Q9C167 (RIR2_NEUCR) 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 small subunit

Gene names

Name:	rnr-2
Synonyms:	rnr2
ORF Names:	NCU07887

Organism

Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]

Taxonomic identifier

367110 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora › Neurospora crassa

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity.
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
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 – 410	410	Ribonucleoside-diphosphate reductase small chain		PRO_0000190462
Sites
	Active site	184	1	By similarity
	Metal binding	146	1	Iron 1 By similarity
	Metal binding	177	1	Iron 1 By similarity
	Metal binding	177	1	Iron 2 By similarity
	Metal binding	180	1	Iron 1 By similarity
	Metal binding	240	1	Iron 2 By similarity
	Metal binding	274	1	Iron 2 By similarity
	Metal binding	277	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9C167 [UniParc]. Last modified December 1, 2001. Version 2. Checksum: FAC2314C4959BE8E	FASTA	410	46,698
	10 20 30 40 50 60 MSVQTSPSKQ VTSGIQNLNM DSPAKKLDFG ATDKENKPFD EDLAKLEAEI DAEHNANKKA 70 80 90 100 110 120 AEAKKMAPTL KPEEANEPLL TENPQRFVLF PIKYHEIWQM YKKAEASFWT AEEIDLSKDL 130 140 150 160 170 180 HDWNNRLNDD EKFFISHILA FFAASDGIVN ENLVERFSGE VQIPEARCFY GFQIMMENIH 190 200 210 220 230 240 SETYSLLIDT YIKEPSQRTY LFNAIDTIPC IRKKADWALR WITDKSSTFA QRLVAFAAVE 250 260 270 280 290 300 GIFFSGAFAS IFWLKKRGLM PGLTFSNELI SRDEGLHTDF ACLLFSHLNN RPSKQLIQEI 310 320 330 340 350 360 IVDAVRIEQE FLTEALPCAL LGMNADLMKQ YIEFVADRLL VALGNEKIYR STNPFDFMEN 370 380 390 400 410 ISLGGKTNFF EKRVGDYQKA GVMNSTKKAD ADAEVAKNEN GGDFTFDEDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Suppressor of un-24 temperature sensitive mutation." Kotierk M., Smith M.L. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FGSC 1131.
[2]	"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY027867 Genomic DNA. Translation: AAK14804.2. AABX02000040 Genomic DNA. Translation: EAA33584.1.
RefSeq	XP_962820.1. XM_957727.2.
UniGene	Ncr.16250.
3D structure databases
ProteinModelPortal	Q9C167.
SMR	Q9C167. Positions 32-360.
ModBase	Search...
Protein-protein interaction databases
STRING	5141.NCU07887.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	EFNCRT00000007516; EFNCRP00000007506; EFNCRG00000007504.
GeneID	3878959.
KEGG	ncr:NCU07887.
Phylogenomic databases
eggNOG	COG0208.
HOGENOM	HOG000255975.
KO	K10808.
OMA	ICNRRCQ.
OrthoDB	EOG4QZBVT.
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_NEUCR

Accession

Primary (citable) accession number: Q9C167
Secondary accession number(s): Q7RVY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program