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P10486

- T1R1_ECOLX

UniProt

P10486 - T1R1_ECOLX

Protein

Type I restriction enzyme EcoR124II R protein

Gene

hsdR

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    The EcoR124/3 I enzyme recognizes 5'-GAAN7RTCG-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 bindingi308 – 3147ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. 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

    REBASEi990. EcoR124I.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type I restriction enzyme EcoR124II R protein (EC:3.1.21.3)
    Short name:
    R.EcoR124II
    Gene namesi
    Name:hsdR
    Synonyms:hsr
    Encoded oniPlasmid IncFIV R124/30 Publication
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10331033Type I restriction enzyme EcoR124II R proteinPRO_0000077260Add
    BLAST

    Proteomic databases

    PRIDEiP10486.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    DIPiDIP-17005N.

    Structurei

    Secondary structure

    1
    1033
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 4614
    Helixi57 – 7216
    Helixi78 – 8710
    Helixi96 – 1049
    Beta strandi108 – 1125
    Beta strandi118 – 1247
    Beta strandi126 – 1283
    Helixi129 – 1313
    Beta strandi134 – 1385
    Beta strandi143 – 1453
    Beta strandi151 – 1566
    Beta strandi159 – 1668
    Helixi173 – 1808
    Beta strandi190 – 1923
    Helixi193 – 1975
    Beta strandi200 – 2045
    Beta strandi209 – 2135
    Helixi218 – 2203
    Helixi223 – 2253
    Beta strandi227 – 2304
    Helixi240 – 2445
    Turni245 – 2484
    Helixi250 – 25910
    Beta strandi260 – 2634
    Beta strandi269 – 2713
    Helixi274 – 29320
    Helixi299 – 3013
    Beta strandi302 – 3076
    Helixi313 – 32412
    Beta strandi332 – 3376
    Helixi339 – 3413
    Helixi344 – 3518
    Beta strandi358 – 3614
    Helixi365 – 3728
    Beta strandi378 – 3825
    Helixi383 – 39210
    Helixi397 – 4004
    Beta strandi403 – 4097
    Helixi414 – 42512
    Beta strandi427 – 43711
    Helixi441 – 4433
    Helixi450 – 4545
    Beta strandi456 – 4616
    Helixi463 – 4686
    Beta strandi475 – 4795
    Helixi484 – 4863
    Helixi487 – 4904
    Helixi495 – 5006
    Turni504 – 5085
    Helixi510 – 52718
    Beta strandi531 – 5344
    Beta strandi539 – 5468
    Helixi547 – 56418
    Turni565 – 5673
    Beta strandi568 – 5703
    Beta strandi576 – 5794
    Helixi601 – 6033
    Helixi606 – 62318
    Helixi631 – 64616
    Beta strandi649 – 6579
    Beta strandi660 – 6623
    Beta strandi668 – 6758
    Helixi679 – 6879
    Beta strandi699 – 7068
    Helixi709 – 71810
    Helixi724 – 7285
    Helixi733 – 7386
    Beta strandi739 – 7413
    Turni743 – 7453
    Beta strandi748 – 7503
    Helixi752 – 76211
    Beta strandi766 – 7694
    Helixi772 – 79221
    Helixi796 – 8049
    Helixi813 – 8219
    Helixi826 – 8316
    Helixi832 – 8343
    Helixi840 – 85516
    Helixi880 – 8845

