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P25241

- T3RE_BACC1

UniProt

P25241 - T3RE_BACC1

Protein

Type III restriction-modification system Bce10987IP enzyme res

Gene

res

Organism
Bacillus cereus (strain ATCC 10987)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (24 May 2004)
      Previous versions | rss
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    Functioni

    This protein cuts the DNA outside of the recognition site. May also act as a helicase involved in unwinding DNA at the cleavage site. Protein only required for restriction but needs the presence of the modification enzyme By similarity.By similarity

    Catalytic activityi

    Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.

    Cofactori

    Magnesium.By similarity

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Endonuclease, Helicase, Hydrolase, Nuclease

    Keywords - Biological processi

    Restriction system

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.1.21.5. 648.

    Protein family/group databases

    REBASEi2841. BceSI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type III restriction-modification system Bce10987IP enzyme res (EC:3.1.21.5)
    Gene namesi
    Name:res
    Synonyms:t3res
    Ordered Locus Names:BCE_1019
    OrganismiBacillus cereus (strain ATCC 10987)
    Taxonomic identifieri222523 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000002527: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 987987Type III restriction-modification system Bce10987IP enzyme resPRO_0000077376Add
    BLAST

    Interactioni

    Subunit structurei

    Contains two different subunits: res and mod.

    Protein-protein interaction databases

    STRINGi222523.BCE_1019.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini886 – 97489VRR-NUCAdd
    BLAST

    Sequence similaritiesi

    Contains 1 VRR-NUC domain.Curated

    Phylogenomic databases

    eggNOGiCOG3587.
    HOGENOMiHOG000218980.
    KOiK01156.
    OMAiRANQREN.
    OrthoDBiEOG6MPWQ7.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR006935. Helicase/UvrB_dom.
    IPR027417. P-loop_NTPase.
    IPR014883. VRR_NUC.
    [Graphical view]
    PfamiPF04851. ResIII. 1 hit.
    PF08774. VRR_NUC. 1 hit.
    [Graphical view]
    SMARTiSM00990. VRR_NUC. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.

    Sequencei

    Sequence statusi: Complete.

    P25241-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKILLEELPH QEESLKAILE NFTGIDNAAN DSDVDYVYAN PLIRGRYNEI    50
    SNIDVKMETG TGKTYVYTRL MYEMHQQYGI FKFVIVVPSP AIKEGAKNFI 100
    QSDYAKQHFS QFYENVRIEL NVINAGDFKS KSGRRNFPAQ LLNFVEGSRQ 150
    NSNTIEVLLI NADMLRSKSM RNNDYDQTLI GGTTSPIEAI QDTRPVVIID 200
    EPHRFPRDKA NYQSIEAIKP QVIIRFGATF PEVTTGKGSN KITKKDYYRK 250
    KPQFDLNAIE SFNNGLVKGI DIYYPNLTEE QAKNRYVVDS VKAKELVLKQ 300
    NSKSWILHVG DNLAEVDSGF EGDIEYAGSK MLSNELELEK GMTLIPGTYR 350
    STYQELIIKD AIDKHFEIEQ ANFLRANQRE NNVPRIKTLS LFFIDSITSY 400
    RQDDGWLKAT FERLLKEKLS RLVAEYEFKR LPREKEYLEF LRATQSSLAS 450
    DNQNVHAGYF GEDRGSGDES IQAEVDDILK NKEKLLSFKD ENGNWQTRRF 500
    LFSKWTLREG WDNPNVFVIA KLRTSGSDNS KIQEVGRGLR LPVDETGHRI 550
    QQDEWPTRLA FLIGYDEKDF AQKLIGEINS DAKLQLNEEK LTEDMIQLIV 600
    TKRKKVNPEF TDERLLEHLD NLGIINRKNE FKESIDIGGV QKSGFEWLVE 650
    LYPELNTNRL REGKVIDTKK HSIKVRVKLR KENWEKVKEL WQQFSNRYML 700
    EFQRIPETIS FMAEQIVGNH SLYEREVPMQ MKESLHASDD NESVVLREQE 750
    NEYQRIYLPG MAYGKFVKRI NIATGIPIKE IHANLFKLMK SSLKGDARYL 800
    SELSLNNIIR EFKKRFDEIF AQAYEYKKLD FQARTAIYNP EMDSFVDDIN 850
    AEVIGVNIDE QAQEDNRYLY ELPPMRYDSV TPERDLLRHG YNDKVTVFGK 900
    LPRRAIQVPK YTGGSTTPDF IYMIEKDNDS SVYVLVETKA ENMRLEDQRI 950
    IDIQKKFFDT LKEHHIEFIE ATSAQQVYSI IRKLSEE 987
    Length:987
    Mass (Da):114,787
    Last modified:May 24, 2004 - v2
    Checksum:i1D0D6CF4112407FC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti410 – 46253TFERL…GYFGE → GDYQFIETKAPTGYDLNAKP IPFTITKGQAQVTSVTALNS LTTGSMELMKVDM in CAA43125. (PubMed:1587478)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007510 Genomic DNA. Translation: CAB40612.1.
    AE017194 Genomic DNA. Translation: AAS39950.1.
    X60713 Genomic DNA. Translation: CAA43125.1.
    PIRiS15518. JC1116.
    RefSeqiNP_977342.1. NC_003909.8.
    WP_000698184.1. NC_003909.8.

    Genome annotation databases

    EnsemblBacteriaiAAS39950; AAS39950; BCE_1019.
    GeneIDi2750767.
    KEGGibca:BCE_1019.
    PATRICi18850934. VBIBacCer118379_0972.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007510 Genomic DNA. Translation: CAB40612.1 .
    AE017194 Genomic DNA. Translation: AAS39950.1 .
    X60713 Genomic DNA. Translation: CAA43125.1 .
    PIRi S15518. JC1116.
    RefSeqi NP_977342.1. NC_003909.8.
    WP_000698184.1. NC_003909.8.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 222523.BCE_1019.

    Protein family/group databases

    REBASEi 2841. BceSI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS39950 ; AAS39950 ; BCE_1019 .
    GeneIDi 2750767.
    KEGGi bca:BCE_1019.
    PATRICi 18850934. VBIBacCer118379_0972.

    Phylogenomic databases

    eggNOGi COG3587.
    HOGENOMi HOG000218980.
    KOi K01156.
    OMAi RANQREN.
    OrthoDBi EOG6MPWQ7.

    Enzyme and pathway databases

    BRENDAi 3.1.21.5. 648.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR006935. Helicase/UvrB_dom.
    IPR027417. P-loop_NTPase.
    IPR014883. VRR_NUC.
    [Graphical view ]
    Pfami PF04851. ResIII. 1 hit.
    PF08774. VRR_NUC. 1 hit.
    [Graphical view ]
    SMARTi SM00990. VRR_NUC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 4 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Genome organization is not conserved between Bacillus cereus and Bacillus subtilis."
      Oekstad O.A., Hegna I.K., Lindbaeck T., Rishovd A.-L., Kolstoe A.-B.
      Microbiology 145:621-631(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
      Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
      Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10987.
    3. "A type-III DNA restriction and modification system in Bacillus cereus?"
      Hegna I.K., Karlstroem E.S., Lopez R., Kristensen T., Kolstoe A.-B.
      Gene 114:149-150(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 410-821.

    Entry informationi

    Entry nameiT3RE_BACC1
    AccessioniPrimary (citable) accession number: P25241
    Secondary accession number(s): Q9XBI5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 24, 2004
    Last modified: October 1, 2014
    This is version 99 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

    Complete proteome

    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