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P07201 (RIR2_SPISO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonucleoside-diphosphate reductase small chain

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase small subunit
p41
OrganismSpisula solidissima (Atlantic surf-clam)
Taxonomic identifier6584 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaHeteroconchiaVeneroidaMactroideaMactridaeSpisula

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384Ribonucleoside-diphosphate reductase small chain
PRO_0000190453

Sites

Active site1681 By similarity
Metal binding1301Iron 1 By similarity
Metal binding1611Iron 1 By similarity
Metal binding1611Iron 2 By similarity
Metal binding1641Iron 1 By similarity
Metal binding2241Iron 2 By similarity
Metal binding2581Iron 2 By similarity
Metal binding2611Iron 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P07201 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: 2F576F7BEA9297B0

FASTA38444,447
        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 

« Hide

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.
PIRRDSS2R. A22259.
S24585.

3D structure databases

ProteinModelPortalP07201.
SMRP07201. Positions 3-344.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

Gene3D1.10.620.20. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]
PANTHERPTHR23409. PTHR23409. 1 hit.
PfamPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR2_SPISO
AccessionPrimary (citable) accession number: P07201
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1993
Last modified: December 11, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways