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P25239

- T257_ECOLX

UniProt

P25239 - T257_ECOLX

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Protein
Type IIS restriction enzyme Eco57I
Gene
eco57IR
Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Recognizes the double-stranded sequences CTGAAG and CTTCAG and cleaves respectively 22 bases after C-1 and 14 bases before C'-1. Also acts as a methylase that causes specific methylation on A-5 on one strand, the other strand being methylated by the Eco57IB methylase.

Catalytic activityi

Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. Type II site-specific deoxyribonuclease activity Source: UniProtKB-EC
  3. site-specific DNA-methyltransferase (adenine-specific) activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Endonuclease, Hydrolase, Methyltransferase, Nuclease, Transferase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

S-adenosyl-L-methionine

Protein family/group databases

REBASEi941. Eco57I.

Names & Taxonomyi

Protein namesi
Recommended name:
Type IIS restriction enzyme Eco57I (EC:3.1.21.4)
Alternative name(s):
Endonuclease Eco57I
Including the following 1 domains:
Adenine-specific methyltransferase activity Eco57IA (EC:2.1.1.72)
Short name:
M.Eco57IA
Gene namesi
Name:eco57IR
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 998998Type IIS restriction enzyme Eco57I
PRO_0000077274Add
BLAST

Proteomic databases

PRIDEiP25239.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP25239.

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR011639. RM_methylase_Eco57I.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF07669. Eco57I. 1 hit.
[Graphical view]
PRINTSiPR00507. N12N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25239-1 [UniParc]FASTAAdd to Basket

« Hide

MNKKDQLQRL IDKYKSDIDY YRSARYNETQ LRTDFLDQLF LILGWDITNA    50
AGKPTNEREV LVEEGLKARA GENTKKPDYT FRLFSERKFF LEAKKPSVDI 100
STTIEPALQV RRYGFTAKLK ISVLSNFEYT AIYDCSNQVK ETDSVANSRI 150
KLYHFTELVD KFDEINNLIG RESVYTGHFD NEWSEIENKI LRFSVDDLFL 200
KQINDWRLLL ANEFLQIKNE LPEEKLNDLV QNYINSIVFL RVCEDRDLEE 250
YETLYHFAQD KDFQSLVKKL KSSDKKYNSG LFSLEYIDEL LSNANSCIWS 300
IIEQLYFPQS TYSFSVFSSD ILGNIYEIFL SEKVRIDELG NVKIQPKEEH 350
IDRDVVTTPT HIVKEIIRNT VVEYCKGKSD IEILNSKFAD IACGSGAFII 400
EAFQFIQDIL IDYYIQNDKS KLQQISEHTY KLKFEVKREI LCKCIYGIDK 450
DYNATKACTF GLLLKLLEGE TTETIGKDTP ILPALDTNIL FGNSLIDSGD 500
KVKQEDIFSI NPFDLTNYQF DVIVGNPPYM ATEHMNQLTP KELDIYKRKY 550
KSAYKQFDKY FLFIERSIQI LKEYGYLGYI LPSRFIKVDA GKKLRKFLSE 600
NKYLSKLISF GSHQVFKNKT TYTCLLFLNK ENHDNFSFYE VKDFKKWLTR 650
EDKYLLSSTY QTSSLDSDTW VLEKKINDIL KLMFSKSEQL GNIVGKSNVA 700
NGIQTSANKY YIHKEIKSEN GFIYFEYDGI EYHIEKELTR PYFETNRSGD 750
DSFYTYKDVE PNSFVVYPYK KVGERIQFIE YDELKRQYPK LFEFLQVVKV 800
HLNDKKRSIK PDPTGPNEWY RYGRSQALEN CDVDQKLIVG ILSNGYKYSI 850
DNHRTFVSSG GTAGYSIINI PNNVRYSIYY IQAILTSKYL EWFASIYGDI 900
FRGRFVARGT KVQTRMPIPT IDFDDPKQKE IHDTISSKQQ YLNKLYSQTQ 950
KSADRDKIIF ERQFEQEKIQ MDYLIKNLFD LGDLDSEIPT VEDLYKNL 998
Length:998
Mass (Da):117,087
Last modified:September 13, 2004 - v2
Checksum:iEDB090A7FBFFCC93
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421I → L in AAA23389. 1 Publication
Sequence conflicti207 – 2071R → G in AAA23389. 1 Publication
Sequence conflicti299 – 32123WSIIE…FSSDI → EHHRTIILPHKAHTLSLFSL LIF in AAA23389. 1 Publication
Add
BLAST
Sequence conflicti401 – 4011E → V in AAA23389. 1 Publication
Sequence conflicti644 – 6441F → N in AAA23389. 1 Publication
Sequence conflicti816 – 8238PNEWYRYG → LMMVQIR in AAA23389. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74821 Genomic DNA. Translation: AAA23389.1.
X61122 Genomic DNA. Translation: CAA43434.3.
PIRiS26426.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74821 Genomic DNA. Translation: AAA23389.1 .
X61122 Genomic DNA. Translation: CAA43434.3 .
PIRi S26426.

3D structure databases

ProteinModelPortali P25239.
ModBasei Search...

Protein family/group databases

REBASEi 941. Eco57I.

Proteomic databases

PRIDEi P25239.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.150. 2 hits.
InterProi IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR011639. RM_methylase_Eco57I.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF07669. Eco57I. 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. "Crystallization and preliminary crystallographic studies of a bifunctional restriction endonuclease Eco57I."
    Tamulaitiene G., Grazulis S., Janulaitis A., Janowski R., Bujacz G., Jaskolski M.
    Biochim. Biophys. Acta 1698:251-254(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS), SEQUENCE REVISION.
  3. "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 nameiT257_ECOLX
AccessioniPrimary (citable) accession number: P25239
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: September 13, 2004
Last modified: June 11, 2014
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Multifunctional enzyme

Documents

  1. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries

External Data

Dasty 3

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