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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. site-specific DNA-methyltransferase (adenine-specific) activity Source: UniProtKB-EC
  3. Type II site-specific deoxyribonuclease activity Source: UniProtKB-EC

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 Eco57IPRO_0000077274Add
BLAST

Proteomic databases

PRIDEiP25239.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP25239.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MNKKDQLQRL IDKYKSDIDY YRSARYNETQ LRTDFLDQLF LILGWDITNA
60 70 80 90 100
AGKPTNEREV LVEEGLKARA GENTKKPDYT FRLFSERKFF LEAKKPSVDI
110 120 130 140 150
STTIEPALQV RRYGFTAKLK ISVLSNFEYT AIYDCSNQVK ETDSVANSRI
160 170 180 190 200
KLYHFTELVD KFDEINNLIG RESVYTGHFD NEWSEIENKI LRFSVDDLFL
210 220 230 240 250
KQINDWRLLL ANEFLQIKNE LPEEKLNDLV QNYINSIVFL RVCEDRDLEE
260 270 280 290 300
YETLYHFAQD KDFQSLVKKL KSSDKKYNSG LFSLEYIDEL LSNANSCIWS
310 320 330 340 350
IIEQLYFPQS TYSFSVFSSD ILGNIYEIFL SEKVRIDELG NVKIQPKEEH
360 370 380 390 400
IDRDVVTTPT HIVKEIIRNT VVEYCKGKSD IEILNSKFAD IACGSGAFII
410 420 430 440 450
EAFQFIQDIL IDYYIQNDKS KLQQISEHTY KLKFEVKREI LCKCIYGIDK
460 470 480 490 500
DYNATKACTF GLLLKLLEGE TTETIGKDTP ILPALDTNIL FGNSLIDSGD
510 520 530 540 550
KVKQEDIFSI NPFDLTNYQF DVIVGNPPYM ATEHMNQLTP KELDIYKRKY
560 570 580 590 600
KSAYKQFDKY FLFIERSIQI LKEYGYLGYI LPSRFIKVDA GKKLRKFLSE
610 620 630 640 650
NKYLSKLISF GSHQVFKNKT TYTCLLFLNK ENHDNFSFYE VKDFKKWLTR
660 670 680 690 700
EDKYLLSSTY QTSSLDSDTW VLEKKINDIL KLMFSKSEQL GNIVGKSNVA
710 720 730 740 750
NGIQTSANKY YIHKEIKSEN GFIYFEYDGI EYHIEKELTR PYFETNRSGD
760 770 780 790 800
DSFYTYKDVE PNSFVVYPYK KVGERIQFIE YDELKRQYPK LFEFLQVVKV
810 820 830 840 850
HLNDKKRSIK PDPTGPNEWY RYGRSQALEN CDVDQKLIVG ILSNGYKYSI
860 870 880 890 900
DNHRTFVSSG GTAGYSIINI PNNVRYSIYY IQAILTSKYL EWFASIYGDI
910 920 930 940 950
FRGRFVARGT KVQTRMPIPT IDFDDPKQKE IHDTISSKQQ YLNKLYSQTQ
960 970 980 990
KSADRDKIIF ERQFEQEKIQ MDYLIKNLFD LGDLDSEIPT VEDLYKNL
Length:998
Mass (Da):117,087
Last modified:September 13, 2004 - v2
Checksum:iEDB090A7FBFFCC93
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421I → L in AAA23389. (PubMed:1334261)Curated
Sequence conflicti207 – 2071R → G in AAA23389. (PubMed:1334261)Curated
Sequence conflicti299 – 32123WSIIE…FSSDI → EHHRTIILPHKAHTLSLFSL LIF in AAA23389. (PubMed:1334261)CuratedAdd
BLAST
Sequence conflicti401 – 4011E → V in AAA23389. (PubMed:1334261)Curated
Sequence conflicti644 – 6441F → N in AAA23389. (PubMed:1334261)Curated
Sequence conflicti816 – 8238PNEWYRYG → LMMVQIR in AAA23389. (PubMed:1334261)Curated

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...
MobiDBi 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: October 1, 2014
This is version 78 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