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C3N7E3 (SYA_SULIY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 20. 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:YG5714_1881
OrganismSulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1) [Complete proteome] [HAMAP]
Taxonomic identifier439386 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length900 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_A

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_A

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_A

Subcellular location

Cytoplasm By similarity HAMAP MF_00036_A.

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_A

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 – 900900Alanine--tRNA ligase HAMAP MF_00036_A
PRO_1000202051

Sites

Metal binding6041Zinc By similarity
Metal binding6081Zinc By similarity
Metal binding7081Zinc By similarity
Metal binding7121Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
C3N7E3 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: AE89FEAD497CB69C

FASTA900103,090
        10         20         30         40         50         60 
MKASEEEYRL NFFIKNDFKR KICKSCKTPF WTRDEKKEYC SDIPCTDYYF FDINIKSQPL 

        70         80         90        100        110        120 
TVKEAREKFL SFFEKRGHTR ISPKPVLARW REDLYLTIAS IVDFQPHVTS GLVPPPANPL 

       130        140        150        160        170        180 
VVSQPSIRLE DIDNVGITFG RHLTTFEMAA HHAFNYPDHY VYWKEETTAY ATEFFTKELG 

       190        200        210        220        230        240 
IPEEELNFKE SWWEGGGNAG PCLEVTVGGL ELATLVFMQY KITDNGNYTP LKLKIVDTGY 

       250        260        270        280        290        300 
GVERIAWITQ KTPSAFHAIY GNLVYKFFNK IGVAYIDETL LKVASRFAGK IDPDNPDTIK 

       310        320        330        340        350        360 
IHRQMVSKEL GIDIKAVEEE LDRAAKVFQI LDHTKTIMLM LADGLVPSNS GEGYLGRLVI 

       370        380        390        400        410        420 
RRALKVLRLL KSDVRLYELV KEQIDFWKED FPQVLKNKDY ILDAVELEQQ RFEKILEKVP 

       430        440        450        460        470        480 
SIASTLARKS EITTEDLIQV YDSNGIPPDL LEEELKKKSV KFELPRNFYA LVAKRHQTST 

       490        500        510        520        530        540 
IKSAYDKVKL PKDMLEYITA LQPTEKLYYK DQYMRSFEGK VLGVYKNYLI LDKTTFYPEG 

       550        560        570        580        590        600 
GGQLGDTGLI IDEKSSKRYE VIDTQKVNDV IVHILKEEPS TIKVGDNVRG EINWERRYRL 

       610        620        630        640        650        660 
MRHHTVTHVI LAAAKKVLGE HVWQAGAEKT PEKGRLDITH HKTLTEEEVK LIENYANSVI 

       670        680        690        700        710        720 
SDRRQVKPLE MNRMEAEMKY GVSIYEGGVP NSATIRLLEI KDWDIESCGG THVSNTSEIG 

       730        740        750        760        770        780 
AVKIINVERI QDGVIRLEYV AGPALVDYIR ETQAKIVEAS KIIGTSPDQL TSRLRRILNE 

       790        800        810        820        830        840 
IEEKNNLIIQ YRRIIETELL NNLKPYEINS NKIYIIEGLG DEEENKEILR KLTSTDNTIA 

       850        860        870        880        890        900 
ISISDNRLQI ATSKNMRVDK IVEELLKGGG KGGGKGTFAN VILNSKKSKE EIIEIVRKSL 

« Hide

References

[1]"Biogeography of the Sulfolobus islandicus pan-genome."
Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.
Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009) [PubMed: 19435847] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Y.G.57.14 / Yellowstone #1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001403 Genomic DNA. Translation: ACP46137.1.
RefSeqYP_002838059.1. NC_012622.1.

3D structure databases

ProteinModelPortalC3N7E3.
ModBaseSearch...

Protein-protein interaction databases

STRINGC3N7E3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7807284.
GenomeReviewsGene locus YG5714_1881 in contig CP001403_GR.
KEGGsiy:YG5714_1881.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAGESKTDQ.
ProtClustDBPRK13902.

Family and domain databases

HAMAPMF_00036_A. Ala_tRNA_synth_A.
[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.
IPR022429. Ala-tRNA_synth_arc.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PfamPF01411. 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.
TIGRFAMsTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_SULIY
AccessionPrimary (citable) accession number: C3N7E3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: January 25, 2012
This is version 20 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