Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q6A8I8 (SYA_PROAC) 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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:PPA1178
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium

Protein attributes

Sequence length892 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 – 892892Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075175

Sites

Metal binding5781Zinc Potential
Metal binding5821Zinc Potential
Metal binding6811Zinc Potential
Metal binding6851Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q6A8I8 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 96A45C65B58F63D0

FASTA89295,845
        10         20         30         40         50         60 
MRTAEIGQRF VDFFESKGHT VVPSASLLYN DPTLLFVNAG MVPFKPYLMG TEPSPWKRAT 

        70         80         90        100        110        120 
SIQKCVRTLD IDEVGKTTRH GTFFQMLGNF SFGDYFKNEA IQYAWELVTK PAEQGGLGFD 

       130        140        150        160        170        180 
PASIWVTVLG PGFHPDYPEG DIEAREAWRA AGIPDEQIQG RSLKDNYWHM GVPGPGGPCS 

       190        200        210        220        230        240 
EIYIDRGPAY GPDGGPEADE DRYLEIWNLV FETEDLSAVR AKDDFDIAGP LRSLNIDTGA 

       250        260        270        280        290        300 
GLERIAYLLQ GVDNMYETDQ VFPVIEKASE MSGKRYGARH DDDVRLRVVA DHVRSGLMLM 

       310        320        330        340        350        360 
TDGVTPGNEA RGYVLRRLLR RVVRAMRLLG VADPVLPELL SVSRDLMADS FPDVLTQWDR 

       370        380        390        400        410        420 
VIGAATAEED TFRRTLSSGT AMLDAAVVET KASGSKTLSG EKAFQLHDTY GFPIDLTLEM 

       430        440        450        460        470        480 
AAEQGLEVDR NKFTALMAEQ RARAKADSQA KKGLLTDREA YSQVRALGET PFLGYTDLTV 

       490        500        510        520        530        540 
DTTVTGIIAN GTSVTAAEPG AVVEIVLAET PFYAEMGGQD SDSGIIRANG IDFEVLDVQR 

       550        560        570        580        590        600 
PVPGLIVHKV HLDGDLAVGD RVTALVNPAT RFGACQAHTA THVIHAALRE LVGPSATQAG 

       610        620        630        640        650        660 
SYNKPGYLRF DFSATKGLSD SLKDEIEERC NVAIHDDFEV TDTQMPLEDA KAMGAMAMFG 

       670        680        690        700        710        720 
EKYPPIVRVV ELAGPWSREL CGGTHVASTG RIGMLSLLGE QSVGSGTRRV EALVSTDAFR 

       730        740        750        760        770        780 
HMAAERALVN ELTGILKVQP DQLADRVSKL AADLKEAERK LGAARTRELL GQVDDIVAGT 

       790        800        810        820        830        840 
TPAGSFDLVA AKVPGVAGSD LRTLAAEIRA RVKDRPAVVT LIGGTHDKPA MIVATTESAR 

       850        860        870        880        890 
AAGAKAGALI KVGVAPIGGR GGGKDDMAQG AGSDPTGIDA ALRAVNTELT AL

« Hide

References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed: 15286373] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017283 Genomic DNA. Translation: AAT82927.1.
RefSeqYP_055885.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6A8I8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2932411.
GenomeReviewsGene locus PPA1178 in contig AE017283_GR.
KEGGpac:PPA1178.
NMPDRfig|267747.1.peg.1162.
PATRIC23037091. VBIProAcn64440_1214.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBQ6A8I8.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycPACN267747:PPA1178-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_PROAC
AccessionPrimary (citable) accession number: Q6A8I8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: September 13, 2004
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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents