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A4FBD3 (SYA_SACEN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:SACE_2052
OrganismSaccharopolyspora erythraea (strain NRRL 23338) [Complete proteome] [HAMAP]
Taxonomic identifier405948 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Saccharopolyspora

Protein attributes

Sequence length890 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 By similarity 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 – 890890Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347773

Sites

Metal binding5721Zinc Potential
Metal binding5761Zinc Potential
Metal binding6741Zinc Potential
Metal binding6781Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A4FBD3 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: E0B60C2EBC7E2E0C

FASTA89095,702
        10         20         30         40         50         60 
MQTHEINQRF TEHFRKAGHT VVPSASLILD DPTLLFVNAG MVQFKPYFLG DAPAPYPRAT 

        70         80         90        100        110        120 
SIQKCVRTGD IDEVGKTTRH NTFFQMAGNF SFGDYFKEGA MEHAWGLLTS SQADGGYGFD 

       130        140        150        160        170        180 
PERLWVTVFE KDEEAAALWQ KVTGIPAERI QVRDAKDNYW DMGVPGPGGP CSEIYYDRGP 

       190        200        210        220        230        240 
KYGREGGPVV DEDRYIEIWN LVFMQDIRGE LPPKEGHPPI GELPTKNIDT GMGVERVACL 

       250        260        270        280        290        300 
LQGVENVYET DLVRPVIAKA EELSGRSYGA NHEDDVRFRV IADHARSGVM LVGDGVTPGN 

       310        320        330        340        350        360 
EARGYVLRRL LRRIIRSTRL LGVHEPVLGE FAAVVRDAMA PSYPELVTEF DRIDSVMRNE 

       370        380        390        400        410        420 
EDAFLSTLTA GSKIFDLAVA DTKKAGGTQL AGAKAFQLHD TYGFPIDLTL EMASEQGLSV 

       430        440        450        460        470        480 
DEHGFRELMS EQRRRAKEDA KSRKSGHGDL STYRTLLDQH GTTEFLGYTD LQAQSRVLGL 

       490        500        510        520        530        540 
LVDGVPAKSA AAGTEVELIL DRTPFYAEGG GQIADTGRLT GPGVEVEVHD VQRAVPGLFV 

       550        560        570        580        590        600 
HRAKVTAGEL GVDTSLEAAV DSKRRHAIER SHSATHLVHA AVRSAYGKRA AQAGSLNSPG 

       610        620        630        640        650        660 
RMRFDFTAPA AVSGAVLGGV EEEVNSYLQN DVEVQSYTTT MDRAMELGAV ALFGEKYGDQ 

       670        680        690        700        710        720 
VRVVDMGDYS RELCGGTHVG RIGQLGVVKL VADSSVGSGV HRVEALVGMD AMRHISKEHL 

       730        740        750        760        770        780 
LVSRLAEQFK VPAEELPERI AGVVSRLRSA EKELEQLRVA QVLQSAGELA GKGTDVHGVT 

       790        800        810        820        830        840 
LVAEQVPDGV DGGALRALAG EVRGRLGSRP AVVALFSADG DKVSFVVGVN TPAQDLGLKA 

       850        860        870        880        890 
GKLVPSFAAE VGGRGGGKPD MAQGGGSNPA GITAAIAALR TGLDQAVARG

« Hide

References

[1]"Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338."
Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F.
Nat. Biotechnol. 25:447-453(2007) [PubMed: 17369815] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NRRL 23338.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM420293 Genomic DNA. Translation: CAM01358.1.
RefSeqYP_001104283.1. NC_009142.1.

3D structure databases

ProteinModelPortalA4FBD3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4FBD3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4941906.
GenomeReviewsGene locus SACE_2052 in contig AM420293_GR.
KEGGsen:SACE_2052.
PATRIC23411528. VBISacEry28377_2059.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycSERY405948:SACE_2052-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_SACEN
AccessionPrimary (citable) accession number: A4FBD3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: April 17, 2007
Last modified: January 25, 2012
This is version 40 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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