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P05102

- MTH1_HAEPH

UniProt

P05102 - MTH1_HAEPH

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Protein

Modification methylase HhaI

Gene

hhaIM

Organism
Haemophilus parahaemolyticus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.PROSITE-ProRule annotation

Kineticsi

  1. KM=69 nM for DNA1 Publication
  2. KM=15 nM for S-adenosyl-L-methionine (SAM)1 Publication

Vmax=87.0 nmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei81 – 811

GO - Molecular functioni

  1. DNA (cytosine-5-)-methyltransferase activity Source: UniProtKB-EC
  2. DNA binding Source: InterPro

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

S-adenosyl-L-methionine

Protein family/group databases

REBASEi3421. M.HhaI.

Names & Taxonomyi

Protein namesi
Recommended name:
Modification methylase HhaI (EC:2.1.1.37)
Short name:
M.HhaI
Alternative name(s):
Cytosine-specific methyltransferase HhaI
Gene namesi
Name:hhaIM
OrganismiHaemophilus parahaemolyticus
Taxonomic identifieri735 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi237 – 2371Q → X: Decrease in enzyme activity due to 98%-99% loss of DNA-binding activity. No change in substrate specificity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Modification methylase HhaIPRO_0000087882Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
327
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 114Combined sources
Beta strandi13 – 175Combined sources
Turni20 – 223Combined sources
Helixi23 – 308Combined sources
Beta strandi34 – 396Combined sources
Helixi43 – 5311Combined sources
Helixi61 – 633Combined sources
Helixi66 – 683Combined sources
Beta strandi73 – 786Combined sources
Turni82 – 843Combined sources
Turni86 – 894Combined sources
Helixi92 – 943Combined sources
Helixi96 – 983Combined sources
Helixi100 – 11112Combined sources
Beta strandi114 – 1218Combined sources
Helixi122 – 1254Combined sources
Helixi127 – 1304Combined sources
Helixi131 – 14212Combined sources
Beta strandi148 – 1536Combined sources
Helixi154 – 1574Combined sources
Beta strandi164 – 1729Combined sources
Helixi173 – 1753Combined sources
Helixi192 – 1943Combined sources
Helixi199 – 2013Combined sources
Helixi203 – 2053Combined sources
Beta strandi213 – 2164Combined sources
Beta strandi228 – 2325Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi244 – 2463Combined sources
Turni258 – 2625Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi270 – 2734Combined sources
Helixi276 – 2827Combined sources
Helixi295 – 30410Combined sources
Helixi308 – 32316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
10MHX-ray2.55A1-327[»]
1FJXX-ray2.26A1-327[»]
1HMYX-ray2.50A1-327[»]
1M0EX-ray2.50A1-327[»]
1MHTX-ray2.60A1-327[»]
1SKMX-ray2.20A1-327[»]
1SVUX-ray2.66A/B1-327[»]
2C7OX-ray1.90A1-327[»]
2C7PX-ray1.70A1-327[»]
2C7QX-ray1.85A1-327[»]
2C7RX-ray1.90A1-327[»]
2HMYX-ray2.61B1-327[»]
2HR1X-ray1.96A1-327[»]
2I9KX-ray2.65A1-327[»]
2UYCX-ray2.00A1-327[»]
2UYHX-ray2.63A1-327[»]
2UZ4X-ray2.10A1-327[»]
2Z6AX-ray2.88A1-327[»]
2Z6QX-ray2.79A1-327[»]
2Z6UX-ray2.72A1-327[»]
2ZCJX-ray2.75A1-327[»]
3EEOX-ray1.94A1-327[»]
3MHTX-ray2.70A1-327[»]
4MHTX-ray2.70A1-327[»]
5MHTX-ray2.70A1-327[»]
6MHTX-ray2.05A1-327[»]
7MHTX-ray2.87A1-327[»]
8MHTX-ray2.76A1-327[»]
9MHTX-ray2.39A1-327[»]
ProteinModelPortaliP05102.
SMRiP05102. Positions 1-327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05102.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 325314SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase C5-type domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERiPTHR10629. PTHR10629. 1 hit.
PfamiPF00145. DNA_methylase. 1 hit.
[Graphical view]
PRINTSiPR00105. C5METTRFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00675. dcm. 1 hit.
PROSITEiPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05102-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIEIKDKQLT GLRFIDLFAG LGGFRLALES CGAECVYSNE WDKYAQEVYE
60 70 80 90 100
MNFGEKPEGD ITQVNEKTIP DHDILCAGFP CQAFSISGKQ KGFEDSRGTL
110 120 130 140 150
FFDIARIVRE KKPKVVFMEN VKNFASHDNG NTLEVVKNTM NELDYSFHAK
160 170 180 190 200
VLNALDYGIP QKRERIYMIC FRNDLNIQNF QFPKPFELNT FVKDLLLPDS
