Q07736 (T1RA_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Type I restriction enzyme EcoAI R protein
Short name=R.EcoAI
EC=3.1.21.3

Gene names

Name:	hsdR
Synonyms:	hsr

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	810 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Restriction system
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Hydrolase
Gene Ontology (GO)
Biological_process	DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW Type I site-specific deoxyribonuclease activity Inferred from electronic annotation. Source: EC helicase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 810	810	Type I restriction enzyme EcoAI R protein		PRO_0000077257
Regions
	Domain	183 – 343	161	Helicase ATP-binding
	Domain	412 – 575	164	Helicase C-terminal
	Nucleotide binding	197 – 203	7	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q07736 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C04E673C8C1DEA51	FASTA	810	92,071
	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

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.
PIR	I41291.
3D structure databases
ProteinModelPortal	Q07736.
ModBase	Search...
Protein family/group databases
REBASE	969. EcoAI.
Proteomic databases
PRIDE	Q07736.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG4096.
OMA	QTCKLIV.
Family and domain databases
InterPro	IPR013670. EcoEI_R_C_dom. IPR006935. Helicase/UvrB_dom. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR007409. Restrct_endonuc_type1_HsdR_N. [Graphical view]
Pfam	PF08463. EcoEI_R_C. 1 hit. PF04313. HSDR_N. 1 hit. PF04851. ResIII. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. [Graphical view]
PROSITE	PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

T1RA_ECOLX

Accession

Primary (citable) accession number: Q07736

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program