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Protein

Type I restriction enzyme EcoKI R protein

Gene

hsdR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

The EcoKI enzyme recognizes 5'-AACN6GTGC-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)DescriptionActionsGraphical viewLength
DNA bindingi431 – 450H-T-H motifBy similarityAdd BLAST20
Nucleotide bindingi472 – 478ATPPROSITE-ProRule annotation7

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10459-MONOMER.
ECOL316407:JW4313-MONOMER.
MetaCyc:EG10459-MONOMER.

Protein family/group databases

REBASEi980. EcoKI.
TCDBi3.A.17.1.1. the phage t7 injectisome (t7 injectisome) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Type I restriction enzyme EcoKI R protein (EC:3.1.21.3)
Short name:
R.EcoKI
Gene namesi
Name:hsdR
Synonyms:hsr
Ordered Locus Names:b4350, JW4313
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10459. hsdR.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000772591 – 1170Type I restriction enzyme EcoKI R proteinAdd BLAST1170

Proteomic databases

PaxDbiP08956.
PRIDEiP08956.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi4262769. 25 interactors.
DIPiDIP-9944N.
IntActiP08956. 15 interactors.
MINTiMINT-1243362.
STRINGi511145.b4350.

Structurei

3D structure databases

ProteinModelPortaliP08956.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini458 – 639Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST182
Domaini714 – 879Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili143 – 229Sequence analysisAdd BLAST87

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi574 – 577DEAH box4

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG4107SCJ. Bacteria.
COG4096. LUCA.
HOGENOMiHOG000295053.
InParanoidiP08956.
KOiK01153.
PhylomeDBiP08956.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR013670. EcoEI_R_C_dom.
IPR006935. Helicase/UvrB_N.
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.
PF00271. Helicase_C. 1 hit.
PF04313. HSDR_N. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08956-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMNKSNFEFL KGVNDFTYAI ACAAENNYPD DPNTTLIKMR MFGEATAKHL
60 70 80 90 100
GLLLNIPPCE NQHDLLRELG KIAFVDDNIL SVFHKLRRIG NQAVHEYHND
110 120 130 140 150
LNDAQMCLRL GFRLAVWYYR LVTKDYDFPV PVFVLPERGE NLYHQEVLTL
160 170 180 190 200
KQQLEQQVRE KAQTQAEVEA QQQKLVALNG YIAILEGKQQ ETEAQTQARL
210 220 230 240 250
AALEAQLAEK NAELAKQTEQ ERKAYHKEIT DQAIKRTLNL SEEESRFLID
260 270 280 290 300
AQLRKAGWQA DSKTLRFSKG ARPEPGVNKA IAEWPTGKDE TGNQGFADYV
310 320 330 340 350
LFVGLKPIAV VEAKRNNIDV PARLNESYRY SKCFDNGFLR ETLLEHYSPD
360 370 380 390 400
EVHEAVPEYE TSWQDTSGKQ RFKIPFCYST NGREYRATMK TKSGIWYRDV
410 420 430 440 450
RDTRNMSKAL PEWHRPEELL EMLGSEPQKQ NQWFADNPGM SELGLRYYQE
460 470 480 490 500
DAVRAVEKAI VKGQQEILLA MATGTGKTRT AIAMMFRLIQ SQRFKRILFL
510 520 530 540 550
VDRRSLGEQA LGAFEDTRIN GDTFNSIFDI KGLTDKFPED STKIHVATVQ
560 570 580 590 600
SLVKRTLQSD EPMPVARYDC IVVDEAHRGY ILDKEQTEGE LQFRSQLDYV
610 620 630 640 650
SAYRRILDHF DAVKIALTAT PALHTVQIFG EPVYRYTYRT AVIDGFLIDQ
660 670 680 690 700
DPPIQIITRN AQEGVYLSKG EQVERISPQG EVINDTLEDD QDFEVADFNR
710 720 730 740 750
GLVIPAFNRA VCNELTNYLD PTGSQKTLVF CVTNAHADMV VEELRAAFKK
760 770 780 790 800
KYPQLEHDAI IKITGDADKD ARKVQTMITR FNKERLPNIV VTVDLLTTGV
810 820 830 840 850
DIPSICNIVF LRKVRSRILY EQMKGRATRL CPEVNKTSFK IFDCVDIYST
860 870 880 890 900
LESVDTMRPV VVRPKVELQT LVNEITDSET YKITEADGRS FAEHSHEQLV
910 920 930 940 950
AKLQRIIGLA TFNRDRSETI DKQVRRLDEL CQDAAGVNFN GFASRLREKG
960 970 980 990 1000
PHWSAEVFNK LPGFIARLEK LKTDINNLND APIFLDIDDE VVSVKSLYGD
1010 1020 1030 1040 1050
YDTPQDFLEA FDSLVQRSPN AQPALQAVIN RPRDLTRKGL VELQEWFDRQ
1060 1070 1080 1090 1100
HFEESSLRKA WKETRNEDIA ARLIGHIRRA AVGDALKPFE ERVDHALTRI
1110 1120 1130 1140 1150
KGENDWSSEQ LSWLDRLAQA LKEKVVLDDD VFKTGNFHRR GGKAMLQRTF
1160 1170
DDNLDTLLGK FSDYIWDELA
Length:1,170
Mass (Da):134,095
Last modified:November 24, 2009 - v3
Checksum:iC5B90A799C455318
GO

