ID   MTH2_HAEPA              Reviewed;         358 AA.
AC   P15446;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   13-SEP-2023, entry version 104.
DE   RecName: Full=Type II methyltransferase M.HpaII {ECO:0000303|PubMed:12654995};
DE            Short=M.HpaII {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase HpaII;
DE   AltName: Full=Modification methylase HpaII;
GN   Name=hpaIIM {ECO:0000303|PubMed:2183189};
OS   Haemophilus parainfluenzae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 49669;
RX   PubMed=2183189; DOI=10.1093/nar/18.6.1377;
RA   Card C.O., Wilson G.G., Weule K., Hasapes J., Kiss A., Roberts R.J.;
RT   "Cloning and characterization of the HpaII methylase gene.";
RL   Nucleic Acids Res. 18:1377-1383(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF CYS-55.
RX   PubMed=7514149; DOI=10.1016/0378-1119(94)90348-4;
RA   Kulakauskas S., Barsomian J.M., Lubys A., Roberts R.J., Wilson G.G.;
RT   "Organization and sequence of the HpaII restriction-modification system and
RT   adjacent genes.";
RL   Gene 142:9-15(1994).
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 the double-stranded sequence 5'-
CC       CCGG-3', methylates C-2 on both strands, and protects the DNA from
CC       cleavage by the HpaII endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:2183189}.
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   -!- SUBUNIT: Monomer.
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; X51322; CAA35705.1; -; Genomic_DNA.
DR   EMBL; L17342; AAA20481.1; -; Genomic_DNA.
DR   PIR; S15908; S15908.
DR   AlphaFoldDB; P15446; -.
DR   SMR; P15446; -.
DR   REBASE; 3432; M.HpaII.
DR   PRO; PR:P15446; -.
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   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   Gene3D; 3.90.120.30; -; 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   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
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 methyltransferase M.HpaII"
FT                   /id="PRO_0000087883"
FT   DOMAIN          32..356
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
FT   MUTAGEN         55
FT                   /note="C->Y: Grows at 30 but not 42 degrees Celsius, has
FT                   reduced methylase activity at 42 degrees Celsius."
FT                   /evidence="ECO:0000269|PubMed:7514149"
SQ   SEQUENCE   358 AA;  40400 MW;  ACE69BFD511C37EB CRC64;
     MKDVLDDNLL EEPAAQYSLF EPESNPNLRE KFTFIDLFAG IGGFRIAMQN LGGKCIFSSE
     WDEQAQKTYE ANFGDLPYGD ITLEETKAFI PEKFDILCAG FPCQAFSIAG KRGGFEDTRG
     TLFFDVAEII RRHQPKAFFL ENVKGLKNHD KGRTLKTILN VLREDLGYFV PEPAIVNAKN
     FGVPQNRERI YIVGFHKSTG VNSFSYPEPL DKIVTFADIR EEKTVPTKYY LSTQYIDTLR
     KHKERHESKG NGFGYEIIPD DGIANAIVVG GMGRERNLVI DHRITDFTPT TNIKGEVNRE
     GIRKMTPREW ARLQGFPDSY VIPVSDASAY KQFGNSVAVP AIQATGKKIL EKLGNLYD
//