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UniProtKB/Swiss-Prot entry P05102


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MTH1_HAEPH
Primary accession number P05102
Secondary accession numbers None
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 84)
Name and origin of the protein
Protein name Modification methylase HhaI
Synonyms M.HhaI
EC 2.1.1.37
Cytosine-specific methyltransferase HhaI
Gene name
Name: hhaIM
From
Haemophilus parahaemolyticus [TaxID: 735] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Haemophilus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 10014 / CCUG 3716 / NCTC 8479;
PubMed=3549710 [NCBI, ExPASy, EBI, Israel, Japan]
Caserta M., Zacharias W., Nwankwo D.O., Wilson G.G., Wells R.D.;
"Cloning, sequencing, in vivo promoter mapping, and expression in Escherichia coli of the gene for the HhaI methyltransferase.";
J. Biol. Chem. 262:4770-4777(1987).
[2]
MUTAGENESIS.
DOI=10.1093/nar/21.10.2459; PubMed=8506140 [NCBI, ExPASy, EBI, Israel, Japan]
Mi S., Roberts R.J.;
"The DNA binding affinity of HhaI methylase is increased by a single amino acid substitution in the catalytic center.";
Nucleic Acids Res. 21:2459-2464(1993).
[3]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLN-237.
DOI=10.1093/nar/23.4.620; PubMed=7899082 [NCBI, ExPASy, EBI, Israel, Japan]
Mi S., Alonso D., Roberts R.J.;
"Functional analysis of Gln-237 mutants of HhaI methyltransferase.";
Nucleic Acids Res. 23:620-627(1995).
[4]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1016/0092-8674(93)90421-L; PubMed=8343957 [NCBI, ExPASy, EBI, Israel, Japan]
Cheng X., Kumar S., Posfai J., Pflugrath J.W., Roberts R.J.;
"Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine.";
Cell 74:299-307(1993).
[5]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
DOI=10.1016/0092-8674(94)90342-5; PubMed=8293469 [NCBI, ExPASy, EBI, Israel, Japan]
Klimasauskas S., Kumar S., Roberts R.J., Cheng X.;
"HhaI methyltransferase flips its target base out of the DNA helix.";
Cell 76:357-369(1994).
[6]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
DOI=10.1093/nar/25.14.2773; PubMed=9207024 [NCBI, ExPASy, EBI, Israel, Japan]
Kumar S., Horton J.R., Jones G.D., Walker R.T., Roberts R.J., Cheng X.;
"DNA containing 4'-thio-2'-deoxycytidine inhibits methylation by HhaI methyltransferase.";
Nucleic Acids Res. 25:2773-2783(1997).
[7]
X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS).
DOI=10.1038/2312; PubMed=9783745 [NCBI, ExPASy, EBI, Israel, Japan]
O'Gara M., Horton J.R., Roberts R.J., Cheng X.;
"Structures of HhaI methyltransferase complexed with substrates containing mismatches at the target base.";
Nat. Struct. Biol. 5:872-877(1998).
[8]
X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS).
DOI=10.1006/jmbi.1999.2608; PubMed=10080885 [NCBI, ExPASy, EBI, Israel, Japan]
O'Gara M., Zhang X., Roberts R.J., 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. 287:201-209(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J02677; AAA24989.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A26260; XYHIH1.
3D structure databases
PDB
10MH; X-ray; 2.55 A; A=1-327.[ExPASy / RCSB / EBI]
1FJX; X-ray; 2.26 A; A=1-327.[ExPASy / RCSB / EBI]
1HMY; X-ray; 2.50 A; A=1-327.[ExPASy / RCSB / EBI]
1M0E; X-ray; 2.50 A; A=1-327.[ExPASy / RCSB / EBI]
1MHT; X-ray; 2.60 A; A=1-327.[ExPASy / RCSB / EBI]
1SKM; X-ray; 2.20 A; A=1-327.[ExPASy / RCSB / EBI]
1SVU; X-ray; 2.66 A; A/B=1-327.[ExPASy / RCSB / EBI]
2C7O; X-ray; 1.90 A; A=1-327.[ExPASy / RCSB / EBI]
2C7P; X-ray; 1.70 A; A=1-327.[ExPASy / RCSB / EBI]
2C7Q; X-ray; 1.85 A; A=1-327.[ExPASy / RCSB / EBI]
2C7R; X-ray; 1.90 A; A=1-327.[ExPASy / RCSB / EBI]
2HMY; X-ray; 2.61 A; B=1-327.[ExPASy / RCSB / EBI]
2HR1; X-ray; 1.96 A; A=1-327.[ExPASy / RCSB / EBI]
2I9K; X-ray; 2.65 A; A=1-327.[ExPASy / RCSB / EBI]
2UYC; X-ray; 2.00 A; A=1-327.[ExPASy / RCSB / EBI]
