P07201 (RIR2_SPISO) 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 p41
Organism	Spisula solidissima (Atlantic surf-clam)
Taxonomic identifier	6584 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Mollusca › Bivalvia › Heteroconchia › Veneroida › Mactroidea › Mactridae › Spisula

Protein attributes

Sequence length	384 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.
Miscellaneous	There is no sign of synthesis of a corresponding large subunit after fertilization. The authors suspect that the unfertilized oocytes contain a stockpile of large subunits ready for combination with newly made small subunits.
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 – 384	384	Ribonucleoside-diphosphate reductase small chain		PRO_0000190453
Sites
	Active site	168	1	By similarity
	Metal binding	130	1	Iron 1 By similarity
	Metal binding	161	1	Iron 1 By similarity
	Metal binding	161	1	Iron 2 By similarity
	Metal binding	164	1	Iron 1 By similarity
	Metal binding	224	1	Iron 2 By similarity
	Metal binding	258	1	Iron 2 By similarity
	Metal binding	261	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P07201 [UniParc]. Last modified April 1, 1993. Version 2. Checksum: 2F576F7BEA9297B0	FASTA	384	44,447
	10 20 30 40 50 60 MLSINTTRKE NELSGNLGKM KITEENKPKK VLGEITNFQR STQKTPLKQE IKPVVKKSQQ 70 80 90 100 110 120 VEPLLADNPR RFVVLPIQYH DIWKMYKKAE ASFWTAEEVD LSKDMAHWES LKKEEKHFIS 130 140 150 160 170 180 HVLAFFAASD GIVNENLVER FSKEVQVTEA RCFYGFQIAM ENIHSEMYSL LIDTYIKDPQ 190 200 210 220 230 240 ERDFLFNAIE TMPCVKEKAD WAMRWINDDS SSYAERVVAF AAVEGIFFSG SFASIFWLKK 250 260 270 280 290 300 RGIMPGLTFS NELISRDEGL HCDFACLMFS HLVNKPSQER IHQIIDEAVK IEQVFLTEAL 310 320 330 340 350 360 PCRLIGMNCD LMRQYIEFVA DRLLLELKCD KLYNKENPFD FMEHISLEGK TNFFEKRVGE 370 380 YQKMGVMSGG NTGDSHAFTL DADF

References

[1]	"Maternal mRNA from clam oocytes can be specifically unmasked in vitro by antisense RNA complementary to the 3'-untranslated region." Standart N.M., Dale M., Stewart E., Hunt T. Genes Dev. 4:2157-2168(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The small subunit of ribonucleotide reductase is encoded by one of the most abundant translationally regulated maternal RNAs in clam and sea urchin eggs." Standart N.M., Bray S.J., George E.L., Hunt T., Ruderman J.V. J. Cell Biol. 100:1968-1976(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-384.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X55125 mRNA. Translation: CAA38919.1. X02471 mRNA. Translation: CAA26307.1.
PIR	RDSS2R. A22259. S24585.
3D structure databases
ProteinModelPortal	P07201.
SMR	P07201. Positions 3-344.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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_SPISO

Accession

Primary (citable) accession number: P07201

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)