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Protein

Phenylalanine--tRNA ligase alpha subunit

Gene

Farsa

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).

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

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine--tRNA ligase alpha subunit (EC:6.1.1.20)
Alternative name(s):
Phenylalanyl-tRNA synthetase alpha subunit
Short name:
PheRS
Gene namesi
Name:Farsa
Synonyms:Farsla
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi1310314. Farsa.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 508507Phenylalanine--tRNA ligase alpha subunitPRO_0000280449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei193 – 1931PhosphoserineBy similarity
Modified residuei301 – 3011PhosphoserineBy similarity
Modified residuei311 – 3111N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ505J8.
PRIDEiQ505J8.

PTM databases

iPTMnetiQ505J8.

Expressioni

Gene expression databases

GenevisibleiQ505J8. RN.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.By similarity

Protein-protein interaction databases

IntActiQ505J8. 1 interaction.
MINTiMINT-4579145.
STRINGi10116.ENSRNOP00000004370.

Structurei

3D structure databases

ProteinModelPortaliQ505J8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2784. Eukaryota.
COG0016. LUCA.
GeneTreeiENSGT00390000006387.
HOGENOMiHOG000230294.
HOVERGENiHBG068046.
InParanoidiQ505J8.
KOiK01889.
OMAiYKYTWKL.
OrthoDBiEOG789CB8.
PhylomeDBiQ505J8.
TreeFamiTF300647.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR006195. aa-tRNA-synth_II.
IPR013196. HTH_11.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08279. HTH_11. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
TIGRFAMsiTIGR00468. pheS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q505J8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADNPVLEQL LRRLEVADGG LDSAELATQL GVEHQAVVGA VKSLQALGEV
60 70 80 90 100
IEAELRSTKC WELTTEGEEI AREGSHEARV FRSIPLEGLV QSELMQLPSG
110 120 130 140 150
KVGFSKAMSN KWIRVDKSAA DGPRVFRVVD SIEDEVQRRL QQVQAGQAEK
160 170 180 190 200
LAEKERNELR KRKLLTEVIL KTYWVSKGKG FSTSVSKQEA ELSPEMISSG
210 220 230 240 250
SWRDRPFKPY NFSARGVLPD SGHLHPLLKV RSQFRQIFLE MGFTEMPTDN
260 270 280 290 300
FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM DYVQRVKRTH
310 320 330 340 350
SQGGYGSQGY KYTWKLEEAR KNLLRTHTTA ASARALYRLA QKKPFTPAKY
360 370 380 390 400
FSIDRVFRNE TLDATHLAEF HQIEGVIADH GLTLGHLMGV LREFFTKLGI
410 420 430 440 450
TQLRFKPAYN PYTEPSMEVF SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE
460 470 480 490 500
NVSVIAWGLS LERPTMIKYG INNIRELVGH KVNLQMVYDS PVCRLDIEPR

SSKTQEAA
Length:508
Mass (Da):57,720
Last modified:June 7, 2005 - v1
Checksum:i78CE0B72EC5BF377
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC094515 mRNA. Translation: AAH94515.1.
RefSeqiNP_001019408.1. NM_001024237.1.
UniGeneiRn.2972.

Genome annotation databases

EnsembliENSRNOT00000004370; ENSRNOP00000004370; ENSRNOG00000003149.
GeneIDi288917.
KEGGirno:288917.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC094515 mRNA. Translation: AAH94515.1.
RefSeqiNP_001019408.1. NM_001024237.1.
UniGeneiRn.2972.

3D structure databases

ProteinModelPortaliQ505J8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ505J8. 1 interaction.
MINTiMINT-4579145.
STRINGi10116.ENSRNOP00000004370.

PTM databases

iPTMnetiQ505J8.

Proteomic databases

PaxDbiQ505J8.
PRIDEiQ505J8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004370; ENSRNOP00000004370; ENSRNOG00000003149.
GeneIDi288917.
KEGGirno:288917.

Organism-specific databases

CTDi2193.
RGDi1310314. Farsa.

Phylogenomic databases

eggNOGiKOG2784. Eukaryota.
COG0016. LUCA.
GeneTreeiENSGT00390000006387.
HOGENOMiHOG000230294.
HOVERGENiHBG068046.
InParanoidiQ505J8.
KOiK01889.
OMAiYKYTWKL.
OrthoDBiEOG789CB8.
PhylomeDBiQ505J8.
TreeFamiTF300647.

Miscellaneous databases

NextBioi628972.
PROiQ505J8.

Gene expression databases

GenevisibleiQ505J8. RN.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR006195. aa-tRNA-synth_II.
IPR013196. HTH_11.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08279. HTH_11. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
TIGRFAMsiTIGR00468. pheS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
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: Brain.
  2. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12 AND 43-59, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.

Entry informationi

Entry nameiSYFA_RAT
AccessioniPrimary (citable) accession number: Q505J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: June 7, 2005
Last modified: May 11, 2016
This is version 87 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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