Skip Header

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

B0CFX4 (SYA_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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

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:AM1_4444
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesAcaryochloris

Protein attributes

Sequence length873 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 – 873873Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347466

Sites

Metal binding5591Zinc Potential
Metal binding5631Zinc Potential
Metal binding6611Zinc Potential
Metal binding6651Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
B0CFX4 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 7AAF9E6767E519C2

FASTA87395,642
        10         20         30         40         50         60 
MVASLSGAQI RQTFLDFYAA KGHKILPSAS LVPEDPTVLL TIAGMLPFKP IFLGQREAEV 

        70         80         90        100        110        120 
PRATTSQKCI RTNDIENVGQ TARHHTYFEM LGNFSFGDYF KEQAIAWAWE LSTEVYKLPP 

       130        140        150        160        170        180 
ERIVPSVFEE DDEAFAIWRD KIGIPEHRIQ RMGAEDNFWA SGPTGPCGPC SELYYDFYPE 

       190        200        210        220        230        240 
KGDDKIDLED DTRFIEYYNL VFMEYNRDSD GKLAPLKNKN IDTGLGLERM AQILQGVPNN 

       250        260        270        280        290        300 
YETDLIFPII ETAAKIAGIK YKKSKAKTKT SLKVVGDHVR SVVQMIADGI TASNVGRGYV 

       310        320        330        340        350        360 
LRRLIRRVVR HGQLIGIDGA FITQVAETAI ASLEVAYPEV REREKIIKTE LEREEAQFLK 

       370        380        390        400        410        420 
TLNRGEKLLG EIMAKKPKQI SGKDAFDLYD TYGFPLELTQ EIAAEQGLTV DEDGFAKAMK 

       430        440        450        460        470        480 
EQQDRGRSAH KTIDLTVQSA LEQLAATVHP TDFLGYTDFS AKAKVAALLV KGETVDQASA 

       490        500        510        520        530        540 
GSEVQIALDQ TPFYAESGGQ IGDRGYLNGK DVVVRIEDVQ KESDIFIHYG RIERGTLEVG 

       550        560        570        580        590        600 
DKLTAQIDLA CRRQVQAHHT ATHLLQAALK NIVDESIGQA GSLVAFDRLR FDFNYNQAVT 

       610        620        630        640        650        660 
PEQIQEIETQ INTWIAEAHT TETEVMPIAE AKAKGAVAMF GEKYGAEVRV MDVPGVSMEL 

       670        680        690        700        710        720 
CGGTHVKNTS EIGLFKIVTE AGVASGVRRI EAIAGPAVLE YLNVRDAVVR DLSDRFKAKP 

       730        740        750        760        770        780 
EELPERITTL QADLKTAQKQ LDTLKAQLAL VKSEQLLDQA EPAGEVKVLV SQLEGVDSES 

       790        800        810        820        830        840 
LKTAAGRLLQ KLGEGAVVLG SVPAEGKVSL VAAFSPKVIE QGLQAGKFVG AIAKQCGGGG 

       850        860        870 
GGRPNLAQAG GRDPSKLADA LDDAQKQLLA QLK 

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000828 Genomic DNA. Translation: ABW29421.1.
RefSeqYP_001518738.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0CFX4.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0CFX4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5683246.
GenomeReviewsGene locus AM1_4444 in contig CP000828_GR.
KEGGamr:AM1_4444.
PATRIC20622972. VBIAcaMar40141_4107.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBB0CFX4.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycAMAR329726:AM1_4444-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_ACAM1
AccessionPrimary (citable) accession number: B0CFX4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 28 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