O36411 (RIR1_ALHV1) 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

Organism

Alcelaphine herpesvirus 1 (strain C500) (AIHV-1) (Malignant catarrhal fever virus) [Reference proteome]

Taxonomic identifier

654901 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Macavirus › Alcelaphine herpesvirus 1

Virus host

Connochaetes taurinus (Brindled gnu) [TaxID: 9927]

Protein attributes

Sequence length	780 AA.
Sequence status	Complete.
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 By similarity.
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 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 – 780	780	Ribonucleoside-diphosphate reductase large subunit		PRO_0000405696
Regions
	Region	192 – 193	2	Substrate binding By similarity
	Region	393 – 397	5	Substrate binding By similarity
	Region	595 – 599	5	Substrate binding By similarity
Sites
	Active site	393	1	Proton acceptor By similarity
	Active site	395	1	Cysteine radical intermediate By similarity
	Active site	397	1	Proton acceptor By similarity
	Binding site	177	1	Substrate By similarity
	Binding site	223	1	Substrate; via amide nitrogen By similarity
	Site	193	1	Important for hydrogen atom transfer By similarity
	Site	409	1	Important for hydrogen atom transfer By similarity
	Site	726	1	Important for electron transfer By similarity
	Site	727	1	Important for electron transfer By similarity
	Site	776	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	779	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	193 ↔ 409		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	O36411 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 0B4C197AB8D76DDC	FASTA	780	87,362
	10 20 30 40 50 60 MASAEATPQQ QIDQLKVNAG WDMKSNIKAG LLHHEEMEKK ATKTVTEYIE KFADVLEENV 70 80 90 100 110 120 LRFLQDNAEM LELCIYMYEQ LPAYKAVKSR GILSAKRFYD TYVLRTADGS CYESVSHCFM 130 140 150 160 170 180 RIAAFCTVQV LTNSALKITI LYLGRDKLFK DLPCSPTMDL FIYFFSPLSH QLVCCATPIM 190 200 210 220 230 240 RSAGLRDANL ASCFLINPDL STEKSTTTAL LQELTMLLSA KSGVGCNVTS FGVDEKCIQS 250 260 270 280 290 300 CVGLINSQVE FFNDQNPRPV SVAAYMEVWH SQIQEFLAVK LPENPSRCAS IYQGLCIPKL 310 320 330 340 350 360 FFEKFIEDPG QNWYLFKPEK SGNLANLYGD EFRSEYERLV GIGCYADAIP IKSLMFLIIN 370 380 390 400 410 420 TIIKTGSPYI IYKEACNEHH WKNMEGCAIA SANLCAEVIQ YPGADVSTCN LANVCLPMCL 430 440 450 460 470 480 VTVSNDSHSP LEKTYCGNVI ESQAVSGVGF SMPILHAAVE VAVFLVNCAI AGGKCVTPGM 490 500 510 520 530 540 ERGQRERSMG IGVHGLADVF AEMGYSYLDE RAARLDVEIF ENMYFRAVKT SNNICRLGGG 550 560 570 580 590 600 RPFEGWGESK LRHGFFHWQG WEDVNLSIPI TEWEKLSRRC ISSGVYNSQF IALMPTVGSS 610 620 630 640 650 660 LLTGFSESYY PYFANISSKV SSKEEVMKPN MTFWNRVSKE DLDTVRFFSG DVALFPEPLK 670 680 690 700 710 720 EKYSLFLSAF DYCAEKQLAR ARLRAPFVDQ SQSHSFHLKE ENVVSARFLK DLILSGYTLG 730 740 750 760 770 780 LKTIMYYCKV KKQSTMSSFQ CLRDQNKSEM TGNDQGVEPE SYIKCTAAGG ETSEACLHCQ

References

[1]	"Primary structure of the alcelaphine herpesvirus 1 genome." Ensser A., Pflanz R., Fleckenstein B. J. Virol. 71:6517-6525(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF005370 Genomic DNA. Translation: AAC58108.1.
PIR	T03156.
RefSeq	NP_065560.1. NC_002531.1.
3D structure databases
ProteinModelPortal	O36411.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	911785.
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_ALHV1

Accession

Primary (citable) accession number: O36411

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 8, 2011
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program