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Q3AGN4 (SYA_SYNSC) 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:Syncc9605_2518
OrganismSynechococcus sp. (strain CC9605) [Complete proteome] [HAMAP]
Taxonomic identifier110662 [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 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 – 889889Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347838

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q3AGN4 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 4B7602BF429832B9

FASTA88995,105
        10         20         30         40         50         60 
MVAVASSSSA ASAPRSGEEI REAFLNFYAE RGHKRMASAS LIPDDPTVLL TIAGMLPFKP 

        70         80         90        100        110        120 
VFLGQQERPA PRATSSQKCI RTNDIENVGR TARHHTFFEM LGNFSFGDYF KQRAIEWAWE 

       130        140        150        160        170        180 
LSTGVYGIDP KNLVVSVFRE DDEAELIWRD VVGVNPKRII RMDEADNFWA SGPTGPCGPC 

       190        200        210        220        230        240 
SEIYYDFKPE LGDEDIDLED DDRFIEFYNL VFMQYNRDAE GTLTPLANRN IDTGMGLERM 

       250        260        270        280        290        300 
AQILQKVPNN YETDLIFPLI QAAADLAGVD YHQLNDKGKT SLKVIGDHSR AVTQLICDGV 

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

       370        380        390        400        410        420 
LQREEARFLE TLERGEKLLA EVLASKPTQI SGAQAFELYD TYGFPLELTQ EIAEEQGLAV 

       430        440        450        460        470        480 
DLDGFEAAME EQRQRAKAAA VSIDLTLQDA IDQVVADQAA TCFEGYEALD HASCVQALVV 

       490        500        510        520        530        540 
NGGPSTTAKA GDAVQVVLDT TPFYGEGGGQ VGDRGVLAGS DLIVRIESVS RSRDVFVHAG 

       550        560        570        580        590        600 
RVERGELALG DTVKAQVDRA CRRRAQANHT ATHLLQAALK QVVDPGIGQA GSLVDFDRLR 

       610        620        630        640        650        660 
FDFHCPTAVT PDQLQQVETL INGWINEAHA LQVQEMAIDQ AKAAGAVAMF GEKYADVVRV 

       670        680        690        700        710        720 
VDVPGVSMEL CGGTHVTNTA EIGLFKIVAE SGVAAGIRRI EAVAGPAVLA YLNERDVVVK 

       730        740        750        760        770        780 
QLGDRFKAQP AEIVDRVAAL QEELKATGKA LAAAQAELAV AKAGALAAKA EAVGDFQLLV 

       790        800        810        820        830        840 
ERLDGVDGAG LQGAAQSLAD QLGDGAAVVI GGLPDPGDMG KVILVAAFGQ QVIAAKLQAG 

       850        860        870        880 
KFIGGIAKQC GGGGGGRPNL AQAGGRDGAA LPGALDAAQA ELTSAFRAL

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9605."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9605.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000110 Genomic DNA. Translation: ABB36248.1.
RefSeqYP_382803.1. NC_007516.1.

3D structure databases

ProteinModelPortalQ3AGN4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3AGN4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3737933.
GenomeReviewsGene locus Syncc9605_2518 in contig CP000110_GR.
KEGGsyd:Syncc9605_2518.
NMPDRfig|110662.3.peg.1145.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBQ3AGN4.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycSSP1131:SYNCC9605_2518-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_SYNSC
AccessionPrimary (citable) accession number: Q3AGN4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: November 22, 2005
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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