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Q8PWU0 (SYA_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. 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:MM_1486
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length926 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
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 – 926926Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000075266

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q8PWU0 [UniParc].

Last modified October 25, 2002. Version 1.
Checksum: 065D616BFFC6B5FF

FASTA926103,730
        10         20         30         40         50         60 
MLEDEYQLDF FKNNGFVRKQ CQKCGTFFWT RDPERNTCGD APCDPYSFIG SPVFSREFNI 

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

       130        140        150        160        170        180 
SQPCIRLNDL DSVGRSGRHL TNFEMMAHHA FNRRDNEIYW KEHTLELCDE LLNSLKVNPL 

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

       250        260        270        280        290        300 
TGYGLERFVW ASRGSPTIYD ALFPGIVNEL MGLAGIEHEL NDSEYANILA QNARLAGFMD 

       310        320        330        340        350        360 
VSEKANLMEL RKKVASSIGM TVDKLSAIME PVEKVYAITD HTRCLTFMLG DGIIPSNVKA 

       370        380        390        400        410        420 
GYLARLVLRR TLRMMKDLDI RIPLSEIVDM HIKNMPEYPG FRENFPVIQD ILESEEEKFN 

       430        440        450        460        470        480 
TTMERGRRII QKSASHFKKT GEKIPLSQLT ELYDSHGIPP EMAKEVAAEI GVGVEFPDNF 

       490        500        510        520        530        540 
YSIIGELHNK AEEKEEEVNP YAERLKHLPK TKRRFYDEPT RLEFEAVVLD VFDNHVVLDN 

       550        560        570        580        590        600 
TFFYAEGGGQ PADIGTIVAE DTVYRVVDVQ VYEGVILHTI ENPGKELAIT KGELITGKVD 

       610        620        630        640        650        660 
EKRRMTLARH HTATHIVNDA ARKVLGKHIW QAGAQKFEDH SRLDLSHYKH ISPEEIRQIE 

       670        680        690        700        710        720 
LLANRTVMEN KRVVTEWMPR TEAEQVYGFG LYQGGVPPGE KIRIVKVGDD VEACGGTHCT 

       730        740        750        760        770        780 
STGIIGPIKI LKTERIQDGV ERIEFAAGTA AVRAMQKLES LLVDSSKTLS VPPEHLPVSV 

       790        800        810        820        830        840 
DRFFGEWKDL KKENERLKEE LARSRVYRML GDASEVSGLK VITEQVSGAD SLELQKIATE 

       850        860        870        880        890        900 
LLKTENVVAL LASDFEGVKI VASAGEKAMK CGVNAGNLVR EMSKIVGGGG GGKPALAMGG 

       910        920 
GTDPTRIQDA LTRGLELVKT AACKEA 

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References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008384 Genomic DNA. Translation: AAM31182.1.
RefSeqNP_633510.1. NC_003901.1.

3D structure databases

ProteinModelPortalQ8PWU0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1479828.
GenomeReviewsGene locus MM_1486 in contig AE008384_GR.
KEGGmma:MM_1486.
NMPDRfig|192952.1.peg.1486.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBQ8PWU0.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycMMAZ192952:MM1486-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_METMA
AccessionPrimary (citable) accession number: Q8PWU0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: October 25, 2002
Last modified: January 25, 2012
This is version 59 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