MTHA_HAEPH
ID MTHA_HAEPH Reviewed; 372 AA.
AC P50192;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Type II methyltransferase M1.HphI {ECO:0000303|PubMed:12654995};
DE Short=M1.HphI {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase HphIA;
DE AltName: Full=M.Hphi(C);
DE AltName: Full=Modification methylase HphIA;
DE Short=M.HphIA {ECO:0000303|PubMed:8759008};
GN Name=hphIAM; Synonyms=hphIMC {ECO:0000303|PubMed:8759008};
OS Haemophilus parahaemolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=735;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 49700;
RX PubMed=8759008; DOI=10.1093/nar/24.14.2760;
RA Lubys A., Lubiene J., Kulakauskkas S., Stankevicius K., Timinskas A.,
RA Janulaitis A.;
RT "Cloning and analysis of the genes encoding the type IIS restriction-
RT modification system HphI from Haemophilus parahaemolyticus.";
RL Nucleic Acids Res. 24:2760-2766(1996).
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 the double-stranded sequence 5'-
CC GGTGA-3' and protects the DNA from cleavage by the HphI endonuclease
CC (PubMed:8759008). Probably methylates C-2 on the bottom strand
CC (Probable) (PubMed:12654995). {ECO:0000269|PubMed:8759008,
CC ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:8759008}.
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 -!- MISCELLANEOUS: Both this methylase and M2.HphI protect DNA from
CC cleavage by HphI. {ECO:0000269|PubMed:8759008}.
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; X85374; CAA59690.1; -; Genomic_DNA.
DR PIR; S70707; S70707.
DR AlphaFoldDB; P50192; -.
DR SMR; P50192; -.
DR REBASE; 203182; M.Bam1267ORF2759P.
DR REBASE; 203184; M.Bam1267ORF990P.
DR REBASE; 203185; M.Bam1267ORF665P.
DR REBASE; 3660; M1.HphI.
DR PRO; PR:P50192; -.
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..372
FT /note="Type II methyltransferase M1.HphI"
FT /id="PRO_0000087884"
FT DOMAIN 45..372
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
SQ SEQUENCE 372 AA; 42248 MW; 8CC8FF7A73017DDE CRC64;
MGFHSKNNSE YNGDFIILSS IYYWMILLYC IKFFLSKYLI YCMSLTYIDL FSGAGGFSLG
FDRAGFHQLL SVEIEPHYCD TYRANFPDHQ VLQQDLTTLS DDNLLRHINH RKVDVVIGGP
PCQGFSMAGK IGRTFADDPR NHLFKEFVRV VKLTQPKFFV MENVARLFTH NSGKTRAEIT
EQFERLGYKV KCKVLNAADF GVPQLRSRIV FIGRKDGGEI TFPEPSHTEY NTVGDAIGHF
PKLNAGENSL ILNHEAMNHS TQMLEKMSFV KNGGDRNDIP ESLRPISGDV RKYIRYHSDK
PSVCVTGDMR KVFHYEQNRA LTVRELAALQ SFPDDFVFLG KKIAQQQQVG NAVPPLLAQA
IAEAVLKMNT NE
