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
Functions
DNA (cytosine-5-)-methyltransferase activity
Processes
DNA 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
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
ResourceLink
UniProtKB IDP05102
UniProtKB Entry NameMTH1_HAEPH
GenBank Gene IDJ02677
General References
  1. 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. [PubMed:3549710]
  2. 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. [PubMed:8506140]
  3. 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. [PubMed:7899082]
  4. 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. [PubMed:8343957]
  5. 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. [PubMed:8293469]
  6. 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. [PubMed:9207024]
  7. 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. [PubMed:9783745]
  8. 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. [PubMed:10080885]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01752S-adenosyl-L-homocysteineexperimentalunknownDetails