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Q9PI05 (SYA_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Cj0506
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length842 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-Rule MF_00036

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP-Rule MF_00036

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00036

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00036.

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-Rule MF_00036

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
tRNA-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

alanine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 842842Alanine--tRNA ligase HAMAP-Rule MF_00036
PRO_0000075083

Sites

Metal binding5491Zinc Potential
Metal binding5531Zinc Potential
Metal binding6501Zinc Potential
Metal binding6541Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q9PI05 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F571EA5A2B60A8B7

FASTA84294,906
        10         20         30         40         50         60 
MDIRKAYLDF FASKGHEITP SSPLVPDDAT LLFTNAGMVP FKSIFTGEIP RPNPPRKTSC 

        70         80         90        100        110        120 
QTCIRAGGKH NDLDNVGYTA RHHTFFEMLG NFSFGDYFKE QAIAYAWEFV TEVLKLPKDR 

       130        140        150        160        170        180 
LYVTVHENDD EAFNLWQKHI QKERIYKFGD KDNFWQMGDT GPCGPCSEIF YDQGQEHFNS 

       190        200        210        220        230        240 
SEDYMGGDGD RFLEIWNLVF MQYERSADGV LSPLPKPSID TGMGLERVTA IKEGKFSNFD 

       250        260        270        280        290        300 
SSLFMPIINE ISKLCNKTYV YESGASFRVI ADHIRSSVFL LAQGVSFDKE GRGYVLRRIL 

       310        320        330        340        350        360 
RRALRHGYLL GFKQAFMYKL VDVVCDLMGG HYTYLNEKKD FIKEQIRLEE ERFLSTIENG 

       370        380        390        400        410        420 
IEIFNEELKN TKEIFSGEVA FKLYDTYGFP LDLTADMLRE KNLKVDEEKF ELFMNEQKAR 

       430        440        450        460        470        480 
AKASWKGSGD KTASGDFKNL LEKFGENHFV GYEKAECESK ILALLDEDFK EVSTLKDAGW 

       490        500        510        520        530        540 
VMLENTPFYA TSGGQSADSG FIAKREVLDT QKFFNLNLSF IKAGEELKVN DIVHARIDTE 

       550        560        570        580        590        600 
KREQIARHHS ATHLLHHALR EILGSHVSQA GSLVESNKLR FDFTHHKALN KEELESIEKR 

       610        620        630        640        650        660 
VNKMIINSSE AILENMPLEE AKKSGAIALF NEKYQGNVRV LTLGESKELC GGTHVKNTAQ 

       670        680        690        700        710        720 
IGSFYIVKES GVSAGVRRIE AVVSKAALEF VKNQLEELSK VKDELKNNDI LSGIKKLKNE 

       730        740        750        760        770        780 
ILSLKNELKN SSKTELDSKN IQGVEICVKR IDNGDIKAMI DDFKNKFAKA VILLIQVKDE 

       790        800        810        820        830        840 
KITLAAGVKD VPLKAGALVK EAAQILGGNG GGRDDFATAG GKDLSKINEA LKQSLETIEK 


AL 

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References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL34653.1.
PIRC81396.
RefSeqYP_002343938.1. NC_002163.1.

3D structure databases

ProteinModelPortalQ9PI05.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING192222.Cj0506.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL34653; CAL34653; Cj0506.
GeneID904835.
KEGGcje:Cj0506.
PATRIC20057954. VBICamJej33762_0499.

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHOG000156965.
KOK01872.
OMAYDIDIFQ.
OrthoDBEOG6Q2SQ2.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-491-MONOMER.

Family and domain databases

HAMAPMF_00036_B. Ala_tRNA_synth_B.
InterProIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR003156. Pesterase_DHHA1.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
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. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsTIGR00344. alaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_CAMJE
AccessionPrimary (citable) accession number: Q9PI05
Secondary accession number(s): Q0PB09
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries