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A6WCF7 (SYA_KINRD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:Krad_3032
OrganismKineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) [Complete proteome] [HAMAP]
Taxonomic identifier266940 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesKineosporiineaeKineosporiaceaeKineococcus

Protein attributes

Sequence length893 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 – 893893Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347640

Sites

Metal binding5731Zinc Potential
Metal binding5771Zinc Potential
Metal binding6761Zinc Potential
Metal binding6801Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A6WCF7 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: EBF344A32DA0DB91

FASTA89395,953
        10         20         30         40         50         60 
MQTAEIRRRW LDFFERKEHT VVPSASLVSS DPSLMFTVAG MVPFIPYLTA QVPAPYKRAT 

        70         80         90        100        110        120 
SVQKCLRTLD IDEVGKTTRH GTFFQMNGNF SFGDYFKREA VAFAWELLTT PEADGGLGFD 

       130        140        150        160        170        180 
PERLWTTVYL DDDEAFQLWR EVGMPAERIQ RRGKADNYWN TGQPGPGGPC SEIYFDRGPA 

       190        200        210        220        230        240 
YGAEGGPEAD EDRYIEIWNL VFMQYQLSAV RTKVDFDVEG ELPAKNIDTG MGLERVAFLK 

       250        260        270        280        290        300 
QGVDNMYEID EVRPVLDKAA ELSGRRYGAV HEDDVRMRVV ADHVRSALML IGDGVTPGNE 

       310        320        330        340        350        360 
GAGYVLRRLV RRAVRAMRLL GVEEPALPHL LPASMEVMSA SYPQLRSDFE RISAVAYAEE 

       370        380        390        400        410        420 
DAFRRTLVSG TAIFETAVAQ TKAAGGSSLS GERAFALHDT YGFPIDLTLE MAAEAGVGVD 

       430        440        450        460        470        480 
EPGFRALMAE QVGRAKADAK AKKTGGVDLA IYRSTLEQLP APVVFTGYEA AAGEARISVV 

       490        500        510        520        530        540 
LQGGVSTPSA PAGTDVEVVL DRTPFYAEGG GQLADHGTVT TTSGAVLAVS DVQQPVRGLY 

       550        560        570        580        590        600 
VHKGTVTSGE LVAGDAVHAV VDAGRRRSIS RAHTATHLVH QVVREHLGDT ATQAGSQNAP 

       610        620        630        640        650        660 
GRMRFDYRST AQVAGDVVRD IEAVVNERIH DDLEVSAAVM DRESALNSGA MALFGEKYGE 

       670        680        690        700        710        720 
KVRVVSIGED WSKELCGGTH TLTSQQVGLV SIVSESSIGS GARRIEALVG ADAFDFLTRE 

       730        740        750        760        770        780 
HLLVNQLTEV VKARPEELPD RIGALLTRLG DAEKEIARLR GGQVLALAPT IAAKPVDKFG 

       790        800        810        820        830        840 
VRVVTHDAGP VSADDLRTLV LDVRSRLGEE RPSVVAVAGV AKDRPVVVVA TNAEARRWGV 

       850        860        870        880        890 
KAGELVRTAA KTLGGGGGGK DDLAQGGGQD PSKVPAALQG IEDFVGARVT GSV 

« Hide

References

[1]"Complete sequence of chromosome of Kineococcus radiotolerans SRS30216."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J., Fliermans C., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-149 / DSM 14245 / SRS30216.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000750 Genomic DNA. Translation: ABS04496.1.
RefSeqYP_001362760.1. NC_009664.2.

3D structure databases

ProteinModelPortalA6WCF7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6WCF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5336979.
GenomeReviewsGene locus Krad_3032 in contig CP000750_GR.
KEGGkra:Krad_3032.
NMPDRfig|266940.1.peg.3403.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycKRAD266940:KRAD_3032-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_KINRD
AccessionPrimary (citable) accession number: A6WCF7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: August 21, 2007
Last modified: January 25, 2012
This is version 36 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