Reviewed, UniProtKB/Swiss-Prot P21524 (RIR1_YEAST)

Names and origin

Protein names

Recommended name:
    Ribonucleoside-diphosphate reductase large chain 1
    EC=1.17.4.1
Alternative name(s):
    Ribonucleotide reductase large subunit 1
    Ribonucleotide reductase R1 subunit 1

Gene names

Name:	RNR1
Synonyms:	CRT7, RIR1, SDS12
Ordered Locus Names:	YER070W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	888 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. Ref.6
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 R1 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. Inhibited by SML1. Ref.4
Pathway	Genetic information processing; DNA replication.
Subunit structure	Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3. RNR1 interacts with the ribonucleotide reductase inhibitor SML1. Ref.4 Ref.5
Subcellular location	Cytoplasm Ref.8.
Induction	Cell cycle-regulated with highest activity in S phase. Moderately induced by DNA-damage. Ref.4 Ref.2
Miscellaneous	Two distinct regulatory sites have been defined: the specificity site, which controls substrate specificity, and the activity site which regulates overall catalytic activity. A substrate-binding catalytic site, located on R1, is formed only in the presence of the second subunit R2 By similarity. Present with 293000 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase large chain family. Contains 1 ATP-cone domain.
Biophysicochemical properties	Kinetic parameters: Vmax=2250 nmol/min/mg enzyme for cytidine 5'-diphosphate Temperature dependence: Optimum temperature is 30 degrees Celsius.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW deoxyribonucleotide biosynthetic process Inferred from direct assay. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ribonucleoside-diphosphate reductase complex Ref.5 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct ribonucleoside-diphosphate reductase activity Ref.5 Ref.6 Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACB1	P31787	1	EBI-15234,EBI-2060
ADE16	P54113	1	EBI-15234,EBI-14213
ADE4	P04046	1	EBI-15234,EBI-14238
ALO1	P54783	1	EBI-15234,EBI-2519
APC9	Q12107	1	EBI-15234,EBI-36475
ARC35	P53731	1	EBI-15234,EBI-2770
ARP2	P32381	1	EBI-15234,EBI-2927
BBC1	P47068	1	EBI-15234,EBI-3437
BCY1	P07278	1	EBI-15234,EBI-9475
CAF20	P12962	1	EBI-15234,EBI-9010
CAP2	P13517	1	EBI-15234,EBI-4013
CCS1	P40202	1	EBI-15234,EBI-10287
CMK2	P22517	1	EBI-15234,EBI-9600
CPR6	P53691	1	EBI-15234,EBI-5429
CTT1	P06115	1	EBI-15234,EBI-4065
CUE5	Q08412	1	EBI-15234,EBI-37580
CWH41	P53008	1	EBI-15234,EBI-5323
DBP5	P20449	1	EBI-15234,EBI-5617
DNM1	P54861	1	EBI-15234,EBI-6002
DYS1	P38791	1	EBI-15234,EBI-5871
EFT1	P32324	1	EBI-15234,EBI-6333
ERG13	P54839	1	EBI-15234,EBI-8373
FAT2	P38137	1	EBI-15234,EBI-6831
GAD1	Q04792	1	EBI-15234,EBI-5668
GCD7	P32502	1	EBI-15234,EBI-6260
GCN1	P33892	1	EBI-15234,EBI-7442
GDH2	P33327	1	EBI-15234,EBI-5815
GET3	Q12154	1	EBI-15234,EBI-2989
GLO2	Q05584	1	EBI-15234,EBI-7672
GPD2	P41911	1	EBI-15234,EBI-7791
GPM2	Q12008	1	EBI-15234,EBI-2063839
HCH1	P53834	1	EBI-15234,EBI-28288
HUG1	Q6Q5K6	1	EBI-15234,EBI-392766
IDI1	P15496	1	EBI-15234,EBI-8902
INO1	P11986	1	EBI-15234,EBI-9257
KRE1	P17260	1	EBI-15234,EBI-2068892
LSP1	Q12230	1	EBI-15234,EBI-34978
MET3	P08536	1	EBI-15234,EBI-10753
MLS1	P30952	1	EBI-15234,EBI-10428
MPG1	P41940	1	EBI-15234,EBI-11191
NAP1	P25293	1	EBI-15234,EBI-11850
NOT1	P25655	1	EBI-15234,EBI-12139
PDC6	P26263	1	EBI-15234,EBI-5700
PEX11	Q12462	1	EBI-15234,EBI-13198
PGM2	P37012	1	EBI-15234,EBI-13296
PRO1	P32264	1	EBI-15234,EBI-13879
RAS1	P01119	1	EBI-15234,EBI-14830
RAS2	P01120	1	EBI-15234,EBI-14838
RFA2	P26754	1	EBI-15234,EBI-14976
RIB1	P38066	1	EBI-15234,EBI-7436
RIB5	P38145	1	EBI-15234,EBI-2083267
RTN2	Q12443	1	EBI-15234,EBI-32591
SCL1	P21243	1	EBI-15234,EBI-13975
SDH4	P37298	1	EBI-15234,EBI-16796
SIS1	P25294	1	EBI-15234,EBI-17244
SLA2	P33338	1	EBI-15234,EBI-17323
SML1	Q04964	1	EBI-15234,EBI-27834
SNC2	P33328	1	EBI-15234,EBI-17512
SNO1	Q03144	1	EBI-15234,EBI-28190
SRV2	P17555	1	EBI-15234,EBI-4024
SSD1	P24276	1	EBI-15234,EBI-18153
SSE2	P32590	1	EBI-15234,EBI-8655
SSM4	P40318	1	EBI-15234,EBI-18208
STI1	P15705	1	EBI-15234,EBI-18418
SYP1	P25623	1	EBI-15234,EBI-21900
TAL1	P15019	1	EBI-15234,EBI-18952
TPD3	P31383	1	EBI-15234,EBI-1936
TRP2	P00899	1	EBI-15234,EBI-19575
TRP4	P07285	1	EBI-15234,EBI-2096870
URA7	P28274	1	EBI-15234,EBI-20128
VMA13	P41807	1	EBI-15234,EBI-20281
VMA7	P39111	1	EBI-15234,EBI-20272
VPS21	P36017	1	EBI-15234,EBI-29399
WRS1	Q12109	1	EBI-15234,EBI-18832
YNK1	P36010	1	EBI-15234,EBI-11968
YPR1	Q12458	1	EBI-15234,EBI-29490
YPT1	P01123	1	EBI-15234,EBI-29496
YPT7	P32939	1	EBI-15234,EBI-29509

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 888

888

Ribonucleoside-diphosphate reductase large chain 1

PRO_0000187203

Regions

Domain

1 – 92

92

ATP-cone

Region

11 – 17

7

Allosteric activator binding By similarity

Region

217 – 218

2

Substrate binding

Region

285 – 288

4

Allosteric effector binding, determines substrate specificity

Region

426 – 430

5

Substrate binding

Region

607 – 611

5

Substrate binding

Sites

Active site

426

1

Proton acceptor

Active site

428

1

Cysteine radical intermediate

Active site

430

1

Proton acceptor

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

Binding site

247

1

Substrate; via amide nitrogen

Site

218

1

Important for hydrogen atom transfer By similarity

Site

226

1

Allosteric effector binding, determines substrate specificity

Site

256

1

Allosteric effector binding, determines substrate specificity

Site

443

1

Important for hydrogen atom transfer By similarity

Site

741

1

Important for electron transfer By similarity

Site

742

1

Important for electron transfer By similarity

Site

883

1

Interacts with thioredoxin/glutaredoxin By similarity

Site

886

1

Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Modified residue

227

1

Phosphoserine Ref.11

Modified residue

809

1

Phosphoserine Ref.11

Modified residue

812

1

Phosphoserine Ref.11

Modified residue

816

1

Phosphoserine Ref.11 Ref.9 Ref.10

Modified residue

837

1

Phosphoserine Ref.11

Modified residue

887

1

Phosphoserine Ref.11

Disulfide bond

218 ↔ 443

Redox-active

Experimental info

Mutagenesis

428

1

C → A: Completely abolishes reductase activity. Ref.6

Sequence conflict

329

1

F → L in CAA49151. Ref.3

Sequence conflict

587 – 589

3

TLR → NLK Ref.3

Sequence conflict

666

1

Q → E Ref.2

Sequence conflict

679

1

E → Q Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

888

Helix Strand Turn

Details...

