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A6L1L8 (SYA_BACV8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BVU_1908
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length871 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 By similarity 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 – 871871Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347502

Sites

Metal binding5621Zinc Potential
Metal binding5661Zinc Potential
Metal binding6641Zinc Potential
Metal binding6681Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A6L1L8 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: E4BE5DE0039667B8

FASTA87197,262
        10         20         30         40         50         60 
MTAKEIRDSF KSFFESKGHQ IVPSAPMVIK DDPTLMFTNA GMNQFKDIIL GNHPAKYKRV 

        70         80         90        100        110        120 
ADSQKCLRVS GKHNDLEEVG HDTYHHTMFE MLGNWSFGDY FKKEAIGWAW EYLVDVLKID 

       130        140        150        160        170        180 
PKDLYATVFE GSPEEGLERD NEAASYWEQF LPKDHILNGN KHDNFWEMGD TGPCGPCSEI 

       190        200        210        220        230        240 
HIDSRSEEEK AQIPGNQLVN KDHPQVIEIW NLVFMQFNRK ADGSLEGLPA KVIDTGMGFE 

       250        260        270        280        290        300 
RLVRTLQGKT SNYDTDVFQP ILKAIAEMAG TTYGQDNQKD IAMRVIADHI RTIAFSITDG 

       310        320        330        340        350        360 
QLPSNAKAGY VIRRILRRAV RYGYTFLGQK QAFMYKLLPV LIENMGEAYP ELNAQKTLIE 

       370        380        390        400        410        420 
KVIKEEEESF LRTLETGIRL LDKTMNDAKA AGKKEISGVD AFTLYDTFGF PLDLTELILR 

       430        440        450        460        470        480 
ENGMTVNEEE FNAEMQKQKE RARNAAAVET GDWITIKEGD THFVGYDFTE YETSILRYRQ 

       490        500        510        520        530        540 
IKQKNQTLYQ IVLSDTPFYA ESGGQVGDTG VIVSEFETIE IIDTKKENNL PIHITKKLPE 

       550        560        570        580        590        600 
HLDVPMMACV DTEKRAACAA NHSCTHLLDE ALRQVLGTHV EQKGSLVTPE SLRFDFSHFQ 

       610        620        630        640        650        660 
KVTDEQLREV EHLVNAKIRE NIPLTEYRNL PIEKAKELGA IALFGEKYGD EVRVVQFGNS 

       670        680        690        700        710        720 
IEFCGGTHVP ATGKIGMVRI ISESSVAAGV RRIEAITGAK VEELMDTVQD TLNDLKALFN 

       730        740        750        760        770        780 
NAPDLKVAIR KYIDENAGLK KQVEEFMKEK GAALKARLVE NAKEINGVKV VKAIIPMSAD 

       790        800        810        820        830        840 
VVKDIAFQLK GEIPANLFVV IGSVDNNKPM LTVMISEDLV KAGQNAGKLV REAAKLIQGG 

       850        860        870 
GGGQPHFATA GGKNPDGLNA AVDKVIELAA L

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000139 Genomic DNA. Translation: ABR39582.1.
RefSeqYP_001299204.1. NC_009614.1.

3D structure databases

ProteinModelPortalA6L1L8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6L1L8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5302874.
GenomeReviewsGene locus BVU_1908 in contig CP000139_GR.
KEGGbvu:BVU_1908.
NMPDRfig|435590.6.peg.1794.
PATRIC21068716. VBIBacVul85104_1976.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAMFTNSGM.
ProtClustDBPRK00252.

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_BACV8
AccessionPrimary (citable) accession number: A6L1L8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: July 24, 2007
Last modified: January 25, 2012
This is version 38 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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