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Protein

Serine--tRNA ligase

Gene

serS

Organism
Synechococcus sp. (strain RCC307)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the attachment of serine to tRNA(Ser). Is also 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).UniRule annotation

Catalytic activityi

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

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).UniRule annotation
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 sitei287SerineUniRule annotation1
Binding sitei385SerineUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi264 – 266ATPUniRule annotation3
Nucleotide bindingi351 – 354ATPUniRule annotation4

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

UniPathwayiUPA00906; UER00895.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine--tRNA ligaseUniRule annotation (EC:6.1.1.11UniRule annotation)
Alternative name(s):
Seryl-tRNA synthetaseUniRule annotation
Short name:
SerRSUniRule annotation
Seryl-tRNA(Ser/Sec) synthetaseUniRule annotation
Gene namesi
Name:serSUniRule annotation
Ordered Locus Names:SynRCC307_0547
OrganismiSynechococcus sp. (strain RCC307)
Taxonomic identifieri316278 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000001115 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000198501 – 425Serine--tRNA ligaseAdd BLAST425

Interactioni

Subunit structurei

Homodimer. The tRNA molecule binds across the dimer.UniRule annotation

Protein-protein interaction databases

STRINGi316278.SynRCC307_0547.

Structurei

3D structure databases

ProteinModelPortaliA5GRE1.
SMRiA5GRE1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni233 – 235Serine bindingUniRule annotation3

Domaini

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

Sequence similaritiesi

Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CGR. Bacteria.
COG0172. LUCA.
HOGENOMiHOG000035938.
KOiK01875.
OMAiYRPERHE.
OrthoDBiPOG091H01YY.

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.

A5GRE1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDQRLLRDN PELISQQLGR RGMEVDLTKL QLIAKQERDL EEQRSNLQAE
60 70 80 90 100
GNRTGKEVGM LIKGGAAPDS DEVKALREKG NRIKQQVAVL EEEEKGLEAK
110 120 130 140 150
LREQLLALPN LPSADAPEGK SEADNVEVKR WGEPRQGKDL EEHWQLADRL
160 170 180 190 200
GLFETERSVR IAQSRFITLM GDGARLERAL ISFMLDLHST KGYTEVMPPI
210 220 230 240 250
LVNSASLTGS GQLPKFAEES FRCADDDLWL TPTAEVPLTS LHRDEVIAVE
260 270 280 290 300
QLPLKYAAYT PCFRREAGSY GRDTRGLIRL HQFNKVELYW FCHPEKSAEA
310 320 330 340 350
HEQLTLDAEA VLEALELPYR RLELCTGDMG FSAARTYDLE VWLPGAGSYR
360 370 380 390 400
EISSCSTCGD FQARRSAIRF KEGKGTQLLH TLNGSGLAIG RTMAALLENG
410 420
QQPDGSIQLP AALVPYFGRE RLTPQ
Length:425
Mass (Da):47,543
Last modified:June 12, 2007 - v1
Checksum:i72BB71DE409ED4EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT978603 Genomic DNA. Translation: CAK27450.1.
RefSeqiWP_011934965.1. NC_009482.1.

Genome annotation databases

EnsemblBacteriaiCAK27450; CAK27450; SynRCC307_0547.
KEGGisyr:SynRCC307_0547.
PATRICi23821954. VBISynSp108374_0540.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT978603 Genomic DNA. Translation: CAK27450.1.
RefSeqiWP_011934965.1. NC_009482.1.

3D structure databases

ProteinModelPortaliA5GRE1.
SMRiA5GRE1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi316278.SynRCC307_0547.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAK27450; CAK27450; SynRCC307_0547.
KEGGisyr:SynRCC307_0547.
PATRICi23821954. VBISynSp108374_0540.

Phylogenomic databases

eggNOGiENOG4105CGR. Bacteria.
COG0172. LUCA.
HOGENOMiHOG000035938.
KOiK01875.
OMAiYRPERHE.
OrthoDBiPOG091H01YY.

Enzyme and pathway databases

UniPathwayiUPA00906; UER00895.

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_SYNR3
AccessioniPrimary (citable) accession number: A5GRE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: November 2, 2016
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.