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A2ST90 (SYA_METLZ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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:Mlab_1380
OrganismMethanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z) [Complete proteome] [HAMAP]
Taxonomic identifier410358 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanocorpusculaceaeMethanocorpusculum

Protein attributes

Sequence length913 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 By similarity 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 – 913913Alanine--tRNA ligase HAMAP MF_00036_A
PRO_1000074509

Sites

Metal binding6081Zinc By similarity
Metal binding6121Zinc By similarity
Metal binding7111Zinc By similarity
Metal binding7151Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A2ST90 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 9081336847C9BDA0

FASTA913101,779
        10         20         30         40         50         60 
MLENEYQLEY FKENGFIRKI CKKCGSAFWT LDPNREICGD APCEPYQFIG NPIFTKHSLT 

        70         80         90        100        110        120 
EMREAYLSFF ERHGHTRINR YPVAARWRDD IYLTIASIAD FQPFVTSGVC PPPANPLTIS 

       130        140        150        160        170        180 
QPCIRLNDLD NVGRSGRHFT CFEMMAHHAF NTDEKPIYWK DRCLELCSGF IESLGGNVFD 

       190        200        210        220        230        240 
LTYKENPWFG GGNAGPSVEV LMGGLEVATL VFMNLSRKNS GKPPVSIDGK DYYEMPLRIV 

       250        260        270        280        290        300 
DTGYGLERFT WASCGTPTAY DAVFPEMIPR ILTAAGMEDR LENPEVERIL GLNAKFAGLM 

       310        320        330        340        350        360 
DIRGEKIRDL RQQVADATNI SVAKLEEIIV PMETVYALCD HTRCLAYMLG DLIVPSNVRE 

       370        380        390        400        410        420 
GYLARLVLRR SIRMMQDLNM DDDLGDLVVS QMKTIGLANF EQDEDIVRHI INREVEKYDT 

       430        440        450        460        470        480 
TIERGTRTVQ RVGQTYVKKN EPVPLAELIT LYDSHGIPVD LMGKILKDTG AEFEIPDDFD 

       490        500        510        520        530        540 
SQIADMHSEN ETEKPVSPLA KYAERIAKIP ETRKSFYERP ADMEFDATVL DIFDNYVVLD 

       550        560        570        580        590        600 
ATLFYPEGGG QPSDTGMLVT KSTMVRVDEV VKWENVILHK VRENTLKRGD RVKGVLDEDR 

       610        620        630        640        650        660 
RWALMRHHSA THMVLRAAKE VLGPHVHQAG SQLSTDVARL DIRHYTHITP EELKQMETIA 

       670        680        690        700        710        720 
NRLVMENLPT MVKIENRVKA EQKFGFALYQ GGVPPGKDIR VVQMGAEVQA CAGTHCQSTG 

       730        740        750        760        770        780 
EIGPIKILKL EHIQDGVERI EFAAGFAALD AMQHIQSLLN TSADTLSVQT ENLPGSVDRF 

       790        800        810        820        830        840 
FTEWKDQRKE IEKLRAKIAE LELSRIEGIN IGGVEVVIKQ IDVSRKELVT VAGKIAERGG 

       850        860        870        880        890        900 
VTVLITTADG LGVVASSGTG KIHAGKLVGE VCAELGGKGG GKENLAQGAG ADPSAVGKAL 

       910 
LKAESFIRAE FNS 

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References

[1]"Complete genome sequence of Methanocorpusculum labreanum type strain Z."
Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L., Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.
Stand. Genomic Sci. 1:197-203(2009) [PubMed: 21304657] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43576 / DSM 4855 / Z.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000559 Genomic DNA. Translation: ABN07546.1.
RefSeqYP_001030813.1. NC_008942.1.

3D structure databases

ProteinModelPortalA2ST90.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2ST90.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4794418.
GenomeReviewsGene locus Mlab_1380 in contig CP000559_GR.
KEGGmla:Mlab_1380.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBA2ST90.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycMLAB410358:MLAB_1380-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_METLZ
AccessionPrimary (citable) accession number: A2ST90
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 6, 2007
Last modified: January 25, 2012
This is version 39 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