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

Gene

serS

Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Status
Reviewed-Annotation score: Annotation score: 5 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).

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 (serS)
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)DescriptionActionsGraphical viewLength
Binding sitei272ATP; via amide nitrogen and carbonyl oxygen1
Binding sitei279Serine1
Binding sitei380Serine1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi256 – 258ATP3
Nucleotide bindingi345 – 348ATP4

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. 2305.
UniPathwayiUPA00906; UER00895.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine--tRNA ligase (EC:6.1.1.11)
Alternative name(s):
Seryl-tRNA synthetase
Short name:
SerRS
Seryl-tRNA(Ser/Sec) synthetase
Gene namesi
Name:serS
Ordered Locus Names:TT_C0520
OrganismiThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Taxonomic identifieri262724 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000592 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001221451 – 421Serine--tRNA ligaseAdd BLAST421

Interactioni

Subunit structurei

Homodimer. A single tRNA molecule binds across the dimer.3 Publications

Protein-protein interaction databases

STRINGi262724.TTC0520.

Structurei

Secondary structure

1421
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 9Combined sources6
Helixi11 – 21Combined sources11
Helixi27 – 36Combined sources10
Helixi49 – 60Combined sources12
Helixi63 – 78Combined sources16
Helixi90 – 98Combined sources9
Beta strandi111 – 113Combined sources3
Helixi114 – 116Combined sources3
Beta strandi118 – 124Combined sources7
Helixi136 – 143Combined sources8
Helixi150 – 154Combined sources5
Helixi164 – 182Combined sources19
Beta strandi186 – 189Combined sources4
Beta strandi192 – 195Combined sources4
Helixi196 – 202Combined sources7
Turni205 – 208Combined sources4
Helixi209 – 211Combined sources3
Beta strandi218 – 222Combined sources5
Helixi227 – 232Combined sources6
Turni233 – 236Combined sources4
Beta strandi238 – 240Combined sources3
Helixi241 – 243Combined sources3
Beta strandi245 – 255Combined sources11
Beta strandi268 – 271Combined sources4
Beta strandi273 – 284Combined sources12
Helixi288 – 308Combined sources21
Beta strandi313 – 317Combined sources5
Helixi320 – 323Combined sources4
Beta strandi328 – 336Combined sources9
Turni338 – 340Combined sources3
Beta strandi341 – 353Combined sources13
Helixi355 – 360Combined sources6
Beta strandi363 – 365Combined sources3
Beta strandi371 – 373Combined sources3
Beta strandi375 – 384Combined sources10
Helixi386 – 395Combined sources10
Helixi406 – 408Combined sources3
Helixi409 – 412Combined sources4
Beta strandi413 – 417Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SERX-ray2.90A/B1-421[»]
1SESX-ray2.50A/B1-421[»]
1SETX-ray2.55A/B1-421[»]
1SRYX-ray2.50A/B1-421[»]
3ERRX-ray2.27A/B94-419[»]
5EIUX-ray1.91A/D49-78[»]
5F7TX-ray2.29E/F/H/L49-78[»]
5IEAX-ray3.26A/B/C/D/F/K49-78[»]
DisProtiDP00514.
ProteinModelPortaliP34945.
SMRiP34945.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34945.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni225 – 227Serine binding3

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CGR. Bacteria.
COG0172. LUCA.
KOiK01875.
OMAiGGEDQVY.

Family and domain databases

CDDicd00770. SerRS_core. 1 hit.
Gene3Di1.10.287.40. 1 hit.
HAMAPiMF_00176. Ser_tRNA_synth_type1. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR033729. SerRS_core.
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.

P34945-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDLKRLRQE PEVFHRAIRE KGVALDLEAL LALDREVQEL KKRLQEVQTE
60 70 80 90 100
RNQVAKRVPK APPEEKEALI ARGKALGEEA KRLEEALREK EARLEALLLQ
110 120 130 140 150
VPLPPWPGAP VGGEEANREI KRVGGPPEFS FPPLDHVALM EKNGWWEPRI
160 170 180 190 200
SQVSGSRSYA LKGDLALYEL ALLRFAMDFM ARRGFLPMTL PSYAREKAFL
210 220 230 240 250
GTGHFPAYRD QVWAIAETDL YLTGTAEVVL NALHSGEILP YEALPLRYAG
260 270 280 290 300
YAPAFRSEAG SFGKDVRGLM RVHQFHKVEQ YVLTEASLEA SDRAFQELLE
310 320 330 340 350
NAEEILRLLE LPYRLVEVAT GDMGPGKWRQ VDIEVYLPSE GRYRETHSCS
360 370 380 390 400
ALLDWQARRA NLRYRDPEGR VRYAYTLNNT ALATPRILAM LLENHQLQDG
410 420
RVRVPQALIP YMGKEVLEPC G
Length:421
Mass (Da):47,813
Last modified:May 24, 2004 - v2
Checksum:i5E89B0D131EFC209
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017221 Genomic DNA. Translation: AAS80868.1.
RefSeqiWP_011172965.1. NC_005835.1.

Genome annotation databases

EnsemblBacteriaiAAS80868; AAS80868; TT_C0520.
KEGGitth:TT_C0520.
PATRICi23951447. VBITheThe54392_0520.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017221 Genomic DNA. Translation: AAS80868.1.
RefSeqiWP_011172965.1. NC_005835.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SERX-ray2.90A/B1-421[»]
1SESX-ray2.50A/B1-421[»]
1SETX-ray2.55A/B1-421[»]
1SRYX-ray2.50A/B1-421[»]
3ERRX-ray2.27A/B94-419[»]
5EIUX-ray1.91A/D49-78[»]
5F7TX-ray2.29E/F/H/L49-78[»]
5IEAX-ray3.26A/B/C/D/F/K49-78[»]
DisProtiDP00514.
ProteinModelPortaliP34945.
SMRiP34945.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC0520.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS80868; AAS80868; TT_C0520.
KEGGitth:TT_C0520.
PATRICi23951447. VBITheThe54392_0520.

Phylogenomic databases

eggNOGiENOG4105CGR. Bacteria.
COG0172. LUCA.
KOiK01875.
OMAiGGEDQVY.

Enzyme and pathway databases

UniPathwayiUPA00906; UER00895.
BRENDAi6.1.1.11. 2305.

Miscellaneous databases

EvolutionaryTraceiP34945.

Family and domain databases

CDDicd00770. SerRS_core. 1 hit.
Gene3Di1.10.287.40. 1 hit.
HAMAPiMF_00176. Ser_tRNA_synth_type1. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR033729. SerRS_core.
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...

Entry informationi

Entry nameiSYS_THET2
AccessioniPrimary (citable) accession number: P34945
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 24, 2004
Last modified: November 30, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  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

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.