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P36602

- RIR1_SCHPO

UniProt

P36602 - RIR1_SCHPO

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Protein

Ribonucleoside-diphosphate reductase large chain

Gene

cdc22

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).By similarity

Pathwayi

Sites

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. nucleoside diphosphate kinase activity Source: PomBase
  3. 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 nuclear cell cycle 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
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-activeBy 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292ATP-conePROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Contains 1 ATP-cone domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0209.
HOGENOMiHOG000057035.
InParanoidiP36602.
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

        10         20         30         40         50
MFVYKRDGRQ EKVAFDKITA RVSRLCYGLD SDHVDPVEIT QKVISGVYPG
60 70 80 90 100
VTTIELDNLA AETAATMTTK HPDYAILAAR IAVSNLHKQT EKVFSTVVQQ
110 120 130 140 150
LHDYVNPKTD KPAPMISDKI YDIVMKHKDE LDSAIIYDRD FTYNFFGFKT
160 170 180 190 200
LERSYLLRID GKVAERPQHM IMRVAVGIHG EDIEAAIETY NLMSQRYFTH
210 220 230 240 250
ASPTLFNAGT PRPQLSSCFL VTMKDDSIEG IYDTLKMCAM ISKTAGGIGI
260 270 280 290 300
NIHNIRATGS YIAGTNGTSN GIVPMIRVYN NTARYVDQGG NKRPGAFAAY
310 320 330 340 350
LEPWHADVMD FLELRKTHGN EDFRAREMFY ALWIPDLFMQ RVERNEQWTF
360 370 380 390 400
FCPNEAPGLA DVWGDEFVAL YEKYEKENRG RRSLPAQKVW YAILQSQVET
410 420 430 440 450
GNPFMLYKDS CNRKSNQKNV GTIRCSNLCT EIVEYSSPDE VAVCNLASVA
460 470 480 490 500
LPTFIKDGKY NFQKLHDVVK VVTRNLNKII DVNYYPVPEA RRSNMRHRPV
510 520 530 540 550
GLGVQGLADA FFALRLPFES AGAKKLNIQI FETIYHAALE ASCEIAQVEG
560 570 580 590 600
TYESYEGSPA SQGILQYDMW NVNPTDLWDW AELKEKIAKH GIRNSLLVAP
610 620 630 640 650
MPTASTSQIL GFNECFEPYT SNMYQRRVLS GEFQIVNPWL LKDLVERDLW
660 670 680 690 700
NEDMKNKLVM LDGSIQAIPE IPQDLKDLYK TVWEISQKTV IDYAADRGPF
710 720 730 740 750
IDQSQSLNIH LKDPSYGKIT SMHFYGWKKG LKTGMYYLRT MAASAAIKFT
760 770 780 790 800
VDPVALRARN EESNEENKKP VIKNGKAEIS AEPTKEEIDI YNEKVLACSI
810
KNPEACEMCS A
Length:811
Mass (Da):91,999
Last modified:February 1, 1996 - v2
Checksum:i6650E0EE4C2E8DF6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511N → Y in CAA46232. (PubMed:8479429)Curated
Sequence conflicti327 – 3271E → Q in CAA46232. (PubMed:8479429)Curated
Sequence conflicti425 – 4251C → S in CAA46232. (PubMed:8479429)Curated
Sequence conflicti560 – 5612AS → CI in CAA46232. (PubMed:8479429)Curated
Sequence conflicti583 – 5831L → F in CAA46232. (PubMed:8479429)Curated

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.
InParanoidi P36602.
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: October 29, 2014
This is version 129 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