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P47534 (SYA_MYCGE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:MG292
OrganismMycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195) [Complete proteome] [HAMAP]
Taxonomic identifier243273 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length900 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-Rule MF_00036

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP-Rule MF_00036

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00036

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00036.

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-Rule MF_00036

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
tRNA-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

alanine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 900900Alanine--tRNA ligase HAMAP-Rule MF_00036
PRO_0000075149

Sites

Metal binding5681Zinc Potential
Metal binding5721Zinc Potential
Metal binding6721Zinc Potential
Metal binding6761Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
P47534 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: AA54520BFB3949A2

FASTA900104,302
        10         20         30         40         50         60 
MNWTTDKVRQ TWLDYFAKKD HLVLASKSLI PINDPSLLWI NSGVATLKDY FSARKTPPSK 

        70         80         90        100        110        120 
RLVNAQICLR VNDIENVGFT SRHQTLFEML GNFSIGDYFK TEAIDFAFDL LVNYYQLDPK 

       130        140        150        160        170        180 
RFYITVYEDD ETTYKRWIKH KIDKNHIIKC DKSRNFWDLG LGPCGPCTEI YYDRGEKFDP 

       190        200        210        220        230        240 
KKIGEKLFFE DIENDRYVEI WNIVFSQFNN DGNGNYTELA QKNIDTGAGI ERLVSVLQNS 

       250        260        270        280        290        300 
PTNFDTDIFL KLIKIIEAFC PFKYDPNSYF TFDPQKVKEQ SYFRIIADHF KAITFTISEG 

       310        320        330        340        350        360 
VLPGPNERNY VVRRLLRRAL IACKKLQLNL AFIEKIIDEI IASYENYYQH LKAKNETVKQ 

       370        380        390        400        410        420 
VVLKEINAFN KTIDLGLVLF EKSVKNNTLT PQLTFQLNET YGFPVEIIRE LVNQKGLTID 

       430        440        450        460        470        480 
WTVFDQLMAK HRSISKQNNQ TINFEKQNIN LVNFKTKSTF FYHKNKINAK VIGLFDENYL 

       490        500        510        520        530        540 
PVKELNNQSG YVVFDQTVLY ATSGGQRYDE GSCINHSNNN DQKISFQGVF KGPNKQHFHY 

       550        560        570        580        590        600 
FLVGSFKLND QVTLSHDETW RKLAANNHSL EHLLHAALQK EIDPLIKQSG AFKSAQKATI 

       610        620        630        640        650        660 
DFNLNRHLTR NELEKVENKI RSLIKQKISS KEIFTDFEGS QKLNAIAYFE EEYSQHEILR 

       670        680        690        700        710        720 
VIRFGDYSVE LCGGTHVANT ASIEDCFITD FYSLGAGRWR IEIISSNETI NNYLKAENQK 

       730        740        750        760        770        780 
LIQLKSELEK VLSLIDSSIF KVELKELQQR LDKFILPEKI TQLRDASDTL LALKNDINQL 

       790        800        810        820        830        840 
KTKNYKVSQQ ALALSIKKQL LSLVDENKSY VIATFNDVEP KLLLQTLHDV FNQNQTKNFL 

       850        860        870        880        890        900 
IINQFNESNS FIVIGNKTTT IIEKLRNSFN LKGGGNDKLF RGSFQDNVTP QKLNELFQNK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L43967 Genomic DNA. Translation: AAC71513.1.
PIRC64232.
RefSeqNP_072959.1. NC_000908.2.

3D structure databases

ProteinModelPortalP47534.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243273.MG_292.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC71513; AAC71513; MG_292.
GeneID875339.
KEGGmge:MG_292.
PATRIC20010114. VBIMycGen98045_0343.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
KOK01872.
OMAWASKGSP.
OrthoDBEOG6Q2SQ2.

Enzyme and pathway databases

BioCycMGEN243273:GH2R-328-MONOMER.

Family and domain databases

HAMAPMF_00036_B. Ala_tRNA_synth_B.
InterProIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamPF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsTIGR00344. alaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_MYCGE
AccessionPrimary (citable) accession number: P47534
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Mycoplasma genitalium

Mycoplasma genitalium (strain G-37): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries