P50646 (RIR1_BHV1C) 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 large subunit

Gene names

Name:

UL39

Organism

Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)

Taxonomic identifier

10323 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Varicellovirus › Bovine herpesvirus 1 › Bovine herpesvirus type 1.1

Virus host

Bos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length	787 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 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.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase large chain family.

Ontologies

Keywords
Biological process	DNA replication
Ligand	ATP-binding Nucleotide-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
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 – 787	787	Ribonucleoside-diphosphate reductase large subunit		PRO_0000187240
Regions
	Region	224 – 225	2	Substrate binding By similarity
	Region	436 – 440	5	Substrate binding By similarity
	Region	618 – 622	5	Substrate binding By similarity
Sites
	Active site	436	1	Proton acceptor By similarity
	Active site	438	1	Cysteine radical intermediate By similarity
	Active site	440	1	Proton acceptor By similarity
	Binding site	209	1	Substrate By similarity
	Binding site	255	1	Substrate; via amide nitrogen By similarity
	Site	225	1	Important for hydrogen atom transfer By similarity
	Site	453	1	Important for hydrogen atom transfer By similarity
	Site	762	1	Important for electron transfer By similarity
	Site	763	1	Important for electron transfer By similarity
	Site	782	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	785	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	225 ↔ 453		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50646 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 8DB0F6327862333E	FASTA	787	86,010
	10 20 30 40 50 60 MASDAFMQTA CPADAAEQLE AEHAEWAQLG CGAVPPPPAA ASRPSRAAVA AYVGEVVDRM 70 80 90 100 110 120 RAQSRADERV YVKCGQLVHL RVRARSVPLD DWLTSAELAL VSEVAEPVRA NRAFVEVSLR 130 140 150 160 170 180 YFELTEYATL RALGLQSALK YEEMYLAKLE GGAIESMGQF FVRIAATAAT WTMREPAFGR 190 200 210 220 230 240 ALVGEGATWC AVFNAYLTAL YRQLVVPATP IMLFAGRARG SLASCYLLNP QVSSSTEAVE 250 260 270 280 290 300 AITTEVARIL LNRGGIGISF QSFDRAVSRD CKRGIMGALK LLDSMAMAIN SDSERPTGIC 310 320 330 340 350 360 VYLEPWHCDV RAVLNMRGLL ARDESTRCDN LFSCLWVPDL LFDRYLAHLE GREGVVWTLF 370 380 390 400 410 420 DDRASHLSRL HGPAFTAEYE RLEREGLGVE TVPVQDLAFL IVRSIVMTGS PFVMFKDACN 430 440 450 460 470 480 RHYHMDTAGD ALTGSNLCTE IVQRASPDAH GVCNLASVNL PRCVREGEGG ALAFDFAALS 490 500 510 520 530 540 TAAATAAIFV NAMMLGGQYP TEKAARGVAR HRSLGIGFQG LHTLLLELGM DMLSPAARRL 550 560 570 580 590 600 NVEIAERLLL AVMATSATLC EYGCAPFEDF ARSKFARGLM PFDGYEGVVL SLPRAWARLR 610 620 630 640 650 660 EKVARHGLYN AQFVALMPTV SSSQVTEGSE GFSPVFTNMF SKVTMSGELL RPNLPLMRAL 670 680 690 700 710 720 RKHFTREASR LGAVRALDRE QWSVAAALGD LAPGHPLAKF KTAFEYDQER LIDLCADRAP 730 740 750 760 770 780 FVDQSQSMSL FVTEPMDGKV PASQIMNLLV YAYKKGLKTG LYYCKIRKAT NNGVFTGGDL VCSGCHL

References

[1]	"Sequence analysis of the UL39, UL38, and UL37 homologues of bovine herpesvirus 1 and expression studies of UL40 and UL39, the subunits of ribonucleotide reductase." Simard C., Langlois I., Styger D., Vogt B., Vlcek C., Chalifour A., Trudel M., Schwyzer M. Virology 212:734-740(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Gene contents in a 31-kb segment at the left genome end of bovine herpesvirus-1." Schwyzer M., Styger D., Vogt B., Lowery D.E., Simard C., LaBoissiere S., Misra V., Vlcek C., Paces V. Vet. Microbiol. 53:67-77(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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	Z54206 Genomic DNA. Translation: CAA90929.1. Z49078 Genomic DNA. Translation: CAA88900.1. AJ004801 Genomic DNA. Translation: CAA06094.1.
RefSeq	NP_045319.1. NC_001847.1.
3D structure databases
ProteinModelPortal	P50646.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1487390.
Phylogenomic databases
ProtClustDB	CLSP2509601.
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_BHV1C

Accession

Primary (citable) accession number: P50646

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program