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A0LUJ2 (SYA_ACIC1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. 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:Acel_1330
OrganismAcidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]
Taxonomic identifier351607 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeAcidothermaceaeAcidothermus

Protein attributes

Sequence length886 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 – 886886Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347470

Sites

Metal binding5701Zinc Potential
Metal binding5741Zinc Potential
Metal binding6721Zinc Potential
Metal binding6761Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A0LUJ2 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: F130E189AD09A27C

FASTA88695,438
        10         20         30         40         50         60 
MESAEIARRW LAFFEKRDHV VVPSTPLVAD DPELLFVVAG MQPFKPYFRG DAPAPWPRAT 

        70         80         90        100        110        120 
SVQKVLRTPD IDEVGKTTRH ATFFHMCGNF SFGDYFKETA IPLAWELLTT PVADGGYGFA 

       130        140        150        160        170        180 
PDRLWVTVYT DDDEAADIWH RVVGLPVDRI QRRGMADNFW SMGVPGPCGP CSEIYYDRGP 

       190        200        210        220        230        240 
EFGVGGGPVA NEERYLEVWN LVFMQYERGP GGAKDNYPIL GELPAKNIDT GMGLERMAAI 

       250        260        270        280        290        300 
LQGVDNIYEI DTTRPILDKA AELTGQRYGS GGQNDVRLRM VADHIRAITM LVNDGVVPSN 

       310        320        330        340        350        360 
EERGYVLRRL MRRVVRAMRL LGAREPTMHE LVATAIAVFT PQYPELSRNA ERIFAVADGE 

       370        380        390        400        410        420 
EASFFSTLAA GTARFEAAVR EAGGGVLSGE QAFVLHDTYG FPIDLTLEMA AEQGVTVDEE 

       430        440        450        460        470        480 
GFRALMAEQR RRAKEDAERR KTGAADRAAY RAAAELLGRP VEFTGYTERS GEAVVRGLLV 

       490        500        510        520        530        540 
DGAAVPAAHA GQRVEVVLDR TPFYAEGGGQ LPDHGVLEFA AGRIDVDDVQ QPLPGLIVHR 

       550        560        570        580        590        600 
GRVADGEITV GETVLARIDV DRRWAISRSH TATHMVHKAF REFLGDTAAQ AGSENAPGRF 

       610        620        630        640        650        660 
RFDFTNPSAV PPSVLGEVEE RVNDLLLHDL EVTAQIMRQQ EAIASGAIAM FGEKYGDQVR 

       670        680        690        700        710        720 
VISIGDWSRE LCGGTHVPHT GHLGVIKIVS ESSIGAGVRR IEALVGLDAY RYLAREAVLV 

       730        740        750        760        770        780 
SQLAEQLKAP ADELPDRIAG MLARLRDAEK ELEKLRQARL LAEAPRLAAA RVDVGGLAVV 

       790        800        810        820        830        840 
AARVDGDGVD ADGLRLLATD LRQRLGGSAV VVLAGVAGGR PVVVAAVGSE ALARGVKAGE 

       850        860        870        880 
LVGVAAKRLG GGGGGRPDFA QGGGTNPAAV DDAVSAALDA VRAQVG 

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References

[1]"Complete sequence of Acidothermus cellulolyticus 11B."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43068 / 11B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000481 Genomic DNA. Translation: ABK53102.1.
RefSeqYP_873088.1. NC_008578.1.

3D structure databases

ProteinModelPortalA0LUJ2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0LUJ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4486383.
GenomeReviewsGene locus Acel_1330 in contig CP000481_GR.
KEGGace:Acel_1330.
PATRIC20673160. VBIAciCel132453_1412.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAMFTNSGM.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycACEL351607:ACEL_1330-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_ACIC1
AccessionPrimary (citable) accession number: A0LUJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: December 12, 2006
Last modified: January 25, 2012
This is version 41 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