Q3KSU5 (RIR1_EBVG) 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 GD1) (HHV-4) (Human herpesvirus 4) [Complete proteome]

Taxonomic identifier

10376 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus

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
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete 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: InterPro 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_0000375966
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)
	Q3KSU5 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: EC04EBDD0A298389	FASTA	826	93,102
	10 20 30 40 50 60 MATTNHVEHE LLSKLIDELK VKANADPEAD 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 SVTLPGEGAI 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 QMLPRPMEPA QVTGPVDIMS 790 800 810 820 KGPGEGPGGW CVPGGLEVCY KYRQLFSEDD LLETDGFTER ACESCQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic sequence analysis of Epstein-Barr virus strain GD1 from a nasopharyngeal carcinoma patient." Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H., Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X. J. Virol. 79:15323-15330(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Tinkering with a viral ribonucleotide reductase." Lembo D., Brune W. Trends Biochem. Sci. 34:25-32(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY961628 Genomic DNA. Translation: AAY41105.1.
3D structure databases
HSSP	HSSP built from PDB template 2CVX based on UniProtKB P21524.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q3KSU5. 2 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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_EBVG

Accession

Primary (citable) accession number: Q3KSU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	November 8, 2005
Last modified:	January 9, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program