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A6US09 (SYA_METVS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:Mevan_1384
OrganismMethanococcus vannielii (strain SB / ATCC 35089 / DSM 1224) [Complete proteome] [HAMAP]
Taxonomic identifier406327 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length892 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 – 892892Alanine--tRNA ligase HAMAP MF_00036_A
PRO_1000074513

Sites

Metal binding5961Zinc By similarity
Metal binding6001Zinc By similarity
Metal binding7001Zinc By similarity
Metal binding7041Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A6US09 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 12FC466D1C26F59E

FASTA892101,699
        10         20         30         40         50         60 
MEITHDYKVK LFEEMNFERK QCSECKQWFW TLDKERITCG DSPCDKYSFI GNPITTKKYT 

        70         80         90        100        110        120 
YNEMVKEFTN FFDERGHSPV KRSPVIAKRW RDDILLTIAS IAVFQPWVTN GLVKPVKNPL 

       130        140        150        160        170        180 
VITQPCIRLN DIDNVGRTGR HLTCFTMGAH HAFNSKDEYK YWTDKTVELC FELMQKLGID 

       190        200        210        220        230        240 
GHTITFIESW WEGGGNAGPC YEVITHGVEL ATLVFMQYKK VGNNYEEIPL KIVDTGYGIE 

       250        260        270        280        290        300 
RFAWASQGTP TVYEALFSDI IEKLKKNANI PIVDEKIMAE SATLAGLMDI ENVGDLKALR 

       310        320        330        340        350        360 
QKVAEKIGMD VNELDRLISP LEYIYAISDH TRCLSFMFGD GIVPSNVKEG YLARLVLRKT 

       370        380        390        400        410        420 
LRYMEKVGIS YSIKEIILMQ LESMKEVYPE LIGMKDYIMD VLDSEEKKYI QTVNKGRGIV 

       430        440        450        460        470        480 
ERMTKLKSEI TLNDLINLYD SNGLPPEIVK DIIDEINKTS KTKISIHVPD NFYTIVAERH 

       490        500        510        520        530        540 
EEEKAEEVAI LKHELPELDL PKTELLFFKN TMQSEFEAKV LKIVDKYIIL DRTVFYAEGG 

       550        560        570        580        590        600 
GQKYDIGQIS GVDVVDVQKK NGIVFHKVLD ISKFKEGNLV KGELNFENRL KLMRNHTATH 

       610        620        630        640        650        660 
VINAALKQVL GKHVWQTGSN VDTEKGRLDV THYERISRKE IKEIEKIANE IVLLGKPVTC 

       670        680        690        700        710        720 
KFMDRNDAEQ EYGFKIYQGG VVPGDTLRIV EIDGIDVEAC GGTHVTNTSE IGYIKVLKTE 

       730        740        750        760        770        780 
RIQDGVERLE YSTGMGSIFE IAALEDILLD SAEVLGVPIE NLPKTAKRFF EEWKEQKKVI 

       790        800        810        820        830        840 
EELQKKVGEL LKYELLEKFE KVGNLEILVE KVSGTSNELM AIADNLATNG KIVILMNDTD 

       850        860        870        880        890 
YILCKKGENV EISMKELIQK IGKGGGKENL AQGKYSTSKE QIREKAFELL KQ 

« Hide

References

[1]"Complete sequence of Methanococcus vannielii SB."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I. expand/collapse author list , Sieprawska-Lupa M., Whitman W.B., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB / ATCC 35089 / DSM 1224.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000742 Genomic DNA. Translation: ABR55281.1.
RefSeqYP_001323893.1. NC_009634.1.

3D structure databases

ProteinModelPortalA6US09.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6US09.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5324766.
GenomeReviewsGene locus Mevan_1384 in contig CP000742_GR.
KEGGmvn:Mevan_1384.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAMFTNSGM.
ProtClustDBPRK13902.

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.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF01411. 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_METVS
AccessionPrimary (citable) accession number: A6US09
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: January 25, 2012
This is version 33 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