Alanine--tRNA ligase, mitochondrial precursor

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Q14CH7 (SYAM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

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

Gene names

Name:	Aars2
Synonyms:	Aarsl, Gm89, Kiaa1270

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	980 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. 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 By similarity.
Subcellular location	Mitochondrion HAMAP-Rule MF_03133.
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
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial alanyl-tRNA aminoacylation Inferred from electronic annotation. Source: Compara mitochondrial respiratory chain complex assembly Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI
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

Transit peptide

1 – 23

Mitochondrion Potential

Chain

24 – 980

957

Alanine--tRNA ligase, mitochondrial HAMAP-Rule MF_03133

PRO_0000250726

Sites

Metal binding

627

Zinc Potential

Metal binding

631

Zinc Potential

Metal binding

744

Zinc Potential

Metal binding

748

Zinc Potential

Experimental info

Sequence conflict

618 – 625

AWRMGCMV → RSRPG in BAD32417. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q14CH7 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 7734BC58CDB5463D
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FASTA

980

106,783

        10         20         30         40         50         60 
MAVALAAAAG KLRRAIGRSC PWQPFSTEPG PPHGAAVRDA FLSFFRDRHG HRLVPSATVR 

        70         80         90        100        110        120 
PRGDPSLLFV NAGMNQFKPI FLGTVDPRSE MAGFRRVVNS QKCVRAGGRH NDLEDVGRDL 

       130        140        150        160        170        180 
SHHTFFEMLG NWAFGGEYFK EEACSMAWEL LTQVYGIPED RLWVSYFSGD SQTGLDPDLE 

       190        200        210        220        230        240 
TRDIWLSLGV PASRVLSFGP QENFWEMGDT GPCGPCTEIH YDLAGGVGSP QLVELWNLVF 

       250        260        270        280        290        300 
MQHYREADGS LQLLPQRHVD TGMGLERLVA VLQGKRSTYD TDLFSPLLDA IHQSCGAPPY 

       310        320        330        340        350        360 
SGRVGAADEG RIDTAYRVVA DHIRTLSVCI ADGVSPGMSG APLVLRRILR RAVRYSTEVL 

       370        380        390        400        410        420 
QAPPGFLGSL VPVVVETLGS AYPELEKNSV KIASLVSEDE AAFLASLQRG RRIIDRTVKR 

       430        440        450        460        470        480 
LGPSDLFPAE VAWSLSLSGN LGIPLDLVEL MLEEKGVKLD TAGLEQLAQK EAQHRAQQAE 

       490        500        510        520        530        540 
ADQEDRLCLD VHALEELHRQ GIPTTDDSPK YNYTLHPNGD YEFGLCEARV LQLYSETGTA 

       550        560        570        580        590        600 
VASVGAGQRC GLLLDRTNFY AEQGGQASDR GYLVRTGQQD MLFPVAGAQL CGGFILHEAM 

       610        620        630        640        650        660 
APERLQVGDQ VQLYVDKAWR MGCMVKHTAT HLLSWALRQT LGPTTEQRGS HLNPERLRFD 

       670        680        690        700        710        720 
VATQTLLTTE QLRTVESYVQ EVVGQDKPVF MEEVPLAHTA RIPGLRSLDE VYPDPVRVVS 

       730        740        750        760        770        780 
VGVPVAHALG PASQAAMHTS VELCCGTHLL STGAVGDLVI IGERQLVKGI TRLLAITGEQ 

       790        800        810        820        830        840 
AQQAREVGQS LSQEVEAASE RLSQGSRDLP EAHRLSKDIG RLTEVAESAV IPQWQRQELQ 

       850        860        870        880        890        900 
TTLKMLQRRA NTAIRKLEKG QATEKSQELL KRHSEGPLIV DTVSAESLSV LVKVVRQLCK 

       910        920        930        940        950        960 
QAPSISVLLL SPQPTGSVLC ACQVAQDATP TFTAEAWALA VCSHMGGKAW GSRVVAQGTG 

       970        980 
HTADLEAALG TARAYALSQL

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References

[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/6. 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC079844 mRNA. Translation: AAH79844.1. BC113172 mRNA. Translation: AAI13173.1. BC113779 mRNA. Translation: AAI13780.1. AK173139 Transcribed RNA. Translation: BAD32417.1.
IPI	IPI00470086.
RefSeq	NP_941010.2. NM_198608.2.
UniGene	Mm.329063.
3D structure databases
ProteinModelPortal	Q14CH7.
SMR	Q14CH7. Positions 20-779.
ModBase	Search...
PTM databases
PhosphoSite	Q14CH7.
Proteomic databases
PaxDb	Q14CH7.
PRIDE	Q14CH7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000024733; ENSMUSP00000024733; ENSMUSG00000023938.
GeneID	224805.
KEGG	mmu:224805.
UCSC	uc008cqr.1. mouse.
Organism-specific databases
CTD	57505.
MGI	MGI:2681839. Aars2.
Rouge	Search...
Phylogenomic databases
eggNOG	COG0013.
GeneTree	ENSGT00390000016019.
HOGENOM	HOG000156964.
HOVERGEN	HBG017874.
InParanoid	Q14CH7.
KO	K01872.
OMA	MQYNREA.
OrthoDB	EOG4320XD.
Gene expression databases
Bgee	Q14CH7.
Genevestigator	Q14CH7.
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. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
Pfam	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
ChiTaRS	AARS2. mouse.
NextBio	377373.
SOURCE	Search...

Entry information

Entry name

SYAM_MOUSE

Accession

Primary (citable) accession number: Q14CH7
Secondary accession number(s): Q68FH3, Q69ZM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	August 22, 2006
Last modified:	May 1, 2013
This is version 61 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents