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P09853

- RIR1_HHV23

UniProt

P09853 - RIR1_HHV23

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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: 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.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei573 – 5731Substrate By similarity
Sitei589 – 5891Important for hydrogen atom transfer By similarity
Binding sitei619 – 6191Substrate; via amide nitrogen By similarity
Active sitei798 – 7981Proton acceptor By similarity
Active sitei800 – 8001Cysteine radical intermediate By similarity
Active sitei802 – 8021Proton acceptor By similarity
Sitei815 – 8151Important for hydrogen atom transfer By similarity
Sitei1118 – 11181Important for electron transfer By similarity
Sitei1119 – 11191Important for electron transfer By similarity
Sitei1139 – 11391Interacts with thioredoxin/glutaredoxin By similarity
Sitei1142 – 11421Interacts with thioredoxin/glutaredoxin By 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
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-active By 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.

Structurei

3D structure databases

ProteinModelPortaliP09853.

Family & Domainsi

Region

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

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MANRPAASAL AGARSPSERQ EPREPEVAPP GGDHVFCRKV SGVMVLSSDP     50
PGPAAYRISD SSFVQCGSNC SMIIDGDVAR GHLRDLEGAT STGAFVAISN 100
VAAGGDGRTA VVALGGTSGP SATTSVGTQT SGEFLHGNPR TPEPQGPQAV 150
PPPPPPPFPW GHECCARRDA RGGAEKDVGA AESWSDGPSS DSETEDSDSS 200
DEDTGSGSET LSRSSSIWAA GATDDDDSDS DSRSDDSVQP DVVVRRRWSD 250
GPAPVAFPKP RRPGDSPGNP GLGAGTGPGS ATDPRASADS DSAAHAAAPQ 300
ADVAPVLDSQ PTVGTDPGYP VPLELTPENA EAVARFLGDA VDREPALMLE 350
YFCRCAREES KRVPPRTFGS APRLTEDDFG LLNYALAEMR RLCLDLPPVP 400
PNAYTPYHLR EYATRLVNGF KPLVRRSARL YRILGILVHL RIRTREASFE 450
EWMRSKEVDL DFGLTERLRE HEAQLMILAQ ALNPYDCLIH STPNTLVERG 500
LQSALKYEEF YLKRFGGHYM ESVFQMYTRI AGFLACRATR GMRHIALGRQ 550
GSWWEMFKFF FHRLYDHQIV PSTPAMLNLG TRNYYTSSCY LVNPQATTNQ 600
ATLRAITGNV SAILARNGGI GLCMQAFNDA SPGTASIMPA LKVLDSLVAA 650
HNKQSTRPTG ACVYLEPWHS DVRAVLRMKG VLAGEEAQRC DNIFSALWMP 700
DLFFKRLIRH LDGEKNVTWS LFDRDTSMSL ADFHGEEFEK LYEHLEAMGF 750
GETIPIQDLA YAIVRSAATT GSPFIMFKDA VNRHYIYDTQ GAAIAGSNLC 800
TEIVHPSSKR SSGVCNLGSV NLARCVSRRT FDFGMLRDAV QACVLMVNIM 850
IDSTLQPTPQ CARGHDNLRS MGIGMQGLHT ACLKMGLDLE SAEFRDLNTH 900
IAEVMLLAAM KTSNALCVRG ARPFSHFKRS MYRAGRFHWE RFSNASPRYE 950
GEWEMLRQSM MKHGLRNSQF IALMPTAASA QISDVSEGFA PLFTNLFSKV 1000
TRDGETLRPN TLLLKELERT FGGKRLLDAM DGLEAKQWSV AQALPCLDPA 1050
HPLRRFKTAF DYDQELLIDL CADRAPYVDH SQSMTLYVTE KADGTLPAST 1100
LVRLLVHAYK RGLKTGMYYC KVRKATNSGV FAGDDNIVCT SCAL 1144
Length:1,144
Mass (Da):125,093
Last modified:October 1, 1996 - v2
Checksum:i4771481C3103FC78
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12700 Genomic DNA. Translation: AAA45806.1.
X00048 Genomic DNA. Translation: CAA24929.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12700 Genomic DNA. Translation: AAA45806.1 .
X00048 Genomic DNA. Translation: CAA24929.1 .

3D structure databases

ProteinModelPortali P09853.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P09853.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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

  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: December 11, 2013
This is version 83 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

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