O64174 (BNRDF_BPSPB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase subunit beta
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase small subunit

Gene names

Name:	bnrdF
Synonyms:	yosP

Organism

Bacillus phage SPbeta (Bacillus phage SPBc2) (Bacteriophage SP-beta) [Reference proteome]

Taxonomic identifier

66797 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Siphoviridae › Spbetalikevirus

Virus host

Bacillus pumilus (Bacillus mesentericus) [TaxID: 1408]
Bacillus subtilis [TaxID: 1423]

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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.
Cofactor	Binds 2 iron ions per subunit By similarity.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Tetramer of two alpha and two beta subunits By similarity.
Miscellaneous	This gene has an intron within which is encoded yosQ, a putative homing endonuclease.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase small chain family.

Ontologies

Keywords
Biological process	DNA replication
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro deoxyribonucleotide biosynthetic process Inferred from electronic annotation. Source: InterPro
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 transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 329	329	Ribonucleoside-diphosphate reductase subunit beta		PRO_0000389011
Sites
	Active site	105	1	By similarity
	Metal binding	66	1	Iron 1 By similarity
	Metal binding	97	1	Iron 1 By similarity
	Metal binding	97	1	Iron 2 By similarity
	Metal binding	101	1	Iron 1 By similarity
	Metal binding	164	1	Iron 2 By similarity
	Metal binding	198	1	Iron 2 By similarity
	Metal binding	201	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	O64174 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: EC36E9DFC12BD269	FASTA	329	38,181
	10 20 30 40 50 60 MTKIYDAANW SKHEDDFTQM FYNQNVKQFW LPEEIALNGD LLTWKYLGKN EQDTYMKVLA 70 80 90 100 110 120 GLTLLDTEQG NTGMPIVAEH VDGHQRKAVL NFMAMMENAV HAKSYSNIFL TLAPTEQINE 130 140 150 160 170 180 VFEWVKNNRF LQKKARTIVS VYKTIKKNDE ISLFKGMVAS VFLESFLFYS GFYYPLYFYG 190 200 210 220 230 240 QGKLMQSGEI INLIIRDEAI HGVYVGLLAQ EIYKKQTPQK QKELYAWALN LLQELYENEL 250 260 270 280 290 300 EYTEDVYDQV GLAPDVKKFI RYNANKALNN LGFDHWFEEE DVNPIVINGL NTKTKSHDFF 310 320 STKGNGYKKA TVEPLKDSDF IFTEKGCIQ

References

[1]

"Introns and intein coding sequence in the ribonucleotide reductase genes of Bacillus subtilis temperate bacteriophage SPbeta." Lazarevic V., Soldo B., Duesterhoeft A., Hilbert H., Maueel C., Karamata D. Proc. Natl. Acad. Sci. U.S.A. 95:1692-1697(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SPLICING.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF020713 Genomic DNA. Translation: AAC13135.1.
PIR	T12926.
RefSeq	NP_046714.1. NC_001884.1.
3D structure databases
ProteinModelPortal	O64174.
SMR	O64174. Positions 5-286.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1261446.
Phylogenomic databases
ProtClustDB	CLSP2494601.
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
Gene3D	1.10.620.20. 1 hit.
InterPro	IPR009078. Ferritin-like_SF. IPR012348. RNR-rel. IPR026494. RNR_1b_NrdF. IPR026023. RNR_bsu_prok. IPR000358. RNR_small. [Graphical view]
PANTHER	PTHR23409. PTHR23409. 1 hit.
Pfam	PF00268. Ribonuc_red_sm. 1 hit. [Graphical view]
PIRSF	PIRSF000355. NrdB. 1 hit.
SUPFAM	SSF47240. Ferritin/RR_like. 1 hit.
TIGRFAMs	TIGR04171. RNR_1b_NrdF. 1 hit.
PROSITE	PS00368. RIBORED_SMALL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BNRDF_BPSPB

Accession

Primary (citable) accession number: O64174

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 24, 2009
Last sequence update:	August 1, 1998
Last modified:	May 29, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program