2UYH; X-ray; 2.63 A; A=1-327.[ExPASy / RCSB / EBI]
2UZ4; X-ray; 2.10 A; A=1-327.[ExPASy / RCSB / EBI]
2Z6A; X-ray; 2.88 A; A=1-327.[ExPASy / RCSB / EBI]
2Z6Q; X-ray; 2.79 A; A=1-327.[ExPASy / RCSB / EBI]
2Z6U; X-ray; 2.72 A; A=1-327.[ExPASy / RCSB / EBI]
2ZCJ; X-ray; 2.75 A; A=1-327.[ExPASy / RCSB / EBI]
3MHT; X-ray; 2.70 A; A=1-327.[ExPASy / RCSB / EBI]
4MHT; X-ray; 2.70 A; A=1-327.[ExPASy / RCSB / EBI]
5MHT; X-ray; 2.70 A; A=1-327.[ExPASy / RCSB / EBI]
6MHT; X-ray; 2.05 A; A=1-327.[ExPASy / RCSB / EBI]
7MHT; X-ray; 2.87 A; A=1-327.[ExPASy / RCSB / EBI]
8MHT; X-ray; 2.76 A; A=1-327.[ExPASy / RCSB / EBI]
9MHT; X-ray; 2.39 A; A=1-327.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 10MH; -.
1FJX; -.
1HMY; -.
1M0E; -.
1MHT; -.
1SKM; -.
1SVU; -.
2C7O; -.
2C7P; -.
2C7Q; -.
2C7R; -.
2HMY; -.
2HR1; -.
2I9K; -.
2UYC; -.
2UYH; -.
2UZ4; -.
2Z6A; -.
2Z6Q; -.
2Z6U; -.
2ZCJ; -.
3MHT; -.
4MHT; -.
5MHT; -.
6MHT; -.
7MHT; -.
8MHT; -.
9MHT; -.
ModBase P05102.
Protein family/group databases
REBASE 3421; M.HhaI.
Ontologies
GO
GO:0003886; Molecular function: DNA (cytosine-5-)-methyltransferase activity (inferred from electronic annotation from EC).
GO:0009307; Biological process: DNA restriction-modification system (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001525; C5_DNA_meth.
Graphical view of domain structure.
PANTHER PTHR10629; C5_DNA_meth; 1.
Pfam PF00145; DNA_methylase; 1.
Pfam graphical view of domain structure.
PRINTS PR00105; C5METTRFRASE.
TIGRFAMs TIGR00675; dcm; 1.
PROSITE PS00094; C5_MTASE_1; 1.
PS00095; C5_MTASE_2; 1.
BLOCKS P05102.
ProtoNet P05102.
Other
LinkHub P05102; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Methyltransferase; Restriction system; S-adenosyl-L-methionine; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   327  327     Modification methylase HhaI. PRO_0000087882
ACT_SITE   81    81         
MUTAGEN   237   237        Q->X: Decrease in enzyme activity due to 98%-99% loss of DNA-binding activity. No change in substrate specificity. 
TURN   8    11  4      
STRAND   13    17  5      
HELIX   23    30  8      
STRAND   34    39  6      
HELIX   43    53  11      
HELIX   61    63  3      
HELIX   66    68  3      
STRAND   73    78  6      
TURN   82    84  3      
HELIX   92    94  3      
HELIX   96    98  3      
HELIX   101   111  11      
STRAND   114   121  8      
HELIX   122   124  3      
HELIX   127   130  4      
HELIX   131   142  12      
STRAND   148   153  6      
HELIX   154   156  3      
STRAND   164   172  9      
HELIX   173   175  3      
HELIX   192   195  4      
HELIX   199   201  3      
HELIX   203   205  3      
STRAND   228   232  5      
STRAND   240   243  4      
TURN   258   262  5      
STRAND   264   267  4      
STRAND   270   273  4      
HELIX   276   282  7      
HELIX   295   304  10      
HELIX   308   323  16      
Sequence information
Length: 327 AA [This is the length of the unprocessed precursor] Molecular weight: 36996 Da [This is the MW of the unprocessed precursor] CRC64: EF8A297E1DF819EB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIEIKDKQLT GLRFIDLFAG LGGFRLALES CGAECVYSNE WDKYAQEVYE MNFGEKPEGD 

        70         80         90        100        110        120 
ITQVNEKTIP DHDILCAGFP CQAFSISGKQ KGFEDSRGTL FFDIARIVRE KKPKVVFMEN 

       130        140        150        160        170        180 
VKNFASHDNG NTLEVVKNTM NELDYSFHAK VLNALDYGIP QKRERIYMIC FRNDLNIQNF 

       190        200        210        220        230        240 
QFPKPFELNT FVKDLLLPDS EVEHLVIDRK DLVMTNQEIE QTTPKTVRLG IVGKGGQGER 

       250        260        270        280        290        300 
IYSTRGIAIT LSAYGGGIFA KTGGYLVNGK TRKLHPRECA RVMGYPDSYK VHPSTSQAYK 

       310        320 
QFGNSVVINV LQYIAYNIGS SLNFKPY 

P05102 in FASTA format

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