Reviewed, UniProtKB/Swiss-Prot Q01037 (RIR1_SHV21)

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) [Complete proteome]

Taxonomic identifier

10383 [NCBI]

Taxonomic lineage

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

Virus host

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

Protein attributes

Sequence length	767 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Heterodimer of a large and a small chain.
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
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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 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
Sites
	Active site	192	1	Hydrogen atom transfer By similarity
	Active site	392	1	Proton acceptor By similarity
	Active site	394	1	Proton acceptor By similarity
	Active site	396	1	Proton acceptor By similarity
	Active site	408	1	Hydrogen atom transfer By similarity
	Active site	709	1	Electron transfer By similarity
	Active site	710	1	Electron transfer By similarity
	Site	200	1	Allosteric effector binding By similarity
	Site	763	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	766	1	Interacts with thioredoxin/glutaredoxin By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q01037-1 [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: 1321287] [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: 1314457] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X64346 Genomic DNA. Translation: CAA45684.1. M86409 Genomic DNA. Translation: AAA46137.1.
RefSeq	NP_040263.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1682460.
Family and domain databases
InterPro	IPR013346. NrdE_NrdA. IPR013509. Ribncl_Rdtase_lsu_N. IPR000788. Ribncl_red_lg_C. [Graphical view]
PANTHER	PTHR11573. Ribncl_red_lg_C. 1 hit.
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:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)