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Protein

Alanine--tRNA ligase, cytoplasmic

Gene

aars-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.UniRule annotation

Catalytic activityi

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi606 – 6061ZincUniRule annotation
Metal bindingi610 – 6101ZincUniRule annotation
Metal bindingi724 – 7241ZincUniRule annotation
Metal bindingi728 – 7281ZincUniRule annotation

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, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligase, cytoplasmicUniRule annotation (EC:6.1.1.7UniRule annotation)
Alternative name(s):
AlaRS A
Alanyl-tRNA synthetaseUniRule annotation
Gene namesi
Name:aars-2UniRule annotation
Synonyms:ars-2
ORF Names:F28H1.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiF28H1.3; CE09768; WBGene00000197; aars-2.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 968968Alanine--tRNA ligase, cytoplasmicPRO_0000402113Add
BLAST

Proteomic databases

EPDiO01541.
PaxDbiO01541.
PRIDEiO01541.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi37458. 1 interaction.
IntActiO01541. 1 interaction.
STRINGi6239.F28H1.3.3.

Structurei

3D structure databases

ProteinModelPortaliO01541.
SMRiO01541. Positions 2-758.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.UniRule annotation

Sequence similaritiesi

Belongs to the class-II aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG0188. Eukaryota.
COG0013. LUCA.
GeneTreeiENSGT00390000016019.
HOGENOMiHOG000156964.
InParanoidiO01541.
KOiK01872.
OMAiFDFNCPR.
PhylomeDBiO01541.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O01541-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHLTASEVR STFINFFREK KEHTYVHSSS VIPHDDPTLL FANAGMNQFK
60 70 80 90 100
PLFLGIADPN SDLAKLKRAV NTQKCIRAGG KHNDLDDVGK DVYHHTYFEM
110 120 130 140 150
LGNWSFGDYF KKEIITWAWE LLTTVYGIPA ERLYVSVFGG DEANGVPADS
160 170 180 190 200
EARDIWRSVG VPDERILNFG MKDNFWEMGD VGPCGPCSEI HYDRIGNRDA
210 220 230 240 250
SHLVNADDPM VVEIWNLVFI QFNREEGGVL KPLPAKHIDC GLGLERLIAV
260 270 280 290 300
MQDKTSNYDT DIFQPIFEAI HKGSGVRAYT GFIGDEDKDG VDMAYRVVAD
310 320 330 340 350
HVRTLTIALS DGGRPDNSGR GYVLRRILRR GVRYASEKLN AQPGFFASLV
360 370 380 390 400
PVVISILGET FPELSRDPVT VMDIINDEEK QFLKTLSRGR VLFQRAVQSL
410 420 430 440 450
PEGTMTFPGD VSWRLYDTYG FPADLTQLMA EEKGLSVDNT AFEEARRKAI
460 470 480 490 500
ETSSAGTGKF RDTLDLDVHA LAELQQKGVP TTDDSPKYAY TFTGEGSDAV
510 520 530 540 550
YKFEPCVGKI LAIRRDGKFV DQLAAGEEGA ILLDRTNFYA EQGGQIYDVG
560 570 580 590 600
VLTKVNDESN EFNVSNCQVR GGYIVLVGSA EGSFSVGDQV NERFDEDRKQ
610 620 630 640 650
LIMKNHTGTH VLNYALRKVL ADSDQKGSLV APDRMRFDFT NKAGMTVQQV
660 670 680 690 700
KKAEEYAQQL IDTKGQVYAK NSPLGEAKKV KGLRAMFDET YPDPVRVVAV
710 720 730 740 750
GTPVEQLLQN PDAEEGQNTT VEFCGGTHLQ NVSHIGRIVI ASEEAIAKGI
760 770 780 790 800
RRIVALTGPE AERAIARADR LTARLEEESK HADKKDELLA NKDKFKALQK
810 820 830 840 850
KIQEIVDEAN GAQLPYWRKD SIREKAKAIQ KTLDGYTKAQ QAAVAEKVLG
860 870 880 890 900
EAKELAAVAE QPTVLVHVFA ANANSKAIDN ALKLLKDTKA VMAFSVNEDS
910 920 930 940 950
GKVLCLAKVD KSLVSNGLKA NEWVNEVCTV LGGKGGGKDA NAQLTGENVD
960
KLDAAVELAQ KFALAAIN
Length:968
Mass (Da):106,782
Last modified:July 1, 1997 - v1
Checksum:iBE81FBDD0D3E2055
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti272 – 2721K → Q in AAA84420 (PubMed:9851916).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081252 Genomic DNA. Translation: CCD70212.1.
U41660 mRNA. Translation: AAA84420.1.
PIRiT29466.
RefSeqiNP_491281.1. NM_058880.3.
UniGeneiCel.17465.

Genome annotation databases

EnsemblMetazoaiF28H1.3.1; F28H1.3.1; WBGene00000197.
F28H1.3.2; F28H1.3.2; WBGene00000197.
F28H1.3.3; F28H1.3.3; WBGene00000197.
GeneIDi171985.
KEGGicel:CELE_F28H1.3.
UCSCiF28H1.3.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081252 Genomic DNA. Translation: CCD70212.1.
U41660 mRNA. Translation: AAA84420.1.
PIRiT29466.
RefSeqiNP_491281.1. NM_058880.3.
UniGeneiCel.17465.

3D structure databases

ProteinModelPortaliO01541.
SMRiO01541. Positions 2-758.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi37458. 1 interaction.
IntActiO01541. 1 interaction.
STRINGi6239.F28H1.3.3.

Proteomic databases

EPDiO01541.
PaxDbiO01541.
PRIDEiO01541.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF28H1.3.1; F28H1.3.1; WBGene00000197.
F28H1.3.2; F28H1.3.2; WBGene00000197.
F28H1.3.3; F28H1.3.3; WBGene00000197.
GeneIDi171985.
KEGGicel:CELE_F28H1.3.
UCSCiF28H1.3.1. c. elegans.

Organism-specific databases

CTDi171985.
WormBaseiF28H1.3; CE09768; WBGene00000197; aars-2.

Phylogenomic databases

eggNOGiKOG0188. Eukaryota.
COG0013. LUCA.
GeneTreeiENSGT00390000016019.
HOGENOMiHOG000156964.
InParanoidiO01541.
KOiK01872.
OMAiFDFNCPR.
PhylomeDBiO01541.

Miscellaneous databases

PROiO01541.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Strong selective pressure to use G:U to mark an RNA acceptor stem for alanine."
    Chihade J.W., Hayashibara K., Shiba K., Schimmel P.
    Biochemistry 37:9193-9202(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-272.
    Strain: Bristol N2.

Entry informationi

Entry nameiSYAC_CAEEL
AccessioniPrimary (citable) accession number: O01541
Secondary accession number(s): Q17371
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: July 1, 1997
Last modified: June 8, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.