Sequence cautioni

The sequence AAA97247 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAE78340 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA29791 differs from that shown. Reason: Frameshift at position 1066.Curated
The sequence CAA29791 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA38116 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti611 – 678DAVKI…ERISP → ECGKNRSHRHPGATYCADFR RAGLPLYLPYRGYRRFSDRP GSAYSDHHPQRAGGGLSLQR RAGRAH in CAA29791 (PubMed:3323532).CuratedAdd BLAST68

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06545 Genomic DNA. Translation: CAA29791.1. Sequence problems.
U14003 Genomic DNA. Translation: AAA97247.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77306.2.
AP009048 Genomic DNA. Translation: BAE78340.1. Different initiation.
X54198 Genomic DNA. Translation: CAA38116.1. Different initiation.
PIRiS56576. NDECKR.
RefSeqiNP_418770.2. NC_000913.3.
WP_000981388.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77306; AAC77306; b4350.
BAE78340; BAE78340; BAE78340.
GeneIDi948878.
KEGGiecj:JW4313.
eco:b4350.
PATRICi32124306. VBIEscCol129921_4496.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06545 Genomic DNA. Translation: CAA29791.1. Sequence problems.
U14003 Genomic DNA. Translation: AAA97247.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77306.2.
AP009048 Genomic DNA. Translation: BAE78340.1. Different initiation.
X54198 Genomic DNA. Translation: CAA38116.1. Different initiation.
PIRiS56576. NDECKR.
RefSeqiNP_418770.2. NC_000913.3.
WP_000981388.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP08956.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262769. 25 interactors.
DIPiDIP-9944N.
IntActiP08956. 15 interactors.
MINTiMINT-1243362.
STRINGi511145.b4350.

Protein family/group databases

REBASEi980. EcoKI.
TCDBi3.A.17.1.1. the phage t7 injectisome (t7 injectisome) family.

Proteomic databases

PaxDbiP08956.
PRIDEiP08956.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77306; AAC77306; b4350.
BAE78340; BAE78340; BAE78340.
GeneIDi948878.
KEGGiecj:JW4313.
eco:b4350.
PATRICi32124306. VBIEscCol129921_4496.

Organism-specific databases

EchoBASEiEB0454.
EcoGeneiEG10459. hsdR.

Phylogenomic databases

eggNOGiENOG4107SCJ. Bacteria.
COG4096. LUCA.
HOGENOMiHOG000295053.
InParanoidiP08956.
KOiK01153.
PhylomeDBiP08956.

Enzyme and pathway databases

BioCyciEcoCyc:EG10459-MONOMER.
ECOL316407:JW4313-MONOMER.
MetaCyc:EG10459-MONOMER.

Miscellaneous databases

PROiP08956.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR013670. EcoEI_R_C_dom.
IPR006935. Helicase/UvrB_N.
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.
PF00271. Helicase_C. 1 hit.
PF04313. HSDR_N. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiT1RK_ECOLI
AccessioniPrimary (citable) accession number: P08956
Secondary accession number(s): Q2M5W6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 24, 2009
Last modified: November 2, 2016
This is version 153 of the entry and version 3 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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.