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Q9UW15

- RIR1_NEUCR

UniProt

Q9UW15 - RIR1_NEUCR

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Protein

Ribonucleoside-diphosphate reductase large chain

Gene
rnr-1, B2A19.30, NCU03539
Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 4 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.1 Publication

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei5 – 51Allosteric activator By similarity
Binding sitei53 – 531Allosteric activator By similarity
Binding sitei88 – 881Allosteric activator By similarity
Binding sitei202 – 2021Substrate By similarity
Sitei218 – 2181Important for hydrogen atom transfer By similarity
Sitei226 – 2261Allosteric effector binding, determines substrate specificity By similarity
Binding sitei247 – 2471Substrate; via amide nitrogen By similarity
Sitei256 – 2561Allosteric effector binding, determines substrate specificity By similarity
Active sitei427 – 4271Proton acceptor By similarity
Active sitei429 – 4291Cysteine radical intermediate By similarity
Active sitei431 – 4311Proton acceptor By similarity
Sitei444 – 4441Important for hydrogen atom transfer By similarity
Sitei738 – 7381Important for electron transfer By similarity
Sitei739 – 7391Important for electron transfer By similarity
Sitei924 – 9241Interacts with thioredoxin/glutaredoxin By similarity
Sitei927 – 9271Interacts with thioredoxin/glutaredoxin By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. 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
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 large subunit
Gene namesi
Name:rnr-1
ORF Names:B2A19.30, NCU03539
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 6, Linkage Group II

Subcellular locationi

GO - Cellular componenti

  1. ribonucleoside-diphosphate reductase complex Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi26 – 261C → Y in un-24; temperature-sensitive mutant. 1 Publication
Mutagenesisi124 – 1241V → I in un-24; temperature-sensitive mutant. 1 Publication
Mutagenesisi125 – 1251M → I in un-24; temperature-sensitive mutant. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 929929Ribonucleoside-diphosphate reductase large chainPRO_0000187202Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi218 ↔ 444Redox-active By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

BioGridi1974838. 3 interactions.
STRINGi5141.NCU03539.1.

Structurei

3D structure databases

ProteinModelPortaliQ9UW15.
SMRiQ9UW15. Positions 15-769.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292ATP-coneAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 177Allosteric activator binding By similarity
Regioni217 – 2182Substrate binding By similarity
Regioni285 – 2884Allosteric effector binding, determines substrate specificity By similarity
Regioni427 – 4315Substrate binding By similarity
Regioni604 – 6085Substrate binding By similarity

Sequence similaritiesi

Contains 1 ATP-cone domain.

Phylogenomic databases

eggNOGiCOG0209.
HOGENOMiHOG000057035.
KOiK10807.
OMAiNKVSMKQ.
OrthoDBiEOG7C5MHR.

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.

Q9UW15-1 [UniParc]FASTAAdd to Basket

« Hide

MYVKKRDGRQ ERVQFDKITA RVSRLCYGLD MNHVDPVAIT QKVISGVYGG    50
VTTAQLDDLA AETAAYMTVT HPDYAILAAR IAVSNLHKQT KKQWSLVISE 100
LYNYVNPRTG KHSPMIAKDV YECVMRHKDE FDSAIVYDRD FNYQYFGFKT 150
LERSYLLKLD GQIAERPQHM IMRVAVGIWG DDVERVIETY NLMSLKTFTH 200
ASPTLFNAGT PQPQLSSCFL VDMKEDSIEG IYDTLKTCAM ISKMAGGIGL 250
NIHRIRATGS YIAGTNGTSN GIVPMLRVFN NTARYVDQGG NKRPGAFAIY 300
LEPWHADVFE FLDLRKNHGK EEVRARDLFL ALWIPDLFMK RVEQNGQWTL 350
MCPHECPGLA DVYGDEFEAL YEKYEKEGKG RKTVKAQKLW YAILEAQTET 400
GNPFMLYKDA CNRKSNQKNL GTIRSSNLCT EIIEYSAPDE VAVCNLASLA 450
LSAFIDYENA SYDFKKLHEV TQVVVRNLNK IIDINHYPVK EAHNSNMRHR 500
PIGVGVQGLA DAFLALRMPF DSDAASKLNI QIFETIYHAA LTASCQLAKE 550
QGPYATYEGS PVSQGILQYD MWNVTPTNLW DWTALKADIK KYGVRNSLLL 600
APMPTASTSQ ILGNNECFEP YTSNIYQRRV LAGEFQVVNP WLLRDLVEMG 650
LWSDAMKNRI IAEGGSIQNI QSIPNDIKAL YKTVWEISQR TIVKMAADRG 700
AFIDQSQSLN IHMREPTMGK ITSMHFAGWK MGLKTGMYYL RTQAAAQPIQ 750
FTVDQEALRA TDDRVAPAHS GLKKRSPPAG TYTSIVLREN TSGPRPYAQT 800
GVSGTSTPIG TRDVPTPAST PPPTEVPETL VQSDNRPRPL VSPAKSAGFK 850
ADLPEPESPK ALATDPIVKT EDIGSPLLER KEGQNEDVDE DSQERDENIY 900
SNAPLSEQQV AACAWNPGAD PSSCEMCSG 929
Length:929
Mass (Da):103,804
Last modified:April 30, 2003 - v2
Checksum:i68C47E8B21C047B8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti912 – 9121A → R in AAD49743. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF171697 Genomic DNA. Translation: AAD49743.1.
AL390092 Genomic DNA. Translation: CAB98233.1.
CM002237 Genomic DNA. Translation: EAA27582.1.
PIRiT43711.
RefSeqiXP_956818.1. XM_951725.2.
UniGeneiNcr.20426.

Genome annotation databases

EnsemblFungiiEFNCRT00000002608; EFNCRP00000002608; EFNCRG00000002605.
GeneIDi3872956.
KEGGincr:NCU03539.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF171697 Genomic DNA. Translation: AAD49743.1 .
AL390092 Genomic DNA. Translation: CAB98233.1 .
CM002237 Genomic DNA. Translation: EAA27582.1 .
PIRi T43711.
RefSeqi XP_956818.1. XM_951725.2.
UniGenei Ncr.20426.

3D structure databases

ProteinModelPortali Q9UW15.
SMRi Q9UW15. Positions 15-769.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1974838. 3 interactions.
STRINGi 5141.NCU03539.1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EFNCRT00000002608 ; EFNCRP00000002608 ; EFNCRG00000002605 .
GeneIDi 3872956.
KEGGi ncr:NCU03539.

Phylogenomic databases

eggNOGi COG0209.
HOGENOMi HOG000057035.
KOi K10807.
OMAi NKVSMKQ.
OrthoDBi EOG7C5MHR.

Enzyme and pathway databases

UniPathwayi UPA00326 .

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. "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.

Entry informationi

Entry nameiRIR1_NEUCR
AccessioniPrimary (citable) accession number: Q9UW15
Secondary accession number(s): Q7RXZ9, Q9P3G2
Entry historyi
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 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi