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Protein

Alanine--tRNA ligase, mitochondrial

Gene

Aars2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 bindingi632 – 6321ZincUniRule annotation
Metal bindingi636 – 6361ZincUniRule annotation
Metal bindingi749 – 7491ZincUniRule annotation
Metal bindingi753 – 7531ZincUniRule 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1310617. Aars2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323MitochondrionUniRule annotationAdd
BLAST
Chaini24 – 985962Alanine--tRNA ligase, mitochondrialPRO_0000402117Add
BLAST

Proteomic databases

PaxDbiD3ZX08.

Expressioni

Gene expression databases

GenevisibleiD3ZX08. RN.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000037568.

Structurei

3D structure databases

ProteinModelPortaliD3ZX08.
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.
InParanoidiD3ZX08.
KOiK01872.
OMAiHGHRLVP.
OrthoDBiEOG7M3HZH.
PhylomeDBiD3ZX08.
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.

D3ZX08-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASVAAAAG RLRRAIGRSC PWQRFSTEPH PPHGAAVRDA FLSFFRDRHG
60 70 80 90 100
HRLVPSASVR PRGDPSLLFV NAGMNQFKPI FLGTVDPRSE MAGFRRVANS
110 120 130 140 150
QKCVRAGGRH NDLEDVGRDL SHHTFFEMLG NWAFGGEYFK KEACSMAWEL
160 170 180 190 200
LTQVYGIPED RLWVSYFSGD SKTGLDPDLE TRDIWLSLGV PASRVLSFGL
210 220 230 240 250
QENFWEMGDT GPCGPCTEIH YDLAGGMGPP QLVELWNLVF MQHYREADGS
260 270 280 290 300
LHLLPQQHVD TGMGLERLVA VLQGKHSTYD TDLFSPLLDA IHQSCRVPPY
310 320 330 340 350
SGRVGAADEG RIDTAYRVVA DHIRTLSVCI ADGVSPGMSG APLVLRRILR
360 370 380 390 400
RAVRYSTEVL QAPPGFLGNL VPVVVATLGA AYPELQKNSV KVLIWEIANL
410 420 430 440 450
VSEDEAAFLA SLQRGRRIID RTVKRLGPSD LFPAEVAWSL SLSGNLGIPL
460 470 480 490 500
DLVQLMLEEK GVKLDTAGLE QLAQKEAQHR AQQAEAAQEE GLCLDVHALE
510 520 530 540 550
ELHRQGIPTT DDSPKYNYSL RPNGDYEFGL CEAQVLQLYS ETGTAVASVG
560 570 580 590 600
EGQRCGLLLD RTNFYAEQGG QASDRGYLIR TGQQDVLFPV ARAQVCGGFI
610 620 630 640 650
LHEAMAPECL QVGDRVQLYV DKAWRMGCMV KHTATHLLNW ALRQTLGPTT
660 670 680 690 700
EQRGSHLNPE RLRFDVATQT PLTTEQLRTV ESYVQEAVGQ DKPVYMEEVP
710 720 730 740 750
LAHTARIPGL RSLDEVYPDP VRVVSVGVPV AQALAPASQA ALQTSVELCC
760 770 780 790 800
GTHLLSTGAV GDLVIIGDRQ LVKGITRLLA ITGEQAQQAR EVGQSLSQEV
810 820 830 840 850
EVASERLSRG SRDLLEAHRL SKDIGRLIEF TESAVIPQWQ RQEQQTTLKM
860 870 880 890 900
LQRRANTAIR KLEKSQATEK SQELLKRHSE GPLIVDTVSA QSLSVLVKVV
910 920 930 940 950
RQLCKQAPSM SVLLLSPQPT GSVLCACQVA QGATPTFTAE AWALAVCSHM
960 970 980
GGKAWGSPVI AQGTGHTADL EAALRTARAY ALNQL
Length:985
Mass (Da):107,806
Last modified:April 20, 2010 - v1
Checksum:iA019BF4379DCADC7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473987 Genomic DNA. Translation: EDM18733.1.
RefSeqiNP_001100361.1. NM_001106891.1.
UniGeneiRn.109849.

Genome annotation databases

GeneIDi301254.
KEGGirno:301254.
UCSCiRGD:1310617. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473987 Genomic DNA. Translation: EDM18733.1.
RefSeqiNP_001100361.1. NM_001106891.1.
UniGeneiRn.109849.

3D structure databases

ProteinModelPortaliD3ZX08.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000037568.

Proteomic databases

PaxDbiD3ZX08.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi301254.
KEGGirno:301254.
UCSCiRGD:1310617. rat.

Organism-specific databases

CTDi57505.
RGDi1310617. Aars2.

Phylogenomic databases

eggNOGiKOG0188. Eukaryota.
COG0013. LUCA.
InParanoidiD3ZX08.
KOiK01872.
OMAiHGHRLVP.
OrthoDBiEOG7M3HZH.
PhylomeDBiD3ZX08.
TreeFamiTF300737.

Miscellaneous databases

NextBioi648405.
PROiD3ZX08.

Gene expression databases

GenevisibleiD3ZX08. RN.

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. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.

Entry informationi

Entry nameiSYAM_RAT
AccessioniPrimary (citable) accession number: D3ZX08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: April 20, 2010
Last modified: May 11, 2016
This is version 41 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. 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.