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Q7U3R9 (SYA_SYNPX) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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:SYNW2360
OrganismSynechococcus sp. (strain WH8102) [Complete proteome] [HAMAP]
Taxonomic identifier84588 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Synechococcus

Protein attributes

Sequence length889 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 – 889889Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075228

Sites

Metal binding5691Zinc Potential
Metal binding5731Zinc Potential
Metal binding6711Zinc Potential
Metal binding6751Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q7U3R9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 1A2B98881C873953

FASTA88994,946
        10         20         30         40         50         60 
MAAAASSSSA ASAPRSGEDI REAFLNFYAE RGHQRMASAS LIPEDPTVLL TIAGMLPFKP 

        70         80         90        100        110        120 
VFLGQQQRPA PRATSSQKCI RTNDIENVGR TARHHTFFEM LGNFSFGDYF KQQAIEWAWE 

       130        140        150        160        170        180 
LSTQVYGIDP RNLVVSVFRE DDEAEQIWRD VVGVNTKRII RMDEADNFWA SGPTGPCGPC 

       190        200        210        220        230        240 
SEIYYDFKPE LGDDGIDLED DDRFIEFYNL VFMQYNRDAE GNLTPLANRN IDTGMGLERM 

       250        260        270        280        290        300 
AQILQKVPNN YETDLIFPLI QAAADLACVD YAQLDDKGKT SLKVIGDHSR AVTQLICDGV 

       310        320        330        340        350        360 
TASNLGRGYI LRRLLRRVVR HGRLLGIDKP FLVTMGEAAI DLLKGAHPGV IERQEVILAE 

       370        380        390        400        410        420 
LQREEARFLE TLERGEKLLA EVLASRPTQI SGAQAFELYD TYGFPLELTQ EIAEEQRITV 

       430        440        450        460        470        480 
DLDGFEVAME EQRQRAKAAA VSIDLTLQDA IEQVAGDQPA TAFKGYDALD HPSTVQALVV 

       490        500        510        520        530        540 
NGAPASTASA GDVVQVVLDS TPFYGEGGGQ VGDRGSLSGV DVIVAIDSVS RSRDVFVHSG 

       550        560        570        580        590        600 
RMERGHLAVG DTVNAQVDRS CRRRAQANHT ATHLLQAALK QVVDPGIGQA GSLVDFDRLR 

       610        620        630        640        650        660 
FDFHCPTAVT AEQLAQIETL INGWIAEAHC LEVQEMAIDQ AKAAGAVAMF GEKYADVVRV 

       670        680        690        700        710        720 
VDVPGVSMEL CGGTHVANTA EIGLFKIVAE SGVAAGIRRI EAVAGPAVLA YLNERDAVVK 

       730        740        750        760        770        780 
QLGDRFKAQP AEIVDRVTAL QEELKATGKA LAAAQAELAV AKAGALAAKA EAVGEFQLLV 

       790        800        810        820        830        840 
ERLDGVEGAG LQGAAQSLAD QLGDGAAVVI GGLPDPGDLG KVILVAAFGK QVIAAKLQAG 

       850        860        870        880 
KFIGGIAKQC GGGGGGRPNL AQAGGRDGAA LPGALAAARS ELAAALPQS

« Hide

References

[1]"The genome of a motile marine Synechococcus."
Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.
Nature 424:1037-1042(2003) [PubMed: 12917641] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WH8102.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX569695 Genomic DNA. Translation: CAE08875.1.
RefSeqNP_898449.1. NC_005070.1.

3D structure databases

ProteinModelPortalQ7U3R9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7U3R9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1730756.
GenomeReviewsGene locus SYNW2360 in contig BX548020_GR.
KEGGsyw:SYNW2360.
PATRIC23836482. VBISynSp27240_2511.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBQ7U3R9.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycSSP84588:SYNW2360OR2518-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_SYNPX
AccessionPrimary (citable) accession number: Q7U3R9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 51 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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