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Protein

Alanine--tRNA ligase, mitochondrial

Gene

Aars2

Organism
Mus musculus (Mouse)
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 bindingi627 – 6271ZincUniRule annotation
Metal bindingi631 – 6311ZincUniRule annotation
Metal bindingi744 – 7441ZincUniRule annotation
Metal bindingi748 – 7481ZincUniRule 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):
Alanyl-tRNA synthetaseUniRule annotation
Short name:
AlaRSUniRule annotation
Gene namesi
Name:Aars2
Synonyms:Aarsl, Gm89, Kiaa1270
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2681839. Aars2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323MitochondrionUniRule annotationAdd
BLAST
Chaini24 – 980957Alanine--tRNA ligase, mitochondrialPRO_0000250726Add
BLAST

Proteomic databases

EPDiQ14CH7.
MaxQBiQ14CH7.
PaxDbiQ14CH7.
PRIDEiQ14CH7.

PTM databases

iPTMnetiQ14CH7.
PhosphoSiteiQ14CH7.

Expressioni

Gene expression databases

BgeeiQ14CH7.
GenevisibleiQ14CH7. MM.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024733.

Structurei

3D structure databases

ProteinModelPortaliQ14CH7.
SMRiQ14CH7. Positions 20-886.
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.
HOVERGENiHBG017874.
InParanoidiQ14CH7.
KOiK01872.
OMAiHGHRLVP.
OrthoDBiEOG7M3HZH.
PhylomeDBiQ14CH7.
TreeFamiTF300737.

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.

Q14CH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVALAAAAG KLRRAIGRSC PWQPFSTEPG PPHGAAVRDA FLSFFRDRHG
60 70 80 90 100
HRLVPSATVR PRGDPSLLFV NAGMNQFKPI FLGTVDPRSE MAGFRRVVNS
110 120 130 140 150
QKCVRAGGRH NDLEDVGRDL SHHTFFEMLG NWAFGGEYFK EEACSMAWEL
160 170 180 190 200
LTQVYGIPED RLWVSYFSGD SQTGLDPDLE TRDIWLSLGV PASRVLSFGP
210 220 230 240 250
QENFWEMGDT GPCGPCTEIH YDLAGGVGSP QLVELWNLVF MQHYREADGS
260 270 280 290 300
LQLLPQRHVD TGMGLERLVA VLQGKRSTYD TDLFSPLLDA IHQSCGAPPY
310 320 330 340 350
SGRVGAADEG RIDTAYRVVA DHIRTLSVCI ADGVSPGMSG APLVLRRILR
360 370 380 390 400
RAVRYSTEVL QAPPGFLGSL VPVVVETLGS AYPELEKNSV KIASLVSEDE
410 420 430 440 450
AAFLASLQRG RRIIDRTVKR LGPSDLFPAE VAWSLSLSGN LGIPLDLVEL
460 470 480 490 500
MLEEKGVKLD TAGLEQLAQK EAQHRAQQAE ADQEDRLCLD VHALEELHRQ
510 520 530 540 550
GIPTTDDSPK YNYTLHPNGD YEFGLCEARV LQLYSETGTA VASVGAGQRC
560 570 580 590 600
GLLLDRTNFY AEQGGQASDR GYLVRTGQQD MLFPVAGAQL CGGFILHEAM
610 620 630 640 650
APERLQVGDQ VQLYVDKAWR MGCMVKHTAT HLLSWALRQT LGPTTEQRGS
660 670 680 690 700
HLNPERLRFD VATQTLLTTE QLRTVESYVQ EVVGQDKPVF MEEVPLAHTA
710 720 730 740 750
RIPGLRSLDE VYPDPVRVVS VGVPVAHALG PASQAAMHTS VELCCGTHLL
760 770 780 790 800
STGAVGDLVI IGERQLVKGI TRLLAITGEQ AQQAREVGQS LSQEVEAASE
810 820 830 840 850
RLSQGSRDLP EAHRLSKDIG RLTEVAESAV IPQWQRQELQ TTLKMLQRRA
860 870 880 890 900
NTAIRKLEKG QATEKSQELL KRHSEGPLIV DTVSAESLSV LVKVVRQLCK
910 920 930 940 950
QAPSISVLLL SPQPTGSVLC ACQVAQDATP TFTAEAWALA VCSHMGGKAW
960 970 980
GSRVVAQGTG HTADLEAALG TARAYALSQL
Length:980
Mass (Da):106,783
Last modified:August 22, 2006 - v1
Checksum:i7734BC58CDB5463D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti618 – 6258AWRMGCMV → RSRPG in BAD32417 (PubMed:15368895).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079844 mRNA. Translation: AAH79844.1.
BC113172 mRNA. Translation: AAI13173.1.
BC113779 mRNA. Translation: AAI13780.1.
AK173139 Transcribed RNA. Translation: BAD32417.1.
CCDSiCCDS28809.1.
RefSeqiNP_941010.2. NM_198608.2.
UniGeneiMm.329063.

Genome annotation databases

EnsembliENSMUST00000024733; ENSMUSP00000024733; ENSMUSG00000023938.
GeneIDi224805.
KEGGimmu:224805.
UCSCiuc008cqr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079844 mRNA. Translation: AAH79844.1.
BC113172 mRNA. Translation: AAI13173.1.
BC113779 mRNA. Translation: AAI13780.1.
AK173139 Transcribed RNA. Translation: BAD32417.1.
CCDSiCCDS28809.1.
RefSeqiNP_941010.2. NM_198608.2.
UniGeneiMm.329063.

3D structure databases

ProteinModelPortaliQ14CH7.
SMRiQ14CH7. Positions 20-886.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024733.

PTM databases

iPTMnetiQ14CH7.
PhosphoSiteiQ14CH7.

Proteomic databases

EPDiQ14CH7.
MaxQBiQ14CH7.
PaxDbiQ14CH7.
PRIDEiQ14CH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024733; ENSMUSP00000024733; ENSMUSG00000023938.
GeneIDi224805.
KEGGimmu:224805.
UCSCiuc008cqr.1. mouse.

Organism-specific databases

CTDi57505.
MGIiMGI:2681839. Aars2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0188. Eukaryota.
COG0013. LUCA.
GeneTreeiENSGT00390000016019.
HOGENOMiHOG000156964.
HOVERGENiHBG017874.
InParanoidiQ14CH7.
KOiK01872.
OMAiHGHRLVP.
OrthoDBiEOG7M3HZH.
PhylomeDBiQ14CH7.
TreeFamiTF300737.

Miscellaneous databases

ChiTaRSiAars2. mouse.
NextBioi377373.
PROiQ14CH7.
SOURCEiSearch...

Gene expression databases

BgeeiQ14CH7.
GenevisibleiQ14CH7. MM.

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

  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].
    Strain: C57BL/6J.
    Tissue: Brain.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 242-980.
    Tissue: Embryonic intestine.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen and Testis.

Entry informationi

Entry nameiSYAM_MOUSE
AccessioniPrimary (citable) accession number: Q14CH7
Secondary accession number(s): Q68FH3, Q69ZM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: August 22, 2006
Last modified: May 11, 2016
This is version 81 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, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.