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Q3ITT7 (SYA_NATPD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:NP0710A
OrganismNatronomonas pharaonis (strain DSM 2160 / ATCC 35678) [Complete proteome] [HAMAP]
Taxonomic identifier348780 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeNatronomonas

Protein attributes

Sequence length932 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 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 – 932932Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000075269

Sites

Metal binding6231Zinc By similarity
Metal binding6271Zinc By similarity
Metal binding7261Zinc By similarity
Metal binding7301Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3ITT7 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 73D472E450675543

FASTA932103,353
        10         20         30         40         50         60 
MSDLDEEYQL DYFHEEGFER KECPSCGAHF WTRDSERDIC GEPPCADYDF IGDPGFDTEY 

        70         80         90        100        110        120 
SLEEMREAFL SFFEDHDHER IEPYPVAANR WRDDVLLTQA SIYDFQPLVT SGETPPPANP 

       130        140        150        160        170        180 
LTISQPCIRM QDIDNVGKTG RHTMAFEMMA HHAFNAREDI DDPDQYAYEG EVYWKSETVA 

       190        200        210        220        230        240 
YCDQLLDELG ADIEDVTYIE DPWVGGGNAG PAIEVIYRGL ELATLVFMCM EQDPDGDYEL 

       250        260        270        280        290        300 
KDGNRYSYMD TYVVDTGYGL ERWTWMSQGT PTVYEAVYPE MISFLKDNAG LDYSDREESL 

       310        320        330        340        350        360 
VNRAARLSGK LDIDDVDDVE AARDDIADEL GVETDELRAL VEPLEDIYAI ADHCRTLAYM 

       370        380        390        400        410        420 
LGDGIVPSNV GTGYLARMVL RRTKRLADGV GVDAPLDELV DMQAERLDYE NRDTVRDIVR 

       430        440        450        460        470        480 
TEVEKYRETL ERGRRHVERL AEEYAQKGDP IPLDEVIELY DSRGIQPETV EEIAADHGAD 

       490        500        510        520        530        540 
VEIPDDFYSL VAERHGEADA DADDGTLAGD DDRIADLPET EKLYYEEPER TDFEAVVLDV 

       550        560        570        580        590        600 
IERDADGETV YDVALDQTMF YPEGGGQPAD TGTLSTDDVA AEVTDVQETN GVVLHRTDEA 

       610        620        630        640        650        660 
PGKGEFVRGQ IDGVRRRRLM QHHTATHIVG HAARQVLGDH VRQAGAQKGV ESARFDIRHY 

       670        680        690        700        710        720 
ERISREEVKR IERVANNIVT DNLPVKQEWP KRNEAEADYG FDIYQGGIPP GETLRLIQVG 

       730        740        750        760        770        780 
EDVQACAGTH VLQTGDIGTI KILSTERVQD GVERLVFAAG DAAIEATQRT EDALYDTAEV 

       790        800        810        820        830        840 
LDVSPQEVPA TAERFFEEWK DRGKRIEELK EQLAEARAHG GDGGEEVDLG GTTAVVQRVD 

       850        860        870        880        890        900 
GDMDDLRATA NALVEDGTVA VLGSGDDSAT FVVAVPDNVD INAGAVVGEL ADRVGGGGGG 

       910        920        930 
PPDFAQGGGP DVDSLDEALD AAPEILRSML EA 

« Hide

References

[1]"Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis."
Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., Oesterhelt D.
Genome Res. 15:1336-1343(2005) [PubMed: 16169924] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2160 / ATCC 35678.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR936257 Genomic DNA. Translation: CAI48446.1.
RefSeqYP_326015.1. NC_007426.1.

3D structure databases

ProteinModelPortalQ3ITT7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3ITT7.

Proteomic databases

PRIDEQ3ITT7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3702499.
GenomeReviewsGene locus NP0710A in contig CR936257_GR.
KEGGnph:NP0710A.
NMPDRfig|348780.3.peg.409.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBQ3ITT7.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycNPHA348780:NP0710A-MONOMER.

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.
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.
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_NATPD
AccessionPrimary (citable) accession number: Q3ITT7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: November 8, 2005
Last modified: January 25, 2012
This is version 42 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