Q9UW15 (RIR1_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase large chain
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase large subunit

Gene names

Name:	rnr-1
ORF Names:	B2A19.30, NCU03539

Organism

Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]

Taxonomic identifier

367110 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora › Neurospora crassa

Protein attributes

Sequence length	929 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.1
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. Ref.1
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.
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 Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway deoxyribonucleotide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 929	929	Ribonucleoside-diphosphate reductase large chain		PRO_0000187202
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	604 – 608	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	738	1	Important for electron transfer By similarity
	Site	739	1	Important for electron transfer By similarity
	Site	924	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	927	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	218 ↔ 444		Redox-active By similarity
Experimental info
	Mutagenesis	26	1	C → Y in un-24; temperature-sensitive mutant. Ref.1
	Mutagenesis	124	1	V → I in un-24; temperature-sensitive mutant. Ref.1
	Mutagenesis	125	1	M → I in un-24; temperature-sensitive mutant. Ref.1
	Sequence conflict	912	1	A → R in AAD49743. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UW15 [UniParc]. Last modified April 30, 2003. Version 2. Checksum: 68C47E8B21C047B8	FASTA	929	103,804
	10 20 30 40 50 60 MYVKKRDGRQ ERVQFDKITA RVSRLCYGLD MNHVDPVAIT QKVISGVYGG VTTAQLDDLA 70 80 90 100 110 120 AETAAYMTVT HPDYAILAAR IAVSNLHKQT KKQWSLVISE LYNYVNPRTG KHSPMIAKDV 130 140 150 160 170 180 YECVMRHKDE FDSAIVYDRD FNYQYFGFKT LERSYLLKLD GQIAERPQHM IMRVAVGIWG 190 200 210 220 230 240 DDVERVIETY NLMSLKTFTH ASPTLFNAGT PQPQLSSCFL VDMKEDSIEG IYDTLKTCAM 250 260 270 280 290 300 ISKMAGGIGL NIHRIRATGS YIAGTNGTSN GIVPMLRVFN NTARYVDQGG NKRPGAFAIY 310 320 330 340 350 360 LEPWHADVFE FLDLRKNHGK EEVRARDLFL ALWIPDLFMK RVEQNGQWTL MCPHECPGLA 370 380 390 400 410 420 DVYGDEFEAL YEKYEKEGKG RKTVKAQKLW YAILEAQTET GNPFMLYKDA CNRKSNQKNL 430 440 450 460 470 480 GTIRSSNLCT EIIEYSAPDE VAVCNLASLA LSAFIDYENA SYDFKKLHEV TQVVVRNLNK 490 500 510 520 530 540 IIDINHYPVK EAHNSNMRHR PIGVGVQGLA DAFLALRMPF DSDAASKLNI QIFETIYHAA 550 560 570 580 590 600 LTASCQLAKE QGPYATYEGS PVSQGILQYD MWNVTPTNLW DWTALKADIK KYGVRNSLLL 610 620 630 640 650 660 APMPTASTSQ ILGNNECFEP YTSNIYQRRV LAGEFQVVNP WLLRDLVEMG LWSDAMKNRI 670 680 690 700 710 720 IAEGGSIQNI QSIPNDIKAL YKTVWEISQR TIVKMAADRG AFIDQSQSLN IHMREPTMGK 730 740 750 760 770 780 ITSMHFAGWK MGLKTGMYYL RTQAAAQPIQ FTVDQEALRA TDDRVAPAHS GLKKRSPPAG 790 800 810 820 830 840 TYTSIVLREN TSGPRPYAQT GVSGTSTPIG TRDVPTPAST PPPTEVPETL VQSDNRPRPL 850 860 870 880 890 900 VSPAKSAGFK ADLPEPESPK ALATDPIVKT EDIGSPLLER KEGQNEDVDE DSQERDENIY 910 920 SNAPLSEQQV AACAWNPGAD PSSCEMCSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An osmotic-remedial, temperature-sensitive mutation in the allosteric activity site of ribonucleotide reductase in Neurospora crassa." Smith M.L., Hubbard S.P., Jacobson D.J., Micali O.C., Glass N.L. Mol. Gen. Genet. 262:1022-1035(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME ACTIVITY, MUTAGENESIS OF CYS-26; VAL-124 AND MET-125. Strain: Oak Ridge.
[2]	"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence." Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U. Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]	"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF171697 Genomic DNA. Translation: AAD49743.1. AL390092 Genomic DNA. Translation: CAB98233.1. AABX02000008 Genomic DNA. Translation: EAA27582.1.
PIR	T43711.
RefSeq	XP_956818.1. XM_951725.2.
UniGene	Ncr.20426.
3D structure databases
ProteinModelPortal	Q9UW15.
SMR	Q9UW15. Positions 15-769.
ModBase	Search...
Protein-protein interaction databases
STRING	5141.NCU03539.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	EFNCRT00000002608; EFNCRP00000002608; EFNCRG00000002605.
GeneID	3872956.
KEGG	ncr:NCU03539.
Phylogenomic databases
eggNOG	COG0209.
HOGENOM	HOG000057035.
KO	K10807.
OMA	ETIYHAS.
OrthoDB	EOG480N4T.
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
InterPro	IPR005144. ATP-cone. IPR013346. NrdE_NrdA. IPR000788. RNR_lg_C. IPR013509. RNR_lsu_N. IPR008926. RNR_R1-su_N. [Graphical view]
Pfam	PF03477. ATP-cone. 1 hit. PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
SUPFAM	SSF48168. Ribonucleo_red_N. 1 hit.
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_NEUCR

Accession

Primary (citable) accession number: Q9UW15
Secondary accession number(s): Q7RXZ9, Q9P3G2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	April 30, 2003
Last modified:	April 3, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program