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   27-MAR-2024, entry version 84.
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; Pseudomonadota; 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   REBASE; 767834; M2.SspSPORF1906P.
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   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
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; IPR031303; C5_meth_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 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; 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
//