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Protein

O-phosphoseryl-tRNA(Sec) selenium transferase

Gene

Sepsecs

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.By similarity

Catalytic activityi

O-phospho-L-seryl-tRNA(Sec) + selenophosphate + H2O = L-selenocysteinyl-tRNA(Sec) + 2 phosphate.

Cofactori

pyridoxal 5'-phosphate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei74 – 741May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate
Binding sitei75 – 751PLP
Binding sitei97 – 971Substrate
Binding sitei98 – 981Substrate
Binding sitei105 – 1051Substrate
Binding sitei271 – 2711tRNA variable armBy similarity
Binding sitei313 – 3131Substrate
Binding sitei398 – 3981tRNA discriminator baseBy similarity

GO - Molecular functioni

  1. pyridoxal phosphate binding Source: InterPro
  2. transferase activity, transferring selenium-containing groups Source: InterPro
  3. tRNA binding Source: HGNC

GO - Biological processi

  1. selenocysteine incorporation Source: HGNC
  2. selenocysteinyl-tRNA(Sec) biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Pyridoxal phosphate, RNA-binding, Selenium, tRNA-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14964.
UniPathwayiUPA00906; UER00898.

Names & Taxonomyi

Protein namesi
Recommended name:
O-phosphoseryl-tRNA(Sec) selenium transferase (EC:2.9.1.2)
Alternative name(s):
Selenocysteine synthase
Short name:
Sec synthase
Selenocysteinyl-tRNA(Sec) synthase
Sep-tRNA:Sec-tRNA synthase
Short name:
SepSecS
UGA suppressor tRNA-associated protein
Gene namesi
Name:Sepsecs
Synonyms:D5Ertd135e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1098791. Sepsecs.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1051Q → E: 50% of wild-type activity. 1 Publication
Mutagenesisi313 – 3131R → E: Virtually inactive. 1 Publication
Mutagenesisi313 – 3131R → S: 30% of wild-type activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504O-phosphoseryl-tRNA(Sec) selenium transferasePRO_0000219876Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei284 – 2841N6-(pyridoxal phosphate)lysine

Proteomic databases

MaxQBiQ6P6M7.
PaxDbiQ6P6M7.
PRIDEiQ6P6M7.

PTM databases

PhosphoSiteiQ6P6M7.

Expressioni

Gene expression databases

BgeeiQ6P6M7.
ExpressionAtlasiQ6P6M7. baseline and differential.
GenevestigatoriQ6P6M7.

Interactioni

Subunit structurei

Homotetramer formed by a catalytic dimer and a non-catalytic dimer serving as a binding platform that orients tRNASec for catalysis.1 Publication

Protein-protein interaction databases

MINTiMINT-1857229.
STRINGi10090.ENSMUSP00000031069.

Structurei

Secondary structure

1
504
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3815Combined sources
Helixi48 – 6013Combined sources
Helixi63 – 653Combined sources
Helixi82 – 876Combined sources
Turni88 – 903Combined sources
Beta strandi95 – 973Combined sources
Helixi109 – 12921Combined sources
Beta strandi136 – 1427Combined sources
Helixi144 – 15815Combined sources
Beta strandi164 – 1685Combined sources
Helixi173 – 1819Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi197 – 1993Combined sources
Helixi202 – 21211Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2259Combined sources
Helixi235 – 24511Combined sources
Beta strandi249 – 2524Combined sources
Turni254 – 2585Combined sources
Helixi260 – 27213Combined sources
Beta strandi277 – 2815Combined sources
Helixi282 – 2865Combined sources
Beta strandi293 – 2986Combined sources
Helixi300 – 30910Combined sources
Helixi317 – 35842Combined sources
Beta strandi370 – 3767Combined sources
Turni378 – 3803Combined sources
Beta strandi381 – 3855Combined sources
Helixi387 – 39711Combined sources
Beta strandi404 – 4063Combined sources
Beta strandi411 – 4144Combined sources
Beta strandi417 – 4204Combined sources
Turni421 – 4255Combined sources
Beta strandi433 – 4375Combined sources
Helixi444 – 46522Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BC8X-ray1.65A19-468[»]
3BCAX-ray2.25A19-468[»]
3BCBX-ray1.85A19-468[»]
ProteinModelPortaliQ6P6M7.
SMRiQ6P6M7. Positions 23-467.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6P6M7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4444TetramerizationAdd
BLAST
Regioni96 – 10611Phosphate loop (P-loop)Add
BLAST

