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P25240

- MT57_ECOLX

UniProt

P25240 - MT57_ECOLX

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Protein
Modification methylase Eco57IB
Gene
eco57IBM, eco57IM
Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

This methylase recognizes the double-stranded sequence 5'-CTGAAG-3' in one strand and 5'-CTTCAG-3' in the other, causes specific methylation on A-5 on one strand, and protects the DNA from cleavage by the Eco57I endonuclease.

Catalytic activityi

S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. N-methyltransferase activity Source: InterPro
  3. site-specific DNA-methyltransferase (adenine-specific) activity Source: UniProtKB-EC

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

REBASEi5234. M.Eco57I.

Names & Taxonomyi

Protein namesi
Recommended name:
Modification methylase Eco57IB (EC:2.1.1.72)
Short name:
M.Eco57IB
Alternative name(s):
Adenine-specific methyltransferase Eco57IB
Gene namesi
Name:eco57IBM
Synonyms:eco57IM
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 544544Modification methylase Eco57IB
PRO_0000087940Add
BLAST

Proteomic databases

PRIDEiP25240.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP25240.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSiPR00507. N12N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25240-1 [UniParc]FASTAAdd to Basket

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MKFKADQTSQ KLRGGYYTPQ NLADYVTKWV LSKNPKTILE PSCGDGVFIQ    50
AIANNGYNSN IELFCFELFD TEASKALERC KLNNFSNATI TEGDFLVWAN 100
ECLKKNKQIF DGALGNPPFI RYQFLERNFQ EQAQLVFEHL DLKFTKHTNA 150
WVPFLLSSLA LLKQGGRIGM VIPSEISHVM HAQSLRSYLG HVCSKIVIID 200
PKEIWFEDTL QGAVILLAEK KQYPDEASQG VGIVSVSGFE FLQEDPNVLF 250
NDTAGINGET VEGKWTKATL SIDELQLIKR VIAHPDVRKF KDIAKVDVGR 300
YCDGANNYFL VDNETVKLYK LERFAHPMFG RSQHCPGIIY DEKQHIENQE 350
KGLPTNFLYI DEEFEYLSKS VKNYIKLGEV EEYHKRYKCR IRKPWFKVPS 400
VYSTEIGMLK RCHDAPRLIH NRVRAYTTDT AYRVSSTVTS TENLVCSFLN 450
PITVITAELE GLFYGGGVLE LVPSEIEKLY ILIVEGLEHN VEELNLLIKD 500
GQIERVIRQQ GSLILGTLGF TQEENEKLVE IGRSLEIEGY VSRV 544
Length:544
Mass (Da):62,013
Last modified:May 1, 1992 - v1
Checksum:i53A1D5D7337AB4FA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74821 Genomic DNA. Translation: AAA23388.1.
X61122 Genomic DNA. Translation: CAA43433.1.
PIRiS26425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74821 Genomic DNA. Translation: AAA23388.1 .
X61122 Genomic DNA. Translation: CAA43433.1 .
PIRi S26425.

3D structure databases

ProteinModelPortali P25240.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 5234. M.Eco57I.

Proteomic databases

PRIDEi P25240.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF02384. N6_Mtase. 1 hit.
[Graphical view ]
PRINTSi PR00507. N12N6MTFRASE.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS00092. N6_MTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and sequence analysis of the genes coding for Eco57I type IV restriction-modification enzymes."
    Janulaitis A., Vaisvila R., Timinskas A., Klimasauskas S., Butkus V.
    Nucleic Acids Res. 20:6051-6056(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: RFL57.
  2. "Purification and properties of the Eco57I restriction endonuclease and methylase -- prototypes of a new class (type IV)."
    Janulaitis A., Petrusyte M., Maneliene Z., Klimasauskas S., Butkus V.
    Nucleic Acids Res. 20:6043-6049(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiMT57_ECOLX
AccessioniPrimary (citable) accession number: P25240
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 11, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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