Reviewed, UniProtKB/Swiss-Prot P36602 (RIR1_SCHPO)

Names and origin

Protein names

Recommended name:
    Ribonucleoside-diphosphate reductase large chain
    EC=1.17.4.1
Alternative name(s):
    Ribonucleotide reductase

Gene names

Name:	cdc22
ORF Names:	SPAC1F7.05

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	811 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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.

Ontologies

Keywords
Biological process	DNA replication
Ligand	ATP-binding Nucleotide-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW S phase of mitotic cell cycle Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW purine deoxyribonucleoside triphosphate biosynthetic process Inferred by curator. Source: GeneDB_SPombe purine nucleoside metabolic process Inferred by curator. Source: GeneDB_SPombe pyrimidine deoxyribonucleoside triphosphate biosynthetic process Inferred by curator. Source: GeneDB_SPombe regulation of DNA replication Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe ribonucleoside-diphosphate reductase complex Ref.1 Traceable author statement. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct ribonucleoside-diphosphate reductase activity Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
spd1	Q10585	1	EBI-969154,EBI-969142

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 811	811	Ribonucleoside-diphosphate reductase large chain		PRO_0000187201
Regions
	Domain	1 – 92	92	ATP-cone
	Region	11 – 17	7	Allosteric activator binding By similarity
	Region	217 – 218	2	Substrate binding By similarity
	Region	285 – 288	4	Allosteric effector binding, determines substrate specificity By similarity
	Region	427 – 431	5	Substrate binding By similarity
	Region	602 – 606	5	Substrate binding By similarity
Sites
	Active site	427	1	Proton acceptor By similarity
	Active site	429	1	Cysteine radical intermediate By similarity
	Active site	431	1	Proton acceptor By similarity
	Binding site	5	1	Allosteric activator By similarity
	Binding site	53	1	Allosteric activator By similarity
	Binding site	88	1	Allosteric activator By similarity
	Binding site	202	1	Substrate By similarity
	Binding site	247	1	Substrate; via amide nitrogen By similarity
	Site	218	1	Important for hydrogen atom transfer By similarity
	Site	226	1	Allosteric effector binding, determines substrate specificity By similarity
	Site	256	1	Allosteric effector binding, determines substrate specificity By similarity
	Site	444	1	Important for hydrogen atom transfer By similarity
	Site	736	1	Important for electron transfer By similarity
	Site	737	1	Important for electron transfer By similarity
	Site	806	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	809	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	218 ↔ 444		Redox-active By similarity
Experimental info
	Sequence conflict	251	1	N → Y in CAA46232. Ref.1
	Sequence conflict	327	1	E → Q in CAA46232. Ref.1
	Sequence conflict	425	1	C → S in CAA46232. Ref.1
	Sequence conflict	560 – 561	2	AS → CI in CAA46232. Ref.1
	Sequence conflict	583	1	L → F in CAA46232. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P36602-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 6650E0EE4C2E8DF6	FASTA	811	91,999
	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

References

	« Hide 'large scale' referencesShow '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: 8479429] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38366 / 972.
[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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X65116 Genomic DNA. Translation: CAA46232.1. CU329670 Genomic DNA. Translation: CAA91952.1.
PIR	S34807. S62577.
RefSeq	NP_594491.1.
3D structure databases
SMR	P36602. Positions 15-752.
ModBase	Search...
Protein-protein interaction databases
IntAct	P36602. 1 interaction.
STRING	P36602.
Genome annotation databases
GeneID	2541695.
GenomeReviews	Gene locus cdc22 in contig CU329670_GR.
KEGG	spo:SPAC1F7.05.
NMPDR	fig|4896.1.peg.4461.
Organism-specific databases
GeneDB_Spombe	SPAC1F7.05.
Phylogenomic databases
eggNOG	fuNOG04736.
HOGENOM	HBG296647.
OMA	GSLWSKG.
OrthoDB	EOG9JDJQ2.
PhylomeDB	P36602.
Enzyme and pathway databases
BRENDA	1.17.4.1. 653.
Gene expression databases
ArrayExpress	P36602.
Family and domain databases
InterPro	IPR005144. ATP-cone. IPR013346. NrdE_NrdA. IPR013509. Ribncl_Rdtase_lsu_N. IPR000788. Ribncl_red_lg_C. IPR008926. Ribnucl_Rdtase_R1-su_N. [Graphical view]
PANTHER	PTHR11573. Ribncl_red_lg_C. 1 hit.
Pfam	PF03477. ATP-cone. 1 hit. PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
TIGRFAMs	TIGR02506. NrdE_NrdA. 1 hit.
PROSITE	PS51161. ATP_CONE. 1 hit. PS00089. RIBORED_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR1_SCHPO

Accession

Primary (citable) accession number: P36602

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	February 1, 1996
Last modified:	February 9, 2010
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)