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A4YH91 (SYA_METS5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:Msed_1638
OrganismMetallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]
Taxonomic identifier399549 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Metallosphaera

Protein attributes

Sequence length904 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 – 904904Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000347883

Sites

Metal binding6001Zinc By similarity
Metal binding6041Zinc By similarity
Metal binding7041Zinc By similarity
Metal binding7081Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A4YH91 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: C7C2BE9F49F38EBF

FASTA904102,487
        10         20         30         40         50         60 
MKGNQEEYRL KFFLDHDYLR RECKVCKTPF WSKDKTREDC ADIPCSDYYF LDMKESNLNW 

        70         80         90        100        110        120 
SVSEARRRFL DFFRRNGHEI IPPKPVLARW REDLYLTIAS IVDFQPYITS GISPPPANPL 

       130        140        150        160        170        180 
VVSQPCIRMD DVDNVGITFG RHLTTFEMGG HHAFNYPDKF LYWKDETVAY AKEFFTKEMG 

       190        200        210        220        230        240 
IPEELLNFKE SWWEGGGNAG PSFEVTVGGL ELATLVFMQY EIRDGEYVPL KLKIVDTGYG 

       250        260        270        280        290        300 
IERLAWFTQK TPTAFHAIYG ELVDKFLEKL GLPSLNPDML KVASRFAGRI DPDVPSTIQG 

       310        320        330        340        350        360 
HREQVAKAMG LPVKEVSEEL TRAARVFQVL DHTKTIALML GDGLVPSSGG EGYLGRLLIR 

       370        380        390        400        410        420 
RALRTLKLLN VDVRLSELVD MQIGFWGKDF TQLVRNRDYI LDAVNLEQEK FNEILNRMSS 

       430        440        450        460        470        480 
VVSSLTKKKE IGVEDLIQLY DSQGIPPDLM AEEMRSKGLK VEVPHNFYSI VAKRHQSAPV 

       490        500        510        520        530        540 
KKEWDTTKLP PEVVKQVKDL PPTEKLYYKD QYARNFEGVI VKSLGKYLVL DRTVFYPEGG 

       550        560        570        580        590        600 
GQLGDQGWLL LDGQRVKVVD TQKVGDVVVH VLEREISAKE GDKVKGEIDW VRRFRMMRHH 

       610        620        630        640        650        660 
TGTHVVLAAA KKLLGDHVWQ AGAEKTPEKA RLDITHHRNL TREEVKRIEE MANLVVDDRR 

       670        680        690        700        710        720 
PVTPFEINRT EAETKYGVSI YEGGVPNKAV IRLLEIKDWD VESCGGTHVA NTADIGGIKI 

       730        740        750        760        770        780 
VNVEKIQDGI IRLEYVAGDV ISSYAGNLED KLEGLASKLE TSTSQIESRV EKLKEENERM 

       790        800        810        820        830        840 
KELIAFYRRQ YLDDLEKHVE TRNVGKVKIV ILPSLKDEDL EREAMRRLTS TQGVVVIHVN 

       850        860        870        880        890        900 
QVNGKLQIEI GTSKDLNVST VVTELVKAGG KGGGRGTFGS VMIEKGTKEE VIDIVERAIK 


GGNS

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References

[1]"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
Appl. Environ. Microbiol. 74:682-692(2008) [PubMed: 18083856] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51363 / DSM 5348.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000682 Genomic DNA. Translation: ABP95793.1.
RefSeqYP_001191717.1. NC_009440.1.

3D structure databases

ProteinModelPortalA4YH91.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4YH91.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5104843.
GenomeReviewsGene locus Msed_1638 in contig CP000682_GR.
KEGGmse:Msed_1638.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBA4YH91.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycMSED399549:MSED_1638-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_METS5
AccessionPrimary (citable) accession number: A4YH91
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 36 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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