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P61699 (SYA_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:DIP1350
OrganismCorynebacterium diphtheriae [Complete proteome] [HAMAP]
Taxonomic identifier1717 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length888 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 – 888888Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075097

Sites

Metal binding5731Zinc Potential
Metal binding5771Zinc Potential
Metal binding6761Zinc Potential
Metal binding6801Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
P61699 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: 4AB1F6B6FCB8FD0D

FASTA88896,354
        10         20         30         40         50         60 
MQTHEIRERF TNHFVKAGHE AVPSASLILD DPNLLFVNAG MVPFKPYFLG QQNPPFPNGT 

        70         80         90        100        110        120 
ATSIQKCVRT LDIEEVGITT RHNTFFQMAG NFSFGQYFKE GAITHAWQLL TGTVAEGGLG 

       130        140        150        160        170        180 
LDPERLWVTV YLDDDEAAEI WNKKIGVPSE RIQRLGMADN YWSMGIPGPC GPCSEIYYDR 

       190        200        210        220        230        240 
GPEYGAEGGP IADDNRYMEI WNLVFMENER GEGIGKDNFE IVGPLPKKNI DTGMGIERVA 

       250        260        270        280        290        300 
CILQGVDNVY ETDLLRPVIN VAEELTGATY GTNDDDNIRF RVIADHSRTG MMLILDGVTP 

       310        320        330        340        350        360 
GNEGRGYILR RLLRRIIRSA HLLGAKGKTL EKFMNTIMDT MTPSYPEIAD NRERILRVAI 

       370        380        390        400        410        420 
TEEKAFLKTL ASGTELFEDK ADQVKNSGNK VLDGAAAFKL HDTYGFPIDL TLEMAAEAGL 

       430        440        450        460        470        480 
NVDIEGFNSL MAEQRARAKA DNRAKKHGHA DLSIYREWVD EHPTVFTGYD ELTTDSKVLG 

       490        500        510        520        530        540 
LLSAGNKVNE IKAGEEVEVI LEASPLYAEA GGQLGDRGQI LMGDTVLKVN DVQKIGKKLW 

       550        560        570        580        590        600 
VHKATVAQGG LSVGDVVTAQ VDSDWRHAAR QAHTGTHLIH AALRQVLGPT AVQAGSMNKP 

       610        620        630        640        650        660 
GYLRFDFNYT ESLTPRQLEE IQNITNQAVD SDWDVNTIET SLEEAKAMGA LALFGENYGS 

       670        680        690        700        710        720 
EVRVIEVGGP FSIELCGGTH VTHSSQIGPV AILGESSVGS GVRRIEAYTG LDSFKYLAKE 

       730        740        750        760        770        780 
QALVENIASS MKVKPEELPD RIAALTQKLK DAEKAIADMR SAQLMAQATG LVAGAIEVNG 

       790        800        810        820        830        840 
VKLVAQRVSD VENMGDLRSL AADIKQRLDD VPAVVALVGE DASGKAPFVV GATKAAVSAG 

       850        860        870        880 
YKANAYAKIL GQYIEGNGGG KPDMAQGSAR NSSGFDQGIA AVKAEMSA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX248357 Genomic DNA. Translation: CAE49878.1.
RefSeqNP_939703.1. NC_002935.2.

3D structure databases

ProteinModelPortalP61699.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2648793.
GenomeReviewsGene locus DIP1350 in contig BX248353_GR.
KEGGcdi:DIP1350.
NMPDRfig|257309.1.peg.1294.
PATRIC21483892. VBICorDip47633_1329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBP61699.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycCDIP257309:DIP1350-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.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF01411. 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_CORDI
AccessionPrimary (citable) accession number: P61699
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: January 25, 2012
This is version 52 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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