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Q10VG8 (SYA_TRIEI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:Tery_4806
OrganismTrichodesmium erythraeum (strain IMS101) [Complete proteome] [HAMAP]
Taxonomic identifier203124 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatorialesTrichodesmium

Protein attributes

Sequence length874 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 – 874874Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347855

Sites

Metal binding5611Zinc Potential
Metal binding5651Zinc Potential
Metal binding6631Zinc Potential
Metal binding6671Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q10VG8 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 65D22B5C5CE87B88

FASTA87496,282
        10         20         30         40         50         60 
MSAKKLTGNE IRKKFLSFYA QREHTILPSA SLVPEDPTVL LTIAGMLPFK PIFLGQQPRQ 

        70         80         90        100        110        120 
YPRATTSQKC IRTNDIENVG RTARHHTFFE MLGNFSFGDY FKPEAIALAW ELSTKIFALP 

       130        140        150        160        170        180 
PERLVVSVFR EDDEAFAIWR DQIGIPAHRI QRMDEADNFW ASGPTGPCGP CSEIYYDFHP 

       190        200        210        220        230        240 
ELGDDHIDLE DDTRFIEFYN LVFMQYNRDA NGNLTPLENR NIDTGMGLER MAQILQKVPN 

       250        260        270        280        290        300 
NYETDLIFPI IKTASDIADI DYRKSDDKTK VSLKVIGDHV RAVANLIADG VTASNVGRGY 

       310        320        330        340        350        360 
ILRRLIRRVV RHGRLIGISG EFTSKVAETA ITLAEDIYPN LRERETVIKA ELQREESRFL 

       370        380        390        400        410        420 
ETLERGEKLL AEIMAKPETK KTQHISGEDA FKLYDTYGFP LELTQEIAEE NGLTVDVSMF 

       430        440        450        460        470        480 
DQEMKLAQIR SQSAHETIDL TAQDGVKLDI DKTQFLGYTD LSSPAQVMAL VGDGEQLETV 

       490        500        510        520        530        540 
QAGAQVQIVL DKTPFYAESG GQIADRGYLS GDSLVVRIED VQKQNNIFVH FGRIERGRLQ 

       550        560        570        580        590        600 
LGMTVNAQID GTCRRRAQAN HTATHLLQAA LRSLVDSSIS QAGSLVSFDR LRFDFNCPRG 

       610        620        630        640        650        660 
LKPEEVEQVE AQVNSWIAEA HSATVAEMPL EVAKAKGAVA MFGEKYADVV RVVDYPGVSM 

       670        680        690        700        710        720 
ELCGGTHVNN TAEIGVFKII SEAGISSGVR RIEAVAGLAV LDYLKVRDAV VKELSDRFKA 

       730        740        750        760        770        780 
KPEELSERVS NLQQELKDSQ KQLEALKGEL AVAKSDQLLG NAETVGEFQI LVAEMPGVDA 

       790        800        810        820        830        840 
EALKTAAERL QQKLDESAVV LGSAAEGKVS LVAAFSKSVN GKGLQAGKFI GGIAKICGGG 

       850        860        870 
GGGRPNLAQA GGRDPSKLKE ALESAKEQLV DGLK 

« Hide

References

[1]"Complete sequence of Trichodesmium erythraeum IMS101."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IMS101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000393 Genomic DNA. Translation: ABG53756.1.
RefSeqYP_724229.1. NC_008312.1.

3D structure databases

ProteinModelPortalQ10VG8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ10VG8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4246460.
GenomeReviewsGene locus Tery_4806 in contig CP000393_GR.
KEGGter:Tery_4806.
NMPDRfig|203124.1.peg.1917.
PATRIC23995387. VBITriEry99848_6095.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBQ10VG8.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycTERY203124:TERY_4806-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_TRIEI
AccessionPrimary (citable) accession number: Q10VG8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: August 22, 2006
Last modified: January 25, 2012
This is version 44 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