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Q5P7Q3 (SYA_AROAE) 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:AZOSEA05360
ORF Names:ebA1021
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum

Protein attributes

Sequence length873 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 – 873873Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075049

Sites

Metal binding5631Zinc Potential
Metal binding5671Zinc Potential
Metal binding6641Zinc Potential
Metal binding6681Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q5P7Q3 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 86A87402C56EFE3D

FASTA87395,217
        10         20         30         40         50         60 
MKSAEIREKF LKFFESKGHQ IVASSSLVPH DDPTLLFTNA GMNQFKDVFL GFDKRPYSRA 

        70         80         90        100        110        120 
TTSQKCVRAG GKHNDLENVG YTARHHTFFE MLGNFSFGDY FKHDAITYAW ELLTEEFGLP 

       130        140        150        160        170        180 
KDKLWVTVYA DDDEAYDIWT KEIGVPAERV IRIGDNKGAR YASDNFWMMG DTGPCGPCTE 

       190        200        210        220        230        240 
IFYDHGPEIW GGPPGSPDED GDRYIEIWNN VFMQFNRDEA GVMHPLPRPS VDTGMGLERV 

       250        260        270        280        290        300 
SAVLQHVHSN YEIDLFQTLI RAAARETGCA DLDSPSLKVI ADHIRACSFL IADGVIPGNE 

       310        320        330        340        350        360 
GRGYVLRRII RRAIRHGYKL GSRAAFFHRL VPDLVTEMGP AYPELKAGQA RVADVLKQEE 

       370        380        390        400        410        420 
ERFFATIENG MAILETELAA MATAGSRTFN GETAFKLHDT YGFPLDLTAD VCRERDVTVD 

       430        440        450        460        470        480 
AAAFDAAMAR QKEQARAAGK FRMAMNLEYE GPETKFHGYE RLEERGTVLA LYKDGAPVVE 

       490        500        510        520        530        540 
LQEGDIGVVV LDNTPFYAES GGQVGDRGEL RGSAGIFEVE DTQKIQAAVY GHHGVVKTGR 

       550        560        570        580        590        600 
LAVGQELGAR VDGEARASTQ RNHSVTHLMH KALREVLGAH VQQKGSQVDP DKTRFDFAHT 

       610        620        630        640        650        660 
APLSPEEIRE VEDLVNAEIL ANVATEARVM SIDDAQKSGA MMLFGEKYGD EVRVLAIGSS 

       670        680        690        700        710        720 
KELCGGTHVA RTGDIGLFKI VSEGGVAAGV RRIEAVTGAN ALRYAQEQER RVQGISALLK 

       730        740        750        760        770        780 
VQPDEVAERI AGILDNVRAL EKELARMKSR LAASQGDELV AQAVEVRGAK VLAAMLEGAD 

       790        800        810        820        830        840 
VATLRETLDK LKDKLKSAVI VLAAVADGRV SLIAGVTSDL TAKLKAGELV NMVAQQVGGK 

       850        860        870 
GGGRPDMAQA GGTDPAHLPA ALASVKAWAE ARL

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR555306 Genomic DNA. Translation: CAI06658.1.
RefSeqYP_157559.1. NC_006513.1.

3D structure databases

ProteinModelPortalQ5P7Q3.
SMRQ5P7Q3. Positions 1-462.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5P7Q3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3181133.
GenomeReviewsGene locus AZOSEA05360 in contig CR555306_GR.
KEGGeba:ebA1021.
NMPDRfig|76114.4.peg.1557.
PATRIC20967143. VBIAroAro98752_0538.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAMFTNSGM.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycASP76114:EBA1021-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_AROAE
AccessionPrimary (citable) accession number: Q5P7Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 4, 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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