Reviewed, UniProtKB/Swiss-Prot Q5RC02 (SYAC_PONAB)

Names and origin

Protein names

Recommended name:
    Alanyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.7
Alternative name(s):
    Alanine--tRNA ligase
      Short name=AlaRS

Gene names

Name:

AARS

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

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

General annotation (Comments)

Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm Potential.
Domain	The C-terminal 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 Potential.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding RNA-binding tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	alanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alanine-tRNA ligase activity Inferred from electronic annotation. Source: EC tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 968	968	Alanyl-tRNA synthetase, cytoplasmic		PRO_0000075283
Regions
	Region	1 – 497	497	Catalytic By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	19	1	N6-acetyllysine By similarity
	Modified residue	555	1	Phosphoserine By similarity
	Modified residue	578	1	Phosphothreonine By similarity
	Modified residue	580	1	Phosphotyrosine By similarity
	Modified residue	876	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5RC02-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 8FB2F1F06ECB1128	FASTA	968	106,779
	10 20 30 40 50 60 MDSTLTASKI RQRFIDFFKR NEHTYIHSSA TIPLDDPTLL FANAGMNQFK PIFLNTIDPS 70 80 90 100 110 120 HPMAKPSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM LGSWSFGDYF KELACKMALE 130 140 150 160 170 180 LLTQEFGIPI ERLYVTYFGG DEAAGLEPDL ECKQIWQNLG LDDTKILPGN MKDNFWEMGD 190 200 210 220 230 240 TGPCGPCSEI HYDRIGGRDA AHLVNQDDPN VLEIWNLVFI QYNREADGIL KPLPKKSIDT 250 260 270 280 290 300 GMGLERLVSV LQNKMSNYDT DLFVPYFEAI QKGTGARPYT GKVGAEDADG IDMAYRVLAD 310 320 330 340 350 360 HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYAHEKLN ASRGFFATLV DVVVQSLGDA 370 380 390 400 410 420 FPELKKDPDM VKDIINEEEV QFLKTLSRGR RILDRKIQSL GDSKTIPGDT AWLLYDTYGF 430 440 450 460 470 480 PVDLTGLIAE EKGLVVDMDG FEEERKLAQL KSQGKGAGGE DLIMLDIYAI EELRARDLEV 490 500 510 520 530 540 TDDSPKYNYH LDSSGSYVFE NTVATVMALR REKMFVEEVS TGQECGVVLD KTCFYAEQGG 550 560 570 580 590 600 QIYDEGYLVK VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GDLKVGDQVW LFIDEPRRRP 610 620 630 640 650 660 IMSNHTATHI LNFALRSVLG EADQKGSLVA PDRLRFDFTA KGAMSTQQIK KAEEIANEMI 670 680 690 700 710 720 EAAKPVYTQD CSLAAAKAIQ GLRAVFDETY PDPVRVVSIG VPVSELLDDP SGPAGSLTSV 730 740 750 760 770 780 EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR RIVAVTGAEA QKALRKAGSL KKPLSVMEAK 790 800 810 820 830 840 VKAQTAPNKD VQREIADLGE ALATAVIPQW QKDELRETLK SLKKVMDDLD RASKADVQKR 850 860 870 880 890 900 VLEKTKQLID SNPNQPLVIL EMESGASAKA LNEALKLFKM HSPQTAAMLF TVDNEAGKIT 910 920 930 940 950 960 CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDVSAQA TGKNVGCLQE ALQLATSFAQ LRLGDVKN

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR858480 mRNA. Translation: CAH90708.1.
RefSeq	NP_001125391.1.
UniGene	Pab.19224
3D structure databases
SMR	Q5RC02. Positions 5-453, 523-754.
ModBase	Search...
Genome annotation databases
GeneID	100172296.
Organism-specific databases
CTD	100172296.
Phylogenomic databases
HOVERGEN	Q5RC02.
Enzyme and pathway databases
BRENDA	6.1.1.7. 269192.
Family and domain databases
InterPro	IPR002318. Ala-tRNA-synth_IIc. IPR018162. Ala-tRNA-synth_IIc_anticod-bd. IPR018165. Ala-tRNA-synth_IIc_core. IPR018164. Ala-tRNA-synth_IIc_N. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
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]
TIGRFAMs	TIGR00344. alaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYAC_PONAB

Accession

Primary (citable) accession number: Q5RC02

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	December 21, 2004
Last modified:	February 9, 2010
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)