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P89462

- RIR1_HHV2H

UniProt

P89462 - RIR1_HHV2H

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Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

UL39

Organism
Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)
Status
Reviewed - Annotation score: 4 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. The N-terminal region confers antiapoptotic activity in differentiated cells such as neurons and is important for viral reactivation to increase neural survivability (By similarity).By similarity

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.
ATP + a protein = ADP + a phosphoprotein.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei571 – 5711SubstrateBy similarity
Sitei587 – 5871Important for hydrogen atom transferBy similarity
Binding sitei617 – 6171Substrate; via amide nitrogenBy similarity
Active sitei796 – 7961Proton acceptorBy similarity
Active sitei798 – 7981Cysteine radical intermediateBy similarity
Active sitei800 – 8001Proton acceptorBy similarity
Sitei813 – 8131Important for hydrogen atom transferBy similarity
Sitei1116 – 11161Important for electron transferBy similarity
Sitei1117 – 11171Important for electron transferBy similarity
Sitei1137 – 11371Interacts with thioredoxin/glutaredoxinBy similarity
Sitei1140 – 11401Interacts with thioredoxin/glutaredoxinBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB-EC

GO - Biological processi

  1. DNA replication Source: UniProtKB-UniPathway
  2. viral process Source: UniProtKB-KW
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 subunit (EC:1.17.4.1)
Short name:
R1
Alternative name(s):
ICP10
Ribonucleotide reductase 136 kDa subunit
Ribonucleotide reductase large subunit
Gene namesi
ORF Names:UL39
OrganismiHuman herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)
Taxonomic identifieri10315 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000001874: Genome

Subcellular locationi

Host cell membrane 1 Publication. Host endosome membrane 1 Publication
Note: Associates with the host cytoskeleton.Curated

GO - Cellular componenti

  1. host cell endosome Source: UniProtKB-KW
  2. host cell plasma membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host endosome, Host membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11421142Ribonucleoside-diphosphate reductase large subunitPRO_0000385162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi587 ↔ 813Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Heterotetramer composed of a homodimer of the large subunit UL39 (R1) and a homodimer of the small subunit UL40 (R2). Larger multisubunit protein complex are also active, composed of (R1)n(R2)n (By similarity).By similarity

Protein-protein interaction databases

BioGridi1677930. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP89462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni294 – 400107alpha-crystallin domainAdd
BLAST
Regioni586 – 5872Substrate bindingBy similarity
Regioni796 – 8005Substrate bindingBy similarity
Regioni973 – 9775Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi151 – 1599Poly-Pro
Compositional biasi186 – 23954Asp/Ser-richAdd
BLAST

Domaini

Contains an alpha-crystallin domain homologous to small heat-shock proteins.

Sequence similaritiesi

Family and domain databases

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.

P89462-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MANRPAASAL AGARSPSERQ EPREPEVAPP GGDHVFCRKV SGVMVLSSDP
60 70 80 90 100
PGPAAYRISD SSFVQCGSNC SMIIDGDVAR GHLRDLEGAT STGAFVAISN
110 120 130 140 150
VAAGGDGRTA VVALGGTSGP SATTSVGTQT SGEFLHGNPR TPEPQGPQAV
160 170 180 190 200
PPPPPPPFPW GHECCARRDA RGGAEKDVGA AESWSDGPSS DSETEDSDSS
210 220 230 240 250
DEDTGSETLS RSSSIWAAGA TDDDDSDSDS RSDDSVQPDV VVRRRWSDGP
260 270 280 290 300
APVAFPKPRR PGDSPGNPGL GAGTGPGSAT DPRASADSDS AAHAAAPQAD
310 320 330 340 350
VAPVLDSQPT VGTDPGYPVP LELTPENAEA VARFLGDAVD REPALMLEYF
360 370 380 390 400
CRCAREESKR VPPRTFGSAP RLTEDDFGLL NYALAEMRRL CLDLPPVPPN
410 420 430 440 450
AYTPYHLREY ATRLVNGFKP LVRRSARLYR ILGVLVHLRI RTREASFEEW
460 470 480 490 500
MRSKEVDLDF GLTERLREHE AQLMILAQAL NPYDCLIHST PNTLVERGLQ
510 520 530 540 550
SALKYEEFYL KRFGGHYMES VFQMYTRIAG FLACRATRGM RHIALGRQGS
560 570 580 590 600
WWEMFKFFFH RLYDHQIVPS TPAMLNLGTR NYYTSSCYLV NPQATTNQAT
610 620 630 640 650
LRAITGNVSA ILARNGGIGL CMQAFNDASP GTASIMPALK VLDSLVAAHN
660 670 680 690 700
KQSTRPTGAC VYLEPWHSDV RAVLRMKGVL AGEEAQRCDN IFSALWMPDL
710 720 730 740 750
FFKRLIRHLD GEKNVTWSLF DRDTSMSLAD FHGEEFEKLY EHLEAMGFGE
760 770 780 790 800
TIPIQDLAYA IVRSAATTGS PFIMFKDAVN RHYIYDTQGA AIAGSNLCTE
810 820 830 840 850
IVHPASKRSS GVCNLGSVNL ARCVSRQTFD FGRLRDAVQA CVLMVNIMID
860 870 880 890 900
STLQPTPQCT RGNDNLRSMG IGMQGLHTAC LKMGLDLESA EFRDLNTHIA
910 920 930 940 950
EVMLLAAMKT SNALCVRGAR PFSHFKRSMY RAGRFHWERF SNASPRYEGE
960 970 980 990 1000
WEMLRQSMMK HGLRNSQFIA LMPTAASAQI SDVSEGFAPL FTNLFSKVTR
1010 1020 1030 1040 1050
DGETLRPNTL LLKELERTFG GKRLLDAMDG LEAKQWSVAQ ALPCLDPAHP
1060 1070 1080 1090 1100
LRRFKTAFDY DQELLIDLCA DRAPYVDHSQ SMTLYVTEKA DGTLPASTLV
1110 1120 1130 1140
RLLVHAYKRG LKTGMYYCKV RKATNSGVFA GDDNIVCTSC AL
Length:1,142
Mass (Da):124,923
Last modified:May 1, 1997 - v1
Checksum:i5A46D3985338BB21
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z86099 Genomic DNA. Translation: CAB06725.1.
PIRiA05247.
RefSeqiNP_044509.1. NC_001798.1.

Genome annotation databases

GeneIDi1487325.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z86099 Genomic DNA. Translation: CAB06725.1 .
PIRi A05247.
RefSeqi NP_044509.1. NC_001798.1.

3D structure databases

ProteinModelPortali P89462.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1677930. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1487325.

Enzyme and pathway databases

UniPathwayi UPA00326 .

Family and domain databases

InterProi IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
[Graphical view ]
Pfami PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view ]
PRINTSi PR01183. RIBORDTASEM1.
TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
PROSITEi PS00089. RIBORED_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of herpes simplex virus type 2."
    Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.
    J. Virol. 72:2010-2021(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Intracellular internalization and signaling pathways triggered by the large subunit of HSV-2 ribonucleotide reductase (ICP10)."
    Hunter J.C., Smith C.C., Bose D., Kulka M., Broderick R., Aurelian L.
    Virology 210:345-360(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  3. "The herpes simplex virus type 2 R1 protein kinase (ICP10 PK) blocks apoptosis in hippocampal neurons, involving activation of the MEK/MAPK survival pathway."
    Perkins D., Pereira E.F., Gober M., Yarowsky P.J., Aurelian L.
    J. Virol. 76:1435-1449(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27."
    Chabaud S., Lambert H., Sasseville A.M., Lavoie H., Guilbault C., Massie B., Landry J., Langelier Y.
    FEBS Lett. 545:213-218(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALPHA-CRYSTALLIN DOMAIN.
  5. "Tinkering with a viral ribonucleotide reductase."
    Lembo D., Brune W.
    Trends Biochem. Sci. 34:25-32(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiRIR1_HHV2H
AccessioniPrimary (citable) accession number: P89462
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 1, 1997
Last modified: October 29, 2014
This is version 85 of the entry and version 1 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

External Data

Dasty 3