Helix

19 – 23

5

Turn

31 – 33

3

Helix

36 – 41

6

Helix

53 – 66

14

Turn

67 – 70

4

Helix

79 – 89

11

Helix

94 – 103

10

Turn

107 – 109

3

Helix

118 – 126

9

Helix

128 – 134

7

Helix

137 – 142

6

Helix

145 – 154

10

Helix

167 – 179

13

Helix

183 – 194

12

Beta strand

197 – 200

4

Helix

202 – 207

6

Beta strand

210 – 212

3

Beta strand

218 – 222

5

Helix

228 – 242

15

Beta strand

247 – 251

5

Beta strand

263 – 266

4

Helix

272 – 285

14

Beta strand

287 – 290

4

Beta strand

297 – 301

5

Helix

308 – 311

4

Turn

312 – 315

4

Beta strand

328 – 334

7

Helix

336 – 343

8

Beta strand

347 – 351

5

Turn

353 – 355

3

Helix

359 – 361

3

Helix

364 – 376

13

Beta strand

380 – 384

5

Helix

385 – 399

15

Beta strand

402 – 406

5

Helix

407 – 412

6

Turn

415 – 418

4

Beta strand

441 – 443

3

Beta strand

445 – 449

5

Helix

450 – 453

4

Beta strand

458 – 461

4

Helix

467 – 487

21

Helix

493 – 502

10

Beta strand

506 – 510

5

Helix

512 – 518

7

Helix

526 – 554

29

Turn

564 – 568

5

Helix

572 – 575

4

Helix

585 – 595

11

Helix

611 – 615

5

Helix

643 – 651

9

Helix

658 – 665

8

Helix

678 – 683

6

Helix

687 – 689

3

Helix

692 – 702

11

Helix

703 – 705

3

Beta strand

714 – 718

5

Helix

721 – 733

13

Beta strand

737 – 741

5

Beta strand

743 – 745

3

Turn

748 – 751

4

Helix

760 – 763

4

Helix

764 – 766

3

Turn

789 – 791

3

Sequences

	Sequence		Length	Mass (Da)
	P21524-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 56BE1B077916E419	FASTA	888	99,561
	10 20 30 40 50 60 MYVYKRDGRK EPVQFDKITA RISRLCYGLD PKHIDAVKVT QRIISGVYEG VTTIELDNLA 70 80 90 100 110 120 AETCAYMTTV HPDYATLAAR IAISNLHKQT TKQFSKVVED LYRYVNAATG KPAPMISDDV 130 140 150 160 170 180 YNIVMENKDK LNSAIVYDRD FQYSYFGFKT LERSYLLRIN GQVAERPQHL IMRVALGIHG 190 200 210 220 230 240 RDIEAALETY NLMSLKYFTH ASPTLFNAGT PKPQMSSCFL VAMKEDSIEG IYDTLKECAL 250 260 270 280 290 300 ISKTAGGIGL HIHNIRSTGS YIAGTNGTSN GLIPMIRVFN NTARYVDQGG NKRPGAFALY 310 320 330 340 350 360 LEPWHADIFD FIDIRKNHGK EEIRARDLFP ALWIPDLFMK RVEENGTWTL FSPTSAPGLS 370 380 390 400 410 420 DCYGDEFEAL YTRYEKEGRG KTIKAQKLWY SILEAQTETG TPFVVYKDAC NRKSNQKNLG 430 440 450 460 470 480 VIKSSNLCCE IVEYSAPDET AVCNLASVAL PAFIETSEDG KTSTYNFKKL HEIAKVVTRN 490 500 510 520 530 540 LNRVIDRNYY PVEEARKSNM RHRPIALGVQ GLADTFMLLR LPFDSEEARL LNIQIFETIY 550 560 570 580 590 600 HASMEASCEL AQKDGPYETF QGSPASQGIL QFDMWDQKPY GMWDWDTLRK DIMKHGVRNS 610 620 630 640 650 660 LTMAPMPTAS TSQILGYNEC FEPVTSNMYS RRVLSGEFQV VNPYLLRDLV DLGIWDEGMK 670 680 690 700 710 720 QYLITQNGSI QGLPNVPQEL KDLYKTVWEI SQKTIINMAA DRSVYIDQSH SLNLFLRAPT 730 740 750 760 770 780 MGKLTSMHFY GWKKGLKTGM YYLRTQAASA AIQFTIDQKI ADQATENVAD ISNLKRPSYM 790 800 810 820 830 840 PSSASYAASD FVPAAVTANA TIPSLDSSSE ASREASPAPT GSHSLTKGMA ELNVQESKVE 850 860 870 880 VPEVPAPTKN EEKAAPIVDD EETEFDIYNS KVIACAIDNP EACEMCSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Two genes differentially regulated in the cell cycle and by DNA-damaging agents encode alternative regulatory subunits of ribonucleotide reductase." Elledge S.J., Davis R.W. Genes Dev. 4:740-751(1990) [PubMed: 2199320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100 AND 653-682, INDUCTION.
[3]	"Use of synthetic lethal mutants to clone and characterize a novel CTP synthetase gene in Saccharomyces cerevisiae." Ozier-Kalogeropoulos O., Adeline M.-T., Yang W.-L., Carman G.M., Lacroute F. Mol. Gen. Genet. 242:431-439(1994) [PubMed: 8121398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-384 AND 546-590.
[4]	"Yeast Sml1, a protein inhibitor of ribonucleotide reductase." Chabes A., Domkin V., Thelander L. J. Biol. Chem. 274:36679-36683(1999) [PubMed: 10593972] [Abstract] Cited for: INTERACTION WITH SML1, ENZYME REGULATION.
[5]	"Yeast ribonucleotide reductase has a heterodimeric iron-radical-containing subunit." Chabes A., Domkin V., Larsson G., Liu A., Graeslund A., Wijmenga S., Thelander L. Proc. Natl. Acad. Sci. U.S.A. 97:2474-2479(2000) [PubMed: 10716984] [Abstract] Cited for: SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[6]	"Yeast DNA damage-inducible Rnr3 has a very low catalytic activity strongly stimulated after the formation of a cross-talking Rnr1/Rnr3 complex." Domkin V., Thelander L., Chabes A. J. Biol. Chem. 277:18574-18578(2002) [PubMed: 11893751] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-428.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways." Yao R., Zhang Z., An X., Bucci B., Perlstein D.L., Stubbe J., Huang M. Proc. Natl. Acad. Sci. U.S.A. 100:6628-6633(2003) [PubMed: 12732713] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816, MASS SPECTROMETRY.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816, MASS SPECTROMETRY.
[11]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-809; SER-812; SER-816; SER-837 AND SER-887, MASS SPECTROMETRY.
[12]	"Structures of eukaryotic ribonucleotide reductase I provide insights into dNTP regulation." Xu H., Faber C., Uchiki T., Fairman J.W., Racca J., Dealwis C. Proc. Natl. Acad. Sci. U.S.A. 103:4022-4027(2006) [PubMed: 16537479] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH CDP; UDP; TTP; GDP; GTP; ADP AND AMPPNP, DISULFIDE BOND.
[13]	"Structures of eukaryotic ribonucleotide reductase I define gemcitabine diphosphate binding and subunit assembly." Xu H., Faber C., Uchiki T., Racca J., Dealwis C. Proc. Natl. Acad. Sci. U.S.A. 103:4028-4033(2006) [PubMed: 16537480] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH GEMCITABINE DIPHOSPHATE AND R2 PEPTIDES, SUBUNIT.
[14]	"The structural basis for peptidomimetic inhibition of eukaryotic ribonucleotide reductase: a conformationally flexible pharmacophore." Xu H., Fairman J.W., Wijerathna S.R., Kreischer N.R., LaMacchia J., Helmbrecht E., Cooperman B.S., Dealwis C. J. Med. Chem. 51:4653-4659(2008) [PubMed: 18610997] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) IN COMPLEX WITH PEPTIDE INHIBITORS, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U18813 Genomic DNA. Translation: AAB64606.1.
X69216 Genomic DNA. Translation: CAA49150.1.
X69217 Genomic DNA. Translation: CAA49151.1.

