P50475 (SYAC_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine--tRNA ligase, cytoplasmic
EC=6.1.1.7

Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS

Gene names

Name:

Aars

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	968 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity. HAMAP-Rule MF_03133
Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP-Rule MF_03133
Cofactor	Binds 1 zinc ion per subunit Potential.
Subunit structure	Monomer.
Subcellular location	Cytoplasm By similarity.
Domain	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 By similarity. HAMAP-Rule MF_03133
Post-translational modification	ISGylated By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	alanyl-tRNA aminoacylation Inferred from direct assay Ref.2. Source: RGD cerebellar Purkinje cell layer development Inferred from electronic annotation. Source: Compara endoplasmic reticulum unfolded protein response Inferred from electronic annotation. Source: Compara hair follicle development Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara neuromuscular process controlling balance Inferred from electronic annotation. Source: Compara protein folding Inferred from electronic annotation. Source: Compara response to amino acid stimulus Inferred from electronic annotation. Source: Compara skin development Inferred from electronic annotation. Source: Compara tRNA modification Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay Ref.2. Source: RGD
Molecular_function	ATP binding Inferred from physical interaction Ref.2. Source: RGD alanine-tRNA ligase activity Inferred from direct assay Ref.2. Source: RGD amino acid binding Inferred from physical interaction Ref.2. Source: RGD aminoacyl-tRNA editing activity Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW tRNA binding Inferred from physical interaction Ref.2. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 968	968	Alanine--tRNA ligase, cytoplasmic HAMAP-Rule MF_03133		PRO_0000075284
Sites
	Metal binding	605	1	Zinc Potential
	Metal binding	609	1	Zinc Potential
	Metal binding	723	1	Zinc Potential
	Metal binding	727	1	Zinc Potential
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	19	1	N6-acetyllysine By similarity
	Modified residue	399	1	Phosphoserine By similarity
	Modified residue	555	1	Phosphoserine By similarity
	Modified residue	876	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	459	1	G → E AA sequence Ref.2
	Sequence conflict	474 – 476	3	RAK → ARA AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P50475 [UniParc]. Last modified October 13, 2009. Version 3. Checksum: 10BF81F46F7AF546	FASTA	968	106,790
	10 20 30 40 50 60 MDSTLTAREI RERFINYFKR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK PIFLNTVDPS 70 80 90 100 110 120 HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM LGSWSFGDYF KELACKMALE 130 140 150 160 170 180 LLTQEFGIPV ERLYVTYFGG DEAAGLEPDL ECRQIWQNLG LDEAKILPGN MKDNFWEMGD 190 200 210 220 230 240 TGPCGPCSEI HYDRIGGRDA AHLVNQDDPN VLEIWNLVFI QYNRESDGVL KPLPKKSIDT 250 260 270 280 290 300 GMGLERLVSV LQNKMSNYDT DLFVPYFEAI QKGTGARPYT GKVGAEDTDG IDMAYRVLAD 310 320 330 340 350 360 HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYSHEKLN ASRGFFATLV DVVVQSLGDA 370 380 390 400 410 420 FPELKKDPDM VKDIINEEEV QFLKTLSRGR RILDRKIQSL GDCQTIPGDT AWLLYDTYGF 430 440 450 460 470 480 PVDLTGLIAE EKGLVVDMDG FEEERKLAQL KSQGKGAGGE DLIMLDIYAI EELRAKGLEA 490 500 510 520 530 540 TDDSPKYNYH SDSSGSYVFE CTVATVLALR REKMFVDEVV TGQECGVVLD KTCFYAEQGG 550 560 570 580 590 600 QIFDEGYLVK VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GNLRVGDQVR LFIDEPRRRP 610 620 630 640 650 660 VMSNHTATHI LNFALRSVLG DADQKGSLVA PDRLRFDFTA KGAMSTEQIK KTEEIVNGMI 670 680 690 700 710 720 EAAKPVYTLD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG VPVSELLDDP SGPAGSLTSV 730 740 750 760 770 780 EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR RIVAVTGAEA QKALRKSETL KKSLSAMEVK 790 800 810 820 830 840 VKAQSAPNKD VQKEIADLGE VLATAVIPQW QKDEQRETLK SLKKVMDDLD RASKADVQKR 850 860 870 880 890 900 VLEKTKQLID SNPNQPLVIL EMESGASAKA LNEALKLFKT HSPQTSAMLF TVDNEAGKIT 910 920 930 940 950 960 CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDMSAQA TGKNVGCLQE ALQLATSFAQ LRLGDVKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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].
[2]	"Alanyl-tRNA synthetase from Escherichia coli, Bombyx mori and Ratus ratus. Existence of common structural features." Dignam J.D., Dignam S.S., Brumley L.L. Eur. J. Biochem. 198:201-210(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 456-476. Tissue: Liver.
[3]	"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] OF 600-968. Tissue: Thymus.
[4]	Maurya D.K., Bhargava P. Submitted (JAN-2009) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH473972 Genomic DNA. Translation: EDL92558.1. BC098738 mRNA. Translation: AAH98738.1.
IPI	IPI00363563.
PIR	S16073.
RefSeq	NP_001093987.1. NM_001100517.1.
UniGene	Rn.8645.
3D structure databases
ProteinModelPortal	P50475.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000025051.
Proteomic databases
PaxDb	P50475.
PRIDE	P50475.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000025052; ENSRNOP00000025051; ENSRNOG00000018404.
GeneID	292023.
KEGG	rno:292023.
UCSC	RGD:1304832. rat.
Organism-specific databases
CTD	16.
RGD	1304832. Aars.
Phylogenomic databases
eggNOG	COG0013.
GeneTree	ENSGT00390000016019.
HOGENOM	HOG000156964.
HOVERGEN	HBG017874.
InParanoid	Q4G057.
KO	K01872.
OrthoDB	EOG45X7VC.
Gene expression databases
ArrayExpress	P50475.
Genevestigator	P50475.
Family and domain databases
HAMAP	MF_00036_B. Ala_tRNA_synth_B.
InterPro	IPR002318. 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. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
Pfam	PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR00980. TRNASYNTHALA.
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
SUPFAM	SSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMs	TIGR00344. alaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	633629.

Entry information

Entry name

SYAC_RAT

Accession

Primary (citable) accession number: P50475
Secondary accession number(s): A6IZ80, Q4G057

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 13, 2009
Last modified:	April 3, 2013
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program