Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P25239

- T257_ECOLX

UniProt

P25239 - T257_ECOLX

Protein

Type IIS restriction enzyme Eco57I

Gene

eco57IR

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 2 (13 Sep 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    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