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Q9HN24 (SYA_HALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:alaS
Ordered Locus Names:VNG_2283G
OrganismHalobacterium salinarium (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
Taxonomic identifier64091 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium

Protein attributes

Sequence length929 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain By similarity. HAMAP MF_00036_A

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_A

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_A

Subcellular location

Cytoplasm HAMAP MF_00036_A.

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 MF_00036_A

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 929929Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000075262

Sites

Metal binding6191Zinc By similarity
Metal binding6231Zinc By similarity
Metal binding7221Zinc By similarity
Metal binding7261Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HN24 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: E373396311005812

FASTA929100,773
        10         20         30         40         50         60 
MSDLESAYRL EYFEEEGFHR RECVSCGAHF WTRDGDRETC GEPPCEDYQF IDNPGFDASY 

        70         80         90        100        110        120 
SLTEMRSAMV SYFERAGHDS IDPYPVAANR WRDDVLLTQA SIYDFQPHVT SGASPPPANP 

       130        140        150        160        170        180 
LVVSQPCIRM QDIDNVGKTG RHTMAFEMLG HHAFNADEGT DYAYDGEVYW KDTAVEHCEG 

       190        200        210        220        230        240 
LLADVGVSLD EVTFIEDPWV GGGNAGAAFE VIYRGLELAT LVFMSLERDP DGEYEMKDGH 

       250        260        270        280        290        300 
TYAEMDRRVV DTGYGVERWT WMSQGTPTVY EAVYPDTIDF LKEQAGIEHT DEEAELVHRA 

       310        320        330        340        350        360 
SKHAGNLDID EVADIEDARA GIAAELGVDA ERLTELVAPL EDIYAIADHS RVLAYMFGDG 

       370        380        390        400        410        420 
IVPSNVGTGY LARMVLRRTK RLVDDIGADV PLDELVDMQA DRLGYENRDT IRSIVRSEVE 

       430        440        450        460        470        480 
KYGETLERGG RRVEQLAEEY ADRGEPVPTD ELIELYDSHG IQPGMVADIA ADVGATVDAP 

       490        500        510        520        530        540 
DDFYSLVAAR HDDGDSGAAG GDGGGDDRLA DLPETETLYY DDAYGSEFEA VVLDVFEREG 

       550        560        570        580        590        600 
EDGDGAFDVV LDQTMFYPEG GGQPADTGVL TGDDHTVDVI DVQERDGVVL HRTTDNPGKG 

       610        620        630        640        650        660 
EFVRGQIDTE RRRRLMAHHT ATHIVVYAAR QVLGEHVRQA GAQKGVDSSR IDVTHYERVD 

       670        680        690        700        710        720 
RETVKEIERV ANEIVRANTS VQCEWPDRHE AEAEYGFDLY QGGIPAGEQI RLVHVDDDVQ 

       730        740        750        760        770        780 
ACGGTHVART GEIGSIKILN AERVQDGVER LTFAAGAAAV EHVQGQEDDL RAAAEVLDVT 

       790        800        810        820        830        840 
PAEVPETAER FFTEWKDRGK TIDDLKEQLA EARASGGGAG EEVDVAGTTA VVQRVDGDMD 

       850        860        870        880        890        900 
ELQATANALV DGGQVAVVGS GADGAQFVVG VPDGVPVNAG EVVGELAAMV GGGGGGPPDF 

       910        920 
AQGGGPDAER LDDALSRAAD VLGDAASAE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004437 Genomic DNA. Translation: AAG20397.1.
PIRA84379.
RefSeqNP_280917.1. NC_002607.1.

3D structure databases

ProteinModelPortalQ9HN24.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1448699.
GenomeReviewsGene locus VNG_2283G in contig AE004437_GR.
KEGGhal:VNG2283G.
NMPDRfig|64091.1.peg.1943.

Phylogenomic databases

HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBQ9HN24.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycHSP64091:VNG2283G-MONOMER.

Family and domain databases

HAMAPMF_00036_A. Ala_tRNA_synth_A.
[Tree]
InterProIPR002318. Ala-tRNA-synth_IIc.
IPR018162. Ala-tRNA-synth_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR022429. Ala-tRNA_synth_arc.
IPR003156. Pesterase_DHHA1.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
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.
TIGRFAMsTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_HALSA
AccessionPrimary (citable) accession number: Q9HN24
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: March 1, 2001
Last modified: January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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