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Protein

Type I restriction enzyme EcoEI R protein

Gene

hsdR

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

Functioni

The EcoEI enzyme recognizes 5'-GAGN7ATGC-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 bindingi195 – 2017ATPPROSITE-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.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 813813Type I restriction enzyme EcoEI R proteinPRO_0000077258Add
BLAST

Proteomic databases

PRIDEiQ47281.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ47281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini181 – 341161Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini410 – 561152Helicase 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

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. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q47281-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVNKTHLT ETDIITKFIL PAVKDAGWDV MSQIRQEVKL RDGKIVVRGK
60 70 80 90 100
LASRIKVKSA DIVLYHKPNL PLAVIEAKAN KHAISKGMQQ GLDYASLLDV
110 120 130 140 150
PFVFASNGDG FIFHDKTNPQ QLESEIALSD FPTPEQLWQK YCAWKGFTQE
160 170 180 190 200
QLPVISQDYF DDGSGKAPRY YQMQAINRTV DAVSAGKNRI LLVMATGTGK
210 220 230 240 250
TYTAFQIIWR LWKAKNKKRI LFLADRNILV DQTKRNDFQP FGNAMTKVTG
260 270 280 290 300
RTIDPAYEVH LALYQAITGP EEHQKAYKQV APDFFDLIVI DECHRGSASE
310 320 330 340 350
DSAWREILEY FGSATQVGLT ATPKETEDVS NIDYFGEPVY TYSLKEGIED
360 370 380 390 400
GFLAPYKVVR VDIDVDVQGW RPVKGQLDKY GEEIEDRIYN LKDFDRTLVI
410 420 430 440 450
DERTMLVAQT ITDYLKRTNP MDKTIVFCND IDHADRMRHA LVVLNPEQVL
460 470 480 490 500
KNEKYVMKIT GDDDIGKAQL DNFINPKKAY PVIATTSELM TTGVDAQTCK
510 520 530 540 550
LVVLDQNIQS MTKFKQIIGR GTRINEKHGK LWFTILDFKK ATELFADPRF
560 570 580 590 600
DGLPEKVLVV KPGDISDKDS DFNEQLDAEN NADGGDNDAS EAREDVADYQ
610 620 630 640 650
VNRDKQAGNG EFHDDDENKV RKFYVNGVDV KVLAKRVQYY DSDGKLVTES
660 670 680 690 700
FQDYTRKTML KDSEYASLDS FVRKWQDAPR KQVIIEELEQ LGILWDVLAE
710 720 730 740 750
EVGKDLDPFD LLCHVVYGQP PLTRQERVAN VRKRNYFTKY AEPAQQVLNT
760 770 780 790 800
LLDKYADEGV QEIEDVQVLK LKPFDTLGRP IEIIKTRFGD KKAYEQAVNE
810
LENEIYQLPP RSA
Length:813
Mass (Da):92,627
Last modified:November 1, 1996 - v1
Checksum:iA1EB1794123F0ADD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18759 Genomic DNA. Translation: AAD15048.1.
PIRiI41292.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18759 Genomic DNA. Translation: AAD15048.1.
PIRiI41292.

3D structure databases

ProteinModelPortaliQ47281.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ47281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. 3 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: A58.

Entry informationi

Entry nameiT1RE_ECOLX
AccessioniPrimary (citable) accession number: Q47281
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 1, 2015
This is version 77 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.