Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alanine--tRNA ligase

Gene

alaS

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi559 – 5591ZincUniRule annotation
Metal bindingi563 – 5631ZincUniRule annotation
Metal bindingi661 – 6611ZincUniRule annotation
Metal bindingi665 – 6651ZincUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding, Zinc

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-925-MONOMER.
BRENDAi6.1.1.7. 396.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligaseUniRule annotation (EC:6.1.1.7UniRule annotation)
Alternative name(s):
Alanyl-tRNA synthetaseUniRule annotation
Short name:
AlaRSUniRule annotation
Gene namesi
Name:alaSUniRule annotation
Ordered Locus Names:aq_1293
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 867867Alanine--tRNA ligasePRO_0000075047Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224324.aq_1293.

Structurei

Secondary structure

1
867
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1713Combined sources
Turni18 – 203Combined sources
Beta strandi22 – 243Combined sources
Helixi45 – 473Combined sources
Helixi48 – 514Combined sources
Beta strandi60 – 6910Combined sources
Helixi78 – 803Combined sources
Turni81 – 833Combined sources
Beta strandi84 – 863Combined sources
Beta strandi89 – 10113Combined sources
Helixi104 – 11714Combined sources
Helixi123 – 1253Combined sources
Beta strandi126 – 1316Combined sources
Helixi135 – 1428Combined sources
Turni143 – 1453Combined sources
Helixi149 – 1513Combined sources
Beta strandi152 – 1554Combined sources
Helixi157 – 1604Combined sources
Beta strandi161 – 17919Combined sources
Beta strandi182 – 1843Combined sources
Helixi186 – 1894Combined sources
Beta strandi190 – 20314Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi209 – 22214Combined sources
Helixi223 – 2308Combined sources
Helixi236 – 2383Combined sources
Turni240 – 2423Combined sources
Helixi243 – 25311Combined sources
Beta strandi257 – 2593Combined sources
Helixi261 – 28222Combined sources
Helixi291 – 30919Combined sources
Helixi317 – 32812Combined sources
Turni329 – 3313Combined sources
Helixi334 – 37340Combined sources
Beta strandi377 – 3793Combined sources
Helixi381 – 3899Combined sources
Helixi395 – 4039Combined sources
Turni404 – 4063Combined sources
Helixi411 – 42313Combined sources
Turni424 – 4263Combined sources
Beta strandi443 – 4453Combined sources
Helixi446 – 4494Combined sources
Turni450 – 4523Combined sources
Beta strandi758 – 7625Combined sources
Beta strandi765 – 77410Combined sources
Helixi777 – 78711Combined sources
Beta strandi790 – 80213Combined sources
Beta strandi805 – 8128Combined sources
Helixi814 – 8163Combined sources
Turni817 – 8193Combined sources
Helixi822 – 83211Combined sources
Beta strandi841 – 8499Combined sources
Helixi851 – 8533Combined sources
Helixi854 – 86613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RIQX-ray2.14A1-454[»]
1YFRX-ray2.15A/B1-454[»]
1YFSX-ray2.08A/B1-454[»]
1YFTX-ray2.23A1-454[»]
1YGBX-ray2.48A1-454[»]
3G98X-ray1.85A/B758-867[»]
3HTZX-ray2.50A2-454[»]
ProteinModelPortaliO67323.
SMRiO67323. Positions 2-454.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO67323.

Family & Domainsi

Domaini

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. The Aquifex aeolicus domain can be used in vitro to replace the corresponding domain in E.coli.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the class-II aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CIM. Bacteria.
COG0013. LUCA.
HOGENOMiHOG000156965.
InParanoidiO67323.
KOiK01872.
OMAiFDFNCPR.
OrthoDBiEOG6Q2SQ2.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O67323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSAHEIRE LFLSFFEKKG HTRVKSAPLV PENDPTLLFV NAGMVPFKNV
60 70 80 90 100
FLGLEKRPYK RATSCQKCLR VSGKHNDLEQ VGYTSRHHTF FEMLGNFSFG
110 120 130 140 150
DYFKKEAIEY AWEFVTEVLK LPKEKLYVSV YKDDEEAYRI WNEHIGIPSE
160 170 180 190 200
RIWRLGEEDN FWQMGDVGPC GPSSEIYVDR GEEYEGDERY LEIWNLVFMQ
210 220 230 240 250
YNRDENGVLT PLPHPNIDTG MGLERIASVL QGKNSNFEID IIFPLIQFGE
260 270 280 290 300
EVSGKKYGEK FETDVALRVI ADHLRAITFA ISDGVIPSNE GRGYVIRRIL
310 320 330 340 350
RRAMRFGYKL GIENPFLYKG VDLVVDIMKE PYPELELSRE FVKGIVKGEE
360 370 380 390 400
KRFIKTLKAG MEYIQEVIQK ALEEGRKTLS GKEVFTAYDT YGFPVDLIDE
410 420 430 440 450
IAREKGLGID LEGFQCELEE QRERARKHFK VEAKKVKPVY SHLKELGKTS
460 470 480 490 500
AFVGYEHMEW ESQVVGLVKG EGLVSELKEG EEGEVVLKET PFYPEGGGQI
510 520 530 540 550
GDAGIIESDK ALFKVEDTQK PTEGIIVHIG KVLKGTLKVG DTVHARVDKE
560 570 580 590 600
RRWDIMRNHT ATHLLHAALR NVLGEHVRQA GSLVADKYLR FDFTHFSALT
610 620 630 640 650
EEELKRVEEL VNEKIRENLP VNVMEMAYDE ALKTGAIAIF EEKYGERVRV
660 670 680 690 700
ISCGEFSKEL CGGTHVSATG DIGYFKIISE SSVGAGVRRI VAQTGRWSVE
710 720 730 740 750
TAFKEHQTLK KASSALGVGE EEVIQKIEEL KEEIKDRERE IQRLKQELLK
760 770 780 790 800
LQIREVVKEE NVGDFTLHYG VFEEVEPEEL RNLADMLRQR TKKDVVFIAS
810 820 830 840 850
RKGDKINFVI GVSKEISDKV NAKEVIREVG KVLKGGGGGR ADLAQGGGKA
860
PDKFPEAVKL LKEILSG
Length:867
Mass (Da):98,436
Last modified:August 1, 1998 - v1
Checksum:iE38C6D376643A149
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07289.1.
PIRiH70411.
RefSeqiNP_213887.1. NC_000918.1.
WP_010880825.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC07289; AAC07289; aq_1293.
GeneIDi1192761.
KEGGiaae:aq_1293.
PATRICi20959788. VBIAquAeo85532_1011.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07289.1.
PIRiH70411.
RefSeqiNP_213887.1. NC_000918.1.
WP_010880825.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RIQX-ray2.14A1-454[»]
1YFRX-ray2.15A/B1-454[»]
1YFSX-ray2.08A/B1-454[»]
1YFTX-ray2.23A1-454[»]
1YGBX-ray2.48A1-454[»]
3G98X-ray1.85A/B758-867[»]
3HTZX-ray2.50A2-454[»]
ProteinModelPortaliO67323.
SMRiO67323. Positions 2-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_1293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC07289; AAC07289; aq_1293.
GeneIDi1192761.
KEGGiaae:aq_1293.
PATRICi20959788. VBIAquAeo85532_1011.

Phylogenomic databases

eggNOGiENOG4105CIM. Bacteria.
COG0013. LUCA.
HOGENOMiHOG000156965.
InParanoidiO67323.
KOiK01872.
OMAiFDFNCPR.
OrthoDBiEOG6Q2SQ2.

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-925-MONOMER.
BRENDAi6.1.1.7. 396.

Miscellaneous databases

EvolutionaryTraceiO67323.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VF5.
  2. "Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase."
    Swairjo M.A., Schimmel P.R.
    Proc. Natl. Acad. Sci. U.S.A. 102:988-993(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-454 WITH SUBSTRATES OR WITH ATP.
  3. "The C-Ala domain brings together editing and aminoacylation functions on one tRNA."
    Guo M., Chong Y.E., Beebe K., Shapiro R., Yang X.-L., Schimmel P.
    Science 325:744-747(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN EXCHANGE EXPERIMENTS, X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 758-867.

Entry informationi

Entry nameiSYA_AQUAE
AccessioniPrimary (citable) accession number: O67323
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: February 17, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.