P03190 (RIR1_EBVB9) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase large subunit
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase 140 kDa subunit
Ribonucleotide reductase large subunit

Gene names

ORF Names:

BORF2

Organism

Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) [Reference proteome]

Taxonomic identifier

10377 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus › Epstein-Barr virus (strain GD1)

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	826 AA.
Sequence status	Complete.
Protein existence	Inferred 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, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity.
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.
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 BaRF1 (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.

Ontologies

Keywords
Biological process	DNA replication
Developmental stage	Early protein
Ligand	ATP-binding Nucleotide-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 826	826	Ribonucleoside-diphosphate reductase large subunit		PRO_0000187234
Regions
	Region	186 – 187	2	Substrate binding By similarity
	Region	387 – 391	5	Substrate binding By similarity
	Region	594 – 598	5	Substrate binding By similarity
Sites
	Active site	387	1	Proton acceptor By similarity
	Active site	389	1	Cysteine radical intermediate By similarity
	Active site	391	1	Proton acceptor By similarity
	Binding site	171	1	Substrate By similarity
	Binding site	217	1	Substrate; via amide nitrogen By similarity
	Site	187	1	Important for hydrogen atom transfer By similarity
	Site	403	1	Important for hydrogen atom transfer By similarity
	Site	725	1	Important for electron transfer By similarity
	Site	726	1	Important for electron transfer By similarity
	Site	822	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	825	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	187 ↔ 403		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P03190 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 6E5C25623D371EF1	FASTA	826	93,031
	10 20 30 40 50 60 MATTSHVEHE LLSKLIDELK VKANSDPEAD VLAGRLLHRL KAESVTHTVA EYLEVFSDKF 70 80 90 100 110 120 YDEEFFQMHR DELETRVSAF AQSPAYERIV SSGYLSALRY YDTYLYVGRS GKQESVQHFY 130 140 150 160 170 180 MRLAGFCAST TCLYAGLRAA LQRARPEIES DMEVFDYYFE HLTSQTVCCS TPFMRFAGVE 190 200 210 220 230 240 NSTLASCILT TPDLSSEWDV TQALYRHLGR YLFQRAGVGV GVTGAGQDGK HISLLMRMIN 250 260 270 280 290 300 SHVEYHNYGC KRPVSVAAYM EPWHSQIFKF LETKLPENHE RCPGIFTGLF VPELFFKLFR 310 320 330 340 350 360 DTPWSDWYLF DPKDAGDLER LYGEEFEREY YRLVTAGKFC GRVSIKSLMF SIVNCAVKAG 370 380 390 400 410 420 SPFILLKEAC NAHFWRDLQG EAMNAANLCA EVLQPSRKSV ATCNLANICL PRCLVNAPLA 430 440 450 460 470 480 VRAQRADTQG DELLLALPRL SVTLPGEGAV GDGFSLARLR DATQCATFVV ACSILQGSPT 490 500 510 520 530 540 YDSRDMASMG LGVQGLADVF ADLGWQYTDP PSRSLNKEIF EHMYFTALCT SSLIGLHTRK 550 560 570 580 590 600 IFPGFKQSKY AGGWFHWHDW AGTDLSIPRE IWSRLSERIV RDGLFNSQFI ALMPTSGCAQ 610 620 630 640 650 660 VTGCSDAFYP FYANASTKVT NKEEALRPNR SFWRHVRLDD REALNLVGGR VSCLPEALRQ 670 680 690 700 710 720 RYLRFQTAFD YNQEDLIQMS RDRAPFVDQS QSHSLFLREE DAARASTLAN LLVRSYELGL 730 740 750 760 770 780 KTIMYYCRIE KAADLGVMEC KASAALSVPR EEQNERSPAE QMPPRPMEPA QVAGPVDIMS 790 800 810 820 KGPGEGPGGW CVPGGLEVCY KYRQLFSEDD LLETDGFTER ACESCQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence and expression of the B95-8 Epstein-Barr virus genome." Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C., Tuffnell P.S., Barrell B.G. Nature 310:207-211(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Homology between two EBV early genes and HSV ribonucleotide reductase and 38K genes." Gibson T.J., Stockwell P., Ginsburg M., Barrell B.G. Nucleic Acids Res. 12:5087-5099(1984) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF PROTEIN.
[3]	"Proteins of purified Epstein-Barr virus." Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E., Illanes D., Sarracino D., Kieff E. Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	V01555 Genomic DNA. Translation: CAA24842.1. AJ507799 Genomic DNA. Translation: CAD53405.1.
PIR	QQBE11. A03753.
RefSeq	YP_401655.1. NC_007605.1.
3D structure databases
ProteinModelPortal	P03190.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-6768227.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3783725.
Phylogenomic databases
ProtClustDB	CLSP2509697.
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
InterPro	IPR013346. NrdE_NrdA. IPR000788. RNR_lg_C. IPR013509. RNR_lsu_N. [Graphical view]
Pfam	PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
TIGRFAMs	TIGR02506. NrdE_NrdA. 1 hit.
PROSITE	PS00089. RIBORED_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR1_EBVB9

Accession

Primary (citable) accession number: P03190
Secondary accession number(s): Q777G1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program