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Q8SR37 (RIR1_ENCCU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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
Gene names
Ordered Locus Names:ECU10_0920
OrganismEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) [Reference proteome]
Taxonomic identifier284813 [NCBI]
Taxonomic lineageEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon

Protein attributes

Sequence length768 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 By similarity.

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 By similarity.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 768768Ribonucleoside-diphosphate reductase large chain
PRO_0000187200

Regions

Region211 – 2122Substrate binding By similarity
Region279 – 2824Allosteric effector binding, determines substrate specificity By similarity
Region420 – 4245Substrate binding By similarity
Region595 – 5995Substrate binding By similarity

Sites

Active site4201Proton acceptor By similarity
Active site4221Cysteine radical intermediate By similarity
Active site4241Proton acceptor By similarity
Binding site1961Substrate By similarity
Binding site2411Substrate; via amide nitrogen By similarity
Site2121Important for hydrogen atom transfer By similarity
Site2201Allosteric effector binding, determines substrate specificity By similarity
Site2501Allosteric effector binding, determines substrate specificity By similarity
Site4371Important for hydrogen atom transfer By similarity
Site7291Important for electron transfer By similarity
Site7301Important for electron transfer By similarity
Site7631Interacts with thioredoxin/glutaredoxin By similarity
Site7661Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond212 ↔ 437Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8SR37 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 3E6BF6826805E20D

FASTA76887,941
        10         20         30         40         50         60 
MENFSNSKRI KSEKLGIDLI RSRIEGYVKD LKLRHVDVDE LVERIVSGWC EDMTRKETID 

        70         80         90        100        110        120 
YCSETAASMI TKHPEYGQIS SRIIVSYIHE ITMDSFVEKI KYIQKHRGMV SEEMYGIILE 

       130        140        150        160        170        180 
HGETIEGMIN YENDFLFSYF GILTLMKSYL IKVGEEIIER PQDMFMRVAL QIHKTDFEKV 

       190        200        210        220        230        240 
REVYNLLSGH YFTHATPTLY NSCLKNPQLA SCFLITPRED SIEGVYHMIN QAAIITKYSG 

       250        260        270        280        290        300 
GIGLNLHGIR SKGSSLRSTG GRSNGIIPLI QVLNATKRYI NQGAERRPGS IAIFLEPWHM 

       310        320        330        340        350        360 
EIFDFLELRK NTGPEEFRAR DIFTALWIND LFMERVKNNE EWSLFCPSQA VGLSDVWGEE 

       370        380        390        400        410        420 
FNALYCKYEK TISRTVVPAQ KLWKAIIEAQ IETGTPYMCY KDACNRLSNQ QHLGTIKSSN 

       430        440        450        460        470        480 
LCAEIVEYSS GEETSVCNLA SICLPMFVKD GWFDFEAFRR VVKILTVNLN RVIDFNYYPV 

       490        500        510        520        530        540 
EEARRSNMRN RPIGIGVQGL ADLFAILRLA FESDGARSLN QDIFEAMYYS AMEASCELAE 

       550        560        570        580        590        600 
KEGPFPSYEG SPISKGIFHF ELAGRKASGN WDWEGLRERI RRHGVRNSLL IALMPTAGTS 

       610        620        630        640        650        660 
QIFGNNEAFE PHASNIYTRR THAGEFQIVN QHLVNDLVRL GLWSYEMKNL VIENEGSIQN 

       670        680        690        700        710        720 
ITSIPHEIRE IYKTAWEIKM KSVIDLAADR QVFVDQSQSL NIFIAKPTYS QLTSMHFYGY 

       730        740        750        760 
HCGLKTGMYY LRTRPITSAI KFTVDKKLAE KTLSSMNDTD DPCSMCSS 

« Hide

References

[1]"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi."
Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P.
Nature 414:450-453(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-M1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590449 Genomic DNA. Translation: CAD25811.1.
RefSeqNP_586207.1. NM_001042040.1.

3D structure databases

ProteinModelPortalQ8SR37.
SMRQ8SR37. Positions 79-734.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6035.ECU10_0920.

Proteomic databases

PRIDEQ8SR37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID859856.
KEGGecu:ECU10_0920.

Organism-specific databases

EuPathDBMicrosporidiaDB:ECU10_0920.

Phylogenomic databases

eggNOGCOG0209.
HOGENOMHOG000057035.
KOK10807.
OMADELIHQR.
OrthoDBEOG7C5MHR.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF48168. SSF48168. 1 hit.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
PROSITEPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_ENCCU
AccessionPrimary (citable) accession number: Q8SR37
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2002
Last modified: May 14, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways