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Protein

Ribonucleoside-diphosphate reductase large subunit

Gene
N/A
Organism
Human herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2)
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. 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.

Pathway: DNA replication

This protein is involved in the pathway DNA replication, which is part of Genetic information processing.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei573 – 5731SubstrateBy similarity
Sitei589 – 5891Important for hydrogen atom transferBy similarity
Binding sitei619 – 6191Substrate; via amide nitrogenBy similarity
Active sitei798 – 7981Proton acceptorBy similarity
Active sitei800 – 8001Cysteine radical intermediateBy similarity
Active sitei802 – 8021Proton acceptorBy similarity
Sitei815 – 8151Important for hydrogen atom transferBy similarity
Sitei1118 – 11181Important for electron transferBy similarity
Sitei1119 – 11191Important for electron transferBy similarity
Sitei1139 – 11391Interacts with thioredoxin/glutaredoxinBy similarity
Sitei1142 – 11421Interacts with thioredoxin/glutaredoxinBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

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)
Alternative name(s):
Ribonucleotide reductase 136 kDa subunit
Ribonucleotide reductase large subunit
OrganismiHuman herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2)
Taxonomic identifieri10313 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11441144Ribonucleoside-diphosphate reductase large subunitPRO_0000187237Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi589 ↔ 815Redox-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

Structurei

3D structure databases

ProteinModelPortaliP09853.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni588 – 5892Substrate bindingBy similarity
Regioni798 – 8025Substrate bindingBy similarity
Regioni975 – 9795Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi151 – 1599Poly-Pro
Compositional biasi224 – 2318Poly-Asp

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.

P09853-1 [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
DEDTGSGSET LSRSSSIWAA GATDDDDSDS DSRSDDSVQP DVVVRRRWSD
260 270 280 290 300
GPAPVAFPKP RRPGDSPGNP GLGAGTGPGS ATDPRASADS DSAAHAAAPQ
310 320 330 340 350
ADVAPVLDSQ PTVGTDPGYP VPLELTPENA EAVARFLGDA VDREPALMLE
360 370 380 390 400
YFCRCAREES KRVPPRTFGS APRLTEDDFG LLNYALAEMR RLCLDLPPVP
410 420 430 440 450
PNAYTPYHLR EYATRLVNGF KPLVRRSARL YRILGILVHL RIRTREASFE
460 470 480 490 500
EWMRSKEVDL DFGLTERLRE HEAQLMILAQ ALNPYDCLIH STPNTLVERG
510 520 530 540 550
LQSALKYEEF YLKRFGGHYM ESVFQMYTRI AGFLACRATR GMRHIALGRQ
560 570 580 590 600
GSWWEMFKFF FHRLYDHQIV PSTPAMLNLG TRNYYTSSCY LVNPQATTNQ
610 620 630 640 650
ATLRAITGNV SAILARNGGI GLCMQAFNDA SPGTASIMPA LKVLDSLVAA
660 670 680 690 700
HNKQSTRPTG ACVYLEPWHS DVRAVLRMKG VLAGEEAQRC DNIFSALWMP
710 720 730 740 750
DLFFKRLIRH LDGEKNVTWS LFDRDTSMSL ADFHGEEFEK LYEHLEAMGF
760 770 780 790 800
GETIPIQDLA YAIVRSAATT GSPFIMFKDA VNRHYIYDTQ GAAIAGSNLC
810 820 830 840 850
TEIVHPSSKR SSGVCNLGSV NLARCVSRRT FDFGMLRDAV QACVLMVNIM
860 870 880 890 900
IDSTLQPTPQ CARGHDNLRS MGIGMQGLHT ACLKMGLDLE SAEFRDLNTH
910 920 930 940 950
IAEVMLLAAM KTSNALCVRG ARPFSHFKRS MYRAGRFHWE RFSNASPRYE
960 970 980 990 1000
GEWEMLRQSM MKHGLRNSQF IALMPTAASA QISDVSEGFA PLFTNLFSKV
1010 1020 1030 1040 1050
TRDGETLRPN TLLLKELERT FGGKRLLDAM DGLEAKQWSV AQALPCLDPA
1060 1070 1080 1090 1100
HPLRRFKTAF DYDQELLIDL CADRAPYVDH SQSMTLYVTE KADGTLPAST
1110 1120 1130 1140
LVRLLVHAYK RGLKTGMYYC KVRKATNSGV FAGDDNIVCT SCAL
Length:1,144
Mass (Da):125,093
Last modified:October 1, 1996 - v2
Checksum:i4771481C3103FC78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12700 Genomic DNA. Translation: AAA45806.1.
X00048 Genomic DNA. Translation: CAA24929.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12700 Genomic DNA. Translation: AAA45806.1.
X00048 Genomic DNA. Translation: CAA24929.1.

3D structure databases

ProteinModelPortaliP09853.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00326.

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]
ProtoNetiSearch...

Publicationsi

  1. "Herpes simplex virus specifies two subunits of ribonucleotide reductase encoded by 3'-coterminal transcripts."
    Swain M.A., Galloway D.A.
    J. Virol. 57:802-808(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Organization of the left-hand end of the herpes simplex virus type 2 BglII N fragment."
    Galloway D.A., Swain M.A.
    J. Virol. 49:724-730(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 981-1144.
  3. "DNA sequence homology between two co-linear loci on the HSV genome which have different transforming abilities."
    McLauchlan J., Clements J.B.
    EMBO J. 2:1953-1961(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1036-1144.
  4. "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_HHV23
AccessioniPrimary (citable) accession number: P09853
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3

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 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.