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Q2J821 (SYA_FRASC) 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:Francci3_3214
OrganismFrankia sp. (strain CcI3) [Complete proteome] [HAMAP]
Taxonomic identifier106370 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Frankiaceae › Frankia

Protein attributes

Sequence length881 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 – 881881Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347618

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q2J821 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 65E5BD77BCFA0B64

FASTA88194,617
        10         20         30         40         50         60 
MDTAEIRSRF LNHFARRGHT VVPSASLVAQ DPTLLLVNAG MVPFKPYFLG DLPAPWPRAA 

        70         80         90        100        110        120 
SVQKCVRTVD IENVGHTARH ASFFQMCGNF SFGDYFKAEA IPFAFELLTE GFGFKADDLW 

       130        140        150        160        170        180 
ATVYLDDDEA EGIWRKLLPA ERIQRRGKED NFWSMGVPGP CGPCSEIYFD RGCAYGREGG 

       190        200        210        220        230        240 
PIADEERYLE VWNLVFMQYE RGEGAGYDYP IERELPARNI DTGMGLERMA TILQGVDNLY 

       250        260        270        280        290        300 
EIDISRPVLD AAGRLTGRRY GADPADDVRL RVIADHTRTA AMLISDGVVP SNEGRGYVLR 

       310        320        330        340        350        360 
RMLRRAIRNA RLLGAHEPVM SELFAVVGSA MGTIYPELLD NAETITGVAV AEEQAFAETL 

       370        380        390        400        410        420 
RTGTTIFDTA ARQARSLGST TLGGEAAFKL HDTYGFPIDL TLEMAAEAGL SVDEAGFRRL 

       430        440        450        460        470        480 
MDRQRQAAKA DRAARRIGNV DLSAFRPILA RSGPTTFTGY EELSRTSGVV GLVGIADGAG 

       490        500        510        520        530        540 
LAAAGEDTEV GVVLDATPFY AESGGQEPDL GRLRFDGGEV EVLDVQRPVP DLVLHRVRVL 

       550        560        570        580        590        600 
GGELRLGVEV FAEVDADRRR AVSRSHTATH LVHTAFRRAL GEGATQAGSL NSPGRLRFDF 

       610        620        630        640        650        660 
HALGAVPPSV LADVEDEINE VALRDLPVRA FVTTQEEARR LGAMALFGEK YGDAVRVVDV 

       670        680        690        700        710        720 
GDYARELCGG THVASSAQLG AVKLLSEASI SAGTRRVEGL VGLDAFRYLA REHLLVSQLS 

       730        740        750        760        770        780 
TALKARPDEL VDRVTDIVGR LRDAERELER LRAAAVLAGA GALAEGAEEV AGVAVVTAEV 

       790        800        810        820        830        840 
PAGTAPDDVR LLALDVRGRL AGRPAVVAVA KADGSSIVVV TDDAARGRGL RAGDLVRQSW 

       850        860        870        880 
ASLGGKGGGK PDVAQGGGGN PQLVPAVFAR LRGLVAEHAS R

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000249 Genomic DNA. Translation: ABD12571.1.
RefSeqYP_482300.1. NC_007777.1.

3D structure databases

ProteinModelPortalQ2J821.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2J821.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3906180.
GenomeReviewsGene locus Francci3_3214 in contig CP000249_GR.
KEGGfra:Francci3_3214.
PATRIC21929750. VBIFraSp10456_3487.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBQ2J821.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycFSP106370:FRANCCI3_3214-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_FRASC
AccessionPrimary (citable) accession number: Q2J821
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: March 7, 2006
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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