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P79732 (RIR1_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. 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 subunit

EC=1.17.4.1
Alternative name(s):
Ribonucleoside-diphosphate reductase subunit M1
Ribonucleotide reductase large subunit
Ribonucleotide reductase protein R1 class I
Gene names
Name:rrm1
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length794 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 M1 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.

Subcellular location

Cytoplasm.

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 – 794794Ribonucleoside-diphosphate reductase large subunit
PRO_0000187192

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
Region603 – 6075Substrate 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
Site7371Important for electron transfer By similarity
Site7381Important for electron transfer By similarity
Site7891Interacts with thioredoxin/glutaredoxin By similarity
Site7921Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond218 ↔ 444Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P79732 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 128355C073B3908C

FASTA79489,816
        10         20         30         40         50         60 
MHVIKRDGGQ EGVMFDKITS RIQKLCYGLN SDFVDPTQIT MKVIQGLYSG VTTVELDTLA 

        70         80         90        100        110        120 
AETAATSTTK HPDYAILAAR IAVSNLHKET KKVFSEVMED LYNYVNPLNS RHSPMISKET 

       130        140        150        160        170        180 
LDIVLANKDR LNSAIIYDRD FSYNFFGFKT LERSYLLKIN GKVAERPQHM LMRVSVGIHK 

       190        200        210        220        230        240 
EDIAAAIETY NLLSEKWFTH ASPTLFNAGT NRPQLSSCFL LAMKDDSIEG IYDTLKQCAL 

       250        260        270        280        290        300 
ISKSAGGIGV AVSCIRATGR YIAGTNGNSN GLVPMLRVNN NTARYVDQGG NKRPGAFAMY 

       310        320        330        340        350        360 
LEPWHFDIFD FLELKKNTGK EEQRARDLFY ALWIPDLFMK RVETNGDWSL MCPNDCPGLD 

       370        380        390        400        410        420 
ECWGEEFEKL YAKYEQEGRA KRVVKAQQLW YAIIESQTET GTPYMLYKDA CNRKSNRQNL 

       430        440        450        460        470        480 
GTIKCSNLCT EIVEYTSADE VAVCNLASIA LNMYVTSERT FDFQKLASVT KVIVKNLNKI 

       490        500        510        520        530        540 
IDINYYPVKE AENSNKRHRP IGIGVQGLAD AFILMRFPFE STEAQLLNTQ IFETIYYAAL 

       550        560        570        580        590        600 
ESSCELAAEY GPYQTYAGCP VSKGILQYDM WEKTPTDLWD WAALKEKIAN DGVRNSLLLA 

       610        620        630        640        650        660 
PMPTASTAQI LGNNESIEPY TSNIYHRRVL SGEFQIVNPH LLKDLTERGL WNEEMKNQII 

       670        680        690        700        710        720 
AQNGSIQTIP AIPDDLKELY KTVWEISQKT ILKMAADRGA YIDQSQSLNI HIAEPNYGKL 

       730        740        750        760        770        780 
TSMHFYGWKQ GLKTGMYYLR TKPGANPIQF TLNKEKLKET QKTTSSEDEE TKERNKAAMV 

       790 
CSLENRHECL MCGS 

« Hide

References

[1]"Cloning and sequencing of cDNAs encoding ribonucleotide reductase from zebrafish Danio rerio."
Mathews C.Z., Sjoeberg B.-M., Karlsson M.
Mol. Mar. Biol. Biotechnol. 5:284-287(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57964 mRNA. Translation: AAB37102.1.
UniGeneDr.33356.

3D structure databases

ProteinModelPortalP79732.
SMRP79732. Positions 15-755.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000010800.

Proteomic databases

PRIDEP79732.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

KEGGdre:30740.

Organism-specific databases

CTD6240.
ZFINZDB-GENE-990415-247. rrm1.

Phylogenomic databases

eggNOGCOG0209.
HOGENOMHOG000057035.
HOVERGENHBG003447.
InParanoidP79732.
KOK10807.
PhylomeDBP79732.

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...

Other

NextBio20807088.
PROP79732.

Entry information

Entry nameRIR1_DANRE
AccessionPrimary (citable) accession number: P79732
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways