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Protein

Ribulose bisphosphate carboxylase small chain

Gene

SELMODRAFT_186173

Organism
Selaginella moellendorffii (Spikemoss)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.UniRule annotationSAAS annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotationSAAS annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotationSAAS annotation

GO - Molecular functioni

  1. monooxygenase activity Source: UniProtKB-KW
  2. ribulose-bisphosphate carboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbon fixation Source: UniProtKB-KW
  2. photorespiration Source: UniProtKB-KW
  3. photosynthesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotation, MonooxygenaseUniRule annotationSAAS annotation, Oxidoreductase

Keywords - Biological processi

Carbon dioxide fixationUniRule annotationSAAS annotation, PhotorespirationUniRule annotation, PhotosynthesisUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Gene namesi
ORF Names:SELMODRAFT_186173Imported
OrganismiSelaginella moellendorffii (Spikemoss)Imported
Taxonomic identifieri88036 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaLycopodiidaeSelaginellalesSelaginellaceaeSelaginella
ProteomesiUP000001514 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

  1. plastid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

PlastidUniRule annotation

Interactioni

Subunit structurei

8 large chains + 8 small chains.UniRule annotationSAAS annotation

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.UniRule annotation

Phylogenomic databases

InParanoidiD8T7L5.
KOiK01602.
OMAiEVINTKH.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamiPF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.

Sequencei

Sequence statusi: Complete.

D8T7L5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTGAASSAV IPMAALSTPV APKVPGFTGL KATTALTANK GGLQWSQKTV
60 70 80 90 100
ANGSRVSCML TWTPYNNPRF ETLSYLPDLS ADQIAKEIDY MLRKGWFPCL
110 120 130 140 150
EFSDKGYVYR ECHKSPGCYD GRYWTMYKLP MFGCQDSAQV LREIQECRRE
160 170
FPTSYIRVLG FDRVRQVQCA GFIVYKPT
Length:178
Mass (Da):20,010
Last modified:October 4, 2010 - v1
Checksum:i77FE33207EF8960E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL377686 Genomic DNA. Translation: EFJ07320.1.
RefSeqiXP_002991566.1. XM_002991520.1.
UniGeneiSmo.41.

Genome annotation databases

EnsemblPlantsiEFJ07320; EFJ07320; SELMODRAFT_186173.
GeneIDi9632372.
KEGGismo:SELMODRAFT_186173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL377686 Genomic DNA. Translation: EFJ07320.1.
RefSeqiXP_002991566.1. XM_002991520.1.
UniGeneiSmo.41.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiEFJ07320; EFJ07320; SELMODRAFT_186173.
GeneIDi9632372.
KEGGismo:SELMODRAFT_186173.

Phylogenomic databases

InParanoidiD8T7L5.
KOiK01602.
OMAiEVINTKH.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamiPF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The Selaginella genome identifies genetic changes associated with the evolution of vascular plants."
    Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D., Chapple C., Cheng C.
    , Correa L.G., Dacre M., DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N., Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.
    Science 332:960-963(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiD8T7L5_SELML
AccessioniPrimary (citable) accession number: D8T7L5
Entry historyi
Integrated into UniProtKB/TrEMBL: October 4, 2010
Last sequence update: October 4, 2010
Last modified: February 3, 2015
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.