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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

Pathwayi: DNA 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)DescriptionActionsGraphical viewLength
Binding sitei52Allosteric activatorBy similarity1
Binding sitei87Allosteric activatorBy similarity1
Binding sitei200SubstrateBy similarity1
Sitei216Important for hydrogen atom transferBy similarity1
Sitei224Allosteric effector binding, determines substrate specificityBy similarity1
Binding sitei245Substrate; via amide nitrogenBy similarity1
Sitei254Allosteric effector binding, determines substrate specificityBy similarity1
Active sitei425Proton acceptorBy similarity1
Active sitei427Cysteine radical intermediateBy similarity1
Active sitei429Proton acceptorBy similarity1
Sitei442Important for hydrogen atom transferBy similarity1
Sitei737Important for electron transferBy similarity1
Sitei738Important for electron transferBy similarity1
Sitei801Interacts with thioredoxin/glutaredoxinBy similarity1
Sitei804Interacts with thioredoxin/glutaredoxinBy similarity1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001871981 – 806Ribonucleoside-diphosphate reductase large subunitAdd BLAST806

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 91ATP-conePROSITE-ProRule annotationAdd BLAST91

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni11 – 17Allosteric activator bindingBy similarity7
Regioni215 – 216Substrate bindingBy similarity2
Regioni283 – 286Allosteric effector binding, determines substrate specificityBy similarity4
Regioni425 – 429Substrate bindingBy similarity5
Regioni603 – 607Substrate bindingBy similarity5

Sequence similaritiesi

Contains 1 ATP-cone domain.PROSITE-ProRule annotation

Family and domain databases

InterProiIPR005144. ATP-cone_dom.
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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00326.

Family and domain databases

InterProiIPR005144. ATP-cone_dom.
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...

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: October 5, 2016
This is version 80 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

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.