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Q07736

- T1RA_ECOLX

UniProt

Q07736 - T1RA_ECOLX

Protein

Type I restriction enzyme EcoAI 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 85 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    The EcoAI enzyme recognizes 5'-GAGN7GTCA-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 bindingi197 – 2037ATPPROSITE-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

    Protein family/group databases

    REBASEi969. EcoAI.

    Names & Taxonomyi

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 810810Type I restriction enzyme EcoAI R proteinPRO_0000077257Add
    BLAST

    Proteomic databases

    PRIDEiQ07736.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ07736.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini183 – 343161Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini412 – 575164Helicase 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

    Phylogenomic databases

    eggNOGiCOG4096.
    OMAiKNNDFKP.

    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. 4 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q07736-1 [UniParc]FASTAAdd to Basket

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    MAELNLSNLT EADIITKCVM PAILNAGWDN TTQIRQEVKL RDGKVIVRGK    50
    VAARRTVKSA DIVLYHKPGI PLAVIEAKAN KHEIGKGMQQ GIEYARLLDV 100
    PFVFATNGDG FIFRDATAAE GECLEKQITL DDFPSPAELW QKFCLWKGYT 150
    QAQLPVITQD YYDDGSGKSP RYYQLQAINK TIEAVSNGQN RVLLVMATGT 200
    GKTYTAFQII WRLWKSKNKK RILFLADRNI LVDQTKNNDF QPFGTAMTKV 250
    SGRTIDPAYE IHLALYQAIT GPEEDQKAFK QVAPDFFDLI VIDECHRGSA 300
    SEDSAWREIL DYFSSATQIG LTATPKETHE VSSTDYFGDP VYVYSLKEGI 350
    EDGFLAPYKV VRVDIDVDLQ GWRPTKGQTD LNGEVIDDRI YNQKDFDRTM 400
    VIDERTELVA RTITDYLKRT NPMDKTIVFC NDIDHAERMR RALVNLNPEQ 450
    VKKNDKYVMK ITGDDEIGKA QLDNFINPKK PYPVIATTSE LMTTGVDAKT 500
    CKLVVLDQNI QSMTKFKQII GRGTRIDERY GKLWFTILDF KKATELFADE 550
    RFDGIPEKVM DTTPEDIADP ESDFEEKLEE ISEHDEEQVT GVDEPPAPPY 600
    QVTDTDDVGP LPEEDEKKIR KFHVNGVAVG VIAQRVQYYD ADGKLVTESF 650
    KDYTRKTLLK EYASLDDFTR KWQDADRKEA IIHELEQQGI IWEVLAEEVG 700
    KDLDPFDMLC HVVYGQPPLT RKERAENVRK RNYFTKYSEA AQAVLDNLLD 750
    KYADAGVQEI ESIQVLKLKP FDSMGTLPEI IKTGFGDRNG YNQALSELEN 800
    EIYQLPPRSA 810
    Length:810
    Mass (Da):92,071
    Last modified:November 1, 1996 - v1
    Checksum:iC04E673C8C1DEA51
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18758 Genomic DNA. Translation: AAA23983.1.
    PIRiI41291.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18758 Genomic DNA. Translation: AAA23983.1 .
    PIRi I41291.

    3D structure databases

    ProteinModelPortali Q07736.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 969. EcoAI.

    Proteomic databases

    PRIDEi Q07736.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG4096.
    OMAi KNNDFKP.

    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. 4 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: 15T.

    Entry informationi

    Entry nameiT1RA_ECOLX
    AccessioniPrimary (citable) accession number: Q07736
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 85 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