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P36602

- RIR1_SCHPO

UniProt

P36602 - RIR1_SCHPO

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Protein

Ribonucleoside-diphosphate reductase large chain

Gene
cdc22, SPAC1F7.05
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 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.

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei5 – 51Allosteric activator By similarity
Binding sitei53 – 531Allosteric activator By similarity
Binding sitei88 – 881Allosteric activator By similarity
Binding sitei202 – 2021Substrate By similarity
Sitei218 – 2181Important for hydrogen atom transfer By similarity
Sitei226 – 2261Allosteric effector binding, determines substrate specificity By similarity
Binding sitei247 – 2471Substrate; via amide nitrogen By similarity
Sitei256 – 2561Allosteric effector binding, determines substrate specificity By similarity
Active sitei427 – 4271Proton acceptor By similarity
Active sitei429 – 4291Cysteine radical intermediate By similarity
Active sitei431 – 4311Proton acceptor By similarity
Sitei444 – 4441Important for hydrogen atom transfer By similarity
Sitei736 – 7361Important for electron transfer By similarity
Sitei737 – 7371Important for electron transfer By similarity
Sitei806 – 8061Interacts with thioredoxin/glutaredoxin By similarity
Sitei809 – 8091Interacts with thioredoxin/glutaredoxin By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. nucleoside diphosphate kinase activity Source: PomBase
  3. protein binding Source: PomBase
  4. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB

GO - Biological processi

  1. deoxyribonucleotide biosynthetic process Source: UniProtKB
  2. DNA replication Source: UniProtKB-UniPathway
  3. dTTP biosynthetic process Source: PomBase
  4. nucleoside diphosphate phosphorylation Source: GOC
  5. purine deoxyribonucleoside triphosphate biosynthetic process Source: PomBase
  6. purine nucleoside metabolic process Source: PomBase
  7. pyrimidine nucleoside metabolic process Source: PomBase
  8. regulation of DNA-dependent DNA replication Source: PomBase
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
Gene namesi
Name:cdc22
ORF Names:SPAC1F7.05
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC1F7.05.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
  3. ribonucleoside-diphosphate reductase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 811811Ribonucleoside-diphosphate reductase large chainPRO_0000187201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi218 ↔ 444Redox-active By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP36602.
PaxDbiP36602.
PRIDEiP36602.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit. Interacts with SPD1.2 Publications

Protein-protein interaction databases

BioGridi278191. 25 interactions.
IntActiP36602. 1 interaction.
MINTiMINT-4688885.
STRINGi4896.SPAC1F7.05-1.

Structurei

3D structure databases

ProteinModelPortaliP36602.
SMRiP36602. Positions 15-752.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292ATP-coneAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 177Allosteric activator binding By similarity
Regioni217 – 2182Substrate binding By similarity
Regioni285 – 2884Allosteric effector binding, determines substrate specificity By similarity
Regioni427 – 4315Substrate binding By similarity
Regioni602 – 6065Substrate binding By similarity

Sequence similaritiesi

Contains 1 ATP-cone domain.

Phylogenomic databases

eggNOGiCOG0209.
HOGENOMiHOG000057035.
KOiK10807.
OMAiANGSIQH.
OrthoDBiEOG7C5MHR.
PhylomeDBiP36602.

Family and domain databases

InterProiIPR005144. ATP-cone.
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.

P36602-1 [UniParc]FASTAAdd to Basket

« Hide

MFVYKRDGRQ EKVAFDKITA RVSRLCYGLD SDHVDPVEIT QKVISGVYPG    50
VTTIELDNLA AETAATMTTK HPDYAILAAR IAVSNLHKQT EKVFSTVVQQ 100
LHDYVNPKTD KPAPMISDKI YDIVMKHKDE LDSAIIYDRD FTYNFFGFKT 150
LERSYLLRID GKVAERPQHM IMRVAVGIHG EDIEAAIETY NLMSQRYFTH 200
ASPTLFNAGT PRPQLSSCFL VTMKDDSIEG IYDTLKMCAM ISKTAGGIGI 250
NIHNIRATGS YIAGTNGTSN GIVPMIRVYN NTARYVDQGG NKRPGAFAAY 300
LEPWHADVMD FLELRKTHGN EDFRAREMFY ALWIPDLFMQ RVERNEQWTF 350
FCPNEAPGLA DVWGDEFVAL YEKYEKENRG RRSLPAQKVW YAILQSQVET 400
GNPFMLYKDS CNRKSNQKNV GTIRCSNLCT EIVEYSSPDE VAVCNLASVA 450
LPTFIKDGKY NFQKLHDVVK VVTRNLNKII DVNYYPVPEA RRSNMRHRPV 500
GLGVQGLADA FFALRLPFES AGAKKLNIQI FETIYHAALE ASCEIAQVEG 550
TYESYEGSPA SQGILQYDMW NVNPTDLWDW AELKEKIAKH GIRNSLLVAP 600
MPTASTSQIL GFNECFEPYT SNMYQRRVLS GEFQIVNPWL LKDLVERDLW 650
NEDMKNKLVM LDGSIQAIPE IPQDLKDLYK TVWEISQKTV IDYAADRGPF 700
IDQSQSLNIH LKDPSYGKIT SMHFYGWKKG LKTGMYYLRT MAASAAIKFT 750
VDPVALRARN EESNEENKKP VIKNGKAEIS AEPTKEEIDI YNEKVLACSI 800
KNPEACEMCS A 811
Length:811
Mass (Da):91,999
Last modified:February 1, 1996 - v2
Checksum:i6650E0EE4C2E8DF6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511N → Y in CAA46232. 1 Publication
Sequence conflicti327 – 3271E → Q in CAA46232. 1 Publication
Sequence conflicti425 – 4251C → S in CAA46232. 1 Publication
Sequence conflicti560 – 5612AS → CI in CAA46232. 1 Publication
Sequence conflicti583 – 5831L → F in CAA46232. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X65116 Genomic DNA. Translation: CAA46232.1.
CU329670 Genomic DNA. Translation: CAA91952.1.
PIRiS34807.
S62577.
RefSeqiNP_594491.1. NM_001019920.2.

Genome annotation databases

EnsemblFungiiSPAC1F7.05.1; SPAC1F7.05.1:pep; SPAC1F7.05.
GeneIDi2541695.
KEGGispo:SPAC1F7.05.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X65116 Genomic DNA. Translation: CAA46232.1 .
CU329670 Genomic DNA. Translation: CAA91952.1 .
PIRi S34807.
S62577.
RefSeqi NP_594491.1. NM_001019920.2.

3D structure databases

ProteinModelPortali P36602.
SMRi P36602. Positions 15-752.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 278191. 25 interactions.
IntActi P36602. 1 interaction.
MINTi MINT-4688885.
STRINGi 4896.SPAC1F7.05-1.

Proteomic databases

MaxQBi P36602.
PaxDbi P36602.
PRIDEi P36602.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC1F7.05.1 ; SPAC1F7.05.1:pep ; SPAC1F7.05 .
GeneIDi 2541695.
KEGGi spo:SPAC1F7.05.

Organism-specific databases

PomBasei SPAC1F7.05.

Phylogenomic databases

eggNOGi COG0209.
HOGENOMi HOG000057035.
KOi K10807.
OMAi ANGSIQH.
OrthoDBi EOG7C5MHR.
PhylomeDBi P36602.

Enzyme and pathway databases

UniPathwayi UPA00326 .

Miscellaneous databases

NextBioi 20802788.
PROi P36602.

Family and domain databases

InterProi IPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view ]
Pfami PF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view ]
PRINTSi PR01183. RIBORDTASEM1.
SUPFAMi SSF48168. SSF48168. 1 hit.
TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
PROSITEi PS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiRIR1_SCHPO
AccessioniPrimary (citable) accession number: P36602
Entry historyi
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 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi