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P36428 (SYA_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine--tRNA ligase
EC=6.1.1.7
Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS
Gene names
Name:ALATS
Synonyms:ALARS
Ordered Locus Names:At1g50200
ORF Names:F14I3.17
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length1003 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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

Mitochondrion. Cytoplasm.

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.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Sequence caution

The sequence AAD50044.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Mitochondrial (identifier: P36428-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Cytoplasmic (identifier: P36428-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4949Mitochondrion
Chain50 – 1003954Alanine--tRNA ligase
PRO_0000035793

Sites

Metal binding6461Zinc Potential
Metal binding6501Zinc Potential
Metal binding7651Zinc Potential
Metal binding7691Zinc Potential

Amino acid modifications

Modified residue521Phosphoserine Ref.6

Natural variations

Alternative sequence1 – 4848Missing in isoform Cytoplasmic.
VSP_018903

Experimental info

Sequence conflict1941G → R in CAA80380. Ref.1
Sequence conflict1941G → R in CAA80381. Ref.1
Sequence conflict7311V → A in CAA80380. Ref.1
Sequence conflict7311V → A in CAA80381. Ref.1
Sequence conflict9101R → Q in CAA80380. Ref.1
Sequence conflict9101R → Q in CAA80381. Ref.1
Sequence conflict9851S → F in CAA73145. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform Mitochondrial [UniParc].

Last modified June 20, 2002. Version 3.
Checksum: 0A85DA940C5BB308

FASTA1,003110,489
        10         20         30         40         50         60 
MRLVKAASLL ISSTKPPSRV FYSSHLRRPF FSHFRFSSSS STSSSVAVMP GSEPSETQWP 

        70         80         90        100        110        120 
AKRVRDTYVD FFRGKGHKFW PSSPVVPHND PTLLFANAGM NQYKPIFLGT ADPNTELSKL 

       130        140        150        160        170        180 
SRACNTQKCI RAGGKHNDLD DVGKDTYHHT FFEMLGNWSF GDYFKKEAIE WAWELLTKVY 

       190        200        210        220        230        240 
GLPTDRIYAT YFGGDEKAGL QPDNEARDIW LKVLPSGRVL PFGCKDNFWE MGDTGPCGPC 

       250        260        270        280        290        300 
TEIHYDRIGN RDAASLVNND DPTCLEIWNL VFIQFNRESD GSLKPLPAKH VDTGMGFERL 

       310        320        330        340        350        360 
TSVLQNKMSN YDTDVFMPIF DDIQKATGAR PYSGKVGPED VDRVDMAYRV VADHIRTLSF 

       370        380        390        400        410        420 
AIADGSRPGN EGREYVLRRI LRRAVRYGKE ILKAEEGFFN GLVSSVIRVM GDVFTELKEH 

       430        440        450        460        470        480 
EKKITDIIKE EEASFCKTLA KGIEKFRKAG QAVQGNTLSG DDAFILWDTY GFPLDLTQLM 

       490        500        510        520        530        540 
AEERGLLVDV DGFNKAMEEA RERSRSAQNK QAGGAIVMDA DATSTLHKAG VSATDDSFKY 

       550        560        570        580        590        600 
IWFQDHESEL KAIYTGSTFL ESSAASDNVG LVLGSTSFYA EQGGQIFDTG LIEGSFGTFN 

       610        620        630        640        650        660 
VCNVQIFGGF VLHIGYLSKE TGEVSVGDKV ICKVDYERRK LIAPNHTCTH MLNYALKEVL 

       670        680        690        700        710        720 
GDHIDQKGSI VLPEKLRFDF SHGKPVDPED LRRIESIVNK QIKDELDVFS KEAVLSEAKR 

       730        740        750        760        770        780 
IKGLRAVFGE VYPDPVRVVS IGRKVEDLLA DPENNEWSLL SSEFCGGTHI TNTREAKAFA 

       790        800        810        820        830        840 
LLSEEGIAKG IRRVTAVTTE CAFDALNAAS LLEREVEDAS RAEGSALEKK VSALKSRVDA 

       850        860        870        880        890        900 
AIIPAAKKAD IRTKIASLQN EVRKAQKKIA EQNLKKSVKL ATEAAESAAS DGKTFCIIQL 

       910        920        930        940        950        960 
DVGLDAAAVR EAVSKVMEKK GMSIMVFSTD ESTNKAVVCA GVPEKSDQFK PLDVTEWLTT 

       970        980        990       1000 
ALGPLKGRCG KGKGGLASGQ GTDASQVQAA LDMASSFASM KLN

« Hide

Isoform Cytoplasmic [UniParc].

Checksum: 78F291B2EFA2662B
Show »

FASTA955105,172

References

« Hide 'large scale' references
[1]"The same Arabidopsis gene encodes both cytosolic and mitochondrial alanyl-tRNA synthetases."
Mireau H., Lancelin D., Small I.
Plant Cell 8:1027-1039(1996) [PubMed: 8672889] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CYTOPLASMIC AND MITOCHONDRIAL).
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYTOPLASMIC).
Strain: cv. Columbia.
[5]"An Arabidopsis embryonic lethal mutant with reduced expression of alanyl-tRNA synthetase gene."
Ge S.J., Yao X.L., Yang Z.X., Zhu Z.P.
Cell Res. 8:119-134(1998) [PubMed: 9669027] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 753-1003.
Strain: cv. Columbia.
[6]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, MASS SPECTROMETRY.
Strain: cv. Columbia.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z22673 mRNA. Translation: CAA80380.1.
Z22673 mRNA. Translation: CAA80381.1.
AC007980 Genomic DNA. Translation: AAD50044.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE32524.1.
BT002526 mRNA. Translation: AAO00886.1.
BT008807 mRNA. Translation: AAP68246.1.
Y12555 mRNA. Translation: CAA73145.1.
IPIIPI00537243.
IPI00760312.
PIRD96538.
RefSeqNP_175439.2. NM_103905.3.
UniGeneAt.1836.

3D structure databases

ProteinModelPortalP36428.
SMRP36428. Positions 17-803.
ModBaseSearch...

Protein-protein interaction databases

STRINGP36428.

Proteomic databases

PRIDEP36428.
ProMEXP36428.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G50200.1; AT1G50200.1; AT1G50200.
GeneID841442.
GenomeReviewsGene locus AT1G50200 in contig CT485782_GR.
KEGGath:AT1G50200.

Organism-specific databases

GeneFarm2386.
TAIRAt1g50200.

Phylogenomic databases

eggNOGKOG0188.
GeneTreeEPGT00070000028951.
HOGENOMHBG354397.
InParanoidP36428.
OMAEGSFGTF.
PhylomeDBP36428.
ProtClustDBPLN02900.

Gene expression databases

ArrayExpressP36428.
GenevestigatorP36428.
GermOnlineAT1G50200. Arabidopsis thaliana.

Family and domain databases

InterProIPR002318. 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]
KOK01872.
PfamPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMsTIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_ARATH
AccessionPrimary (citable) accession number: P36428
Secondary accession number(s): O04159, Q8GUG2, Q9SX40
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 20, 2002
Last modified: January 25, 2012
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents