Modification methylase HhaI
Details
- Name
- Modification methylase HhaI
- Synonyms
- 2.1.1.37
- Cytosine-specific methyltransferase HhaI
- M.HhaI
- Gene Name
- hhaIM
- Organism
- Haemophilus parahaemolyticus
- Amino acid sequence
>lcl|BSEQ0016814|Modification methylase HhaI MIEIKDKQLTGLRFIDLFAGLGGFRLALESCGAECVYSNEWDKYAQEVYEMNFGEKPEGD ITQVNEKTIPDHDILCAGFPCQAFSISGKQKGFEDSRGTLFFDIARIVREKKPKVVFMEN VKNFASHDNGNTLEVVKNTMNELDYSFHAKVLNALDYGIPQKRERIYMICFRNDLNIQNF QFPKPFELNTFVKDLLLPDSEVEHLVIDRKDLVMTNQEIEQTTPKTVRLGIVGKGGQGER IYSTRGIAITLSAYGGGIFAKTGGYLVNGKTRKLHPRECARVMGYPDSYKVHPSTSQAYK QFGNSVVINVLQYIAYNIGSSLNFKPY
- Number of residues
- 327
- Molecular Weight
- 36996.04
- Theoretical pI
- 7.82
- GO Classification
- FunctionsDNA (cytosine-5-)-methyltransferase activityProcessesDNA restriction-modification system
- General Function
- Dna (cytosine-5-)-methyltransferase activity
- Specific Function
- This methylase recognizes the double-stranded sequence GCGC, causes specific methylation on C-2 on both strands, and protects the DNA from cleavage by the HhaI endonuclease.
- Pfam Domain Function
- DNA_methylase (PF00145)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0004954|984 bp ATGATTGAAATAAAAGATAAACAGCTCACAGGATTACGCTTTATTGACCTTTTTGCAGGA TTAGGTGGCTTTAGACTTGCTTTAGAATCTTGCGGTGCTGAGTGCGTTTATTCTAATGAA TGGGATAAATATGCACAAGAAGTATATGAGATGAATTTTGGTGAAAAGCCTGAGGGCGAC ATTACCCAAGTAAATGAGAAAACCATTCCTGATCACGACATTTTATGTGCAGGGTTTCCG TGCCAAGCGTTTTCTATTAGTGGAAAACAAAAAGGATTCGAGGACAGCAGAGGTACGCTC TTTTTTGATATTGCACGTATTGTCCGTGAAAAAAAACCTAAAGTGGTTTTTATGGAAAAT GTGAAAAATTTTGCATCGCATGATAATGGAAATACGTTAGAAGTTGTAAAAAATACAATG AATGAATTGGACTATTCTTTTCATGCTAAAGTATTAAATGCTTTAGATTATGGGATTCCA CAGAAAAGGGAACGTATCTATATGATTTGTTTTCGCAATGATCTCAATATTCAAAATTTC CAATTTCCAAAACCTTTTGAGCTTAATACTTTTGTGAAAGATTTGTTATTACCTGATAGC GAGGTGGAACACTTAGTTATTGATAGAAAAGATTTGGTAATGACAAACCAAGAAATTGAG CAAACAACCCCCAAAACAGTTCGACTTGGTATTGTAGGAAAAGGTGGGCAAGGAGAACGA ATTTATAGCACAAGAGGCATTGCAATTACCTTATCTGCTTATGGTGGCGGCATTTTCGCT AAGACAGGGGGATATTTAGTAAACGGGAAGACACGGAAATTACACCCTAGAGAGTGTGCT AGAGTAATGGGCTACCCAGATAGTTATAAAGTCCACCCGTCAACCAGCCAAGCATATAAA CAATTTGGTAACTCAGTTGTTATCAATGTACTTCAATATATTGCTTATAACATTGGTTCA TCATTAAATTTCAAACCATATTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P05102 UniProtKB Entry Name MTH1_HAEPH GenBank Gene ID J02677 - General References
- Caserta M, Zacharias W, Nwankwo D, Wilson GG, Wells RD: Cloning, sequencing, in vivo promoter mapping, and expression in Escherichia coli of the gene for the HhaI methyltransferase. J Biol Chem. 1987 Apr 5;262(10):4770-7. [Article]
- Mi S, Roberts RJ: The DNA binding affinity of HhaI methylase is increased by a single amino acid substitution in the catalytic center. Nucleic Acids Res. 1993 May 25;21(10):2459-64. [Article]
- Mi S, Alonso D, Roberts RJ: Functional analysis of Gln-237 mutants of HhaI methyltransferase. Nucleic Acids Res. 1995 Feb 25;23(4):620-7. [Article]
- Cheng X, Kumar S, Posfai J, Pflugrath JW, Roberts RJ: Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine. Cell. 1993 Jul 30;74(2):299-307. [Article]
- Klimasauskas S, Kumar S, Roberts RJ, Cheng X: HhaI methyltransferase flips its target base out of the DNA helix. Cell. 1994 Jan 28;76(2):357-69. [Article]
- Kumar S, Horton JR, Jones GD, Walker RT, Roberts RJ, Cheng X: DNA containing 4'-thio-2'-deoxycytidine inhibits methylation by HhaI methyltransferase. Nucleic Acids Res. 1997 Jul 15;25(14):2773-83. [Article]
- O'Gara M, Horton JR, Roberts RJ, Cheng X: Structures of HhaI methyltransferase complexed with substrates containing mismatches at the target base. Nat Struct Biol. 1998 Oct;5(10):872-7. [Article]
- O'Gara M, Zhang X, Roberts RJ, Cheng X: Structure of a binary complex of HhaI methyltransferase with S-adenosyl-L-methionine formed in the presence of a short non-specific DNA oligonucleotide. J Mol Biol. 1999 Mar 26;287(2):201-9. [Article]