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Q9UW15 (RIR1_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length929 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 929929Ribonucleoside-diphosphate reductase large chain
PRO_0000187202

Regions

Domain1 – 9292ATP-cone
Region11 – 177Allosteric activator binding By similarity
Region217 – 2182Substrate binding By similarity
Region285 – 2884Allosteric effector binding, determines substrate specificity By similarity
Region427 – 4315Substrate binding By similarity
Region604 – 6085Substrate binding By similarity

Sites

Active site4271Proton acceptor By similarity
Active site4291Cysteine radical intermediate By similarity
Active site4311Proton acceptor By similarity
Binding site51Allosteric activator By similarity
Binding site531Allosteric activator By similarity
Binding site881Allosteric activator By similarity
Binding site2021Substrate By similarity
Binding site2471Substrate; via amide nitrogen By similarity
Site2181Important for hydrogen atom transfer By similarity
Site2261Allosteric effector binding, determines substrate specificity By similarity
Site2561Allosteric effector binding, determines substrate specificity By similarity
Site4441Important for hydrogen atom transfer By similarity
Site7381Important for electron transfer By similarity
Site7391Important for electron transfer By similarity
Site9241Interacts with thioredoxin/glutaredoxin By similarity
Site9271Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond218 ↔ 444Redox-active By similarity

Experimental info

Mutagenesis261C → Y in un-24; temperature-sensitive mutant. Ref.1
Mutagenesis1241V → I in un-24; temperature-sensitive mutant. Ref.1
Mutagenesis1251M → I in un-24; temperature-sensitive mutant. Ref.1
Sequence conflict9121A → R in AAD49743. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9UW15 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: 68C47E8B21C047B8

FASTA929103,804
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
CM002237 Genomic DNA. Translation: EAA27582.1.
PIRT43711.
RefSeqXP_956818.1. XM_951725.2.
UniGeneNcr.20426.

3D structure databases

ProteinModelPortalQ9UW15.
SMRQ9UW15. Positions 15-769.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1974838. 3 interactions.
STRING5141.NCU03539.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000002608; EFNCRP00000002608; EFNCRG00000002605.
GeneID3872956.
KEGGncr:NCU03539.

Phylogenomic databases

eggNOGCOG0209.
HOGENOMHOG000057035.
KOK10807.
OMANKVSMKQ.
OrthoDBEOG7C5MHR.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF48168. SSF48168. 1 hit.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
PROSITEPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_NEUCR
AccessionPrimary (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: May 14, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways