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Q5YTJ9 (SYA_NOCFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:NFA_36440
OrganismNocardia farcinica (strain IFM 10152) [Complete proteome] [HAMAP]
Taxonomic identifier247156 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Nocardia

Protein attributes

Sequence length888 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_B

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_B

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_B

Subcellular location

Cytoplasm HAMAP MF_00036_B.

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_B

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 – 888888Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075163

Sites

Metal binding5711Zinc Potential
Metal binding5751Zinc Potential
Metal binding6741Zinc Potential
Metal binding6781Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q5YTJ9 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 06D87E81551659D9

FASTA88895,639
        10         20         30         40         50         60 
MQTHEIRRRF LDHFVRAGHT EVPSASLILA DPNLLFVNAG MVQFKPYFLG QEAPPYPRAT 

        70         80         90        100        110        120 
SVQKCVRTGD IEEVGVTTRH NTFFQMAGNF SFGDYFKEGA ITLAWELISK PQSEGGFGFD 

       130        140        150        160        170        180 
PERIWVTAYQ DDPEAAEIWH RMAGIPKERI QFRDGKDNYW DMGVPGPGGP CSEIYFDRGP 

       190        200        210        220        230        240 
AYGKDGGPVA DEDRYLEIWN LVFMQDVRGE LSPKQGHPPI GSLPKKNIDT GMGIERVAML 

       250        260        270        280        290        300 
LQGVDNVYET DLLRPIIGKA EELTGRRYGA EHASDVRFRV IADHARTAAM LISDGVNPGN 

       310        320        330        340        350        360 
DGRGYVLRRL LRRIVRSARL LGAEKPVMAE FMQVVSDLMS PSYPELATDF DRIRTVAVGE 

       370        380        390        400        410        420 
ETAFLKTLTT GSTLFDNTAA AVKAKGGTKI AGADAFTLHD TYGFPIDLTL EMAAEAGLSV 

       430        440        450        460        470        480 
DEEGFRSLMA EQRRRAKEDA AARKHAHADL SIYKELVDRG ATEFTGFDEL TSEAHVLALI 

       490        500        510        520        530        540 
ADGVRVPTAT QGQDVEVILD RSPLYAESGG QIADRGSITA SGLKLRVNDV QKIAKKLWVH 

       550        560        570        580        590        600 
KTTVEQGQIT EGDVVLAQAD PAWRRGATQG HSGTHMVHAA LRQVLGPNAV QAGSLNKPGY 

       610        620        630        640        650        660 
LRFDFNWQGQ LSEQQKADIE AVSNDAVGAD FPVNTFVTDL PKAKQMGALA LFGENYGDEV 

       670        680        690        700        710        720 
RVVEIGGPFS MELCGGTHVQ HSSQIGPITL LGESSVGSGV RRVEAFVGLD SYKYLAKERA 

       730        740        750        760        770        780 
LLAGVASSLK VPSEEVPARV EQLVERLKVA EKELERTKIA AVLSSAGKFV EEAERVGRVL 

       790        800        810        820        830        840 
LVAAAAPEGV AAGDLRTLAT DIRGRFGSEP AVVVLLGNAD GKVPFVVAVN KSAQEIGVKA 

       850        860        870        880 
GELVGSFGPS IAGRGGGKPE MAQGAGSDPS GIPAGLAAVR ARVAEIAG

« Hide

References

[1]"The complete genomic sequence of Nocardia farcinica IFM 10152."
Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K., Shiba T., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004) [PubMed: 15466710] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IFM 10152.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP006618 Genomic DNA. Translation: BAD58492.1.
RefSeqYP_119856.1. NC_006361.1.

3D structure databases

ProteinModelPortalQ5YTJ9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3109920.
GenomeReviewsGene locus NFA_36440 in contig AP006618_GR.
KEGGnfa:nfa36440.
NMPDRfig|247156.1.peg.3557.
PATRIC22736908. VBINocFar94200_3690.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAGESKTDQ.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycNFAR247156:NFA36440-MONOMER.

Family and domain databases

HAMAPMF_00036_B. Ala_tRNA_synth_B.
[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.
IPR023033. Ala_tRNA_synth_euk/bac.
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.
TIGRFAMsTIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_NOCFA
AccessionPrimary (citable) accession number: Q5YTJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: November 23, 2004
Last modified: January 25, 2012
This is version 50 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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