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A8FFM9 (SYA_BACP2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:BPUM_2380
OrganismBacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]
Taxonomic identifier315750 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length878 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 – 878878Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347499

Sites

Metal binding5661Zinc Potential
Metal binding5701Zinc Potential
Metal binding6681Zinc Potential
Metal binding6721Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A8FFM9 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 4B26A30C1E8700CC

FASTA87897,040
        10         20         30         40         50         60 
MKTLTSAQVR QMFLDFFKEK GHAVEPSASL VPHDDPTLLW INSGVATLKK YFDGRVVPDN 

        70         80         90        100        110        120 
PRICNAQKSI RTNDIENVGK TARHHTFFEM LGNFSIGDYF KEEAIEWAWE FLTSDEWIGF 

       130        140        150        160        170        180 
DPNLLSVTVH PEDEEAYVLW RDKIGVPEER IIRLEGNFWD IGEGPSGPNT EIFYDRGESY 

       190        200        210        220        230        240 
GHDMNDPELY PGGENERYLE VWNLVFSEFN HNPDGSYTPL PKKNIDTGMG LERMVSVIQN 

       250        260        270        280        290        300 
VPTNFDTDLF MPIIRAVETI SGESYGETKE KDTAFKVIAD HIRTVAFAVS DGALPSNEGR 

       310        320        330        340        350        360 
GYVLRRLLRR AVRYAKTIHI HRPFMFDLVP VVAEIMKDFY PDVQAKEEFI AKVIKNEEER 

       370        380        390        400        410        420 
FHETLNEGLA ILSEVIKKER DKGSSQISGE DVFKLYDTYG FPVELTEEYA EDEHMTVDRE 

       430        440        450        460        470        480 
GFQAEMEKQR ERARNARQDV GSMQVQGGAL GDIKVESTFV GYENLTAVAH MIELLQNGEI 

       490        500        510        520        530        540 
VSEAHEGDTV QILLDETPFY AESGGQVADK GTLKSAEVII DIKDVKKAPN GQHVHEGVVV 

       550        560        570        580        590        600 
SGTAKKGLVV TAEVESALRK GIVKNHTATH LLHQALKDVL GSHVNQAGSL VNENRLRFDF 

       610        620        630        640        650        660 
SHFGQVTKEE LSQIEKIVNE KIWEGISVAI DLKPIAEAKE MGAMALFGEK YGDIVRVVQV 

       670        680        690        700        710        720 
GDYSIELCGG CHVQNTAEIG LFKIASESGI GAGTRRIEAV TGKGAYEELN DQLGILEQAA 

       730        740        750        760        770        780 
SELKSNTKDV PKRIASLQAD LKEVQRENES LLAKLSQAEA GSILEKVTEI GGVKVLTEKV 

       790        800        810        820        830        840 
NAKDMNHLRT MVDDLKAKLG SAVIVLGAVQ NGKVNISAGV TKDVIEKGLH AGKLVKQAAE 

       850        860        870 
ICGGGGGGRP DMAQAGGKQP EKLEEALTSV EESVKSVL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000813 Genomic DNA. Translation: ABV63046.1.
RefSeqYP_001487606.1. NC_009848.1.

3D structure databases

ProteinModelPortalA8FFM9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8FFM9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000064652; EBBACP00000062985; EBBACG00000064643.
GeneID5621649.
GenomeReviewsGene locus BPUM_2380 in contig CP000813_GR.
KEGGbpu:BPUM_2380.
PATRIC18968676. VBIBacPum16546_2433.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
GeneTreeEBGT00050000001776.
HOGENOMHBG354397.
OMAMFTNSGM.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycBPUM315750:BPUM_2380-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_BACP2
AccessionPrimary (citable) accession number: A8FFM9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: November 13, 2007
Last modified: January 25, 2012
This is version 31 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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