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Q8TU79 (SYA_METAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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:alaS
Ordered Locus Names:MA_0194
OrganismMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifier188937 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length925 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 925925Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000075263

Sites

Metal binding6111Zinc By similarity
Metal binding6151Zinc By similarity
Metal binding7141Zinc By similarity
Metal binding7181Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TU79 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 01A32F452240DB2E

FASTA925103,654
        10         20         30         40         50         60 
MLEDEYQLDF FKNNGFVRKQ CQKCGKFFWT RDPERNTCGD APCDPYSFIG SPVFSREFNI 

        70         80         90        100        110        120 
SEMREYYLSF FEARGHTRLD RYPVVARWRD DIYLTIASIA DFQPFVTSGQ VPPPANPLTI 

       130        140        150        160        170        180 
SQPCIRLNDL DSVGRSGRHL TNFEMMAHHA FNKRGNEIYW KEHTLELCDE LLTSLKVDPF 

       190        200        210        220        230        240 
AVTYKEEPWA GGGNAGPCVE VIVHGLELAT LVFMDLKTDK KGDILIKGET YSKMDNYIVD 

       250        260        270        280        290        300 
TGYGLERFVW ASKGSPTIYD ALFPGIVNEL MGLAGLEHEL NNTEYSNILA QNARLAGFMD 

       310        320        330        340        350        360 
VSEKANLLEL RKKVASSIGM TVDKLSVIME PVEKVYAITD HTRCLTFMLG DGIIPSNVKA 

       370        380        390        400        410        420 
GYLARLVLRR TLRMMKDLDI RTPLSEIVDM HIRNMPEYPE FRANFPVIQD ILESEEEKFN 

       430        440        450        460        470        480 
ITMERGRRII QKSASHFKKT GEKIPLSQLT ELYDSHGIPP EMAKEVAADI GVGVEFPDNF 

       490        500        510        520        530        540 
YSIIGELHNK AEEKEEEVIP FAERLKHLPK TKRRFYDEPT RLEFEAVVLD VFDNHIVLDN 

       550        560        570        580        590        600 
TFFYAEGGGQ PADIGTISVG DIVYKVVDVQ VYEGVIVHTV DIPDGELEIT KGDIITGKVD 

       610        620        630        640        650        660 
ERRRMTLARH HTATHIVNDA ARKVLGKHIW QAGAQKFEDH SRLDLSHYKH ISPEELKQIE 

       670        680        690        700        710        720 
LLANRTVMEN KRVITEWMPR IEAEQVYGFG LYQGGVPPGE KIRIVKVGDD VEACGGTHCL 

       730        740        750        760        770        780 
STGVIGPIKI LKTERIQDGV ERVEFAAGIA AVRAMQKMES LLVDSAKTLS VPPEHLPVSV 

       790        800        810        820        830        840 
ERFFGEWKDL KKENERLKED LARSRVYRML GDASELAGLR VVSEQVPGAD SLELQKIATE 

       850        860        870        880        890        900 
LLKQENVVTL LASDLEGVKL VASVGEKAIE CGINAGNLVR EMSKIVGGGG GGKPALAMGG 

       910        920 
GTDPTRIQDA LSRGLELVKE ACKEA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010299 Genomic DNA. Translation: AAM03647.1.
RefSeqNP_615167.1. NC_003552.1.

3D structure databases

ProteinModelPortalQ8TU79.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1472086.
GenomeReviewsGene locus MA_0194 in contig AE010299_GR.
KEGGmac:MA0194.
NMPDRfig|188937.1.peg.193.

Phylogenomic databases

HOGENOMHBG392147.
OMAMFTNSGM.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycMACE188937:MA0194-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.
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_METAC
AccessionPrimary (citable) accession number: Q8TU79
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 2002
Last modified: January 25, 2012
This is version 61 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