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Protein

Ribonucleoside-diphosphate reductase large chain

Gene

rnr-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.1 Publication

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.1 Publication

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 sitei5Allosteric activatorBy similarity1
Binding sitei53Allosteric activatorBy similarity1
Binding sitei88Allosteric activatorBy similarity1
Binding sitei202SubstrateBy similarity1
Sitei218Important for hydrogen atom transferBy similarity1
Sitei226Allosteric effector binding, determines substrate specificityBy similarity1
Binding sitei247Substrate; via amide nitrogenBy similarity1
Sitei256Allosteric effector binding, determines substrate specificityBy similarity1
Active sitei427Proton acceptorBy similarity1
Active sitei429Cysteine radical intermediateBy similarity1
Active sitei431Proton acceptorBy similarity1
Sitei444Important for hydrogen atom transferBy similarity1
Sitei738Important for electron transferBy similarity1
Sitei739Important for electron transferBy similarity1
Sitei924Interacts with thioredoxin/glutaredoxinBy similarity1
Sitei927Interacts 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 chain (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase large subunit
Gene namesi
Name:rnr-1
ORF Names:B2A19.30, NCU03539
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
Proteomesi
  • UP000001805 Componenti: Chromosome 6, Linkage Group II

Organism-specific databases

EuPathDBiFungiDB:NCU03539.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi26C → Y in un-24; temperature-sensitive mutant. 1 Publication1
Mutagenesisi124V → I in un-24; temperature-sensitive mutant. 1 Publication1
Mutagenesisi125M → I in un-24; temperature-sensitive mutant. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001872021 – 929Ribonucleoside-diphosphate reductase large chainAdd BLAST929

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi218 ↔ 444Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

BioGridi1974838. 3 interactors.

Structurei

3D structure databases

ProteinModelPortaliQ9UW15.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 92ATP-conePROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni11 – 17Allosteric activator bindingBy similarity7
Regioni217 – 218Substrate bindingBy similarity2
Regioni285 – 288Allosteric effector binding, determines substrate specificityBy similarity4
Regioni427 – 431Substrate bindingBy similarity5
Regioni604 – 608Substrate bindingBy similarity5

Sequence similaritiesi

Contains 1 ATP-cone domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000057035.
InParanoidiQ9UW15.
KOiK10807.
OMAiYELLWQM.
OrthoDBiEOG092C0QYB.

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.

Q9UW15-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYVKKRDGRQ ERVQFDKITA RVSRLCYGLD MNHVDPVAIT QKVISGVYGG
60 70 80 90 100
VTTAQLDDLA AETAAYMTVT HPDYAILAAR IAVSNLHKQT KKQWSLVISE
110 120 130 140 150
LYNYVNPRTG KHSPMIAKDV YECVMRHKDE FDSAIVYDRD FNYQYFGFKT
160 170 180 190 200
LERSYLLKLD GQIAERPQHM IMRVAVGIWG DDVERVIETY NLMSLKTFTH
210 220 230 240 250
ASPTLFNAGT PQPQLSSCFL VDMKEDSIEG IYDTLKTCAM ISKMAGGIGL
260 270 280 290 300
NIHRIRATGS YIAGTNGTSN GIVPMLRVFN NTARYVDQGG NKRPGAFAIY
310 320 330 340 350
LEPWHADVFE FLDLRKNHGK EEVRARDLFL ALWIPDLFMK RVEQNGQWTL
360 370 380 390 400
MCPHECPGLA DVYGDEFEAL YEKYEKEGKG RKTVKAQKLW YAILEAQTET
410 420 430 440 450
GNPFMLYKDA CNRKSNQKNL GTIRSSNLCT EIIEYSAPDE VAVCNLASLA
460 470 480 490 500
LSAFIDYENA SYDFKKLHEV TQVVVRNLNK IIDINHYPVK EAHNSNMRHR
510 520 530 540 550
PIGVGVQGLA DAFLALRMPF DSDAASKLNI QIFETIYHAA LTASCQLAKE
560 570 580 590 600
QGPYATYEGS PVSQGILQYD MWNVTPTNLW DWTALKADIK KYGVRNSLLL
610 620 630 640 650
APMPTASTSQ ILGNNECFEP YTSNIYQRRV LAGEFQVVNP WLLRDLVEMG
660 670 680 690 700
LWSDAMKNRI IAEGGSIQNI QSIPNDIKAL YKTVWEISQR TIVKMAADRG
710 720 730 740 750
AFIDQSQSLN IHMREPTMGK ITSMHFAGWK MGLKTGMYYL RTQAAAQPIQ
760 770 780 790 800
FTVDQEALRA TDDRVAPAHS GLKKRSPPAG TYTSIVLREN TSGPRPYAQT
810 820 830 840 850
GVSGTSTPIG TRDVPTPAST PPPTEVPETL VQSDNRPRPL VSPAKSAGFK
860 870 880 890 900
ADLPEPESPK ALATDPIVKT EDIGSPLLER KEGQNEDVDE DSQERDENIY
910 920
SNAPLSEQQV AACAWNPGAD PSSCEMCSG
Length:929
Mass (Da):103,804
Last modified:April 30, 2003 - v2
Checksum:i68C47E8B21C047B8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti912A → R in AAD49743 (PubMed:10660063).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF171697 Genomic DNA. Translation: AAD49743.1.
AL390092 Genomic DNA. Translation: CAB98233.1.
CM002237 Genomic DNA. Translation: EAA27582.1.
PIRiT43711.
RefSeqiXP_956818.1. XM_951725.3.

Genome annotation databases

EnsemblFungiiEAA27582; EAA27582; NCU03539.
GeneIDi3872956.
KEGGincr:NCU03539.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF171697 Genomic DNA. Translation: AAD49743.1.
AL390092 Genomic DNA. Translation: CAB98233.1.
CM002237 Genomic DNA. Translation: EAA27582.1.
PIRiT43711.
RefSeqiXP_956818.1. XM_951725.3.

3D structure databases

ProteinModelPortaliQ9UW15.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1974838. 3 interactors.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAA27582; EAA27582; NCU03539.
GeneIDi3872956.
KEGGincr:NCU03539.

Organism-specific databases

EuPathDBiFungiDB:NCU03539.

Phylogenomic databases

HOGENOMiHOG000057035.
InParanoidiQ9UW15.
KOiK10807.
OMAiYELLWQM.
OrthoDBiEOG092C0QYB.

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_NEUCR
AccessioniPrimary (citable) accession number: Q9UW15
Secondary accession number(s): Q7RXZ9, Q9P3G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: November 2, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

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.