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O28029 (SYA_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:AF_2255
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length906 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. 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. Ref.3

Subunit structure

Homodimer. Ref.3

Subcellular location

Cytoplasm 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 906906Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000075260

Sites

Metal binding6001Zinc
Metal binding6041Zinc
Metal binding7031Zinc
Metal binding7071Zinc

Experimental info

Mutagenesis7031C → A: Loss of tRNA editing activity. Ref.2

Secondary structure

1 ................................................................................................... 906
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O28029 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 2AD39B7B65C72C8B

FASTA906102,536
        10         20         30         40         50         60 
MTLDEEYLDI TFLTENGFVR KRCPKCGKHF WTADPEREIC GDPPCESYSF IGNPVFKKPF 

        70         80         90        100        110        120 
ELDEMREYYL NFFERRGHGR IERYPVVARW RTDIYLTIAS IADFQPFVTS GVAPPPANPL 

       130        140        150        160        170        180 
TISQPCIRLD DLDSVGRTGR HLTLFEMMAH HAFNYPGKEI YWKNETVAYC TELLNELGVK 

       190        200        210        220        230        240 
KEDIVYKEEP WAGGGNAGPC LEAIVGGLEV ATLVFMNLEE HPEGDIEIKG ARYRKMDNYI 

       250        260        270        280        290        300 
VDTGYGLERF VWASKGTPTV YDAIFPEVVD TIIDNSNVSF NREDERVRRI VAESSKLAGI 

       310        320        330        340        350        360 
MGELRGERLN QLRKSVADTV GVSVEELEGI VVPLEKVYSL ADHTRCILFM LGDGLVPSNA 

       370        380        390        400        410        420 
GAGYLARLMI RRSLRLAEEL ELGLDLYDLV EMHKKILGFE FDVPLSTVQE ILELEKERYR 

       430        440        450        460        470        480 
TTVSKGTRLV ERLVERKKKL EKDDLIELYD SHGIPVELAV GIAAEKGAEV EMPKDIYAEL 

       490        500        510        520        530        540 
AKRHSKAEKV QEKKITLQNE YPATEKLYYD DPTLLEFEAE VIGVEGDFVI LNRSAFYPES 

       550        560        570        580        590        600 
GGQDNDVGYL IANGGKFEVV DVLEADGVVL HVVKGAKPEV GTKVKGVIDS DVRWRHMRHH 

       610        620        630        640        650        660 
SATHVLLYSL QKVLGNHVWQ AGARKEFSKA RLDVTHFRRP SEEEIKEIEM LANREILANK 

       670        680        690        700        710        720 
PIKWEWMDRI EAERKFGFRL YQGGVPPGRK IRVVQVGDDV QACGGTHCRS TGEIGMLKIL 

       730        740        750        760        770        780 
KVESIQDGVI RFEFAAGEAA IEAVEEMERL LREASSILRV EPAKLPKTVE RFFEEWKDQR 

       790        800        810        820        830        840 
KEIERLKSVI ADLWADILME RAEEFDSMKV VAEVVDADMQ ALQKLAERLA EKGAVGCLMA 

       850        860        870        880        890        900 
KGEGKVFVVT FSGQKYDARE LLREIGRVAK GSGGGRKDVA QGAVQQLLDR EEMLDVIFRF 


LSEHEG

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. expand/collapse author list , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Nature 390:364-370(1997) [PubMed: 9389475] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]"Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii."
Fukunaga R., Yokoyama S.
Acta Crystallogr. D 63:390-400(2007) [PubMed: 17327676] [Abstract]
Cited for: MUTAGENESIS OF CYS-703.
[3]"Unique protein architecture of alanyl-tRNA synthetase for aminoacylation, editing, and dimerization."
Naganuma M., Sekine S., Fukunaga R., Yokoyama S.
Proc. Natl. Acad. Sci. U.S.A. 106:8489-8494(2009) [PubMed: 19423669] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-739 WITH AN ALANYL-ADENYLATE ANALOG, X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 737-906, ZINC-BINDING, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000782 Genomic DNA. Translation: AAB89002.1.
PIRG69531.
RefSeqNP_071080.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZTGX-ray2.20A1-739[»]
2ZVFX-ray3.20A/B/C/D/E/F/G/H737-906[»]
ProteinModelPortalO28029.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48856N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1485486.
GenomeReviewsGene locus AF_2255 in contig AE000782_GR.
KEGGafu:AF2255.
NMPDRfig|224325.1.peg.2241.
TIGRAF_2255.

Phylogenomic databases

HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBO28029.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycAFUL224325:AF_2255-MONOMER.

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.
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.
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_ARCFU
AccessionPrimary (citable) accession number: O28029
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 81 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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