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P10486 (T1R1_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Type I restriction enzyme EcoR124II R protein

Short name=R.EcoR124II
EC=3.1.21.3
Gene names
Name:hsdR
Synonyms:hsr
Encoded onPlasmid IncFIV R124/3
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1033 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The EcoR124/3 I enzyme recognizes 5'-GAAN7RTCG-3'. Subunit R is required for both nuclease and ATPase activities, but not for modification.

Catalytic activity

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

Subunit structure

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

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.

Sequence similarities

Belongs to the HsdR family.

Contains 1 helicase ATP-binding domain.

Ontologies

Keywords
   Biological processRestriction system
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical term3D-structure
Plasmid
Gene Ontology (GO)
   Biological_processDNA restriction-modification system

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Type I site-specific deoxyribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10331033Type I restriction enzyme EcoR124II R protein
PRO_0000077260

Regions

Domain294 – 456163Helicase ATP-binding
Nucleotide binding308 – 3147ATP By similarity

Secondary structure

.................................................................................................................................................. 1033
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10486 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: B55F3991356C1506

FASTA1,033119,657
        10         20         30         40         50         60 
MTHQTHTIAE SNNFIVLDKY IKAEPTGDSY QSESDLEREL IQDLRNQGYE FISVKSQSAM 

        70         80         90        100        110        120 
LANVREQLQN LNGVVFNDSE WRRFTEQYLD NPSDGILDKT RKIHIDYICD FIFDDERLEN 

       130        140        150        160        170        180 
IYLIDKKNLM RNKVQIIQQF EQAGSHANRY DVTILVNGLP LVQIELKKRG VAIREAFNQI 

       190        200        210        220        230        240 
HRYSKESFNS ENSLFKYLQL FVISNGTDTR YFANTTKRDK NSFDFTMNWA KSDNTLIKDL 

       250        260        270        280        290        300 
KDFTATCFQK HTLLNVLVNY SVFDSSQTLL VMRPYQIAAT ERILWKIKSS FTAKNWSKPE 

       310        320        330        340        350        360 
SGGYIWHTTG SGKTLTSFKA ARLATELDFI DKVFFVVDRK DLDYQTMKEY QRFSPDSVNG 

       370        380        390        400        410        420 
SENTAGLKRN LDKDDNKIIV TTIQKLNNLM KAESDLPVYN QQVVFIFDEC HRSQFGEAQK 

       430        440        450        460        470        480 
NLKKKFKRYY QFGFTGTPIF PENALGSETT ASVFGRELHS YVITDAIRDE KVLKFKVDYN 

       490        500        510        520        530        540 
DVRPQFKSLE TETDEKKLSA AENQQAFLHP MRIQEITQYI LNNFRQKTHR TFPGSKGFNA 

       550        560        570        580        590        600 
MLAVSSVDAA KAYYATFKRL QEEAANKSAT YKPLRIATIF SFAANEEQNA IGEISDETFD 

       610        620        630        640        650        660 
TSAMDSSAKE FLDAAIREYN SHFKTNFSTD SNGFQNYYRD LAQRVKNQDI DLLIVVGMFL 

       670        680        690        700        710        720 
TGFDAPTLNT LFVDKNLRYH GLMQAFSRTN RIYDATKTFG NIVTFRDLER STIDAITLFG 

       730        740        750        760        770        780 
DKNTKNVVLE KSYTEYMEGF TDAATGEAKR GFMTVVSELE QRFPDPTSIE SEKEKKDFVK 

       790        800        810        820        830        840 
LFGEYLRAEN ILQNYDEFAT LKALQQIDLS DPVAVEKFKA EHYVDDEKFA ELQTIRLPAD 

       850        860        870        880        890        900 
RKIQDYRSAY NDIRDWQRRE KEAEKKEKST TDWDDVVFEV DLLKSQEINL DYILGLIFEH 

       910        920        930        940        950        960 
NRQNKGKGEM IEEVKRLIRS SLGNRAKEGL VVDFIQQTNL DDLPDKASII DAFFTFAQRE 

       970        980        990       1000       1010       1020 
QQREAEALIK EENLNEDAAK RYIRTSLKRE YATENGTELN ETLPKLSPLN PQYKTKKQAV 

      1030 
FRKSSRLLRS LKA 

« Hide

References

[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13145 Genomic DNA. Translation: CAA31543.1.
PIRS02168.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP10486.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-17005N.

Protein family/group databases

REBASE990. EcoR124I.

Proteomic databases

PRIDEP10486.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR006935. 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]
PfamPF12008. EcoR124_C. 1 hit.
PF04313. HSDR_N. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00348. hsdR. 1 hit.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10486.

Entry information

Entry nameT1R1_ECOLX
AccessionPrimary (citable) accession number: P10486
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references