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P10486

- T1R1_ECOLX

UniProt

P10486 - T1R1_ECOLX

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Protein

Type I restriction enzyme EcoR124II R protein

Gene

hsdR

Organism
Escherichia coli
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi308 – 3147ATPPROSITE-ProRule annotation

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

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

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10331033Type I restriction enzyme EcoR124II R proteinPRO_0000077260Add
BLAST

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

1
1033
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 4614Combined sources
Helixi57 – 7216Combined sources
Helixi78 – 8710Combined sources
Helixi96 – 1049Combined sources
Beta strandi108 – 1125Combined sources
Beta strandi118 – 1247Combined sources
Beta strandi126 – 1283Combined sources
Helixi129 – 1313Combined sources
Beta strandi134 – 1385Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi159 – 1668Combined sources
Helixi173 – 1808Combined sources
Beta strandi190 – 1923Combined sources
Helixi193 – 1975Combined sources
Beta strandi200 – 2045Combined sources
Beta strandi209 – 2135Combined sources
Helixi218 – 2203Combined sources
Helixi223 – 2253Combined sources
Beta strandi227 – 2304Combined sources
Helixi240 – 2445Combined sources
Turni245 – 2484Combined sources
Helixi250 – 25910Combined sources
Beta strandi260 – 2634Combined sources
Beta strandi269 – 2713Combined sources
Helixi274 – 29320Combined sources
Helixi299 – 3013Combined sources
Beta strandi302 – 3076Combined sources
Helixi313 – 32412Combined sources
Beta strandi332 – 3376Combined sources
Helixi339 – 3413Combined sources
Helixi344 – 3518Combined sources
Beta strandi358 – 3614Combined sources
Helixi365 – 3728Combined sources
Beta strandi378 – 3825Combined sources
Helixi383 – 39210Combined sources
Helixi397 – 4004Combined sources
Beta strandi403 – 4097Combined sources
Helixi414 – 42512Combined sources
Beta strandi427 – 43711Combined sources
Helixi441 – 4433Combined sources
Helixi450 – 4545Combined sources
Beta strandi456 – 4616Combined sources
Helixi463 – 4686Combined sources
Beta strandi475 – 4795Combined sources
Helixi484 – 4863Combined sources
Helixi487 – 4904Combined sources
Helixi495 – 5006Combined sources
Turni504 – 5085Combined sources
Helixi510 – 52718Combined sources
Beta strandi531 – 5344Combined sources
Beta strandi539 – 5468Combined sources
Helixi547 – 56418Combined sources
Turni565 – 5673Combined sources
Beta strandi568 – 5703Combined sources
Beta strandi576 – 5794Combined sources
Helixi601 – 6033Combined sources
Helixi606 – 62318Combined sources
Helixi631 – 64616Combined sources
Beta strandi649 – 6579Combined sources
Beta strandi660 – 6623Combined sources
Beta strandi668 – 6758Combined sources
Helixi679 – 6879Combined sources
Beta strandi699 – 7068Combined sources
Helixi709 – 71810Combined sources
Helixi724 – 7285Combined sources
Helixi733 – 7386Combined sources
Beta strandi739 – 7413Combined sources
Turni743 – 7453Combined sources
Beta strandi748 – 7503Combined sources
Helixi752 – 76211Combined sources
Beta strandi766 – 7694Combined sources
Helixi772 – 79221Combined sources
Helixi796 – 8049Combined sources
Helixi813 – 8219Combined sources
Helixi826 – 8316Combined sources
Helixi832 – 8343Combined sources
Helixi840 – 85516Combined sources
Helixi880 – 8845Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP10486.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10486.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini294 – 456163Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST

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_dom.
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 .
PIRi S02168.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2W00 X-ray 2.60 A/B 1-1032 [» ]
4BE7 X-ray 2.74 B/D 1-1032 [» ]
4BEB X-ray 2.99 A/B/C/D 1-1032 [» ]
4BEC X-ray 2.84 A/B 1-1032 [» ]
ProteinModelPortali P10486.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-17005N.

Protein family/group databases

REBASEi 990. EcoR124I.

Proteomic databases

PRIDEi P10486.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P10486.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR006935. Helicase/UvrB_dom.
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 ]
Pfami PF12008. EcoR124_C. 1 hit.
PF04313. HSDR_N. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00348. hsdR. 1 hit.
PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Basis for changes in DNA recognition by the EcoR124 and EcoR124/3 type I DNA restriction and modification enzymes."
    Price C., Lingner J., Bickle J., Firman T.A., Glover S.W.
    J. Mol. Biol. 205:115-125(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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 26, 2014
This is version 109 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

External Data

Dasty 3