P42491 (RIR1_ASFB7) 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

Ordered Locus Names:	Ba71V-045
ORF Names:	F778R

Organism

African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV) [Reference proteome]

Taxonomic identifier

10498 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Asfarviridae › Asfivirus › African swine fever virus

Virus host

Ornithodoros (relapsing fever ticks) [TaxID: 6937]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length	778 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. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity.
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.
Enzyme regulation	Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction By similarity.
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	Allosteric enzyme 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 – 778	778	Ribonucleoside-diphosphate reductase large subunit		PRO_0000187227
Regions
	Region	192 – 193	2	Substrate binding By similarity
	Region	419 – 423	5	Substrate binding By similarity
	Region	613 – 617	5	Substrate binding By similarity
Sites
	Active site	419	1	Proton acceptor By similarity
	Active site	421	1	Cysteine radical intermediate By similarity
	Active site	423	1	Proton acceptor By similarity
	Binding site	177	1	Substrate By similarity
	Binding site	221	1	Substrate; via amide nitrogen By similarity
	Site	193	1	Important for hydrogen atom transfer By similarity
	Site	200	1	Allosteric effector binding By similarity
	Site	230	1	Allosteric effector binding By similarity
	Site	439	1	Important for hydrogen atom transfer By similarity
	Site	747	1	Important for electron transfer By similarity
	Site	748	1	Important for electron transfer By similarity
	Site	773	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	776	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	193 ↔ 439		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P42491 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 9DB88008677A877F	FASTA	778	87,492
	10 20 30 40 50 60 METFFIETLA SDVYGKALNV DLDRLSQAQV KYTLQELISY CSALTILHYD YSTLAARLSV 70 80 90 100 110 120 YQLHQSTASS FSKAVRLQAA QSCSRLSPQF VDVVYKYKAI FDSYIDYNRD YKLSLLGIET 130 140 150 160 170 180 MKNSYLLKNK DGVIMERPQD AYMRVAIMIY GMGKVVNIKM ILLTYDLLSR HVITHASPTM 190 200 210 220 230 240 FNAGTKKPQL SSCFLLNVND NLENLYDMVK TAGIISGGGG GIGLCLSGIR AKNSFISGSG 250 260 270 280 290 300 LRSNGIQNYI MLQNASQCYA NQGGLRPGAY AVYLELWHQD IFTFLQMPRL KGQMAEQRLN 310 320 330 340 350 360 APNLKYGLWV PDLFMEILED QIHNRGDGTW YLFSPDQAPN LHKVFDLERS QHENAHREFK 370 380 390 400 410 420 KLYYQYVAEK RYTGVTTAKE IIKEWFKTVI QVGNPYIGFK DAINRKSNLS HVGTITNSNL 430 440 450 460 470 480 CIEVTIPCWE GDKAEQGVCN LAAVNLAAFI RENGYDYRGL IEASGNVTEN LDNIIDNGYY 490 500 510 520 530 540 PTEATRRSNM RHRPIGIGVF GLADVFASLK MKFGSPEAIA MDEAIHAALY YGAMRRSIEL 550 560 570 580 590 600 AKEKGSHPSF PGSAASKGLL QPDLWVRCGD LSSSWEERVA QTTQGVLTRK SWWQLRLAAM 610 620 630 640 650 660 QGVRNGYLTA LMPTATSSNS TGKNECFEPF TSNLYTRRTL SGEFIVLNKY LIDDLKEIDL 670 680 690 700 710 720 WTEAIQQQLL NAGGSIQHIL DIPAEIRDRY KTSREMNQKI LTKHAAARNP FVSQSMSLNY 730 740 750 760 770 YFYEPELSQV LTVLVLGWKK GLTTGSYYCH FSPGAGTQKK IIRNSEKACN ADCEACLL

References

[1]	"Analysis of the complete nucleotide sequence of African swine fever virus." Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C., Rodriguez J.F., Vinuela E. Virology 208:249-278(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U18466 Genomic DNA. Translation: AAA65275.1.
RefSeq	NP_042739.1. NC_001659.1.
3D structure databases
ProteinModelPortal	P42491.
ModBase	Search...
Proteomic databases
PRIDE	P42491.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1488810.
Phylogenomic databases
ProtClustDB	CLSP2509774.
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
InterPro	IPR013346. NrdE_NrdA. IPR000788. RNR_lg_C. IPR013509. RNR_lsu_N. IPR008926. RNR_R1-su_N. [Graphical view]
Pfam	PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
SUPFAM	SSF48168. Ribonucleo_red_N. 1 hit.
TIGRFAMs	TIGR02506. NrdE_NrdA. 1 hit.
PROSITE	PS00089. RIBORED_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR1_ASFB7

Accession

Primary (citable) accession number: P42491

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program