210 220 230 240 250
EVEHLVIDRK DLVMTNQEIE QTTPKTVRLG IVGKGGQGER IYSTRGIAIT
260 270 280 290 300
LSAYGGGIFA KTGGYLVNGK TRKLHPRECA RVMGYPDSYK VHPSTSQAYK
310 320
QFGNSVVINV LQYIAYNIGS SLNFKPY
Length:327
Mass (Da):36,996
Last modified:August 13, 1987 - v1
Checksum:iEF8A297E1DF819EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02677 Genomic DNA. Translation: AAA24989.1.
PIRiA26260. XYHIH1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02677 Genomic DNA. Translation: AAA24989.1 .
PIRi A26260. XYHIH1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
10MH X-ray 2.55 A 1-327 [» ]
1FJX X-ray 2.26 A 1-327 [» ]
1HMY X-ray 2.50 A 1-327 [» ]
1M0E X-ray 2.50 A 1-327 [» ]
1MHT X-ray 2.60 A 1-327 [» ]
1SKM X-ray 2.20 A 1-327 [» ]
1SVU X-ray 2.66 A/B 1-327 [» ]
2C7O X-ray 1.90 A 1-327 [» ]
2C7P X-ray 1.70 A 1-327 [» ]
2C7Q X-ray 1.85 A 1-327 [» ]
2C7R X-ray 1.90 A 1-327 [» ]
2HMY X-ray 2.61 B 1-327 [» ]
2HR1 X-ray 1.96 A 1-327 [» ]
2I9K X-ray 2.65 A 1-327 [» ]
2UYC X-ray 2.00 A 1-327 [» ]
2UYH X-ray 2.63 A 1-327 [» ]
2UZ4 X-ray 2.10 A 1-327 [» ]
2Z6A X-ray 2.88 A 1-327 [» ]
2Z6Q X-ray 2.79 A 1-327 [» ]
2Z6U X-ray 2.72 A 1-327 [» ]
2ZCJ X-ray 2.75 A 1-327 [» ]
3EEO X-ray 1.94 A 1-327 [» ]
3MHT X-ray 2.70 A 1-327 [» ]
4MHT X-ray 2.70 A 1-327 [» ]
5MHT X-ray 2.70 A 1-327 [» ]
6MHT X-ray 2.05 A 1-327 [» ]
7MHT X-ray 2.87 A 1-327 [» ]
8MHT X-ray 2.76 A 1-327 [» ]
9MHT X-ray 2.39 A 1-327 [» ]
ProteinModelPortali P05102.
SMRi P05102. Positions 1-327.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 3421. M.HhaI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P05102.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR10629. PTHR10629. 1 hit.
Pfami PF00145. DNA_methylase. 1 hit.
[Graphical view ]
PRINTSi PR00105. C5METTRFRASE.
SUPFAMi SSF53335. SSF53335. 1 hit.
TIGRFAMsi TIGR00675. dcm. 1 hit.
PROSITEi PS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, sequencing, in vivo promoter mapping, and expression in Escherichia coli of the gene for the HhaI methyltransferase."
    Caserta M., Zacharias W., Nwankwo D.O., Wilson G.G., Wells R.D.
    J. Biol. Chem. 262:4770-4777(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 10014 / CCUG 3716 / NCTC 8479.
  2. "The DNA binding affinity of HhaI methylase is increased by a single amino acid substitution in the catalytic center."
    Mi S., Roberts R.J.
    Nucleic Acids Res. 21:2459-2464(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  3. "Functional analysis of Gln-237 mutants of HhaI methyltransferase."
    Mi S., Alonso D., Roberts R.J.
    Nucleic Acids Res. 23:620-627(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLN-237.
  4. "Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine."
    Cheng X., Kumar S., Posfai J., Pflugrath J.W., Roberts R.J.
    Cell 74:299-307(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  5. "HhaI methyltransferase flips its target base out of the DNA helix."
    Klimasauskas S., Kumar S., Roberts R.J., Cheng X.
    Cell 76:357-369(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  6. "DNA containing 4'-thio-2'-deoxycytidine inhibits methylation by HhaI methyltransferase."
    Kumar S., Horton J.R., Jones G.D., Walker R.T., Roberts R.J., Cheng X.
    Nucleic Acids Res. 25:2773-2783(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
  7. "Structures of HhaI methyltransferase complexed with substrates containing mismatches at the target base."
    O'Gara M., Horton J.R., Roberts R.J., Cheng X.
    Nat. Struct. Biol. 5:872-877(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS).
  8. "Structure of a binary complex of HhaI methyltransferase with S-adenosyl-L-methionine formed in the presence of a short non-specific DNA oligonucleotide."
    O'Gara M., Zhang X., Roberts R.J., Cheng X.
    J. Mol. Biol. 287:201-209(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS).

Entry informationi

Entry nameiMTH1_HAEPH
AccessioniPrimary (citable) accession number: P05102
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 26, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Strain ATCC 10014 was originally thought to originate from H.haemolyticus.Curated

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3