Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q5PBJ0 (SYA_ANAMM)

Last modified November 3, 2009. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alanyl-tRNA synthetase
    EC=6.1.1.7
Alternative name(s):
    Alanine--tRNA ligase
      Short name=AlaRS
Gene names
Name: alaS
Ordered Locus Names: AM224
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length882 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Subcellular location

Cytoplasm. HAMAP MF_00036

Domain

The C-terminal 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.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
RNA-binding
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

alanine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 882882Alanyl-tRNA synthetase HAMAP MF_00036
PRO_0000075046

Sequences

Sequence LengthMass (Da)Tools
Q5PBJ0-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 62FCE6D20CB03F1F

FASTA88295,968
        10         20         30         40         50         60 
MSSGSLSSIR KKFLEFFVKN GHKLYASAPL VATGDASLLF TSAGMVPFKQ AFTSGSSVDG 

        70         80         90        100        110        120 
AKTAVSSQKC LRAGGKHNDL ENVGYTNRHH TFFEMLGNFS FGDYFKERAI ELAWRFVTEE 

       130        140        150        160        170        180 
MCLSKDRLWI TVYSEDQEAF DIWKKITGFP DDRIIKISTS DNFWSMGDTG PCGPCSEIFY 

       190        200        210        220        230        240 
DYGEHVQGGP PGSKDADGPR FTEVWNLVFM QFCRDEHGEL NPLPHKCIDT GMGLERAAAV 

       250        260        270        280        290        300 
VQGVCDNYDT DLFKAVIRKS QDVFGSPDNS IAHRVIADHI RAAAFLISEG LSPGNEGRNY 

       310        320        330        340        350        360 
VLRRIIRRAV RYAYQLDPSN VAIHEVLPVL TKEGSAGYMG DAYPELVRCE QSITSTLRSE 

       370        380        390        400        410        420 
GEGFVDTLRR GMALLEKEIG GLSPGQVLLG DVAFKLYDTF GFPLDITLDI AKERGLKFDQ 

       430        440        450        460        470        480 
EGFNKGMGEQ KARSRKHWVG SGEDASHRLW EELQAQHKNT RFVGYDCCST KASVLSITRD 

       490        500        510        520        530        540 
GMAVQSVNSG EKACLLLDVS PFYAESGGQE GDKGSITGVS GVKNSGGANI AEVTYTRKAS 

       550        560        570        580        590        600 
NLHIHECTIT SGVFNVGDTV DAAIDVDRRE RLKANHSATH ILHSVLRTHI DGNIQQKGSL 

       610        620        630        640        650        660 
VAEDKLRFDF NYASALTKEQ IALIEREVNR RIMSNKPVLT DHCSFEAAVQ GGAIALFGEK 

       670        680        690        700        710        720 
YSEHSVRVVS MGDSKELCGG THVRYTGDIG AFKIVSESGI ALGVRRIEAI TGQSVVDGLR 

       730        740        750        760        770        780 
KDGDILLHIS ERLGVPVGEV SEGLERLLKE KLELKKKLVC AWHEIIKSSI SPVNCGAGVV 

       790        800        810        820        830        840 
LHCGYFPTIP VDAIMEFMKS ARKAERGIFA IATAVDGKAV LIIGVGDTAS KVLGASELVK 

       850        860        870        880 
TLADLQGKGG GNAGLARVSL EVGNVQEALS TILNKVTAAF PT 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000030 Genomic DNA. Translation: AAV86339.1.
RefSeqYP_153594.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5PBJ0.

Genome annotation databases

GeneID3171157.
GenomeReviewsGene locus AM224 in contig CP000030_GR.
KEGGama:AM224.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5PBJ0.
OMATLMFTNS.

Enzyme and pathway databases

BioCycAMAR234826:AM224-MON.

Family and domain databases

HAMAPMF_00036.
[Tree]
InterProIPR002318. Ala-tRNA-synth_IIc.
IPR018165. Ala-tRNA-synth_IIc_cons-reg.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR003156. Pesterase_DHHA1.
IPR012947. tRNA_SAD.
[Graphical view]
PfamPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
TIGRFAMsTIGR00344. alaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_ANAMM
AccessionPrimary (citable) accession number: Q5PBJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 4, 2005
Last modified: November 3, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents