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O61065 (RIR1_CRYPV) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 chain

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase R1 subunit
Gene names
Name:RNR1
OrganismCryptosporidium parvum
Taxonomic identifier5807 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaCryptosporidiidaeCryptosporidium

Protein attributes

Sequence length803 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 – 803803Ribonucleoside-diphosphate reductase large chain
PRO_0000187196

Regions

Domain1 – 9191ATP-cone
Region11 – 177Allosteric activator binding By similarity
Region215 – 2162Substrate binding By similarity
Region283 – 2864Allosteric effector binding, determines substrate specificity By similarity
Region425 – 4295Substrate binding By similarity
Region603 – 6075Substrate binding By similarity

Sites

Active site4251Proton acceptor By similarity
Active site4271Cysteine radical intermediate By similarity
Active site4291Proton acceptor By similarity
Binding site521Allosteric activator By similarity
Binding site871Allosteric activator By similarity
Binding site2001Substrate By similarity
Binding site2451Substrate; via amide nitrogen By similarity
Site2161Important for hydrogen atom transfer By similarity
Site2241Allosteric effector binding, determines substrate specificity By similarity
Site2541Allosteric effector binding, determines substrate specificity By similarity
Site4421Important for hydrogen atom transfer By similarity
Site7371Important for electron transfer By similarity
Site7381Important for electron transfer By similarity
Site7981Interacts with thioredoxin/glutaredoxin By similarity
Site8011Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond216 ↔ 442Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O61065 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 9DBE7F2AC337F97F

FASTA80391,123
        10         20         30         40         50         60 
MYVVNRKGEE EPVSFDQILS RITKLSYGLH PLVDPARVTQ AVINGLYSGI KTSELDELAS 

        70         80         90        100        110        120 
QTCAYMAATH NDFSKLAARI STSNLHKNTS SDIGDVASQL YNFKDNQGCP APLISKPVYD 

       130        140        150        160        170        180 
FIMENRERIN SKIDFSKDFE YDYFAFKTLE RSYLLKIDNK VVERPQHLLM RVSCGIHCGD 

       190        200        210        220        230        240 
IEAALETYEL LSQKYFTHAT PTLFNSGTPR PQMSSCFLLR IPEDSINGIF DTLTKCANIS 

       250        260        270        280        290        300 
KTAGGLGVAV SNIRGTGSYI RGTNGRSNGL IPMLRVYNDT ARYIDQGGGK RKGAIAIYLE 

       310        320        330        340        350        360 
PWHVDVVEFI EIRKNHGKEE MRCRDLFPAL WVPDLFMERV EKDQDWTLMC PDECRGLQDV 

       370        380        390        400        410        420 
WGDDFKKLYE EYEKQGRGRK TMKAQKLWFL ILQAQIETGT PFICYKDAAN SKSNQKNLGT 

       430        440        450        460        470        480 
IVSSNLCTEI IEYTSTDEVA VCNLASIGLP KFVDKNNKTF DFDKLKEVTK VITRNLNKLI 

       490        500        510        520        530        540 
DVGYYSLKEC KKSNLRHRPL GIGIQGLADC FMMLRMPYES EGAKKLNKQI FEVIYYAALD 

       550        560        570        580        590        600 
ASCELAEKYG PYETYSGSPA SKGILQFDMW GVTPDSGLCD WDLLKDRISK HGIRNSLLIS 

       610        620        630        640        650        660 
PMPTASTSQI LGNNESFEPF TSNIYHRRVL SGEFFVVNPH LLNDLLELGL WDDRLKQNII 

       670        680        690        700        710        720 
ANNGSIQNIL TIPEDIRELY KTVWEIKQKT VIDMAADRGP YVCQSQSLNI HMENANFAKL 

       730        740        750        760        770        780 
SSMHFYGWKK GLKTGIYYLR TQSATRPIQF TVDQQLLKSE TKEKDSLETN KRQALEPEAQ 

       790        800 
KLIACPLRPT NMKDDEECMM CSG 

« Hide

References

[1]"Molecular characterization of ribonucleotide reductase from Cryptosporidium parvum."
Akiyoshi D.E., Balakrishnan R., Huettinger C., Widmer G., Tzipori S.
DNA Seq. 13:167-172(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: GCH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF043243 Genomic DNA. Translation: AAC12280.2.

3D structure databases

ProteinModelPortalO61065.
SMRO61065. Positions 15-789.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0209.

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...

Entry information

Entry nameRIR1_CRYPV
AccessionPrimary (citable) accession number: O61065
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 14, 2001
Last modified: October 16, 2013
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways