000087877"
FT DOMAIN 4..304
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
SQ SEQUENCE 318 AA; 35670 MW; CA879CF66731D434 CRC64;
MKEYKTIDLF AGIGGIRLGF EAFGCKNVFS SEWDKYAQSM YEVNFGEKPF GDINDISPSD
IPDHDILLAG FPCQPFSIAG KGLGFADTRG TLFFNIEAIL KAKKPKAFLL ENVKRLTTHD
NGNTFKVIND KLNKLGYTVY HKVLNTLDFG LPQKRERIYI VGFLDKLHFE FPKPIGKYEE
LSNILESDDV VPNNYFLSDE LKRKRLSSIT KDVPYPSIWH ENISGNVSAL PYSCALSVGG
SYNYLVVNGV RRLTGPEMLR LQGFPDTFEI NIPYSQVRKV AGNSVSVPVI RAIAGSMINS
LNMATRKIYQ AIQLSLLD
