Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine--tRNA ligase, cytoplasmic

Gene

SES1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).1 Publication

Catalytic activityi

ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser).
ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec).

Pathwayi: selenocysteinyl-tRNA(Sec) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-seryl-tRNA(Sec) from L-serine and tRNA(Sec).
Proteins known to be involved in this subpathway in this organism are:
  1. Serine--tRNA ligase, cytoplasmic (SES1)
This subpathway is part of the pathway selenocysteinyl-tRNA(Sec) biosynthesis, which is itself part of Aminoacyl-tRNA biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-seryl-tRNA(Sec) from L-serine and tRNA(Sec), the pathway selenocysteinyl-tRNA(Sec) biosynthesis and in Aminoacyl-tRNA biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei295 – 2951ATP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei302 – 3021SerineBy similarity
Binding sitei404 – 4041SerineBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi279 – 2813ATPBy similarity
Nucleotide bindingi366 – 3694ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.1.1.11. 1096.
UniPathwayiUPA00906; UER00895.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine--tRNA ligase, cytoplasmic (EC:6.1.1.11)
Alternative name(s):
Seryl-tRNA synthetase
Short name:
SerRS
Seryl-tRNA(Ser/Sec) synthetase
Gene namesi
Name:SES1
ORF Names:CaO19.7901
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Serine--tRNA ligase, cytoplasmicPRO_0000122197Add
BLAST

2D gel databases

COMPLUYEAST-2DPAGEQ9HGT6.

Interactioni

Subunit structurei

Homodimer. The tRNA molecule binds across the dimer (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-59702N.

Structurei

Secondary structure

1
462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74Combined sources
Helixi9 – 113Combined sources
Helixi15 – 2511Combined sources
Helixi30 – 6839Combined sources
Helixi74 – 10532Combined sources
Helixi122 – 1243Combined sources
Beta strandi126 – 1316Combined sources
Beta strandi138 – 1425Combined sources
Turni144 – 1463Combined sources
Helixi154 – 1607Combined sources
Helixi166 – 1738Combined sources
Helixi183 – 20018Combined sources
Turni201 – 2033Combined sources
Beta strandi205 – 2084Combined sources
Beta strandi211 – 2144Combined sources
Helixi215 – 2217Combined sources
Helixi224 – 2274Combined sources
Turni228 – 2303Combined sources
Beta strandi233 – 2364Combined sources
Beta strandi239 – 2435Combined sources
Helixi248 – 2547Combined sources
Turni255 – 2573Combined sources
Beta strandi259 – 2624Combined sources
Helixi263 – 2664Combined sources
Beta strandi269 – 27810Combined sources
Beta strandi291 – 2944Combined sources
Beta strandi296 – 30712Combined sources
Helixi309 – 3113Combined sources
Helixi312 – 32918Combined sources
Beta strandi334 – 3385Combined sources
Helixi341 – 3433Combined sources
Beta strandi349 – 35810Combined sources
Turni359 – 3624Combined sources
Beta strandi363 – 37210Combined sources
Helixi376 – 3805Combined sources
Beta strandi399 – 4079Combined sources
Helixi408 – 41811Combined sources
Beta strandi419 – 4213Combined sources
Beta strandi424 – 4263Combined sources
Helixi429 – 4346Combined sources
Beta strandi440 – 4434Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QNEX-ray2.00A1-462[»]
3QO5X-ray2.30A1-462[»]
3QO7X-ray2.55A1-462[»]
3QO8X-ray2.00A1-462[»]
ProteinModelPortaliQ9HGT6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HGT6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni246 – 2483Serine bindingBy similarity

Domaini

Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.By similarity

Sequence similaritiesi

Phylogenomic databases

InParanoidiQ9HGT6.
KOiK01875.
OrthoDBiEOG7PVWZM.

