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Q47281

- T1RE_ECOLX

UniProt

Q47281 - T1RE_ECOLX

Protein

Type I restriction enzyme EcoEI R protein

Gene

hsdR

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    • Comment

    Functioni

    The EcoEI enzyme recognizes 5'-GAGN7ATGC-3'. Subunit R is required for both nuclease and ATPase activities, but not for modification.

    Catalytic activityi

    Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates; ATP is simultaneously hydrolyzed.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi195 – 2017ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. helicase activity Source: InterPro
    4. Type I site-specific deoxyribonuclease activity Source: UniProtKB-EC

    GO - Biological processi

    1. DNA restriction-modification system Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Restriction system

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type I restriction enzyme EcoEI R protein (EC:3.1.21.3)
    Short name:
    R.EcoEI
    Gene namesi
    Name:hsdR
    Synonyms:hsr
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 813813Type I restriction enzyme EcoEI R proteinPRO_0000077258Add
    BLAST

    Proteomic databases

    PRIDEiQ47281.

    Interactioni

    Subunit structurei

    The type I restriction/modification system is composed of three polypeptides R, M and S.

    Structurei

    3D structure databases

    ProteinModelPortaliQ47281.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini181 – 341161Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini410 – 561152Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the HsdR family.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR013670. EcoEI_R_C_dom.
    IPR006935. Helicase/UvrB_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR007409. Restrct_endonuc_type1_HsdR_N.
    [Graphical view]
    PfamiPF08463. EcoEI_R_C. 1 hit.
    PF04313. HSDR_N. 1 hit.
    PF04851. ResIII. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q47281-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGVNKTHLT ETDIITKFIL PAVKDAGWDV MSQIRQEVKL RDGKIVVRGK    50
    LASRIKVKSA DIVLYHKPNL PLAVIEAKAN KHAISKGMQQ GLDYASLLDV 100
    PFVFASNGDG FIFHDKTNPQ QLESEIALSD FPTPEQLWQK YCAWKGFTQE 150
    QLPVISQDYF DDGSGKAPRY YQMQAINRTV DAVSAGKNRI LLVMATGTGK 200
    TYTAFQIIWR LWKAKNKKRI LFLADRNILV DQTKRNDFQP FGNAMTKVTG 250
    RTIDPAYEVH LALYQAITGP EEHQKAYKQV APDFFDLIVI DECHRGSASE 300
    DSAWREILEY FGSATQVGLT ATPKETEDVS NIDYFGEPVY TYSLKEGIED 350
    GFLAPYKVVR VDIDVDVQGW RPVKGQLDKY GEEIEDRIYN LKDFDRTLVI 400
    DERTMLVAQT ITDYLKRTNP MDKTIVFCND IDHADRMRHA LVVLNPEQVL 450
    KNEKYVMKIT GDDDIGKAQL DNFINPKKAY PVIATTSELM TTGVDAQTCK 500
    LVVLDQNIQS MTKFKQIIGR GTRINEKHGK LWFTILDFKK ATELFADPRF 550
    DGLPEKVLVV KPGDISDKDS DFNEQLDAEN NADGGDNDAS EAREDVADYQ 600
    VNRDKQAGNG EFHDDDENKV RKFYVNGVDV KVLAKRVQYY DSDGKLVTES 650
    FQDYTRKTML KDSEYASLDS FVRKWQDAPR KQVIIEELEQ LGILWDVLAE 700
    EVGKDLDPFD LLCHVVYGQP PLTRQERVAN VRKRNYFTKY AEPAQQVLNT 750
    LLDKYADEGV QEIEDVQVLK LKPFDTLGRP IEIIKTRFGD KKAYEQAVNE 800
    LENEIYQLPP RSA 813
    Length:813
    Mass (Da):92,627
    Last modified:November 1, 1996 - v1
    Checksum:iA1EB1794123F0ADD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18759 Genomic DNA. Translation: AAD15048.1.
    PIRiI41292.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18759 Genomic DNA. Translation: AAD15048.1 .
    PIRi I41292.

    3D structure databases

    ProteinModelPortali Q47281.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q47281.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR013670. EcoEI_R_C_dom.
    IPR006935. Helicase/UvrB_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR007409. Restrct_endonuc_type1_HsdR_N.
    [Graphical view ]
    Pfami PF08463. EcoEI_R_C. 1 hit.
    PF04313. HSDR_N. 1 hit.
    PF04851. ResIII. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conservation of motifs within the unusually variable polypeptide sequences of type I restriction and modification enzymes."
      Murray N.E., Daniel A.S., Cowan G.M., Sharp P.M.
      Mol. Microbiol. 9:133-143(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: A58.

    Entry informationi

    Entry nameiT1RE_ECOLX
    AccessioniPrimary (citable) accession number: Q47281
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and magnesium as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.

    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