PIR

S50573.

RefSeq

NP_010993.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZYZ	X-ray	2.90	A/B	1-888	[»]
1ZZD	X-ray	2.60	A	1-888	[»]
2CVS	X-ray	2.60	A	1-888	[»]
2CVT	X-ray	3.20	A	1-888	[»]
2CVU	X-ray	2.90	A	1-888	[»]
2CVV	X-ray	2.90	A	1-888	[»]
2CVW	X-ray	2.40	A	1-888	[»]
2CVX	X-ray	2.20	A	1-888	[»]
2CVY	X-ray	2.40	A	1-888	[»]
2EUD	X-ray	2.30	A	1-888	[»]
2ZLF	X-ray	2.59	A	1-888	[»]
2ZLG	X-ray	2.52	A	1-888	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6299N.

IntAct

P21524. 110 interactions.

STRING

P21524.

Proteomic databases

PeptideAtlas

P21524.

PRIDE

P21524.

Genome annotation databases

Ensembl

YER070W; YER070W; YER070W; Saccharomyces cerevisiae. [Genome view]

GeneID

856801.

KEGG

sce:YER070W.

NMPDR

fig|4932.3.peg.2059.

Organism-specific databases

CYGD

YER070w.

SGD

S000000872. RNR1.

Phylogenomic databases

eggNOG

fuNOG04736.

HOGENOM

HBG296647.

OMA

VERPQQM.

OrthoDB

EOG9JDJQ2.

PhylomeDB

P21524.

Enzyme and pathway databases

BRENDA

1.17.4.1. 250.

Gene expression databases

ArrayExpress

P21524.

Genevestigator

P21524.

GermOnline

YER070W. Saccharomyces cerevisiae.

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...

Other Resources

NextBio

983047.

Entry information

Entry name

RIR1_YEAST

Accession

Primary (citable) accession number: P21524

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	February 1, 1995
Last modified:	February 9, 2010
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)