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A6TQZ4 (SYA_ALKMQ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:Amet_2458
OrganismAlkaliphilus metalliredigens (strain QYMF) [Complete proteome] [HAMAP]
Taxonomic identifier293826 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length880 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.

Sequence caution

The sequence ABR48612.1 differs from that shown. Reason: Erroneous initiation.

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 – 880880Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347485

Sites

Metal binding5661Zinc Potential
Metal binding5701Zinc Potential
Metal binding6681Zinc Potential
Metal binding6721Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A6TQZ4 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 6C28E39B758456C9

FASTA88098,968
        10         20         30         40         50         60 
MKKMGLNEIR KLFLDFYEEK EHYVQSSYPL VPHNDKSLLL INAGMAPLKN YFSGVETPPS 

        70         80         90        100        110        120 
KRMATCQKCI RTGDIENVGK TSRHATFFEM LGSFAFGDYF KTESIQWGWE FATKYLEMPE 

       130        140        150        160        170        180 
DKIWASVYEE DDEAYGIWEN QIKMPKERIV RLGKEDNFWE IGVGPCGPCS ELYFDRGDKY 

       190        200        210        220        230        240 
SCGHDDCKPG CDCDRFVEFW NHVFTQFDKD EAGNYNLLPN PNIDTGMGLE RVACIMQDVD 

       250        260        270        280        290        300 
SIFEVDTMKH ILNSVCTATN TQYNKDVKTN ISLRIITDHL RSITFMIGDG ILPSNEGRGY 

       310        320        330        340        350        360 
VLRRLLRRAA RHGKLLGVSK SFLYELMDTV TETYGGAYSE LVEKKDYIKK IIQVEEDRFQ 

       370        380        390        400        410        420 
ETIHQGLEIL NQHIEEMIGK SENMLNGTYA FKLYDTYGFP LDLTKEILEE REMTVDESEF 

       430        440        450        460        470        480 
ESEMEKQRNR ARKARSGGDT EGWKEDAFDA LDKNIQTSFK GYETLRAEGK VLAIIEENQS 

       490        500        510        520        530        540 
VNLTSAGKEV VIVLDKTPFY PESGGQIGDI GHIFKDEFEG QVLDTKQGKN QRIHQYIKIL 

       550        560        570        580        590        600 
RGILQVGDSI QGEVDKEPRH NTERNHTATH LLHKALKGII GEHVEQAGSL VTPEKLRFDF 

       610        620        630        640        650        660 
SHFEGLSSAD LSKVELEVNQ EILNALNVDT VEASLEEAKK MGAMALFGEK YGDDVRVVKT 

       670        680        690        700        710        720 
GDYSVELCGG THVKNSSEIG TFLILSETGV AAGVRRIEAV TGQEAYHHIK REQGLIQDIE 

       730        740        750        760        770        780 
SLLKTKGEQL TKRVEELLKE TKEKDKELQQ LKSKLANQSI DEILNQIEVI EGTNLLVHHF 

       790        800        810        820        830        840 
GEQSMEDLRN IGDSLKQKIG SGVIALGAES NDKASFFVTA TKDVVEKGVH SGNMIREVAK 

       850        860        870        880 
IAGGGGGGRP DMAQAGGKNP EKIQSALSIV KGLLKNQLNG 

« Hide

References

[1]"Complete sequence of Alkaliphilus metalliredigens QYMF."
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., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J., Fields M., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: QYMF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000724 Genomic DNA. Translation: ABR48612.1. Different initiation.
RefSeqYP_001320271.1. NC_009633.1.

3D structure databases

ProteinModelPortalA6TQZ4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6TQZ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5312530.
GenomeReviewsGene locus Amet_2458 in contig CP000724_GR.
KEGGamt:Amet_2458.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycAMET293826:AMET_2458-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_ALKMQ
AccessionPrimary (citable) accession number: A6TQZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: January 25, 2012
This is version 31 of the entry and version 2 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