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Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

RIR1

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.UniRule annotation

Catalytic activityi

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

Pathwayi: DNA replication

This protein is involved in the pathway DNA replication, which is part of Genetic information processing.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway DNA replication and in Genetic information processing.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei566SubstrateUniRule annotation1
Sitei582Important for hydrogen atom transferUniRule annotation1
Binding sitei612Substrate; via amide nitrogenUniRule annotation1
Active sitei791Proton acceptorUniRule annotation1
Active sitei793Cysteine radical intermediateUniRule annotation1
Active sitei795Proton acceptorUniRule annotation1
Sitei808Important for hydrogen atom transferUniRule annotation1
Sitei1111Important for electron transferUniRule annotation1
Sitei1112Important for electron transferUniRule annotation1
Sitei1132Interacts with thioredoxin/glutaredoxinUniRule annotation1
Sitei1135Interacts with thioredoxin/glutaredoxinUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication, Host-virus interaction

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunitUniRule annotation (EC:1.17.4.1UniRule annotation)
Short name:
R1UniRule annotation
Alternative name(s):
Ribonucleotide reductase large subunitUniRule annotation
Gene namesi
Name:RIR1UniRule annotation
Ordered Locus Names:UL39
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009294 Componenti: Genome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3840.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001872361 – 1137Ribonucleoside-diphosphate reductase large subunitAdd BLAST1137

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi582 ↔ 808Redox-activeUniRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP08543.

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

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.UniRule annotation

Protein-protein interaction databases

BioGridi971405. 1 interactor.
DIPiDIP-57653N.
IntActiP08543. 4 interactors.
MINTiMINT-6732628.

Chemistry databases

BindingDBiP08543.

Structurei

3D structure databases

ProteinModelPortaliP08543.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni581 – 582Substrate bindingUniRule annotation2
Regioni791 – 795Substrate bindingUniRule annotation5
Regioni968 – 972Substrate bindingUniRule annotation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi150 – 154Poly-Pro5
Compositional biasi190 – 239Asp/Ser-richAdd BLAST50

Sequence similaritiesi

Belongs to the ribonucleoside diphosphate reductase large chain family.UniRule annotation

Phylogenomic databases

KOiK19448.

Family and domain databases

HAMAPiMF_04026. HSV_RIR1. 1 hit.
InterProiIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
[Graphical view]
PfamiPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08543-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRPAASSP VEARAPVGGQ EAGGPSAATQ GEAAGAPLAH GHHVYCQRVN
60 70 80 90 100
GVMVLSDKTP GSASYRISDN NFVQCGSNCT MIIDGDVVRG RPQDPGAAAS
110 120 130 140 150
PAPFVAVTNI GAGSDGGTAV VAFGGTPRRS AGTSTGTQTA DVPTEALGGP
160 170 180 190 200
PPPPRFTLGG GCCSCRDTRR RSAVFGGEGD PVGPAEFVSD DRSSDSDSDD
210 220 230 240 250
SEDTDSETLS HASSDVSGGA TYDDALDSDS SSDDSLQIDG PVCRPWSNDT
260 270 280 290 300
APLDVCPGTP GPGADAGGPS AVDPHAPTPE AGAGLAADPA VARDDAEGLS
310 320 330 340 350
DPRPRLGTGT AYPVPLELTP ENAEAVARFL GDAVNREPAL MLEYFCRCAR
360 370 380 390 400
EETKRVPPRT FGSPPRLTED DFGLLNYALV EMQRLCLDVP PVPPNAYMPY
410 420 430 440 450
YLREYVTRLV NGFKPLVSRS ARLYRILGVL VHLRIRTREA SFEEWLRSKE
460 470 480 490 500
VALDFGLTER LREHEAQLVI LAQALDHYDC LIHSTPHTLV ERGLQSALKY
510 520 530 540 550
EEFYLKRFGG HYMESVFQMY TRIAGFLACR ATRGMRHIAL GREGSWWEMF
560 570 580 590 600
KFFFHRLYDH QIVPSTPAML NLGTRNYYTS SCYLVNPQAT TNKATLRAIT
610 620 630 640 650
SNVSAILARN GGIGLCVQAF NDSGPGTASV MPALKVLDSL VAAHNKESAR
660 670 680 690 700
PTGACVYLEP WHTDVRAVLR MKGVLAGEEA QRCDNIFSAL WMPDLFFKRL
710 720 730 740 750
IRHLDGEKNV TWTLFDRDTS MSLADFHGEE FEKLYQHLEV MGFGEQIPIQ
760 770 780 790 800
ELAYGIVRSA ATTGSPFVMF KDAVNRHYIY DTQGAAIAGS NLCTEIVHPA
810 820 830 840 850
SKRSSGVCNL GSVNLARCVS RQTFDFGRLR DAVQACVLMV NIMIDSTLQP
860 870 880 890 900
TPQCTRGNDN LRSMGIGMQG LHTACLKLGL DLESAEFQDL NKHIAEVMLL
910 920 930 940 950
SAMKTSNALC VRGARPFNHF KRSMYRAGRF HWERFPDARP RYEGEWEMLR
960 970 980 990 1000
QSMMKHGLRN SQFVALMPTA ASAQISDVSE GFAPLFTNLF SKVTRDGETL
1010 1020 1030 1040 1050
RPNTLLLKEL ERTFSGKRLL EVMDSLDAKQ WSVAQALPCL EPTHPLRRFK
1060 1070 1080 1090 1100
TAFDYDQKLL IDLCADRAPY VDHSQSMTLY VTEKADGTLP ASTLVRLLVH
1110 1120 1130
AYKRGLKTGM YYCKVRKATN SGVFGGDDNI VCMSCAL
Length:1,137
Mass (Da):124,051
Last modified:July 1, 1989 - v2
Checksum:i8A3777F4C22D8F85
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1034A → P in AAA45805 (PubMed:2835765).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti70N → S in strain: Nonneuroinvasive mutant HF10, 17 syn+ and Isolate pYN1. 1
Natural varianti1133M → T in strain: Nonneuroinvasive mutant HF10. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32314.1.
M18410 Genomic DNA. Translation: AAA45805.1.
DQ889502 Genomic DNA. Translation: ABI63501.1.
FJ593289 Genomic DNA. Translation: ACM62262.1.
PIRiA26536. WMBEB1.
RefSeqiYP_009137114.1. NC_001806.2.

Genome annotation databases

GeneIDi2703361.
KEGGivg:2703361.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32314.1.
M18410 Genomic DNA. Translation: AAA45805.1.
DQ889502 Genomic DNA. Translation: ABI63501.1.
FJ593289 Genomic DNA. Translation: ACM62262.1.
PIRiA26536. WMBEB1.
RefSeqiYP_009137114.1. NC_001806.2.

3D structure databases

ProteinModelPortaliP08543.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971405. 1 interactor.
DIPiDIP-57653N.
IntActiP08543. 4 interactors.
MINTiMINT-6732628.

Chemistry databases

BindingDBiP08543.
ChEMBLiCHEMBL3840.

Proteomic databases

PRIDEiP08543.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703361.
KEGGivg:2703361.

Phylogenomic databases

KOiK19448.

Enzyme and pathway databases

UniPathwayiUPA00326.

Family and domain databases

HAMAPiMF_04026. HSV_RIR1. 1 hit.
InterProiIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
[Graphical view]
PfamiPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRIR1_HHV11
AccessioniPrimary (citable) accession number: P08543
Secondary accession number(s): B9VQG7, Q09I94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.