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Reviewed, UniProtKB/Swiss-Prot P79732 (RIR1_DANRE)

Last modified September 1, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length794 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionOxidoreductase
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentribonucleoside-diphosphate reductase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from electronic annotation. Source: InterPro

ribonucleoside-diphosphate reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 794794Ribonucleoside-diphosphate reductase large subunit
PRO_0000187192

Regions

Domain1 – 9292ATP-cone

Sites

Active site2181Hydrogen atom transfer By similarity
Active site4271Proton acceptor By similarity
Active site4291Proton acceptor By similarity
Active site4311Proton acceptor By similarity
Active site4441Hydrogen atom transfer By similarity
Active site7371Electron transfer By similarity
Active site7381Electron transfer By similarity
Site2261Allosteric effector binding By similarity
Site2561Allosteric effector binding By similarity
Site7891Interacts with thioredoxin/glutaredoxin By similarity
Site7921Interacts with thioredoxin/glutaredoxin By similarity

Sequences

Sequence LengthMass (Da)Tools
P79732-1 [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 

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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: 8983196] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

U57964 mRNA. Translation: AAB37102.1.
IPIIPI00482388.
RefSeqNP_571530.1.
UniGeneDr.33356

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP79732.

Proteomic databases

PRIDEP79732.

Genome annotation databases

EnsemblENSDART00000012091; ENSDARP00000010800; ENSDARG00000014017; Danio rerio. [Genome view]
GeneID30740.
KEGGdre:30740.

Organism-specific databases

CTD30740.
ZFINZDB-GENE-990415-247. rrm1.

Phylogenomic databases

HOGENOMP79732.
HOVERGENP79732.

Enzyme and pathway databases

BRENDA1.17.4.1. 96826.

Gene expression databases

ArrayExpressP79732.
BgeeP79732.

Family and domain databases

InterProIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR013509. Ribncl_Rdtase_lsu_N.
IPR000788. Ribncl_red_lg_C.
[Graphical view]
PANTHERPTHR11573. Ribncl_red_lg_C. 1 hit.
PfamPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
PROSITEPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

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: September 1, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectZebrafish annotation project

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents