MTH2_HAEPA
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 03-AUG-2022, entry version 100.
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; Proteobacteria; 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 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 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..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
