Q6GZT8 (RIR1_FRG3G) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative ribonucleoside-diphosphate reductase large subunit
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase large subunit

Gene names

ORF Names:

FV3-038R

Organism

Frog virus 3 (isolate Goorha) (FV-3) [Reference proteome]

Taxonomic identifier

654924 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Iridoviridae › Ranavirus › Frog virus 3

Virus host

Ambystoma (mole salamanders) [TaxID: 8295]
Hyla versicolor (chameleon treefrog) [TaxID: 30343]
Notophthalmus viridescens (Eastern newt) (Triturus viridescens) [TaxID: 8316]
Rana pipiens (Northern leopard frog) [TaxID: 8404]
Rana sylvatica (Wood frog) [TaxID: 45438]

Protein attributes

Sequence length	565 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
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	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 – 565	565	Putative ribonucleoside-diphosphate reductase large subunit		PRO_0000410591
Regions
	Region	74 – 75	2	Substrate binding By similarity
	Region	256 – 260	5	Substrate binding By similarity
	Region	400 – 404	5	Substrate binding By similarity
Sites
	Active site	256	1	Proton acceptor By similarity
	Active site	258	1	Cysteine radical intermediate By similarity
	Active site	260	1	Proton acceptor By similarity
	Binding site	60	1	Substrate By similarity
	Binding site	103	1	Substrate; via amide nitrogen By similarity
	Site	75	1	Important for hydrogen atom transfer By similarity
	Site	82	1	Allosteric effector binding By similarity
	Site	112	1	Allosteric effector binding By similarity
	Site	273	1	Important for hydrogen atom transfer By similarity
	Site	534	1	Important for electron transfer By similarity
	Site	535	1	Important for electron transfer By similarity
	Site	560	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	563	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	75 ↔ 273		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6GZT8 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 790187621FAFC2E7	FASTA	565	62,363
	10 20 30 40 50 60 MTSAVSFPIT SQASDMLSKF YGSDLGSLYG TLAEKYSGGK PELAEKLRDY ACKGWFGYSS 70 80 90 100 110 120 PILTSVTGSG LPISCFLLYV PDTIEGLVDH TSELRWLSVM GGGVAGHWDD VRGPSAKSCG 130 140 150 160 170 180 TIPFLHTVDA DMSAYWQGKV RRGSYAAYMS ISHPDLIEFI TMRTPTGDVN RKNLNLHHGV 190 200 210 220 230 240 NITDTFMRCV ERGENWDLVD PKSGAVAHTV SARELWERIL ETRFRTGEPY LNFIDTANRG 250 260 270 280 290 300 LHPALKRKGL KIRGSNLCNE IHLPTAADRT AVCCLSSVNL ERYDEWRETD LVECLVEMLD 310 320 330 340 350 360 NVIQTFVDEA PLKTPHTARA VRSAAGERSI GLGAMGWARY LQKHRIPFDS EEAVRLTGII 370 380 390 400 410 420 FRGIKSAAVR ATRALAKERG EAPDLTGYGV RNAHLLAVAP NANSALLLGT SPSVEPEIGA 430 440 450 460 470 480 AYVHRTRVGS HQAVNPYLKR DLESLGLDTE EVWDSIVSNK GSVQHIAALP DSLKKVYKTS 490 500 510 520 530 540 FEMDQRVIVR QAAERQRHLC QGQSLNLFFP IGADKTNLSD VHRLAWKSGC KGLYYLRTCA 550 560 GRTGHKIFEA KKNPEKTEEC TACQG

References

[1]	"Comparative genomic analyses of frog virus 3, type species of the genus Ranavirus (family Iridoviridae)." Tan W.G., Barkman T.J., Gregory Chinchar V., Essani K. Virology 323:70-84(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY548484 Genomic DNA. Translation: AAT09697.1.
RefSeq	YP_031616.1. NC_005946.1.
3D structure databases
ProteinModelPortal	Q6GZT8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2947817.
Phylogenomic databases
ProtClustDB	CLSP2511488.
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
InterPro	IPR000788. RNR_lg_C. [Graphical view]
Pfam	PF02867. Ribonuc_red_lgC. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
ProtoNet	Search...

Entry information

Entry name

RIR1_FRG3G

Accession

Primary (citable) accession number: Q6GZT8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 28, 2011
Last sequence update:	July 19, 2004
Last modified:	January 9, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program