O15910 (RIR2_TRYBB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase small chain
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase R2 subunit
Ribonucleotide reductase small subunit

Gene names

Name:	RNR2
Synonyms:	NRDB

Organism

Trypanosoma brucei brucei

Taxonomic identifier

5702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Trypanozoon › Trypanosoma brucei

Protein attributes

Sequence length	337 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.
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	Heterodimer of a large and a small subunit.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase small chain family.

Ontologies

Keywords
Biological process	DNA replication
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway deoxyribonucleoside diphosphate metabolic 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 – 337	337	Ribonucleoside-diphosphate reductase small chain		PRO_0000190460
Sites
	Active site	123	1	By similarity
	Metal binding	85	1	Iron 1 By similarity
	Metal binding	116	1	Iron 1 By similarity
	Metal binding	116	1	Iron 2 By similarity
	Metal binding	119	1	Iron 1 By similarity
	Metal binding	178	1	Iron 2 By similarity
	Metal binding	212	1	Iron 2 By similarity
	Metal binding	215	1	Iron 2 By similarity
Experimental info
	Sequence conflict	8 – 10	3	CSR → RSA in CAA71741. Ref.2
	Sequence conflict	43	1	E → K in CAA71741. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O15910 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: BD39919280C65CAE	FASTA	337	39,009
	10 20 30 40 50 60 MPPKSHKCSR KEGEVEEPLL TENPDRYVIF PIKYPDIWQK YKEAESSIWT VEEIDLGNDM 70 80 90 100 110 120 TDWEKLDDGE RHFIKHVLAF FAASDGIVLE NLAERFMCEV QVPEVRCFYG FQIAMENIHS 130 140 150 160 170 180 ETYSVLIDTY VVDPDEKQRL LHAIRTIPCI EKKAKWAIEW IGSQTSFPTR LVAFAAVEGI 190 200 210 220 230 240 FFSGSFCAIF WLKKRGLMPG LTFSNELISR DEGLHTDFAC LLYEKYIVNK LPRDRVLEII 250 260 270 280 290 300 CNAVSIEREF ICDALPVRLI GMNSQLMTQY IEFVADRLLV SLGYDRHYNS KNPFDFMDMI 310 320 330 SLQGKTNFFE KKVGEYQKAG VMSSERSSKV FSLDADF

References

[1]	"Cloning and characterization of the R1 and R2 subunits of ribonucleotide reductase from Trypanosoma brucei." Hofer A., Schmidt P.P., Graslund A., Thelander L. Proc. Natl. Acad. Sci. U.S.A. 94:6959-6964(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 427.
[2]	"Cloning, sequencing and expression of ribonucleotide reductase R2 from Trypanosoma brucei." Dormeyer M., Schoneck R., Dittmar G.A.G., Krauth-Siegel R.L. FEBS Lett. 414:449-453(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U80911 mRNA. Translation: AAB70705.1. Y10768 Genomic DNA. Translation: CAA71741.1.
3D structure databases
ProteinModelPortal	O15910.
SMR	O15910. Positions 16-298.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG0208.
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. IPR000358. RNR_small. [Graphical view]
PANTHER	PTHR23409. PTHR23409. 1 hit.
Pfam	PF00268. Ribonuc_red_sm. 1 hit. [Graphical view]
SUPFAM	SSF47240. Ferritin/RR_like. 1 hit.
PROSITE	PS00368. RIBORED_SMALL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR2_TRYBB

Accession

Primary (citable) accession number: O15910
Secondary accession number(s): O15880

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)