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Q07736 (T1RA_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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 EcoAI R protein

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

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The EcoAI enzyme recognizes 5'-GAGN7GTCA-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 – 810810Type I restriction enzyme EcoAI R protein
PRO_0000077257

Regions

Domain183 – 343161Helicase ATP-binding
Domain412 – 575164Helicase C-terminal
Nucleotide binding197 – 2037ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q07736 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C04E673C8C1DEA51

FASTA81092,071
        10         20         30         40         50         60 
MAELNLSNLT EADIITKCVM PAILNAGWDN TTQIRQEVKL RDGKVIVRGK VAARRTVKSA 

        70         80         90        100        110        120 
DIVLYHKPGI PLAVIEAKAN KHEIGKGMQQ GIEYARLLDV PFVFATNGDG FIFRDATAAE 

       130        140        150        160        170        180 
GECLEKQITL DDFPSPAELW QKFCLWKGYT QAQLPVITQD YYDDGSGKSP RYYQLQAINK 

       190        200        210        220        230        240 
TIEAVSNGQN RVLLVMATGT GKTYTAFQII WRLWKSKNKK RILFLADRNI LVDQTKNNDF 

       250        260        270        280        290        300 
QPFGTAMTKV SGRTIDPAYE IHLALYQAIT GPEEDQKAFK QVAPDFFDLI VIDECHRGSA 

       310        320        330        340        350        360 
SEDSAWREIL DYFSSATQIG LTATPKETHE VSSTDYFGDP VYVYSLKEGI EDGFLAPYKV 

       370        380        390        400        410        420 
VRVDIDVDLQ GWRPTKGQTD LNGEVIDDRI YNQKDFDRTM VIDERTELVA RTITDYLKRT 

       430        440        450        460        470        480 
NPMDKTIVFC NDIDHAERMR RALVNLNPEQ VKKNDKYVMK ITGDDEIGKA QLDNFINPKK 

       490        500        510        520        530        540 
PYPVIATTSE LMTTGVDAKT CKLVVLDQNI QSMTKFKQII GRGTRIDERY GKLWFTILDF 

       550        560        570        580        590        600 
KKATELFADE RFDGIPEKVM DTTPEDIADP ESDFEEKLEE ISEHDEEQVT GVDEPPAPPY 

       610        620        630        640        650        660 
QVTDTDDVGP LPEEDEKKIR KFHVNGVAVG VIAQRVQYYD ADGKLVTESF KDYTRKTLLK 

       670        680        690        700        710        720 
EYASLDDFTR KWQDADRKEA IIHELEQQGI IWEVLAEEVG KDLDPFDMLC HVVYGQPPLT 

       730        740        750        760        770        780 
RKERAENVRK RNYFTKYSEA AQAVLDNLLD KYADAGVQEI ESIQVLKLKP FDSMGTLPEI 

       790        800        810 
IKTGFGDRNG YNQALSELEN EIYQLPPRSA 

« 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: 15T.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L18758 Genomic DNA. Translation: AAA23983.1.
PIRI41291.

3D structure databases

ProteinModelPortalQ07736.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE969. EcoAI.

Proteomic databases

PRIDEQ07736.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG4096.
OMAKNNDFKP.

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. 4 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameT1RA_ECOLX
AccessionPrimary (citable) accession number: Q07736
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 84 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