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2W00X-ray2.60A/B1-1032[»]
    4BE7X-ray2.74B/D1-1032[»]
    4BEBX-ray2.99A/B/C/D1-1032[»]
    4BECX-ray2.84A/B1-1032[»]
    ProteinModelPortaliP10486.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10486.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini294 – 456163Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR006935. Helicase/UvrB_dom.
    IPR014001. Helicase_ATP-bd.
    IPR027417. P-loop_NTPase.
    IPR007409. Restrct_endonuc_type1_HsdR_N.
    IPR004473. Restrct_endonuc_typeI_HsdR.
    IPR022625. TypeI_RM_Rsu_C.
    [Graphical view]
    PfamiPF12008. EcoR124_C. 1 hit.
    PF04313. HSDR_N. 1 hit.
    PF04851. ResIII. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00348. hsdR. 1 hit.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10486-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTHQTHTIAE SNNFIVLDKY IKAEPTGDSY QSESDLEREL IQDLRNQGYE     50
    FISVKSQSAM LANVREQLQN LNGVVFNDSE WRRFTEQYLD NPSDGILDKT 100
    RKIHIDYICD FIFDDERLEN IYLIDKKNLM RNKVQIIQQF EQAGSHANRY 150
    DVTILVNGLP LVQIELKKRG VAIREAFNQI HRYSKESFNS ENSLFKYLQL 200
    FVISNGTDTR YFANTTKRDK NSFDFTMNWA KSDNTLIKDL KDFTATCFQK 250
    HTLLNVLVNY SVFDSSQTLL VMRPYQIAAT ERILWKIKSS FTAKNWSKPE 300
    SGGYIWHTTG SGKTLTSFKA ARLATELDFI DKVFFVVDRK DLDYQTMKEY 350
    QRFSPDSVNG SENTAGLKRN LDKDDNKIIV TTIQKLNNLM KAESDLPVYN 400
    QQVVFIFDEC HRSQFGEAQK NLKKKFKRYY QFGFTGTPIF PENALGSETT 450
    ASVFGRELHS YVITDAIRDE KVLKFKVDYN DVRPQFKSLE TETDEKKLSA 500
    AENQQAFLHP MRIQEITQYI LNNFRQKTHR TFPGSKGFNA MLAVSSVDAA 550
    KAYYATFKRL QEEAANKSAT YKPLRIATIF SFAANEEQNA IGEISDETFD 600
    TSAMDSSAKE FLDAAIREYN SHFKTNFSTD SNGFQNYYRD LAQRVKNQDI 650
    DLLIVVGMFL TGFDAPTLNT LFVDKNLRYH GLMQAFSRTN RIYDATKTFG 700
    NIVTFRDLER STIDAITLFG DKNTKNVVLE KSYTEYMEGF TDAATGEAKR 750
    GFMTVVSELE QRFPDPTSIE SEKEKKDFVK LFGEYLRAEN ILQNYDEFAT 800
    LKALQQIDLS DPVAVEKFKA EHYVDDEKFA ELQTIRLPAD RKIQDYRSAY 850
    NDIRDWQRRE KEAEKKEKST TDWDDVVFEV DLLKSQEINL DYILGLIFEH 900
    NRQNKGKGEM IEEVKRLIRS SLGNRAKEGL VVDFIQQTNL DDLPDKASII 950
    DAFFTFAQRE QQREAEALIK EENLNEDAAK RYIRTSLKRE YATENGTELN 1000
    ETLPKLSPLN PQYKTKKQAV FRKSSRLLRS LKA 1033
    Length:1,033
    Mass (Da):119,657
    Last modified:July 1, 1989 - v1
    Checksum:iB55F3991356C1506
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13145 Genomic DNA. Translation: CAA31543.1.
    PIRiS02168.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13145 Genomic DNA. Translation: CAA31543.1 .
    PIRi S02168.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2W00 X-ray 2.60 A/B 1-1032 [» ]
    4BE7 X-ray 2.74 B/D 1-1032 [» ]
    4BEB X-ray 2.99 A/B/C/D 1-1032 [» ]
    4BEC X-ray 2.84 A/B 1-1032 [» ]
    ProteinModelPortali P10486.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-17005N.

    Protein family/group databases

    REBASEi 990. EcoR124I.

    Proteomic databases

    PRIDEi P10486.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P10486.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR006935. Helicase/UvrB_dom.
    IPR014001. Helicase_ATP-bd.
    IPR027417. P-loop_NTPase.
    IPR007409. Restrct_endonuc_type1_HsdR_N.
    IPR004473. Restrct_endonuc_typeI_HsdR.
    IPR022625. TypeI_RM_Rsu_C.
    [Graphical view ]
    Pfami PF12008. EcoR124_C. 1 hit.
    PF04313. HSDR_N. 1 hit.
    PF04851. ResIII. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00348. hsdR. 1 hit.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Basis for changes in DNA recognition by the EcoR124 and EcoR124/3 type I DNA restriction and modification enzymes."
      Price C., Lingner J., Bickle J., Firman T.A., Glover S.W.
      J. Mol. Biol. 205:115-125(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiT1R1_ECOLX
    AccessioniPrimary (citable) accession number: P10486
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 108 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.

    Keywords - Technical termi

    3D-structure, Plasmid

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Restriction enzymes and methylases
      Classification of restriction enzymes and methylases and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3