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O55716 (RIR1_IIV6) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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

Cleaved into the following chain:

  1. IIV-6 RIR1 intein
Gene names
ORF Names:IIV6-085L
OrganismInvertebrate iridescent virus 6 (IIV-6) (Chilo iridescent virus) [Reference proteome]
Taxonomic identifier176652 [NCBI]
Taxonomic lineageViruses › dsDNA viruses, no RNA stage › Iridoviridae › Iridovirus
Virus hostAcheta domesticus (House cricket) [TaxID: 6997]
Chilo suppressalis (striped riceborer) [TaxID: 168631]
Gryllus bimaculatus (Two-spotted cricket) [TaxID: 6999]
Gryllus campestris [TaxID: 58607]
Spodoptera frugiperda (Fall armyworm) [TaxID: 7108]

Protein attributes

Sequence length959 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 DOD-type homing endonuclease domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Ribonucleoside-diphosphate reductase large subunit, 1st part
PRO_0000376951
Chain272 – 611340IIV-6 RIR1 intein Potential
PRO_0000376952
Chain612 – 959348Ribonucleoside-diphosphate reductase large subunit, 2nd part
PRO_0000377536

Regions

Domain378 – 508131DOD-type homing endonuclease
Region83 – 842Substrate binding By similarity
Region751 – 7555Substrate binding By similarity

Sites

Active site2701Proton acceptor By similarity
Active site6111Cysteine radical intermediate By similarity
Active site6131Proton acceptor By similarity
Binding site681Substrate By similarity
Binding site1121Substrate; via amide nitrogen By similarity
Site841Important for hydrogen atom transfer By similarity
Site911Allosteric effector binding By similarity
Site1201Allosteric effector binding By similarity
Site6261Important for hydrogen atom transfer By similarity
Site8901Important for electron transfer By similarity
Site8911Important for electron transfer By similarity
Site9551Interacts with thioredoxin/glutaredoxin By similarity
Site9581Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond84 ↔ 626Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O55716 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: CA051A57E685F419

FASTA959108,770
        10         20         30         40         50         60 
MSDIIIDLSR DSKFDELGLK RLRESYMMRE ETSPQERFAY VCKQVGTDRD HSQRLYEYTS 

        70         80         90        100        110        120 
KHWLSLSTPI LSFGKANHGL PISCYLSWIE DTKEGLIDTL SEVNQLSMLG GGVGVGVGIR 

       130        140        150        160        170        180 
TSDNKSTGVM SHLNTYDACS LAYKQDGVRR GSYAMYLNNN HPDVLQFIEM RKPTGDHNIR 

       190        200        210        220        230        240 
CLNLHHGLNI SDEFMELIEK CDGGGNIDDT WNLIDPHTKK ITTVGARDLW QRILETRMKT 

       250        260        270        280        290        300 
GEPYICFIDT CNKHMYDFQK KKGLTIKQSN LCVAPETMIL TEDGQFPIKD LEGKIIKVWN 

       310        320        330        340        350        360 
GNEFSSVTVV KTGTEKELLE VELSNGCTLS CTPEHKFIIV KSYTEAKKQK TDDNAIANAE 

       370        380        390        400        410        420 
RVDAQDLKPR MKLIKFDLPT LFGNSEHDIK YPYTHGFFCG DGTYTKYGKP QLSLYGDKKE 

       430        440        450        460        470        480 
LLTYLDVRTM TGLEDASGRL NTWLPLDLAP KFDVPINSSL ECRMEWLAGY LDADGCVFRN 

       490        500        510        520        530        540 
GTNESIQVSC IHLDFLKRIQ LLLIGMGVTS KITKLHDEKI TTMPDGKGGQ KPYSCKPIWR 

       550        560        570        580        590        600 
LFISSSGLYH LSEQGFETRR LKWEPRQPQR NAERFVEVLK VNKTGRVDDT YCFTEPINHA 

       610        620        630        640        650        660 
GVFNGILTGQ CSEIILPTDS TRTAVCCLSS LNLEYYDEWK DNDLFIKDVM EMLDNALTIF 

       670        680        690        700        710        720 
IEKAPPTISR AVNSAKKERS IGIGVLGFHS FLQQKNISFE SDEAAKLNID IFTKLRSKID 

       730        740        750        760        770        780 
TFNLVLGSLR GSPEDAEGTG RRFCCTMAVA PTATSSIIMG NTSPSVEPFR ANAYRQDTLS 

       790        800        810        820        830        840 
GSFLNKNRYL SRILSQRLNV KEINEVWSNI VSNGGSVQQL PNNLLSEQEK QVFKTAFEIN 

       850        860        870        880        890        900 
QKWVIKHAAD RQKYIDQSQS INLFLKPDIH KRELHSLHLN AWKSGLKTLY YLRSEKIADA 

       910        920        930        940        950 
DKISSNHMIN SINFTNIKES IKDSIKVSIL EVRNKEKNYE EKICKLTNGR RLSGCFACE

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the first complete DNA sequence of an invertebrate iridovirus: coding strategy of the genome of Chilo iridescent virus."
Jakob N.J., Mueller K., Bahr U., Darai G.
Virology 286:182-196(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Comparative genomic analysis of the family Iridoviridae: re-annotating and defining the core set of iridovirus genes."
Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.
Virol. J. 4:11-11(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF303741 Genomic DNA. Translation: AAB94427.1.
PIRT03053.
RefSeqNP_149548.1. NC_003038.1.

3D structure databases

HSSPHSSP built from PDB template 2CVT based on UniProtKB P21524.
ProteinModelPortalO55716.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1733256.

Phylogenomic databases

ProtClustDBCLSP2491473.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR003586. Hint_dom_C.
IPR003587. Hint_dom_N.
IPR006142. INTEIN.
IPR004042. Intein_endonuc.
IPR006141. Intein_splice_site.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF02867. Ribonuc_red_lgC. 3 hits.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR00379. INTEIN.
SMARTSM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
[Graphical view]
SUPFAMSSF48168. Ribonucleo_red_N. 1 hit.
TIGRFAMsTIGR01445. intein_Nterm. 1 hit.
PROSITEPS50818. INTEIN_C_TER. False negative.
PS50819. INTEIN_ENDONUCLEASE. 1 hit.
PS50817. INTEIN_N_TER. 1 hit.
PS00089. RIBORED_LARGE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_IIV6
AccessionPrimary (citable) accession number: O55716
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: June 1, 1998
Last modified: April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

Intein-containing proteins

List of intein-containing protein entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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