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Q47281 (T1RE_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 EcoEI R protein

Short name=R.EcoEI
EC=3.1.21.3
Gene names
Name:hsdR
Synonyms:hsr
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length813 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The EcoEI enzyme recognizes 5'-GAGN7ATGC-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.

Contains 1 helicase C-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 813813Type I restriction enzyme EcoEI R protein
PRO_0000077258

Regions

Domain181 – 341161Helicase ATP-binding
Domain410 – 561152Helicase C-terminal
Nucleotide binding195 – 2017ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47281 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A1EB1794123F0ADD

FASTA81392,627
        10         20         30         40         50         60 
MAGVNKTHLT ETDIITKFIL PAVKDAGWDV MSQIRQEVKL RDGKIVVRGK LASRIKVKSA 

        70         80         90        100        110        120 
DIVLYHKPNL PLAVIEAKAN KHAISKGMQQ GLDYASLLDV PFVFASNGDG FIFHDKTNPQ 

       130        140        150        160        170        180 
QLESEIALSD FPTPEQLWQK YCAWKGFTQE QLPVISQDYF DDGSGKAPRY YQMQAINRTV 

       190        200        210        220        230        240 
DAVSAGKNRI LLVMATGTGK TYTAFQIIWR LWKAKNKKRI LFLADRNILV DQTKRNDFQP 

       250        260        270        280        290        300 
FGNAMTKVTG RTIDPAYEVH LALYQAITGP EEHQKAYKQV APDFFDLIVI DECHRGSASE 

       310        320        330        340        350        360 
DSAWREILEY FGSATQVGLT ATPKETEDVS NIDYFGEPVY TYSLKEGIED GFLAPYKVVR 

       370        380        390        400        410        420 
VDIDVDVQGW RPVKGQLDKY GEEIEDRIYN LKDFDRTLVI DERTMLVAQT ITDYLKRTNP 

       430        440        450        460        470        480 
MDKTIVFCND IDHADRMRHA LVVLNPEQVL KNEKYVMKIT GDDDIGKAQL DNFINPKKAY 

       490        500        510        520        530        540 
PVIATTSELM TTGVDAQTCK LVVLDQNIQS MTKFKQIIGR GTRINEKHGK LWFTILDFKK 

       550        560        570        580        590        600 
ATELFADPRF DGLPEKVLVV KPGDISDKDS DFNEQLDAEN NADGGDNDAS EAREDVADYQ 

       610        620        630        640        650        660 
VNRDKQAGNG EFHDDDENKV RKFYVNGVDV KVLAKRVQYY DSDGKLVTES FQDYTRKTML 

       670        680        690        700        710        720 
KDSEYASLDS FVRKWQDAPR KQVIIEELEQ LGILWDVLAE EVGKDLDPFD LLCHVVYGQP 

       730        740        750        760        770        780 
PLTRQERVAN VRKRNYFTKY AEPAQQVLNT LLDKYADEGV QEIEDVQVLK LKPFDTLGRP 

       790        800        810 
IEIIKTRFGD KKAYEQAVNE LENEIYQLPP RSA 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L18759 Genomic DNA. Translation: AAD15048.1.
PIRI41292.

3D structure databases

ProteinModelPortalQ47281.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ47281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR013670. 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]
PfamPF08463. EcoEI_R_C. 1 hit.
PF04313. HSDR_N. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameT1RE_ECOLX
AccessionPrimary (citable) accession number: Q47281
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 74 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