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Q07736

- T1RA_ECOLX

UniProt

Q07736 - T1RA_ECOLX

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Protein
Type I restriction enzyme EcoAI R protein
Gene
hsdR, hsr
Organism
Escherichia coli
Status
Reviewed - 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 – 2037ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. Type I site-specific deoxyribonuclease activity Source: UniProtKB-EC
  4. helicase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

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 protein
PRO_0000077257Add
BLAST

Proteomic databases

PRIDEiQ07736.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ07736.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini183 – 343161Helicase ATP-binding
Add
BLAST
Domaini412 – 575164Helicase C-terminal
Add
BLAST

Sequence similaritiesi

Belongs to the HsdR family.

Phylogenomic databases

eggNOGiCOG4096.
OMAiKNNDFKP.

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

MAELNLSNLT EADIITKCVM PAILNAGWDN TTQIRQEVKL RDGKVIVRGK    50
VAARRTVKSA DIVLYHKPGI PLAVIEAKAN KHEIGKGMQQ GIEYARLLDV 100
PFVFATNGDG FIFRDATAAE GECLEKQITL DDFPSPAELW QKFCLWKGYT 150
QAQLPVITQD YYDDGSGKSP RYYQLQAINK TIEAVSNGQN RVLLVMATGT 200
GKTYTAFQII WRLWKSKNKK RILFLADRNI LVDQTKNNDF QPFGTAMTKV 250
SGRTIDPAYE IHLALYQAIT GPEEDQKAFK QVAPDFFDLI VIDECHRGSA 300
SEDSAWREIL DYFSSATQIG LTATPKETHE VSSTDYFGDP VYVYSLKEGI 350
EDGFLAPYKV VRVDIDVDLQ GWRPTKGQTD LNGEVIDDRI YNQKDFDRTM 400
VIDERTELVA RTITDYLKRT NPMDKTIVFC NDIDHAERMR RALVNLNPEQ 450
VKKNDKYVMK ITGDDEIGKA QLDNFINPKK PYPVIATTSE LMTTGVDAKT 500
CKLVVLDQNI QSMTKFKQII GRGTRIDERY GKLWFTILDF KKATELFADE 550
RFDGIPEKVM DTTPEDIADP ESDFEEKLEE ISEHDEEQVT GVDEPPAPPY 600
QVTDTDDVGP LPEEDEKKIR KFHVNGVAVG VIAQRVQYYD ADGKLVTESF 650
KDYTRKTLLK EYASLDDFTR KWQDADRKEA IIHELEQQGI IWEVLAEEVG 700
KDLDPFDMLC HVVYGQPPLT RKERAENVRK RNYFTKYSEA AQAVLDNLLD 750
KYADAGVQEI ESIQVLKLKP FDSMGTLPEI IKTGFGDRNG YNQALSELEN 800
EIYQLPPRSA 810
Length:810
Mass (Da):92,071
Last modified:November 1, 1996 - v1
Checksum:iC04E673C8C1DEA51
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L18758 Genomic DNA. Translation: AAA23983.1.
PIRiI41291.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L18758 Genomic DNA. Translation: AAA23983.1 .
PIRi I41291.

3D structure databases

ProteinModelPortali Q07736.
ModBasei Search...

Protein family/group databases

REBASEi 969. EcoAI.

Proteomic databases

PRIDEi Q07736.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG4096.
OMAi KNNDFKP.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR013670. 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 ]
Pfami PF08463. EcoEI_R_C. 1 hit.
PF04313. HSDR_N. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 4 hits.
PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 84 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

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