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Protein

Modification methylase Eco57IB

Gene

eco57IBM

Organism
Escherichia coli
Status
Reviewed-Annotation score: 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

GO - Biological processi

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 Eco57IBPRO_0000087940Add
BLAST

Proteomic databases

PRIDEiP25240.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP25240.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the N(4)/N(6)-methyltransferase family.Curated

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P25240-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFKADQTSQ KLRGGYYTPQ NLADYVTKWV LSKNPKTILE PSCGDGVFIQ
60 70 80 90 100
AIANNGYNSN IELFCFELFD TEASKALERC KLNNFSNATI TEGDFLVWAN
110 120 130 140 150
ECLKKNKQIF DGALGNPPFI RYQFLERNFQ EQAQLVFEHL DLKFTKHTNA
160 170 180 190 200
WVPFLLSSLA LLKQGGRIGM VIPSEISHVM HAQSLRSYLG HVCSKIVIID
210 220 230 240 250
PKEIWFEDTL QGAVILLAEK KQYPDEASQG VGIVSVSGFE FLQEDPNVLF
260 270 280 290 300
NDTAGINGET VEGKWTKATL SIDELQLIKR VIAHPDVRKF KDIAKVDVGR
310 320 330 340 350
YCDGANNYFL VDNETVKLYK LERFAHPMFG RSQHCPGIIY DEKQHIENQE
360 370 380 390 400
KGLPTNFLYI DEEFEYLSKS VKNYIKLGEV EEYHKRYKCR IRKPWFKVPS
410 420 430 440 450
VYSTEIGMLK RCHDAPRLIH NRVRAYTTDT AYRVSSTVTS TENLVCSFLN
460 470 480 490 500
PITVITAELE GLFYGGGVLE LVPSEIEKLY ILIVEGLEHN VEELNLLIKD
510 520 530 540
GQIERVIRQQ GSLILGTLGF TQEENEKLVE IGRSLEIEGY VSRV
Length:544
Mass (Da):62,013
Last modified:May 1, 1992 - v1
Checksum:i53A1D5D7337AB4FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74821 Genomic DNA. Translation: AAA23388.1.
X61122 Genomic DNA. Translation: CAA43433.1.
PIRiS26425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74821 Genomic DNA. Translation: AAA23388.1.
X61122 Genomic DNA. Translation: CAA43433.1.
PIRiS26425.

3D structure databases

ProteinModelPortaliP25240.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi5234. M.Eco57I.

Proteomic databases

PRIDEiP25240.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

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

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: April 29, 2015
This is version 71 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.