Alanine--tRNA ligase, cytoplasmic - Pongo abelii (Sumatran orangutan)

Preferred order of sections

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

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)

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.
Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
Cofactor	Binds 1 zinc ion per subunit Potential.
Subunit structure	Monomer By similarity.
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.
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
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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

Alanine--tRNA ligase, cytoplasmic

PRO_0000075283

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

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)

Tools

Q5RC02 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 8FB2F1F06ECB1128
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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

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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. NM_001131919.1.
UniGene	Pab.19224.
3D structure databases
ProteinModelPortal	Q5RC02.
ModBase	Search...
Proteomic databases
PRIDE	Q5RC02.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100172296.
KEGG	pon:100172296.
Organism-specific databases
CTD	16.
Phylogenomic databases
HOVERGEN	HBG017874.
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. IPR023033. Ala_tRNA_synth_euk/bac. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
KO	K01872.
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...

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:	January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents