P26685 (RIR1_ASFM2) 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:

Mal-053

Organism

African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV)

Taxonomic identifier

10500 [NCBI]

Taxonomic lineage

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

Virus host

Ornithodoros (relapsing fever ticks) [TaxID: 6937]
Phacochoerus aethiopicus (Warthog) [TaxID: 85517]
Phacochoerus africanus (Warthog) [TaxID: 41426]
Potamochoerus larvatus (Bushpig) [TaxID: 273792]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length	779 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
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 – 779	779	Ribonucleoside-diphosphate reductase large subunit		PRO_0000187228
Regions
	Region	193 – 194	2	Substrate binding By similarity
	Region	420 – 424	5	Substrate binding By similarity
	Region	614 – 618	5	Substrate binding By similarity
Sites
	Active site	420	1	Proton acceptor By similarity
	Active site	422	1	Cysteine radical intermediate By similarity
	Active site	424	1	Proton acceptor By similarity
	Binding site	178	1	Substrate By similarity
	Binding site	222	1	Substrate; via amide nitrogen By similarity
	Site	194	1	Important for hydrogen atom transfer By similarity
	Site	201	1	Allosteric effector binding By similarity
	Site	231	1	Allosteric effector binding By similarity
	Site	440	1	Important for hydrogen atom transfer By similarity
	Site	748	1	Important for electron transfer By similarity
	Site	749	1	Important for electron transfer By similarity
	Site	774	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	777	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	194 ↔ 440		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P26685 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 88A3D0C8D5D10819	FASTA	779	87,388
	10 20 30 40 50 60 MENFFIVKKL ASATYGKALN VDLNKLLQAL NHHSLQGLIS YCSALTILHY DYSTLAARLS 70 80 90 100 110 120 VYLLHQSTAS SFSKAVSLQA AQSCSRLSSH FVDVVYKYKA IFDSYIDYSR DYKLSLLGIE 130 140 150 160 170 180 TMKNSYLLKN KDGVIMERPQ DAYMRVAIMI HGMGRVVNMK MILLTYDLLS RHVITHASPT 190 200 210 220 230 240 MFNAGTKKPQ LSSCFLLNVN DNLENLYDMV KTAGIISGGG GGIGLCLSGI RAKNSFISGS 250 260 270 280 290 300 GLRSNGIQNY IVLQNASQCY ANQGGLRPGA YAVYLELWHQ DIFTFLQMPR LKGQMAEQRL 310 320 330 340 350 360 NAPNLKYGLW VPDLFMEILE DQIHNRGDGT WYLFSPDQAP NLHKVFDLER SQHENAHREF 370 380 390 400 410 420 KKLYYQYVAE KRYTGVTTAK EIIKEWFKTV VQVGNPYIGF KDAINRKSNL SHVGTITNSN 430 440 450 460 470 480 LCIEITIPCW EGNEAEQGVC NLAAVNLAAF IRESSYDYRG LIEAAGNVTE NLDNIIDNGY 490 500 510 520 530 540 YPTEATRRSN MRHRPIGIGV FGLADVFASL KMKFGSPEAI AIDEAIHAAL YYGAMRRSIE 550 560 570 580 590 600 LAKEKGSHPS FPGSAASKGL LQPDLWVRCG DLIPSWENRV AQTTQGVLTP KKWWQLRLAA 610 620 630 640 650 660 IQGVRNGYLT ALMPTATSSN STGKNECFEP FTSNLYTRRT LSGEFIILNK YLMDDLEEIN 670 680 690 700 710 720 LWSEDIQQQL LNAGGSIQHI LDIPAEIRER YKTSREMNQK ILTKHAAARN PFVSQSMSLN 730 740 750 760 770 YYFYEPELSQ VLTVLVLGWK KGLTTGSYYC HFSPGAGTQK KIIRNSEKAC NADCEACLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequences of the ribonucleotide reductase genes from African swine fever virus show considerable homology with those of the orthopoxvirus, vaccinia virus." Boursnell M., Shaw K., Yanez R.J., Vinuela E., Dixon L. Virology 184:411-416(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"African swine fever virus genomes." Kutish G.F., Rock D.L. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64728 Genomic DNA. Translation: AAA42732.1.
PIR	WMVZAL. A40568.
3D structure databases
ProteinModelPortal	P26685.
ModBase	Search...
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. 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_ASFM2

Accession

Primary (citable) accession number: P26685

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program