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Q5UZE6 (SYA_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:rrnAC2561
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length927 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 – 927927Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000075261

Sites

Metal binding6181Zinc By similarity
Metal binding6221Zinc By similarity
Metal binding7211Zinc By similarity
Metal binding7251Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5UZE6 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 5E45BC5834309669

FASTA927102,893
        10         20         30         40         50         60 
MSDLDEAYQL DYFEEEGFHR QECVSCGDMF WSRVKRETCG EPPCAEYDFI DNPGFDESHS 

        70         80         90        100        110        120 
LTEMREAFLS FFEDRDHERI DPYPVAANRW RDDVLLTQAS IYDFQPLVTS GTTPPPANPL 

       130        140        150        160        170        180 
CISQPCIRMQ DIDNVGKTGR HTMAFEMMAH HAFNAREDIE DPEQYAYEGE VYWKNETVQY 

       190        200        210        220        230        240 
CDELFEEMGA NLDEIVYIED PWVGGGNAGP AIEVIYRGAE LATLVFMSME QDSDGEYEMK 

       250        260        270        280        290        300 
DGNRYSPMDT YIVDTGYGLE RWTWMSQGTP TVYEAVYPDM IAFLKDNAGI ELTDEEERIV 

       310        320        330        340        350        360 
HEAAKLAGRM DIDEAEDIEA ERDTIAAEVG VEVEEMRDLM APLEDIYAIA DHCRTLAYML 

       370        380        390        400        410        420 
GDGIVPSNVG TGYLARMVLR RTKRLVDGVG VDAPLDELVD MQAERLDYEN RDTIRDIVRT 

       430        440        450        460        470        480 
EVEKYRETLD RGGRRVRQLA DEYAEKGEPI PTSELVELYD SHGIQPDMVE EIAAEKGVAV 

       490        500        510        520        530        540 
DVPDDFYAVV AQRHGGDDTA TEESQTPYED RLEELPETDR LYYEDQQRTE FEAVVLEVFD 

       550        560        570        580        590        600 
RDEDTYDVVL DQTMFYPEGG GQPPDKGTLS TDDVSAEVTD VQQYGDVIVH TCDDDPGKGE 

       610        620        630        640        650        660 
FVRGQVDATR RQRLMQHHTA THIVIHSARQ VLGEHVRQAG AQKGTDSARI DIRHYESVSR 

       670        680        690        700        710        720 
EKVKEIERLA NDIIQDNITV SQEWPDRNDA EERYGFDLYQ GGIPAGEQIR LITVGDDVQA 

       730        740        750        760        770        780 
CGGTHVARTG DIGAVKLLNT ERIQDGVIRL TFAAGNAAIE ATQRTEDALT EAADILDVAP 

       790        800        810        820        830        840 
DAVPETAERF FDEWKARGKE IEQLKEQLAE ARASGGGDNE EVGVGDATAV VGRIDADMDE 

       850        860        870        880        890        900 
LRAQANAIVE QGNIAVLGSG LDGAQFVVSV PDGVDVDAGE VVGELAGRVG GGGGGPPDFA 

       910        920 
QGGGPDADAL DDALDDAPEI LRTVANA 

« Hide

References

[1]"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea."
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.
Genome Res. 14:2221-2234(2004) [PubMed: 15520287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY596297 Genomic DNA. Translation: AAV47357.1.
RefSeqYP_137063.1. NC_006396.1.

3D structure databases

ProteinModelPortalQ5UZE6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3128743.
GenomeReviewsGene locus rrnAC2561 in contig AY596297_GR.
KEGGhma:rrnAC2561.
NMPDRfig|272569.1.peg.2344.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBQ5UZE6.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycHMAR272569:RRNAC2561-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_HALMA
AccessionPrimary (citable) accession number: Q5UZE6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: December 7, 2004
Last modified: January 25, 2012
This is version 47 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