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Protein

Type I restriction enzyme EcoR124II R protein

Gene

hsdR

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The EcoR124/3 I enzyme recognizes 5'-GAAN7RTCG-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
Nucleotide bindingi308 – 314ATPPROSITE-ProRule annotation7

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

Protein family/group databases

REBASEi990. EcoR124I.

Names & Taxonomyi

Protein namesi
Recommended name:
Type I restriction enzyme EcoR124II R protein (EC:3.1.21.3)
Short name:
R.EcoR124II
Gene namesi
Name:hsdR
Synonyms:hsr
Encoded oniPlasmid IncFIV R124/30 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000772601 – 1033Type I restriction enzyme EcoR124II R proteinAdd BLAST1033

Proteomic databases

PRIDEiP10486.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-17005N.

Structurei

Secondary structure

11033
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi33 – 46Combined sources14
Helixi57 – 72Combined sources16
Helixi78 – 87Combined sources10
Helixi96 – 104Combined sources9
Beta strandi108 – 112Combined sources5
Beta strandi118 – 124Combined sources7
Beta strandi126 – 128Combined sources3
Helixi129 – 131Combined sources3
Beta strandi134 – 138Combined sources5
Beta strandi143 – 145Combined sources3
Beta strandi151 – 156Combined sources6
Beta strandi159 – 166Combined sources8
Helixi173 – 180Combined sources8
Turni190 – 192Combined sources3
Helixi193 – 197Combined sources5
Beta strandi200 – 204Combined sources5
Beta strandi209 – 213Combined sources5
Helixi218 – 220Combined sources3
Helixi223 – 225Combined sources3
Beta strandi227 – 230Combined sources4
Helixi240 – 246Combined sources7
Helixi250 – 258Combined sources9
Beta strandi260 – 263Combined sources4
Beta strandi269 – 271Combined sources3
Helixi274 – 292Combined sources19
Turni299 – 301Combined sources3
Beta strandi302 – 307Combined sources6
Helixi313 – 324Combined sources12
Beta strandi332 – 337Combined sources6
Helixi339 – 341Combined sources3
Helixi344 – 351Combined sources8
Beta strandi359 – 361Combined sources3
Helixi365 – 371Combined sources7
Beta strandi378 – 382Combined sources5
Helixi383 – 392Combined sources10
Helixi397 – 400Combined sources4
Beta strandi401 – 409Combined sources9
Beta strandi412 – 414Combined sources3
Helixi415 – 425Combined sources11
Beta strandi427 – 437Combined sources11
Helixi441 – 443Combined sources3
Helixi450 – 454Combined sources5
Beta strandi456 – 461Combined sources6
Helixi463 – 468Combined sources6
Beta strandi475 – 479Combined sources5
Turni484 – 486Combined sources3
Helixi487 – 490Combined sources4
Helixi495 – 500Combined sources6
Turni504 – 508Combined sources5
Helixi510 – 527Combined sources18
Beta strandi531 – 534Combined sources4
Beta strandi539 – 546Combined sources8
Helixi547 – 566Combined sources20
Beta strandi568 – 570Combined sources3
Beta strandi576 – 579Combined sources4
Beta strandi586 – 589Combined sources4
Beta strandi591 – 593Combined sources3
Helixi601 – 603Combined sources3
Helixi606 – 623Combined sources18
Helixi631 – 646Combined sources16
Beta strandi649 – 657Combined sources9
Beta strandi660 – 662Combined sources3
Beta strandi668 – 675Combined sources8
Helixi679 – 686Combined sources8
Helixi687 – 689Combined sources3
Beta strandi699 – 706Combined sources8
Helixi709 – 718Combined sources10
Helixi724 – 728Combined sources5
Helixi733 – 738Combined sources6
Beta strandi739 – 741Combined sources3
Turni743 – 745Combined sources3
Beta strandi748 – 750Combined sources3
Helixi752 – 762Combined sources11
Beta strandi766 – 769Combined sources4
Helixi772 – 792Combined sources21
Helixi796 – 804Combined sources9
Beta strandi811 – 813Combined sources3
Helixi818 – 821Combined sources4
Helixi826 – 832Combined sources7
Helixi840 – 852Combined sources13
Helixi880 – 883Combined sources4
Beta strandi884 – 886Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W00X-ray2.60A/B1-1032[»]
4BE7X-ray2.74B/D1-1032[»]
4BEBX-ray2.99A/B/C/D1-1032[»]
4BECX-ray2.84A/B1-1032[»]
4XJXX-ray2.40A/B1-1032[»]
ProteinModelPortaliP10486.
SMRiP10486.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10486.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini294 – 456Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST163

Sequence similaritiesi

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

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006935. Helicase/UvrB_N.
IPR014001. Helicase_ATP-bd.
IPR027417. P-loop_NTPase.
IPR007409. Restrct_endonuc_type1_HsdR_N.
IPR004473. Restrct_endonuc_typeI_HsdR.
IPR022625. TypeI_RM_Rsu_C.
[Graphical view]
PfamiPF12008. EcoR124_C. 1 hit.
PF04313. HSDR_N. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00348. hsdR. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10486-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHQTHTIAE SNNFIVLDKY IKAEPTGDSY QSESDLEREL IQDLRNQGYE
60 70 80 90 100
FISVKSQSAM LANVREQLQN LNGVVFNDSE WRRFTEQYLD NPSDGILDKT
110 120 130 140 150
RKIHIDYICD FIFDDERLEN IYLIDKKNLM RNKVQIIQQF EQAGSHANRY
160 170 180 190 200
DVTILVNGLP LVQIELKKRG VAIREAFNQI HRYSKESFNS ENSLFKYLQL
210 220 230 240 250
FVISNGTDTR YFANTTKRDK NSFDFTMNWA KSDNTLIKDL KDFTATCFQK
260 270 280 290 300
HTLLNVLVNY SVFDSSQTLL VMRPYQIAAT ERILWKIKSS FTAKNWSKPE
310 320 330 340 350
SGGYIWHTTG SGKTLTSFKA ARLATELDFI DKVFFVVDRK DLDYQTMKEY
360 370 380 390 400
QRFSPDSVNG SENTAGLKRN LDKDDNKIIV TTIQKLNNLM KAESDLPVYN
410 420 430 440 450
QQVVFIFDEC HRSQFGEAQK NLKKKFKRYY QFGFTGTPIF PENALGSETT
460 470 480 490 500
ASVFGRELHS YVITDAIRDE KVLKFKVDYN DVRPQFKSLE TETDEKKLSA
510 520 530 540 550
AENQQAFLHP MRIQEITQYI LNNFRQKTHR TFPGSKGFNA MLAVSSVDAA
560 570 580 590 600
KAYYATFKRL QEEAANKSAT YKPLRIATIF SFAANEEQNA IGEISDETFD
610 620 630 640 650
TSAMDSSAKE FLDAAIREYN SHFKTNFSTD SNGFQNYYRD LAQRVKNQDI
660 670 680 690 700
DLLIVVGMFL TGFDAPTLNT LFVDKNLRYH GLMQAFSRTN RIYDATKTFG
710 720 730 740 750
NIVTFRDLER STIDAITLFG DKNTKNVVLE KSYTEYMEGF TDAATGEAKR
760 770 780 790 800
GFMTVVSELE QRFPDPTSIE SEKEKKDFVK LFGEYLRAEN ILQNYDEFAT
810 820 830 840 850
LKALQQIDLS DPVAVEKFKA EHYVDDEKFA ELQTIRLPAD RKIQDYRSAY
860 870 880 890 900
NDIRDWQRRE KEAEKKEKST TDWDDVVFEV DLLKSQEINL DYILGLIFEH
910 920 930 940 950
NRQNKGKGEM IEEVKRLIRS SLGNRAKEGL VVDFIQQTNL DDLPDKASII
960 970 980 990 1000
DAFFTFAQRE QQREAEALIK EENLNEDAAK RYIRTSLKRE YATENGTELN
1010 1020 1030
ETLPKLSPLN PQYKTKKQAV FRKSSRLLRS LKA
Length:1,033
Mass (Da):119,657
Last modified:July 1, 1989 - v1
Checksum:iB55F3991356C1506
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13145 Genomic DNA. Translation: CAA31543.1.
PIRiS02168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13145 Genomic DNA. Translation: CAA31543.1.
PIRiS02168.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W00X-ray2.60A/B1-1032[»]
4BE7X-ray2.74B/D1-1032[»]
4BEBX-ray2.99A/B/C/D1-1032[»]
4BECX-ray2.84A/B1-1032[»]
4XJXX-ray2.40A/B1-1032[»]
ProteinModelPortaliP10486.
SMRiP10486.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-17005N.

Protein family/group databases

REBASEi990. EcoR124I.

Proteomic databases

PRIDEiP10486.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP10486.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006935. Helicase/UvrB_N.
IPR014001. Helicase_ATP-bd.
IPR027417. P-loop_NTPase.
IPR007409. Restrct_endonuc_type1_HsdR_N.
IPR004473. Restrct_endonuc_typeI_HsdR.
IPR022625. TypeI_RM_Rsu_C.
[Graphical view]
PfamiPF12008. EcoR124_C. 1 hit.
PF04313. HSDR_N. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00348. hsdR. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiT1R1_ECOLX
AccessioniPrimary (citable) accession number: P10486
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 115 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.

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.