Q6R7H4 (RIR1_OSHVF) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Ribonucleoside-diphosphate reductase large subunit EC=1.17.4.1
Organism	Ostreid herpesvirus 1 (isolate France) (OsHV-1) (Pacific oyster herpesvirus) [Reference proteome]
Taxonomic identifier	654903 [NCBI]
Taxonomic lineage	Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Malacoherpesviridae › Ostreavirus › Ostreid herpesvirus 1
Virus host	Crassostrea gigas (Pacific oyster) (Crassostrea angulata) [TaxID: 29159] Pecten maximus (King scallop) (Pilgrim's clam) [TaxID: 6579]

Protein attributes

Sequence length	835 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. 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 (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 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: 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 – 835	835	Ribonucleoside-diphosphate reductase large subunit		PRO_0000385023
Regions
	Region	237 – 238	2	Substrate binding By similarity
	Region	447 – 451	5	Substrate binding By similarity
	Region	660 – 664	5	Substrate binding By similarity
Sites
	Active site	447	1	Proton acceptor By similarity
	Active site	449	1	Cysteine radical intermediate By similarity
	Active site	451	1	Proton acceptor By similarity
	Binding site	222	1	Substrate By similarity
	Binding site	266	1	Substrate; via amide nitrogen By similarity
	Site	238	1	Important for hydrogen atom transfer By similarity
	Site	464	1	Important for hydrogen atom transfer By similarity
	Site	797	1	Important for electron transfer By similarity
	Site	798	1	Important for electron transfer By similarity
	Site	830	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	833	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	238 ↔ 464		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6R7H4 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 4C5813635B9E5F47	FASTA	835	93,356
	10 20 30 40 50 60 MACSMANAVR PGLSDLPEGV DLSNPKEVRS LLIKLTHARK STVYDTKIRR LHGVIVNSIM 70 80 90 100 110 120 ENYNSAEGEL DMAITPLIPS HPDYAFLAGR VSAYMTQINT PKTFTDAVYG IQMAVGETNG 130 140 150 160 170 180 FRSPMKPVKG GLSDEIVDFV NEHGARLDGM IDDVRDYSHN YMGITGLLNG VAIKVNKKLY 190 200 210 220 230 240 ERPQYVFMRV AMAMTDLSSE TALEDIWQTY MLISGQCLSM ASPVLFNGGT SSSNTASCFL 250 260 270 280 290 300 LDMGDNMVSI TKKVAQTMTL IAKNGGIGIN FSKLRATGSK IGMAGKSSGI GGKLNLFDRV 310 320 330 340 350 360 AQSVDQGENK RPGAIAGYLT DWHADMYDWL YSRYSGSGNE VNKRHVLNMG LVMSDLFMER 370 380 390 400 410 420 VENDKEWSLF SPNDVVGLEE LYGEKFVRAY RAHEANPKIK RTTVSARKLF SDIANMMWST 430 440 450 460 470 480 GEPYILFKDA VNERSNHKHL GTIKNSNLCC EIVQYCDTNE IAVCNLATIC VSNFVNVETG 490 500 510 520 530 540 EIDFEGIADA AGVACKGINN LIDKQNYDLG NEQLMRLADE RTEEVVEVNG IKFDAKYNLV 550 560 570 580 590 600 SYSNLKHRPQ GIGMQGLHDV FMKLKIPYDS EMAFRLAALI QEAIYYGAVR ESVKIAEEKG 610 620 630 640 650 660 PYPSYYWDNN THREGKLQFD FLEGFDRDRD LTHELFNWRE VLKKFEKFGI NNSVVTAQPP 670 680 690 700 710 720 SASSSQLNDN VESIEAITSN RFTKGIKDGK FIIINKHLQK DLEDLGMWDA QMVGDIEAND 730 740 750 760 770 780 GSIQNIERIP KNIREIYKTA REIDHKAVVK ICAAIQPFID QTISKNMFVP KNVDNPVQLI 790 800 810 820 830 MENVILGHKM KLKTGMYYTR GIPAMKQQNF GKMNFQDKDI GKPVPELVDC EACSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel class of herpesvirus with bivalve hosts." Davison A.J., Trus B.L., Cheng N., Steven A.C., Watson M.S., Cunningham C., Le Deuff R.M., Renault T. J. Gen. Virol. 86:41-53(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	AY509253 Genomic DNA. Translation: AAS00941.1.
RefSeq	YP_024594.1. NC_005881.1.
3D structure databases
ProteinModelPortal	Q6R7H4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2948194.
Phylogenomic databases
ProtClustDB	CLSP2509774.
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
InterPro	IPR013346. NrdE_NrdA. IPR000788. RNR_lg_C. IPR013509. RNR_lsu_N. IPR008926. RNR_R1-su_N. [Graphical view]
Pfam	PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
SUPFAM	SSF48168. Ribonucleo_red_N. 1 hit.
TIGRFAMs	TIGR02506. NrdE_NrdA. 1 hit.
PROSITE	PS00089. RIBORED_LARGE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR1_OSHVF

Accession

Primary (citable) accession number: Q6R7H4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	July 5, 2004
Last modified:	May 29, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program