Family and domain databases

Gene3Di1.10.287.40. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR010978. tRNA-bd_arm.
[Graphical view]
PANTHERiPTHR11778. PTHR11778. 1 hit.
PfamiPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFiPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSiPR00981. TRNASYNTHSER.
SUPFAMiSSF46589. SSF46589. 1 hit.
TIGRFAMsiTIGR00414. serS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HGT6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDINAFLVE KGGDPEIIKA SQKKRGDSVE LVDEIIAEYK EWVKLRFDLD
60 70 80 90 100
EHNKKLNSVQ KEIGKRFKAK EDAKDLIAEK EKLSNEKKEI IEKEAEADKN
110 120 130 140 150
LRSKINQVGN IVHESVVDSQ DEENNELVRT WTPENYKKPE QIAAATGAPA
160 170 180 190 200
KLSHHEVLLR LDGYDPERGV RIVGHRGYFL RNYGVFLNQA LINYGLSFLS
210 220 230 240 250
SKGYVPLQAP VMMNKEVMAK TAQLSQFDEE LYKVIDGEDE KYLIATSEQP
260 270 280 290 300
ISAYHAGEWF ESPAEQLPVR YAGYSSCFRR EAGSHGKDAW GIFRVHAFEK
310 320 330 340 350
IEQFVLTEPE KSWEEFDRMI GCSEEFYQSL GLPYRVVGIV SGELNNAAAK
360 370 380 390 400
KYDLEAWFPF QQEYKELVSC SNCTDYQSRN LEIRCGIKQQ NQQEKKYVHC
410 420 430 440 450
LNSTLSATER TICCILENYQ KEDGLVIPEV LRKYIPGEPE FIPYIKELPK
460
NTTSVKKAKG KN
Length:462
Mass (Da):52,991
Last modified:March 1, 2001 - v1
Checksum:i9111C72CF7B37CDF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF290915 Genomic DNA. Translation: AAG02209.1.
AACQ01000026 Genomic DNA. Translation: EAL01244.1.
RefSeqiXP_720099.1. XM_715006.1.

Genome annotation databases

EnsemblFungiiEAL01244; EAL01244; CaO19.7901.
GeneIDi3638226.
KEGGical:CaO19.7901.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF290915 Genomic DNA. Translation: AAG02209.1.
AACQ01000026 Genomic DNA. Translation: EAL01244.1.
RefSeqiXP_720099.1. XM_715006.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QNEX-ray2.00A1-462[»]
3QO5X-ray2.30A1-462[»]
3QO7X-ray2.55A1-462[»]
3QO8X-ray2.00A1-462[»]
ProteinModelPortaliQ9HGT6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59702N.

2D gel databases

COMPLUYEAST-2DPAGEQ9HGT6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAL01244; EAL01244; CaO19.7901.
GeneIDi3638226.
KEGGical:CaO19.7901.

Phylogenomic databases

InParanoidiQ9HGT6.
KOiK01875.
OrthoDBiEOG7PVWZM.

Enzyme and pathway databases

UniPathwayiUPA00906; UER00895.
BRENDAi6.1.1.11. 1096.

Miscellaneous databases

EvolutionaryTraceiQ9HGT6.

Family and domain databases

Gene3Di1.10.287.40. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR010978. tRNA-bd_arm.
[Graphical view]
PANTHERiPTHR11778. PTHR11778. 1 hit.
PfamiPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFiPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSiPR00981. TRNASYNTHSER.
SUPFAMiSSF46589. SSF46589. 1 hit.
TIGRFAMsiTIGR00414. serS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Seryl-tRNA synthetase is not responsible for the evolution of CUG codon reassignment in Candida albicans."
    O'Sullivan J.M., Mihr M.J., Santos M.A.S., Tuite M.F.
    Yeast 18:313-322(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: ATCC 32032 / CBS 5736 / DSM 3454 / NBRC 1856.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.

Entry informationi

Entry nameiSYSC_CANAL
AccessioniPrimary (citable) accession number: Q9HGT6
Secondary accession number(s): Q5AEY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 1, 2001
Last modified: February 17, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Candida albicans
    Candida albicans: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.