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Q8U425 (SYA_PYRFU) 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
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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:PF0270
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length914 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
Reference 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 – 914914Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000075273

Sites

Metal binding6131Zinc By similarity
Metal binding6171Zinc By similarity
Metal binding7171Zinc By similarity
Metal binding7211Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8U425 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 467F593731BD8BC1

FASTA914104,906
        10         20         30         40         50         60 
MEFVMKTRMF EEEGWIRKTC KVCGKPFWTL DPDRETCGDP PCDEYQFIGK PGIPKKYTLD 

        70         80         90        100        110        120 
EMREKFLSFF EKHEVYPHGR VKRYPVLPRW RDDVLLVGAS IMDFQPWVIS GEADPPANPL 

       130        140        150        160        170        180 
TISQPSIRFT DIDNVGITGR HFTIFEMMAH HAFNYPGKHI YWIDETVELA FEFFTKELKM 

       190        200        210        220        230        240 
KPEDITFKEN PWAGGGNAGP AFEVLYKGLE VATLVFMQYK KAPANADPSQ VVIIKGEKYV 

       250        260        270        280        290        300 
PMETKVVDTG YGLERLVWMS QGTPTAYDAV LGYVIEPLKR MAGVEKIDER ILMENSRLAG 

       310        320        330        340        350        360 
MFDIEDMGDL RYLREQVAKR VGISVEELER LIRPYELIYA IADHTKALTF MLADGVVPSN 

       370        380        390        400        410        420 
VKAGYLARLL IRKSIRHLRE LGLEVPLAEI VAMHIKELSP TFPEFKEMED IILEMIELEE 

       430        440        450        460        470        480 
KKYAETLRRG SDLVKREIAK LKKKGANEIP LEKLITFYES HGLTPEIVKE IAEKEGVKVH 

       490        500        510        520        530        540 
IPDNFYSLVA KEAEKQVEEK EEEVVDFELV KDLPDTRTLY YEDPFMKEFD AKVLKVIEDW 

       550        560        570        580        590        600 
VVLDQTAFYP EGGGQPYDTG ILVVDGEEVK VTNVQKVGKV ILHKVERPEL FKEGTIVHGR 

       610        620        630        640        650        660 
IDWERRIQHM RHHTGTHVLM GALVRVLGKH VWQAGSQLST DWARLDITHY KRISDEEIKE 

       670        680        690        700        710        720 
IERLANRVVM ENRRVRWEWL PRTEADEKYG FRLYQGGVVP GRIIRILNIE DWDVQACGGT 

       730        740        750        760        770        780 
HLPSTGLIGP IKILRTERIQ DGVERIIFAC GEAAVREWQK EREIIKRTSQ ILRVPPEKLP 

       790        800        810        820        830        840 
ETAERFFNEW KEARKEVEKL RKELAKLLVY ELESKVEKVG EIEFIGEIVE GSMDDLREAA 

       850        860        870        880        890        900 
NKLRKENRVV VLVNKEGHFV VAVGDKLPYT AGEFAKLITS VAGGGGGGRK ELAQGKIRDI 

       910 
EKAKEAIEKV KGSL

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References

[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE009950 Genomic DNA. Translation: AAL80394.1.
RefSeqNP_577999.1. NC_003413.1.

3D structure databases

ProteinModelPortalQ8U425.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000005140; EBPYRP00000005001; EBPYRG00000005139.
GeneID1468104.
GenomeReviewsGene locus PF0270 in contig AE009950_GR.
KEGGpfu:PF0270.
NMPDRfig|186497.1.peg.275.

Phylogenomic databases

GeneTreeEBGT00050000022658.
HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBQ8U425.
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.
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_PYRFU
AccessionPrimary (citable) accession number: Q8U425
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 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

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