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Q67MV8 (SYA_SYMTH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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:STH2000
OrganismSymbiobacterium thermophilum [Complete proteome] [HAMAP]
Taxonomic identifier2734 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiales Family XVIII. Incertae Sedis › Symbiobacterium

Protein attributes

Sequence length872 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_B

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_B

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_B

Subcellular location

Cytoplasm HAMAP MF_00036_B.

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_B

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 – 872872Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075225

Sites

Metal binding5711Zinc Potential
Metal binding5751Zinc Potential
Metal binding6741Zinc Potential
Metal binding6781Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q67MV8 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 993BDEAB6D9E3B49

FASTA87296,315
        10         20         30         40         50         60 
MTSAEIRQKF IDFFKSKGHV HVPSSSLVPH NDPTLLFTNA GMNQFKDTFL GLEKREYTRA 

        70         80         90        100        110        120 
VTAQKCVRAG GKHNDLDEVG FTARHHTFFE MLGNFSFGDY FKEDALAYAW EFITSPEWLG 

       130        140        150        160        170        180 
LPKDRLWVSI YKDDEQAFDV WHNKVGVPAD RIVRLGEKDN FWRMGDTGPC GPCSEIFWDM 

       190        200        210        220        230        240 
GPEYACDHPD GCRIDTCGCD RWREFWNNVF MQYNQTPEGL VPLERTGVDT GLGLERMATI 

       250        260        270        280        290        300 
MQGVWSNWDI DLWQPIFARI HELSGKKYEG EGPEAVAFRV IADHARCCTF LIADGVRFSN 

       310        320        330        340        350        360 
EGRGYVMRRI LRRAVRFGRV LGFAEPFIWK VAGAVADVMG DAYPEVRERL PVIQDELRRE 

       370        380        390        400        410        420 
EERFLRTLEQ GMNRLEEILA RMRQKGETVI SGQDAFVLYD TYGFPLDIVR DVAREQGFTV 

       430        440        450        460        470        480 
DEQGYQAAMA EQRARARAAR DVSYITEVQS RIAGHLEGVA PTRFVGYTEL AGEGRVLAVF 

       490        500        510        520        530        540 
DQEGNATGAG EGSSVIIVLD RTPFYAEGGG QVGDTGQIVA PGLRVEVEDC RKLPSGHHLH 

       550        560        570        580        590        600 
YGTVQEGFLE VGQQVEARVD ARKRKDTQKN HTATHLLHKA LREVLGTHVQ QAGSLVAPDR 

       610        620        630        640        650        660 
LRFDFTHTGP MTPEQIAAVE EMINAEIEAA EPVTWTEMPL DEARALGAMA LFGEKYGEIV 

       670        680        690        700        710        720 
RVVSVGDGWS RELCGGCHVS NTSEVQYFKI LSESGIGGGV RRIEAVTGPG VIRHLEEAQA 

       730        740        750        760        770        780 
RAVEAQEQLR SRMKEMEKEL EQLRAKLAAS QTDSLVERAQ EVGGVKVVAG TAPVATMEDL 

       790        800        810        820        830        840 
RNMTDAIRAK LGSGVVVLGA VTSEGKVNLV AAVTKDLAGR VHAGNLIREV ARICGGGGGG 

       850        860        870 
RPDMATAGGK NPERLGEALN AVPGLVGSQL GL

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References

[1]"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
Nucleic Acids Res. 32:4937-4944(2004) [PubMed: 15383646] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T / IAM 14863.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP006840 Genomic DNA. Translation: BAD40985.1.
RefSeqYP_075829.1. NC_006177.1.

3D structure databases

ProteinModelPortalQ67MV8.
SMRQ67MV8. Positions 1-470.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2980417.
GenomeReviewsGene locus STH2000 in contig AP006840_GR.
KEGGsth:STH2000.
NMPDRfig|292459.1.peg.1929.
PATRIC23782177. VBISymThe116959_2005.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAGESKTDQ.

Enzyme and pathway databases

BioCycSTHE292459:STH2000-MONOMER.

Family and domain databases

HAMAPMF_00036_B. Ala_tRNA_synth_B.
[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.
IPR023033. Ala_tRNA_synth_euk/bac.
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.
TIGRFAMsTIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_SYMTH
AccessionPrimary (citable) accession number: Q67MV8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 49 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

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