Q01037 (RIR1_SHV21) 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:	61
Synonyms:	EELF2

Organism

Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri) [Reference proteome]

Taxonomic identifier

10383 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Rhadinovirus › Saimiriine herpesvirus 2

Virus host

Saimiri sciureus (Common squirrel monkey) [TaxID: 9521]

Protein attributes

Sequence length	767 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
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 – 767	767	Ribonucleoside-diphosphate reductase large subunit		PRO_0000187243
Regions
	Region	191 – 192	2	Substrate binding By similarity
	Region	392 – 396	5	Substrate binding By similarity
	Region	578 – 582	5	Substrate binding By similarity
Sites
	Active site	392	1	Proton acceptor By similarity
	Active site	394	1	Cysteine radical intermediate By similarity
	Active site	396	1	Proton acceptor By similarity
	Binding site	176	1	Substrate By similarity
	Binding site	222	1	Substrate; via amide nitrogen By similarity
	Site	192	1	Important for hydrogen atom transfer By similarity
	Site	408	1	Important for hydrogen atom transfer By similarity
	Site	709	1	Important for electron transfer By similarity
	Site	710	1	Important for electron transfer By similarity
	Site	763	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	766	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	192 ↔ 408		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q01037 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: FE5922B11FFCA6DF	FASTA	767	87,216
	10 20 30 40 50 60 MSQETIISNL IDMLKVSAGW DREANEISGR LFHKLMDMSS TETISQYMSL FGPLLEPHIL 70 80 90 100 110 120 EFIQNYEQEI DEVCLEYRAS YDFMCLRNCG ILPAKRFYDT YVLPPRTEMN GKYESIPHFF 130 140 150 160 170 180 ARIAAYCAWN CIMCEPLKDT LVYVQKRDWN VEIKTDMQIF KYFYKVISSQ LVCCATPVMR 190 200 210 220 230 240 SAGVAGENLS SCFIIAPTLD TEKSTISSIF GELAPLLASR SGVGVDVTKF SFGGKNIHSC 250 260 270 280 290 300 LKLINAQVEF FNDKSVRPVS VATYIEVWHC QIHEFLSAKL PENPDRCNSI FQGVCVPSLF 310 320 330 340 350 360 FKMYESDPNG LWYLFDPQDA PNLTRLYGLE FEEEYLRLVS EKKYKQSVTL KSLMFSLINT 370 380 390 400 410 420 IIKTGSPYVI SKEAMNKHHW YETQGEAINC SNLCAEIVQQ PKQFTSTCNL ANVCLPKCLN 430 440 450 460 470 480 SSNFPYTCSN TAQFDFSKLE YAVQAAVFII NACILSPSPT SSATVGQRER SMGIGCHGLA 490 500 510 520 530 540 DVFSEMGYGY LDLESECLDR DIFETMYYTA VKTSSEICSV GKGQPFAGFR KSKLAHGVFH 550 560 570 580 590 600 WATWDAMPQR VPMKQWIHLQ DNIKKFGVFN SQFIALMPTA GTSQLTGYTD SFYPYFANMS 610 620 630 640 650 660 SKVSNKEEIM KPNITFLKNV KPQDLCTVRF YGGDVSMMPE DVSTRYKHFL TAFDYCPEAQ 670 680 690 700 710 720 MRRASIRAPY VDQSQSLTLF LTEENVQSAK YLKDLLLLGF RLGLKTIMYY CRVKKTTKLL 730 740 750 760 QLECLKLDEH TKKDAQIVLA DLARELPDSH KTEDACPLDQ SECIACQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the herpesvirus saimiri genome." Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B., Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B., Honess R.W. J. Virol. 66:5047-5058(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Analysis of nucleotide sequence of the rightmost 43 kbp of herpesvirus saimiri (HVS) L-DNA: general conservation of genetic organization between HVS and Epstein-Barr virus." Nicholas J., Cameron K.R., Coleman H., Newman C., Honess R.W. Virology 188:296-310(1992) [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	X64346 Genomic DNA. Translation: CAA45684.1. M86409 Genomic DNA. Translation: AAA46137.1.
RefSeq	NP_040263.1. NC_001350.1.
3D structure databases
ProteinModelPortal	Q01037.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1682460.
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_SHV21

Accession

Primary (citable) accession number: Q01037

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program