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A0B6X3 (SYA_METTP) 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
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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:Mthe_0657
OrganismMethanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP]
Taxonomic identifier349307 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosaetaceaeMethanosaeta

Protein attributes

Sequence length913 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 – 913913Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000347887

Sites

Metal binding6001Zinc By similarity
Metal binding6041Zinc By similarity
Metal binding7031Zinc By similarity
Metal binding7071Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A0B6X3 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 04FB68F30E7F63D1

FASTA913101,963
        10         20         30         40         50         60 
MFPEDEYQLE FFRTEGFVRK VCESCGGSFW TRDASRRTCG DPPCDPYSFI GSPVFREMEL 

        70         80         90        100        110        120 
DSMREHYLSF FEAHGHTRVQ RYPVVARWRD DIYLTIASIA DFQPFVTSGQ VPPPANPLTI 

       130        140        150        160        170        180 
SQPCIRLDDL DSVGRSGRHL TTFEMMAHHV FNTKEHEIYW KDRTVELCDE LLLGLGVDPE 

       190        200        210        220        230        240 
SITYKESPWA GGGNAGPSLE VLVGGLELAT LVFMNLRLDS SGEYVIKGER YSRMDNYIVD 

       250        260        270        280        290        300 
TGYGLERFVW ASKGSPTIYD AVFPDIVREL SDLAGVEHDL HDPEYAEIFA RNARLAGMID 

       310        320        330        340        350        360 
LGEASLRDLR KRIAESINTT PERLERIMAP MERIYAIADH TRCLAYMLGD GIIPSNVKAG 

       370        380        390        400        410        420 
YLARLVIRRT LRMMKDLKLE IPLSEIVEMQ ISKLDYDDWR ERMETISEIL SLEEERYAET 

       430        440        450        460        470        480 
LEKGSRMVSK IASHYSKKGG RIPLTELVSL YDTHGIPPEI ARETAGALGV DVELPDNFYS 

       490        500        510        520        530        540 
IVASTHSRAE QREVETRSPP FEKTERLFYY RPFDQEFDAT VLGIFEGSVV LDRTLFYPEG 

       550        560        570        580        590        600 
GGQPADRGVL VRDGQVFNVN DVQMIDGVVL HRVEQEGLSP GDRVTGRIDM RRRMAHARHH 

       610        620        630        640        650        660 
TATHIVNDSA KRVLGRHVWQ AGAQKSEDRA RLDISHYRRI SDEELKAIEL EANRRVMEMI 

       670        680        690        700        710        720 
PVITEFMPRE EAERLFGFQL YQGGVPPGRE IRVVRVGSDI EACAGTHVTN TGMIGPIKIL 

       730        740        750        760        770        780 
RTERVQDGVE RIEFAAGEAA VQRIQERDDI LAEAASILRV PIEQLPRTVF RFFEEWKDQQ 

       790        800        810        820        830        840 
KVIEHLKEEI AGIRILTLSS EAVDVNGVSI VARDMGESDG ETLLKAATML SERDITAILG 

       850        860        870        880        890        900 
GASGGAAKIV VSVGRSGLER GLNAADIVRA AAKYIGGGGG GKPDLAQGGG PNVGGLRAAI 

       910 
DAGMSAARKA LQV 

« Hide

References

[1]"Complete sequence of Methanosaeta thermophila PT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Smith K.S., Ingram-Smith C., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6194 / PT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000477 Genomic DNA. Translation: ABK14447.1.
RefSeqYP_843087.1. NC_008553.1.

3D structure databases

ProteinModelPortalA0B6X3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0B6X3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4463151.
GenomeReviewsGene locus Mthe_0657 in contig CP000477_GR.
KEGGmtp:Mthe_0657.
NMPDRfig|349307.7.peg.680.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBA0B6X3.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycMTHE349307:MTHE_0657-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_METTP
AccessionPrimary (citable) accession number: A0B6X3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: November 28, 2006
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