Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

RNR1

Organism
Plasmodium falciparum (isolate Dd2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Enzyme regulationi

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the large subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site (By similarity).By similarity

Pathway:iDNA replication

This protein is involved in the pathway DNA replication, which is part of Genetic information processing.
View all proteins of this organism that are known to be involved in the pathway DNA replication and in Genetic information processing.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521Allosteric activatorBy similarity
Binding sitei87 – 871Allosteric activatorBy similarity
Binding sitei200 – 2001SubstrateBy similarity
Sitei216 – 2161Important for hydrogen atom transferBy similarity
Sitei224 – 2241Allosteric effector binding, determines substrate specificityBy similarity
Binding sitei245 – 2451Substrate; via amide nitrogenBy similarity
Sitei254 – 2541Allosteric effector binding, determines substrate specificityBy similarity
Active sitei425 – 4251Proton acceptorBy similarity
Active sitei427 – 4271Cysteine radical intermediateBy similarity
Active sitei429 – 4291Proton acceptorBy similarity
Sitei442 – 4421Important for hydrogen atom transferBy similarity
Sitei737 – 7371Important for electron transferBy similarity
Sitei738 – 7381Important for electron transferBy similarity
Sitei801 – 8011Interacts with thioredoxin/glutaredoxinBy similarity
Sitei804 – 8041Interacts with thioredoxin/glutaredoxinBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase R1 subunit
Gene namesi
Name:RNR1
OrganismiPlasmodium falciparum (isolate Dd2)
Taxonomic identifieri57267 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 806806Ribonucleoside-diphosphate reductase large subunitPRO_0000187198Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi216 ↔ 442Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Structurei

3D structure databases

ProteinModelPortaliP50648.
SMRiP50648. Positions 15-762.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9191ATP-conePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 177Allosteric activator bindingBy similarity
Regioni215 – 2162Substrate bindingBy similarity
Regioni283 – 2864Allosteric effector binding, determines substrate specificityBy similarity
Regioni425 – 4295Substrate bindingBy similarity
Regioni603 – 6075Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 ATP-cone domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0209.

Family and domain databases

InterProiIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50648-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYVLNRKGEE EDISFDQILK RIQRLSYGLH ELVDPARVTQ GVINGMYSGI
60 70 80 90 100
KTCELDELAA QTCAYMATTH PDFSILAARI TTDNLHKNTS DDVAEVAEAL
110 120 130 140 150
YTYKDVRGRP ASLISKEVYD FILLHKDRLN KEIDYTRDFN YDYFGFKTLE
160 170 180 190 200
RSYLLRINNK IIERPQHLLM RVSIGIHIDD IDKALETYHL MSQKYFTHAT
210 220 230 240 250
PTLFNSGTPR PQMSSCFLLS MKADSIEGIF ETLKQCALIS KTAGGIGVAV
260 270 280 290 300
QDIRGQNSYI RGTNGISNGL VPMLRVFNDT ARYVDQGGGK RKGSFAVYIE
310 320 330 340 350
PWHSDIFEFL DLRKNHGKEE LRARDLFYAV WVPDLFMKRV KENKNWTLMC
360 370 380 390 400
PNECPGLSET WGEEFEKLYT KYEEENMGKK TVLAQDLWFA ILQSQIETGV
410 420 430 440 450
PYMLYKDSCN AKSNQKNLGT IKCSNLCCEI IEYTSPDEVA VCNLASIALC
460 470 480 490 500
KFVDLEKKEF NFKKLYEITK IITRNLDKII ERNYYPVKEA KTSNTRHRPI
510 520 530 540 550
GIGVQGLADT FMLLRYPYES DAAKELNKRI FETMYYAALE MSVELASIHG
560 570 580 590 600
PYESYQGSPA SQGILQFDMW NAKVDNKYWD WDELKAKIRK HGLRNSLLLA
610 620 630 640 650
PMPTASTSQI LGNNESFEPY TSNIYYRRVL SGEFFVVNPH LLKDLFDRGL
660 670 680 690 700
WDEDMKQQLI AHNGSIQYIS EIPDDLKELY KTVWEIKQKN IIDMAADRGI
710 720 730 740 750
FIDQSQSLNI YIQKPTFAKL SSMHFYGWEK GLKTGAYYLR TQAATDAIKF
760 770 780 790 800
TVDTHVAKNA VKLKNADGVQ ITREVSRETI STESTVTQNV CPLRRNNDEQ

CLMCSG
Length:806
Mass (Da):92,513
Last modified:October 1, 1996 - v1
Checksum:iA23B414A687B275F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01323 mRNA. Translation: AAA50171.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01323 mRNA. Translation: AAA50171.1.

3D structure databases

ProteinModelPortaliP50648.
SMRiP50648. Positions 15-762.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0209.

Enzyme and pathway databases

UniPathwayiUPA00326.

Family and domain databases

InterProiIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of subunit genes of ribonucleotide reductase, a cell-cycle-regulated enzyme, from Plasmodium falciparum."
    Chakrabarti D., Schuster S.M., Chakrabarti R.
    Proc. Natl. Acad. Sci. U.S.A. 90:12020-12024(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiRIR1_PLAF4
AccessioniPrimary (citable) accession number: P50648
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.