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Protein

Alanine--tRNA ligase, mitochondrial

Gene

aars-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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 bindingi594 – 5941ZincUniRule annotation
Metal bindingi598 – 5981ZincUniRule annotation
Metal bindingi706 – 7061ZincUniRule annotation
Metal bindingi710 – 7101ZincUniRule 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, mitochondrialUniRule annotation (EC:6.1.1.7UniRule annotation)
Alternative name(s):
AlaRS B
Alanyl-tRNA synthetaseUniRule annotation
Gene namesi
Name:aars-1UniRule annotation
Synonyms:alas, ars-1
ORF Names:W02B12.6
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiW02B12.6a; CE28096; WBGene00000196; aars-1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 793Alanine--tRNA ligase, mitochondrialPRO_0000402118
Transit peptidei1 – ?MitochondrionUniRule annotation

Proteomic databases

EPDiQ23122.
PaxDbiQ23122.
PRIDEiQ23122.

Interactioni

Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi6239.W02B12.6a.

Structurei

3D structure databases

ProteinModelPortaliQ23122.
SMRiQ23122. Positions 22-741.
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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0188. Eukaryota.
COG0013. LUCA.
GeneTreeiENSGT00390000016019.
HOGENOMiHOG000156964.
InParanoidiQ23122.
KOiK01872.
OMAiRFDYSTG.
OrthoDBiEOG7M3HZH.
PhylomeDBiQ23122.

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.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF01411. 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.

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

Q23122-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIGSKILEN NIQKSISLGF YHSHSELRKS FYEFFKSKNH EILRSSSVIP
60 70 80 90 100
DENDGTLLFT NAGMNQFKPL ILSSTESRRV ANIQKCIRAG GKHNDLDDVG
110 120 130 140 150
KDLHHQTFFE MMGNWSFNDA FSKEEACRYA WEYLVEILGI NADRLYVSYF
160 170 180 190 200
GGIEKLGLPE DRECREIWKR IGVSSNRILP FVAENFWEMG AAGPCGPCTE
210 220 230 240 250
IHYDRIGGRD ASRLVNIDDS VVEIWNIVFM SSVRDSCGQI RHLGKNHIDT
260 270 280 290 300
GMGFERLLSV VQNKTSNFDT DVFTPILEKT SELAKKQYTG SLDSRQDATF
310 320 330 340 350
RLVADHIRAA TVAISDGAVP DGTGCGFIVR KMMRRAFLQG ISKLGIERYA
360 370 380 390 400
MSELVPVVAS TMKEVYPEIH DTSTHIRKIF NDEEAQFWKT VDKAKKMFDS
410 420 430 440 450
VAAESKSPII SGRKAFNLFE THGLPLAVTV ELARNIGREV DETEFERCRL
460 470 480 490 500
EAQKVSQKAS QFKLPISADD FPSHSDKEKY SYVFRNGKYE FPQVKTRILQ
510 520 530 540 550
VYKDQQKAES LEANDRGFLV LEECQFYGEQ GGQTSDTGHL LIDGREVFEV
560 570 580 590 600
ENAKKIAGGA VTVLFGRALL PIRRDLRVEQ KLDETRREGV MRAHSATHLL
610 620 630 640 650
NWALQKLGVG SGQKGSSVDC DRFRFDYSTG DEDLSKEQRT ELLIKCEMKM
660 670 680 690 700
REFIQNGGFT EIIETSLEEA KKIENLQSDV KEDRIGGASV RVVALGSGAD
710 720 730 740 750
VPVECCSGTH IHDVRVIDDV AIMSDKSMGQ RLRRIIVLTG KEAAACRNYT
760 770 780 790
KSIYEDLRST DPKERSKTGK NIDWKRVPIA DQARISILLK QKK
Length:793
Mass (Da):89,502
Last modified:October 1, 2001 - v2
Checksum:i6A9F309B13D39A26
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188715 mRNA. Translation: AAF05590.1.
Z66521 Genomic DNA. Translation: CAA91396.2.
PIRiT26086.
RefSeqiNP_496444.1. NM_064043.5.
UniGeneiCel.22616.

Genome annotation databases

EnsemblMetazoaiW02B12.6a; W02B12.6a; WBGene00000196.
GeneIDi174749.
KEGGicel:CELE_W02B12.6.
UCSCiW02B12.6a. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188715 mRNA. Translation: AAF05590.1.
Z66521 Genomic DNA. Translation: CAA91396.2.
PIRiT26086.
RefSeqiNP_496444.1. NM_064043.5.
UniGeneiCel.22616.

3D structure databases

ProteinModelPortaliQ23122.
SMRiQ23122. Positions 22-741.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.W02B12.6a.

Proteomic databases

EPDiQ23122.
PaxDbiQ23122.
PRIDEiQ23122.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiW02B12.6a; W02B12.6a; WBGene00000196.
GeneIDi174749.
KEGGicel:CELE_W02B12.6.
UCSCiW02B12.6a. c. elegans.

Organism-specific databases

CTDi174749.
WormBaseiW02B12.6a; CE28096; WBGene00000196; aars-1.

Phylogenomic databases

eggNOGiKOG0188. Eukaryota.
COG0013. LUCA.
GeneTreeiENSGT00390000016019.
HOGENOMiHOG000156964.
InParanoidiQ23122.
KOiK01872.
OMAiRFDYSTG.
OrthoDBiEOG7M3HZH.
PhylomeDBiQ23122.

Miscellaneous databases

PROiQ23122.

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.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF01411. 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. "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], SUBUNIT, PROBABLE SUBCELLULAR LOCATION.
    Strain: Bristol N2.
  2. "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.

Entry informationi

Entry nameiSYAM_CAEEL
AccessioniPrimary (citable) accession number: Q23122
Secondary accession number(s): Q9U6B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: October 1, 2001
Last modified: July 6, 2016
This is version 111 of the entry and version 2 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.