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P36602 (RIR1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 127. 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 chain

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase
Gene names
Name:cdc22
ORF Names:SPAC1F7.05
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length811 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Ref.4

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. Interacts with SPD1. Ref.3 Ref.4

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Contains 1 ATP-cone domain.

Ontologies

Keywords
   Biological processDNA replication
   LigandATP-binding
Nucleotide-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-UniPathway

dTTP biosynthetic process

Inferred from mutant phenotype PubMed 6273154. Source: PomBase

deoxyribonucleotide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoside diphosphate phosphorylation

Inferred from mutant phenotype PubMed 6273154. Source: GOC

purine deoxyribonucleoside triphosphate biosynthetic process

Inferred by curator. Source: PomBase

purine nucleoside metabolic process

Inferred by curator. Source: PomBase

pyrimidine nucleoside metabolic process

Inferred by curator. Source: PomBase

regulation of DNA-dependent DNA replication

Inferred from mutant phenotype Ref.1. Source: PomBase

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16823372. Source: PomBase

cytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

ribonucleoside-diphosphate reductase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside diphosphate kinase activity

Inferred from mutant phenotype PubMed 6273154. Source: PomBase

protein binding

Inferred from physical interaction Ref.4. Source: PomBase

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 811811Ribonucleoside-diphosphate reductase large chain
PRO_0000187201

Regions

Domain1 – 9292ATP-cone
Region11 – 177Allosteric activator binding By similarity
Region217 – 2182Substrate binding By similarity
Region285 – 2884Allosteric effector binding, determines substrate specificity By similarity
Region427 – 4315Substrate binding By similarity
Region602 – 6065Substrate binding By similarity

Sites

Active site4271Proton acceptor By similarity
Active site4291Cysteine radical intermediate By similarity
Active site4311Proton acceptor By similarity
Binding site51Allosteric activator By similarity
Binding site531Allosteric activator By similarity
Binding site881Allosteric activator By similarity
Binding site2021Substrate By similarity
Binding site2471Substrate; via amide nitrogen By similarity
Site2181Important for hydrogen atom transfer By similarity
Site2261Allosteric effector binding, determines substrate specificity By similarity
Site2561Allosteric effector binding, determines substrate specificity By similarity
Site4441Important for hydrogen atom transfer By similarity
Site7361Important for electron transfer By similarity
Site7371Important for electron transfer By similarity
Site8061Interacts with thioredoxin/glutaredoxin By similarity
Site8091Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond218 ↔ 444Redox-active By similarity

Experimental info

Sequence conflict2511N → Y in CAA46232. Ref.1
Sequence conflict3271E → Q in CAA46232. Ref.1
Sequence conflict4251C → S in CAA46232. Ref.1
Sequence conflict560 – 5612AS → CI in CAA46232. Ref.1
Sequence conflict5831L → F in CAA46232. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P36602 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 6650E0EE4C2E8DF6

FASTA81191,999
        10         20         30         40         50         60 
MFVYKRDGRQ EKVAFDKITA RVSRLCYGLD SDHVDPVEIT QKVISGVYPG VTTIELDNLA 

        70         80         90        100        110        120 
AETAATMTTK HPDYAILAAR IAVSNLHKQT EKVFSTVVQQ LHDYVNPKTD KPAPMISDKI 

       130        140        150        160        170        180 
YDIVMKHKDE LDSAIIYDRD FTYNFFGFKT LERSYLLRID GKVAERPQHM IMRVAVGIHG 

       190        200        210        220        230        240 
EDIEAAIETY NLMSQRYFTH ASPTLFNAGT PRPQLSSCFL VTMKDDSIEG IYDTLKMCAM 

       250        260        270        280        290        300 
ISKTAGGIGI NIHNIRATGS YIAGTNGTSN GIVPMIRVYN NTARYVDQGG NKRPGAFAAY 

       310        320        330        340        350        360 
LEPWHADVMD FLELRKTHGN EDFRAREMFY ALWIPDLFMQ RVERNEQWTF FCPNEAPGLA 

       370        380        390        400        410        420 
DVWGDEFVAL YEKYEKENRG RRSLPAQKVW YAILQSQVET GNPFMLYKDS CNRKSNQKNV 

       430        440        450        460        470        480 
GTIRCSNLCT EIVEYSSPDE VAVCNLASVA LPTFIKDGKY NFQKLHDVVK VVTRNLNKII 

       490        500        510        520        530        540 
DVNYYPVPEA RRSNMRHRPV GLGVQGLADA FFALRLPFES AGAKKLNIQI FETIYHAALE 

       550        560        570        580        590        600 
ASCEIAQVEG TYESYEGSPA SQGILQYDMW NVNPTDLWDW AELKEKIAKH GIRNSLLVAP 

       610        620        630        640        650        660 
MPTASTSQIL GFNECFEPYT SNMYQRRVLS GEFQIVNPWL LKDLVERDLW NEDMKNKLVM 

       670        680        690        700        710        720 
LDGSIQAIPE IPQDLKDLYK TVWEISQKTV IDYAADRGPF IDQSQSLNIH LKDPSYGKIT 

       730        740        750        760        770        780 
SMHFYGWKKG LKTGMYYLRT MAASAAIKFT VDPVALRARN EESNEENKKP VIKNGKAEIS 

       790        800        810 
AEPTKEEIDI YNEKVLACSI KNPEACEMCS A 

« Hide

References

« Hide 'large scale' references
[1]"The cell cycle genes cdc22+ and suc22+ of the fission yeast Schizosaccharomyces pombe encode the large and small subunits of ribonucleotide reductase."
Fernandez-Sarabia M.J., McInerny C., Harris P., Gordon C., Fantes P.
Mol. Gen. Genet. 238:241-251(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"A novel S phase inhibitor in fission yeast."
Woollard A., Basi G., Nurse P.
EMBO J. 15:4603-4612(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPD1.
[4]"The Schizosaccharomyces pombe replication inhibitor Spd1 regulates ribonucleotide reductase activity and dNTPs by binding to the large Cdc22 subunit."
Hakansson P., Dahl L., Chilkova O., Domkin V., Thelander L.
J. Biol. Chem. 281:1778-1783(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDC22.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65116 Genomic DNA. Translation: CAA46232.1.
CU329670 Genomic DNA. Translation: CAA91952.1.
PIRS34807.
S62577.
RefSeqNP_594491.1. NM_001019920.2.

3D structure databases

ProteinModelPortalP36602.
SMRP36602. Positions 15-752.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278191. 25 interactions.
IntActP36602. 1 interaction.
MINTMINT-4688885.
STRING4896.SPAC1F7.05-1.

Proteomic databases

MaxQBP36602.
PaxDbP36602.
PRIDEP36602.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC1F7.05.1; SPAC1F7.05.1:pep; SPAC1F7.05.
GeneID2541695.
KEGGspo:SPAC1F7.05.

Organism-specific databases

PomBaseSPAC1F7.05.

Phylogenomic databases

eggNOGCOG0209.
HOGENOMHOG000057035.
KOK10807.
OMAANGSIQH.
OrthoDBEOG7C5MHR.
PhylomeDBP36602.

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

NextBio20802788.
PROP36602.

Entry information

Entry nameRIR1_SCHPO
AccessionPrimary (citable) accession number: P36602
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 127 of the entry and version 2 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

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways