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Q03604 (RIR1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonucleoside-diphosphate reductase large subunit

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase large subunit
Gene names
Name:rnr-1
ORF Names:T23G5.1
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length788 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

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.

Pathway

Genetic information processing; DNA replication.

Subunit structure

Heterodimer of a large and a small subunit.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Contains 1 ATP-cone domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 788788Ribonucleoside-diphosphate reductase large subunit
PRO_0000187194

Regions

Domain7 – 9892ATP-cone
Region17 – 237Allosteric activator binding By similarity
Region223 – 2242Substrate binding By similarity
Region291 – 2944Allosteric effector binding, determines substrate specificity By similarity
Region433 – 4375Substrate binding By similarity
Region609 – 6135Substrate binding By similarity

Sites

Active site4331Proton acceptor By similarity
Active site4351Cysteine radical intermediate By similarity
Active site4371Proton acceptor By similarity
Binding site111Allosteric activator By similarity
Binding site591Allosteric activator By similarity
Binding site941Allosteric activator By similarity
Binding site2081Substrate By similarity
Binding site2531Substrate; via amide nitrogen By similarity
Site2241Important for hydrogen atom transfer By similarity
Site2321Allosteric effector binding, determines substrate specificity By similarity
Site2621Allosteric effector binding, determines substrate specificity By similarity
Site4501Important for hydrogen atom transfer By similarity
Site7431Important for electron transfer By similarity
Site7441Important for electron transfer By similarity
Site7831Interacts with thioredoxin/glutaredoxin By similarity
Site7861Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond224 ↔ 450Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03604 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: B1AF398B173407D4

FASTA78888,970
        10         20         30         40         50         60 
MQRYNSTYVV KRDGRKEDVH FDKITSRIQK LSYGLNMDFV DPVAVAIKVI SGLYKGVTTV 

        70         80         90        100        110        120 
ELDNLAAETA ASMTTQHPEY ALLAARIAVS NLHKKTNKVF SEVMKTLHEF HHPHTGKHAP 

       130        140        150        160        170        180 
MISDETWAII EKNADKLNSA IVYDRDYSYT YFGFKTLERS YLLKINKEIV ERPQQMLMRV 

       190        200        210        220        230        240 
SIGIHGDDIT SAIETYNLMS ERYMTHASPT LFNSGTCRPQ MSSCFLLTMS EDSILGIYDT 

       250        260        270        280        290        300 
LKQCALISKS AGGIGLNVHK IRATGSVIAG TNGTSNGLIP MLRVYNNTAR YVDQGGNKRP 

       310        320        330        340        350        360 
GAFAIYLEPW HADIFEFVSL RKNTGPEEER ARDLFLALWI PDLFMKRVEK DQEWSLMCPC 

       370        380        390        400        410        420 
ECPGLDDCWG EEFEALYAKY EAEGRVRKTV KARKLWEHIV SNQIETGLPY ITYKDAANRK 

       430        440        450        460        470        480 
SNQQNLGTIK CSNLCTEIIE YSAPDEIAVC NLASIALNRY VTPEKKFDFV KLAEVTKVIT 

       490        500        510        520        530        540 
RNLNKIIDVN YYPVEEARNS NMRHRPIGLG VQGLADCFML MRYPFTSAEA RDLNKRIFET 

       550        560        570        580        590        600 
IYYAALEASC ELAELNGPYS TYEGSPVSKG QLQFDMWGVT PTDQCDWATL RKKIAKHGIR 

       610        620        630        640        650        660 
NSLLMAPMPT ASTAQILGNN ESIEPYTSNI YSRRVLSGDF QIVNPHMLKD LVERGLWTDE 

       670        680        690        700        710        720 
MKNRLIANNG SIQNIDGIPS DIKELYRTVW EISQKDIIEM AADRGAYIDQ SQSLNIHMAK 

       730        740        750        760        770        780 
PSYAGITSMH FYGWKKGLKT GMYYLRTKPA VNAVQFTVDK NALKTNQQAE TPATVAESQD 


EGCLMCSG 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z19158 Genomic DNA. Translation: CAA79574.1.
PIRS28302.
RefSeqNP_499039.1. NM_066638.4.
UniGeneCel.7791.

3D structure databases

ProteinModelPortalQ03604.
SMRQ03604. Positions 21-748.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid41500. 3 interactions.
DIPDIP-26889N.
IntActQ03604. 3 interactions.
MINTMINT-1080458.
STRING6239.T23G5.1.2.

Proteomic databases

PaxDbQ03604.
PRIDEQ03604.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaT23G5.1.1; T23G5.1.1; T23G5.1.
T23G5.1.2; T23G5.1.2; T23G5.1.
T23G5.1.3; T23G5.1.3; T23G5.1.
GeneID176301.
KEGGcel:CELE_T23G5.1.
UCSCT23G5.1.2. c. elegans.

Organism-specific databases

CTD176301.
WormBaseT23G5.1; CE00331; WBGene00004391; rnr-1.

Phylogenomic databases

eggNOGCOG0209.
HOGENOMHOG000057035.
InParanoidQ03604.
KOK10807.
OMAKSHIQFY.
PhylomeDBQ03604.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF48168. SSF48168. 1 hit.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
PROSITEPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio891992.
PROQ03604.

Entry information

Entry nameRIR1_CAEEL
AccessionPrimary (citable) accession number: Q03604
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase