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A3MXP1 (SYA_PYRCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:Pcal_1993
OrganismPyrobaculum calidifontis (strain JCM 11548 / VA1) [Complete proteome] [HAMAP]
Taxonomic identifier410359 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length896 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_A

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_A

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_A

Subcellular location

Cytoplasm By similarity HAMAP MF_00036_A.

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_A

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 – 896896Alanine--tRNA ligase HAMAP MF_00036_A
PRO_1000074514

Sites

Metal binding5991Zinc By similarity
Metal binding6031Zinc By similarity
Metal binding7071Zinc By similarity
Metal binding7111Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A3MXP1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: D44383DF1B4BA50E

FASTA896100,700
        10         20         30         40         50         60 
MQKTQMLSAE IFRRRGHIRK QCPLCKSHFW TLRPDQEVCG DQPCTPYGFI GNPPTKVAVE 

        70         80         90        100        110        120 
SLRDVRERFL SFFERHGHAR IKRYPVVARW RDDVYLVGAS IYDFQPWVTS GAVPPPANPL 

       130        140        150        160        170        180 
TISQPSIRLT DVDKVGRSGR HLTGFEMMAH HAFNYPDKYV YWIDETTEYA YRFFTEELGI 

       190        200        210        220        230        240 
PPEEITFKES MWEGGGNAGE CFEVLVRGLE AATLVFMHYE VKDGKYVELP LKIVDTGYGL 

       250        260        270        280        290        300 
ERIYWLIKGT PTIYDAVFGP YLAKVRERLG VPEPPRDVMA KASIYFGQMD PEVISLDKAY 

       310        320        330        340        350        360 
DIIAEKIGVD GKWLREVVKP QEALYVLADH SRTVAWMIAD GVIPSNSGAG YLARLLIRRA 

       370        380        390        400        410        420 
LRGLMLAGVD APLVELFDLH LKELRYDYPE VWEARSLILE LVDMEEKKYR EVLKSAPAVV 

       430        440        450        460        470        480 
KRALEENRRR GKAGLDKEDL VTLYDSYGLP PEVVAEAAKS MGIEVKVPDD FYSLLASRHV 

       490        500        510        520        530        540 
RREKGREATL VEMAKVADLP RTRELFYEDA YMRTFKAKVL RVIDGKYVVL DQTAFYAEGG 

       550        560        570        580        590        600 
GQPADTGVLR HSGGVAKVVD VQRVGHVIVH VVEGDVPQEG SEVVGEVDWE RRYALMKMHT 

       610        620        630        640        650        660 
GTHVLIQSIR RVLGPHIWQA GAQKDIPFSR IDVTHYKLPT PEEVAKIERL ANDVVQRDLP 

       670        680        690        700        710        720 
VYVKVMPRNE AEAKYGFILY QGGVVPAREI RVVQIGPDDE PYDVQACGGT HLRRTGEIGL 

       730        740        750        760        770        780 
IKVHKVERIA DGVVRFIFTT GPHAVAYVQE LERQAAEAAA LGGGSKEELV EVVKRLLKRA 

       790        800        810        820        830        840 
EEAEKKARHY AELYAAALAE NLKAEAVGQR RLAVVELDDE ELAKRVALLA TKRDPDLVLV 

       850        860        870        880        890 
VKAGERVTIY TGGVDVGPIV KALREIGFRG GGSKTFAQGV YAGDVEKLKE AIRRAL 

« Hide

References

[1]"Complete sequence of Pyrobaculum calidifontis JCM 11548."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 11548 / VA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000561 Genomic DNA. Translation: ABO09408.1.
RefSeqYP_001056874.1. NC_009073.1.

3D structure databases

ProteinModelPortalA3MXP1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3MXP1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4908986.
GenomeReviewsGene locus Pcal_1993 in contig CP000561_GR.
KEGGpcl:Pcal_1993.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBA3MXP1.
ProtClustDBPRK13902.

Family and domain databases

HAMAPMF_00036_A. Ala_tRNA_synth_A.
[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.
IPR022429. Ala-tRNA_synth_arc.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF01411. 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.
TIGRFAMsTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_PYRCJ
AccessionPrimary (citable) accession number: A3MXP1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 3, 2007
Last modified: January 25, 2012
This is version 33 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