Skip Header

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

Q0VNK2 (SYA_ALCBS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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
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:ABO_1798
OrganismAlcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]
Taxonomic identifier393595 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length863 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 CAL17246.1 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 – 863863Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347483

Sites

Metal binding5521Zinc Potential
Metal binding5561Zinc Potential
Metal binding6561Zinc Potential
Metal binding6601Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q0VNK2 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: E7D0C86144E21574

FASTA86393,888
        10         20         30         40         50         60 
MKSAELRQAF LDYFASQGHT KVSSSSLVPA NDPTLLFTNA GMNQFKDVFL GRESRDYTRA 

        70         80         90        100        110        120 
TSSQRCVRAG GKHNDLENVG YTARHHTFFE MLGNFSFGDY FKREAIKFAW EFLTGTLGLP 

       130        140        150        160        170        180 
EERLWVTVHV SDDEAADIWL KEMGVSAERF SRLDEDNFWQ MGDTGPCGPS SEIFYDHGAD 

       190        200        210        220        230        240 
VPGGPPGSAD EDLDRYIEIW NLVFMQYDRQ PDGELQPLPK PSVDTGMGLE RIAAVLQGVH 

       250        260        270        280        290        300 
SNYEIDLFQA LLQAAAKATG CTDLEEKSLR VIADHIRSAS FLICDGVIPS NEGRGYVLRR 

       310        320        330        340        350        360 
IIRRALRHGH KLGQDKPFFS TLVAALVAEM GEAYPELGRE QARIEKALLA EEEQFGRTLA 

       370        380        390        400        410        420 
AGMKVLESAI EQLDGRVLPG DVLFNLYDTH GFPPDLTADV ARERDLSVDM DGFEAAMAAQ 

       430        440        450        460        470        480 
RERARGAGSF ANDYSDRLNI DAITDFSGYE KLADDNTVVA LYKDGAAVDT LNAGEEGMVV 

       490        500        510        520        530        540 
LDRTPFYAES GGQVGDTGAL IADEARFMVT DTRKRQAAHV HVGKQVSGSL TIGGKVSACV 

       550        560        570        580        590        600 
DVDRRLAVMR NHSATHLMHA ALRNVLGEHV QQKGSLVSAD YLRFDFSHGE AVSEAQREEI 

       610        620        630        640        650        660 
EILVNRQILA NTAVTTELMD IESAREAGAM ALFGEKYDDQ VRVLSMGSDG FSKELCGGTH 

       670        680        690        700        710        720 
VNRTGDIGLF RITLEASAAA GVRRIEAVTG EHALAVMRRQ ERALSEIAAT VKSSLDNAAD 

       730        740        750        760        770        780 
RVRSQAQKVR ELEKEIERLK QKLASGAGGD LTSEVQDING VKVLATQIDG ADGKTLRVTM 

       790        800        810        820        830        840 
DKLKDKLGSA VIVLAAVEGE KVALVAGVTK DLTTKYKAGD LLKFVAEQVD GRGGGRPDMA 

       850        860 
QGGGNNPAAL PGALESVKAW VAE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM286690 Genomic DNA. Translation: CAL17246.1. Different initiation.
RefSeqYP_693518.1. NC_008260.1.

3D structure databases

ProteinModelPortalQ0VNK2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0VNK2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4211293.
GenomeReviewsGene locus ABO_1798 in contig AM286690_GR.
KEGGabo:ABO_1798.
NMPDRfig|393595.12.peg.1802.
PATRIC20841419. VBIAlcBor124741_1886.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.

Enzyme and pathway databases

BioCycABOR393595:ABO_1798-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_ALCBS
AccessionPrimary (citable) accession number: Q0VNK2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: January 25, 2012
This is version 43 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents