P50642 (RIR1_EHV4) 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
Organism	Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus)
Taxonomic identifier	10333 [NCBI]
Taxonomic lineage	Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Varicellovirus › Equid herpesvirus 4
Virus host	Equus caballus (Horse) [TaxID: 9796]

Protein attributes

Sequence length	789 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 (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
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 – 789	789	Ribonucleoside-diphosphate reductase large subunit		PRO_0000187242
Regions
	Region	222 – 223	2	Substrate binding By similarity
	Region	435 – 439	5	Substrate binding By similarity
	Region	620 – 624	5	Substrate binding By similarity
Sites
	Active site	435	1	Proton acceptor By similarity
	Active site	437	1	Cysteine radical intermediate By similarity
	Active site	439	1	Proton acceptor By similarity
	Binding site	207	1	Substrate By similarity
	Binding site	253	1	Substrate; via amide nitrogen By similarity
	Site	223	1	Important for hydrogen atom transfer By similarity
	Site	452	1	Important for hydrogen atom transfer By similarity
	Site	764	1	Important for electron transfer By similarity
	Site	765	1	Important for electron transfer By similarity
	Site	784	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	787	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	223 ↔ 452		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50642 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 7CD9A24F3147988B	FASTA	789	88,047
	10 20 30 40 50 60 MALDFLSTDC PLGIVSDIIS NVNTIKEYGY SSELSTTLAP RPSREQVLEY ITRVVDKLKP 70 80 90 100 110 120 LCRVDERLYI ACGELVHLRI KARNTDLKYW LKSSEIDLSD VVEQAILEHI DFVQKTLNSF 130 140 150 160 170 180 ETSEYRDLCS LGLQSALKYE EMYLAKMRGG RLESMGQFFL RLATTATHYT MEQPAMARVL 190 200 210 220 230 240 VSGEVGWTYI FRAFFTALAG QVVIPATPIM LFGGRDCGSM ASCYLLNPRV TDMNSAIPAL 250 260 270 280 290 300 MEEVGPILCN RGGIGLSLQR FNTPPTEGCS RGVMALLKLL DSMTMAINSD GERPTGVCVY 310 320 330 340 350 360 FEPWHADIRA ILNMRGMLAR DETVRCDNIF ACMWTPDLFF DRYQRYVDGE SGIMWTLFDD 370 380 390 400 410 420 TASHLCHMYG NDFTREYERL ERCGFGIDAI PIQDMAFIIV RSAVMTGSPF LMFKDACNRH 430 440 450 460 470 480 YHFDMRQRGA IMGSNLCTEI IQHADETQNG VCNLASINLP KCLALPPPNI AGVPYFDFAA 490 500 510 520 530 540 LGRAAATATI FVNAMMCAST YPTVKSQKGV EENRSLGLGI QGLHTTFLML DLDMASPEAH 550 560 570 580 590 600 QLNKQIAERL LLNSMKASAT LCKLGMQPFK GFEDSKYSRG ELPFDAYPNV TLTNRNAWRR 610 620 630 640 650 660 LRTDIKQYGL YNSQFVAYMP TVSSSQVTES SEGFSPVYTN LFSKVTATGE VLRPNVLLMR 670 680 690 700 710 720 TIRSIFPQEC ARLQALSTLE AAKWSVVGAF GDLPVGHPLS KFKTAFEYDQ TMLINMCADR 730 740 750 760 770 780 AAFVDQSQSM SLFITEPADG KLPASRIMNL LVHAYKRGLK TGMYYCKIKK ATNNGVFVGG DLVCTSCSL

References

[1]	"Sequences of the ribonucleotide reductase-encoding genes of equine herpesvirus 4." Riggio M.P., Onions D.E. Gene 143:217-222(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75354 Genomic DNA. Translation: CAA53100.1.
3D structure databases
ProteinModelPortal	P50642.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-6732615.
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_EHV4

Accession

Primary (citable) accession number: P50642

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program