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Protein

Type I restriction enzyme EcoAI R protein

Gene

hsdR

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

The EcoAI enzyme recognizes 5'-GAGN7GTCA-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 bindingi197 – 2037ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.1.21.3. 2026.

Protein family/group databases

REBASEi969. EcoAI.

Names & Taxonomyi

Protein namesi
Recommended name:
Type I restriction enzyme EcoAI R protein (EC:3.1.21.3)
Short name:
R.EcoAI
Gene namesi
Name:hsdR
Synonyms:hsr
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 810810Type I restriction enzyme EcoAI R proteinPRO_0000077257Add
BLAST

Proteomic databases

PRIDEiQ07736.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi199310.c5425.

Structurei

3D structure databases

ProteinModelPortaliQ07736.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini183 – 343161Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini412 – 575164Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG4096.
OMAiDGFIFHD.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR013670. 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]
PfamiPF08463. EcoEI_R_C. 1 hit.
PF04313. HSDR_N. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07736-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELNLSNLT EADIITKCVM PAILNAGWDN TTQIRQEVKL RDGKVIVRGK
60 70 80 90 100
VAARRTVKSA DIVLYHKPGI PLAVIEAKAN KHEIGKGMQQ GIEYARLLDV
110 120 130 140 150
PFVFATNGDG FIFRDATAAE GECLEKQITL DDFPSPAELW QKFCLWKGYT
160 170 180 190 200
QAQLPVITQD YYDDGSGKSP RYYQLQAINK TIEAVSNGQN RVLLVMATGT
210 220 230 240 250
GKTYTAFQII WRLWKSKNKK RILFLADRNI LVDQTKNNDF QPFGTAMTKV
260 270 280 290 300
SGRTIDPAYE IHLALYQAIT GPEEDQKAFK QVAPDFFDLI VIDECHRGSA
310 320 330 340 350
SEDSAWREIL DYFSSATQIG LTATPKETHE VSSTDYFGDP VYVYSLKEGI
360 370 380 390 400
EDGFLAPYKV VRVDIDVDLQ GWRPTKGQTD LNGEVIDDRI YNQKDFDRTM
410 420 430 440 450
VIDERTELVA RTITDYLKRT NPMDKTIVFC NDIDHAERMR RALVNLNPEQ
460 470 480 490 500
VKKNDKYVMK ITGDDEIGKA QLDNFINPKK PYPVIATTSE LMTTGVDAKT
510 520 530 540 550
CKLVVLDQNI QSMTKFKQII GRGTRIDERY GKLWFTILDF KKATELFADE
560 570 580 590 600
RFDGIPEKVM DTTPEDIADP ESDFEEKLEE ISEHDEEQVT GVDEPPAPPY
610 620 630 640 650
QVTDTDDVGP LPEEDEKKIR KFHVNGVAVG VIAQRVQYYD ADGKLVTESF
660 670 680 690 700
KDYTRKTLLK EYASLDDFTR KWQDADRKEA IIHELEQQGI IWEVLAEEVG
710 720 730 740 750
KDLDPFDMLC HVVYGQPPLT RKERAENVRK RNYFTKYSEA AQAVLDNLLD
760 770 780 790 800
KYADAGVQEI ESIQVLKLKP FDSMGTLPEI IKTGFGDRNG YNQALSELEN
810
EIYQLPPRSA
Length:810
Mass (Da):92,071
Last modified:November 1, 1996 - v1
Checksum:iC04E673C8C1DEA51
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18758 Genomic DNA. Translation: AAA23983.1.
PIRiI41291.
RefSeqiWP_000819019.1. NZ_LM997219.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18758 Genomic DNA. Translation: AAA23983.1.
PIRiI41291.
RefSeqiWP_000819019.1. NZ_LM997219.1.

3D structure databases

ProteinModelPortaliQ07736.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi199310.c5425.

Protein family/group databases

REBASEi969. EcoAI.

Proteomic databases

PRIDEiQ07736.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG4096.
OMAiDGFIFHD.

Enzyme and pathway databases

BRENDAi3.1.21.3. 2026.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR013670. 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]
PfamiPF08463. EcoEI_R_C. 1 hit.
PF04313. HSDR_N. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiT1RA_ECOLX
AccessioniPrimary (citable) accession number: Q07736
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 91 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.

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.