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Q7T6Y8 (RIR1_MIMIV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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):
Ribonucleotide reductase large subunit
Gene names
Name:RNR1
Ordered Locus Names:MIMI_R313
OrganismAcanthamoeba polyphaga mimivirus (APMV) [Reference proteome]
Taxonomic identifier212035 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageMimiviridaeMimivirus
Virus hostAcanthamoeba polyphaga (Amoeba) [TaxID: 5757]

Protein attributes

Sequence length881 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity.

Catalytic activity

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Enzyme regulation

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. 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 By similarity.

Pathway

Genetic information processing; DNA replication.

Subunit structure

Heterotetramer composed of a homodimer of the large subunit (R1) and a homodimer of the small subunit (R2). Larger multisubunit protein complex are also active, composed of (R1)n(R2)n By similarity.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Contains 1 ATP-cone domain.

Ontologies

Keywords
   Biological processDNA replication
   Developmental stageEarly protein
   LigandATP-binding
Nucleotide-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentribonucleoside-diphosphate reductase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 881881Ribonucleoside-diphosphate reductase large subunit
PRO_0000187229

Regions

Domain69 – 16092ATP-cone
Region286 – 2872Substrate binding By similarity
Region493 – 4975Substrate binding By similarity
Region675 – 6795Substrate binding By similarity

Sites

Active site4931Proton acceptor By similarity
Active site4951Cysteine radical intermediate By similarity
Active site4971Proton acceptor By similarity
Binding site2711Substrate By similarity
Binding site3151Substrate; via amide nitrogen By similarity
Site2871Important for hydrogen atom transfer By similarity
Site2941Allosteric effector binding By similarity
Site3241Allosteric effector binding By similarity
Site5101Important for hydrogen atom transfer By similarity
Site8091Important for electron transfer By similarity
Site8101Important for electron transfer By similarity
Site8761Interacts with thioredoxin/glutaredoxin By similarity
Site8791Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond287 ↔ 510Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7T6Y8 [UniParc].

Last modified December 7, 2004. Version 2.
Checksum: BC4A893F2212E068

FASTA881101,472
        10         20         30         40         50         60 
MNSKNSIILD NLADVSDIID YEQNSIDYQR SIKNIEQLKS TEATEITNKL AINKAKKSSN 

        70         80         90        100        110        120 
ILLEVPKETI YLDHNGSIQV ITSEIIRTYV EKIFEKMEVT HLDIDKMTKN IFPKLKSINT 

       130        140        150        160        170        180 
IKDIDNQIIS TASEMVTDHY DYPKIAVWIL MTNLHDNTSD DFLETAEKLY NNKSESNKNA 

       190        200        210        220        230        240 
PIISENIYNF IKKHIKEINR VIRYDRDYNL TIFGFRTLEK SYLKRINKKI VERPQHLFMR 

       250        260        270        280        290        300 
VAITLHYRKN DLDRIFETYK YLSKGYFTHA TPTLFNAGTT HEQLSSCFLL GIGDSLEEIS 

       310        320        330        340        350        360 
ECWKECALIS KHAGGIGIHM TNIRVEGAYI ASTQGEAGGL RVLTIFNDIS RYANQGGKRP 

       370        380        390        400        410        420 
GSFAIFIEPW HGDIFFFLDL KKNTGAETER ARDLFLGLMI NDIFMERVYK DDVWSLMCPS 

       430        440        450        460        470        480 
QCPNLLNKYG DEFTKEYLKY ESEGIYLKQI RAIDLWFKIM ESQIETGVPY VMFKDAINDK 

       490        500        510        520        530        540 
SNQINIGVVN GSNLCCEIVE VSDKNNFSVC NLSSICLPRF VKIIDEVPTF NYQKLFKISR 

       550        560        570        580        590        600 
ILTRNLNNII DINFYPLDKT RITNLRDRPI GIGVQGLADV FAMFKTPFDS EIARDLNRKI 

       610        620        630        640        650        660 
FETIYYGALT ESNKLAREFG TYQTYQGSPI SQGKFQFDLW NFDKSQLSGM WDWELLRQEI 

       670        680        690        700        710        720 
LNHGVRNSLV TTCMPTASTS QIMGWNECIE PYTENIYSRS TMAGEYFVIN KHLIKDLIEL 

       730        740        750        760        770        780 
GVWNSEMVDL IKYYKGSVAN IPNIPDNIKA IYRTVWEIPQ KSIIEMAADR APFVDQTQSM 

       790        800        810        820        830        840 
NLYIDKPSFA RLNSCLFYAW RKGLKTGMYY LRSKPASSAN QFGIDIDKIK EIESKNGIKK 

       850        860        870        880 
QEDTFDLTDL TNTINQQVSG MVCRFVPAHL RKPGECLSCD G 

« Hide

References

[1]"The 1.2-megabase genome sequence of Mimivirus."
Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H., La Scola B., Susan M., Claverie J.-M.
Science 306:1344-1350(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Rowbotham-Bradford.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY653733 Genomic DNA. Translation: AAQ09572.2.
RefSeqYP_003986816.1. NC_014649.1.

3D structure databases

ProteinModelPortalQ7T6Y8.
SMRQ7T6Y8. Positions 145-814.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9924930.

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]
PfamPF02867. 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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_MIMIV
AccessionPrimary (citable) accession number: Q7T6Y8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: December 7, 2004
Last modified: May 14, 2014
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways