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Q2GJ36 (SYA_ANAPZ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:APH_1059
OrganismAnaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP]
Taxonomic identifier212042 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group

Protein attributes

Sequence length876 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 – 876876Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347490

Sites

Metal binding5681Zinc Potential
Metal binding5721Zinc Potential
Metal binding6701Zinc Potential
Metal binding6741Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q2GJ36 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 93320B0A64AC0E1E

FASTA87696,764
        10         20         30         40         50         60 
MSSSSVSGIR EAFLDFFEKQ GHTRYPSAPL IAEGDASLLF TNAGMVPFKQ RFITGVSDVK 

        70         80         90        100        110        120 
TATTSQKCLR AGGKHNDLEN VGYTNRHHTF FEMLGNFSFG DYFKETAIEL AWRFVTKELG 

       130        140        150        160        170        180 
LSKERLWITV YSEDQEAFDI WKKITGYTDH KIIRISTSDN FWSMGDTGPC GPCSEIFYDY 

       190        200        210        220        230        240 
GDGVPGGLPG TDESDGARYT EIWNLVFMQY NRDESGELHK LPRGCIDTGM GLERIAAVMQ 

       250        260        270        280        290        300 
GVCDNYETDM FQAIIDRSRS IFGSHDHPIA HRVIADHVRA ASFLIAEGLT PGNEGRNYVL 

       310        320        330        340        350        360 
RRIIRRAVRY IYQIVGDKFS LHEVVPVLTR EGSAGYMGNA YPEIVKAEQS IVSTLKIEED 

       370        380        390        400        410        420 
GFADTLRRGT GILEQEIRGL KSGEVLSGEI AFKLYDTYGF PLDITLDVAK ERGLKFDEDG 

       430        440        450        460        470        480 
FNRCMAKQKE QSRKHWKGSG EAQTASSHIL NKHKATSFVG YENHRVKSMV KEIFCSGEAV 

       490        500        510        520        530        540 
TSMGEGEEGI AVLDITPFYA ESGGQEGDTG LLKVVTTKCG SVAEVVDTTK SNNVHLHKIR 

       550        560        570        580        590        600 
VIRGTLKVGD VVEAVVDKQR REKLRANHSA THILQSVLRT LIGEGIQQKG SLVAADKLRF 

       610        620        630        640        650        660 
DFSHALPLTK EQLRTVEMEV NRQIMANQPV IIDHCSLEDA VQEGAIALFG EKYNDQNVRV 

       670        680        690        700        710        720 
VSMGSSKELC GGTHVRFTGD IGAFRIISET GIAQGVRRIE AITGHEVVSS MNRDSESLQQ 

       730        740        750        760        770        780 
VAECLSVPVD QVIEKLKKVF VEQREINKKM ATICYTHMNS CAKCIEVGSE IKLYVGEFSN 

       790        800        810        820        830        840 
IPVEVVASYV KEKMHTNEVL AISTTDGKRT TFIVGVGESA IKRIKATDIV KALQQIQGKG 

       850        860        870 
GGNASIARAS LPSEYSAKAA EIIRQTVIDA IQNSGA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000235 Genomic DNA. Translation: ABD44304.1.
RefSeqYP_505615.1. NC_007797.1.

3D structure databases

ProteinModelPortalQ2GJ36.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2GJ36.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3930808.
GenomeReviewsGene locus APH_1059 in contig CP000235_GR.
KEGGaph:APH_1059.
NMPDRfig|212042.5.peg.1003.
PATRIC20950868. VBIAnaPha602_1133.
TIGRAPH_1059.

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBQ2GJ36.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycAPHA212042:APH_1059-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_ANAPZ
AccessionPrimary (citable) accession number: Q2GJ36
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: March 21, 2006
Last modified: January 25, 2012
This is version 47 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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