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Q2IG40 (SYA_ANADE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:Adeh_3784
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length905 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 – 905905Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347488

Sites

Metal binding5951Zinc Potential
Metal binding5991Zinc Potential
Metal binding6961Zinc Potential
Metal binding7001Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q2IG40 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 08BB48C42CE1E0CC

FASTA90598,444
        10         20         30         40         50         60 
MKTPTAAEIR ELFQRYFEEH GHRRVASSSL VPQNDPTLLF TNAGMVQFKD VFTGRERRDY 

        70         80         90        100        110        120 
SRATTAQKCV RAGGKHNDLE NVGFTARHHT FFEMMGNFSF GDYFKADAIA WAWELVTSPA 

       130        140        150        160        170        180 
WLGIAKDRLA ATVFAGEGTL PWDEEAFELW KAQGVPVERI HKLGAKDNFW AMGDTGPCGP 

       190        200        210        220        230        240 
CSELHYFQGN DVPCAEEQAG RKCQGVACDC DRWLEIWNLV FMQFERGQDG GLTPLPKPSI 

       250        260        270        280        290        300 
DTGAGLERLA AVAQGKRSNY DTDLFRSIIH AVEGLSDKRY DAASDDGVSM RVIADHARAT 

       310        320        330        340        350        360 
TFLVGDGVLP SNEGRGYVLR RIMRRAIRHG KRLGLERPFL AAVCGAVIDE MGAAYPETRE 

       370        380        390        400        410        420 
NRAFIEKVAQ QEEESFRRTL DKGLAILEGE MRKLVPDATH DGKPATPAPD RARPIIDGKV 

       430        440        450        460        470        480 
AFQLYDTFGF PLDLTRVIAA ERGFDVDEQG FDRHMAEQRA RSEWKGSGEQ GVDDLHKQIA 

       490        500        510        520        530        540 
GELGEVKFLG YELPAARAQV KAILANGARV ARAGKGDKVE IVTDATPFYG ESGGQVGDVG 

       550        560        570        580        590        600 
HITGAGLEIR VDDAQRPVPG LVTHVGEVLR GEVAVGDAVE LSVDDRRRDL VRANHSATHL 

       610        620        630        640        650        660 
LQLALREVLG EHVKQAGSVV APDYLRFDFS HFQPVTEEEL AAVERRVNEL VRENAETETA 

       670        680        690        700        710        720 
VLKLEEARHA GAMMIFGEKY GDVVRVVRIG PSKELCGGTH VRRSGDIAFF KIGSEESIAS 

       730        740        750        760        770        780 
GVRRLVAYTG ARAVEVQQRE AEELRRAAAL LKAGALEVSQ KIEQTQRRVK DLERALEEAR 

       790        800        810        820        830        840 
SKAAAAQSGD LAALAKDVGG AKVLAARVEG DGKALRELAD KLRDRLGKGV VALGAEQDGK 

       850        860        870        880        890        900 
AILLVAVTRD LTARLKAGDL VKEAAKLVGG SGGGKPDMAQ AGGSDPAGLE KALEKVAELA 


ARALA 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000251 Genomic DNA. Translation: ABC83550.1.
RefSeqYP_466987.1. NC_007760.1.

3D structure databases

ProteinModelPortalQ2IG40.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2IG40.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3888281.
GenomeReviewsGene locus Adeh_3784 in contig CP000251_GR.
KEGGade:Adeh_3784.
PATRIC20923811. VBIAnaDeh31384_3862.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAMFTNSGM.
PhylomeDBQ2IG40.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycADEH290397:ADEH_3784-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_ANADE
AccessionPrimary (citable) accession number: Q2IG40
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 44 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