Sequence similaritiesi

Belongs to the SepSecS family.Curated

Phylogenomic databases

eggNOGiCOG0076.
GeneTreeiENSGT00390000007332.
HOGENOMiHOG000254245.
HOVERGENiHBG061363.
InParanoidiQ6P6M7.
KOiK03341.
OMAiPCPYLNA.
OrthoDBiEOG71G9TX.
PhylomeDBiQ6P6M7.
TreeFamiTF314381.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR019872. Sec-tRNA_Se_transferase.
IPR008829. SLA/LP_auto_ag.
[Graphical view]
PANTHERiPTHR12944. PTHR12944. 1 hit.
PfamiPF05889. SLA_LP_auto_ag. 1 hit.
[Graphical view]
PIRSFiPIRSF017689. SepSecS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR03531. selenium_SpcS. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6P6M7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPESFAAGE RRVSPAYVRQ GCEARRAHEH LIRLLLEQGK CPEDGWDEST
60 70 80 90 100
LELFLHELAV MDSNNFLGNC GVGEREGRVA SALVARRHYR FIHGIGRSGD
110 120 130 140 150
ISAVQPKAAG SSLLNKITNS LVLNVIKLAG VHSVASCFVV PMATGMSLTL
160 170 180 190 200
CFLTLRHKRP KAKYIIWPRI DQKSCFKSMV TAGFEPVVIE NVLEGDELRT
210 220 230 240 250
DLKAVEAKIQ ELGPEHILCL HSTTACFAPR VPDRLEELAV ICANYDIPHV
260 270 280 290 300
VNNAYGLQSS KCMHLIQQGA RVGRIDAFVQ SLDKNFMVPV GGAIIAGFNE
310 320 330 340 350
PFIQDISKMY PGRASASPSL DVLITLLSLG CSGYRKLLKE RKEMFVYLST
360 370 380 390 400
QLKKLAEAHN ERLLQTPHNP ISLAMTLKTI DGHHDKAVTQ LGSMLFTRQV
410 420 430 440 450
SGARAVPLGN VQTVSGHTFR GFMSHADNYP CAYLNAAAAI GMKMQDVDLF
460 470 480 490 500
IKRLDKCLNI VRKEQTRASV VSGADRNKAE DADIEEMALK LDDVLGDVGQ

GPAL
Length:504
Mass (Da):55,326
Last modified:March 28, 2005 - v2
Checksum:iE106674A0C80D98B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001E → D in AAH62133 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033654 mRNA. Translation: BAC28410.1.
BC062133 mRNA. Translation: AAH62133.1.
CCDSiCCDS19286.1.
RefSeqiNP_766078.1. NM_172490.3.
UniGeneiMm.244719.

Genome annotation databases

EnsembliENSMUST00000031069; ENSMUSP00000031069; ENSMUSG00000029173.
GeneIDi211006.
KEGGimmu:211006.
UCSCiuc008xko.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033654 mRNA. Translation: BAC28410.1.
BC062133 mRNA. Translation: AAH62133.1.
CCDSiCCDS19286.1.
RefSeqiNP_766078.1. NM_172490.3.
UniGeneiMm.244719.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BC8X-ray1.65A19-468[»]
3BCAX-ray2.25A19-468[»]
3BCBX-ray1.85A19-468[»]
ProteinModelPortaliQ6P6M7.
SMRiQ6P6M7. Positions 23-467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1857229.
STRINGi10090.ENSMUSP00000031069.

PTM databases

PhosphoSiteiQ6P6M7.

Proteomic databases

MaxQBiQ6P6M7.
PaxDbiQ6P6M7.
PRIDEiQ6P6M7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031069; ENSMUSP00000031069; ENSMUSG00000029173.
GeneIDi211006.
KEGGimmu:211006.
UCSCiuc008xko.1. mouse.

Organism-specific databases

CTDi51091.
MGIiMGI:1098791. Sepsecs.

Phylogenomic databases

eggNOGiCOG0076.
GeneTreeiENSGT00390000007332.
HOGENOMiHOG000254245.
HOVERGENiHBG061363.
InParanoidiQ6P6M7.
KOiK03341.
OMAiPCPYLNA.
OrthoDBiEOG71G9TX.
PhylomeDBiQ6P6M7.
TreeFamiTF314381.

Enzyme and pathway databases

UniPathwayiUPA00906; UER00898.
BioCyciMetaCyc:MONOMER-14964.

Miscellaneous databases

EvolutionaryTraceiQ6P6M7.
NextBioi373121.
PROiQ6P6M7.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P6M7.
ExpressionAtlasiQ6P6M7. baseline and differential.
GenevestigatoriQ6P6M7.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR019872. Sec-tRNA_Se_transferase.
IPR008829. SLA/LP_auto_ag.
[Graphical view]
PANTHERiPTHR12944. PTHR12944. 1 hit.
PfamiPF05889. SLA_LP_auto_ag. 1 hit.
[Graphical view]
PIRSFiPIRSF017689. SepSecS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR03531. selenium_SpcS. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cecum.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Limb.
  3. "Structure and catalytic mechanism of eukaryotic selenocysteine synthase."
    Ganichkin O.M., Xu X.M., Carlson B.A., Mix H., Hatfield D.L., Gladyshev V.N., Wahl M.C.
    J. Biol. Chem. 283:5849-5865(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 19-468 IN COMPLEX WITH PYRIDOXAL PHOSPHATE, SUBUNIT, SUBSTRATE-BINDING SITES, COFACTOR, MUTAGENESIS OF GLN-105 AND ARG-313.

Entry informationi

Entry nameiSPCS_MOUSE
AccessioniPrimary (citable) accession number: Q6P6M7
Secondary accession number(s): Q8BZS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2005
Last sequence update: March 28, 2005
Last modified: January 6, 2015
This is version 90 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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.