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Protein

Selenocysteine lyase

Gene

Scly

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium.By similarity

Catalytic activityi

L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor.

Cofactori

pyridoxal 5'-phosphate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei375 – 3751S-selanylcysteine intermediate1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi4.4.1.16. 5301.
ReactomeiR-RNO-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.

Names & Taxonomyi

Protein namesi
Recommended name:
Selenocysteine lyase (EC:4.4.1.16)
Gene namesi
Name:Scly
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi1359514. Scly.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Selenocysteine lyasePRO_0000317014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei117 – 1171PhosphoserineBy similarity
Modified residuei247 – 2471N6-(pyridoxal phosphate)lysine

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ68FT9.
PRIDEiQ68FT9.

Expressioni

Gene expression databases

GenevisibleiQ68FT9. RN.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027220.

Structurei

Secondary structure

1
432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni24 – 263Combined sources
Helixi32 – 4413Combined sources
Helixi54 – 7421Combined sources
Helixi78 – 803Combined sources
Beta strandi81 – 855Combined sources
Helixi87 – 10822Combined sources
Beta strandi125 – 1295Combined sources
Helixi134 – 14512Combined sources
Beta strandi150 – 1545Combined sources
Turni158 – 1603Combined sources
Helixi165 – 1706Combined sources
Beta strandi176 – 1805Combined sources
Turni186 – 1883Combined sources
Helixi194 – 21118Combined sources
Beta strandi217 – 2215Combined sources
Turni223 – 2286Combined sources
Helixi233 – 2364Combined sources
Beta strandi239 – 2446Combined sources
Helixi245 – 2473Combined sources
Beta strandi254 – 2585Combined sources
Turni259 – 2635Combined sources
Helixi276 – 2794Combined sources
Helixi287 – 32640Combined sources
Helixi327 – 3293Combined sources
Beta strandi330 – 3345Combined sources
Beta strandi345 – 3506Combined sources
Helixi357 – 3637Combined sources
Beta strandi365 – 3684Combined sources
Beta strandi370 – 3723Combined sources
Helixi374 – 3796Combined sources
Helixi385 – 3895Combined sources
Helixi394 – 3974Combined sources
Beta strandi400 – 4045Combined sources
Helixi411 – 42919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A9XX-ray2.00A/B1-432[»]
3A9YX-ray1.85A/B1-432[»]
3A9ZX-ray1.55A/B1-432[»]
DisProtiDP00620.
ProteinModelPortaliQ68FT9.
SMRiQ68FT9. Positions 18-429.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ68FT9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1549. Eukaryota.
COG1104. LUCA.
GeneTreeiENSGT00530000063513.
HOGENOMiHOG000017510.
HOVERGENiHBG003708.
InParanoidiQ68FT9.
KOiK01763.
OMAiVRPNTCL.
OrthoDBiEOG7D85XM.
PhylomeDBiQ68FT9.
TreeFamiTF313550.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR016454. Cysteine_dSase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF005572. NifS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q68FT9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVARNGARG SVESPPNRKV YMDYNATTPL EPEVIQAVTE AMKEAWGNPS
60 70 80 90 100
SSYVAGRKAK DIINTARASL AKMIGGKPQD IIFTSGGTES NNLVIHSTVR
110 120 130 140 150
CFHEQQTLQG RTVDQISPEE GTRPHFITCT VEHDSIRLPL EHLVEDQVAE
160 170 180 190 200
VTFVPVSKVN GQVEVEDILA AVRPTTCLVT IMLANNETGV IMPISEISRR
210 220 230 240 250
IKALNQIRAA SGLPRVLVHT DAAQALGKRR VDVEDLGVDF LTIVGHKFYG
260 270 280 290 300
PRIGALYVRG VGKLTPLYPM LFGGGQERNF RPGTENTPMI AGLGKAADLV
310 320 330 340 350
SENCETYEAH MRDIRDYLEE RLEAEFGKRI HLNSRFPGVE RLPNTCNFSI
360 370 380 390 400
QGSQLRGYMV LAQCQTLLAS VGASCHSDHE DRPSPVLLSC GIPVDVARNA
410 420 430
VRLSVGRSTT RAEVDLIVQD LKQAVNQLEG PV
Length:432
Mass (Da):47,256
Last modified:October 11, 2004 - v1
Checksum:iFA5BB9DD941516A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079358 mRNA. Translation: AAH79358.1.
RefSeqiNP_001007756.1. NM_001007755.1.
UniGeneiRn.23954.

Genome annotation databases

EnsembliENSRNOT00000027220; ENSRNOP00000027220; ENSRNOG00000020083.
GeneIDi363285.
KEGGirno:363285.
UCSCiRGD:1359514. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079358 mRNA. Translation: AAH79358.1.
RefSeqiNP_001007756.1. NM_001007755.1.
UniGeneiRn.23954.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A9XX-ray2.00A/B1-432[»]
3A9YX-ray1.85A/B1-432[»]
3A9ZX-ray1.55A/B1-432[»]
DisProtiDP00620.
ProteinModelPortaliQ68FT9.
SMRiQ68FT9. Positions 18-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027220.

Proteomic databases

PaxDbiQ68FT9.
PRIDEiQ68FT9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027220; ENSRNOP00000027220; ENSRNOG00000020083.
GeneIDi363285.
KEGGirno:363285.
UCSCiRGD:1359514. rat.

Organism-specific databases

CTDi51540.
RGDi1359514. Scly.

Phylogenomic databases

eggNOGiKOG1549. Eukaryota.
COG1104. LUCA.
GeneTreeiENSGT00530000063513.
HOGENOMiHOG000017510.
HOVERGENiHBG003708.
InParanoidiQ68FT9.
KOiK01763.
OMAiVRPNTCL.
OrthoDBiEOG7D85XM.
PhylomeDBiQ68FT9.
TreeFamiTF313550.

Enzyme and pathway databases

BRENDAi4.4.1.16. 5301.
ReactomeiR-RNO-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.

Miscellaneous databases

EvolutionaryTraceiQ68FT9.
NextBioi683124.
PROiQ68FT9.

Gene expression databases

GenevisibleiQ68FT9. RN.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR016454. Cysteine_dSase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF005572. NifS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  2. "Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase."
    Omi R., Kurokawa S., Mihara H., Hayashi H., Goto M., Miyahara I., Kurihara T., Hirotsu K., Esaki N.
    J. Biol. Chem. 285:12133-12139(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), COFACTOR, SUBUNIT, ACTIVE SITE.

Entry informationi

Entry nameiSCLY_RAT
AccessioniPrimary (citable) accession number: Q68FT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 11, 2004
Last modified: February 17, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.